ID   PHR_CARAU               Reviewed;         556 AA.
AC   P34205;
DT   01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1994, sequence version 1.
DT   03-AUG-2022, entry version 93.
DE   RecName: Full=Deoxyribodipyrimidine photo-lyase;
DE            EC=4.1.99.3;
DE   AltName: Full=DNA photolyase;
DE   AltName: Full=Photoreactivating enzyme;
GN   Name=phr;
OS   Carassius auratus (Goldfish).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC   Cyprinidae; Cyprininae; Carassius.
OX   NCBI_TaxID=7957;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=1339447; DOI=10.1016/s0021-9258(18)35652-7;
RA   Yasuhira S., Yasui A.;
RT   "Visible light-inducible photolyase gene from the goldfish Carassius
RT   auratus.";
RL   J. Biol. Chem. 267:25644-25647(1992).
CC   -!- FUNCTION: Involved in repair of UV radiation-induced DNA damage.
CC       Catalyzes the light-dependent monomerization (300-600 nm) of cyclobutyl
CC       pyrimidine dimers (in cis-syn configuration), which are formed between
CC       adjacent bases on the same DNA strand upon exposure to ultraviolet
CC       radiation.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=cyclobutadipyrimidine (in DNA) = 2 pyrimidine residues (in
CC         DNA).; EC=4.1.99.3;
CC   -!- COFACTOR:
CC       Name=FAD; Xref=ChEBI:CHEBI:57692; Evidence={ECO:0000250};
CC       Note=Binds 1 FAD per subunit. {ECO:0000250};
CC   -!- INDUCTION: By visible light.
CC   -!- SIMILARITY: Belongs to the DNA photolyase class-2 family.
CC       {ECO:0000305}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; D11391; BAA01987.1; -; mRNA.
DR   PIR; A45098; A45098.
DR   AlphaFoldDB; P34205; -.
DR   SMR; P34205; -.
DR   Ensembl; ENSCART00000007477; ENSCARP00000007068; ENSCARG00000003289.
DR   Proteomes; UP000515129; Genome assembly.
DR   GO; GO:0003904; F:deoxyribodipyrimidine photo-lyase activity; IEA:UniProtKB-EC.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0006281; P:DNA repair; IEA:UniProtKB-KW.
DR   Gene3D; 3.40.50.620; -; 1.
DR   InterPro; IPR036134; Crypto/Photolyase_FAD-like_sf.
DR   InterPro; IPR036155; Crypto/Photolyase_N_sf.
DR   InterPro; IPR008148; DNA_photolyase_2.
DR   InterPro; IPR032673; DNA_photolyase_2_CS.
DR   InterPro; IPR006050; DNA_photolyase_N.
DR   InterPro; IPR014729; Rossmann-like_a/b/a_fold.
DR   Pfam; PF00875; DNA_photolyase; 1.
DR   SUPFAM; SSF48173; SSF48173; 1.
DR   SUPFAM; SSF52425; SSF52425; 1.
DR   TIGRFAMs; TIGR00591; phr2; 1.
DR   PROSITE; PS01083; DNA_PHOTOLYASES_2_1; 1.
DR   PROSITE; PS01084; DNA_PHOTOLYASES_2_2; 1.
DR   PROSITE; PS51645; PHR_CRY_ALPHA_BETA; 1.
PE   2: Evidence at transcript level;
KW   Chromophore; DNA damage; DNA repair; DNA-binding; FAD; Flavoprotein; Lyase;
KW   Reference proteome.
FT   CHAIN           1..556
FT                   /note="Deoxyribodipyrimidine photo-lyase"
FT                   /id="PRO_0000085119"
FT   DOMAIN          108..240
FT                   /note="Photolyase/cryptochrome alpha/beta"
FT   REGION          43..65
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          378..386
FT                   /note="Interaction with DNA"
FT                   /evidence="ECO:0000250"
FT   REGION          452..453
FT                   /note="Interaction with DNA"
FT                   /evidence="ECO:0000250"
FT   BINDING         333
FT                   /ligand="DNA"
FT                   /ligand_id="ChEBI:CHEBI:16991"
FT                   /evidence="ECO:0000250"
FT   BINDING         478..480
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   556 AA;  63868 MW;  28318FB406DC5646 CRC64;
     MSGECMLHIR LFSTNLYIRS TLLRSVSDPN TLLHYCSMSA NKRKLKRQRE SPDSGGGKQP
     RLAEGRARES GWLLREVNEL RRAAQGCEVN KKRLRYLSDT QKIKQGSDGF LYWMSRDQRV
     QDNWALIYAQ QLALAEKLPL HICFCLVPRY LDATYRQYAF MLKGLQEVAK ECKSLDIQFH
     LLSGEPGQNL PSFVEKWKFG AVVTDFNPLR IPLQWIETVK KHLPADVPFI QVDAHNVVPC
     WEASGKLEYG ARTIRGKITK LLPEFLTEIP LVDTHPHSAS RAAEPVDWEE VLSSLEVERS
     VGEVDWAQPG TSGGMNMLES FIDQRLRLFA THRNNPNYDA LSHLSPWIHT GQLSAQRVVK
     QVKREKNASE SVASFIEELV VRRELADNFC FYNPSYDNIS GAYDWAKKTL QDHAKDSRQY
     LYTKEQLENA KTHDQLWNAA QRQLVSEGKM HGFLRMYWAK KILEWTASPE EALSIAIYLN
     DRLSLDGCDP NGYVGCMWSI CGIHDQGWAE RPIFGKIRFM NYAGCKRKFD VAQFERKYTA
     VKENSNKDSK KSSSKN