ID A0A073INW0_9BACT Unreviewed; 798 AA.
AC A0A073INW0;
DT 01-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 01-OCT-2014, sequence version 1.
DT 24-JAN-2024, entry version 38.
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=EH55_09555 {ECO:0000313|EMBL:KEJ91444.1};
OS Synergistes jonesii.
OC Bacteria; Synergistota; Synergistia; Synergistales; Synergistaceae;
OC Synergistes.
OX NCBI_TaxID=2754 {ECO:0000313|EMBL:KEJ91444.1, ECO:0000313|Proteomes:UP000027665};
RN [1] {ECO:0000313|EMBL:KEJ91444.1, ECO:0000313|Proteomes:UP000027665}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=78-1 {ECO:0000313|EMBL:KEJ91444.1,
RC ECO:0000313|Proteomes:UP000027665};
RA Coil D.A., Eisen J.A., Holland-Moritz H.E.;
RT "Draft Genome Sequence of Synergistes jonesii.";
RL Submitted (APR-2014) to the EMBL/GenBank/DDBJ databases.
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 -!- 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:KEJ91444.1}.
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DR EMBL; JMKI01000047; KEJ91444.1; -; Genomic_DNA.
DR RefSeq; WP_037977824.1; NZ_JQEL01000049.1.
DR AlphaFoldDB; A0A073INW0; -.
DR STRING; 2754.EH55_09555; -.
DR PATRIC; fig|2754.20.peg.886; -.
DR eggNOG; COG1185; Bacteria.
DR OrthoDB; 9804305at2; -.
DR Proteomes; UP000027665; Unassembled WGS sequence.
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 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; 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; 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|HAMAP-Rule:MF_01595};
KW Nucleotidyltransferase {ECO:0000256|ARBA:ARBA00022695, ECO:0000256|HAMAP-
KW Rule:MF_01595}; Reference proteome {ECO:0000313|Proteomes:UP000027665};
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 621..689
FT /note="S1 motif"
FT /evidence="ECO:0000259|PROSITE:PS50126"
FT REGION 710..798
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 485
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01595"
FT BINDING 491
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01595"
SQ SEQUENCE 798 AA; 88365 MW; 80DC6AFB1514CC68 CRC64;
MKKIYELDFY GKKMSFEVGR LAKQANAAVL ARHGDTALLV TSVLAEKARE GMDFFPLLVD
YEERYYSAGK VPGGYIKREG RPSESAILSG RMIDRSIRSL FPEWMRNDVH VVATVMSVDQ
KNPANILGIN GASFALAISD IPWDGPIGAV RIGCLDGKLV VNPDESDLPR STLDLVVAGH
KGGITMVEAG AKEVSEELLV DAMELASEAV RKIVEFIEGA VTEIGKEKVQ LPVPEVIKEI
DDWMRENLTD EIYEAVQINQ KQPRGAAIAA AQQRAEERFA EEYPDSPKYI AGVMDEMVKK
AVRRLLVVDR KRADGRAMDE LRPISCEIDI LPMTHGSALF TRGETQSLGV TTLGMIGLDD
QMMDGLKIDE PAKRFILHYN FPPYSVGEVR PMRGPGRREI GHGALAERAL RALFPEEEEF
PYVVRQVSDI LESNGSSSMA SVCSGSLSMM AAGVPIKKAV AGIAMGLIAD GGEMCILTDI
QGLEDHYGDM DFKVAGTRDG VTALQMDNKA GGINRDILTR ALAQAKKGRF QILDIMDRTI
AAPRPELSPN APKIITFNID PEKIRDVIGS GGKTIRGIVQ QTGAKIDVED SGKVSVAAVN
EESARLAEKI IRDLVRDVEA GETFVGTVTR MLSFGAFVEV LPGKEGLLHV SEVSNYRVPT
IEDAFGIGEK VLVTVKEIDD MHRVNLSRKR LLGQLDELAL NPEFAAQIPA ERAREERYSH
FPKGGERREG GHDRDRDRGD RDRGDRGDRG ERGERGERNF DRDRERDRSR GFERQRGGDF
EEEKPHRPAR RFERERKN
//
