Tag | Content |
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CPLM ID | CPLM-001830 |
UniProt Accession | |
Genbank Protein ID | |
Genbank Nucleotide ID | |
Protein Name | Deoxyribodipyrimidine photo-lyase |
Protein Synonyms/Alias | DNA photolyase; Photoreactivating enzyme |
Gene Name | phrB |
Gene Synonyms/Alias | phr; b0708; JW0698 |
Created Date | July 27, 2013 |
Organism | Escherichia coli (strain K12) |
NCBI Taxa ID | 83333 |
Lysine Modification | Position | Peptide | Type | References |
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206 | AHFPVEEKAAIAQLR | acetylation | [1] | 408 | NPTTQGEKFDHEGEF | acetylation | [1] | 436 | KVVHEPWKWAQKAGV | acetylation | [1] |
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Reference | [1] Acetyl-Phosphate Is a Critical Determinant of Lysine Acetylation in E. coli. Weinert BT, Iesmantavicius V, Wagner SA, Schölz C, Gummesson B, Beli P, Nyström T, Choudhary C. Mol Cell. 2013 Jul 25;51(2):265-72. [ PMID: 23830618] |
Functional Description | Involved in repair of UV radiation-induced DNA damage. Catalyzes the light-dependent monomerization (300-600 nm) of cyclobutyl pyrimidine dimers (in cis-syn configuration), which are formed between adjacent bases on the same DNA strand upon exposure to ultraviolet radiation. |
Sequence Annotation | DOMAIN 2 134 Photolyase/cryptochrome alpha/beta. NP_BIND 235 239 FAD. NP_BIND 275 282 FAD. NP_BIND 373 375 FAD. REGION 109 110 MTF binding. REGION 275 282 Interaction with DNA (By similarity). REGION 342 343 Interaction with DNA (By similarity). BINDING 223 223 FAD. BINDING 227 227 DNA (By similarity). BINDING 272 272 FAD. BINDING 405 405 DNA (By similarity). |
Keyword | 3D-structure; Chromophore; Complete proteome; DNA damage; DNA repair; DNA-binding; FAD; Flavoprotein; Lyase; Nucleotide-binding; Reference proteome. |
Sequence Source | UniProt (SWISSPROT/TrEMBL); GenBank; EMBL |
Protein Length | 472 AA |
Protein Sequence | MTTHLVWFRQ DLRLHDNLAL AAACRNSSAR VLALYIATPR QWATHNMSPR QAELINAQLN 60 GLQIALAEKG IPLLFREVDD FVASVEIVKQ VCAENSVTHL FYNYQYEVNE RARDVEVERA 120 LRNVVCEGFD DSVILPPGAV MTGNHEMYKV FTPFKNAWLK RLREGMPECV AAPKVRSSGS 180 IEPSPSITLN YPRQSFDTAH FPVEEKAAIA QLRQFCQNGA GEYEQQRDFP AVEGTSRLSA 240 SLATGGLSPR QCLHRLLAEQ PQALDGGAGS VWLNELIWRE FYRHLITYHP SLCKHRPFIA 300 WTDRVQWQSN PAHLQAWQEG KTGYPIVDAA MRQLNSTGWM HNRLRMITAS FLVKDLLIDW 360 REGERYFMSQ LIDGDLAANN GGWQWAASTG TDAAPYFRIF NPTTQGEKFD HEGEFIRQWL 420 PELRDVPGKV VHEPWKWAQK AGVTLDYPQP IVEHKEARVQ TLAAYEAARK GK 472 |
Gene Ontology | GO:0003904; F:deoxyribodipyrimidine photo-lyase activity; IDA:EcoCyc. GO:0003677; F:DNA binding; IEA:UniProtKB-KW. GO:0000166; F:nucleotide binding; IEA:UniProtKB-KW. GO:0006281; P:DNA repair; IEA:UniProtKB-KW. GO:0018298; P:protein-chromophore linkage; IDA:EcoCyc. |
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