Tag | Content |
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CPLM ID | CPLM-001724 |
UniProt Accession | |
Genbank Protein ID | |
Genbank Nucleotide ID | |
Protein Name | Cytochrome c2 |
Protein Synonyms/Alias | |
Gene Name | cycA |
Gene Synonyms/Alias | RPA1535 |
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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46 | MTCHRADKNMVGPAL | acetylation | [1] | 129 | LANEQQRKDVVAYLA | 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 c2 is found mainly in purple, non-sulfur, photosynthetic bacteria where it functions as the electron donor to the oxidized bacteriochlorophyll in the photophosphorylation pathway. However, it may also have a role in the respiratory chain and is found in some non-photosynthetic bacteria. |
Sequence Annotation | METAL 42 42 Iron (heme axial ligand). METAL 118 118 Iron (heme axial ligand). BINDING 38 38 Heme (covalent). BINDING 41 41 Heme (covalent). MOD_RES 26 26 Pyrrolidone carboxylic acid. |
Keyword | 3D-structure; Complete proteome; Direct protein sequencing; Electron transport; Heme; Iron; Metal-binding; Photosynthesis; Pyrrolidone carboxylic acid; Signal; Transport. |
Sequence Source | UniProt (SWISSPROT/TrEMBL); GenBank; EMBL |
Protein Length | 139 AA |
Protein Sequence | MVKKLLTILS IAATAGSLSI GTASAQDAKA GEAVFKQCMT CHRADKNMVG PALGGVVGRK 60 AGTAAGFTYS PLNHNSGEAG LVWTADNIIN YLNDPNAFLK KFLTDKGKAD QAVGVTKMTF 120 KLANEQQRKD VVAYLATLK 139 |
Gene Ontology | |
Interpro | |
Pfam | |
SMART | |
PROSITE | |
PRINTS | |