ID E4RKT0_HALHG Unreviewed; 696 AA.
AC E4RKT0;
DT 08-FEB-2011, integrated into UniProtKB/TrEMBL.
DT 08-FEB-2011, sequence version 1.
DT 27-MAR-2024, entry version 71.
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=Halsa_1323 {ECO:0000313|EMBL:ADQ14750.1};
OS Halanaerobium hydrogeniformans (Halanaerobium sp. (strain sapolanicus)).
OC Bacteria; Bacillota; Clostridia; Halanaerobiales; Halanaerobiaceae;
OC Halanaerobium.
OX NCBI_TaxID=656519 {ECO:0000313|EMBL:ADQ14750.1, ECO:0000313|Proteomes:UP000007434};
RN [1] {ECO:0000313|EMBL:ADQ14750.1, ECO:0000313|Proteomes:UP000007434}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=sapolanicus {ECO:0000313|Proteomes:UP000007434};
RG US DOE Joint Genome Institute;
RA Lucas S., Copeland A., Lapidus A., Cheng J.-F., Bruce D., Goodwin L.,
RA Pitluck S., Davenport K., Detter J.C., Han C., Tapia R., Land M.,
RA Hauser L., Jeffries C., Kyrpides N., Ivanova N., Mikhailova N.,
RA Begemann M.B., Mormile M.R., Wall J.D., Elias D.A., Woyke T.;
RT "Complete sequence of Halanaerobium sp. sapolanicus.";
RL Submitted (NOV-2010) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:ADQ14750.1, ECO:0000313|Proteomes:UP000007434}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=sapolanicus {ECO:0000313|Proteomes:UP000007434};
RX PubMed=21602336; DOI=10.1128/JB.05209-11;
RA Brown S.D., Begemann M.B., Mormile M.R., Wall J.D., Han C.S., Goodwin L.A.,
RA Pitluck S., Land M.L., Hauser L.J., Elias D.A.;
RT "Complete Genome Sequence of the Haloalkaliphilic, Hydrogen Producing
RT Halanaerobium hydrogenoformans.";
RL J. Bacteriol. 193:3682-3683(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}.
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DR EMBL; CP002304; ADQ14750.1; -; Genomic_DNA.
DR RefSeq; WP_013405831.1; NC_014654.1.
DR AlphaFoldDB; E4RKT0; -.
DR STRING; 656519.Halsa_1323; -.
DR KEGG; has:Halsa_1323; -.
DR eggNOG; COG1185; Bacteria.
DR HOGENOM; CLU_004217_2_2_9; -.
DR OrthoDB; 9804305at2; -.
DR Proteomes; UP000007434; 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:UP000007434};
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; 76709 MW; 16C4599B956D8A80 CRC64;
MKEWTLEYAG SDFHIETGKL AKQANGSVMV RSGDSQVLVT ATMDEPRPGM NYFPLMVNYE
ERVYAIGKIP GGVLRREGRP RDEATLAARV IDRSIRPLFP DGYRKDVQVV ATILSVDDDH
DPEMLALNGA SIALTISDIP FDGPIGGVKV GLVDGEIIIN PNEEERENSE LDLVVAGSKD
AIMMVEASAN EVEEAVILEA MDLAHQEIQK MIKIQKTIRE EAGKEKEVFI EPTVDDELAE
KVEELLGDRL KEAIQIQKKQ ARGEKIASLK AELKENLNPD EDEDIDSQLN LAFENMIKKS
VKSLIIDDGI RPDGREHDEI RPIWAEVGVV PRSHGSGVFT RGETQALSVL TLGASSDEQI
LFGLGEKETK RYMHHYNFPS FCVGETSPMR SPGRREIGHG TLGEKALLPV IPEKDDFPYT
IRIVSEVLES NGSSSQASIC GSTLSLMDAG VPIKAPVSGI AMGLMKKDDE IVVLSDIQGF
EDFHGDMDFK VAGTENGVTA LQMDMKLKGL SKDVLEEALN KAKKGRMHIM EKMLEVIAEP
RPELSKNAPA LISMKINPEK IRFVIGPGGK TINEIIDKTG AQIDIDDDGT VMILTDDQES
GKEAKKMVEN LTKEVEVGEI YQGTVKRIMN FGAFVEILPN KEGLVHISKI ADRHIKEVSD
VLSVGDEIPV KVIEIDNQDR INLSLKAAKK ELEDKE
//
