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Database: UniProt
Entry: A0A0T2QH85_9SPHN
LinkDB: A0A0T2QH85_9SPHN
Original site: A0A0T2QH85_9SPHN 
ID   A0A0T2QH85_9SPHN        Unreviewed;       772 AA.
AC   A0A0T2QH85;
DT   17-FEB-2016, integrated into UniProtKB/TrEMBL.
DT   17-FEB-2016, sequence version 1.
DT   24-JAN-2024, entry version 34.
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=ASD76_09045 {ECO:0000313|EMBL:KRA84123.1};
OS   Altererythrobacter sp. Root672.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC   Erythrobacteraceae; Altererythrobacter.
OX   NCBI_TaxID=1736584 {ECO:0000313|EMBL:KRA84123.1, ECO:0000313|Proteomes:UP000051125};
RN   [1] {ECO:0000313|EMBL:KRA84123.1, ECO:0000313|Proteomes:UP000051125}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Root672 {ECO:0000313|EMBL:KRA84123.1,
RC   ECO:0000313|Proteomes:UP000051125};
RA   Gilbert D.G.;
RL   Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:KRA84123.1, ECO:0000313|Proteomes:UP000051125}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Root672 {ECO:0000313|EMBL:KRA84123.1,
RC   ECO:0000313|Proteomes:UP000051125};
RA   Schulze-Lefert P.;
RT   "Functional overlap of the Arabidopsis leaf and root microbiotas.";
RL   Submitted (NOV-2015) 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:KRA84123.1}.
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DR   EMBL; LMHH01000001; KRA84123.1; -; Genomic_DNA.
DR   RefSeq; WP_055921449.1; NZ_LMHH01000001.1.
DR   AlphaFoldDB; A0A0T2QH85; -.
DR   STRING; 1736584.ASD76_09045; -.
DR   OrthoDB; 9804305at2; -.
DR   Proteomes; UP000051125; 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   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|ARBA:ARBA00022842, 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:UP000051125};
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          620..688
FT                   /note="S1 motif"
FT                   /evidence="ECO:0000259|PROSITE:PS50126"
FT   REGION          691..772
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         484
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01595"
FT   BINDING         490
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01595"
SQ   SEQUENCE   772 AA;  83417 MW;  27A61DB1C5686B2E CRC64;
     MFDTKTVSLE WGGKTLTLET GRIARQADGA VLATYGETVV LCAVTAAKSV KEGQDFFPLT
     VHYQEKFSAA GRIPGGFFKR ERGATEKETL TSRLIDRPIR PLFPEGFYNE INVIAQVLSY
     DGETEADIVA MIAASAALTI SGVPFMGPIG GARVGFKDGE YQLNPSMAEV AEGRLDLVVA
     ATQDAVMMVE SEAKELTEEE MLGAVMFAHE ESRKVIGAII KLAEQAAKDP WDLEVSDNSA
     MKAEIKKLVG TDIAAAYKLT DKSARSNALN EARAKVKAAY AEADGQTSMT ANKLTKKVEA
     DIVRTAILKD GSRIDGRKLD QVRPIEATVG FLPRTHGSAL FTRGETQAIC TTTLGTKDSE
     QMIDGLNGLS YESFMLHYNF PPYSVGEVGR FGAPGRREVG HGKLAWRALR PMLPSKEDFP
     YTIRILSDIT ESNGSSSMAT VCGGCLAMMD AGVPIARPVS GIAMGLILEG KDFAVLSDIL
     GDEDHLGDMD FKVAGTEAGI TSLQMDIKIA GITKEIMAQA LEQAKAGRAH ILGEMTKALG
     SARTELSAHA PRIETMQIDK SKIRDVIGTG GKVIREIVAE TGAKVDIDDE GVIKISSSDL
     SQIEAARKWI AGIVEEAEVG KVYDGKVVNI VDFGAFVNFM GGKDGLVHVS EMKNERVEKP
     TDVVTEGQAV KVKVLEIDQR GKVRLSMRVV DQETGEELED TRPPREPREP RGDRGDRGDR
     GGDRRPRRDG GGGGRGGDRD RGPRRDRDDR GPRSDRNEGG DPNHLPAFLK DD
//
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