ID A0A060XP51_ONCMY Unreviewed; 825 AA. AC A0A060XP51; DT 03-SEP-2014, integrated into UniProtKB/TrEMBL. DT 03-SEP-2014, sequence version 1. DT 02-OCT-2024, entry version 30. DE RecName: Full=Photolyase/cryptochrome alpha/beta domain-containing protein {ECO:0000259|PROSITE:PS51645}; GN ORFNames=GSONMT00048473001 {ECO:0000313|EMBL:CDQ78675.1}; OS Oncorhynchus mykiss (Rainbow trout) (Salmo gairdneri). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Actinopterygii; Neopterygii; Teleostei; Protacanthopterygii; Salmoniformes; OC Salmonidae; Salmoninae; Oncorhynchus. OX NCBI_TaxID=8022 {ECO:0000313|EMBL:CDQ78675.1, ECO:0000313|Proteomes:UP000193380}; RN [1] {ECO:0000313|EMBL:CDQ78675.1} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=24755649; DOI=10.1038/ncomms4657; RA Berthelot C., Brunet F., Chalopin D., Juanchich A., Bernard M., Noel B., RA Bento P., Da Silva C., Labadie K., Alberti A., Aury J.M., Louis A., RA Dehais P., Bardou P., Montfort J., Klopp C., Cabau C., Gaspin C., RA Thorgaard G.H., Boussaha M., Quillet E., Guyomard R., Galiana D., Bobe J., RA Volff J.N., Genet C., Wincker P., Jaillon O., Roest Crollius H., RA Guiguen Y.; RT "The rainbow trout genome provides novel insights into evolution after RT whole-genome duplication in vertebrates."; RL Nat. Commun. 5:3657-3657(2014). RN [2] {ECO:0000313|EMBL:CDQ78675.1} RP NUCLEOTIDE SEQUENCE. RA Genoscope - CEA; RL Submitted (MAR-2014) to the EMBL/GenBank/DDBJ databases. CC -!- COFACTOR: CC Name=FAD; Xref=ChEBI:CHEBI:57692; CC Evidence={ECO:0000256|PIRSR:PIRSR602081-1}; CC Note=Binds 1 FAD per subunit. {ECO:0000256|PIRSR:PIRSR602081-1}; CC -!- SIMILARITY: Belongs to the DNA photolyase class-1 family. CC {ECO:0000256|ARBA:ARBA00005862}. 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; FR905356; CDQ78675.1; -; Genomic_DNA. DR AlphaFoldDB; A0A060XP51; -. DR STRING; 8022.A0A060XP51; -. DR PaxDb; 8022-A0A060XP51; -. DR Proteomes; UP000193380; Unassembled WGS sequence. DR GO; GO:0097159; F:organic cyclic compound binding; IEA:UniProt. DR GO; GO:0006139; P:nucleobase-containing compound metabolic process; IEA:UniProt. DR GO; GO:0006950; P:response to stress; IEA:UniProt. 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; IPR005101; Cryptochr/Photolyase_FAD-bd. DR InterPro; IPR002081; Cryptochrome/DNA_photolyase_1. DR InterPro; IPR018394; DNA_photolyase_1_CS_C. DR InterPro; IPR006050; DNA_photolyase_N. DR InterPro; IPR014729; Rossmann-like_a/b/a_fold. DR PANTHER; PTHR11455; CRYPTOCHROME; 1. DR PANTHER; PTHR11455:SF18; DEOXYRIBODIPYRIMIDINE PHOTO-LYASE, MITOCHONDRIAL; 1. DR Pfam; PF00875; DNA_photolyase; 1. DR Pfam; PF03441; FAD_binding_7; 1. DR PRINTS; PR00147; DNAPHOTLYASE. DR SUPFAM; SSF48173; Cryptochrome/photolyase FAD-binding domain; 1. DR SUPFAM; SSF52425; Cryptochrome/photolyase, N-terminal domain; 1. DR PROSITE; PS00394; DNA_PHOTOLYASES_1_1; 1. DR PROSITE; PS51645; PHR_CRY_ALPHA_BETA; 1. PE 3: Inferred from homology; KW Chromophore {ECO:0000256|ARBA:ARBA00022991}; KW FAD {ECO:0000256|ARBA:ARBA00022827, ECO:0000256|PIRSR:PIRSR602081-1}; KW Flavoprotein {ECO:0000256|ARBA:ARBA00022630, ECO:0000256|PIRSR:PIRSR602081- KW 1}; Reference proteome {ECO:0000313|Proteomes:UP000193380}. FT DOMAIN 182..323 FT /note="Photolyase/cryptochrome alpha/beta" FT /evidence="ECO:0000259|PROSITE:PS51645" FT REGION 86..112 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 147..168 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 776..825 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 776..809 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT BINDING 428 FT /ligand="FAD" FT /ligand_id="ChEBI:CHEBI:57692" FT /evidence="ECO:0000256|PIRSR:PIRSR602081-1" FT BINDING 440..444 FT /ligand="FAD" FT /ligand_id="ChEBI:CHEBI:57692" FT /evidence="ECO:0000256|PIRSR:PIRSR602081-1" FT BINDING 471 FT /ligand="FAD" FT /ligand_id="ChEBI:CHEBI:57692" FT /evidence="ECO:0000256|PIRSR:PIRSR602081-1" FT BINDING 581..583 FT /ligand="FAD" FT /ligand_id="ChEBI:CHEBI:57692" FT /evidence="ECO:0000256|PIRSR:PIRSR602081-1" SQ SEQUENCE 825 AA; 92841 MW; 3AC7B227FCCD5F6B CRC64; MPVSGGEDPM SQVRQMLREL LVGRENAEGF FCLCVSVLGH NDTRTHFLPL IQLLATDHNR LHTTLTSIYL EYFSKVRLFV CVYSTSPRRS SGHGSSPQTE SQRGPTQTQK QTDIKWSNVT QDVCASIATL TSNLNQTKDD VTVVECKVDQ SEKPKRSKNR RQRRKGYGQQ VVGVPRCPSA PPPVLLWFRR DLRLHDNPAV IGSLEAGGPV IPVFIWCPEE EEGPGVTVAM GGACKFWLHQ ALSCLSSALE HIGSHLVFLR PDEEREGIGS SLLALRSLVR ETGAQTVLAS ALYEPWLRER DQVVVSALQK DRVEVNMVHS YCLRDPYTVT TEGVGLRGIG SVSHFMSCCQ MNPGPGLGVP LDPPISLPSP SVWPRGCPLE GLGLARMPCR KDGTTIDWAA NIRSSWDFSE EGAQSRLEAF LNDGVYRYEK ESGRADAPNT SCLSPYLHFG QLSARWLLWD TKGARCRSPK FIRKLAWRDL AYWQLTLFPD LPWESLRPPY KARTGNERGH LKAWQKGRTG YPLVDAAMRQ LWLTGWMNNY MRHVVASFLI AYLHLPWQEG YRWFQVRLTR CRFQGADTLV DADVAIDAMM WQNGGMCGLD HWNFVMHPVD AAMTCDPYGS YVRKWCPELA VLHDDHIHKP WKCPASMLRR AGVVLGQSYP ERVVTDLEER RSQSLQDVAL VRRRFGQYVD PCSGCDLVPL PPRLVSEAMG GGMVNTGGQF LLPVITRMEF KHQSDDPDAA SNPYNAVLKG YVSRRRNETI AFLNQTDFTA SVINEGAERR ERQEQDQRRM EGLPRPLAVE RRGKRTPAAK DRFSTVPGGV ATSHR //