ID W5N081_LEPOC Unreviewed; 675 AA.
AC W5N081;
DT 16-APR-2014, integrated into UniProtKB/TrEMBL.
DT 16-APR-2014, sequence version 1.
DT 27-MAR-2024, entry version 54.
DE SubName: Full=Cryptochrome circadian regulator 3a {ECO:0000313|Ensembl:ENSLOCP00000014040.1};
OS Lepisosteus oculatus (Spotted gar).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Holostei; Semionotiformes; Lepisosteidae;
OC Lepisosteus.
OX NCBI_TaxID=7918 {ECO:0000313|Ensembl:ENSLOCP00000014040.1, ECO:0000313|Proteomes:UP000018468};
RN [1] {ECO:0000313|Proteomes:UP000018468}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Di Palma F., Alfoldi J., Johnson J., Berlin A., Gnerre S., Jaffe D.,
RA MacCallum I., Young S., Walker B.J., Lander E.S., Lindblad-Toh K.;
RT "The Draft Genome of Lepisosteus oculatus.";
RL Submitted (DEC-2011) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSLOCP00000014040.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
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}.
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DR EMBL; AHAT01016727; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AHAT01016728; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR AlphaFoldDB; W5N081; -.
DR STRING; 7918.ENSLOCP00000014040; -.
DR Ensembl; ENSLOCT00000014069.1; ENSLOCP00000014040.1; ENSLOCG00000011417.1.
DR eggNOG; KOG0133; Eukaryota.
DR GeneTree; ENSGT00940000165925; -.
DR HOGENOM; CLU_010348_3_4_1; -.
DR InParanoid; W5N081; -.
DR OMA; GASTFRC; -.
DR Proteomes; UP000018468; Linkage group LG3.
DR Bgee; ENSLOCG00000011417; Expressed in camera-type eye and 13 other cell types or tissues.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0003677; F:DNA binding; IBA:GO_Central.
DR GO; GO:0071949; F:FAD binding; IBA:GO_Central.
DR GO; GO:0032922; P:circadian regulation of gene expression; IBA:GO_Central.
DR GO; GO:0043153; P:entrainment of circadian clock by photoperiod; IBA:GO_Central.
DR GO; GO:0045892; P:negative regulation of DNA-templated transcription; IBA:GO_Central.
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:SF10; CRYPTOCHROME 2B-RELATED; 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 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:UP000018468}.
FT DOMAIN 3..132
FT /note="Photolyase/cryptochrome alpha/beta"
FT /evidence="ECO:0000259|PROSITE:PS51645"
FT REGION 523..567
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 593..675
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 523..552
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 593..611
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 633..665
FT /note="Basic and acidic residues"
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 675 AA; 75654 MW; 51CFB4DDB161FB98 CRC64;
MGPNSIHWFR KGLRLHDNPA LKEAIRGAST VRCVYFLDPW FAGSSNLGVN RWRFLLQCLE
DLDANLRKLN SRLFVIRGQP ANVFPRLFKE WKISRLTFEY DSEPFGKERD AAIKKLAKEA
GVEVIVKISH TLYDLDRIIE LNGGQPPLTY KRFQTLISRM DPPELPVDPL SEVFMGKCVT
PVSDDHGDKY GVPSLEELGF DTEGLPSAVW PGGETEALTR IERHLERKAW VANFERPRMN
ANSLLASPTG LSPYLRFGCL SCRLFYFKLT DLYRKVKKNS SPPLSLYGQL LWREFFYTAA
TTNPRFDKME GNPICVRIPW DRNSEALAKW AEAKTGFPWI DAIMTQLRQE GWIHHLARHA
VACFLTRGDL WISWEEGMKV FEELLLDADW SVNAGSWMWL SCSSFFQQFF HCYCPVGFGR
RTDPNGDYIR RYLPVLRGFP AKYIYDPWNA PDSVQNAAKC VIGVHYPKPM VNHAEASRLN
IERMKQIYQQ LSRYRGLGLL ASVPSNHNGN GNGGMMAYSP GEQQPAHGTT YGAAPGSSVA
SGNGSSSILL NFDGEEQPGP SGVHHGEGAA CGHTLASALL FCWHIGYHTV SEPGQGSTSH
RLYQSSGSHE FAVPQHPGRW AHGGAGGGSS APGKRERETE RDAAGDEEAR SSALKVQRQC
NEKSEDLQDV NMASY
//
