CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
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
206AHFPVEEKAAIAQLRacetylation[1]
408NPTTQGEKFDHEGEFacetylation[1]
436KVVHEPWKWAQKAGVacetylation[1]
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. 
Interpro
 IPR002081; Cryptochrome/DNA_photolyase_1.
 IPR018394; DNA_photolyase_1_CS_C.
 IPR006050; DNA_photolyase_N.
 IPR005101; Photolyase_FAD-bd/Cryptochr_C.
 IPR014729; Rossmann-like_a/b/a_fold. 
Pfam
 PF00875; DNA_photolyase
 PF03441; FAD_binding_7 
SMART
  
PROSITE
 PS00394; DNA_PHOTOLYASES_1_1
 PS00691; DNA_PHOTOLYASES_1_2
 PS51645; PHR_CRY_ALPHA_BETA 
PRINTS
 PR00147; DNAPHOTLYASE.