ID A0A091L2W6_CATAU Unreviewed; 568 AA.
AC A0A091L2W6;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 27-MAR-2024, entry version 25.
DE RecName: Full=Cryptochrome-1 {ECO:0000256|ARBA:ARBA00021159};
DE Flags: Fragment;
GN ORFNames=N323_08073 {ECO:0000313|EMBL:KFP50794.1};
OS Cathartes aura (Turkey vulture) (Vultur aura).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Accipitriformes; Cathartidae; Cathartes.
OX NCBI_TaxID=43455 {ECO:0000313|EMBL:KFP50794.1, ECO:0000313|Proteomes:UP000053745};
RN [1] {ECO:0000313|EMBL:KFP50794.1, ECO:0000313|Proteomes:UP000053745}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BGI_N323 {ECO:0000313|EMBL:KFP50794.1};
RA Zhang G., Li C.;
RT "Genome evolution of avian class.";
RL Submitted (APR-2014) to the EMBL/GenBank/DDBJ databases.
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 EMBL; KL298319; KFP50794.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A091L2W6; -.
DR SMR; A0A091L2W6; -.
DR Proteomes; UP000053745; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0000166; F:nucleotide binding; IEA:UniProtKB-KW.
DR GO; GO:0009881; F:photoreceptor activity; IEA:UniProtKB-KW.
DR GO; GO:0050896; P:response to stimulus; IEA:UniProtKB-KW.
DR GO; GO:0048511; P:rhythmic process; IEA:UniProtKB-KW.
DR Gene3D; 1.25.40.80; -; 2.
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:UP000053745};
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 1..80
FT /note="Photolyase/cryptochrome alpha/beta"
FT /evidence="ECO:0000259|PROSITE:PS51645"
FT REGION 541..568
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 237..244
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR602081-1"
FT BINDING 335..337
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR602081-1"
FT SITE 268
FT /note="Electron transfer via tryptophanyl radical"
FT /evidence="ECO:0000256|PIRSR:PIRSR602081-2"
FT SITE 322
FT /note="Electron transfer via tryptophanyl radical"
FT /evidence="ECO:0000256|PIRSR:PIRSR602081-2"
FT SITE 345
FT /note="Electron transfer via tryptophanyl radical"
FT /evidence="ECO:0000256|PIRSR:PIRSR602081-2"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:KFP50794.1"
FT NON_TER 568
FT /evidence="ECO:0000313|EMBL:KFP50794.1"
SQ SEQUENCE 568 AA; 63663 MW; 05D810A79F2E44AD CRC64;
RFLLQCLEDL DANLRKLNSR LFVIRGQPAD VFPRLFKEWN IAKLSIEYDS EPFGKERDAA
IKKLASEAGV EVIVRISHTL YDLDKIIELN GGQPPLTYKR FQTLISRMEP LEMPVETITP
EVMEKCTTPV SDDHDEKYGV PSLEELGFDT DGLPSAVWPG GETEALTRLE RHLERKAWVA
NFERPRMNAN SLLASPTGLS PYLRFGCLSC RLFYFKLTDL YKKVKKNSSP PLSLYGQLLW
REFFYTAATN NPRFDKMEGN PICVQIPWDK NPEALAKWAE GRTGFPWIDA IMTQLRQEGW
IHHLARHAVA CFLTRGDLWI SWEEGMKVFE ELLLDADWSV NAGSWMWLSC SSFFQQFFHC
YCPVGFGRRT DPNGDYIRRY LPVLRGFPAK YIYDPWNAPE SVQKAAKCII GVNYPKPMVN
HAEASRLNIE RMKQIYQQLS RYRGLGLLAT VPSTPNGNGN GGLMGYSPGE SISGCGSTGG
AQLGTGDGHT VVQPCALGDS HTGASGIQQQ GYCQASSILH YAHGDNQQSH LLQAGRTALG
TGISAGKRPN PEEETQSVGP KVQRQSTN
//
