ID D7FPP0_ECTSI Unreviewed; 542 AA.
AC D7FPP0;
DT 10-AUG-2010, integrated into UniProtKB/TrEMBL.
DT 10-AUG-2010, sequence version 1.
DT 27-MAR-2024, entry version 39.
DE SubName: Full=Cryptochrome 1 {ECO:0000313|EMBL:CBJ30497.1};
GN Name=CRY1 {ECO:0000313|EMBL:CBJ30497.1};
GN ORFNames=Esi_0194_0049 {ECO:0000313|EMBL:CBJ30497.1};
OS Ectocarpus siliculosus (Brown alga) (Conferva siliculosa).
OC Eukaryota; Sar; Stramenopiles; Ochrophyta; PX clade; Phaeophyceae;
OC Ectocarpales; Ectocarpaceae; Ectocarpus.
OX NCBI_TaxID=2880 {ECO:0000313|EMBL:CBJ30497.1, ECO:0000313|Proteomes:UP000002630};
RN [1] {ECO:0000313|EMBL:CBJ30497.1, ECO:0000313|Proteomes:UP000002630}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Ec32 / CCAP1310/4 {ECO:0000313|Proteomes:UP000002630};
RX PubMed=20520714; DOI=10.1038/nature09016;
RA Cock J.M., Sterck L., Rouze P., Scornet D., Allen A.E., Amoutzias G.,
RA Anthouard V., Artiguenave F., Aury J.M., Badger J.H., Beszteri B.,
RA Billiau K., Bonnet E., Bothwell J.H., Bowler C., Boyen C., Brownlee C.,
RA Carrano C.J., Charrier B., Cho G.Y., Coelho S.M., Collen J., Corre E.,
RA Da Silva C., Delage L., Delaroque N., Dittami S.M., Doulbeau S., Elias M.,
RA Farnham G., Gachon C.M., Gschloessl B., Heesch S., Jabbari K., Jubin C.,
RA Kawai H., Kimura K., Kloareg B., Kupper F.C., Lang D., Le Bail A.,
RA Leblanc C., Lerouge P., Lohr M., Lopez P.J., Martens C., Maumus F.,
RA Michel G., Miranda-Saavedra D., Morales J., Moreau H., Motomura T.,
RA Nagasato C., Napoli C.A., Nelson D.R., Nyvall-Collen P., Peters A.F.,
RA Pommier C., Potin P., Poulain J., Quesneville H., Read B., Rensing S.A.,
RA Ritter A., Rousvoal S., Samanta M., Samson G., Schroeder D.C., Segurens B.,
RA Strittmatter M., Tonon T., Tregear J.W., Valentin K., von Dassow P.,
RA Yamagishi T., Van de Peer Y., Wincker P.;
RT "The Ectocarpus genome and the independent evolution of multicellularity in
RT brown algae.";
RL Nature 465:617-621(2010).
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; FN648369; CBJ30497.1; -; Genomic_DNA.
DR AlphaFoldDB; D7FPP0; -.
DR SMR; D7FPP0; -.
DR STRING; 2880.D7FPP0; -.
DR EnsemblProtists; CBJ30497; CBJ30497; Esi_0194_0049.
DR eggNOG; KOG0133; Eukaryota.
DR InParanoid; D7FPP0; -.
DR OMA; TPYKNAW; -.
DR OrthoDB; 124765at2759; -.
DR Proteomes; UP000002630; Chromosome LG19.
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:SF9; 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 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:UP000002630}.
FT DOMAIN 7..137
FT /note="Photolyase/cryptochrome alpha/beta"
FT /evidence="ECO:0000259|PROSITE:PS51645"
FT REGION 496..542
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 254..258
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR602081-1"
FT BINDING 392..394
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR602081-1"
FT SITE 325
FT /note="Electron transfer via tryptophanyl radical"
FT /evidence="ECO:0000256|PIRSR:PIRSR602081-2"
FT SITE 379
FT /note="Electron transfer via tryptophanyl radical"
FT /evidence="ECO:0000256|PIRSR:PIRSR602081-2"
FT SITE 402
FT /note="Electron transfer via tryptophanyl radical"
FT /evidence="ECO:0000256|PIRSR:PIRSR602081-2"
SQ SEQUENCE 542 AA; 60492 MW; 4E5C8CF5BB10BEFA CRC64;
MSSSKEPSSI HWFRKGLRLH DNRALLEACN GTASLYPLFV LDSDPASPES RAGPLRTAFL
LESLQDLDEQ LRAKGSRLFV VRGKPEEVLP QLFEEWNVKK LTFEADSEPR SRARDREVGS
LAKEAGVQVL IRGTSTLRNL QNYHMLMGKK QGTYLKTYGA FLKLHDNAGP VPDCAPDISG
DLPAPGASPD DAEYDRFSIP SLSDLGVEPL AKALKFRGGE REALARLERV MAREDWISKF
EKPKTSPNSI EPSTTVLSMY ISHGCLSTRR FWHALCKVYT KKGGSKPPVS LKGQLLWKEF
NYFSGYSIPS FDKMVGNPVI RQIPWDKDEE KLMAWKEART GFPWIDAAMT QLKDEGWIHH
LARHAVACFL TRGDLWQSWE DGAAVFDELL LDADWSINNF NWQWLSCSAF FYQYFRCYSP
IAFGKKTDQN GDYIKKYLPA LRKFPSKYIY EPWTAPLQVQ RGCGCIIGKD YPKPIVDHAD
TSKANMAKMN DAYDAHQEAQ AAESHDDGGS GSGGGGSGGG SGGGARSRAR GAQPASSKRV
KR
//
