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CCSR_ASPCL
ID   CCSR_ASPCL              Reviewed;         534 AA.
AC   A1CLY6;
DT   30-NOV-2016, integrated into UniProtKB/Swiss-Prot.
DT   30-NOV-2016, sequence version 2.
DT   03-AUG-2022, entry version 45.
DE   RecName: Full=Cytochalasin cluster regulator ccsR {ECO:0000303|PubMed:21983160};
DE   AltName: Full=Cytochalasin biosynthesis protein R {ECO:0000303|PubMed:21983160};
GN   Name=ccsR {ECO:0000303|PubMed:21983160}; ORFNames=ACLA_078640;
OS   Aspergillus clavatus (strain ATCC 1007 / CBS 513.65 / DSM 816 / NCTC 3887 /
OS   NRRL 1 / QM 1276 / 107).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC   Aspergillus subgen. Fumigati.
OX   NCBI_TaxID=344612;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 1007 / CBS 513.65 / DSM 816 / NCTC 3887 / NRRL 1;
RX   PubMed=18404212; DOI=10.1371/journal.pgen.1000046;
RA   Fedorova N.D., Khaldi N., Joardar V.S., Maiti R., Amedeo P., Anderson M.J.,
RA   Crabtree J., Silva J.C., Badger J.H., Albarraq A., Angiuoli S., Bussey H.,
RA   Bowyer P., Cotty P.J., Dyer P.S., Egan A., Galens K., Fraser-Liggett C.M.,
RA   Haas B.J., Inman J.M., Kent R., Lemieux S., Malavazi I., Orvis J.,
RA   Roemer T., Ronning C.M., Sundaram J.P., Sutton G., Turner G., Venter J.C.,
RA   White O.R., Whitty B.R., Youngman P., Wolfe K.H., Goldman G.H.,
RA   Wortman J.R., Jiang B., Denning D.W., Nierman W.C.;
RT   "Genomic islands in the pathogenic filamentous fungus Aspergillus
RT   fumigatus.";
RL   PLoS Genet. 4:E1000046-E1000046(2008).
RN   [2]
RP   FUNCTION.
RC   STRAIN=ATCC 1007 / CBS 513.65 / DSM 816 / NCTC 3887 / NRRL 1;
RX   PubMed=21983160; DOI=10.1016/j.ymben.2011.09.008;
RA   Qiao K., Chooi Y.H., Tang Y.;
RT   "Identification and engineering of the cytochalasin gene cluster from
RT   Aspergillus clavatus NRRL 1.";
RL   Metab. Eng. 13:723-732(2011).
CC   -!- FUNCTION: Transcription factor involved in regulation of gene cluster
CC       that mediates the biosynthesis of the mycotoxins cytochalasins E and K
CC       (PubMed:21983160). {ECO:0000269|PubMed:21983160}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00227}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=EAW09115.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR   EMBL; DS027057; EAW09115.1; ALT_INIT; Genomic_DNA.
DR   RefSeq; XP_001270541.1; XM_001270540.1.
DR   AlphaFoldDB; A1CLY6; -.
DR   EnsemblFungi; EAW09115; EAW09115; ACLA_078640.
DR   GeneID; 4702674; -.
DR   KEGG; act:ACLA_078640; -.
DR   eggNOG; ENOG502SX45; Eukaryota.
DR   HOGENOM; CLU_674351_0_0_1; -.
DR   OrthoDB; 1576792at2759; -.
DR   Proteomes; UP000006701; Unassembled WGS sequence.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; IEA:InterPro.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   GO; GO:0008152; P:metabolic process; IEA:UniProt.
DR   CDD; cd00067; GAL4; 1.
DR   Gene3D; 4.10.240.10; -; 1.
DR   InterPro; IPR001138; Zn2-C6_fun-type_DNA-bd.
DR   InterPro; IPR036864; Zn2-C6_fun-type_DNA-bd_sf.
DR   SMART; SM00066; GAL4; 1.
DR   SUPFAM; SSF57701; SSF57701; 1.
DR   PROSITE; PS50048; ZN2_CY6_FUNGAL_2; 1.
PE   3: Inferred from homology;
KW   DNA-binding; Metal-binding; Nucleus; Reference proteome; Transcription;
KW   Transcription regulation; Zinc.
FT   CHAIN           1..534
FT                   /note="Cytochalasin cluster regulator ccsR"
FT                   /id="PRO_0000438562"
FT   DNA_BIND        13..54
FT                   /note="Zn(2)-C6 fungal-type"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00227"
FT   REGION          88..170
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          350..378
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        92..123
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        136..155
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   534 AA;  58491 MW;  E9E6C9597465E49A CRC64;
     MVRNMDLYRR SACDRCRRQK LRCVRPLKHG ACEHPNNIEA LEPCERCSRA GTPCVSTLPP
     PRKLSRVERL SGLTSVGQLD NLPLQPLIPK QASSHRPGSG SAKSCIPPTG QNKGINDANA
     VTGSLSMPLP DHRSGSNVHR QPEARPLKRR SRDIHPFGTG SPPTELLDAP SFSTRRSPIF
     SQAEPFALND LDFAMQPHSG GDLPSHGDDL FADVLFSPHQ KPPAGPTVGE SLFDNTKAQE
     LDTRECCLRR LTSLSSRLFH DFNNTNSVKL PDLLSFSPCR NLTAPNQATD CPQNIIGRVL
     ESSHTFLDIL HGLAPDPRPT SSSDSECSYS NYWEDDEFVP ISDEMTYNST SARPEFRDSS
     DMCASSSNRD SSDLSAASPT IDMPTTLTIL TCYTWLLQAY DTIFSQIYSS LLAGTDSTSP
     SMPPVLPGLQ IGGFSLDQHC DLQIEILIQL SARMLDRIEG KLGVTDTKDS NAPVDDQEWS
     RNGSILDTAS ASTILDALFK QNHSETRAKP GKGARAGSVR NIMKNIRAEL TVHK
 
 
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