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Database: UniProt
Entry: A0A177R7T0_9BACT
LinkDB: A0A177R7T0_9BACT
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ID   A0A177R7T0_9BACT        Unreviewed;       710 AA.
AC   A0A177R7T0;
DT   07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT   07-SEP-2016, sequence version 1.
DT   16-JAN-2019, entry version 14.
DE   RecName: Full=Polyribonucleotide nucleotidyltransferase {ECO:0000256|HAMAP-Rule:MF_01595};
DE            EC=2.7.7.8 {ECO:0000256|HAMAP-Rule:MF_01595};
DE   AltName: Full=Polynucleotide phosphorylase {ECO:0000256|HAMAP-Rule:MF_01595};
DE            Short=PNPase {ECO:0000256|HAMAP-Rule:MF_01595};
GN   Name=pnp {ECO:0000256|HAMAP-Rule:MF_01595};
GN   ORFNames=AYO49_01145 {ECO:0000313|EMBL:OAI55515.1};
OS   Verrucomicrobiaceae bacterium SCGC AG-212-N21.
OC   Bacteria; Verrucomicrobia; Verrucomicrobiae; Verrucomicrobiales;
OC   Verrucomicrobiaceae; unclassified Verrucomicrobiaceae.
OX   NCBI_TaxID=1799659 {ECO:0000313|EMBL:OAI55515.1};
RN   [1] {ECO:0000313|EMBL:OAI55515.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SCGC AG-212-N21 {ECO:0000313|EMBL:OAI55515.1};
RA   Wen L., He K., Yang H.;
RL   Submitted (FEB-2016) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Involved in mRNA degradation. Catalyzes the
CC       phosphorolysis of single-stranded polyribonucleotides processively
CC       in the 3'- to 5'-direction. {ECO:0000256|HAMAP-Rule:MF_01595,
CC       ECO:0000256|SAAS:SAAS00979022}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=phosphate + RNA(n+1) = a ribonucleoside 5'-diphosphate +
CC         RNA(n); Xref=Rhea:RHEA:22096, Rhea:RHEA-COMP:11128, Rhea:RHEA-
CC         COMP:11129, ChEBI:CHEBI:43474, ChEBI:CHEBI:57930,
CC         ChEBI:CHEBI:83400; EC=2.7.7.8; Evidence={ECO:0000256|HAMAP-
CC         Rule:MF_01595, ECO:0000256|SAAS:SAAS01115795};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000256|HAMAP-
CC         Rule:MF_01595, ECO:0000256|SAAS:SAAS00979019};
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_01595,
CC       ECO:0000256|SAAS:SAAS00979031}.
CC   -!- SIMILARITY: Belongs to the polyribonucleotide
CC       nucleotidyltransferase family. {ECO:0000256|HAMAP-Rule:MF_01595,
CC       ECO:0000256|SAAS:SAAS00979043}.
CC   -!- CAUTION: The sequence shown here is derived from an
CC       EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is
CC       preliminary data. {ECO:0000313|EMBL:OAI55515.1}.
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DR   EMBL; LSTJ01000144; OAI55515.1; -; Genomic_DNA.
DR   EnsemblBacteria; OAI55515; OAI55515; AYO49_01145.
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; 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; 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; 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; 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   PROSITE; PS50126; S1; 1.
PE   3: Inferred from homology;
KW   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_01595,
KW   ECO:0000256|SAAS:SAAS00979026};
KW   Magnesium {ECO:0000256|HAMAP-Rule:MF_01595,
KW   ECO:0000256|SAAS:SAAS00979039};
KW   Metal-binding {ECO:0000256|HAMAP-Rule:MF_01595,
KW   ECO:0000256|SAAS:SAAS00979046};
KW   Nucleotidyltransferase {ECO:0000256|HAMAP-Rule:MF_01595,
KW   ECO:0000256|SAAS:SAAS00979037};
KW   RNA-binding {ECO:0000256|HAMAP-Rule:MF_01595,
KW   ECO:0000256|SAAS:SAAS00979024};
KW   Transferase {ECO:0000256|HAMAP-Rule:MF_01595,
KW   ECO:0000256|SAAS:SAAS00979029, ECO:0000313|EMBL:OAI55515.1}.
FT   DOMAIN      627    695       S1 motif. {ECO:0000259|PROSITE:PS50126}.
FT   METAL       492    492       Magnesium. {ECO:0000256|HAMAP-Rule:
FT                                MF_01595}.
FT   METAL       498    498       Magnesium. {ECO:0000256|HAMAP-Rule:
FT                                MF_01595}.
SQ   SEQUENCE   710 AA;  76175 MW;  7739C5ACBE4731F0 CRC64;
     MAIHNVTAAL PNGDITIETG KLAKLADGAV TVRMGETIVI VTAVSATKVK EGQDFFPLSV
     EYKEKAAAAG KFPGGYFKRE GRPTEKEILT CRMTDRPLRP LFPKGYYFDT QIVALLLSAD
     GENDSDILAM NGASAALCVS DIPFAGPIGA VRIGRVNGQF IVNPTHAQRD KSDLDLVYVG
     SKTDVIMIEG AANELPEDEF IKALAFAQEQ VQVLVAAQEQ LKAAAGKAKR EVKLMLVKDE
     LLEVAYEIAG SRIEDAIYRP SKTERAKAIG ALKDEVEAAI KAKFPEAGNF EISQAFDYLQ
     KKSFRISILD KQKRADGRGV DQLRQLSGEV GVLPRAHGSA LFARGETQAL ALATLAPLDE
     AQEMDTYAGG ADSKRFILHY NFPPFSVGET GRFGGQNRRE IGHGALAERS VEPVVPSEED
     FPYAIRVSSE VMESNGSTSM ASVCSGVMAL LDAGVPLKRP VAGISVGLVT EFDASEKMSR
     YLTMLDIIGS EDHFGDMDFK LCGTDLGVTG FQLDLKLPGI PLSILNEAVA KAKTGRTDIL
     AVMNSSIAEA KPLSQYAPRI EKTKINPDKI GELIGPGGKN IKAIQAESGA DISIQDDGTV
     LIYASSKEAL ERALELVNNT VGEVEVGRNY TGRVVSTTNF GAFMSLGGKK DGLIHISELA
     DFRVERVEDV VKVGDTVTAK CIGVDDKGRV KMSRKAVLKE KDKGAPAPQA
//
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