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Database: UniProt
Entry: D1W0T5_9BACT
LinkDB: D1W0T5_9BACT
Original site: D1W0T5_9BACT 
ID   D1W0T5_9BACT            Unreviewed;       766 AA.
AC   D1W0T5;
DT   09-FEB-2010, integrated into UniProtKB/TrEMBL.
DT   09-FEB-2010, sequence version 1.
DT   05-JUN-2019, entry version 53.
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   ECO:0000313|EMBL:EFA97001.1};
GN   ORFNames=HMPREF9019_1221 {ECO:0000313|EMBL:EFA97001.1};
OS   Prevotella timonensis CRIS 5C-B1.
OC   Bacteria; Bacteroidetes; Bacteroidia; Bacteroidales; Prevotellaceae;
OC   Prevotella.
OX   NCBI_TaxID=679189 {ECO:0000313|EMBL:EFA97001.1, ECO:0000313|Proteomes:UP000004001};
RN   [1] {ECO:0000313|EMBL:EFA97001.1, ECO:0000313|Proteomes:UP000004001}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CRIS 5C-B1 {ECO:0000313|EMBL:EFA97001.1,
RC   ECO:0000313|Proteomes:UP000004001};
RA   Durkin A.S., Madupu R., Torralba M., Methe B., Sutton G.,
RA   Strausberg R.L., Nelson K.E.;
RT   "Genome Sequence of Prevotella timonensis CRIS 5C-B1.";
RL   Submitted (DEC-2009) 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:EFA97001.1}.
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DR   EMBL; ADEF01000048; EFA97001.1; -; Genomic_DNA.
DR   STRING; 679189.HMPREF9019_1221; -.
DR   EnsemblBacteria; EFA97001; EFA97001; HMPREF9019_1221.
DR   eggNOG; ENOG4105C62; Bacteria.
DR   eggNOG; COG1185; LUCA.
DR   Proteomes; UP000004001; Unassembled WGS sequence.
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   Complete proteome {ECO:0000313|Proteomes:UP000004001};
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, ECO:0000313|EMBL:EFA97001.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000004001};
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:EFA97001.1}.
FT   DOMAIN      625    695       S1 motif. {ECO:0000259|PROSITE:PS50126}.
FT   REGION      703    766       Disordered. {ECO:0000256|MobiDB-lite:
FT                                D1W0T5}.
FT   COMPBIAS    703    759       Polyampholyte. {ECO:0000256|MobiDB-lite:
FT                                D1W0T5}.
FT   METAL       486    486       Magnesium. {ECO:0000256|HAMAP-Rule:
FT                                MF_01595}.
FT   METAL       492    492       Magnesium. {ECO:0000256|HAMAP-Rule:
FT                                MF_01595}.
SQ   SEQUENCE   766 AA;  85518 MW;  DCF3668ED90B0958 CRC64;
     MPDGRTISIE TGKVAKQADG SAVVRLGNTV LLATVCAAKD AVPGTDFMPL QVDYREQYSA
     AGRFPGGFTK REGKPSDNEI LTSRLVDRAL RPLFPSNYHA EVYVQIMLLS ADGVDQPDAL
     AGLAASAAMA CSDIPFDFYI SEVRVARING EYVVNPTFEQ MKSADMDLMV GATKDNIMMV
     EGEMNEVSEL DLIEALKAAH EAIKPMCTVQ EELNKELGKD VKREYDHEVN DEDLRQQMND
     ELYQPAYDIT KQALPKQERH DAFDKIIADF LEKYDAAHAD LTEEELEEKH AEATRYYDDV
     LKNAMRRCIL DEGKRLDGRK TDEIRPIWCE VSPLPMPHGS AIFTRGETQS LSTCTLGTKL
     DEKMVDDVLD KSYQRFLLHY NFPPFSTGEA KAQRGVGRRE IGHGHLAWRG LKGQIPEDFP
     YTVRLVSQIL ESNGSSSMAT VCAGTLALMD AGVPMKKPVS GIAMGLIKNP GEDKYVILSD
     ILGDEDHLGD MDFKTTGTRD GLTATQMDIK CDGLSFEILE KALMQAKAGR EHILGKMLET
     MPEPRSEMKP QVPRIEAFEI PKEFIGAIIG PGGKIIQQMQ EDTGATITID ELDGVGKIQV
     SAPNKEAIDS AIAKIKGIVA IPEIGEVYEG TVRSIMPYGC FVEILPGKDG LLHISEIDWK
     RLETVEDAGI HEGDKIKVKL LEIDPKTGKY KLSRKVLLEK PEGYVERERR PRPERRNNMN
     NERRPRRDDD NGYHHRNNGG YGDRPQRRFE HHDDNVDSVD NTSNDF
//
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