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Database: UniProt
Entry: D1B9J9_THEAS
LinkDB: D1B9J9_THEAS
Original site: D1B9J9_THEAS 
ID   D1B9J9_THEAS            Unreviewed;       752 AA.
AC   D1B9J9;
DT   19-JAN-2010, integrated into UniProtKB/TrEMBL.
DT   19-JAN-2010, sequence version 1.
DT   24-JAN-2024, entry version 86.
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   OrderedLocusNames=Taci_0719 {ECO:0000313|EMBL:ACZ18952.1};
OS   Thermanaerovibrio acidaminovorans (strain ATCC 49978 / DSM 6589 / Su883)
OS   (Selenomonas acidaminovorans).
OC   Bacteria; Synergistota; Synergistia; Synergistales; Synergistaceae;
OC   Thermanaerovibrio.
OX   NCBI_TaxID=525903 {ECO:0000313|EMBL:ACZ18952.1, ECO:0000313|Proteomes:UP000002030};
RN   [1] {ECO:0000313|EMBL:ACZ18952.1, ECO:0000313|Proteomes:UP000002030}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 49978 / DSM 6589 / Su883
RC   {ECO:0000313|Proteomes:UP000002030};
RX   PubMed=21304665; DOI=10.4056/sigs.40645;
RA   Chovatia M., Sikorski J., Schroder M., Lapidus A., Nolan M., Tice H.,
RA   Glavina Del Rio T., Copeland A., Cheng J.F., Lucas S., Chen F., Bruce D.,
RA   Goodwin L., Pitluck S., Ivanova N., Mavromatis K., Ovchinnikova G.,
RA   Pati A., Chen A., Palaniappan K., Land M., Hauser L., Chang Y.J.,
RA   Jeffries C.D., Chain P., Saunders E., Detter J.C., Brettin T., Rohde M.,
RA   Goker M., Spring S., Bristow J., Markowitz V., Hugenholtz P.,
RA   Kyrpides N.C., Klenk H.P., Eisen J.A.;
RT   "Complete genome sequence of Thermanaerovibrio acidaminovorans type strain
RT   (Su883).";
RL   Stand. Genomic Sci. 1:254-261(2009).
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; CP001818; ACZ18952.1; -; Genomic_DNA.
DR   RefSeq; WP_012869467.1; NC_013522.1.
DR   RefSeq; YP_003317234.1; NC_013522.1.
DR   AlphaFoldDB; D1B9J9; -.
DR   STRING; 525903.Taci_0719; -.
DR   EnsemblBacteria; ACZ18952; ACZ18952; Taci_0719.
DR   KEGG; tai:Taci_0719; -.
DR   PATRIC; fig|525903.6.peg.720; -.
DR   eggNOG; COG1185; Bacteria.
DR   HOGENOM; CLU_004217_2_2_0; -.
DR   OMA; DEMSPNA; -.
DR   OrthoDB; 9804305at2; -.
DR   Proteomes; UP000002030; 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; 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:UP000002030};
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          717..752
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        729..745
FT                   /note="Basic and acidic residues"
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   752 AA;  82300 MW;  25A3827B21CCA74B CRC64;
     MHKVVQLELG GRVLSFETGR MAKQANGAVY ASYGETAVLV TSVMSEKPRE GLDFFPLLVD
     YEERFYSAGK IPGGFIKREG RPSETAILSG RMVDRSIRSL FPEHMRNDVH VVATVLSVDQ
     HNPPNVLAIN AASAALAISD IPWDGPIGAV RIGCIDGQLL VNPTEPQMAE STLDLLVAGH
     DGGITMVEAG ANEVSEDLLV DAMELAHQEI RRIVAFIRDL QAQVGLKKVE IAPPARIDEI
     DAWIEAELKE EIYKAVQIHH KVERKDALSA ITKRAVERFE ESHPGCAGYV ASVVEEWVKK
     GLRRLLLDEG RRADGRAMDQ LRPITCEVGV LPKVHGSALF TRGETQALAV TTLGMMGEDD
     QILDGLKIDE PAKRFLLHYN FPPYSVGEVR PMRGPGRREI GHGALAERAL RPMLPSEDQF
     PYVVRVVSDI LESNGSSSMA SVCGGSLSMM DAGVPIKKAV AGVAMGLVTD GSRVCILTDI
     QGLEDHYGDM DFKVAGTRDG VTALQMDNKA GGITREILKR ALDQARDGRM RILDIMDGAI
     RSPRDQISPN APRIMTITID PDKIRDVIGP GGKTIRSIIA QTGAKVDVQD DGRVCVAAQT
     EEAASQAIKI ISDLTREVQA GEIFVGRITR MLGFGYFVEV LPGKEGLLHV SEISSHHIPK
     IEDAFSIGDE VLVVVREIDD MNRINLSRRR LIDRYDQLAK DPALAAQVEV ERAREIRYGT
     LKPEGGSPKG PQGRRDSDRR PSGGDRRDKH HR
//
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