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Database: UniProt
Entry: A0A1F7IH88_9BACT
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ID   A0A1F7IH88_9BACT        Unreviewed;       698 AA.
AC   A0A1F7IH88;
DT   15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT   15-FEB-2017, sequence version 1.
DT   16-JAN-2019, entry version 10.
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=A3A74_00815 {ECO:0000313|EMBL:OGK42739.1};
OS   Candidatus Roizmanbacteria bacterium RIFCSPLOWO2_01_FULL_35_13.
OC   Bacteria; Candidatus Roizmanbacteria.
OX   NCBI_TaxID=1802055 {ECO:0000313|EMBL:OGK42739.1};
RN   [1] {ECO:0000313|EMBL:OGK42739.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=27774985; DOI=10.1038/ncomms13219;
RA   Anantharaman K., Brown C.T., Hug L.A., Sharon I., Castelle C.J.,
RA   Probst A.J., Thomas B.C., Singh A., Wilkins M.J., Karaoz U.,
RA   Brodie E.L., Williams K.H., Hubbard S.S., Banfield J.F.;
RT   "Thousands of microbial genomes shed light on interconnected
RT   biogeochemical processes in an aquifer system.";
RL   Nat. Commun. 7:13219-13219(2016).
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   -!- 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};
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_01595}.
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:OGK42739.1}.
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DR   EMBL; MGAF01000004; OGK42739.1; -; Genomic_DNA.
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; 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; 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   Coiled coil {ECO:0000256|SAM:Coils};
KW   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_01595};
KW   Magnesium {ECO:0000256|HAMAP-Rule:MF_01595};
KW   Metal-binding {ECO:0000256|HAMAP-Rule:MF_01595};
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:OGK42739.1}.
FT   DOMAIN      629    697       S1 motif. {ECO:0000259|PROSITE:PS50126}.
FT   COILED      212    232       {ECO:0000256|SAM:Coils}.
FT   METAL       493    493       Magnesium. {ECO:0000256|HAMAP-Rule:
FT                                MF_01595}.
FT   METAL       499    499       Magnesium. {ECO:0000256|HAMAP-Rule:
FT                                MF_01595}.
SQ   SEQUENCE   698 AA;  76652 MW;  814D21F3D4677B76 CRC64;
     MTKKIIDKST EIDGQKLTLQ FGKFAQAVDT SVFATIGDTA VLITIAVGPE NPNIDYFPLS
     VEYAEKLYAG GIIKGSRWVK REGRPSDDAV LKGRIIDRSI RPLFPKTYKK QVQVVVTLLS
     IDGVNDAEIL SAIAVSAGLS VSSIPWAGPI STVRVGYITS SENKESAFIL YPTENEQEFS
     DLDLVISSTK DKVLMIETKA NRISEEIIQE GIEKAKEENK KIIEFIEKIA KEIGKKKDDI
     PAEVKNSEIL KLVKTKYAKS IEESIKQAAA TAGSEDKMIQ EIVMKIYEDL DKKYDIKQIM
     GVITKNNYAN IKENILKKKI RPDGRKFNQV RELNVEVSLL PRTHGSALFQ RGQTQILSIA
     TLGSTTLEQL IEGPEGKEVK RYIHHYSDGP YSYGQTGRMM GPSRRAIGHG ALAEKAIEPV
     LPSTDDFPYA IRVVSEILSE NGSSSMGSVS GSSLSLMDAG VPLKEAVAGV AMGLVSKSDN
     EYAVLTDIVG LEDFAGEMDF KIAGTKDGIT AIQLDVKNQG LTSKMIADIF KQGKEARLEI
     LEAMNKVISK PRKEVSRYAP KVVVLTPPPD KIGEIIGPGG KNIRALIART QTEINVEDDG
     RVTVSGLDRE KVDEAVKHIG NITREIEVGE EFEGEVKRIL PFGAFVEMVP GKEGLVHVSK
     MGKGFVRNPE EVVKLGQKVK VKVYQIDNQG RVNLQMIS
//
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