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