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ID D3VIN3_XENNA Unreviewed; 712 AA.
AC D3VIN3;
DT 20-APR-2010, integrated into UniProtKB/TrEMBL.
DT 20-APR-2010, sequence version 1.
DT 16-JAN-2019, entry version 57.
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 ECO:0000313|EMBL:CBJ88583.1};
GN OrderedLocusNames=XNC1_0509 {ECO:0000313|EMBL:CBJ88583.1};
OS Xenorhabdus nematophila (strain ATCC 19061 / DSM 3370 / LMG 1036 /
OS NCIB 9965 / AN6).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Morganellaceae; Xenorhabdus.
OX NCBI_TaxID=406817 {ECO:0000313|EMBL:CBJ88583.1, ECO:0000313|Proteomes:UP000008075};
RN [1] {ECO:0000313|Proteomes:UP000008075}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 19061 / DSM 3370 / LMG 1036 / NCIB 9965 / AN6
RC {ECO:0000313|Proteomes:UP000008075};
RA Goodrich-Blair H., Barbazuk B., Bode H.B., Darby C., Du Z., Forst S.,
RA Gaudriault S., Goldman B.S., Goodner B., Henkhaus J., Latreille P.,
RA Medigue C., Miller N., Norton S., Ogier J.C., Rouy Z., Slater S.,
RA Suen G.;
RT "Complete genome sequence of Xenorhabdus nematophila (strain ATCC
RT 19061 / DSM 3370 / LMG 1036 / NCIB 9965 / AN6).";
RL Submitted (FEB-2010) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:CBJ88583.1, ECO:0000313|Proteomes:UP000008075}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 19061 / DSM 3370 / LMG 1036 / NCIB 9965 / AN6
RC {ECO:0000313|Proteomes:UP000008075};
RX PubMed=22125637; DOI=10.1371/journal.pone.0027909;
RA Chaston J.M., Suen G., Tucker S.L., Andersen A.W., Bhasin A., Bode E.,
RA Bode H.B., Brachmann A.O., Cowles C.E., Cowles K.N., Darby C.,
RA de Leon L., Drace K., Du Z., Givaudan A., Herbert Tran E.E.,
RA Jewell K.A., Knack J.J., Krasomil-Osterfeld K.C., Kukor R., Lanois A.,
RA Latreille P., Leimgruber N.K., Lipke C.M., Liu R., Lu X.,
RA Martens E.C., Marri P.R., Medigue C., Menard M.L., Miller N.M.,
RA Morales-Soto N., Norton S., Ogier J.C., Orchard S.S., Park D.,
RA Park Y., Qurollo B.A., Sugar D.R., Richards G.R., Rouy Z.,
RA Slominski B., Slominski K., Snyder H., Tjaden B.C., van der Hoeven R.,
RA Welch R.D., Wheeler C., Xiang B., Barbazuk B., Gaudriault S.,
RA Goodner B., Slater S.C., Forst S., Goldman B.S., Goodrich-Blair H.;
RT "The entomopathogenic bacterial endosymbionts xenorhabdus and
RT photorhabdus: convergent lifestyles from divergent genomes.";
RL PLoS ONE 6:e27909-e27909(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 -!- 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}.
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DR EMBL; FN667742; CBJ88583.1; -; Genomic_DNA.
DR RefSeq; WP_013183301.1; NC_014228.1.
DR STRING; 406817.XNC1_0509; -.
DR EnsemblBacteria; CBJ88583; CBJ88583; XNC1_0509.
DR KEGG; xne:XNC1_0509; -.
DR eggNOG; ENOG4105C62; Bacteria.
DR eggNOG; COG1185; LUCA.
DR HOGENOM; HOG000218326; -.
DR KO; K00962; -.
DR OMA; RYMHNYN; -.
DR Proteomes; UP000008075; 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;
DR PRODOM; D3VIN3.
DR SWISS-2DPAGE; D3VIN3.
KW Complete proteome {ECO:0000313|Proteomes:UP000008075};
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, ECO:0000313|EMBL:CBJ88583.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000008075};
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:CBJ88583.1}.
FT DOMAIN 626 694 S1 motif. {ECO:0000259|PROSITE:PS50126}.
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; 77286 MW; 18ADA638B37871A3 CRC64;
MLNPIVRKFQ YGQHTVTIET GMMARQATAA VMVNMDDTAV FVTVVGQKKM KPGQDFFPLT
VNYQERTYAA GRIPGSFFRR EGRPGEGETL VARLIDRPLR PLFPEGFLNE VQIIATVVSV
NPQVNPDIVA MIGASAALAL SGIPFNGPIG AARVGYINDQ YVLNPTSDEL KNSRLDLVVA
GTESAVLMVE SEAELLTEDQ MLGAVVFGHE QQQIVIENIN SLAAEAGKEK WDWAPEPINQ
SLHDRVAELA ESRLGDAYRI TEKQERYAQV NIIKEEVSVV ILAESAEKGV ELEEGEVLDA
LSGLEKNVVR GRVLSGEPRI DGREKDMVRA LDVRTGVLPR THGSSLFTRG ETQALVAATL
GTERDAQVID ELMGERTDRF LFHYNFPPYS VGETGMVGSP KRREIGHGRL AKRGVLAVMP
NASEFPYTVR VVSEITESNG SSSMASVCGA SLALMDAGVP IKAAVAGIAM GLVKEGDNFV
VLSDILGDED HLGDMDFKVA GSRDGISALQ MDIKIEGITR EIMQIALNQA KGARLHILSV
MEQAIESPRN DISEFAPRIH TIKINPDKIK DVIGKGGSVI RALTEETGTT IEIEDDGTVK
IAATDGDKAR HAISRIEEIT AEVEVGRIYT GKVTRIVDFG AFVAIGGGKE GLVHISQIAD
KRVEKVTDYL QVGQEVPVKV LEIDRQGRIR LSMKEAVATT DEAPQSPESS VE
//
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