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Database: UniProt
Entry: U5P528_9STRE
LinkDB: U5P528_9STRE
Original site: U5P528_9STRE 
ID   U5P528_9STRE            Unreviewed;       738 AA.
AC   U5P528;
DT   22-JAN-2014, integrated into UniProtKB/TrEMBL.
DT   22-JAN-2014, sequence version 1.
DT   05-JUN-2019, entry version 33.
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=N597_07755 {ECO:0000313|EMBL:AGY38854.1};
OS   Streptococcus sp. I-P16.
OC   Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC   Streptococcus.
OX   NCBI_TaxID=1156433 {ECO:0000313|EMBL:AGY38854.1, ECO:0000313|Proteomes:UP000017124};
RN   [1] {ECO:0000313|EMBL:AGY38854.1, ECO:0000313|Proteomes:UP000017124}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=I-P16 {ECO:0000313|Proteomes:UP000017124};
RA   Hyun D.-W.;
RT   "Genome sequence of Streptococcus SP. I-P16 isolated from human ileal
RT   fluid.";
RL   Submitted (SEP-2013) 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; CP006776; AGY38854.1; -; Genomic_DNA.
DR   EnsemblBacteria; AGY38854; AGY38854; N597_07755.
DR   KEGG; sip:N597_07755; -.
DR   PATRIC; fig|1156433.3.peg.1529; -.
DR   KO; K00962; -.
DR   Proteomes; UP000017124; 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   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   Complete proteome {ECO:0000313|Proteomes:UP000017124};
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:UP000017124};
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      625    693       S1 motif. {ECO:0000259|PROSITE:PS50126}.
FT   REGION      691    738       Disordered. {ECO:0000256|MobiDB-lite:
FT                                U5P528}.
FT   COMPBIAS    699    714       Polyampholyte. {ECO:0000256|MobiDB-lite:
FT                                U5P528}.
FT   COMPBIAS    724    738       Polyampholyte. {ECO:0000256|MobiDB-lite:
FT                                U5P528}.
FT   METAL       489    489       Magnesium. {ECO:0000256|HAMAP-Rule:
FT                                MF_01595}.
FT   METAL       495    495       Magnesium. {ECO:0000256|HAMAP-Rule:
FT                                MF_01595}.
SQ   SEQUENCE   738 AA;  80956 MW;  6576C098CE976462 CRC64;
     MTKQVFQTTF AGRELIVETG QVAKQANGSV VVRYGESTVL TAAVMSKKMA TGDFFPLQVN
     YEEKMYAAGK FPGGFMKREG RPSTDATLTA RLIDRPIRPM FAEGFRNEVQ VINTVLSYDE
     NASAPMAAMF GSSLALSISD IPFDGPIAGV QVGYVDGEII INPTQEQAER SLLELTVAGT
     KHAINMVESG AKELSEEIML EALLKGHEAV KELIAFQEEI VAAVGKEKAG VELLHVDADL
     QAEIIAAYNS DLQKAVQVEE KLAREAATQA IKDQVTAVYE EKYADHEEFD RIMRDVAEIL
     EQMEHAEVRR LITEDKVRPD GRKVDEIRPL DAQVDYLPRV HGSGLFTRGQ TQALSVLTLA
     PMGETQIIDG LDPEYKKRFM HHYNFPQYSV GETGRYGAPG RREIGHGALG ERALAQVLPS
     LEEFPYAIRL VAEVLESNGS SSQASICAGT LALMAGGVPI KAPVAGIAMG LISDGNNYTV
     LTDIQGLEDH FGDMDFKVAG TRDGITALQM DIKIQGITAE ILTEALAQAK KARFEILDVI
     EATIPEVRPE LAPTAPKIDT IKIDVDKIKI VIGKGGETID KIIAETGVKI DIDEEGNVSI
     YSSDQDAINR AKEIIAGLVR EAKVDEVYHA KVVRIEKFGA FVNLFDKTDA LVHISEMAWT
     RTNLVEDLVA IGDEVDVKII KIDEKGRIDA SMKALLPRPP KPEHSEERGE KGHRHGDRPR
     HHKPRKDFAK DVGEETKE
//
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