(data stored in ACNUC7421 zone)

SWISSPROT: A4ATJ5_MARSH

ID   A4ATJ5_MARSH            Unreviewed;       737 AA.
AC   A4ATJ5;
DT   03-APR-2007, integrated into UniProtKB/TrEMBL.
DT   03-APR-2007, sequence version 1.
DT   08-MAY-2019, entry version 78.
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   OrderedLocusNames=FB2170_16811 {ECO:0000313|EMBL:EAR00765.1};
OS   Maribacter sp. (strain HTCC2170 / KCCM 42371).
OC   Bacteria; Bacteroidetes; Flavobacteriia; Flavobacteriales;
OC   Flavobacteriaceae; Maribacter.
OX   NCBI_TaxID=313603 {ECO:0000313|EMBL:EAR00765.1, ECO:0000313|Proteomes:UP000001602};
RN   [1] {ECO:0000313|EMBL:EAR00765.1, ECO:0000313|Proteomes:UP000001602}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=HTCC2170 / KCCM 42371 {ECO:0000313|Proteomes:UP000001602};
RX   PubMed=21037013; DOI=10.1128/JB.01207-10;
RA   Oh H.M., Kang I., Yang S.J., Jang Y., Vergin K.L., Giovannoni S.J.,
RA   Cho J.C.;
RT   "Complete genome sequence of strain HTCC2170, a novel member of the
RT   genus Maribacter in the family Flavobacteriaceae.";
RL   J. Bacteriol. 193:303-304(2011).
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; CP002157; EAR00765.1; -; Genomic_DNA.
DR   RefSeq; WP_013304568.1; NC_014472.1.
DR   STRING; 313603.FB2170_16811; -.
DR   EnsemblBacteria; EAR00765; EAR00765; FB2170_16811.
DR   KEGG; fbc:FB2170_16811; -.
DR   eggNOG; ENOG4105C62; Bacteria.
DR   eggNOG; COG1185; LUCA.
DR   HOGENOM; HOG000218326; -.
DR   KO; K00962; -.
DR   OMA; RYMHNYN; -.
DR   OrthoDB; 122725at2; -.
DR   BioCyc; MSP313603:G1GNS-139-MONOMER; -.
DR   Proteomes; UP000001602; 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; 3.30.230.70; -; 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;
DR   PRODOM; A4ATJ5.
DR   SWISS-2DPAGE; A4ATJ5.
KW   Complete proteome {ECO:0000313|Proteomes:UP000001602};
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:UP000001602};
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:EAR00765.1}.
FT   DOMAIN      628    699       S1 motif. {ECO:0000259|PROSITE:PS50126}.
FT   METAL       487    487       Magnesium. {ECO:0000256|HAMAP-Rule:
FT                                MF_01595}.
FT   METAL       493    493       Magnesium. {ECO:0000256|HAMAP-Rule:
FT                                MF_01595}.
SQ   SEQUENCE   737 AA;  81676 MW;  3856AB18AAE27FA5 CRC64;
     MIPQVFKEVI DLGDGREISI ETGKLAKQAH GSVVVQSGKC MLLCTVVSNY KQADVDFLPL
     TVDYREKFAA AGRYPGGFFK REARPSDGEV LTMRLVDRVL RPLFPKDYHA ETQVMIQLMS
     HDENVMPEAM AGLAASAAIQ LSDFPFECAI SEARVGRVNG EFVINPTRAQ LEESDIEMMI
     GASADSVMMV EGEMDEISEE EMADAIKFAH EAIKVQIAAQ LRLAEAFGKK EVREYETAEV
     NEDLQKRIHD LAYDKCYAIA KQGTSKVERS NAFAEVKEEV KASFTEEEME EFGHLVGGYY
     GKAEKEAVRE LTLSEGLRLD GRKTDEIRPI WCEVDYLPST HGSSIFTRGE TQALATVTLG
     TSRDANKIDM PSHEGEENFY LHYNFPPFCT GEARPLRGTS RREVGHGNLA QRALKGMVPE
     DCPYTVRVVS EVLESNGSSS MATVCAGTMA MMDAGVQMTR PVSGIAMGLI SDGDRYAVLS
     DILGDEDHLG DMDFKVTGTS EGITACQMDI KIKGLSYEIL VNALKQAREG RLHILGKITD
     TIATPAQNVK EHAPTMVTRR IPNEFIGALI GPGGKVIQEM QKETETTIVI NEDPVTEEGI
     VEILGVGSEG IAAVEAKIDS LMFKPEVGSV YEVKVIKMLD FGAVVEYMEA PGNEVLLHVS
     ELAWERTENV SDVVNMGDVF DVKYFGLDKR TRKDKVSRKA LLPKPEGYVE RPPRNNDRRG
     RDDRRGRDNR DRKPRRD
//

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