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Database: UniProt
Entry: A0A0F6A9S2_9GAMM
LinkDB: A0A0F6A9S2_9GAMM
Original site: A0A0F6A9S2_9GAMM 
ID   A0A0F6A9S2_9GAMM        Unreviewed;       709 AA.
AC   A0A0F6A9S2;
DT   24-JUN-2015, integrated into UniProtKB/TrEMBL.
DT   24-JUN-2015, sequence version 1.
DT   16-JAN-2019, entry version 21.
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=N479_01165 {ECO:0000313|EMBL:KKE82947.1};
OS   Pseudoalteromonas luteoviolacea S4054.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales;
OC   Pseudoalteromonadaceae; Pseudoalteromonas.
OX   NCBI_TaxID=1129367 {ECO:0000313|EMBL:KKE82947.1, ECO:0000313|Proteomes:UP000033434};
RN   [1] {ECO:0000313|EMBL:KKE82947.1, ECO:0000313|Proteomes:UP000033434}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=S4054 {ECO:0000313|EMBL:KKE82947.1,
RC   ECO:0000313|Proteomes:UP000033434};
RX   PubMed=25879706; DOI=10.1186/s12864-015-1365-z;
RA   Machado H., Sonnenschein E.C., Melchiorsen J., Gram L.;
RT   "Genome mining reveals unlocked bioactive potential of marine Gram-
RT   negative bacteria.";
RL   BMC Genomics 16:158-158(2015).
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   -!- SUBUNIT: Component of the RNA degradosome, which is a multiprotein
CC       complex involved in RNA processing and mRNA degradation.
CC       {ECO:0000256|HAMAP-Rule:MF_01595}.
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:KKE82947.1}.
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DR   EMBL; AUXW01000154; KKE82947.1; -; Genomic_DNA.
DR   RefSeq; WP_046356589.1; NZ_AUXW01000154.1.
DR   EnsemblBacteria; KKE82947; KKE82947; N479_01165.
DR   GeneID; 31724206; -.
DR   PATRIC; fig|1129367.4.peg.3027; -.
DR   Proteomes; UP000033434; 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:UP000033434};
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}.
FT   DOMAIN      624    692       S1 motif. {ECO:0000259|PROSITE:PS50126}.
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   709 AA;  75909 MW;  E19036C30503096D CRC64;
     MQAIIKEFQL GQHTVTLETG AIARQADGAV LASIGDTSVL VTVVGKREAA PGQDFFPLTV
     NYQEKMYAAG RIPGGFLKRE GRPSDSETLT ARLIDRPIRP LFPDGFVNEV QVIATVVSSD
     PEIQPDMVAL IGTSAALAIS GVPFNGPIGA ARVGYIDGQY VLNPTVTELA ESKLDLVVAG
     TENAVLMVES EAEILTEEEM LGAVVYGHDQ SQAIIKAIEE FKAEAGKPAW DWAAPEKNVA
     LADKVAAIAE EKVGTAYRIT DKVARKESLS EAKAEVIEKL TAELAEGEAL DEQEVGKLFS
     SLEKKIVRGR IIAGEKRIDG REPDMVRALD VMTGVLPRTH GSSIFTRGET QALVTATLGT
     ERDAQMMDDL VGTHKHHFML HYNFPPFCVG ETGFIGSPKR REIGHGNLAK RGVQAVMPSL
     EEFPYSVRVV SEITESNGSS SMASVCGTSL ALMDAGVPVK ASVAGIAMGL VKEGEEFVVL
     SDILGDEDHL GDMDFKVAGS SAGVTALQMD IKIEGITKEI MQIALSQAKA ARMHILSVMD
     QAIAAPSQEL SEFAPRIYTM NIPPKKIADV IGKGGATIRQ LTEETDTTIE IEDDGTVKIA
     ATNGNSAKEA IARIEALTAE LEVGTIYNGK VNRIVDFGAF VNVLPGKDGL VHISQISKER
     VNNVSDHLKV GQEVKVKVLE VDRQGRVRLS IKEALEPSEP AAEQAPKGE
//
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