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There are several matches for 'probable methylesterase'.
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organism
protein
Homo sapiens
PPP2R4 - Serine/threonine-protein phosphatase 2A activator; PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides. Acts as a regulatory subunit for serine/threonine- protein phosphatase 2A (PP2A) modulating its activity or substrate specificity,
probably
by inducing a conformational change in the catalytic subunit, a proposed direct target of the PPIase. Can reactivate inactive phosphatase PP2A-phosphatase
methylesterase
complexes (PP2A(i)) in presence of ATP and Mg(2+) (By similarity). Reversibly stimulates the var [...]
[a.k.a. PTPA, PPP2R4-019, Q15258]
Mus musculus
Ppp2r4 - Serine/threonine-protein phosphatase 2A activator; PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides. Acts as a regulatory subunit for serine/threonine- protein phosphatase 2A (PP2A) modulating its activity or substrate specificity,
probably
by inducing a conformational change in the catalytic subunit, a proposed direct target of the PPIase. Can reactivate inactive phosphatase PP2A-phosphatase
methylesterase
complexes (PP2A(i)) in presence of ATP and Mg(2+). Reversibly stimulates the variable phosphotyr [...]
[a.k.a. Ptpa, AK049184, C330011K21]
Caenorhabditis elegans
B0464.9 -
Probable
protein phosphatase
methylesterase
1; Demethylates proteins that have been reversibly carboxymethylated
[a.k.a. UPI000013B6C3, WBGene00007188, 181999]
Pseudomonas stutzeri A1501
PST_3947 - Protein-glutamate methylesterase; Code: NT; COG: COG2201
[a.k.a. ABP81570.1, A4VRG9, GI:145572464,
probable methylesterase
,
Probable methylesterase
, ...]
Campylobacter jejuni NCTC11168
cheB - Protein-glutamate
methylesterase
; Original (2000) note: Cj0924c, cheB'
probable
MCP protein-glutamate
methylesterase
, len: 184 aa; similar to the
methylesterase
domain of e.g. CHEB_ECOLI protein-glutamate
methylesterase
(EC 3.1.1.61) (349 aa),fasta scores; opt: 339 z-score: 430.2 E(): 1.1e-16, 34.4% identity in 183 aa overlap. Note that the 'response reciever domain' normally found in cheB is not present. No Hp match; Updated (2006) note: Characterised within Escherichia coli, however, identity scores were marginal. Possible truncated protein as missing receiver domain of CheB protein. [...]
[a.k.a. Cj0924c, CAL35044.1, putative MCP protein-glutamate methylesterase]
Pseudogulbenkiania ferrooxidans
EEG07419.1 - PFAM: CheB
methylesterase
; KEGG: cvi:CV_3139
probable
protein-glutamate
methylesterase
[a.k.a. FuraDRAFT_3240, CheB methylesterase, GI:224601237]
Arabidopsis thaliana
AT1G62770 - Plant invertase/pectin
methylesterase
inhibitor superfamily protein; Pectin
methylesterase
(PME) inhibitor that
probably
targets root-expressed PME, regulates de-methylesterification of pectins in roots and affects root growth
[a.k.a. PMEI9, F23N19.14, At1g62770]
Streptomyces coelicolor
SCO0188 - SCJ1.37, crtV,
probable
methylesterase
, len: 336 aa. Highly similar to Streptomyces griseus TR:P72448 (EMBL; X95596)
methylesterase
(338 aa), fasta scores opt: 1315 z-score: 1538.7 E(): 0 60.5% identity in 337 aa overlap
[a.k.a. crtV, NP_624524.1, NP_624524]
Fusarium fujikuroi
LW93_7898 -
Probable
pectin
methylesterase
family protein
[a.k.a. S0DYA2, UPI000351E571, A0A0J0CR84]
Camelina sativa
XP_010421921.1 -
Probable
protein phosphatase
methylesterase
1
[a.k.a. XP_010421921.1, XM_010423619.1, probable protein phosphatase methylesterase 1]
Camelina sativa
XP_010437647.1 -
Probable
protein phosphatase
methylesterase
1
[a.k.a. XP_010437647.1, XP_010437647, probable protein phosphatase methylesterase 1]
Camelina sativa
XP_010455401.1 -
Probable
protein phosphatase
methylesterase
1
[a.k.a. XP_010455401.1, GeneID:104737000, 727566066]
Dictyostelium discoideum
ppme1 -
Probable
protein phosphatase
methylesterase
1; Demethylates proteins that have been reversibly carboxymethylated
[a.k.a. DDB_G0281651, DDB0305014, Q54TN3]
Arabidopsis thaliana
ICME-LIKE2 -
Probable
isoprenylcysteine alpha-carbonyl
methylesterase
ICMEL2; Catalyzes the demethylation of isoprenylcysteine methylesters. May act as a negative regulator of ABA signaling; Belongs to the AB hydrolase superfamily. Isoprenylcysteine
methylesterase
family
[a.k.a. F16B3.4, At3g02410, ICMEL2]
Arabidopsis thaliana
ICME-LIKE1 -
Probable
isoprenylcysteine alpha-carbonyl
methylesterase
ICMEL1; Catalyzes the demethylation of isoprenylcysteine methylesters. May be involved in the regulation of ABA signaling (By similarity); Belongs to the AB hydrolase superfamily. Isoprenylcysteine
methylesterase
family
[a.k.a. ICMEL1, At1g26120, F28B23.20]
Bacteroides caccae
EDM21043.1 - Uncharacterized protein; KEGG: blo:BL1723 0.79 orn;
probable
oligoribonuclease; COG: COG4677 Pectin
methylesterase
[a.k.a. BACCAC_01749, hypothetical protein, Uncharacterized protein]
Camelina sativa
XP_010460369.1 -
Probable
isoprenylcysteine alpha-carbonyl
methylesterase
ICMEL1
[a.k.a. XP_010460369.1, XP_010460369, 104741260]
Camelina sativa
XP_010463644.1 -
Probable
isoprenylcysteine alpha-carbonyl
methylesterase
ICMEL2
[a.k.a. XP_010463644.1, 104744314, EC 3.1.1.-]
Camelina sativa
XP_010485486.1 -
Probable
isoprenylcysteine alpha-carbonyl
methylesterase
ICMEL2
[a.k.a. XP_010485486.1, 104763804, GI:727629116]
Camelina sativa
XP_010486759.1 -
Probable
isoprenylcysteine alpha-carbonyl
methylesterase
ICMEL2
[a.k.a. XP_010486759.1, GI:727410484, EC 3.1.1.-]
Ceratitis capitata
XP_004528818.1 -
Probable
isoprenylcysteine alpha-carbonyl
methylesterase
ICMEL1-like
[a.k.a. XP_004528818.1, XP_004528818, 498978305]
Cicer arietinum
XP_004509595.1 -
Probable
isoprenylcysteine alpha-carbonyl
methylesterase
ICMEL1; Derived by automated computational analysis using gene prediction method: Gnomon. Supporting evidence includes similarity to: 1 EST, 8 Proteins, and 100% coverage of the annotated genomic feature by RNAseq alignments, including 2 samples with support for all annotated introns
[a.k.a. LOC101514519, XP_004509595.1, cam:101514519]
Citrus sinensis
XP_006484386.1 - Uncharacterized protein;
Probable
isoprenylcysteine alpha-carbonyl
methylesterase
ICMEL1-like
[a.k.a. CISIN_1g011866mg, XP_006484386.1, Uncharacterized protein]
Cucumis melo
XP_008457187.1 -
Probable
isoprenylcysteine alpha-carbonyl
methylesterase
ICMEL2 isoform X1
[a.k.a. LOC103496926, XP_008457187.1, A0A1S3C4X6]
Cucumis sativus
XP_004169028.1 -
Probable
isoprenylcysteine alpha-carbonyl
methylesterase
ICMEL1-like
[a.k.a. XP_004169028.1, 101230533, 449524034]
Esox lucius
XP_010875280.1 -
Probable
isoprenylcysteine alpha-carbonyl
methylesterase
ICMEL1 isoform X1
[a.k.a. XP_010875280.1, els:105014562, LOC105014562]
Eucalyptus grandis
XP_010032602.1 - Uncharacterized protein;
Probable
isoprenylcysteine alpha-carbonyl
methylesterase
ICMEL2
[a.k.a. EUGRSUZ_J01457, XP_010032602.1, egr:104422076]
Eucalyptus grandis
XP_010044310.1 - Uncharacterized protein;
Probable
isoprenylcysteine alpha-carbonyl
methylesterase
ICMEL1
[a.k.a. EUGRSUZ_B03069, XP_010044310.1, A0A059D859_EUCGR]
Fragaria vesca
XP_004298317.1 -
Probable
isoprenylcysteine alpha-carbonyl
methylesterase
ICMEL1-like
[a.k.a. XP_004298317.1, XM_004298269.1, GI:470124637]
Fragaria vesca
XP_004304151.1 -
Probable
isoprenylcysteine alpha-carbonyl
methylesterase
ICMEL2-like
[a.k.a. XP_004304151.1, EC 3.1.1.-, GI:470136759]
Haplochromis burtoni
XP_005924521.1 -
Probable
isoprenylcysteine alpha-carbonyl
methylesterase
ICME-like isoform X1
[a.k.a. XP_005924521.1, LOC102311780, GI:554827834]
Haplochromis burtoni
XP_005924586.1 -
Probable
isoprenylcysteine alpha-carbonyl
methylesterase
ICMEL1-like
[a.k.a. XP_005924586.1, XM_005924524.1, GI:554827965]
Larimichthys crocea
EH28_01184 -
Probable
isoprenylcysteine alpha-carbonyl
methylesterase
ICME
[a.k.a. XP_010734253.1, 104922982, 734613484]
Malus domestica
XP_008339723.1 -
Probable
isoprenylcysteine alpha-carbonyl
methylesterase
ICMEL1
[a.k.a. XP_008339723.1, mdm:103402743, 103402743]
Malus domestica
XP_008341855.1 -
Probable
isoprenylcysteine alpha-carbonyl
methylesterase
ICMEL2
[a.k.a. XP_008341855.1, GI:658013118, 103404698]
Malus domestica
XP_008368510.1 -
Probable
isoprenylcysteine alpha-carbonyl
methylesterase
ICMEL2
[a.k.a. XP_008368510.1, GI:658065123, 103432123]
Maylandia zebra
XP_004547024.1 -
Probable
isoprenylcysteine alpha-carbonyl
methylesterase
ICME-like isoform X1
[a.k.a. XP_004547024.1, XP_004547024, LOC101484211]
Nelumbo nucifera
XP_010265336.1 -
Probable
isoprenylcysteine alpha-carbonyl
methylesterase
ICMEL2 isoform X1; Derived by automated computational analysis using gene prediction method: Gnomon. Supporting evidence includes similarity to: 7 Proteins, and 100% coverage of the annotated genomic feature by RNAseq alignments, including 16 samples with support for all annotated introns
[a.k.a. LOC104603088, XP_010265336.1, 104603088]
Neolamprologus brichardi
XP_006790158.1 -
Probable
isoprenylcysteine alpha-carbonyl
methylesterase
ICME-like
[a.k.a. XP_006790158.1, 583989914, GI:583989914]
Neolamprologus brichardi
XP_006810543.1 -
Probable
isoprenylcysteine alpha-carbonyl
methylesterase
ICME-like
[a.k.a. XP_006810543.1, 584032261, XM_006810480.1]
Nicotiana sylvestris
XP_009769054.1 -
Probable
isoprenylcysteine alpha-carbonyl
methylesterase
ICMEL1 isoform X1
[a.k.a. LOC104219985, XP_009769054.1, EC 3.1.1.-]
Nicotiana sylvestris
XP_009775000.1 -
Probable
isoprenylcysteine alpha-carbonyl
methylesterase
ICMEL2 isoform X1
[a.k.a. LOC104224962, XP_009775000.1, A0A1U7WL71_NICSY]
Nicotiana tomentosiformis
XP_009623680.1 -
Probable
isoprenylcysteine alpha-carbonyl
methylesterase
ICMEL2 isoform X1
[a.k.a. XP_009623680.1, GeneID:104114848, LOC104114848]
Oryza sativa
IMCEL2 -
Probable
isoprenylcysteine alpha-carbonyl
methylesterase
ICMEL2; Catalyzes the demethylation of isoprenylcysteine methylesters
[a.k.a. Os01g0642000, P0039G05.24, P0510C12.9]
Oryza sativa
IMCE -
Probable
isoprenylcysteine alpha-carbonyl
methylesterase
ICME; Catalyzes the demethylation of isoprenylcysteine methylesters
[a.k.a. Os05g0577200, LOC_Os05g50170, OJ1126_B10.7]
Oryza sativa
IMCEL1 -
Probable
isoprenylcysteine alpha-carbonyl
methylesterase
ICMEL1; Catalyzes the demethylation of isoprenylcysteine methylesters
[a.k.a. Os06g0708100, P0655A07.1-1, P0621D05.41-1]
Phoenix dactylifera
XP_008801967.1 -
Probable
isoprenylcysteine alpha-carbonyl
methylesterase
ICMEL2 isoform X1
[a.k.a. XP_008801967.1, XM_008803745.1, EC 3.1.1.-]
Poecilia reticulata
XP_008416310.1 -
Probable
isoprenylcysteine alpha-carbonyl
methylesterase
ICMEL2 isoform X1
[a.k.a. XP_008416310.1, EC 3.1.1.-, pret:103469989]
Prunus mume
XP_008243142.1 -
Probable
isoprenylcysteine alpha-carbonyl
methylesterase
ICMEL1
[a.k.a. XP_008243142.1, LOC103341406, EC 3.1.1.-]
Pundamilia nyererei
XP_005738233.1 -
Probable
isoprenylcysteine alpha-carbonyl
methylesterase
ICMEL1-like
[a.k.a. XP_005738233.1, XM_005738176.1, LOC102214345]
Pundamilia nyererei
XP_005738335.1 -
Probable
isoprenylcysteine alpha-carbonyl
methylesterase
ICME-like
[a.k.a. XP_005738335.1, 102192414, XM_005738278.1]
Pyrus x bretschneideri
XP_009336650.1 -
Probable
isoprenylcysteine alpha-carbonyl
methylesterase
ICMEL1
[a.k.a. XP_009336650.1, pxb:103929220, GeneID:103929220]
Pyrus x bretschneideri
XP_009355992.1 -
Probable
isoprenylcysteine alpha-carbonyl
methylesterase
ICMEL1 isoform X1
[a.k.a. XP_009355992.1, GI:694311047, EC 3.1.1.-]
Stegastes partitus
XP_008293394.1 -
Probable
isoprenylcysteine alpha-carbonyl
methylesterase
ICME
[a.k.a. XP_008293394.1, XP_008293394, GI:657578991]
Tarenaya hassleriana
XP_010549954.1 -
Probable
isoprenylcysteine alpha-carbonyl
methylesterase
ICMEL2
[a.k.a. XP_010549954.1, EC 3.1.1.-, 104820970]
Tarenaya hassleriana
XP_010551319.1 -
Probable
isoprenylcysteine alpha-carbonyl
methylesterase
ICMEL1 isoform X1
[a.k.a. XP_010551319.1, XP_010551319, EC 3.1.1.-]
Rhizobium etli CFN42
cheY2 -
Probable
chemotaxis response regulator protein-glutamate
methylesterase
1; Involved in the modulation of the chemotaxis system; catalyzes the demethylation of specific methylglutamate residues introduced into the chemoreceptors (methyl-accepting chemotaxis proteins) by CheR
[a.k.a. RHE_CH00643, cheB1, RHE_CH00642]
Magnetococcus marinus
Mmc1_2113 - PFAM: CheB
methylesterase
; MCP methyltransferase, CheR-type; KEGG: cvi:CV1580
probable
two-component hybrid sensor-regulator protein
[a.k.a. ABK44614.1, A0L9H1_MAGMM, 2.1.1.80]
Aspergillus flavus
rhgC -
Probable
rhamnogalacturonase C; Pectinolytic enzymes consist of four classes of enzymes: pectine lyase, polygalacturonase, pectin
methylesterase
and rhamnogalacturonase. Hydrolyzes alpha-D-galacturonopyranosyl- (1,2)-alpha-L-rhamnopyranosyl linkages in the backbone of the hairy regions of pectins (By similarity)
[a.k.a. AFLA_136750, UPI00018F5C8E, XP_002379688]
Aspergillus flavus
rhgA -
Probable
rhamnogalacturonase A; Pectinolytic enzymes consist of four classes of enzymes: pectine lyase, polygalacturonase, pectin
methylesterase
and rhamnogalacturonase. Hydrolyzes alpha-D-galacturonopyranosyl- (1,2)-alpha-L-rhamnopyranosyl linkages in the backbone of the hairy regions of pectins (By similarity)
[a.k.a. AFLA_070940, 7914456, XM_002380612.1]
Aspergillus flavus
rhgE -
Probable
rhamnogalacturonase E; Pectinolytic enzymes consist of four classes of enzymes: pectine lyase, polygalacturonase, pectin
methylesterase
and rhamnogalacturonase. Hydrolyzes alpha-D-galacturonopyranosyl- (1,2)-alpha-L-rhamnopyranosyl linkages in the backbone of the hairy regions of pectins (By similarity)
[a.k.a. AFLA_089930, CADAFLAG00008679, UPI00018F62E5]
Aspergillus fumigatus
rhgB -
Probable
rhamnogalacturonase B; Pectinolytic enzymes consist of four classes of enzymes: pectine lyase, polygalacturonase, pectin
methylesterase
and rhamnogalacturonase. Hydrolyzes alpha-D-galacturonopyranosyl- (1,2)-alpha-L-rhamnopyranosyl linkages in the backbone of the hairy regions of pectins (By similarity)
[a.k.a. AFUA_5G10530, RHGB_ASPFU, CADAFUBT00005794]
Aspergillus terreus
ATEG_07607 -
Probable
rhamnogalacturonase B; Pectinolytic enzymes consist of four classes of enzymes: pectine lyase, polygalacturonase, pectin
methylesterase
and rhamnogalacturonase. Hydrolyzes alpha-D-galacturonopyranosyl- (1,2)-alpha-L-rhamnopyranosyl linkages in the backbone of the hairy regions of pectins (By similarity)
[a.k.a. rhgB, XM_001216228.1, CADATEAP00001304]
Neosartorya fischeri
rhgB -
Probable
rhamnogalacturonase B; Pectinolytic enzymes consist of four classes of enzymes: pectine lyase, polygalacturonase, pectin
methylesterase
and rhamnogalacturonase. Hydrolyzes alpha-D-galacturonopyranosyl- (1,2)-alpha-L-rhamnopyranosyl linkages in the backbone of the hairy regions of pectins (By similarity)
[a.k.a. NFIA_076680, XM_001259634.1, CADNFIAP00007568]
Aspergillus clavatus
rglA -
Probable
rhamnogalacturonate lyase A; Pectinolytic enzymes consist of four classes of enzymes: pectin lyase, polygalacturonase, pectin
methylesterase
and rhamnogalacturonase. Degrades the rhamnogalacturonan I (RG-I) backbone of pectin. Active against linseed rhamnogalacturonan (By similarity)
[a.k.a. ACLA_054660, CADACLAT00005324, PWY-6771]
Aspergillus clavatus
plyE -
Probable
pectate lyase E; Pectinolytic enzyme consist of four classes of enzymes: pectin lyase, polygalacturonase, pectin
methylesterase
and rhamnogalacturonase. Among pectinolytic enzymes, pectin lyase is the most important in depolymerization of pectin, since it cleaves internal glycosidic bonds of highly methylated pectins. Favors pectate, the anion, over pectin, the methyl ester (By similarity); Belongs to the polysaccharide lyase 3 family
[a.k.a. ACLA_059210, EAW15258.1, PLYE_ASPCL]
Aspergillus clavatus
pelA -
Probable
pectin lyase A; Pectinolytic enzymes consist of four classes of enzymes: pectin lyase, polygalacturonase, pectin
methylesterase
and rhamnogalacturonase. Among pectinolytic enzymes, pectin lyase is the most important in depolymerization of pectin, since it cleaves internal glycosidic bonds of highly methylated pectins (By similarity)
[a.k.a. ACLA_094210, A1CFS2, XM_001273146]
Aspergillus flavus
pelF -
Probable
pectin lyase F; Pectinolytic enzymes consist of four classes of enzymes: pectin lyase, polygalacturonase, pectin
methylesterase
and rhamnogalacturonase. Among pectinolytic enzymes, pectin lyase is the most important in depolymerization of pectin, since it cleaves internal glycosidic bonds of highly methylated pectins (By similarity)
[a.k.a. AFLA_025400, XM_002374010.1, CADAFLAP00001916]
Aspergillus flavus
rglB -
Probable
rhamnogalacturonate lyase B; Pectinolytic enzymes consist of four classes of enzymes: pectin lyase, polygalacturonase, pectin
methylesterase
and rhamnogalacturonase. Degrades the rhamnogalacturonan I (RG-I) backbone of pectin (By similarity)
[a.k.a. AFLA_014290, CADAFLAT00003314, afv:AFLA_014290]
Aspergillus flavus
pelA -
Probable
pectin lyase A; Pectinolytic enzymes consist of four classes of enzymes: pectin lyase, polygalacturonase, pectin
methylesterase
and rhamnogalacturonase. Among pectinolytic enzymes, pectin lyase is the most important in depolymerization of pectin, since it cleaves internal glycosidic bonds of highly methylated pectins (By similarity)
[a.k.a. AFLA_017180, XP_002375738, CADAFLAG00003603]
Aspergillus flavus
rglA -
Probable
rhamnogalacturonate lyase A; Pectinolytic enzymes consist of four classes of enzymes: pectin lyase, polygalacturonase, pectin
methylesterase
and rhamnogalacturonase. Degrades the rhamnogalacturonan I (RG-I) backbone of pectin (By similarity)
[a.k.a. AFLA_041820, AFLA_041820A, afv:AFLA_041820]
Aspergillus flavus
plyB -
Probable
pectate lyase B; Pectinolytic enzyme consist of four classes of enzymes: pectin lyase, polygalacturonase, pectin
methylesterase
and rhamnogalacturonase. Among pectinolytic enzymes, pectin lyase is the most important in depolymerization of pectin, since it cleaves internal glycosidic bonds of highly methylated pectins. Favors pectate, the anion, over pectin, the methyl ester (By similarity); Belongs to the polysaccharide lyase 1 family
[a.k.a. AFLA_044970, XM_002377918, 4.2.2.2]
Aspergillus flavus
plyA -
Probable
pectate lyase A; Pectinolytic enzyme consist of four classes of enzymes: pectin lyase, polygalacturonase, pectin
methylesterase
and rhamnogalacturonase. Among pectinolytic enzymes, pectin lyase is the most important in depolymerization of pectin, since it cleaves internal glycosidic bonds of highly methylated pectins. Favors pectate, the anion, over pectin, the methyl ester (By similarity); Belongs to the polysaccharide lyase 1 family
[a.k.a. AFLA_057770, CADAFLAT00006386, CADAFLAG00006386]
Aspergillus flavus
plyF -
Probable
pectate lyase F; Pectinolytic enzyme consist of four classes of enzymes: pectin lyase, polygalacturonase, pectin
methylesterase
and rhamnogalacturonase. Among pectinolytic enzymes, pectin lyase is the most important in depolymerization of pectin, since it cleaves internal glycosidic bonds of highly methylated pectins. Favors pectate, the anion, over pectin, the methyl ester (By similarity); Belongs to the polysaccharide lyase 3 family
[a.k.a. AFLA_070460, CADAFLAG00008470, 7914408]
Aspergillus flavus
plyC -
Probable
pectate lyase C; Pectinolytic enzyme consist of four classes of enzymes: pectin lyase, polygalacturonase, pectin
methylesterase
and rhamnogalacturonase. Among pectinolytic enzymes, pectin lyase is the most important in depolymerization of pectin, since it cleaves internal glycosidic bonds of highly methylated pectins. Favors pectate, the anion, over pectin, the methyl ester (By similarity); Belongs to the polysaccharide lyase 1 family
[a.k.a. AFLA_002010, EED47560.1, B8NQQ7]
Aspergillus flavus
pelD -
Probable
pectin lyase D; Pectinolytic enzymes consist of four classes of enzymes: pectin lyase, polygalacturonase, pectin
methylesterase
and rhamnogalacturonase. Among pectinolytic enzymes, pectin lyase is the most important in depolymerization of pectin, since it cleaves internal glycosidic bonds of highly methylated pectins (By similarity)
[a.k.a. AFLA_116040, CADAFLAP00012176, G3F4I3_ASPFL]
Aspergillus flavus
plyE -
Probable
pectate lyase E; Pectinolytic enzyme consist of four classes of enzymes: pectin lyase, polygalacturonase, pectin
methylesterase
and rhamnogalacturonase. Among pectinolytic enzymes, pectin lyase is the most important in depolymerization of pectin, since it cleaves internal glycosidic bonds of highly methylated pectins. Favors pectate, the anion, over pectin, the methyl ester (By similarity); Belongs to the polysaccharide lyase 3 family
[a.k.a. AFLA_121970, CADAFLAT00012769, 7918450]
Aspergillus fumigatus
plyC -
Probable
pectate lyase C; Pectinolytic enzyme consist of four classes of enzymes: pectin lyase, polygalacturonase, pectin
methylesterase
and rhamnogalacturonase. Among pectinolytic enzymes, pectin lyase is the most important in depolymerization of pectin, since it cleaves internal glycosidic bonds of highly methylated pectins. Favors pectate, the anion, over pectin, the methyl ester (By similarity); Belongs to the polysaccharide lyase 1 family
[a.k.a. AFUA_6G14400, Probable pectate lyase C, 3508631]
Aspergillus fumigatus
rglB -
Probable
rhamnogalacturonate lyase B; Pectinolytic enzymes consist of four classes of enzymes: pectin lyase, polygalacturonase, pectin
methylesterase
and rhamnogalacturonase. Degrades the rhamnogalacturonan I (RG-I) backbone of pectin (By similarity)
[a.k.a. AFUA_1G17230, XP_753091, afm:AFUA_1G17230]
Aspergillus fumigatus
plyA -
Probable
pectate lyase A; Pectinolytic enzyme consist of four classes of enzymes: pectin lyase, polygalacturonase, pectin
methylesterase
and rhamnogalacturonase. Among pectinolytic enzymes, pectin lyase is the most important in depolymerization of pectin, since it cleaves internal glycosidic bonds of highly methylated pectins. Favors pectate, the anion, over pectin, the methyl ester (By similarity); Belongs to the polysaccharide lyase 1 family
[a.k.a. AFUA_2G00760, 3507249, CADAFUBT00001779]
Aspergillus fumigatus
pelB -
Probable
pectin lyase B; Pectinolytic enzymes consist of four classes of enzymes: pectin lyase, polygalacturonase, pectin
methylesterase
and rhamnogalacturonase. Among pectinolytic enzymes, pectin lyase is the most important in depolymerization of pectin, since it cleaves internal glycosidic bonds of highly methylated pectins (By similarity)
[a.k.a. AFUA_2G00800, PELB_ASPFU, Probable pectin lyase B]
Aspergillus fumigatus
pelA -
Probable
pectin lyase A; Pectinolytic enzymes consist of four classes of enzymes: pectin lyase, polygalacturonase, pectin
methylesterase
and rhamnogalacturonase. Among pectinolytic enzymes, pectin lyase is the most important in depolymerization of pectin, since it cleaves internal glycosidic bonds of highly methylated pectins (By similarity)
[a.k.a. AFUA_5G10380, afm:AFUA_5G10380, Pectin lyase, putative]
Aspergillus fumigatus
plyF -
Probable
pectate lyase F; Pectinolytic enzyme consist of four classes of enzymes: pectin lyase, polygalacturonase, pectin
methylesterase
and rhamnogalacturonase. Among pectinolytic enzymes, pectin lyase is the most important in depolymerization of pectin, since it cleaves internal glycosidic bonds of highly methylated pectins. Favors pectate, the anion, over pectin, the methyl ester (By similarity); Belongs to the polysaccharide lyase 3 family
[a.k.a. AFUA_1G01120, Q4WKV8, 4.2.2.2]
Aspergillus fumigatus
plyE -
Probable
pectate lyase E; Pectinolytic enzyme consist of four classes of enzymes: pectin lyase, polygalacturonase, pectin
methylesterase
and rhamnogalacturonase. Among pectinolytic enzymes, pectin lyase is the most important in depolymerization of pectin, since it cleaves internal glycosidic bonds of highly methylated pectins. Favors pectate, the anion, over pectin, the methyl ester (By similarity); Belongs to the polysaccharide lyase 3 family
[a.k.a. AFUA_8G05910, afm:AFUA_8G05910, 4.2.2.2]
Aspergillus fumigatus
plyD -
Probable
pectate lyase D; Pectinolytic enzyme consist of four classes of enzymes: pectin lyase, polygalacturonase, pectin
methylesterase
and rhamnogalacturonase. Among pectinolytic enzymes, pectin lyase is the most important in depolymerization of pectin, since it cleaves internal glycosidic bonds of highly methylated pectins. Favors pectate, the anion, over pectin, the methyl ester (By similarity); Belongs to the polysaccharide lyase 3 family
[a.k.a. AFUA_7G06400, Probable pectate lyase D, afm:AFUA_7G06400]
Aspergillus fumigatus
rglA -
Probable
rhamnogalacturonate lyase A; Pectinolytic enzymes consist of four classes of enzymes: pectin lyase, polygalacturonase, pectin
methylesterase
and rhamnogalacturonase. Degrades the rhamnogalacturonan I (RG-I) backbone of pectin (By similarity)
[a.k.a. AFUA_4G03780, CADAFUBP00009644, CADAFUBT00009820]
Aspergillus nidulans
pelC -
Probable
pectin lyase C; Pectinolytic enzymes consist of four classes of enzymes: pectin lyase, polygalacturonase, pectin
methylesterase
and rhamnogalacturonase. Among pectinolytic enzymes, pectin lyase is the most important in depolymerization of pectin, since it cleaves internal glycosidic bonds of highly methylated pectins (By similarity)
[a.k.a. AN1111, UPI0001B786CD, ANIA_10147]
Aspergillus nidulans
AN5333.2 -
Probable
pectate lyase C; Pectinolytic enzyme consist of four classes of enzymes: pectin lyase, polygalacturonase, pectin
methylesterase
and rhamnogalacturonase. Among pectinolytic enzymes, pectin lyase is the most important in depolymerization of pectin, since it cleaves internal glycosidic bonds of highly methylated pectins. Favors pectate, the anion, over pectin, the methyl ester (By similarity); Belongs to the polysaccharide lyase 1 family
[a.k.a. plyC, AN5333, Q5B297_EMENI]
Aspergillus nidulans
AN4139.2 -
Probable
rhamnogalacturonate lyase C; Pectinolytic enzymes consist of four classes of enzymes: pectin lyase, polygalacturonase, pectin
methylesterase
and rhamnogalacturonase. Degrades the rhamnogalacturonan I (RG-I) backbone of pectin (By similarity)
[a.k.a. rglC, AN4139, rhamnogalacturonan lyase (Eurofung)]
Aspergillus nidulans
AN4882.2 -
Probable
pectin lyase F; Pectinolytic enzymes consist of four classes of enzymes: pectin lyase, polygalacturonase, pectin
methylesterase
and rhamnogalacturonase. Among pectinolytic enzymes, pectin lyase is the most important in depolymerization of pectin, since it cleaves internal glycosidic bonds of highly methylated pectins (By similarity)
[a.k.a. pelF, AN4882, C8V9T8]
Aspergillus nidulans
AN6106.2 -
Probable
pectate lyase F; Pectinolytic enzyme consist of four classes of enzymes: pectin lyase, polygalacturonase, pectin
methylesterase
and rhamnogalacturonase. Among pectinolytic enzymes, pectin lyase is the most important in depolymerization of pectin, since it cleaves internal glycosidic bonds of highly methylated pectins. Favors pectate, the anion, over pectin, the methyl ester (By similarity); Belongs to the polysaccharide lyase 1 family
[a.k.a. AN6106, plyF, XM_658618]
Aspergillus nidulans
AN6748.2 -
Probable
pectate lyase G; Pectinolytic enzyme consist of four classes of enzymes: pectin lyase, polygalacturonase, pectin
methylesterase
and rhamnogalacturonase. Among pectinolytic enzymes, pectin lyase is the most important in depolymerization of pectin, since it cleaves internal glycosidic bonds of highly methylated pectins. Favors pectate, the anion, over pectin, the methyl ester (By similarity); Belongs to the polysaccharide lyase 3 family
[a.k.a. AN6748, plyG, 2870360]
Aspergillus nidulans
AN9439.2 -
Probable
pectin lyase D; Pectinolytic enzymes consist of four classes of enzymes: pectin lyase, polygalacturonase, pectin
methylesterase
and rhamnogalacturonase. Among pectinolytic enzymes, pectin lyase is the most important in depolymerization of pectin, since it cleaves internal glycosidic bonds of highly methylated pectins (By similarity)
[a.k.a. AN9439, pelD, XM_863728.1]
Aspergillus nidulans
AN2542.2 -
Probable
pectate lyase D; Pectinolytic enzyme consist of four classes of enzymes: pectin lyase, polygalacturonase, pectin
methylesterase
and rhamnogalacturonase. Among pectinolytic enzymes, pectin lyase is the most important in depolymerization of pectin, since it cleaves internal glycosidic bonds of highly methylated pectins. Favors pectate, the anion, over pectin, the methyl ester (By similarity); Belongs to the polysaccharide lyase 3 family
[a.k.a. plyD, AN2542, AN2542.4]
Aspergillus niger
pelC -
Probable
pectin lyase C; Pectinolytic enzymes consist of four classes of enzymes: pectin lyase, polygalacturonase, pectin
methylesterase
and rhamnogalacturonase. Among pectinolytic enzymes, pectin lyase is the most important in depolymerization of pectin, since it cleaves internal glycosidic bonds of highly methylated pectins (By similarity)
[a.k.a. ANI_1_554094, An11g04030, Q5MBK3]
Aspergillus niger
pelF -
Probable
pectin lyase F; Pectinolytic enzymes consist of four classes of enzymes: pectin lyase, polygalacturonase, pectin
methylesterase
and rhamnogalacturonase. Among pectinolytic enzymes, pectin lyase is the most important in depolymerization of pectin, since it cleaves internal glycosidic bonds of highly methylated pectins (By similarity)
[a.k.a. ANI_1_1744134, An15g07160, PELF_ASPNC]
Aspergillus terreus
ATEG_02193 -
Probable
rhamnogalacturonate lyase A; Pectinolytic enzymes consist of four classes of enzymes: pectin lyase, polygalacturonase, pectin
methylesterase
and rhamnogalacturonase. Degrades the rhamnogalacturonan I (RG-I) backbone of pectin (By similarity)
[a.k.a. rglA, UPI0000E2A9BD, XP_001211371.1]
Aspergillus terreus
ATEG_01216 -
Probable
pectin lyase A; Pectinolytic enzymes consist of four classes of enzymes: pectin lyase, polygalacturonase, pectin
methylesterase
and rhamnogalacturonase. Among pectinolytic enzymes, pectin lyase is the most important in depolymerization of pectin, since it cleaves internal glycosidic bonds of highly methylated pectins (By similarity)
[a.k.a. pelA, Q0CYL8, 4315566]
Aspergillus terreus
ATEG_10327 -
Probable
rhamnogalacturonate lyase B; Pectinolytic enzymes consist of four classes of enzymes: pectin lyase, polygalacturonase, pectin
methylesterase
and rhamnogalacturonase. Degrades the rhamnogalacturonan I (RG-I) backbone of pectin (By similarity)
[a.k.a. rglB, UPI0000E2DCE1, Q0C7K7]
Aspergillus terreus
ATEG_05467 -
Probable
pectate lyase C; Pectinolytic enzyme consist of four classes of enzymes: pectin lyase, polygalacturonase, pectin
methylesterase
and rhamnogalacturonase. Among pectinolytic enzymes, pectin lyase is the most important in depolymerization of pectin, since it cleaves internal glycosidic bonds of highly methylated pectins. Favors pectate, the anion, over pectin, the methyl ester (By similarity); Belongs to the polysaccharide lyase 1 family
[a.k.a. plyC, EAU34536.1, XM_001214645]
Aspergillus terreus
ATEG_08626 -
Probable
pectate lyase F; Pectinolytic enzyme consist of four classes of enzymes: pectin lyase, polygalacturonase, pectin
methylesterase
and rhamnogalacturonase. Among pectinolytic enzymes, pectin lyase is the most important in depolymerization of pectin, since it cleaves internal glycosidic bonds of highly methylated pectins. Favors pectate, the anion, over pectin, the methyl ester (By similarity); Belongs to the polysaccharide lyase 3 family
[a.k.a. plyF, XP_001217212.1, Q0CCF8]
Aspergillus terreus
ATEG_06314 -
Probable
pectate lyase G; Pectinolytic enzyme consist of four classes of enzymes: pectin lyase, polygalacturonase, pectin
methylesterase
and rhamnogalacturonase. Among pectinolytic enzymes, pectin lyase is the most important in depolymerization of pectin, since it cleaves internal glycosidic bonds of highly methylated pectins. Favors pectate, the anion, over pectin, the methyl ester (By similarity); Belongs to the polysaccharide lyase 3 family
[a.k.a. plyG, UPI0000E2C97A, XM_001215492.1]
Aspergillus terreus
ATEG_08834 -
Probable
pectate lyase B; Pectinolytic enzyme consist of four classes of enzymes: pectin lyase, polygalacturonase, pectin
methylesterase
and rhamnogalacturonase. Among pectinolytic enzymes, pectin lyase is the most important in depolymerization of pectin, since it cleaves internal glycosidic bonds of highly methylated pectins. Favors pectate, the anion, over pectin, the methyl ester (By similarity); Belongs to the polysaccharide lyase 1 family
[a.k.a. plyB, 4323471, XM_001217419]
Aspergillus terreus
ATEG_06285 -
Probable
pectate lyase D; Pectinolytic enzyme consist of four classes of enzymes: pectin lyase, polygalacturonase, pectin
methylesterase
and rhamnogalacturonase. Among pectinolytic enzymes, pectin lyase is the most important in depolymerization of pectin, since it cleaves internal glycosidic bonds of highly methylated pectins. Favors pectate, the anion, over pectin, the methyl ester (By similarity); Belongs to the polysaccharide lyase 3 family
[a.k.a. plyD, Probable pectate lyase D, XM_001215463]
Neosartorya fischeri
plyF -
Probable
pectate lyase F; Pectinolytic enzyme consist of four classes of enzymes: pectin lyase, polygalacturonase, pectin
methylesterase
and rhamnogalacturonase. Among pectinolytic enzymes, pectin lyase is the most important in depolymerization of pectin, since it cleaves internal glycosidic bonds of highly methylated pectins. Favors pectate, the anion, over pectin, the methyl ester (By similarity); Belongs to the polysaccharide lyase 3 family
[a.k.a. NFIA_023470, CADNFIAG00000826, UPI0000EA6CAA]
Neosartorya fischeri
rglB -
Probable
rhamnogalacturonate lyase B; Pectinolytic enzymes consist of four classes of enzymes: pectin lyase, polygalacturonase, pectin
methylesterase
and rhamnogalacturonase. Degrades the rhamnogalacturonan I (RG-I) backbone of pectin (By similarity)
[a.k.a. NFIA_008140, A1D144, 4591405]
Neosartorya fischeri
plyD -
Probable
pectate lyase D; Pectinolytic enzyme consist of four classes of enzymes: pectin lyase, polygalacturonase, pectin
methylesterase
and rhamnogalacturonase. Among pectinolytic enzymes, pectin lyase is the most important in depolymerization of pectin, since it cleaves internal glycosidic bonds of highly methylated pectins. Favors pectate, the anion, over pectin, the methyl ester (By similarity); Belongs to the polysaccharide lyase 3 family
[a.k.a. NFIA_027690, Probable pectate lyase D, A1DCY5]
Neosartorya fischeri
rglA -
Probable
rhamnogalacturonate lyase A; Pectinolytic enzymes consist of four classes of enzymes: pectin lyase, polygalacturonase, pectin
methylesterase
and rhamnogalacturonase. Degrades the rhamnogalacturonan I (RG-I) backbone of pectin (By similarity)
[a.k.a. NFIA_029620, XP_001262427.1, CADNFIAT00002788]
Neosartorya fischeri
pelA -
Probable
pectin lyase A; Pectinolytic enzymes consist of four classes of enzymes: pectin lyase, polygalacturonase, pectin
methylesterase
and rhamnogalacturonase. Among pectinolytic enzymes, pectin lyase is the most important in depolymerization of pectin, since it cleaves internal glycosidic bonds of highly methylated pectins (By similarity)
[a.k.a. NFIA_033080, CADNFIAP00003264, 4592857]
Neosartorya fischeri
plyA -
Probable
pectate lyase A; Pectinolytic enzyme consist of four classes of enzymes: pectin lyase, polygalacturonase, pectin
methylesterase
and rhamnogalacturonase. Among pectinolytic enzymes, pectin lyase is the most important in depolymerization of pectin, since it cleaves internal glycosidic bonds of highly methylated pectins. Favors pectate, the anion, over pectin, the methyl ester (By similarity); Belongs to the polysaccharide lyase 1 family
[a.k.a. NFIA_033040, XP_001265635, XM_001265634]
Neosartorya fischeri
plyC -
Probable
pectate lyase C; Pectinolytic enzyme consist of four classes of enzymes: pectin lyase, polygalacturonase, pectin
methylesterase
and rhamnogalacturonase. Among pectinolytic enzymes, pectin lyase is the most important in depolymerization of pectin, since it cleaves internal glycosidic bonds of highly methylated pectins. Favors pectate, the anion, over pectin, the methyl ester (By similarity); Belongs to the polysaccharide lyase 1 family
[a.k.a. NFIA_060270, XM_001258567, Probable pectate lyase C]
Neosartorya fischeri
pelF -
Probable
pectin lyase F; Pectinolytic enzymes consist of four classes of enzymes: pectin lyase, polygalacturonase, pectin
methylesterase
and rhamnogalacturonase. Among pectinolytic enzymes, pectin lyase is the most important in depolymerization of pectin, since it cleaves internal glycosidic bonds of highly methylated pectins (By similarity)
[a.k.a. NFIA_077100, XM_001259673.1, XM_001259673]
Neosartorya fischeri
plyE -
Probable
pectate lyase E; Pectinolytic enzyme consist of four classes of enzymes: pectin lyase, polygalacturonase, pectin
methylesterase
and rhamnogalacturonase. Among pectinolytic enzymes, pectin lyase is the most important in depolymerization of pectin, since it cleaves internal glycosidic bonds of highly methylated pectins. Favors pectate, the anion, over pectin, the methyl ester (By similarity); Belongs to the polysaccharide lyase 3 family
[a.k.a. NFIA_098670, XP_001262134, XP_001262134.1]
Aspergillus terreus
ATEG_07577 -
Probable
pectin lyase F-1; Pectinolytic enzymes consist of four classes of enzymes: pectin lyase, polygalacturonase, pectin
methylesterase
and rhamnogalacturonase. Among pectinolytic enzymes, pectin lyase is the most important in depolymerization of pectin, since it cleaves internal glycosidic bonds of highly methylated pectins (By similarity)
[a.k.a. pelF-1, XP_001216198, CADATEAG00002786]
Aspergillus terreus
ATEG_00950 -
Probable
pectin lyase F-2; Pectinolytic enzymes consist of four classes of enzymes: pectin lyase, polygalacturonase, pectin
methylesterase
and rhamnogalacturonase. Among pectinolytic enzymes, pectin lyase is the most important in depolymerization of pectin, since it cleaves internal glycosidic bonds of highly methylated pectins (By similarity)
[a.k.a. pelF-2, Probable pectin lyase F-2, XP_001211036]
Aspergillus fumigatus
rrd2 - Serine/threonine-protein phosphatase 2A activator 2; PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides. Acts as a regulatory subunit for PP2A-like phosphatases modulating their activity or substrate specificity,
probably
by inducing a conformational change in the catalytic subunit, a direct target of the PPIase. Can reactivate inactive phosphatase PP2A-phosphatase
methylesterase
complexes (PP2Ai) in presence of ATP and Mg(2+) by dissociating the inactive form from the complex (By similarity)
[a.k.a. AfA34E6.015c, AFUA_1G13420, CADAFUBT00001296]
Aspergillus fumigatus
rrd1 - Serine/threonine-protein phosphatase 2A activator 1; PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides. Acts as a regulatory subunit for PP2A-like phosphatases modulating their activity or substrate specificity,
probably
by inducing a conformational change in the catalytic subunit, a direct target of the PPIase. Can reactivate inactive phosphatase PP2A-phosphatase
methylesterase
complexes (PP2Ai) in presence of ATP and Mg(2+) by dissociating the inactive form from the complex (By similarity)
[a.k.a. AFUA_6G08680, Peptidyl-prolyl cis-trans isomerase PTPA-1, CADAFUBG00007404]
Aspergillus nidulans
AN0679.2 - Serine/threonine-protein phosphatase 2A activator 2; PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides. Acts as a regulatory subunit for PP2A-like phosphatases modulating their activity or substrate specificity,
probably
by inducing a conformational change in the catalytic subunit, a direct target of the PPIase. Can reactivate inactive phosphatase PP2A-phosphatase
methylesterase
complexes (PP2Ai) in presence of ATP and Mg(2+) by dissociating the inactive form from the complex (By similarity)
[a.k.a. rrd2, AN10111, CADANIAT00001994]
Aspergillus nidulans
AN3905.2 - Serine/threonine-protein phosphatase 2A activator 1; PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides. Acts as a regulatory subunit for PP2A-like phosphatases modulating their activity or substrate specificity,
probably
by inducing a conformational change in the catalytic subunit, a direct target of the PPIase. Can reactivate inactive phosphatase PP2A-phosphatase
methylesterase
complexes (PP2Ai) in presence of ATP and Mg(2+) by dissociating the inactive form from the complex (By similarity)
[a.k.a. rrd1, AN3905, Q5B6C5]
Candida albicans
RRD1 - Serine/threonine-protein phosphatase 2A activator 1; PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides. Acts as a regulatory subunit for PP2A-like phosphatases modulating their activity or substrate specificity,
probably
by inducing a conformational change in the catalytic subunit, a direct target of the PPIase. Can reactivate inactive phosphatase PP2A-phosphatase
methylesterase
complexes (PP2Ai) in presence of ATP and Mg(2+) by dissociating the inactive form from the complex (By similarity)
[a.k.a. CAALFM_C307080WA, CaO19.6792, YPA1]
Candida albicans
RRD2 - Serine/threonine-protein phosphatase 2A activator 2; PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides. Acts as a regulatory subunit for PP2A-like phosphatases modulating their activity or substrate specificity,
probably
by inducing a conformational change in the catalytic subunit, a direct target of the PPIase. Can reactivate inactive phosphatase PP2A-phosphatase
methylesterase
complexes (PP2Ai) in presence of ATP and Mg(2+) by dissociating the inactive form from the complex (By similarity)
[a.k.a. CAALFM_C303830WA, CaO19.6933, CaO19.14195]
Candida glabrata
RRD1 - Serine/threonine-protein phosphatase 2A activator 1; PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides. Acts as a regulatory subunit for PP2A-like phosphatases modulating their activity or substrate specificity,
probably
by inducing a conformational change in the catalytic subunit, a direct target of the PPIase. Can reactivate inactive phosphatase PP2A-phosphatase
methylesterase
complexes (PP2Ai) in presence of ATP and Mg(2+) by dissociating the inactive form from the complex (By similarity)
[a.k.a. CAGL0H06655g, XP_447085.1, Q6FRQ9]
Candida glabrata
RRD2 - Serine/threonine-protein phosphatase 2A activator 2; PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides. Acts as a regulatory subunit for PP2A-like phosphatases modulating their activity or substrate specificity,
probably
by inducing a conformational change in the catalytic subunit, a direct target of the PPIase. Can reactivate inactive phosphatase PP2A-phosphatase
methylesterase
complexes (PP2Ai) in presence of ATP and Mg(2+) by dissociating the inactive form from the complex (By similarity)
[a.k.a. CAGL0M02255g, XP_449444.1, XP_449444]
Cryptococcus neoformans
RRD2 - Serine/threonine-protein phosphatase 2A activator 2; PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides. Acts as a regulatory subunit for PP2A-like phosphatases modulating their activity or substrate specificity,
probably
by inducing a conformational change in the catalytic subunit, a direct target of the PPIase. Can reactivate inactive phosphatase PP2A-phosphatase
methylesterase
complexes (PP2Ai) in presence of ATP and Mg(2+) by dissociating the inactive form from the complex (By similarity)
[a.k.a. CNH01590, Q55J30, CNH01590-1]
Cryptococcus neoformans
RRD1 - Serine/threonine-protein phosphatase 2A activator 1; PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides. Acts as a regulatory subunit for PP2A-like phosphatases modulating their activity or substrate specificity,
probably
by inducing a conformational change in the catalytic subunit, a direct target of the PPIase. Can reactivate inactive phosphatase PP2A-phosphatase
methylesterase
complexes (PP2Ai) in presence of ATP and Mg(2+) by dissociating the inactive form from the complex (By similarity)
[a.k.a. CNK00750, AAW46120, 3254580]
Debaryomyces hansenii
RRD2 - Serine/threonine-protein phosphatase 2A activator 2; PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides. Acts as a regulatory subunit for PP2A-like phosphatases modulating their activity or substrate specificity,
probably
by inducing a conformational change in the catalytic subunit, a direct target of the PPIase. Can reactivate inactive phosphatase PP2A-phosphatase
methylesterase
complexes (PP2Ai) in presence of ATP and Mg(2+) by dissociating the inactive form from the complex (By similarity)
[a.k.a. DEHA2C12584g, XP_458222.2, XM_458222.1]
Debaryomyces hansenii
RRD1 - Serine/threonine-protein phosphatase 2A activator 1; PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides. Acts as a regulatory subunit for PP2A-like phosphatases modulating their activity or substrate specificity,
probably
by inducing a conformational change in the catalytic subunit, a direct target of the PPIase. Can reactivate inactive phosphatase PP2A-phosphatase
methylesterase
complexes (PP2Ai) in presence of ATP and Mg(2+) by dissociating the inactive form from the complex (By similarity)
[a.k.a. DEHA2E18502g, XP_460106.2, GI:294657806]
Eremothecium gossypii
RRD2 - Serine/threonine-protein phosphatase 2A activator 2; PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides. Acts as a regulatory subunit for PP2A-like phosphatases modulating their activity or substrate specificity,
probably
by inducing a conformational change in the catalytic subunit, a direct target of the PPIase. Can reactivate inactive phosphatase PP2A-phosphatase
methylesterase
complexes (PP2Ai) in presence of ATP and Mg(2+) by dissociating the inactive form from the complex (By similarity)
[a.k.a. AGOS_ACR139C, ACR139C, AAS51365]
Eremothecium gossypii
RRD1 - Serine/threonine-protein phosphatase 2A activator 1; PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides. Acts as a regulatory subunit for PP2A-like phosphatases modulating their activity or substrate specificity,
probably
by inducing a conformational change in the catalytic subunit, a direct target of the PPIase. Can reactivate inactive phosphatase PP2A-phosphatase
methylesterase
complexes (PP2Ai) in presence of ATP and Mg(2+) by dissociating the inactive form from the complex (By similarity)
[a.k.a. AGOS_AFR293C, AFR293C, PTPA1_ASHGO]
Fusarium graminearum
FG01092.1 - Serine/threonine-protein phosphatase 2A activator 2; PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides. Acts as a regulatory subunit for PP2A-like phosphatases modulating their activity or substrate specificity,
probably
by inducing a conformational change in the catalytic subunit, a direct target of the PPIase. Can reactivate inactive phosphatase PP2A-phosphatase
methylesterase
complexes (PP2Ai) in presence of ATP and Mg(2+) by dissociating the inactive form from the complex (By similarity)
[a.k.a. RRD2, FGSG_01092, FGRRES_01092]
Fusarium graminearum
FG09229.1 - Serine/threonine-protein phosphatase 2A activator 1; PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides. Acts as a regulatory subunit for PP2A-like phosphatases modulating their activity or substrate specificity,
probably
by inducing a conformational change in the catalytic subunit, a direct target of the PPIase. Can reactivate inactive phosphatase PP2A-phosphatase
methylesterase
complexes (PP2Ai) in presence of ATP and Mg(2+) by dissociating the inactive form from the complex (By similarity)
[a.k.a. FGSG_09229, FGRRES_09229, RRD1]
Kluyveromyces lactis
RRD1 - Serine/threonine-protein phosphatase 2A activator 1; PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides. Acts as a regulatory subunit for PP2A-like phosphatases modulating their activity or substrate specificity,
probably
by inducing a conformational change in the catalytic subunit, a direct target of the PPIase. Can reactivate inactive phosphatase PP2A-phosphatase
methylesterase
complexes (PP2Ai) in presence of ATP and Mg(2+) by dissociating the inactive form from the complex (By similarity)
[a.k.a. KLLA0A00462g, XP_451018.1, PTPA1_KLULA]
Kluyveromyces lactis
RRD2 - Serine/threonine-protein phosphatase 2A activator 2; PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides. Acts as a regulatory subunit for PP2A-like phosphatases modulating their activity or substrate specificity,
probably
by inducing a conformational change in the catalytic subunit, a direct target of the PPIase. Can reactivate inactive phosphatase PP2A-phosphatase
methylesterase
complexes (PP2Ai) in presence of ATP and Mg(2+) by dissociating the inactive form from the complex (By similarity)
[a.k.a. KLLA0F11187g, XP_455589.1, XM_455589.1]
Schizosaccharomyces pombe
rrd2 - Serine/threonine-protein phosphatase 2A activator 2; PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides. Acts as a regulatory subunit for PP2A-like phosphatases modulating their activity or substrate specificity,
probably
by inducing a conformational change in the catalytic subunit, a direct target of the PPIase. Can reactivate inactive phosphatase PP2A-phosphatase
methylesterase
complexes (PP2Ai) in presence of ATP and Mg(2+) by dissociating the inactive form from the complex (By similarity)
[a.k.a. SPAC1782.05, spo:SPAC1782.05, RRD2]
Schizosaccharomyces pombe
rrd1 - Serine/threonine-protein phosphatase 2A activator 1; PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides. Acts as a regulatory subunit for PP2A-like phosphatases modulating their activity or substrate specificity,
probably
by inducing a conformational change in the catalytic subunit, a direct target of the PPIase. Can reactivate inactive phosphatase PP2A-phosphatase
methylesterase
complexes (PP2Ai) in presence of ATP and Mg(2+) by dissociating the inactive form from the complex (By similarity)
[a.k.a. SPAC4F10.04, SPAC4F10.04.1, NP_594747.1]
Ustilago maydis
UM02103.1 - Serine/threonine-protein phosphatase 2A activator 2; PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides. Acts as a regulatory subunit for PP2A-like phosphatases modulating their activity or substrate specificity,
probably
by inducing a conformational change in the catalytic subunit, a direct target of the PPIase. Can reactivate inactive phosphatase PP2A-phosphatase
methylesterase
complexes (PP2Ai) in presence of ATP and Mg(2+) by dissociating the inactive form from the complex (By similarity)
[a.k.a. RRD2, UMAG_02103, EAK83158.1]
Ustilago maydis
UM04850.1 - Serine/threonine-protein phosphatase 2A activator 1; PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides. Acts as a regulatory subunit for PP2A-like phosphatases modulating their activity or substrate specificity,
probably
by inducing a conformational change in the catalytic subunit, a direct target of the PPIase. Can reactivate inactive phosphatase PP2A-phosphatase
methylesterase
complexes (PP2Ai) in presence of ATP and Mg(2+) by dissociating the inactive form from the complex (By similarity)
[a.k.a. UMAG_04850, RRD1, UM04850P0]
Bos taurus
PPP2R4 - Serine/threonine-protein phosphatase 2A activator; PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides. Acts as a regulatory subunit for serine/threonine- protein phosphatase 2A (PP2A) modulating its activity or substrate specificity,
probably
by inducing a conformational change in the catalytic subunit, a proposed direct target of the PPIase. Can reactivate inactive phosphatase PP2A-phosphatase
methylesterase
complexes (PP2A(i)) in presence of ATP and Mg(2+) (By similarity). Reversibly stimulates the var [...]
[a.k.a. PTPA, NM_001046173, XP_005213309]
Oryctolagus cuniculus
PPP2R4 - Serine/threonine-protein phosphatase 2A activator; PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides. Acts as a regulatory subunit for serine/threonine- protein phosphatase 2A (PP2A) modulating its activity or substrate specificity,
probably
by inducing a conformational change in the catalytic subunit, a proposed direct target of the PPIase. Can reactivate inactive phosphatase PP2A-phosphatase
methylesterase
complexes (PP2A(i)) in presence of ATP and Mg(2+). Reversibly stimulates the variable phosphotyr [...]
[a.k.a. PTPA, G1TX59, ENSOCUT00000021358]
Arabidopsis thaliana
MES16 -
Probable
pheophorbidase; Encodes a protein shown to have carboxylesterase activity, methyl IAA esterase activity, and methyl jasmonate esterase activity in vitro. This protein does not act on MeSA, MeGA4, or MEGA9 in vitro. Although MES16 is similar to MES17, a MeIAA hydrolase, two mes16 mutant lines (SALK_151578) and (SALK_139756) do not show altered sensitivity to MeIAA in root growth assays. MES16 transcripts appear to be more than 10-fold less abundant than those of MES17 in roots; Belongs to the AB hydrolase superfamily.
Methylesterase
family
[a.k.a. At4g16690, PPD, FCAALL.12]