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Database: UniProt
Entry: G3PJN7_GASAC
LinkDB: G3PJN7_GASAC
Original site: G3PJN7_GASAC 
ID   G3PJN7_GASAC            Unreviewed;       530 AA.
AC   G3PJN7;
DT   16-NOV-2011, integrated into UniProtKB/TrEMBL.
DT   16-NOV-2011, sequence version 1.
DT   24-JAN-2024, entry version 57.
DE   RecName: Full=Cryptochrome-1 {ECO:0000256|ARBA:ARBA00021159};
OS   Gasterosteus aculeatus (Three-spined stickleback).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC   Eupercaria; Perciformes; Cottioidei; Gasterosteales; Gasterosteidae;
OC   Gasterosteus.
OX   NCBI_TaxID=69293 {ECO:0000313|Ensembl:ENSGACP00000017817.1, ECO:0000313|Proteomes:UP000007635};
RN   [1] {ECO:0000313|Ensembl:ENSGACP00000017817.1, ECO:0000313|Proteomes:UP000007635}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Lindblad-Toh K., Mauceli E., Grabherr M., Chang J.L., Lander E.S.;
RL   Submitted (JAN-2006) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|Ensembl:ENSGACP00000017817.1}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (JUL-2023) to UniProtKB.
CC   -!- COFACTOR:
CC       Name=(6R)-5,10-methylene-5,6,7,8-tetrahydrofolate;
CC         Xref=ChEBI:CHEBI:15636; Evidence={ECO:0000256|ARBA:ARBA00001932};
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   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
CC       Nucleus {ECO:0000256|ARBA:ARBA00004123}.
CC   -!- SIMILARITY: Belongs to the DNA photolyase class-1 family.
CC       {ECO:0000256|ARBA:ARBA00005862}.
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DR   AlphaFoldDB; G3PJN7; -.
DR   STRING; 69293.ENSGACP00000017817; -.
DR   Ensembl; ENSGACT00000017852.1; ENSGACP00000017817.1; ENSGACG00000013480.1.
DR   eggNOG; KOG0133; Eukaryota.
DR   GeneTree; ENSGT00940000155455; -.
DR   InParanoid; G3PJN7; -.
DR   OMA; PYKSEFA; -.
DR   TreeFam; TF323191; -.
DR   Proteomes; UP000007635; Unassembled WGS sequence.
DR   Bgee; ENSGACG00000013480; Expressed in camera-type eye and 12 other cell types or tissues.
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; IPR006050; DNA_photolyase_N.
DR   InterPro; IPR014729; Rossmann-like_a/b/a_fold.
DR   PANTHER; PTHR11455; CRYPTOCHROME; 1.
DR   PANTHER; PTHR11455:SF16; CRYPTOCHROME-1; 1.
DR   Pfam; PF00875; DNA_photolyase; 1.
DR   Pfam; PF03441; FAD_binding_7; 1.
DR   SUPFAM; SSF48173; Cryptochrome/photolyase FAD-binding domain; 1.
DR   SUPFAM; SSF52425; Cryptochrome/photolyase, N-terminal domain; 1.
DR   PROSITE; PS51645; PHR_CRY_ALPHA_BETA; 1.
PE   3: Inferred from homology;
KW   Biological rhythms {ECO:0000256|ARBA:ARBA00023108};
KW   Chromophore {ECO:0000256|ARBA:ARBA00022991};
KW   Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW   FAD {ECO:0000256|ARBA:ARBA00022827, ECO:0000256|PIRSR:PIRSR602081-1};
KW   Flavoprotein {ECO:0000256|ARBA:ARBA00022630, ECO:0000256|PIRSR:PIRSR602081-
KW   1}; Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW   Photoreceptor protein {ECO:0000256|ARBA:ARBA00022543};
KW   Receptor {ECO:0000256|ARBA:ARBA00023170};
KW   Reference proteome {ECO:0000313|Proteomes:UP000007635};
KW   Repressor {ECO:0000256|ARBA:ARBA00022491};
KW   Sensory transduction {ECO:0000256|ARBA:ARBA00022606};
KW   Transcription {ECO:0000256|ARBA:ARBA00023163};
KW   Transcription regulation {ECO:0000256|ARBA:ARBA00023015}.
FT   DOMAIN          3..132
FT                   /note="Photolyase/cryptochrome alpha/beta"
FT                   /evidence="ECO:0000259|PROSITE:PS51645"
FT   REGION          511..530
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         289..296
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR602081-1"
FT   BINDING         387..389
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR602081-1"
FT   SITE            320
FT                   /note="Electron transfer via tryptophanyl radical"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR602081-2"
FT   SITE            374
FT                   /note="Electron transfer via tryptophanyl radical"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR602081-2"
FT   SITE            397
FT                   /note="Electron transfer via tryptophanyl radical"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR602081-2"
SQ   SEQUENCE   530 AA;  60658 MW;  3E133453002F94CF CRC64;
     MVVNTIHWFR KGLRLHDNPS LRDSIRDADS LRCVYILDPW FAGSSNVGIN RWRFLLQCLE
     DLDASLRKLN SRLFVIRGQP TDVFPRIFKE WQTTRLSYEY DSEPFGKERD AAIQKLASEA
     GVEVMVRTAH TLYNLDRIIE LNDGQSPLTY KRFQTLVNRM DAVELPAETI TAEVVQRCAT
     PLSKDHDDKF AVPSLEELGF ETEGLTTAVW PGGETEALMR LERHLERKAW VANFERPRMN
     ANSLLASPTG LSPYLRFGCL SCRLFYFKLT DLYRKVKKNS TPPLSLYGQL LWREFFYTTA
     TNNPCFDKME GNPVCVQIPW DRNPEALAKW AEGRTGFPWI DAIMTQLRQE GWIHHLARHA
     VACFLTRGDL WVSWEEGMKV FEELLIDADW SVNAGSWMWL SCSSFFQQFF HCYCPVGFGR
     RTDPNGDFIR RYLPVLRGFP AKYIYDPWNA PEEVQKAAKC IVGVHYPRPM VNHAESSRVN
     IERMKQIYQQ LSSYRGLGLL AAVPANPNSV ANDGVLNSGT SRGPGGSSEG
//
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