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YICR_SALHS
ID   YICR_SALHS              Reviewed;         221 AA.
AC   B4T9C3;
DT   24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT   23-SEP-2008, sequence version 1.
DT   03-AUG-2022, entry version 70.
DE   RecName: Full=UPF0758 protein YicR {ECO:0000255|HAMAP-Rule:MF_00018};
GN   Name=yicR {ECO:0000255|HAMAP-Rule:MF_00018}; OrderedLocusNames=SeHA_C4055;
OS   Salmonella heidelberg (strain SL476).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Salmonella.
OX   NCBI_TaxID=454169;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SL476;
RX   PubMed=21602358; DOI=10.1128/jb.00297-11;
RA   Fricke W.F., Mammel M.K., McDermott P.F., Tartera C., White D.G.,
RA   Leclerc J.E., Ravel J., Cebula T.A.;
RT   "Comparative genomics of 28 Salmonella enterica isolates: evidence for
RT   CRISPR-mediated adaptive sublineage evolution.";
RL   J. Bacteriol. 193:3556-3568(2011).
CC   -!- SIMILARITY: Belongs to the UPF0758 family. YicR subfamily.
CC       {ECO:0000255|HAMAP-Rule:MF_00018}.
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DR   EMBL; CP001120; ACF65969.1; -; Genomic_DNA.
DR   RefSeq; WP_000380129.1; NC_011083.1.
DR   AlphaFoldDB; B4T9C3; -.
DR   SMR; B4T9C3; -.
DR   KEGG; seh:SeHA_C4055; -.
DR   HOGENOM; CLU_073529_0_1_6; -.
DR   OMA; AMPDYEL; -.
DR   Proteomes; UP000001866; Chromosome.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0008237; F:metallopeptidase activity; IEA:UniProtKB-KW.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR   CDD; cd08071; MPN_DUF2466; 1.
DR   HAMAP; MF_00018; UPF0758_YicR; 1.
DR   InterPro; IPR037518; MPN.
DR   InterPro; IPR025657; RadC_JAB.
DR   InterPro; IPR010994; RuvA_2-like.
DR   InterPro; IPR001405; UPF0758.
DR   InterPro; IPR020891; UPF0758_CS.
DR   InterPro; IPR022820; UPF0758_YicR.
DR   PANTHER; PTHR30471; PTHR30471; 1.
DR   Pfam; PF04002; RadC; 1.
DR   SUPFAM; SSF47781; SSF47781; 1.
DR   TIGRFAMs; TIGR00608; radc; 1.
DR   PROSITE; PS50249; MPN; 1.
DR   PROSITE; PS01302; UPF0758; 1.
PE   3: Inferred from homology;
KW   Hydrolase; Metal-binding; Metalloprotease; Protease; Zinc.
FT   CHAIN           1..221
FT                   /note="UPF0758 protein YicR"
FT                   /id="PRO_1000089841"
FT   DOMAIN          99..221
FT                   /note="MPN"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01182"
FT   MOTIF           170..183
FT                   /note="JAMM motif"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01182"
FT   BINDING         170
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01182"
FT   BINDING         172
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01182"
FT   BINDING         183
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01182"
SQ   SEQUENCE   221 AA;  24890 MW;  07E83A9DD9D50444 CRC64;
     MDTLDELLPR EKMLRSGIAS LSDVELLALF LRTGTPGKDV MTLAKEILQH FGSLYGLLSA
     DFAQFRGVNG IGLAKFAQLK GIAELARRYY SVRMNEESAL LSPEMTREFL QSQLTGEERE
     IFLVIFLDAQ HRVLQHSRLF SGTLNHVEVH PREIVREAIK LNASAVILAH NHPSGCAEPS
     KADKLITERV IKCCQFMDIR VLDHLIIGRG EYVSFAERGW I
 
 
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