ID A0A0G0H194_9BACT Unreviewed; 690 AA.
AC A0A0G0H194;
DT 22-JUL-2015, integrated into UniProtKB/TrEMBL.
DT 22-JUL-2015, sequence version 1.
DT 27-MAR-2024, entry version 31.
DE RecName: Full=polyribonucleotide nucleotidyltransferase {ECO:0000256|ARBA:ARBA00012416};
DE EC=2.7.7.8 {ECO:0000256|ARBA:ARBA00012416};
DE Flags: Fragment;
GN ORFNames=US48_C0028G0005 {ECO:0000313|EMBL:KKQ32300.1};
OS Candidatus Levybacteria bacterium GW2011_GWA2_37_36.
OC Bacteria; Candidatus Levybacteria.
OX NCBI_TaxID=1618457 {ECO:0000313|EMBL:KKQ32300.1, ECO:0000313|Proteomes:UP000034000};
RN [1] {ECO:0000313|EMBL:KKQ32300.1, ECO:0000313|Proteomes:UP000034000}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Brown C.T., Hug L.A., Thomas B.C., Sharon I., Castelle C.J., Singh A.,
RA Wilkins M.J., Williams K.H., Banfield J.F.;
RT "rRNA introns, odd ribosomes, and small enigmatic genomes across a large
RT radiation of phyla.";
RL Nature 0:0-0(2015).
CC -!- SIMILARITY: Belongs to the polyribonucleotide nucleotidyltransferase
CC family. {ECO:0000256|ARBA:ARBA00007404}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KKQ32300.1}.
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DR EMBL; LBTD01000028; KKQ32300.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0G0H194; -.
DR Proteomes; UP000034000; Unassembled WGS sequence.
DR GO; GO:0004654; F:polyribonucleotide nucleotidyltransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-UniRule.
DR GO; GO:0006402; P:mRNA catabolic process; IEA:InterPro.
DR GO; GO:0006396; P:RNA processing; IEA:InterPro.
DR CDD; cd02393; KH-I_PNPase; 1.
DR CDD; cd11364; RNase_PH_PNPase_2; 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; 1.
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};
KW Nucleotidyltransferase {ECO:0000256|ARBA:ARBA00022695};
KW RNA-binding {ECO:0000256|ARBA:ARBA00022884, ECO:0000256|PROSITE-
KW ProRule:PRU00117};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:KKQ32300.1}.
FT DOMAIN 627..690
FT /note="S1 motif"
FT /evidence="ECO:0000259|PROSITE:PS50126"
FT NON_TER 690
FT /evidence="ECO:0000313|EMBL:KKQ32300.1"
SQ SEQUENCE 690 AA; 74921 MW; 3772B3678B0884F0 CRC64;
MTTNNSIITQ EIDLSGRVLT LEVGRYAQQA SGAVVARLGD TVVLATVVAG RENPDIDYLP
LSVEYQEKLY SGGKIKGSRW VKREGRPSDE AILTARLIDR SLRPLFPKSL RREIQVVVTT
LSVDSENDPD TPAIVAVSAA LSLTDLPFAG PVGAVRVGFV PQNGTGNFLT NPTYQDREYS
DLDLIVSGNR DGIVMVEAGV RELSEANTIL AIRHGHAEII KIIDAIAELR QKLGKKPAPV
DLSENQEISA LAKKIFKNFP RELQDLVNTM AAKEADADTA GLVDIISQKE ALEDKNLVAA
ALDKAATMLV RQNILEKVLR PDGRKPDEIR PITCRVSELP RTHGSAMFQR GSTQALTITT
LASPSMEQWI ESPEHEEKKR YIHHYNMPPF SVGETGRMGW PSRREIGHGA LAERALVPVI
PAEKDFPYTI RVVSEIMSSN GSTSMASVCG STLSLMDAGV PIKSPVAGIA MGLIIDGQKQ
VILSDIAGIE DFKGDMDFKV AGTTAGITAL QMDVKVPGLS FDILETALEQ ARVGRLSILE
KMLAVLPKSK LEVSKYAPKI VILQIDVEKI GDVIGPGGKT IKKIIAETEA EIDVEDDGTV
VVSGIDHDKI QRAVDWIKGL TKEIKIGEEY DGTVVRITDF GAFVNLTPGK DGLVHISKLS
TGYLSHPSEV ISEGQNLKVR VENIDDQNRV
//