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DFI_11880 DFI_11880 DFI_13745 DFI_13745 cysS cysS leuS leuS truD truD DFI_06540 DFI_06540 gluQ gluQ ileS ileS hisS hisS aspS-2 aspS-2 asnS asnS miaA miaA DFI_07030 DFI_07030 argS argS aspS aspS trmD trmD DFI_07745 DFI_07745 valS valS gltX gltX rlmN rlmN proS-2 proS-2 kptA kptA proS proS glyQS glyQS DFI_10515 DFI_10515 queA queA thrS thrS hisZ hisZ dtd dtd gatA gatA trmB trmB fmt fmt pheT pheT pheS pheS tgt tgt GCA_000419625_01406 GCA_000419625_01406 DFI_12865 DFI_12865 lysS lysS pth pth tyrS tyrS DFI_00040 DFI_00040 DFI_00645 DFI_00645 truA truA DFI_00800 DFI_00800 trmH trmH DFI_01610 DFI_01610 DFI_01710 DFI_01710 rph rph DFI_02145 DFI_02145 DFI_02430 DFI_02430 gatB gatB DFI_02870 DFI_02870 gatC gatC hemA hemA trmFO trmFO DFI_04465 DFI_04465 truB truB alaS alaS trmJ trmJ metG metG trpS trpS
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second shell of interactors
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proteins of unknown 3D structure
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a 3D structure is known or predicted
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DFI_11880Ribonuclease P protein component; RNaseP catalyzes the removal of the 5'-leader sequence from pre-tRNA to produce the mature 5'-terminus. It can also cleave other RNA substrates such as 4.5S RNA. The protein component plays an auxiliary but essential role in vivo by binding to the 5'-leader sequence and broadening the substrate specificity of the ribozyme. (163 aa)
DFI_13745Methionine--tRNA ligase; Belongs to the class-I aminoacyl-tRNA synthetase family. (518 aa)
cysSCysteine--tRNA ligase; Belongs to the class-I aminoacyl-tRNA synthetase family. (491 aa)
leuSLeucine--tRNA ligase; Belongs to the class-I aminoacyl-tRNA synthetase family. (826 aa)
truDtRNA pseudouridine synthase D; Responsible for synthesis of pseudouridine from uracil-13 in transfer RNAs; Belongs to the pseudouridine synthase TruD family. (364 aa)
DFI_06540Serine-tRNA(Ala) deacylase AlaX. (406 aa)
gluQGlutamyl-Q tRNA(Asp) synthetase; Catalyzes the tRNA-independent activation of glutamate in presence of ATP and the subsequent transfer of glutamate onto a tRNA(Asp). Glutamate is transferred on the 2-amino-5-(4,5-dihydroxy-2- cyclopenten-1-yl) moiety of the queuosine in the wobble position of the QUC anticodon; Belongs to the class-I aminoacyl-tRNA synthetase family. GluQ subfamily. (298 aa)
ileSIsoleucine--tRNA ligase; Catalyzes the attachment of isoleucine to tRNA(Ile). As IleRS can inadvertently accommodate and process structurally similar amino acids such as valine, to avoid such errors it has two additional distinct tRNA(Ile)-dependent editing activities. One activity is designated as 'pretransfer' editing and involves the hydrolysis of activated Val-AMP. The other activity is designated 'posttransfer' editing and involves deacylation of mischarged Val-tRNA(Ile). Belongs to the class-I aminoacyl-tRNA synthetase family. IleS type 2 subfamily. (1063 aa)
hisSHistidine--tRNA ligase. (441 aa)
aspS-2Aspartate--tRNA ligase; Catalyzes the attachment of L-aspartate to tRNA(Asp) in a two-step reaction: L-aspartate is first activated by ATP to form Asp- AMP and then transferred to the acceptor end of tRNA(Asp). Belongs to the class-II aminoacyl-tRNA synthetase family. Type 1 subfamily. (580 aa)
asnSAsparagine--tRNA ligase. (444 aa)
miaAtRNA dimethylallyltransferase; Catalyzes the transfer of a dimethylallyl group onto the adenine at position 37 in tRNAs that read codons beginning with uridine, leading to the formation of N6-(dimethylallyl)adenosine (i(6)A); Belongs to the IPP transferase family. (307 aa)
DFI_07030Uncharacterized protein. (173 aa)
argSArginine--tRNA ligase. (615 aa)
aspSAspartate--tRNA(Asp/Asn) ligase; Aspartyl-tRNA synthetase with relaxed tRNA specificity since it is able to aspartylate not only its cognate tRNA(Asp) but also tRNA(Asn). Reaction proceeds in two steps: L-aspartate is first activated by ATP to form Asp-AMP and then transferred to the acceptor end of tRNA(Asp/Asn); Belongs to the class-II aminoacyl-tRNA synthetase family. Type 2 subfamily. (452 aa)
trmDtRNA (guanine-N(1)-)-methyltransferase; Specifically methylates guanosine-37 in various tRNAs. Belongs to the RNA methyltransferase TrmD family. (271 aa)
DFI_07745Amidase. (461 aa)
valSValine--tRNA ligase; Catalyzes the attachment of valine to tRNA(Val). As ValRS can inadvertently accommodate and process structurally similar amino acids such as threonine, to avoid such errors, it has a 'posttransfer' editing activity that hydrolyzes mischarged Thr-tRNA(Val) in a tRNA- dependent manner; Belongs to the class-I aminoacyl-tRNA synthetase family. ValS type 1 subfamily. (917 aa)
gltXGlutamate--tRNA ligase; Catalyzes the attachment of glutamate to tRNA(Glu) in a two- step reaction: glutamate is first activated by ATP to form Glu-AMP and then transferred to the acceptor end of tRNA(Glu); Belongs to the class-I aminoacyl-tRNA synthetase family. Glutamate--tRNA ligase type 1 subfamily. (477 aa)
rlmNProbable dual-specificity RNA methyltransferase RlmN; Specifically methylates position 2 of adenine 2503 in 23S rRNA and position 2 of adenine 37 in tRNAs; Belongs to the radical SAM superfamily. RlmN family. (343 aa)
proS-2Proline--tRNA ligase; Catalyzes the attachment of proline to tRNA(Pro) in a two- step reaction: proline is first activated by ATP to form Pro-AMP and then transferred to the acceptor end of tRNA(Pro). As ProRS can inadvertently accommodate and process non-cognate amino acids such as alanine and cysteine, to avoid such errors it has two additional distinct editing activities against alanine. One activity is designated as 'pretransfer' editing and involves the tRNA(Pro)-independent hydrolysis of activated Ala-AMP. The other activity is designated 'posttransfer' editing and involves deacy [...] (594 aa)
kptAProbable RNA 2'-phosphotransferase; Removes the 2'-phosphate from RNA via an intermediate in which the phosphate is ADP-ribosylated by NAD followed by a presumed transesterification to release the RNA and generate ADP-ribose 1''-2''- cyclic phosphate (APPR>P). May function as an ADP-ribosylase. (173 aa)
proSProline--tRNA ligase; Catalyzes the attachment of proline to tRNA(Pro) in a two- step reaction: proline is first activated by ATP to form Pro-AMP and then transferred to the acceptor end of tRNA(Pro). (497 aa)
glyQSGlycine--tRNA ligase; Catalyzes the attachment of glycine to tRNA(Gly). Belongs to the class-II aminoacyl-tRNA synthetase family. (504 aa)
DFI_10515tRNA-dihydrouridine(20/20a) synthase; Catalyzes the synthesis of 5,6-dihydrouridine (D), a modified base found in the D-loop of most tRNAs, via the reduction of the C5-C6 double bond in target uridines. Specifically modifies U20 and U20a in tRNAs; Belongs to the Dus family. DusA subfamily. (318 aa)
queAS-adenosylmethionine:tRNA ribosyltransferase-isomerase; Transfers and isomerizes the ribose moiety from AdoMet to the 7-aminomethyl group of 7-deazaguanine (preQ1-tRNA) to give epoxyqueuosine (oQ-tRNA). (350 aa)
thrSThreonine--tRNA ligase; Catalyzes the attachment of threonine to tRNA(Thr) in a two- step reaction: L-threonine is first activated by ATP to form Thr-AMP and then transferred to the acceptor end of tRNA(Thr). (649 aa)
hisZATP phosphoribosyltransferase regulatory subunit; Required for the first step of histidine biosynthesis. May allow the feedback regulation of ATP phosphoribosyltransferase activity by histidine. (370 aa)
dtdD-aminoacyl-tRNA deacylase; An aminoacyl-tRNA editing enzyme that deacylates mischarged D-aminoacyl-tRNAs. Also deacylates mischarged glycyl-tRNA(Ala), protecting cells against glycine mischarging by AlaRS. Acts via tRNA- based rather than protein-based catalysis; rejects L-amino acids rather than detecting D-amino acids in the active site. By recycling D- aminoacyl-tRNA to D-amino acids and free tRNA molecules, this enzyme counteracts the toxicity associated with the formation of D-aminoacyl- tRNA entities in vivo and helps enforce protein L-homochirality. Belongs to the DTD family. (148 aa)
gatAGlutamyl-tRNA(Gln) amidotransferase subunit A; Allows the formation of correctly charged Gln-tRNA(Gln) through the transamidation of misacylated Glu-tRNA(Gln) in organisms which lack glutaminyl-tRNA synthetase. The reaction takes place in the presence of glutamine and ATP through an activated gamma-phospho-Glu- tRNA(Gln). (485 aa)
trmBtRNA (guanine-N(7)-)-methyltransferase; Catalyzes the formation of N(7)-methylguanine at position 46 (m7G46) in tRNA. (332 aa)
fmtMethionyl-tRNA formyltransferase; Attaches a formyl group to the free amino group of methionyl- tRNA(fMet). The formyl group appears to play a dual role in the initiator identity of N-formylmethionyl-tRNA by promoting its recognition by IF2 and preventing the misappropriation of this tRNA by the elongation apparatus; Belongs to the Fmt family. (319 aa)
pheTPhenylalanine--tRNA ligase beta subunit; Belongs to the phenylalanyl-tRNA synthetase beta subunit family. Type 1 subfamily. (821 aa)
pheSPhenylalanine--tRNA ligase alpha subunit; Belongs to the class-II aminoacyl-tRNA synthetase family. Phe-tRNA synthetase alpha subunit type 1 subfamily. (339 aa)
tgtQueuine tRNA-ribosyltransferase; Catalyzes the base-exchange of a guanine (G) residue with the queuine precursor 7-aminomethyl-7-deazaguanine (PreQ1) at position 34 (anticodon wobble position) in tRNAs with GU(N) anticodons (tRNA-Asp, - Asn, -His and -Tyr). Catalysis occurs through a double-displacement mechanism. The nucleophile active site attacks the C1' of nucleotide 34 to detach the guanine base from the RNA, forming a covalent enzyme-RNA intermediate. The proton acceptor active site deprotonates the incoming PreQ1, allowing a nucleophilic attack on the C1' of the ribose to form t [...] (384 aa)
GCA_000419625_01406annotation not available (152 aa)
DFI_12865Glutamine--tRNA ligase. (801 aa)
lysSLysine--tRNA ligase; Belongs to the class-II aminoacyl-tRNA synthetase family. (517 aa)
pthPeptidyl-tRNA hydrolase; The natural substrate for this enzyme may be peptidyl-tRNAs which drop off the ribosome during protein synthesis. Belongs to the PTH family. (220 aa)
tyrSTyrosine--tRNA ligase; Catalyzes the attachment of tyrosine to tRNA(Tyr) in a two- step reaction: tyrosine is first activated by ATP to form Tyr-AMP and then transferred to the acceptor end of tRNA(Tyr); Belongs to the class-I aminoacyl-tRNA synthetase family. TyrS type 2 subfamily. (431 aa)
DFI_00040tRNA (Adenine-N(1))-methyltransferase. (231 aa)
DFI_00645Tryptophan--tRNA ligase; Belongs to the class-I aminoacyl-tRNA synthetase family. (342 aa)
truAtRNA pseudouridine synthase A; Formation of pseudouridine at positions 38, 39 and 40 in the anticodon stem and loop of transfer RNAs. (265 aa)
DFI_00800SAM-dependent methyltransferase. (221 aa)
trmHtRNA (guanosine(18)-2'-O)-methyltransferase; Catalyzes the 2'-O methylation of guanosine at position 18 in tRNA; Belongs to the class IV-like SAM-binding methyltransferase superfamily. RNA methyltransferase TrmH family. (222 aa)
DFI_01610Putative tRNA (cytidine(34)-2'-O)-methyltransferase; Could methylate the ribose at the nucleotide 34 wobble position in tRNA; Belongs to the class IV-like SAM-binding methyltransferase superfamily. RNA methyltransferase TrmH family. TrmL subfamily. (161 aa)
DFI_01710tRNA-dihydrouridine synthase; Catalyzes the synthesis of 5,6-dihydrouridine (D), a modified base found in the D-loop of most tRNAs, via the reduction of the C5-C6 double bond in target uridines; Belongs to the dus family. (339 aa)
rphRibonuclease PH; Phosphorolytic 3'-5' exoribonuclease that plays an important role in tRNA 3'-end maturation. Removes nucleotide residues following the 3'-CCA terminus of tRNAs; can also add nucleotides to the ends of RNA molecules by using nucleoside diphosphates as substrates, but this may not be physiologically important. Probably plays a role in initiation of 16S rRNA degradation (leading to ribosome degradation) during starvation. (252 aa)
DFI_02145RNA methyltransferase. (370 aa)
DFI_02430Ribonuclease Z. (332 aa)
gatBAspartyl/glutamyl-tRNA(Asn/Gln) amidotransferase subunit B; Allows the formation of correctly charged Asn-tRNA(Asn) or Gln-tRNA(Gln) through the transamidation of misacylated Asp-tRNA(Asn) or Glu-tRNA(Gln) in organisms which lack either or both of asparaginyl- tRNA or glutaminyl-tRNA synthetases. The reaction takes place in the presence of glutamine and ATP through an activated phospho-Asp- tRNA(Asn) or phospho-Glu-tRNA(Gln); Belongs to the GatB/GatE family. GatB subfamily. (480 aa)
DFI_02870Serine--tRNA ligase. (425 aa)
gatCAspartyl/glutamyl-tRNA(Asn/Gln) amidotransferase subunit C; Allows the formation of correctly charged Asn-tRNA(Asn) or Gln-tRNA(Gln) through the transamidation of misacylated Asp-tRNA(Asn) or Glu-tRNA(Gln) in organisms which lack either or both of asparaginyl- tRNA or glutaminyl-tRNA synthetases. The reaction takes place in the presence of glutamine and ATP through an activated phospho-Asp- tRNA(Asn) or phospho-Glu-tRNA(Gln); Belongs to the GatC family. (96 aa)
hemAGlutamyl-tRNA reductase; Catalyzes the NADPH-dependent reduction of glutamyl-tRNA(Glu) to glutamate 1-semialdehyde (GSA). (367 aa)
trmFOMethylenetetrahydrofolate--tRNA-(uracil-5-)-methyltransferase TrmFO; Catalyzes the folate-dependent formation of 5-methyl-uridine at position 54 (M-5-U54) in all tRNAs; Belongs to the MnmG family. TrmFO subfamily. (467 aa)
DFI_04465Uncharacterized protein. (556 aa)
truBtRNA pseudouridine synthase B; Responsible for synthesis of pseudouridine from uracil-55 in the psi GC loop of transfer RNAs; Belongs to the pseudouridine synthase TruB family. Type 1 subfamily. (318 aa)
alaSAlanine--tRNA ligase; Catalyzes the attachment of alanine to tRNA(Ala) in a two- step reaction: alanine is first activated by ATP to form Ala-AMP and then transferred to the acceptor end of tRNA(Ala). Also edits incorrectly charged Ser-tRNA(Ala) and Gly-tRNA(Ala) via its editing domain. (878 aa)
trmJtRNA (cytidine/uridine-2'-O-)-methyltransferase TrmJ; Catalyzes the formation of 2'O-methylated cytidine (Cm32) or 2'O-methylated uridine (Um32) at position 32 in tRNA. (256 aa)
metGMethionine--tRNA ligase; Is required not only for elongation of protein synthesis but also for the initiation of all mRNA translation through initiator tRNA(fMet) aminoacylation; Belongs to the class-I aminoacyl-tRNA synthetase family. MetG type 2B subfamily. (666 aa)
trpSTryptophan--tRNA ligase; Catalyzes the attachment of tryptophan to tRNA(Trp). Belongs to the class-I aminoacyl-tRNA synthetase family. (332 aa)
Your Current Organism:
Deinococcus ficus
NCBI taxonomy Id: 317577
Other names: CCUG 51391, CIP 108832, D. ficus, DSM 17424 [[Deinococcus mumbaiensis Shashidhar and Bandekar 2006]], DSM 19119, Deinococcus ficus Lai et al. 2006 emend. Kampfer 2009, Deinococcus mumbaiensis, Deinococcus mumbaiensis Shashidhar and Bandekar 2006, Deinococcus sp. 2009, Deinococcus sp. CC-FR2-10, Deinococcus sp. UK, MTCC 7297 [[Deinococcus mumbaiensis Shashidhar and Bandekar 2006]], strain CC-FR2-10, strain CON-1 [[Deinococcus mumbaiensis Shashidhar and Bandekar 2006]]
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