GenomeNet

Database: UniProt
Entry: E1X0D7_HALMS
LinkDB: E1X0D7_HALMS
Original site: E1X0D7_HALMS 
ID   E1X0D7_HALMS            Unreviewed;       709 AA.
AC   E1X0D7;
DT   30-NOV-2010, integrated into UniProtKB/TrEMBL.
DT   30-NOV-2010, sequence version 1.
DT   24-JAN-2024, entry version 73.
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=pnpA {ECO:0000313|EMBL:CBW26365.1};
GN   Synonyms=pnp {ECO:0000256|HAMAP-Rule:MF_01595};
GN   OrderedLocusNames=BMS_1508 {ECO:0000313|EMBL:CBW26365.1};
OS   Halobacteriovorax marinus (strain ATCC BAA-682 / DSM 15412 / SJ)
OS   (Bacteriovorax marinus).
OC   Bacteria; Bdellovibrionota; Bacteriovoracia; Bacteriovoracales;
OC   Halobacteriovoraceae; Halobacteriovorax.
OX   NCBI_TaxID=862908 {ECO:0000313|EMBL:CBW26365.1, ECO:0000313|Proteomes:UP000008963};
RN   [1] {ECO:0000313|Proteomes:UP000008963}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-682 / DSM 15412 / SJ
RC   {ECO:0000313|Proteomes:UP000008963};
RX   PubMed=22955231; DOI=10.1038/ismej.2012.90;
RA   Crossman L.C., Chen H., Cerdeno-Tarraga A.M., Brooks K., Quail M.A.,
RA   Pineiro S.A., Hobley L., Sockett R.E., Bentley S.D., Parkhill J.,
RA   Williams H.N., Stine O.C.;
RT   "A small predatory core genome in the divergent marine Bacteriovorax
RT   marinus SJ and the terrestrial Bdellovibrio bacteriovorus.";
RL   ISME J. 7:148-160(2013).
CC   -!- FUNCTION: Involved in mRNA degradation. Catalyzes the phosphorolysis of
CC       single-stranded polyribonucleotides processively in the 3'- to 5'-
CC       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:14527, Rhea:RHEA-
CC         COMP:17342, ChEBI:CHEBI:43474, ChEBI:CHEBI:57930, ChEBI:CHEBI:140395;
CC         EC=2.7.7.8; Evidence={ECO:0000256|HAMAP-Rule:MF_01595};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000256|HAMAP-Rule:MF_01595};
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_01595}.
CC   -!- SIMILARITY: Belongs to the polyribonucleotide nucleotidyltransferase
CC       family. {ECO:0000256|ARBA:ARBA00007404, ECO:0000256|HAMAP-
CC       Rule:MF_01595}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; FQ312005; CBW26365.1; -; Genomic_DNA.
DR   RefSeq; WP_014244148.1; NC_016620.1.
DR   AlphaFoldDB; E1X0D7; -.
DR   STRING; 862908.BMS_1508; -.
DR   KEGG; bmx:BMS_1508; -.
DR   PATRIC; fig|862908.3.peg.1437; -.
DR   eggNOG; COG1185; Bacteria.
DR   HOGENOM; CLU_004217_2_2_7; -.
DR   OMA; DEMSPNA; -.
DR   Proteomes; UP000008963; Chromosome.
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   CDD; cd02393; KH-I_PNPase; 1.
DR   CDD; cd11363; RNase_PH_PNPase_1; 1.
DR   CDD; cd11364; RNase_PH_PNPase_2; 1.
DR   CDD; cd04472; S1_PNPase; 1.
DR   Gene3D; 3.30.230.70; GHMP Kinase, N-terminal domain; 2.
DR   Gene3D; 3.30.1370.10; K Homology domain, type 1; 1.
DR   Gene3D; 2.40.50.140; Nucleic acid-binding proteins; 1.
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_Su5_D2-typ_SF.
DR   InterPro; IPR003029; S1_domain.
DR   NCBIfam; TIGR03591; polynuc_phos; 1.
DR   PANTHER; PTHR11252; POLYRIBONUCLEOTIDE NUCLEOTIDYLTRANSFERASE; 1.
DR   PANTHER; PTHR11252:SF0; POLYRIBONUCLEOTIDE NUCLEOTIDYLTRANSFERASE 1, MITOCHONDRIAL; 1.
DR   Pfam; PF00013; KH_1; 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; SSF54791; Eukaryotic type KH-domain (KH-domain type I); 1.
DR   SUPFAM; SSF50249; Nucleic acid-binding proteins; 1.
DR   SUPFAM; SSF46915; Polynucleotide phosphorylase/guanosine pentaphosphate synthase (PNPase/GPSI), domain 3; 1.
DR   SUPFAM; SSF55666; Ribonuclease PH domain 2-like; 2.
DR   SUPFAM; SSF54211; Ribosomal protein S5 domain 2-like; 2.
DR   PROSITE; PS50084; KH_TYPE_1; 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|ARBA:ARBA00022695, ECO:0000256|HAMAP-
KW   Rule:MF_01595}; Reference proteome {ECO:0000313|Proteomes:UP000008963};
KW   RNA-binding {ECO:0000256|ARBA:ARBA00022884, ECO:0000256|HAMAP-
KW   Rule:MF_01595};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW   Rule:MF_01595}.
FT   DOMAIN          630..698
FT                   /note="S1 motif"
FT                   /evidence="ECO:0000259|PROSITE:PS50126"
FT   BINDING         494
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01595"
FT   BINDING         500
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01595"
SQ   SEQUENCE   709 AA;  77060 MW;  7DC1E94CE53232B7 CRC64;
     MLNDKKVYSL NYGGKEVTVE TGRLAKQADG SVLVSCNGTQ VLVTVCSAHE VKDGQDFFPL
     LVEYTEKFYS AGKFVGGFLK REGRPSTSET LNARLIDRPL RPLFPEGYMF DTVVSCNVLS
     YSDEGDAEVL AGLGASAALT ISDIPFNGPI GTCKVGRVDG KLVLNPSHSQ WAESDLEIAV
     AASADAILMV EGEAKVVPEK EVLEAIYFGH DNIKEYVKLM EQMRSEIGRP KREFVSAAAN
     ETMMSKMRSD FASGARNCIS IDDKMDRQRA VKALEKEVKN AMSEAPEAFG LTADDSFGKE
     AYKGVDELLY EMMRGDILNE EKRIAGRGMT EVREIETEAN LLEHVHGSSL FTRGETQVMA
     AVTIGGKHGE KMEDSIRGTE FQKFYLHYNF PPFSVGEARG VRGVGRRELG HGNLAERAVK
     AVMPSEEEFA YTTRVVCEVM ESNGSSSMGS VCSASMALMD AGVPISNPVA GIAMGLITDG
     ERFKVLTDIL GDEDHLGDMD FKVAGTVDGI TAIQMDIKIT GLTREIVEKS IEQAREGRLH
     ILGEMAKTIS TKRAEFKDGV PRIVTVQIPV DKIGALIGPG GKNIKKLQED FDVTVEITEE
     GLVKVLGTDT DILNNCVASI DLQINGPEVG SIYEAVVVTI KEYGAFVDII PGVSGLVHVS
     ELSDERVKDV SEYLSEGDKV SVKVVEVDRM GRLKLSAKAV KPVEKKADK
//
DBGET integrated database retrieval system