GenomeNet

Database: UniProt
Entry: F6ZXR9_XENTR
LinkDB: F6ZXR9_XENTR
Original site: F6ZXR9_XENTR 
ID   F6ZXR9_XENTR            Unreviewed;       570 AA.
AC   F6ZXR9;
DT   27-JUL-2011, integrated into UniProtKB/TrEMBL.
DT   02-JUN-2021, sequence version 4.
DT   27-MAR-2024, entry version 50.
DE   SubName: Full=Cryptochrome 4 {ECO:0000313|Ensembl:ENSXETP00000033570};
GN   Name=cry4 {ECO:0000313|Ensembl:ENSXETP00000033570};
OS   Xenopus tropicalis (Western clawed frog) (Silurana tropicalis).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC   Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Silurana.
OX   NCBI_TaxID=8364 {ECO:0000313|Ensembl:ENSXETP00000033570};
RN   [1] {ECO:0000313|Ensembl:ENSXETP00000033570}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Nigerian {ECO:0000313|Ensembl:ENSXETP00000033570};
RX   PubMed=20431018; DOI=10.1126/science.1183670;
RA   Hellsten U., Harland R.M., Gilchrist M.J., Hendrix D., Jurka J.,
RA   Kapitonov V., Ovcharenko I., Putnam N.H., Shu S., Taher L., Blitz I.L.,
RA   Blumberg B., Dichmann D.S., Dubchak I., Amaya E., Detter J.C., Fletcher R.,
RA   Gerhard D.S., Goodstein D., Graves T., Grigoriev I.V., Grimwood J.,
RA   Kawashima T., Lindquist E., Lucas S.M., Mead P.E., Mitros T., Ogino H.,
RA   Ohta Y., Poliakov A.V., Pollet N., Robert J., Salamov A., Sater A.K.,
RA   Schmutz J., Terry A., Vize P.D., Warren W.C., Wells D., Wills A.,
RA   Wilson R.K., Zimmerman L.B., Zorn A.M., Grainger R., Grammer T.,
RA   Khokha M.K., Richardson P.M., Rokhsar D.S.;
RT   "The genome of the Western clawed frog Xenopus tropicalis.";
RL   Science 328:633-636(2010).
RN   [2] {ECO:0000313|Ensembl:ENSXETP00000033570}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (JUN-2011) 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}.
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   AlphaFoldDB; F6ZXR9; -.
DR   STRING; 8364.ENSXETP00000033570; -.
DR   PaxDb; 8364-ENSXETP00000002924; -.
DR   Ensembl; ENSXETT00000033570; ENSXETP00000033570; ENSXETG00000015354.
DR   AGR; Xenbase:XB-GENE-978401; -.
DR   Xenbase; XB-GENE-5945160; cry4.
DR   HOGENOM; CLU_010348_3_4_1; -.
DR   InParanoid; F6ZXR9; -.
DR   OrthoDB; 2919077at2759; -.
DR   Bgee; ENSXETG00000015354; Expressed in testis 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:SF61; CRYPTOCHROME-LIKE PROTEIN; 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}.
FT   DOMAIN          16..146
FT                   /note="Photolyase/cryptochrome alpha/beta"
FT                   /evidence="ECO:0000259|PROSITE:PS51645"
FT   BINDING         260..264
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR602081-1"
FT   BINDING         301..308
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR602081-1"
FT   BINDING         399..401
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR602081-1"
FT   SITE            332
FT                   /note="Electron transfer via tryptophanyl radical"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR602081-2"
FT   SITE            386
FT                   /note="Electron transfer via tryptophanyl radical"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR602081-2"
FT   SITE            409
FT                   /note="Electron transfer via tryptophanyl radical"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR602081-2"
SQ   SEQUENCE   570 AA;  66139 MW;  C0E7F55A3D2E0ABE CRC64;
     MYKSSIRFRS CSTMPHRTIH IFRKGLRLHD NPTLVTALET SDVVYPVYIL DRNFMTSSSV
     IGSKRWNFFL QSIEDLHCNL QKLNSCLFVI QGDYERVLRE HVEKWNITQV TFDLEIEPYY
     KGLDERIRAM GQELGFEVVS MVAHTLYDIK TILALNCGKP PLTYKNFLRV LSMIGNPDKP
     ARQITSEDFI KCITPTKLAA EEYYRIPKPE DLGISKDCPT NWVGGESEAL SRLEQHLEKQ
     GWVANFKKPQ TIPNSLLPST TGLSPYFSLG CLSVRVFFHR LSNIYAQSKN HSLPPVSLQG
     QLLWREFFYT VASSTPNFTH MVGNPICLQI DWYKNEEQLQ KWKEAKTGFP WIDAIMTQLH
     NEGWIHHLAR HAVACFLTRG DLWISWEEGM KVFEEFLLDA DYCINAGNWM WLSASAFFHH
     YTRIFCPVRF GRRSDPEGNY IRKYLPVLKN FPAKYIYEPW TAPEEIQKQA GCLIGKDYPL
     PMVDHKTASE HNLQLMRQVR EEQQKTAQLT KDIADDPMEL NLKHPFKNDK ECGLENNKVK
     RRCLEEMTAE DGTRQSDLVQ SLDPCEVKVC
//
DBGET integrated database retrieval system