Tag | Content |
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CPLM ID | CPLM-001726 |
UniProt Accession | |
Genbank Protein ID | |
Genbank Nucleotide ID | |
Protein Name | Cytochrome c' |
Protein Synonyms/Alias | |
Gene Name | cycA |
Gene Synonyms/Alias | RPA2314 |
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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118 | TAAQGTIKDEASLKA | 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 | Cytochrome c' is the most widely occurring bacterial c- type cytochrome. Cytochromes c' are high-spin proteins and the heme has no sixth ligand. Their exact function is not known. |
Sequence Annotation | METAL 138 138 Iron (heme axial ligand). BINDING 134 134 Heme (covalent). BINDING 137 137 Heme (covalent). |
Keyword | 3D-structure; Complete proteome; Direct protein sequencing; Electron transport; Heme; Iron; Metal-binding; Signal; Transport. |
Sequence Source | UniProt (SWISSPROT/TrEMBL); GenBank; EMBL |
Protein Length | 146 AA |
Protein Sequence | MKLRIATIAG LVVLGSGFAV AQTDVIAQRK AILKQMGEAT KPIAAMLKGE AKFDQAVVQK 60 SLAAIADDSK KLPALFPADS KTGGDTAALP KIWEDKAKFD DLFAKLAAAA TAAQGTIKDE 120 ASLKANIGGV LGNCKSCHDD FRAKKS 146 |
Gene Ontology | |
Interpro | |
Pfam | |
SMART | |
PROSITE | |
PRINTS | |