GenomeNet

Database: UniProt
Entry: E3DRZ4_HALPG
LinkDB: E3DRZ4_HALPG
Original site: E3DRZ4_HALPG 
ID   E3DRZ4_HALPG            Unreviewed;       696 AA.
AC   E3DRZ4;
DT   11-JAN-2011, integrated into UniProtKB/TrEMBL.
DT   11-JAN-2011, sequence version 1.
DT   27-MAR-2024, entry version 74.
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   OrderedLocusNames=Hprae_0964 {ECO:0000313|EMBL:ADO77118.1};
OS   Halanaerobium praevalens (strain ATCC 33744 / DSM 2228 / GSL).
OC   Bacteria; Bacillota; Clostridia; Halanaerobiales; Halanaerobiaceae;
OC   Halanaerobium.
OX   NCBI_TaxID=572479 {ECO:0000313|EMBL:ADO77118.1, ECO:0000313|Proteomes:UP000006866};
RN   [1] {ECO:0000313|Proteomes:UP000006866}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 33744 / DSM 2228 / GSL
RC   {ECO:0000313|Proteomes:UP000006866};
RG   US DOE Joint Genome Institute (JGI-PGF);
RA   Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA   Bruce D., Goodwin L., Pitluck S., Kyrpides N., Mavromatis K., Ivanova N.,
RA   Ovchinnikova G., Chertkov O., Detter J.C., Han C., Larimer F., Land M.,
RA   Hauser L., Markowitz V., Cheng J.-F., Hugenholtz P., Woyke T., Wu D.,
RA   Tindall B., Pomrenke H.G., Brambilla E., Klenk H.-P., Eisen J.A.;
RT   "The complete genome of Halanaerobium praevalens DSM 2228.";
RL   Submitted (OCT-2010) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:ADO77118.1, ECO:0000313|Proteomes:UP000006866}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 33744 / DSM 2228 / GSL
RC   {ECO:0000313|Proteomes:UP000006866};
RX   PubMed=21886858;
RA   Ivanova N., Sikorski J., Chertkov O., Nolan M., Lucas S., Hammon N.,
RA   Deshpande S., Cheng J.F., Tapia R., Han C., Goodwin L., Pitluck S.,
RA   Huntemann M., Liolios K., Pagani I., Mavromatis K., Ovchinikova G.,
RA   Pati A., Chen A., Palaniappan K., Land M., Hauser L., Brambilla E.M.,
RA   Kannan K.P., Rohde M., Tindall B.J., Goker M., Detter J.C., Woyke T.,
RA   Bristow J., Eisen J.A., Markowitz V., Hugenholtz P., Kyrpides N.C.,
RA   Klenk H.P., Lapidus A.;
RT   "Complete genome sequence of the extremely halophilic Halanaerobium
RT   praevalens type strain (GSL).";
RL   Stand. Genomic Sci. 4:312-321(2011).
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; CP002175; ADO77118.1; -; Genomic_DNA.
DR   RefSeq; WP_014553151.1; NC_017455.1.
DR   AlphaFoldDB; E3DRZ4; -.
DR   STRING; 572479.Hprae_0964; -.
DR   KEGG; hpk:Hprae_0964; -.
DR   PATRIC; fig|572479.3.peg.974; -.
DR   eggNOG; COG1185; Bacteria.
DR   HOGENOM; CLU_004217_2_2_9; -.
DR   OrthoDB; 9804305at2; -.
DR   Proteomes; UP000006866; 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; IPR015848; PNPase_PH_RNA-bd_bac/org-type.
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; 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; 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|ARBA:ARBA00022490, ECO:0000256|HAMAP-Rule:MF_01595};
KW   Magnesium {ECO:0000256|HAMAP-Rule:MF_01595};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723, ECO:0000256|HAMAP-
KW   Rule:MF_01595};
KW   Nucleotidyltransferase {ECO:0000256|ARBA:ARBA00022695, ECO:0000256|HAMAP-
KW   Rule:MF_01595}; Reference proteome {ECO:0000313|Proteomes:UP000006866};
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          618..686
FT                   /note="S1 motif"
FT                   /evidence="ECO:0000259|PROSITE:PS50126"
FT   BINDING         482
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01595"
FT   BINDING         488
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01595"
SQ   SEQUENCE   696 AA;  76483 MW;  192217BDD4498A59 CRC64;
     MKEWTIDYAG DQFNFQTGKL AKQANGSVVV RCGDSQVLVT AVMDEPRPGM NYFPLMVNYE
     ERVYAIGQIP GSVMRREGRP RDEATLAARV IDRSIRPLFP EGFRHDVQIV ATILSVDDDH
     DPEVLALNGA SAALTLSDIP FAGPIGGVKV ALVDEQIIIN PNEEERENSD LDLVVAGSKD
     AIMMVEASAN EVSEATVLEA MKVAHAEIKK IISLQEEMRQ EAGEDKFHFE SPTVDSEIQS
     KVDEILGNKL KEAIQIQEKQ ARSDKIDELK AELKATINPD EESELDSQIG MAFEKMLKKS
     VKSLVVEDGI RPDGRDYDEI RPIWAEVDFV PRAHGSGVFT RGETQALSVL TLGSARDEQT
     LFGLGENETK RYMHHYNFPS FCVGETSPMR SPGRREIGHG TLGEKALLPV IPSEEEFPYT
     IRIVSEVLES NGSSSQASIC GSSLALMAAG VPIKAPVAGI AMGLMKKDDD VVILSDIQGF
     EDFNGDMDFK VAGTEAGITA LQMDIKLKGL SYDILEEALE KAKKGRMHIM GKMLDVIPEA
     RPELSENAPA IITMNIDPEK IRFVIGPGGK MINKIIDETG ASIDIEDDGL VKIMTDDQEG
     GQQAQEMIAR LTEEVEVGKI YQGKVKRIMN FGAFVEILPN KEGLVHISKL ADRHVKEVGD
     IVSVGDEIPV KVIEIDNQDR INLSLKDAKK ELEAKE
//
DBGET integrated database retrieval system