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Database: UniProt/TrEMBL
Entry: C9XRQ8_CLODC
LinkDB: C9XRQ8_CLODC
Original site: C9XRQ8_CLODC 
ID   C9XRQ8_CLODC            Unreviewed;       449 AA.
AC   C9XRQ8;
DT   24-NOV-2009, integrated into UniProtKB/TrEMBL.
DT   24-NOV-2009, sequence version 1.
DT   19-FEB-2014, entry version 31.
DE   SubName: Full=Ribonuclease Ph;
GN   Name=rph; OrderedLocusNames=CD196_3123;
OS   Clostridium difficile (strain CD196).
OC   Bacteria; Firmicutes; Clostridia; Clostridiales;
OC   Peptostreptococcaceae.
OX   NCBI_TaxID=645462;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CD196;
RX   PubMed=19781061; DOI=10.1186/gb-2009-10-9-r102;
RA   Stabler R.A., He M., Dawson L., Martin M., Valiente E., Corton C.,
RA   Lawley T.D., Sebaihia M., Quail M.A., Rose G., Gerding D.N.,
RA   Gibert M., Popoff M.R., Parkhill J., Dougan G., Wren B.W.;
RT   "Comparative genome and phenotypic analysis of Clostridium difficile
RT   027 strains provides insight into the evolution of a hypervirulent
RT   bacterium.";
RL   Genome Biol. 10:R102.1-R102.15(2009).
CC   -!- FUNCTION: Phosphorolytic exoribonuclease that removes nucleotide
CC       residues following the -CCA terminus of tRNA and adds nucleotides
CC       to the ends of RNA molecules by using nucleoside diphosphates as
CC       substrates (By similarity).
CC   -!- CATALYTIC ACTIVITY: A nucleoside triphosphate + H(2)O = a
CC       nucleotide + diphosphate.
CC   -!- CATALYTIC ACTIVITY: tRNA(n+1) + phosphate = tRNA(n) + a nucleoside
CC       diphosphate.
CC   -!- COFACTOR: Binds 1 divalent metal cation ion per subunit; can use
CC       either magnesium or manganese (By similarity).
CC   -!- SUBUNIT: Homodimer (By similarity).
CC   -!- SIMILARITY: Belongs to the HAM1 NTPase family.
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DR   EMBL; FN538970; CBA66330.1; -; Genomic_DNA.
DR   RefSeq; YP_003216137.1; NC_013315.1.
DR   STRING; 645462.CD196_3123; -.
DR   EnsemblBacteria; CBA66330; CBA66330; CD196_3123.
DR   GeneID; 8465516; -.
DR   KEGG; cdc:CD196_3123; -.
DR   PATRIC; 19452738; VBICloDif125228_3278.
DR   eggNOG; COG0689; -.
DR   HOGENOM; HOG000122621; -.
DR   OMA; HCTLVFA; -.
DR   OrthoDB; EOG6CZQQP; -.
DR   BioCyc; CDIF645462:GJED-3212-MONOMER; -.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0017111; F:nucleoside-triphosphatase activity; IEA:InterPro.
DR   GO; GO:0000166; F:nucleotide binding; IEA:UniProtKB-KW.
DR   GO; GO:0016779; F:nucleotidyltransferase activity; IEA:UniProtKB-KW.
DR   GO; GO:0000049; F:tRNA binding; IEA:InterPro.
DR   GO; GO:0004549; F:tRNA-specific ribonuclease activity; IEA:InterPro.
DR   GO; GO:0009143; P:nucleoside triphosphate catabolic process; IEA:InterPro.
DR   GO; GO:0009117; P:nucleotide metabolic process; IEA:UniProtKB-KW.
DR   GO; GO:0090501; P:RNA phosphodiester bond hydrolysis; IEA:GOC.
DR   GO; GO:0008033; P:tRNA processing; IEA:UniProtKB-KW.
DR   Gene3D; 3.30.230.70; -; 1.
DR   HAMAP; MF_00564; RNase_PH; 1.
DR   HAMAP; MF_01405; Non_canon_purine_NTPase; 1.
DR   InterPro; IPR001247; ExoRNase_PH_dom1.
DR   InterPro; IPR015847; ExoRNase_PH_dom2.
DR   InterPro; IPR002637; Ham1p-like.
DR   InterPro; IPR020922; NTPase.
DR   InterPro; IPR027408; PNPase/RNase_PH_dom.
DR   InterPro; IPR020568; Ribosomal_S5_D2-typ_fold.
DR   InterPro; IPR002381; RNase_PH_bac-type.
DR   InterPro; IPR018336; RNase_PH_CS.
DR   PANTHER; PTHR11067; PTHR11067; 1.
DR   Pfam; PF01725; Ham1p_like; 1.
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   TIGRFAMs; TIGR00042; TIGR00042; 1.
DR   PROSITE; PS01277; RIBONUCLEASE_PH; 1.
PE   3: Inferred from homology;
KW   Complete proteome; Hydrolase; Magnesium; Manganese; Metal-binding;
KW   Nucleotide metabolism; Nucleotide-binding; Nucleotidyltransferase;
KW   Transferase; tRNA processing.
SQ   SEQUENCE   449 AA;  50066 MW;  0F0A68EC1DCB9408 CRC64;
     MTRSYDRSNE QIRPVKITRD YTKYAEGSVL IEMGETKVIC TASVEEKVPP FLRNSGTGWI
     NAEYSMLPRA TQQRKIRDAS RGKIDGRTQE IQRLIGRAIR SVVDLNKLGE RTIWVDCDVI
     QADGGTRTAS ITGAFVAVAE AIYKLYKAKT IKEMPITNFV SAISVGIVNG IHMLDLCYEE
     DSKAQVDMNI IMTDKCEFVE VQGTGEEKPF SRADLNLLLE LGEKGNKELI RLQREALGEI
     ADEILGMDYG NEVVIATNNA HKLEEIGEIL KDFEYKVYSL KDVDLAGIEI VEDGKTFEHN
     ALIKARAIAK KTKLIAISDD SGLEVDALGK KPGVYSARYA GEHATDEENR KKLLKAMQNV
     PMSKRNARFV SAIAVVFPDG KEFVVRGICE GMIGFEEKGK NGFGYDSLFI VKGYDKTFGE
     IPSVIKNSIS HRANALKLMK QEFIKRVVK
//
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