ID A0A172TR00_9BACT Unreviewed; 772 AA.
AC A0A172TR00;
DT 07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT 07-SEP-2016, sequence version 1.
DT 24-JAN-2024, entry version 37.
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=SY85_01840 {ECO:0000313|EMBL:ANE49428.1};
OS Flavisolibacter tropicus.
OC Bacteria; Bacteroidota; Chitinophagia; Chitinophagales; Chitinophagaceae;
OC Flavisolibacter.
OX NCBI_TaxID=1492898 {ECO:0000313|EMBL:ANE49428.1, ECO:0000313|Proteomes:UP000077177};
RN [1] {ECO:0000313|Proteomes:UP000077177}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LCS9 {ECO:0000313|Proteomes:UP000077177};
RA Kim M.K., Srinivasan S., Lee J.-J.;
RT "Flavisolibacter sp./LCS9/ whole genome sequencing.";
RL Submitted (JAN-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:ANE49428.1, ECO:0000313|Proteomes:UP000077177}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LCS9 {ECO:0000313|EMBL:ANE49428.1,
RC ECO:0000313|Proteomes:UP000077177};
RX PubMed=27259556; DOI=10.1099/ijsem.0.001207;
RA Lee J.J., Kang M.S., Kim G.S., Lee C.S., Lim S., Lee J., Roh S.H., Kang H.,
RA Ha J.M., Bae S., Jung H.Y., Kim M.K.;
RT "Flavisolibacter tropicus sp. nov., isolated from tropical soil.";
RL Int. J. Syst. Evol. Microbiol. 66:3413-3419(2016).
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; CP011390; ANE49428.1; -; Genomic_DNA.
DR RefSeq; WP_066401518.1; NZ_CP011390.1.
DR AlphaFoldDB; A0A172TR00; -.
DR STRING; 1492898.SY85_01840; -.
DR KEGG; fla:SY85_01840; -.
DR PATRIC; fig|1492898.3.peg.403; -.
DR OrthoDB; 9804305at2; -.
DR Proteomes; UP000077177; 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; 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:UP000077177};
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 636..705
FT /note="S1 motif"
FT /evidence="ECO:0000259|PROSITE:PS50126"
FT REGION 705..772
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 705..751
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 756..772
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 497
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01595"
FT BINDING 503
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01595"
SQ SEQUENCE 772 AA; 85929 MW; 6F55A8C0969EA65C CRC64;
MLTQKFSKTF DIGDGREVTI ETGRLARQAD GAVTVRMGNN ILLATVVATE EPKPGQDFFP
LSVDYMEKFA SAGRIPGSFF KREGRLSDYE ILISRLIDRA LRPLFPEDYF CEVQVIVTLI
SSDSEIMPDA LACLAASAAL AVSNIPIQEI ISEVRVSRID GQFKINPTRS EMEKSDMDFI
IAATEKNIMM VEGEAKECSE EDLVKALEVA HDAIRVQIRA QQELRDMVGA GAKRDYPKPV
VNEVLRQRVE EFAKARMEEL SRANLPKAER KETYKKISDD LKEVLAREAN LPEGEEIDDD
TKKLVKNYLG DLQYYVVRDM ILNDKVRLDG RNLEQVRPLD MEVDVLPTPH GAALFTRGET
QSLTTITLGT PLDELLVESA AKSEYSKFIL HYNFPPFSTG EVKFLRGPGR REVGHGNLAQ
RSLKQMMPGA DYAYTVRIVS DILESNGSSS MATVCAGSLA LMDAGVPLPK HVAGVAMGLI
SKGDQFAVLT DILGDEDHLG DMDFKVTGTR DGICGIQMDI KVDGLSMDVM RQALEQARRG
RMHILDAMYN CIPEHRADVK PHAPRMVKMF IDREFIGAVI GPGGKVIQEM QRETGTTINI
EEKNNQGEVS IFGTDKEKVD RAHNWIKGIV AVPVVGDEYE AVVKSIMPYG AFVEFLPGKQ
GLLHISEVSW KRLETLEGVL NENDKVKVKL TGTDPKTGKF KLSRKVLLPK PEGMKEESGD
RGERRDGGQR REGGQRFEGR GDRRESGYGG QRREPRQGGE NQQSQSSQEN EQ
//