node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
Cj0390 | alaS | Cj0390 | Cj0506 | Original (2000) note: Cj0390, possible transmembrane protein, len: 820 aa; 28.7% identity in 703 aa overlap to HP1479. Contains possible transmembrane domain around aa 100 and Pfam match to entry PF00515 TPR,TPR Domain, score 26.90, E-value 0.00047; Updated (2006) note: Pfam domains x4 PF07719 Tetratricopeptide repeat were identified within CDS. Functional classification - Membranes, lipoproteins and porins. | alanyl-tRNA synthetase; 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. | 0.980 |
Cj0390 | napL | Cj0390 | Cj0784 | Original (2000) note: Cj0390, possible transmembrane protein, len: 820 aa; 28.7% identity in 703 aa overlap to HP1479. Contains possible transmembrane domain around aa 100 and Pfam match to entry PF00515 TPR,TPR Domain, score 26.90, E-value 0.00047; Updated (2006) note: Pfam domains x4 PF07719 Tetratricopeptide repeat were identified within CDS. Functional classification - Membranes, lipoproteins and porins. | Putative periplasmic protein; Original (2000) note: Cj0784, probable periplasmic protein, len: 304 aa; no Hp match. Contains N-terminal signal sequence; Updated (2006) note: Some characterisation work within Wolinella succinogenes with acceptable identity score. Functional classification - Miscellaneous periplasmic proteins; PMID:12823811. | 0.978 |
Cj0497 | alaS | Cj0497 | Cj0506 | Putative lipoprotein; Original (2000) note: Cj0497, probable lipoprotein,len: 425 aa; some similarity to hypothetical prteins e.g. TR:O67021 (EMBL:AE000710) Aquifex aeolicus AQ_854 (545 aa), fasta scores; opt: 266 z-score: 326.7 E(): 6.7e-11,29.1% identity in 412 aa overlap. 26.7% identity to HP0275 (misannotated as ATP-dependent nuclease (addB)). Contains N-terminal signal sequence and PS00013 Prokaryotic membrane lipoprotein lipid attachment site. Functional classification - Membranes, lipoproteins and porins. | alanyl-tRNA synthetase; 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. | 0.978 |
Cj0497 | napL | Cj0497 | Cj0784 | Putative lipoprotein; Original (2000) note: Cj0497, probable lipoprotein,len: 425 aa; some similarity to hypothetical prteins e.g. TR:O67021 (EMBL:AE000710) Aquifex aeolicus AQ_854 (545 aa), fasta scores; opt: 266 z-score: 326.7 E(): 6.7e-11,29.1% identity in 412 aa overlap. 26.7% identity to HP0275 (misannotated as ATP-dependent nuclease (addB)). Contains N-terminal signal sequence and PS00013 Prokaryotic membrane lipoprotein lipid attachment site. Functional classification - Membranes, lipoproteins and porins. | Putative periplasmic protein; Original (2000) note: Cj0784, probable periplasmic protein, len: 304 aa; no Hp match. Contains N-terminal signal sequence; Updated (2006) note: Some characterisation work within Wolinella succinogenes with acceptable identity score. Functional classification - Miscellaneous periplasmic proteins; PMID:12823811. | 0.978 |
Cj1472c | alaS | Cj1472c | Cj0506 | Putative membrane protein; Original (2000) note: Cj1472c, probable membrane protein, len: 195 aa; no Hp match; Updated (2006) note: One probable transmembrane helix predicted by TMHMM2.0. Literature search identified paper giving further clues to product function. Functional classification - Membranes, lipoproteins and porins; PMID:12949093. | alanyl-tRNA synthetase; 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. | 0.978 |
Cj1472c | napL | Cj1472c | Cj0784 | Putative membrane protein; Original (2000) note: Cj1472c, probable membrane protein, len: 195 aa; no Hp match; Updated (2006) note: One probable transmembrane helix predicted by TMHMM2.0. Literature search identified paper giving further clues to product function. Functional classification - Membranes, lipoproteins and porins; PMID:12949093. | Putative periplasmic protein; Original (2000) note: Cj0784, probable periplasmic protein, len: 304 aa; no Hp match. Contains N-terminal signal sequence; Updated (2006) note: Some characterisation work within Wolinella succinogenes with acceptable identity score. Functional classification - Miscellaneous periplasmic proteins; PMID:12823811. | 0.978 |
alaS | Cj0390 | Cj0506 | Cj0390 | alanyl-tRNA synthetase; 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. | Original (2000) note: Cj0390, possible transmembrane protein, len: 820 aa; 28.7% identity in 703 aa overlap to HP1479. Contains possible transmembrane domain around aa 100 and Pfam match to entry PF00515 TPR,TPR Domain, score 26.90, E-value 0.00047; Updated (2006) note: Pfam domains x4 PF07719 Tetratricopeptide repeat were identified within CDS. Functional classification - Membranes, lipoproteins and porins. | 0.980 |
alaS | Cj0497 | Cj0506 | Cj0497 | alanyl-tRNA synthetase; 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. | Putative lipoprotein; Original (2000) note: Cj0497, probable lipoprotein,len: 425 aa; some similarity to hypothetical prteins e.g. TR:O67021 (EMBL:AE000710) Aquifex aeolicus AQ_854 (545 aa), fasta scores; opt: 266 z-score: 326.7 E(): 6.7e-11,29.1% identity in 412 aa overlap. 26.7% identity to HP0275 (misannotated as ATP-dependent nuclease (addB)). Contains N-terminal signal sequence and PS00013 Prokaryotic membrane lipoprotein lipid attachment site. Functional classification - Membranes, lipoproteins and porins. | 0.978 |
alaS | Cj1472c | Cj0506 | Cj1472c | alanyl-tRNA synthetase; 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. | Putative membrane protein; Original (2000) note: Cj1472c, probable membrane protein, len: 195 aa; no Hp match; Updated (2006) note: One probable transmembrane helix predicted by TMHMM2.0. Literature search identified paper giving further clues to product function. Functional classification - Membranes, lipoproteins and porins; PMID:12949093. | 0.978 |
alaS | ileS | Cj0506 | Cj1061c | alanyl-tRNA synthetase; 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. | isoleucyl-tRNA synthetase; 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 1 subfamily. | 0.866 |
alaS | leuS | Cj0506 | Cj1091c | alanyl-tRNA synthetase; 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. | leucyl-tRNA synthetase; Original (2000) note: Cj1091c, leuS, probable leucyl-tRNA synthetase, len: 809 aa; similar to many e.g. SYL_ECOLI leucyl-tRNA synthetase (EC 6.1.1.4) (860 aa),fasta scores; opt: 1941 z-score: 2210.5 E(): 0, 44.1% identity in 869 aa overlap. 62.7% identity to HP1547. Contains PS00017 ATP/GTP-binding site motif A (P-loop),PS00178 Aminoacyl-transfer RNA synthetases class-I signature, and Pfam match to entry PF00133 tRNA-synt_1,tRNA synthetases class I; Updated (2006) note: Characterised in Escherichia coli with acceptable identity score. Putative not added to produ [...] | 0.884 |
alaS | metS | Cj0506 | Cj0838c | alanyl-tRNA synthetase; 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. | methionyl-tRNA synthetase; Is required not only for elongation of protein synthesis but also for the initiation of all mRNA translation through initiator tRNA(fMet) aminoacylation. | 0.852 |
alaS | napL | Cj0506 | Cj0784 | alanyl-tRNA synthetase; 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. | Putative periplasmic protein; Original (2000) note: Cj0784, probable periplasmic protein, len: 304 aa; no Hp match. Contains N-terminal signal sequence; Updated (2006) note: Some characterisation work within Wolinella succinogenes with acceptable identity score. Functional classification - Miscellaneous periplasmic proteins; PMID:12823811. | 0.997 |
alaS | pheT | Cj0506 | Cj0896c | alanyl-tRNA synthetase; 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. | Original (2000) note: Cj0896c, pheT, probable phenylalanyl-tRNA synthetase beta chain, len: 773 aa; similar to many e.g. SYFB_ECOLI phenylalanyl-tRNA synthetase beta chain (EC 6.1.1.20) (795 aa), fasta scores; opt: 585 z-score: 663.2 E(): 1.2e-29, 27.8% identity in 802 aa overlap. 36.0% identity to HP0402; Updated (2006) note: Pfam domains PF03484 tRNA synthetase B5 domain, PF03483 B3/4 domain and PF01588 Putative tRNA binding domain were identified within CDS. Further support given to product function. Characterised in Escherichia coli with marginal identity score. Appropriate motfis [...] | 0.899 |
alaS | thrS | Cj0506 | Cj0206 | alanyl-tRNA synthetase; 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. | threonyl-tRNA synthetase; 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). Also edits incorrectly charged L-seryl-tRNA(Thr). | 0.857 |
alaS | valS | Cj0506 | Cj0775c | alanyl-tRNA synthetase; 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. | valyl-tRNA synthetase; 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. | 0.825 |
ileS | alaS | Cj1061c | Cj0506 | isoleucyl-tRNA synthetase; 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 1 subfamily. | alanyl-tRNA synthetase; 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. | 0.866 |
ileS | leuS | Cj1061c | Cj1091c | isoleucyl-tRNA synthetase; 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 1 subfamily. | leucyl-tRNA synthetase; Original (2000) note: Cj1091c, leuS, probable leucyl-tRNA synthetase, len: 809 aa; similar to many e.g. SYL_ECOLI leucyl-tRNA synthetase (EC 6.1.1.4) (860 aa),fasta scores; opt: 1941 z-score: 2210.5 E(): 0, 44.1% identity in 869 aa overlap. 62.7% identity to HP1547. Contains PS00017 ATP/GTP-binding site motif A (P-loop),PS00178 Aminoacyl-transfer RNA synthetases class-I signature, and Pfam match to entry PF00133 tRNA-synt_1,tRNA synthetases class I; Updated (2006) note: Characterised in Escherichia coli with acceptable identity score. Putative not added to produ [...] | 0.992 |
ileS | metS | Cj1061c | Cj0838c | isoleucyl-tRNA synthetase; 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 1 subfamily. | methionyl-tRNA synthetase; Is required not only for elongation of protein synthesis but also for the initiation of all mRNA translation through initiator tRNA(fMet) aminoacylation. | 0.994 |
ileS | pheT | Cj1061c | Cj0896c | isoleucyl-tRNA synthetase; 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 1 subfamily. | Original (2000) note: Cj0896c, pheT, probable phenylalanyl-tRNA synthetase beta chain, len: 773 aa; similar to many e.g. SYFB_ECOLI phenylalanyl-tRNA synthetase beta chain (EC 6.1.1.20) (795 aa), fasta scores; opt: 585 z-score: 663.2 E(): 1.2e-29, 27.8% identity in 802 aa overlap. 36.0% identity to HP0402; Updated (2006) note: Pfam domains PF03484 tRNA synthetase B5 domain, PF03483 B3/4 domain and PF01588 Putative tRNA binding domain were identified within CDS. Further support given to product function. Characterised in Escherichia coli with marginal identity score. Appropriate motfis [...] | 0.983 |