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Database: UniProt
Entry: W7UYH2_RUMFL
LinkDB: W7UYH2_RUMFL
Original site: W7UYH2_RUMFL 
ID   W7UYH2_RUMFL            Unreviewed;       704 AA.
AC   W7UYH2;
DT   16-APR-2014, integrated into UniProtKB/TrEMBL.
DT   16-APR-2014, sequence version 1.
DT   10-APR-2019, entry version 26.
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=RF007C_06485 {ECO:0000313|EMBL:EWM53705.1};
OS   Ruminococcus flavefaciens 007c.
OC   Bacteria; Firmicutes; Clostridia; Clostridiales; Ruminococcaceae;
OC   Ruminococcus.
OX   NCBI_TaxID=1341157 {ECO:0000313|EMBL:EWM53705.1, ECO:0000313|Proteomes:UP000019365};
RN   [1] {ECO:0000313|EMBL:EWM53705.1, ECO:0000313|Proteomes:UP000019365}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=007c {ECO:0000313|EMBL:EWM53705.1,
RC   ECO:0000313|Proteomes:UP000019365};
RX   PubMed=24992679;
RA   Dassa B., Borovok I., Ruimy-Israeli V., Lamed R., Flint H.J.,
RA   Duncan S.H., Henrissat B., Coutinho P., Morrison M., Mosoni P.,
RA   Yeoman C.J., White B.A., Bayer E.A.;
RT   "Rumen cellulosomics: divergent fiber-degrading strategies revealed by
RT   comparative genome-wide analysis of six ruminococcal strains.";
RL   PLoS ONE 9:E99221-E99221(2014).
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:EWM53705.1}.
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DR   EMBL; ATAX01000024; EWM53705.1; -; Genomic_DNA.
DR   RefSeq; WP_037299131.1; NZ_ATAX01000024.1.
DR   STRING; 1341157.RF007C_06485; -.
DR   EnsemblBacteria; EWM53705; EWM53705; RF007C_06485.
DR   PATRIC; fig|1341157.4.peg.1730; -.
DR   Proteomes; UP000019365; 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:UP000019365};
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:EWM53705.1}.
FT   DOMAIN      624    692       S1 motif. {ECO:0000259|PROSITE:PS50126}.
FT   METAL       487    487       Magnesium. {ECO:0000256|HAMAP-Rule:
FT                                MF_01595}.
FT   METAL       493    493       Magnesium. {ECO:0000256|HAMAP-Rule:
FT                                MF_01595}.
SQ   SEQUENCE   704 AA;  77145 MW;  ACA6465F95CFB148 CRC64;
     MFENYRTFET TYAGRPLVVE TGKTCGLSNG SCWVRYGETV VMANVTASAK PREGIDFFPL
     SVDYEERLYS VGKIPGSFTK REGKPSEKAI LTSRCVDRPI RPLFPKDMRN DVSVVMTVLA
     VEPDNSPEIA GMIATSIAIS ISDIPWNGPI AGINVGLVDG EIVLNPTLEQ RAKTDLTLTV
     AGTADKIVMI EAGANEVPED TMLDAILKGH EEIKKMVSFI NDIRAQIGKP KFEFESMEVD
     HDMFDAIEAF ASDRVKIALD TNDKNVRDER LAPIIDDIHA NFDEKYPEQI PMIDECIYKL
     QKKIVRTWLY EGKRVDGRGI DEIRPLAAEV GVLPRVHGSG LFTRGQTQVL TIATLGPVSD
     AQKIDGLDEE DSKRYMHQYN FPSYSVGETK PSRGPGRREI GHGALAERAL APVIPPVEEF
     PYALRLVSEV LSSNGSTSQG SICGSTLALM DAGVPIKAPV AGISCGLITL PDSDEFMTMV
     DIQGLEDFFG DMDFKVGGTH KGITAIQVDI KVDGLTPAII KEAFEKTRKA RLYILDEIML
     KAIPESRPTV NKYAPKMLQT KIPVDKIREV IGQGGKVIQK ISADCDVKID ISDDGNVFIS
     GVDADNANKA LQIVHTIAND PEVGAIYKGK VVRIMDFGAF VEIAPGKDGL VHISKLDKQR
     VEKVEDVVSI GDEIVVKVTE IDRQGRINLS RKDALADIEA KKNN
//
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