CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-002215
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Deoxyribodipyrimidine photo-lyase, mitochondrial 
Protein Synonyms/Alias
 DNA photolyase; Photoreactivating enzyme 
Gene Name
 PHR1 
Gene Synonyms/Alias
 YOR386W 
Created Date
 July 27, 2013 
Organism
 Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) 
NCBI Taxa ID
 559292 
Lysine Modification
Position
Peptide
Type
References
15SSNAYASKRSRLDIEacetylation[1]
Reference
 [1] Proteome-wide analysis of lysine acetylation suggests its broad regulatory scope in Saccharomyces cerevisiae.
 Henriksen P, Wagner SA, Weinert BT, Sharma S, Bacinskaja G, Rehman M, Juffer AH, Walther TC, Lisby M, Choudhary C.
 Mol Cell Proteomics. 2012 Nov;11(11):1510-22. [PMID: 22865919] 
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 75 226 Photolyase/cryptochrome alpha/beta.
 NP_BIND 338 342 FAD (By similarity).
 NP_BIND 482 484 FAD (By similarity).
 REGION 384 391 Interaction with DNA (By similarity).
 REGION 451 452 Interaction with DNA (By similarity).
 BINDING 326 326 FAD (By similarity).
 BINDING 514 514 DNA (By similarity).  
Keyword
 Chromophore; Complete proteome; DNA damage; DNA repair; DNA-binding; FAD; Flavoprotein; Lyase; Mitochondrion; Nucleotide-binding; Nucleus; Reference proteome; Transit peptide. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 565 AA 
Protein Sequence
MKRTVISSSN AYASKRSRLD IEHDFEQYHS LNKKYYPRPI TRTGANQFNN KSRAKPMEIV 60
EKLQKKQKTS FENVSTVMHW FRNDLRLYDN VGLYKSVALF QQLRQKNAKA KLYAVYVINE 120
DDWRAHMDSG WKLMFIMGAL KNLQQSLAEL HIPLLLWEFH TPKSTLSNSK EFVEFFKEKC 180
MNVSSGTGTI ITANIEYQTD ELYRDIRLLE NEDHRLQLKY YHDSCIVAPG LITTDRGTNY 240
SVFTPWYKKW VLYVNNYKKS TSEICHLHII EPLKYNETFE LKPFQYSLPD EFLQYIPKSK 300
WCLPDVSEEA ALSRLKDFLG TKSSKYNNEK DMLYLGGTSG LSVYITTGRI STRLIVNQAF 360
QSCNGQIMSK ALKDNSSTQN FIKEVAWRDF YRHCMCNWPY TSMGMPYRLD TLDIKWENNP 420
VAFEKWCTGN TGIPIVDAIM RKLLYTGYIN NRSRMITASF LSKNLLIDWR WGERWFMKHL 480
IDGDSSSNVG GWGFCSSTGI DAQPYFRVFN MDIQAKKYDP QMIFVKQWVP ELISSENKRP 540
ENYPKPLVDL KHSRERALKV YKDAM 565 
Gene Ontology
 GO:0005739; C:mitochondrion; IDA:SGD.
 GO:0005634; C:nucleus; TAS:SGD.
 GO:0003904; F:deoxyribodipyrimidine photo-lyase activity; IDA:SGD.
 GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
 GO:0003729; F:mRNA binding; IDA:SGD.
 GO:0000166; F:nucleotide binding; IEA:UniProtKB-KW.
 GO:0000719; P:photoreactive repair; TAS:SGD.
 GO:0018298; P:protein-chromophore linkage; IEA:UniProtKB-KW. 
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.