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PNP_ANAMF
ID   PNP_ANAMF               Reviewed;         805 AA.
AC   B9KIE3;
DT   01-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT   24-MAR-2009, sequence version 1.
DT   03-AUG-2022, entry version 71.
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=AMF_391;
OS   Anaplasma marginale (strain Florida).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rickettsiales;
OC   Anaplasmataceae; Anaplasma.
OX   NCBI_TaxID=320483;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Florida;
RX   PubMed=19134224; DOI=10.1186/1471-2164-10-16;
RA   Dark M.J., Herndon D.R., Kappmeyer L.S., Gonzales M.P., Nordeen E.,
RA   Palmer G.H., Knowles D.P. Jr., Brayton K.A.;
RT   "Conservation in the face of diversity: multistrain analysis of an
RT   intracellular bacterium.";
RL   BMC Genomics 10:16-16(2009).
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; CP001079; ACM49255.1; -; Genomic_DNA.
DR   RefSeq; WP_012658930.1; NC_012026.1.
DR   AlphaFoldDB; B9KIE3; -.
DR   SMR; B9KIE3; -.
DR   STRING; 320483.AMF_391; -.
DR   EnsemblBacteria; ACM49255; ACM49255; AMF_391.
DR   GeneID; 7397935; -.
DR   KEGG; amf:AMF_391; -.
DR   PATRIC; fig|320483.3.peg.455; -.
DR   eggNOG; COG1185; Bacteria.
DR   HOGENOM; CLU_004217_2_2_5; -.
DR   OMA; LHILDVM; -.
DR   Proteomes; UP000007307; 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   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; IPR015847; ExoRNase_PH_dom2.
DR   InterPro; IPR036345; ExoRNase_PH_dom2_sf.
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; 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; PF01138; RNase_PH; 2.
DR   Pfam; PF03725; RNase_PH_C; 1.
DR   Pfam; PF00575; S1; 1.
DR   PIRSF; PIRSF005499; PNPase; 1.
DR   SMART; SM00322; KH; 1.
DR   SMART; SM00316; S1; 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   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..805
FT                   /note="Polyribonucleotide nucleotidyltransferase"
FT                   /id="PRO_0000381865"
FT   DOMAIN          558..617
FT                   /note="KH"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01595"
FT   DOMAIN          627..694
FT                   /note="S1 motif"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01595"
FT   REGION          702..805
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         491
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01595"
FT   BINDING         497
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01595"
SQ   SEQUENCE   805 AA;  87147 MW;  58EB5A9260C4E15A CRC64;
     MFDITRKCVE WGDRLLVIES GKIARQADGA VVVDYGGTSV LSTVVSQKSK EPVDFLPLTV
     QFLAKSYAIG RIPGGFFKRE GKPSDRETLI SRLVDRSIRP LFPTGFCDEI VIVCNLLSYD
     QVSPPETVAL IGAAAALAIS GIPFPTPIAG AKIGYIREEE RYILNPSAEE LARSELDMFY
     SGTKSSVVMV ESEASELSEE EMLGAVTFGH ENCAQVLDLI EEFAEAAGPK DVVEFVPHDI
     GKVVSDISSG YSEKFSVAYS DHNKKPECSS LMPPGKACTQ ICAGKHVEES GEYTEQEVLL
     AIKTFERSLV RARVLDTLKR VDGRGFDQIR NIEIEVDLIP RSHGSALFTR GDTQALVITA
     LGTPQDEQVV DGFDGDRRER FLLHYNFPSY AVGEAAALRP PGRREIGHGK LAWRAIHPVL
     PTKADFPYTI RVVSEITESD GSSSMATVCG ASLALMDTGV PLKSSVAGIA MGLIKEGDRY
     AVLSDIIGDE DYLGDMDFKV AGTKDGITAL QMDMKIRGIG FDIIEKSLQQ AKDGRLFIIG
     KMDKVIKESR EGVRDHVPRM ESMIIDKNKI KNVIGTGGKN VREICEKTGV KIEISQDGTV
     MIYAVSRDAV EEAKNMIMCI VSEPEVGKVF SGVISEIAKY GAFVSFLGGR RGLVHISEIK
     NEHIGSVSDV LAVDDKVKVL VIGIDKDHVQ LSMRRVDQDS GDLLEHESYS SNKKNGPQFG
     DASGGASGFR DYASGPARER RRSGGSGGRP VRRRSAGSSG SGSGGCYSVP QHVGTPDPVH
     GNDRRRGSGP QHASGGGGNK KPRFF
 
 
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