ID   CRY2_VIBCH              Reviewed;         504 AA.
AC   Q9KS67;
DT   16-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2000, sequence version 1.
DT   03-AUG-2022, entry version 102.
DE   RecName: Full=Cryptochrome-like protein cry2;
GN   Name=cry2; Synonyms=VcCry2; OrderedLocusNames=VC_1392;
OS   Vibrio cholerae serotype O1 (strain ATCC 39315 / El Tor Inaba N16961).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC   Vibrio.
OX   NCBI_TaxID=243277;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 39315 / El Tor Inaba N16961;
RX   PubMed=10952301; DOI=10.1038/35020000;
RA   Heidelberg J.F., Eisen J.A., Nelson W.C., Clayton R.A., Gwinn M.L.,
RA   Dodson R.J., Haft D.H., Hickey E.K., Peterson J.D., Umayam L.A., Gill S.R.,
RA   Nelson K.E., Read T.D., Tettelin H., Richardson D.L., Ermolaeva M.D.,
RA   Vamathevan J.J., Bass S., Qin H., Dragoi I., Sellers P., McDonald L.A.,
RA   Utterback T.R., Fleischmann R.D., Nierman W.C., White O., Salzberg S.L.,
RA   Smith H.O., Colwell R.R., Mekalanos J.J., Venter J.C., Fraser C.M.;
RT   "DNA sequence of both chromosomes of the cholera pathogen Vibrio
RT   cholerae.";
RL   Nature 406:477-483(2000).
RN   [2]
RP   CHARACTERIZATION, COFACTOR, AND LACK OF PHOTOLYASE ACTIVITY.
RX   PubMed=12878596; DOI=10.1074/jbc.m305792200;
RA   Worthington E.N., Kavakli I.H., Berrocal-Tito G., Bondo B.E., Sancar A.;
RT   "Purification and characterization of three members of the
RT   photolyase/cryptochrome family blue-light photoreceptors from Vibrio
RT   cholerae.";
RL   J. Biol. Chem. 278:39143-39154(2003).
CC   -!- FUNCTION: Has no photolyase activity.
CC   -!- COFACTOR:
CC       Name=FAD; Xref=ChEBI:CHEBI:57692;
CC         Evidence={ECO:0000269|PubMed:12878596};
CC       Note=Binds 1 FAD per subunit. {ECO:0000269|PubMed:12878596};
CC   -!- COFACTOR:
CC       Name=(6R)-5,10-methylene-5,6,7,8-tetrahydrofolate;
CC         Xref=ChEBI:CHEBI:15636; Evidence={ECO:0000269|PubMed:12878596};
CC       Note=Binds 1 5,10-methylenetetrahydrofolate (MTHF) non-covalently per
CC       subunit. The occupancy is 0.2. Binds the FAD cofactor more tightly than
CC       the MTHF cofactor. {ECO:0000269|PubMed:12878596};
CC   -!- SIMILARITY: Belongs to the DNA photolyase class-1 family.
CC       {ECO:0000305}.
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DR   EMBL; AE003852; AAF94550.1; -; Genomic_DNA.
DR   PIR; A82205; A82205.
DR   RefSeq; NP_231036.1; NC_002505.1.
DR   RefSeq; WP_000411504.1; NZ_LT906614.1.
DR   AlphaFoldDB; Q9KS67; -.
DR   SMR; Q9KS67; -.
DR   STRING; 243277.VC_1392; -.
DR   PRIDE; Q9KS67; -.
DR   DNASU; 2614024; -.
DR   EnsemblBacteria; AAF94550; AAF94550; VC_1392.
DR   KEGG; vch:VC_1392; -.
DR   PATRIC; fig|243277.26.peg.1323; -.
DR   eggNOG; COG0415; Bacteria.
DR   HOGENOM; CLU_010348_7_1_6; -.
DR   OMA; IWFRHGL; -.
DR   BioCyc; VCHO:VC1392-MON; -.
DR   Proteomes; UP000000584; Chromosome 1.
DR   GO; GO:0003904; F:deoxyribodipyrimidine photo-lyase activity; 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:0051716; P:cellular response to stimulus; IEA:UniProt.
DR   GO; GO:0006139; P:nucleobase-containing compound metabolic process; IEA:UniProt.
DR   GO; GO:0009416; P:response to light stimulus; IBA:GO_Central.
DR   GO; GO:0006950; P:response to stress; IEA:UniProt.
DR   Gene3D; 3.40.50.620; -; 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; IPR018394; DNA_photolyase_1_CS_C.
DR   InterPro; IPR006050; DNA_photolyase_N.
DR   InterPro; IPR014729; Rossmann-like_a/b/a_fold.
DR   PANTHER; PTHR11455; PTHR11455; 1.
DR   Pfam; PF00875; DNA_photolyase; 1.
DR   Pfam; PF03441; FAD_binding_7; 1.
DR   PRINTS; PR00147; DNAPHOTLYASE.
DR   SUPFAM; SSF48173; SSF48173; 1.
DR   SUPFAM; SSF52425; SSF52425; 1.
DR   PROSITE; PS00394; DNA_PHOTOLYASES_1_1; 1.
DR   PROSITE; PS51645; PHR_CRY_ALPHA_BETA; 1.
PE   1: Evidence at protein level;
KW   Chromophore; FAD; Flavoprotein; Reference proteome.
FT   CHAIN           1..504
FT                   /note="Cryptochrome-like protein cry2"
FT                   /id="PRO_0000235314"
FT   DOMAIN          3..133
FT                   /note="Photolyase/cryptochrome alpha/beta"
FT   REGION          483..504
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   504 AA;  58436 MW;  B2CA108EAA0480BF CRC64;
     MEKINLVWLK RDLRLTDHAP LQAALTSGRP TLLLYLFEPM LLGDAHYSER HWRFVWQSLQ
     AINRDLAQSK GEVLIVTSDW QTCFARIAER YAIEAIYSHQ EVGLACTFQR DLALAQWCQQ
     HDIVWHEFPY AAVIRGAQTR KNWDEHWQQV MRSPCCDPDL TRANWLKLDA ATLGLRSDIP
     ATWQSKQAGM QTGGSDMAWA TLEDFFARRG REYYRSISSP SLARHACSRM SPYLAWGNIS
     LREMYQTLLK HWSVAGFRRS LIALSSRLHW HCHFIQKFES ECEMEFRCVN RAYDSLLQQS
     SDAPAAQLAA WQTGHTGIPL VDACMRCLIQ TGYLNFRMRA MLVSVLTHHM NVDWRAGVTY
     LAQLFLDFEP GIHYPQFQMQ AGVTGTNTIR IYNPTKQAQE HDSEGQFIHK WVPELAQVPV
     PLLFEPWLMT PLEAQMYQVP LESPYLKPVM DLEASAKQAR DRLWQWQKLP AVQAEAMRIL
     ARHVRQAKPR TSPRQPNKRQ PEMD