(data stored in SCRATCH zone)

SWISSPROT: A0A0H2Y3T3_YERPA

ID   A0A0H2Y3T3_YERPA        Unreviewed;       185 AA.
AC   A0A0H2Y3T3;
DT   16-SEP-2015, integrated into UniProtKB/TrEMBL.
DT   16-SEP-2015, sequence version 1.
DT   08-MAY-2019, entry version 19.
DE   RecName: Full=Protein SprT {ECO:0000256|HAMAP-Rule:MF_00746, ECO:0000256|SAAS:SAAS00012266};
GN   Name=sprT {ECO:0000256|HAMAP-Rule:MF_00746};
GN   OrderedLocusNames=YPA_0334 {ECO:0000313|EMBL:ABG12302.1};
OS   Yersinia pestis bv. Antiqua (strain Antiqua).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Yersiniaceae; Yersinia.
OX   NCBI_TaxID=360102 {ECO:0000313|EMBL:ABG12302.1, ECO:0000313|Proteomes:UP000001971};
RN   [1] {ECO:0000313|EMBL:ABG12302.1, ECO:0000313|Proteomes:UP000001971}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Antiqua {ECO:0000313|EMBL:ABG12302.1,
RC   ECO:0000313|Proteomes:UP000001971};
RX   PubMed=16740952; DOI=10.1128/JB.00124-06;
RA   Chain P.S., Hu P., Malfatti S.A., Radnedge L., Larimer F.,
RA   Vergez L.M., Worsham P., Chu M.C., Andersen G.L.;
RT   "Complete genome sequence of Yersinia pestis strains Antiqua and
RT   Nepal516: evidence of gene reduction in an emerging pathogen.";
RL   J. Bacteriol. 188:4453-4463(2006).
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000256|HAMAP-
CC         Rule:MF_00746};
CC       Note=Binds 1 zinc ion. {ECO:0000256|HAMAP-Rule:MF_00746};
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00746,
CC       ECO:0000256|SAAS:SAAS00846174}.
CC   -!- SIMILARITY: Belongs to the SprT family. {ECO:0000256|HAMAP-
CC       Rule:MF_00746, ECO:0000256|SAAS:SAAS00846167}.
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DR   EMBL; CP000308; ABG12302.1; -; Genomic_DNA.
DR   EnsemblBacteria; ABG12302; ABG12302; YPA_0334.
DR   KEGG; ypa:YPA_0334; -.
DR   KO; K02742; -.
DR   OMA; QPHGEEW; -.
DR   Proteomes; UP000001971; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-UniRule.
DR   HAMAP; MF_00746; SprT; 1.
DR   InterPro; IPR006640; SprT-like_domain.
DR   InterPro; IPR035240; SprT_Zn_ribbon.
DR   InterPro; IPR023483; Uncharacterised_SprT.
DR   Pfam; PF10263; SprT-like; 1.
DR   Pfam; PF17283; Zn_ribbon_SprT; 1.
DR   SMART; SM00731; SprT; 1.
PE   3: Inferred from homology;
DR   PRODOM; A0A0H2Y3T3.
DR   SWISS-2DPAGE; A0A0H2Y3T3.
KW   Complete proteome {ECO:0000313|Proteomes:UP000001971};
KW   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00746,
KW   ECO:0000256|SAAS:SAAS00846153};
KW   Metal-binding {ECO:0000256|HAMAP-Rule:MF_00746,
KW   ECO:0000256|SAAS:SAAS00846161};
KW   Zinc {ECO:0000256|HAMAP-Rule:MF_00746, ECO:0000256|SAAS:SAAS00846170}.
FT   DOMAIN       31    180       SprT-like. {ECO:0000259|SMART:SM00731}.
FT   ACT_SITE     94     94       {ECO:0000256|HAMAP-Rule:MF_00746}.
FT   METAL        93     93       Zinc. {ECO:0000256|HAMAP-Rule:MF_00746}.
FT   METAL        97     97       Zinc. {ECO:0000256|HAMAP-Rule:MF_00746}.
SQ   SEQUENCE   185 AA;  21676 MW;  8937CD54776BB434 CRC64;
     MSACIWLSTV LFFRIMSTLR IPIALQQAVM QCLRHYLQLA NQHLGTAYPE PKVNYHQRGT
     NAGSAYLQSF EIRLNPVLLL ENKQPFIDEV VPHELAHLLV YRQFGRVAPH GKEWRWMMEQ
     VLKVPASRTH QFEVASVRSK TFNYQCKCQQ HALTIRRHNK VLRGESEYRC RQCGEKLQFI
     TINPD
//

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