(data stored in ACNUC1104 zone)

SWISSPROT: D3VGY4_XENNA

ID   D3VGY4_XENNA            Unreviewed;       247 AA.
AC   D3VGY4;
DT   20-APR-2010, integrated into UniProtKB/TrEMBL.
DT   20-APR-2010, sequence version 1.
DT   08-MAY-2019, entry version 51.
DE   RecName: Full=Ribonuclease PH {ECO:0000256|HAMAP-Rule:MF_00564, ECO:0000256|SAAS:SAAS00104182};
DE            Short=RNase PH {ECO:0000256|HAMAP-Rule:MF_00564};
DE            EC=2.7.7.56 {ECO:0000256|HAMAP-Rule:MF_00564, ECO:0000256|SAAS:SAAS01092908};
DE   AltName: Full=tRNA nucleotidyltransferase {ECO:0000256|HAMAP-Rule:MF_00564};
GN   Name=rph {ECO:0000256|HAMAP-Rule:MF_00564,
GN   ECO:0000313|EMBL:CBJ88269.1};
GN   OrderedLocusNames=XNC1_0181 {ECO:0000313|EMBL:CBJ88269.1};
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:CBJ88269.1, 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:CBJ88269.1, 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: Phosphorolytic 3'-5' exoribonuclease that plays an
CC       important role in tRNA 3'-end maturation. Removes nucleotide
CC       residues following the 3'-CCA terminus of tRNAs; can also add
CC       nucleotides to the ends of RNA molecules by using nucleoside
CC       diphosphates as substrates, but this may not be physiologically
CC       important. Probably plays a role in initiation of 16S rRNA
CC       degradation (leading to ribosome degradation) during starvation.
CC       {ECO:0000256|HAMAP-Rule:MF_00564, ECO:0000256|SAAS:SAAS01092914}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=phosphate + tRNA(n+1) = a ribonucleoside 5'-diphosphate +
CC         tRNA(n); Xref=Rhea:RHEA:10628, Rhea:RHEA-COMP:11132, Rhea:RHEA-
CC         COMP:11133, ChEBI:CHEBI:43474, ChEBI:CHEBI:57930,
CC         ChEBI:CHEBI:83401; EC=2.7.7.56; Evidence={ECO:0000256|HAMAP-
CC         Rule:MF_00564, ECO:0000256|SAAS:SAAS01125748};
CC   -!- SUBUNIT: Homohexameric ring arranged as a trimer of dimers.
CC       {ECO:0000256|HAMAP-Rule:MF_00564, ECO:0000256|SAAS:SAAS01092913}.
CC   -!- SIMILARITY: Belongs to the RNase PH family. {ECO:0000256|HAMAP-
CC       Rule:MF_00564, ECO:0000256|SAAS:SAAS00578435}.
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DR   EMBL; FN667742; CBJ88269.1; -; Genomic_DNA.
DR   RefSeq; WP_010847636.1; NC_014228.1.
DR   STRING; 406817.XNC1_0181; -.
DR   EnsemblBacteria; CBJ88269; CBJ88269; XNC1_0181.
DR   KEGG; xne:XNC1_0181; -.
DR   eggNOG; ENOG4105ED0; Bacteria.
DR   eggNOG; COG0689; LUCA.
DR   HOGENOM; HOG000229516; -.
DR   KO; K00989; -.
DR   OMA; KGKGQGW; -.
DR   Proteomes; UP000008075; Chromosome.
DR   GO; GO:0000175; F:3'-5'-exoribonuclease activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0000049; F:tRNA binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0009022; F:tRNA nucleotidyltransferase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0016075; P:rRNA catabolic process; IEA:UniProtKB-UniRule.
DR   GO; GO:0006364; P:rRNA processing; IEA:UniProtKB-KW.
DR   GO; GO:0008033; P:tRNA processing; IEA:UniProtKB-UniRule.
DR   CDD; cd11362; RNase_PH_bact; 1.
DR   Gene3D; 3.30.230.70; -; 1.
DR   HAMAP; MF_00564; RNase_PH; 1.
DR   InterPro; IPR001247; ExoRNase_PH_dom1.
DR   InterPro; IPR015847; ExoRNase_PH_dom2.
DR   InterPro; IPR036345; ExoRNase_PH_dom2_sf.
DR   InterPro; IPR027408; PNPase/RNase_PH_dom_sf.
DR   InterPro; IPR020568; Ribosomal_S5_D2-typ_fold.
DR   InterPro; IPR002381; RNase_PH_bac-type.
DR   InterPro; IPR018336; RNase_PH_CS.
DR   Pfam; PF01138; RNase_PH; 1.
DR   Pfam; PF03725; RNase_PH_C; 1.
DR   SUPFAM; SSF54211; SSF54211; 1.
DR   SUPFAM; SSF55666; SSF55666; 1.
DR   TIGRFAMs; TIGR01966; RNasePH; 1.
DR   PROSITE; PS01277; RIBONUCLEASE_PH; 1.
PE   3: Inferred from homology;
DR   PRODOM; D3VGY4.
DR   SWISS-2DPAGE; D3VGY4.
KW   Complete proteome {ECO:0000313|Proteomes:UP000008075};
KW   Nucleotidyltransferase {ECO:0000256|HAMAP-Rule:MF_00564,
KW   ECO:0000256|SAAS:SAAS01092912, ECO:0000313|EMBL:CBJ88269.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000008075};
KW   RNA-binding {ECO:0000256|SAAS:SAAS01092910};
KW   rRNA processing {ECO:0000256|HAMAP-Rule:MF_00564,
KW   ECO:0000256|SAAS:SAAS01092909};
KW   Transferase {ECO:0000256|HAMAP-Rule:MF_00564,
KW   ECO:0000256|SAAS:SAAS01092911, ECO:0000313|EMBL:CBJ88269.1};
KW   tRNA processing {ECO:0000256|HAMAP-Rule:MF_00564,
KW   ECO:0000256|SAAS:SAAS00469605};
KW   tRNA-binding {ECO:0000256|HAMAP-Rule:MF_00564,
KW   ECO:0000256|SAAS:SAAS01092906}.
FT   DOMAIN       15    145       RNase_PH. {ECO:0000259|Pfam:PF01138}.
FT   DOMAIN      163    229       RNase_PH_C. {ECO:0000259|Pfam:PF03725}.
FT   REGION      129    131       Phosphate (substrate) binding.
FT                                {ECO:0000256|HAMAP-Rule:MF_00564}.
FT   BINDING      91     91       Phosphate (substrate) binding.
FT                                {ECO:0000256|HAMAP-Rule:MF_00564}.
SQ   SEQUENCE   247 AA;  26465 MW;  AE96F0D042D2E68C CRC64;
     MSLVGKRPAG RTAGQVRPIK MTRHYTKHAE GSVLVEFGDT KVLCNASVEE GIPRFLKGQG
     QGWITAEYGM LPRATNSRNA REAARGKQTG RTMEIQRLIA RSLRAAVDLK KLGEFTITLD
     CDVIQADGGT RTAAISGACV ALVDALNKLV ADGKLKESPL KSMVAAVSVG IVGGEGLCDL
     EYVEDSAAET DMNVVMIDDG RMIEVQGTAE GEPFSHDELL SLLSLAKEGL ETIFEAQRDA
     LKQDSSK
//

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