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ORN_YERPS
ID   ORN_YERPS               Reviewed;         181 AA.
AC   Q66FC2;
DT   15-FEB-2005, integrated into UniProtKB/Swiss-Prot.
DT   11-OCT-2004, sequence version 1.
DT   25-MAY-2022, entry version 86.
DE   RecName: Full=Oligoribonuclease {ECO:0000255|HAMAP-Rule:MF_00045};
DE            EC=3.1.15.- {ECO:0000255|HAMAP-Rule:MF_00045};
GN   Name=orn {ECO:0000255|HAMAP-Rule:MF_00045}; OrderedLocusNames=YPTB0418;
OS   Yersinia pseudotuberculosis serotype I (strain IP32953).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Yersiniaceae; Yersinia.
OX   NCBI_TaxID=273123;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=IP32953;
RX   PubMed=15358858; DOI=10.1073/pnas.0404012101;
RA   Chain P.S.G., Carniel E., Larimer F.W., Lamerdin J., Stoutland P.O.,
RA   Regala W.M., Georgescu A.M., Vergez L.M., Land M.L., Motin V.L.,
RA   Brubaker R.R., Fowler J., Hinnebusch J., Marceau M., Medigue C.,
RA   Simonet M., Chenal-Francisque V., Souza B., Dacheux D., Elliott J.M.,
RA   Derbise A., Hauser L.J., Garcia E.;
RT   "Insights into the evolution of Yersinia pestis through whole-genome
RT   comparison with Yersinia pseudotuberculosis.";
RL   Proc. Natl. Acad. Sci. U.S.A. 101:13826-13831(2004).
CC   -!- FUNCTION: 3'-to-5' exoribonuclease specific for small
CC       oligoribonucleotides. {ECO:0000255|HAMAP-Rule:MF_00045}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00045}.
CC   -!- SIMILARITY: Belongs to the oligoribonuclease family.
CC       {ECO:0000255|HAMAP-Rule:MF_00045}.
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DR   EMBL; BX936398; CAH19658.1; -; Genomic_DNA.
DR   RefSeq; WP_011191612.1; NZ_CP009712.1.
DR   AlphaFoldDB; Q66FC2; -.
DR   SMR; Q66FC2; -.
DR   EnsemblBacteria; CAH19658; CAH19658; YPTB0418.
DR   GeneID; 66843167; -.
DR   KEGG; ypo:BZ17_2151; -.
DR   KEGG; yps:YPTB0418; -.
DR   PATRIC; fig|273123.14.peg.2275; -.
DR   OMA; AFFHYRN; -.
DR   Proteomes; UP000001011; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0000175; F:3'-5'-exoribonuclease activity; IEA:InterPro.
DR   GO; GO:0003676; F:nucleic acid binding; IEA:InterPro.
DR   CDD; cd06135; Orn; 1.
DR   Gene3D; 3.30.420.10; -; 1.
DR   HAMAP; MF_00045; Oligoribonuclease; 1.
DR   InterPro; IPR013520; Exonuclease_RNaseT/DNA_pol3.
DR   InterPro; IPR022894; Oligoribonuclease.
DR   InterPro; IPR012337; RNaseH-like_sf.
DR   InterPro; IPR036397; RNaseH_sf.
DR   PANTHER; PTHR11046; PTHR11046; 1.
DR   Pfam; PF00929; RNase_T; 1.
DR   SMART; SM00479; EXOIII; 1.
DR   SUPFAM; SSF53098; SSF53098; 1.
PE   3: Inferred from homology;
KW   Cytoplasm; Exonuclease; Hydrolase; Nuclease.
FT   CHAIN           1..181
FT                   /note="Oligoribonuclease"
FT                   /id="PRO_0000111089"
FT   DOMAIN          8..171
FT                   /note="Exonuclease"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00045"
FT   ACT_SITE        129
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00045"
SQ   SEQUENCE   181 AA;  20906 MW;  3558A0C8E5648EC4 CRC64;
     MAENQNNLIW IDLEMTGLDP ERDRIIEIAT LVTDANLNIL AEGPVLAVHQ SAEQLGLMDE
     WNVRTHTGSG LVERVKTSPF NDRDAELQTI EFLKQWVPAG VSPICGNSVG QDRRFLFRYM
     PELEAYFHYR YVDVSTLKEL ARRWKPEILA GFKKQNTHQA LDDIRESVAE LAYYREHFIQ
     S
 
 
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