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Database: UniProt
Entry: V6S9L3_9FLAO
LinkDB: V6S9L3_9FLAO
Original site: V6S9L3_9FLAO 
ID   V6S9L3_9FLAO            Unreviewed;       716 AA.
AC   V6S9L3;
DT   19-FEB-2014, integrated into UniProtKB/TrEMBL.
DT   19-FEB-2014, sequence version 1.
DT   24-JAN-2024, entry version 44.
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=Q767_05905 {ECO:0000313|EMBL:KGO96438.1};
OS   Flavobacterium enshiense DK69.
OC   Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC   Flavobacteriaceae; Flavobacterium.
OX   NCBI_TaxID=1107311 {ECO:0000313|EMBL:KGO96438.1, ECO:0000313|Proteomes:UP000030149};
RN   [1] {ECO:0000313|Proteomes:UP000030149}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DK69 {ECO:0000313|Proteomes:UP000030149};
RA   Zeng Z., Chen C.;
RL   Submitted (SEP-2013) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:KGO96438.1, ECO:0000313|Proteomes:UP000030149}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DK69 {ECO:0000313|EMBL:KGO96438.1,
RC   ECO:0000313|Proteomes:UP000030149};
RX   PubMed=26561515; DOI=10.1186/s40793-015-0084-z;
RA   Zeng Z., Chen C., Du H., Wang G., Li M.;
RT   "High quality draft genomic sequence of Flavobacterium enshiense DK69(T)
RT   and comparison among Flavobacterium genomes.";
RL   Stand. Genomic Sci. 10:92-92(2015).
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:KGO96438.1}.
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DR   EMBL; JRLZ01000004; KGO96438.1; -; Genomic_DNA.
DR   RefSeq; WP_023573490.1; NZ_JRLZ01000004.1.
DR   AlphaFoldDB; V6S9L3; -.
DR   STRING; 1107311.Q767_05905; -.
DR   PATRIC; fig|1107311.3.peg.1459; -.
DR   eggNOG; COG1185; Bacteria.
DR   OrthoDB; 9804305at2; -.
DR   Proteomes; UP000030149; 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:UP000030149};
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          627..698
FT                   /note="S1 motif"
FT                   /evidence="ECO:0000259|PROSITE:PS50126"
FT   REGION          691..716
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         488
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01595"
FT   BINDING         494
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01595"
SQ   SEQUENCE   716 AA;  78200 MW;  FD410629DF83D867 CRC64;
     MIPKVFQEII DLGDGRSISI ETGKLAKQAD GSVVVRMGDA MLLATAVSAR TSNPGVDFLP
     LTVDYREKFA AAGRFPGGFF KREARPSDNE VLTMRLVDRV LRPLFPDDYH AETQVMIQLM
     SHDDNIMPDA LAGLAASAAL AVSDIPFYNL ISEVRVARID GKFVINPSRE ELEQSDIDMM
     IGASMDSVAM VEGEMKEISE AEMVEAIKFA HEAIKVQIQA QERLRAAVGT PAYREYEGEK
     EDEAIYAKVK AAAYDKCYAI AKEASGKSER SEKFAAVKEE VKALFTEEEL AENGDLVSKY
     FSKTNKEAVR NVILELGLRL DGRKTTEIRP IWCETDYLPS VHGSALFTRG ETQALATVTL
     GTSREANIID SPSEQGEEKF YLHYNFPPFS TGEAKPLRGT SRREVGHGNL AQRALVNMIP
     ADCPYTIRIV SEVLESNGSS SMATVCAGTM ALMDAGVQMT KPVSGIAMGL ITDGQKFAVL
     SDILGDEDHL GDMDFKVTGT ADGITACQMD IKIDGLRYDI MEQALDQARE GRLHILGKIT
     ETIAQPRPEV KPKAPKIITR TIPGNFIGAL IGPGGKVIQE LQKATGTTIV INEVDEQGVV
     EILGTSPEGI AAVLAKIDSI IFKPVLGESY EVKVIKMLDF GAVVEYTAAP GNEVLLHVSE
     LAWERTENVA DVVKMGDVFM VKYLGVDPKT RKEKVSKKAL LPRPPREEKK EVSEKG
//
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