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Database: UniProt
Entry: W7C3T1_9LIST
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ID   W7C3T1_9LIST            Unreviewed;       733 AA.
AC   W7C3T1;
DT   16-APR-2014, integrated into UniProtKB/TrEMBL.
DT   16-APR-2014, sequence version 1.
DT   03-JUL-2019, entry version 32.
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=MFLO_08097 {ECO:0000313|EMBL:EUJ31757.1};
OS   Listeria floridensis FSL S10-1187.
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Listeriaceae; Listeria.
OX   NCBI_TaxID=1265817 {ECO:0000313|EMBL:EUJ31757.1, ECO:0000313|Proteomes:UP000019249};
RN   [1] {ECO:0000313|EMBL:EUJ31757.1, ECO:0000313|Proteomes:UP000019249}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=FSL S10-1187 {ECO:0000313|EMBL:EUJ31757.1,
RC   ECO:0000313|Proteomes:UP000019249};
RX   PubMed=24599893; DOI=10.1099/ijs.0.052720-0;
RA   den Bakker H.C., Warchocki S., Wright E.M., Allred A.F., Ahlstrom C.,
RA   Manuel C.S., Stasiewicz M.J., Burrell A., Roof S., Strawn L.,
RA   Fortes E.D., Nightingale K.K., Kephart D., Wiedmann M.;
RT   "Listeria floridensis sp. nov., Listeria aquatica sp. nov., Listeria
RT   cornellensis sp. nov., Listeria riparia sp. nov. and Listeria
RT   grandensis sp. nov., from agricultural and natural environments.";
RL   Int. J. Syst. Evol. Microbiol. 64:1882-1889(2014).
CC   -!- FUNCTION: Involved in mRNA degradation. Catalyzes the
CC       phosphorolysis of single-stranded polyribonucleotides processively
CC       in the 3'- to 5'-direction. {ECO:0000256|HAMAP-Rule:MF_01595,
CC       ECO:0000256|SAAS:SAAS00979022}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=phosphate + RNA(n+1) = a ribonucleoside 5'-diphosphate +
CC         RNA(n); Xref=Rhea:RHEA:22096, Rhea:RHEA-COMP:11128, Rhea:RHEA-
CC         COMP:11129, ChEBI:CHEBI:43474, ChEBI:CHEBI:57930,
CC         ChEBI:CHEBI:83400; EC=2.7.7.8; Evidence={ECO:0000256|HAMAP-
CC         Rule:MF_01595, ECO:0000256|SAAS:SAAS01115795};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000256|HAMAP-
CC         Rule:MF_01595, ECO:0000256|SAAS:SAAS00979019};
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_01595,
CC       ECO:0000256|SAAS:SAAS00979031}.
CC   -!- SIMILARITY: Belongs to the polyribonucleotide
CC       nucleotidyltransferase family. {ECO:0000256|HAMAP-Rule:MF_01595,
CC       ECO:0000256|SAAS:SAAS00979043}.
CC   -!- CAUTION: The sequence shown here is derived from an
CC       EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is
CC       preliminary data. {ECO:0000313|EMBL:EUJ31757.1}.
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DR   EMBL; AODF01000015; EUJ31757.1; -; Genomic_DNA.
DR   RefSeq; WP_036097272.1; NZ_AODF01000015.1.
DR   EnsemblBacteria; EUJ31757; EUJ31757; MFLO_08097.
DR   PATRIC; fig|1265817.5.peg.1611; -.
DR   OrthoDB; 122725at2; -.
DR   Proteomes; UP000019249; 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   Gene3D; 3.30.1370.10; -; 1.
DR   Gene3D; 3.30.230.70; -; 2.
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_S5_D2-typ_fold.
DR   InterPro; IPR022967; S1_dom.
DR   InterPro; IPR003029; S1_domain.
DR   PANTHER; PTHR11252; PTHR11252; 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; SSF46915; SSF46915; 1.
DR   SUPFAM; SSF50249; SSF50249; 1.
DR   SUPFAM; SSF54211; SSF54211; 2.
DR   SUPFAM; SSF54791; SSF54791; 1.
DR   SUPFAM; SSF55666; SSF55666; 2.
DR   TIGRFAMs; TIGR03591; polynuc_phos; 1.
DR   PROSITE; PS50126; S1; 1.
PE   3: Inferred from homology;
KW   Coiled coil {ECO:0000256|SAM:Coils};
KW   Complete proteome {ECO:0000313|Proteomes:UP000019249};
KW   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_01595,
KW   ECO:0000256|SAAS:SAAS00979026};
KW   Magnesium {ECO:0000256|HAMAP-Rule:MF_01595,
KW   ECO:0000256|SAAS:SAAS00979039};
KW   Metal-binding {ECO:0000256|HAMAP-Rule:MF_01595,
KW   ECO:0000256|SAAS:SAAS00979046};
KW   Nucleotidyltransferase {ECO:0000256|HAMAP-Rule:MF_01595,
KW   ECO:0000256|SAAS:SAAS00979037};
KW   Reference proteome {ECO:0000313|Proteomes:UP000019249};
KW   RNA-binding {ECO:0000256|HAMAP-Rule:MF_01595,
KW   ECO:0000256|SAAS:SAAS00979024};
KW   Transferase {ECO:0000256|HAMAP-Rule:MF_01595,
KW   ECO:0000256|SAAS:SAAS00979029}.
FT   DOMAIN      624    692       S1 motif. {ECO:0000259|PROSITE:PS50126}.
FT   REGION      697    733       Disordered. {ECO:0000256|MobiDB-lite:
FT                                W7C3T1}.
FT   COILED      285    305       {ECO:0000256|SAM:Coils}.
FT   METAL       488    488       Magnesium. {ECO:0000256|HAMAP-Rule:
FT                                MF_01595}.
FT   METAL       494    494       Magnesium. {ECO:0000256|HAMAP-Rule:
FT                                MF_01595}.
SQ   SEQUENCE   733 AA;  81022 MW;  B1E0D41E42B48CDC CRC64;
     MSEKQVFTTE LAGKTLAIEV GQLAKQASGA AMVRFGDTAV LTAAVGSKKP RPGDFFPLTV
     NYEEKMYSVG KVPGGFLKRE GRPSDRATLT ARLIDRPIRP LFAEGFRNEV QITSTVFSVE
     QDCSPEMAAM LGSSISLCIS DIPFDGPIAG VEVGRVDGEY IINPTMEQAE KSDISLTVAG
     TYDAINMVEA GAKEVSEEAM LEAIMFGHEE IKRLCKFQEE IVKAVGKEKR EIELFVTDPE
     LEREVKAVSE AKMKQAIQTE EKKAREAAID AVKEEVLESY KVKELENEED VLDEVAQILE
     IIEKDEMRRL ISQEKIRPDG RKVDEIRPLS SEVGLLPRVH GSGLFTRGQT QALSVCTLAP
     LREHQIIDGL GAEEYKRFMH HYNFPQFSVG ETGPRRGPGR REIGHGALGE RALSYVIPDE
     ESFPYTVRLV SEVLESNGSS SQASICGSTL ALMDAGVPIK APVAGIAMGL VKLGEDYTIL
     SDIQGMEDHF GDMDFKVAGT RDGITALQMD IKIDGLSRQI LEEALTQAKA GRLHILEHLM
     TTISAPREHL SAYAPKIMTM HIKEEKIKDV IGPGGKQINQ IIDETGVKID IEQDGTIYIA
     SQDEAMNKKA MAIIEDIVRE VQVGEIYTGK VRRIEKFGAF VELFKGTDGL VHISELAYER
     VGKVEDVLKL GDEVTVKVIE VDNQGRVNLS RKALLEKPEG YEEKKPRDNK DFKGRGNGGN
     DRPRKPRFNK EDK
//
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