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YR260_MIMIV
ID   YR260_MIMIV             Reviewed;         398 AA.
AC   Q5UP23;
DT   13-SEP-2005, integrated into UniProtKB/Swiss-Prot.
DT   07-DEC-2004, sequence version 1.
DT   23-FEB-2022, entry version 73.
DE   RecName: Full=DnaJ-like protein R260;
GN   OrderedLocusNames=MIMI_R260;
OS   Acanthamoeba polyphaga mimivirus (APMV).
OC   Viruses; Varidnaviria; Bamfordvirae; Nucleocytoviricota; Megaviricetes;
OC   Imitervirales; Mimiviridae; Mimivirus.
OX   NCBI_TaxID=212035;
OH   NCBI_TaxID=5757; Acanthamoeba polyphaga (Amoeba).
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Rowbotham-Bradford;
RX   PubMed=15486256; DOI=10.1126/science.1101485;
RA   Raoult D., Audic S., Robert C., Abergel C., Renesto P., Ogata H.,
RA   La Scola B., Susan M., Claverie J.-M.;
RT   "The 1.2-megabase genome sequence of Mimivirus.";
RL   Science 306:1344-1350(2004).
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250};
CC       Note=Binds 2 Zn(2+) ions per monomer. {ECO:0000250};
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DR   EMBL; AY653733; AAV50532.1; -; Genomic_DNA.
DR   RefSeq; YP_003986758.1; NC_014649.1.
DR   SMR; Q5UP23; -.
DR   GeneID; 9924869; -.
DR   KEGG; vg:9924869; -.
DR   Proteomes; UP000001134; Genome.
DR   GO; GO:0030544; F:Hsp70 protein binding; IEA:InterPro.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0051082; F:unfolded protein binding; IEA:InterPro.
DR   GO; GO:0006457; P:protein folding; IEA:InterPro.
DR   CDD; cd06257; DnaJ; 1.
DR   CDD; cd10719; DnaJ_zf; 1.
DR   Gene3D; 1.10.287.110; -; 1.
DR   InterPro; IPR002939; DnaJ_C.
DR   InterPro; IPR001623; DnaJ_domain.
DR   InterPro; IPR018253; DnaJ_domain_CS.
DR   InterPro; IPR044713; DNJA1/2-like.
DR   InterPro; IPR008971; HSP40/DnaJ_pept-bd.
DR   InterPro; IPR001305; HSP_DnaJ_Cys-rich_dom.
DR   InterPro; IPR036410; HSP_DnaJ_Cys-rich_dom_sf.
DR   InterPro; IPR036869; J_dom_sf.
DR   PANTHER; PTHR43888; PTHR43888; 1.
DR   Pfam; PF00226; DnaJ; 1.
DR   Pfam; PF01556; DnaJ_C; 1.
DR   Pfam; PF00684; DnaJ_CXXCXGXG; 1.
DR   PRINTS; PR00625; JDOMAIN.
DR   SMART; SM00271; DnaJ; 1.
DR   SUPFAM; SSF46565; SSF46565; 1.
DR   SUPFAM; SSF49493; SSF49493; 1.
DR   SUPFAM; SSF57938; SSF57938; 1.
DR   PROSITE; PS00636; DNAJ_1; 1.
DR   PROSITE; PS50076; DNAJ_2; 1.
DR   PROSITE; PS51188; ZF_CR; 1.
PE   3: Inferred from homology;
KW   Chaperone; Metal-binding; Reference proteome; Repeat; Zinc; Zinc-finger.
FT   CHAIN           1..398
FT                   /note="DnaJ-like protein R260"
FT                   /id="PRO_0000071165"
FT   DOMAIN          7..72
FT                   /note="J"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00286"
FT   REPEAT          131..138
FT                   /note="CXXCXGXG motif"
FT   REPEAT          147..154
FT                   /note="CXXCXGXG motif"
FT   REPEAT          173..180
FT                   /note="CXXCXGXG motif"
FT   REPEAT          190..197
FT                   /note="CXXCXGXG motif"
FT   ZN_FING         118..202
FT                   /note="CR-type"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00546"
FT   REGION          364..398
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        371..386
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   398 AA;  45201 MW;  81BCDBAD8270BBE2 CRC64;
     MNKESTDLYE ILGLTPSASE EDIKKAYRKL AIKYHPDKNK GNPEAEEMFK KINHANSILS
     NSEKRRVYDQ YGEEAVNNGL NEDSFDPMSM FMRMHQPGNK KLRAQMRHQI SLQDYFTKKT
     VKVTITVDSK CDDCDATGFS DKQKHVCKVC RGKGIVVNEI RNGPFIQQIQ QHCHGCQGKK
     YDTTAKDLHC PSCKGAGINK SEEETEVNVP FDILRNPKVI LEGKGPWVDG KNIDLEIVFI
     LAFSDGFELT DNHKLIYTME INFPETLCGF RRIIDHPSGD SLLIVANPGF VINPHYIYLL
     ERKGLNNDTL YLKFKINYSK LIHIPKKKVF NFENLEIALG TRYVPDVSDD IGTEPENVFN
     LSTLRQINTD PSDESQDRDS EESYGGHGRP EGVGCAQQ
 
 
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