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Database: UniProt
Entry: A0A1M4V3P9_9CLOT
LinkDB: A0A1M4V3P9_9CLOT
Original site: A0A1M4V3P9_9CLOT 
ID   A0A1M4V3P9_9CLOT        Unreviewed;       702 AA.
AC   A0A1M4V3P9;
DT   15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT   15-MAR-2017, sequence version 1.
DT   13-FEB-2019, entry version 12.
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=SAMN05443638_106127 {ECO:0000313|EMBL:SHE63549.1};
OS   Clostridium fallax.
OC   Bacteria; Firmicutes; Clostridia; Clostridiales; Clostridiaceae;
OC   Clostridium.
OX   NCBI_TaxID=1533 {ECO:0000313|EMBL:SHE63549.1, ECO:0000313|Proteomes:UP000184035};
RN   [1] {ECO:0000313|EMBL:SHE63549.1, ECO:0000313|Proteomes:UP000184035}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 2631 {ECO:0000313|EMBL:SHE63549.1,
RC   ECO:0000313|Proteomes:UP000184035};
RA   Jaros S., Januszkiewicz K., Wedrychowicz H.;
RL   Submitted (NOV-2016) 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}.
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DR   EMBL; FQVM01000006; SHE63549.1; -; Genomic_DNA.
DR   RefSeq; WP_072894139.1; NZ_UAVV01000002.1.
DR   BioCyc; GCF_900129365:BUA70_RS05015-MONOMER; -.
DR   Proteomes; UP000184035; 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; 1.
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   Complete proteome {ECO:0000313|Proteomes:UP000184035};
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:UP000184035};
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:SHE63549.1}.
FT   DOMAIN      621    689       S1 motif. {ECO:0000259|PROSITE:PS50126}.
FT   METAL       485    485       Magnesium. {ECO:0000256|HAMAP-Rule:
FT                                MF_01595}.
FT   METAL       491    491       Magnesium. {ECO:0000256|HAMAP-Rule:
FT                                MF_01595}.
SQ   SEQUENCE   702 AA;  77336 MW;  A1A7E3BE9D3D5696 CRC64;
     MNKSHSVNIA GREMKVELGN IGMLSNAAIF MSYGDTVILT NTNASESPRD GIDFFPLSVE
     YEERLYAVGK IPGGFIKREG KPSEKAILNG RAIDRPLRPL FPKGYRNDVQ VVCTVVSVEK
     DNLPEILAIN AASTALCLSS IPFTTPVAAV QVGIVNGEFV INPTSKEREE STLALTVCAT
     KDRVMMIEAG GDEIEEEKMI EAIEFGFEAC KKIVAFQEEV MAKFGKEKVE PVLYKVDEEI
     EKEVREFSFD MIKDAMYITD RDERNAAMDI VKEKISEEFS EKYPDNQSDV NDVVYRTQKE
     IVRNMLLKDH RRPDGRAFDE VRPISCEVGI LPRTHGTGLF TRGLTQVMTV ATLGAIGDVQ
     ILDGIGEEES KRYMHHYNFP AYSVGEVKPL RGPGRREIGH GALAERALEP LIPSEEEFPY
     TIRLVSEVLS SNGSTSQASV CGSTLALLDA GVPIKRPAAG IAMGLITSED LSEEEVLTDI
     QGIEDFFGDM DFKVAGTEKG ITSIQVDTKI AGLSDNCIRN AIHGARKARL FILEKIKECI
     PAPREEVSLY APKTSTLQID PEKIRDVIGA GGKVINKIIA DTGVKIDIKD DGKIFVSSPD
     HEGVNEAIKI IEGLTKEVKV GEIYLGKVIK IAQFGAFVEI LPNKEGLVHI SKLDVNRVNK
     VEDIVSVGDE ILVKVTDIDN QGRINLSRKD AIIDKEEKKT EE
//
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