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Database: UniProt
Entry: A0A1Y4SZW2_9FIRM
LinkDB: A0A1Y4SZW2_9FIRM
Original site: A0A1Y4SZW2_9FIRM 
ID   A0A1Y4SZW2_9FIRM        Unreviewed;       712 AA.
AC   A0A1Y4SZW2;
DT   30-AUG-2017, integrated into UniProtKB/TrEMBL.
DT   30-AUG-2017, sequence version 1.
DT   13-FEB-2019, entry version 11.
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=B5E75_03940 {ECO:0000313|EMBL:OUQ35414.1};
OS   Massiliomicrobiota timonensis.
OC   Bacteria; Firmicutes; Erysipelotrichia; Erysipelotrichales;
OC   Erysipelotrichaceae; Massiliomicrobiota.
OX   NCBI_TaxID=1776392 {ECO:0000313|EMBL:OUQ35414.1, ECO:0000313|Proteomes:UP000195305};
RN   [1] {ECO:0000313|EMBL:OUQ35414.1, ECO:0000313|Proteomes:UP000195305}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=An13 {ECO:0000313|EMBL:OUQ35414.1,
RC   ECO:0000313|Proteomes:UP000195305};
RA   Medvecky M., Cejkova D., Polansky O., Karasova D., Kubasova T.,
RA   Cizek A., Rychlik I.;
RT   "Function of individual gut microbiota members based on whole genome
RT   sequencing of pure cultures obtained from chicken caecum.";
RL   Submitted (APR-2017) to the EMBL/GenBank/DDBJ databases.
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:OUQ35414.1}.
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DR   EMBL; NFLJ01000008; OUQ35414.1; -; Genomic_DNA.
DR   BioCyc; GCF_002160865:B5E75_RS03945-MONOMER; -.
DR   Proteomes; UP000195305; 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; 3.30.230.70; -; 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:UP000195305};
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   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, ECO:0000313|EMBL:OUQ35414.1}.
FT   DOMAIN      627    694       S1 motif. {ECO:0000259|PROSITE:PS50126}.
FT   COILED      287    307       {ECO:0000256|SAM:Coils}.
FT   METAL       490    490       Magnesium. {ECO:0000256|HAMAP-Rule:
FT                                MF_01595}.
FT   METAL       496    496       Magnesium. {ECO:0000256|HAMAP-Rule:
FT                                MF_01595}.
SQ   SEQUENCE   712 AA;  78544 MW;  5245A2E702DEA8D6 CRC64;
     MSKHVMSLDF YGKKITVETG ELAKQANGSV LVRYDDTVIL STAVAGKEPK DVDFFPLTVT
     YEEKLYSVGK IPGGFLKREG RPSEHGTLTA RMIDRPIRPL FADGFRNEVQ VVNTVLSVDQ
     NASPEMAAML GASLALCLSD IPFNGPIAGV NVGLIDGEFT INAGPEEMER SLINLEVAGT
     KEAINMVEAD AKEVDEETML NALMFGHEAI KQLIAFEEEI VTLYGKEKIE IPLFELDQNI
     VDEVTALAKE RMISAVSIPG KLERYAAIDT INEEVVALFE AREYADLKEQ ESVLKQVKIV
     LHDLEKDEVR RLITEDKVRP DGRRIDEVRP LDAQVDLLPR VHGSALFTRG ETQVLSVCTL
     GALGEHQKID GLGLEDQKRF MHHYNFPPYS VGETGRMGAP GRREIGHGAL GERALAQVIP
     NEEEFPYTIR VVSEVLESNG SSSQASICAS SMALMAAGVP ISNPVSGVAM GLVKKGDDYT
     ILTDIQGMED HLGDMDFKVA GTKNGICALQ MDIKIDGITK EILQEALAQA KAGRQQIMDC
     MMSAINEPRD HLSPYAPKVY MMKIEPDQIK DVIGTGGKTI NEIIEKSNDV KIDIEQDGRV
     TIYHYDQEAI ETAAKLIENI VRKAQVGEIY DGKVVRVEDK YAFVELFEGT NGFLHVGDIA
     HERIHKASDV LKLGDIIKVK VTKITDKGVN VSRKALLPKP IHKEEKKDKE HD
//
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