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Database: UniProt
Entry: A0A1U7LFH4_9BACT
LinkDB: A0A1U7LFH4_9BACT
Original site: A0A1U7LFH4_9BACT 
ID   A0A1U7LFH4_9BACT        Unreviewed;       737 AA.
AC   A0A1U7LFH4;
DT   10-MAY-2017, integrated into UniProtKB/TrEMBL.
DT   10-MAY-2017, sequence version 1.
DT   05-JUN-2019, entry version 11.
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=BHV81_01110 {ECO:0000313|EMBL:OKZ21157.1};
OS   Butyricimonas synergistica.
OC   Bacteria; Bacteroidetes; Bacteroidia; Bacteroidales; Odoribacteraceae;
OC   Butyricimonas.
OX   NCBI_TaxID=544644 {ECO:0000313|EMBL:OKZ21157.1};
RN   [1] {ECO:0000313|EMBL:OKZ21157.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=43_13 {ECO:0000313|EMBL:OKZ21157.1};
RX   PubMed=27819664; DOI=10.1038/nbt.3704;
RA   Brown C.T., Olm M.R., Thomas B.C., Banfield J.F.;
RT   "Measurement of bacterial replication rates in microbial
RT   communities.";
RL   Nat. Biotechnol. 34:1256-1263(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};
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   -!- 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:OKZ21157.1}.
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DR   EMBL; MNQW01000007; OKZ21157.1; -; 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; IPR015848; PNPase_PH_RNA-bd_bac/org-type.
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; 2.
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; PS50126; S1; 1.
PE   3: Inferred from homology;
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   RNA-binding {ECO:0000256|HAMAP-Rule:MF_01595};
KW   Transferase {ECO:0000256|HAMAP-Rule:MF_01595,
KW   ECO:0000313|EMBL:OKZ21157.1}.
FT   DOMAIN      614    683       S1 motif. {ECO:0000259|PROSITE:PS50126}.
FT   REGION      684    737       Disordered. {ECO:0000256|MobiDB-lite:
FT                                A0A1U7LFH4}.
FT   METAL       475    475       Magnesium. {ECO:0000256|HAMAP-Rule:
FT                                MF_01595}.
FT   METAL       481    481       Magnesium. {ECO:0000256|HAMAP-Rule:
FT                                MF_01595}.
SQ   SEQUENCE   737 AA;  81983 MW;  AA0FFC4F0456EE40 CRC64;
     MNIIEKSITL KDGRVITLET GKLAKQADGA VMLKMGNTML LATVCSAQEA GPDVDFMPLS
     VDYKEKFSAV GRFPGGFTRR EGRASDYERP LFPDDYHAET FVQVTLYSAD EESMPDCLAG
     LAASAAIAVS DIPFHGPISE VRVARVNGEL MINPTKSELA TADLDIMVAA TYENIMMVEG
     EMNEVSEKEM LDAIKFAHEA IKDHCLVQME LAKAVNKEKR AYCHEVNDEE LRKDIWAKCY
     DKAYAVARQC NADKHLREKL FTEVKEEYLE SLPEEEREAK KNMVSRYYHD VEKEAVRRMI
     LDEGLRLDGR TTEQIRPIWC EAGPLPGPHG SSIFTRGETQ SLSTVTLGTK LDEKIIDEAT
     EQGKEKFLLH YNFPPFSTGE AKASRGVGRR EVGHGNLAHR ALKRMLPDNY PYTVRVVSDI
     LESNGSSSMA TVCAGTLALM DAGIPIKKPV TGIAMGLITD NEKYAVLSDI LGDEDHLGDM
     DFKVTGTVDG ITATQMDIKV DGLPYEILEK ALDQARRGRL HIMNIIKETL PEPRPDLKPH
     APRMVTLTVD KDQIGAIIGP GGKIIQDIQE KSGAVIVIEE VGNQGIVDIA ATNAESIEIA
     VARIKAIACK PEVGEIYEGV VKTITAFGAF VEFLPGKDGL LHVSEIDHKR VEKVEDVLKE
     GDRVRVKLID IDPKTGKFKL SRKVLLPKPE GMEQNDRQNR SERQDRGERQ DRGPRQDRGD
     RPHRDRGPRP ERKENQE
//
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