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CRYD_VIBCH
ID   CRYD_VIBCH              Reviewed;         461 AA.
AC   Q9KR33;
DT   16-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2000, sequence version 1.
DT   03-AUG-2022, entry version 111.
DE   RecName: Full=Cryptochrome DASH;
GN   Name=cry1; Synonyms=VcCry1; OrderedLocusNames=VC_1814;
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: May have a photoreceptor function. Binds DNA; probably
CC       functions as a transcriptional repressor (By similarity). Has no
CC       photolyase activity. Upon purification from either V.cholerae or E.coli
CC       an approximately 60 nucleotide RNA is associated with the protein.
CC       {ECO:0000250}.
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-methenyltetrahydrofolate (MTHF) non-covalently per
CC       subunit. Binds the MTHF cofactor more tightly than the FAD cofactor.
CC       {ECO:0000269|PubMed:12878596};
CC   -!- SIMILARITY: Belongs to the DNA photolyase class-1 family.
CC       {ECO:0000305}.
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DR   EMBL; AE003852; AAF94962.1; -; Genomic_DNA.
DR   PIR; B82155; B82155.
DR   RefSeq; NP_231448.1; NC_002505.1.
DR   RefSeq; WP_000037642.1; NZ_LT906614.1.
DR   AlphaFoldDB; Q9KR33; -.
DR   SMR; Q9KR33; -.
DR   STRING; 243277.VC_1814; -.
DR   DNASU; 2613694; -.
DR   EnsemblBacteria; AAF94962; AAF94962; VC_1814.
DR   GeneID; 57740452; -.
DR   KEGG; vch:VC_1814; -.
DR   PATRIC; fig|243277.26.peg.1733; -.
DR   eggNOG; COG0415; Bacteria.
DR   HOGENOM; CLU_010348_6_2_6; -.
DR   OMA; NWNYTAG; -.
DR   BioCyc; VCHO:VC1814-MON; -.
DR   BRENDA; 4.1.99.3; 15862.
DR   Proteomes; UP000000584; Chromosome 1.
DR   GO; GO:0003677; F:DNA binding; IBA:GO_Central.
DR   GO; GO:0003913; F:DNA photolyase activity; IEA:InterPro.
DR   GO; GO:0071949; F:FAD binding; IBA:GO_Central.
DR   GO; GO:0000719; P:photoreactive repair; IBA:GO_Central.
DR   Gene3D; 3.40.50.620; -; 1.
DR   InterPro; IPR014133; Cry_DASH.
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; 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   TIGRFAMs; TIGR02765; crypto_DASH; 1.
DR   PROSITE; PS51645; PHR_CRY_ALPHA_BETA; 1.
PE   1: Evidence at protein level;
KW   Chromophore; DNA-binding; FAD; Flavoprotein; Reference proteome; Repressor;
KW   Transcription; Transcription regulation.
FT   CHAIN           1..461
FT                   /note="Cryptochrome DASH"
FT                   /id="PRO_0000235312"
FT   DOMAIN          4..137
FT                   /note="Photolyase/cryptochrome alpha/beta"
SQ   SEQUENCE   461 AA;  52736 MW;  60389A943801DEFC CRC64;
     MSKKIGLYWF TNDLRVNDNP LLEQASQQVD RLICLYCYPS ITPFLARYAQ QTQWGEAKKR
     FLNQTLADLD HSLSTLGQKL WVTPLLPYQA LRHLLTQVEI TDIYVDAVAG SDERQAIARI
     HQDFSSVHIH QQALHSLLSE PQLPFALEAL PSTFTQFRKQ VETISLSAPM GYPHVLPPIE
     QGWQLPLMDI VTEPNHSAFV GGEQAGLTHC QNYFSSLLPS RYKETRNGLD GMDYSTKFSP
     WLALGAVSPK TIYAMLQRYE AVHGANDSTY WIFFELLWRE YFYWYARRYG AKLFRFSGIG
     EKKPLTSFYA QRFLQWKHGE TPFPIVNACM RQLNQTGYMS NRGRQLVASC LVHELGLDWR
     YGAAYFETQL VDYDVGSNWG NWQYLAGVGA DPRGSRQFNL EKQAHTYDPK GEFVAKWCGT
     ACDKLNALEN LALDSVDMVD WPIAASAYLL IHHPQNKESS S
 
 
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