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PNP_CORU7
ID   PNP_CORU7               Reviewed;         765 AA.
AC   B1VDC1;
DT   01-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT   20-MAY-2008, sequence version 1.
DT   03-AUG-2022, entry version 88.
DE   RecName: Full=Polyribonucleotide nucleotidyltransferase {ECO:0000255|HAMAP-Rule:MF_01595};
DE            EC=2.7.7.8 {ECO:0000255|HAMAP-Rule:MF_01595};
DE   AltName: Full=Polynucleotide phosphorylase {ECO:0000255|HAMAP-Rule:MF_01595};
DE            Short=PNPase {ECO:0000255|HAMAP-Rule:MF_01595};
GN   Name=pnp {ECO:0000255|HAMAP-Rule:MF_01595}; OrderedLocusNames=cu0859;
OS   Corynebacterium urealyticum (strain ATCC 43042 / DSM 7109).
OC   Bacteria; Actinobacteria; Corynebacteriales; Corynebacteriaceae;
OC   Corynebacterium.
OX   NCBI_TaxID=504474;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 43042 / DSM 7109;
RX   PubMed=18367281; DOI=10.1016/j.jbiotec.2008.02.009;
RA   Tauch A., Trost E., Tilker A., Ludewig U., Schneiker S., Goesmann A.,
RA   Arnold W., Bekel T., Brinkrolf K., Brune I., Goetker S., Kalinowski J.,
RA   Kamp P.-B., Lobo F.P., Viehoever P., Weisshaar B., Soriano F., Droege M.,
RA   Puehler A.;
RT   "The lifestyle of Corynebacterium urealyticum derived from its complete
RT   genome sequence established by pyrosequencing.";
RL   J. Biotechnol. 136:11-21(2008).
CC   -!- FUNCTION: Involved in mRNA degradation. Catalyzes the phosphorolysis of
CC       single-stranded polyribonucleotides processively in the 3'- to 5'-
CC       direction. {ECO:0000255|HAMAP-Rule:MF_01595}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=phosphate + RNA(n+1) = a ribonucleoside 5'-diphosphate +
CC         RNA(n); Xref=Rhea:RHEA:22096, Rhea:RHEA-COMP:14527, Rhea:RHEA-
CC         COMP:17342, ChEBI:CHEBI:43474, ChEBI:CHEBI:57930, ChEBI:CHEBI:140395;
CC         EC=2.7.7.8; Evidence={ECO:0000255|HAMAP-Rule:MF_01595};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_01595};
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_01595}.
CC   -!- SIMILARITY: Belongs to the polyribonucleotide nucleotidyltransferase
CC       family. {ECO:0000255|HAMAP-Rule:MF_01595}.
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DR   EMBL; AM942444; CAQ04819.1; -; Genomic_DNA.
DR   AlphaFoldDB; B1VDC1; -.
DR   SMR; B1VDC1; -.
DR   STRING; 504474.cu0859; -.
DR   EnsemblBacteria; CAQ04819; CAQ04819; cu0859.
DR   KEGG; cur:cu0859; -.
DR   eggNOG; COG1185; Bacteria.
DR   HOGENOM; CLU_004217_2_2_11; -.
DR   OMA; LHILDVM; -.
DR   OrthoDB; 122725at2; -.
DR   Proteomes; UP000001727; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0004654; F:polyribonucleotide nucleotidyltransferase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0003723; F:RNA binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0006402; P:mRNA catabolic process; IEA:UniProtKB-UniRule.
DR   GO; GO:0006396; P:RNA processing; IEA:InterPro.
DR   Gene3D; 2.40.50.140; -; 1.
DR   Gene3D; 3.30.1370.10; -; 1.
DR   Gene3D; 3.30.230.70; -; 2.
DR   HAMAP; MF_01595; PNPase; 1.
DR   InterPro; IPR001247; ExoRNase_PH_dom1.
DR   InterPro; IPR036345; ExoRNase_PH_dom2_sf.
DR   InterPro; IPR014069; GPSI/PNP.
DR   InterPro; IPR004087; KH_dom.
DR   InterPro; IPR004088; KH_dom_type_1.
DR   InterPro; IPR036612; KH_dom_type_1_sf.
DR   InterPro; IPR012340; NA-bd_OB-fold.
DR   InterPro; IPR012162; PNPase.
DR   InterPro; IPR027408; PNPase/RNase_PH_dom_sf.
DR   InterPro; IPR015848; PNPase_PH_RNA-bd_bac/org-type.
DR   InterPro; IPR036456; PNPase_PH_RNA-bd_sf.
DR   InterPro; IPR020568; Ribosomal_S5_D2-typ_fold.
DR   InterPro; IPR022967; S1_dom.
DR   InterPro; IPR003029; S1_domain.
DR   PANTHER; PTHR11252; PTHR11252; 1.
DR   Pfam; PF00013; KH_1; 1.
DR   Pfam; PF03726; PNPase; 1.
DR   Pfam; PF01138; RNase_PH; 2.
DR   Pfam; PF00575; S1; 1.
DR   PIRSF; PIRSF005499; PNPase; 1.
DR   SMART; SM00322; KH; 1.
DR   SMART; SM00316; S1; 1.
DR   SUPFAM; SSF46915; SSF46915; 1.
DR   SUPFAM; SSF50249; SSF50249; 1.
DR   SUPFAM; SSF54211; SSF54211; 2.
DR   SUPFAM; SSF54791; SSF54791; 1.
DR   SUPFAM; SSF55666; SSF55666; 2.
DR   TIGRFAMs; TIGR03591; polynuc_phos; 1.
DR   TIGRFAMs; TIGR02696; pppGpp_PNP; 1.
DR   PROSITE; PS50084; KH_TYPE_1; 1.
DR   PROSITE; PS50126; S1; 1.
PE   3: Inferred from homology;
KW   Cytoplasm; Magnesium; Metal-binding; Nucleotidyltransferase;
KW   Reference proteome; RNA-binding; Transferase.
FT   CHAIN           1..765
FT                   /note="Polyribonucleotide nucleotidyltransferase"
FT                   /id="PRO_0000381880"
FT   DOMAIN          622..681
FT                   /note="KH"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01595"
FT   DOMAIN          693..762
FT                   /note="S1 motif"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01595"
FT   BINDING         556
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01595"
FT   BINDING         562
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01595"
SQ   SEQUENCE   765 AA;  82266 MW;  35F3EC377B492883 CRC64;
     MKGRGTHAMS SKKNNLPKNV SVEMVDPDAG IWEATATIDN GDFGSRTLRF ETGLLARQAD
     GAVTAYLDED TILLSTTTAS RSPREGIDFF PLTVDVEERM YSAGRIPGSF FRREGRPGTD
     AILAARLIDR PLRPTFVKGL RNEVQVVITV MSIDPNEMYD VLAINGASAS TQLSGLPVSS
     SVGGVRMALV VDEEHPEGQW VAFPTREQVS QSVFELVVAG RVTEPAKGGR GKKSQPNVAV
     MMVEAGATDN VVERIAEGAP APTEAVVAEG IEAAKPFIAT LCAAQDALRD AVDTESREFE
     LFPPFDEDVY SAVEAECDAD VAQIMTIADK QERDESLAEN MQETVDALIE QFPERESEIR
     AAHNDLTRTI VRQRILEDGF RIDGRDHTSI RDLGIVVQLL PRAHGSALFE RGETQILGVT
     TLDTLKMEQT IDSLGPETSK RYIHHYNFPP YSTGETGRVG SPKRREIGHG ALAERALTPV
     LPSREEFPYT IRQVSEALGS NGSTSMGSVC ASTLSLYNAG VPLKAPVAGI AMGLVSGLVD
     GKEKFVSLTD ILGAEDAFGD MDFKVAGTSE YVTALQLDTK LDGLPSEVLA SALGQARSAR
     LEILQLMEDA IDAPDQMSEL APRITKISIP QNKIGEVIGP KGKTINQITE ETGANISIED
     DGTVFVSAVG GEAAEAAIEK INAIANPQQP KVGDRFLGTV VKTTAFGAFI SLLPGRDGLL
     HISNIGGDRR IEKVEDELNV GDKIQVEIAD IDNRGKISLV PVDED
 
 
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