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ECDB_ASPRU
ID   ECDB_ASPRU              Reviewed;         545 AA.
AC   K0E2F6;
DT   25-APR-2018, integrated into UniProtKB/Swiss-Prot.
DT   28-NOV-2012, sequence version 1.
DT   25-MAY-2022, entry version 24.
DE   RecName: Full=Putative transcription factor ecdB {ECO:0000303|PubMed:22998630};
GN   Name=ecdB {ECO:0000303|PubMed:22998630};
OS   Aspergillus rugulosus (Emericella rugulosa).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
OX   NCBI_TaxID=41736;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 58397 / NRRL 11440;
RX   PubMed=22998630; DOI=10.1021/ja307220z;
RA   Cacho R.A., Jiang W., Chooi Y.H., Walsh C.T., Tang Y.;
RT   "Identification and characterization of the echinocandin B biosynthetic
RT   gene cluster from Emericella rugulosa NRRL 11440.";
RL   J. Am. Chem. Soc. 134:16781-16790(2012).
RN   [2]
RP   CLUSTER REVISION.
RX   PubMed=27502607; DOI=10.1186/s12864-016-2885-x;
RA   Huettel W., Youssar L., Gruening B.A., Guenther S., Hugentobler K.G.;
RT   "Echinocandin B biosynthesis: a biosynthetic cluster from Aspergillus
RT   nidulans NRRL 8112 and reassembly of the subclusters Ecd and Hty from
RT   Aspergillus pachycristatus NRRL 11440 reveals a single coherent gene
RT   cluster.";
RL   BMC Genomics 17:570-570(2016).
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00227}.
CC   -!- CAUTION: EcdB, ecdC, ecdD, ecdE and ecdF have previously been
CC       identified as being part of the echinocandin B biosynthetic cluster,
CC       but it was later realized that this was due to a genome misassembly and
CC       these 5 proteins are now considered as artifacts and not part of the
CC       cluster. {ECO:0000269|PubMed:27502607}.
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DR   EMBL; JX421684; AFT91385.1; -; Genomic_DNA.
DR   AlphaFoldDB; K0E2F6; -.
DR   SMR; K0E2F6; -.
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   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   Pfam; PF00172; Zn_clus; 1.
DR   SMART; SM00066; GAL4; 1.
DR   SUPFAM; SSF57701; SSF57701; 1.
DR   PROSITE; PS00463; ZN2_CY6_FUNGAL_1; 1.
DR   PROSITE; PS50048; ZN2_CY6_FUNGAL_2; 1.
PE   3: Inferred from homology;
KW   DNA-binding; Metal-binding; Nucleus; Transcription;
KW   Transcription regulation; Zinc.
FT   CHAIN           1..545
FT                   /note="Putative transcription factor ecdB"
FT                   /id="PRO_0000443827"
FT   DNA_BIND        12..39
FT                   /note="Zn(2)-C6 fungal-type"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00227"
FT   REGION          79..99
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   545 AA;  60610 MW;  CBF03EE1544618F7 CRC64;
     MVKMRKRLAV ACDACRSRRV KCDGQRPSCM GCLSRGLDCS YQRLPEPPAT RLETELANVN
     MRLDYLAMLL SRQSQPQAPP PVLLASARPS SNPLSSHEDS PFRLLATDSI MSVLGLEDHF
     ARRLVQLERA SLLASTTTLS RMFFISHQQV TDALIAFSER VHTFYPILPL DFSERYFATL
     SGPLAPSCQT CLALLVAAIG CIARDPTMGD EYFEAALASL PTVLAECTLA SIQCLVFLSI
     YYCCRLKPCQ AHDYCLIASF KIQNLFKSEL SVQLDVATSD TWKLDEYIPL PNCRYTWQFS
     CPPLPGNLAG VSPESASSSS SSISIDSTNS STSTASDQAQ SFFLAEIAMR RMLHRCNSAV
     AQSSDGRFCY APSIALELER QLEEWYDYLP ASIRFVREPA GGSFNGDQSA LSPLSTFLNV
     QYCCCKLSIY WPAVYQVIQD DKATPQLLEH CQRFIDSYVQ LLPRIALAID KCLIYKWTLS
     VTFFVTTMAA LKVANTAALR AAQHERLHES LALAGTVGWK NTEDSPSLEL LRLNLSQHLR
     EAKQK
 
 
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