ID Q91186_ORYLA Unreviewed; 504 AA.
AC Q91186;
DT 01-NOV-1996, integrated into UniProtKB/TrEMBL.
DT 01-NOV-1996, sequence version 1.
DT 27-MAR-2024, entry version 102.
DE RecName: Full=Deoxyribodipyrimidine photo-lyase {ECO:0000256|ARBA:ARBA00014046};
DE EC=4.1.99.3 {ECO:0000256|ARBA:ARBA00013149};
DE AltName: Full=DNA photolyase {ECO:0000256|ARBA:ARBA00031671};
OS Oryzias latipes (Japanese rice fish) (Japanese killifish).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Ovalentaria; Atherinomorphae; Beloniformes; Adrianichthyidae; Oryziinae;
OC Oryzias.
OX NCBI_TaxID=8090 {ECO:0000313|EMBL:BAA05043.1};
RN [1] {ECO:0000313|EMBL:BAA05043.1}
RP NUCLEOTIDE SEQUENCE.
RX PubMed=7813451;
RA Yasui A., Eker A.P., Yasuhira S., Yajima H., Kobayashi T., Takao M.,
RA Oikawa A.;
RT "A new class of DNA photolyases present in various organisms including
RT aplacental mammals.";
RL EMBO J. 13:6143-6151(1994).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=cyclobutadipyrimidine (in DNA) = 2 pyrimidine residues (in
CC DNA).; EC=4.1.99.3; Evidence={ECO:0000256|ARBA:ARBA00033999};
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000256|ARBA:ARBA00001974};
CC -!- SIMILARITY: Belongs to the DNA photolyase class-2 family.
CC {ECO:0000256|ARBA:ARBA00006409}.
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DR EMBL; D26022; BAA05043.1; -; mRNA.
DR PIR; S52048; S52048.
DR RefSeq; NP_001098271.1; NM_001104801.1.
DR AlphaFoldDB; Q91186; -.
DR GeneID; 100049426; -.
DR KEGG; ola:100049426; -.
DR CTD; 394039; -.
DR OrthoDB; 1341644at2759; -.
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; 1.25.40.80; -; 1.
DR Gene3D; 1.10.579.10; DNA Cyclobutane Dipyrimidine Photolyase, subunit A, domain 3; 1.
DR Gene3D; 3.40.50.620; HUPs; 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 NCBIfam; TIGR00591; phr2; 1.
DR PANTHER; PTHR10211:SF0; DEOXYRIBODIPYRIMIDINE PHOTO-LYASE; 1.
DR PANTHER; PTHR10211; DEOXYRIBODIPYRIMIDINE PHOTOLYASE; 1.
DR Pfam; PF00875; DNA_photolyase; 1.
DR SUPFAM; SSF48173; Cryptochrome/photolyase FAD-binding domain; 1.
DR SUPFAM; SSF52425; Cryptochrome/photolyase, N-terminal domain; 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 {ECO:0000256|ARBA:ARBA00022991};
KW DNA damage {ECO:0000256|ARBA:ARBA00022763};
KW DNA repair {ECO:0000256|ARBA:ARBA00023204};
KW DNA-binding {ECO:0000256|ARBA:ARBA00023125};
KW FAD {ECO:0000256|ARBA:ARBA00022827};
KW Flavoprotein {ECO:0000256|ARBA:ARBA00022630};
KW Lyase {ECO:0000256|ARBA:ARBA00023239, ECO:0000313|EMBL:BAA05043.1}.
FT DOMAIN 70..203
FT /note="Photolyase/cryptochrome alpha/beta"
FT /evidence="ECO:0000259|PROSITE:PS51645"
FT REGION 1..32
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 504 AA; 57645 MW; B02F5DD2E35BB608 CRC64;
MSDKKKRKAT ATAGDAEPSA KQPREDKPTK AAGWLHSLIR QQREDKKDMK FSKKRQRFIS
ETQKVRQGSG GVLYWMLRDQ RVQDNWALIR AQQLAAKESL PLHVCFCLVV PKSELSTLRH
YSFLLKGLEE VQKECKHLNI QFHLLHGAAG DVLPGFVTGH NFGAVVTDFS PLREPLQWLE
AVKKGLPEDI PFIQVDAHNI VPCWVASPKL EYSARTIRGK ITNLLSEFLT DFPLVDKHPF
SATKTAKAVD WDKTLASLKV DRTVGEPKLA KPGTEAGLAM LESFIDVRLK LFGTQRNDPN
AAALSQLSPW LRFGQLSAQR VALQVRKNSS PSVPAFIEEL VVRRELTDNF CFYNKNYDSV
TGAYEWAQKT LKDHAKDKRE YLYTREQFEK AQTHDKLWNA AQIQMVTEGK MHGFLRMYWA
KKILEWSTSP EEALSIALYL NDRYELDGQD PNGFVGCMWS ICGIHDQGWA ERAVFGKIRF
MNYKGCLRKF NVAQFERKYC SKKV
//
