Tag | Content |
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CPLM ID | CPLM-026695 |
UniProt Accession | |
Genbank Protein ID | |
Genbank Nucleotide ID | |
Protein Name | Putative biotin-protein ligase birA |
Protein Synonyms/Alias | |
Gene Name | birA |
Gene Synonyms/Alias | RPA2936 |
Created Date | July 27, 2013 |
Organism | Rhodopseudomonas palustris (strain ATCC BAA-98 / CGA009) |
NCBI Taxa ID | 258594 |
Lysine Modification | Position | Peptide | Type | References |
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117 | TDFGFRLKWPNDVLA | acetylation | [1] |
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Reference | [1] System-wide studies of N-lysine acetylation in Rhodopseudomonas palustris reveal substrate specificity of protein acetyltransferases. Crosby HA, Pelletier DA, Hurst GB, Escalante-Semerena JC. J Biol Chem. 2012 May 4;287(19):15590-601. [ PMID: 22416131] |
Functional Description | |
Sequence Annotation | |
Keyword | Complete proteome; Ligase. |
Sequence Source | UniProt (SWISSPROT/TrEMBL); GenBank; EMBL |
Protein Length | 268 AA |
Protein Sequence | MTALHLGSKA AAAGYKLAAF DSTGSTNAEA LASARAGEAG PMWFVTTEQT AGRGRRQRAW 60 IAPRGNLASS VLEVMRVPPG TAATLGFAAG LALEAALQQV SLEARARSGT DFGFRLKWPN 120 DVLASGKKLA GILLEVENVG DRLAVVVGIG TNVIAAPTDT PYPAVSLHDL GISVTAEDLF 180 AALSDAWTEL LGIWDNGRGF PEIRRRWLER AAGLGEPVSI RSGDSALEGV FDSIDDTGCL 240 IVRTTDGRRV PVSAGDVYFK GVASMGAA 268 |
Gene Ontology | GO:0004077; F:biotin-[acetyl-CoA-carboxylase] ligase activity; IEA:EC. GO:0006464; P:cellular protein modification process; IEA:InterPro. |
Interpro | |
Pfam | |
SMART | |
PROSITE | |
PRINTS | |