(data stored in ACNUC7421 zone)

SWISSPROT: CCA_PSEAB

ID   CCA_PSEAB               Reviewed;         410 AA.
AC   Q02TH9;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   14-NOV-2006, sequence version 1.
DT   07-JUN-2017, entry version 65.
DE   RecName: Full=Multifunctional CCA protein {ECO:0000255|HAMAP-Rule:MF_01261};
DE   Includes:
DE     RecName: Full=CCA-adding enzyme {ECO:0000255|HAMAP-Rule:MF_01261};
DE              EC=2.7.7.72 {ECO:0000255|HAMAP-Rule:MF_01261};
DE     AltName: Full=CCA tRNA nucleotidyltransferase {ECO:0000255|HAMAP-Rule:MF_01261};
DE     AltName: Full=tRNA CCA-pyrophosphorylase {ECO:0000255|HAMAP-Rule:MF_01261};
DE     AltName: Full=tRNA adenylyl-/cytidylyl-transferase {ECO:0000255|HAMAP-Rule:MF_01261};
DE     AltName: Full=tRNA nucleotidyltransferase {ECO:0000255|HAMAP-Rule:MF_01261};
DE     AltName: Full=tRNA-NT {ECO:0000255|HAMAP-Rule:MF_01261};
DE   Includes:
DE     RecName: Full=2'-nucleotidase {ECO:0000255|HAMAP-Rule:MF_01261};
DE              EC=3.1.3.- {ECO:0000255|HAMAP-Rule:MF_01261};
DE   Includes:
DE     RecName: Full=2',3'-cyclic phosphodiesterase {ECO:0000255|HAMAP-Rule:MF_01261};
DE              EC=3.1.4.- {ECO:0000255|HAMAP-Rule:MF_01261};
DE   Includes:
DE     RecName: Full=Phosphatase {ECO:0000255|HAMAP-Rule:MF_01261};
DE              EC=3.1.3.- {ECO:0000255|HAMAP-Rule:MF_01261};
GN   Name=cca {ECO:0000255|HAMAP-Rule:MF_01261};
GN   OrderedLocusNames=PA14_07620;
OS   Pseudomonas aeruginosa (strain UCBPP-PA14).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas.
OX   NCBI_TaxID=208963;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=UCBPP-PA14;
RX   PubMed=17038190; DOI=10.1186/gb-2006-7-10-r90;
RA   Lee D.G., Urbach J.M., Wu G., Liberati N.T., Feinbaum R.L., Miyata S.,
RA   Diggins L.T., He J., Saucier M., Deziel E., Friedman L., Li L.,
RA   Grills G., Montgomery K., Kucherlapati R., Rahme L.G., Ausubel F.M.;
RT   "Genomic analysis reveals that Pseudomonas aeruginosa virulence is
RT   combinatorial.";
RL   Genome Biol. 7:R90.1-R90.14(2006).
CC   -!- FUNCTION: Catalyzes the addition and repair of the essential 3'-
CC       terminal CCA sequence in tRNAs without using a nucleic acid
CC       template. Adds these three nucleotides in the order of C, C, and A
CC       to the tRNA nucleotide-73, using CTP and ATP as substrates and
CC       producing inorganic pyrophosphate. Also shows phosphatase, 2'-
CC       nucleotidase and 2',3'-cyclic phosphodiesterase activities. These
CC       phosphohydrolase activities are probably involved in the repair of
CC       the tRNA 3'-CCA terminus degraded by intracellular RNases.
CC       {ECO:0000255|HAMAP-Rule:MF_01261}.
CC   -!- CATALYTIC ACTIVITY: A tRNA precursor + 2 CTP + ATP = a tRNA with a
CC       3' CCA end + 3 diphosphate. {ECO:0000255|HAMAP-Rule:MF_01261}.
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_01261};
CC       Note=Magnesium is required for nucleotidyltransferase activity.
CC       {ECO:0000255|HAMAP-Rule:MF_01261};
CC   -!- COFACTOR:
CC       Name=Ni(2+); Xref=ChEBI:CHEBI:49786;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_01261};
CC       Note=Nickel for phosphatase activity. {ECO:0000255|HAMAP-
CC       Rule:MF_01261};
CC   -!- SUBUNIT: Monomer. Can also form homodimers and oligomers.
CC       {ECO:0000255|HAMAP-Rule:MF_01261}.
CC   -!- DOMAIN: Comprises two domains: an N-terminal domain containing the
CC       nucleotidyltransferase activity and a C-terminal HD domain
CC       associated with both phosphodiesterase and phosphatase activities.
CC       {ECO:0000255|HAMAP-Rule:MF_01261}.
CC   -!- MISCELLANEOUS: A single active site specifically recognizes both
CC       ATP and CTP and is responsible for their addition.
CC       {ECO:0000255|HAMAP-Rule:MF_01261}.
CC   -!- SIMILARITY: Belongs to the tRNA nucleotidyltransferase/poly(A)
CC       polymerase family. Bacterial CCA-adding enzyme type 1 subfamily.
CC       {ECO:0000255|HAMAP-Rule:MF_01261}.
DR   EMBL; CP000438; ABJ15548.1; -; Genomic_DNA.
DR   RefSeq; WP_003117955.1; NC_008463.1.
DR   ProteinModelPortal; Q02TH9; -.
DR   SMR; Q02TH9; -.
DR   EnsemblBacteria; ABJ15548; ABJ15548; PA14_07620.
DR   KEGG; pau:PA14_07620; -.
DR   HOGENOM; HOG000007368; -.
DR   KO; K00974; -.
DR   OMA; GWTFHGH; -.
DR   Proteomes; UP000000653; Chromosome.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0052929; F:ATP:3'-cytidine-cytidine-tRNA adenylyltransferase activity; IEA:UniProtKB-EC.
DR   GO; GO:0052928; F:CTP:3'-cytidine-tRNA cytidylyltransferase activity; IEA:UniProtKB-EC.
DR   GO; GO:0052927; F:CTP:tRNA cytidylyltransferase activity; IEA:UniProtKB-EC.
DR   GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0042245; P:RNA repair; IEA:UniProtKB-KW.
DR   GO; GO:0001680; P:tRNA 3'-terminal CCA addition; IEA:UniProtKB-EC.
DR   CDD; cd05398; NT_ClassII-CCAase; 1.
DR   HAMAP; MF_01261; CCA_bact_type1; 1.
DR   HAMAP; MF_01262; CCA_bact_type2; 1.
DR   InterPro; IPR012006; CCA_bact.
DR   InterPro; IPR006674; HD_domain.
DR   InterPro; IPR002646; PolA_pol_head_dom.
DR   InterPro; IPR032828; PolyA_RNA-bd.
DR   Pfam; PF01966; HD; 1.
DR   Pfam; PF01743; PolyA_pol; 1.
DR   Pfam; PF12627; PolyA_pol_RNAbd; 1.
DR   PIRSF; PIRSF000813; CCA_bact; 1.
DR   PROSITE; PS51831; HD; 1.
PE   3: Inferred from homology;
DR   PRODOM; Q02TH9.
DR   SWISS-2DPAGE; Q02TH9.
KW   ATP-binding; Complete proteome; Hydrolase; Magnesium; Metal-binding;
KW   Multifunctional enzyme; Nickel; Nucleotide-binding;
KW   Nucleotidyltransferase; RNA repair; RNA-binding; Transferase;
KW   tRNA processing.
FT   CHAIN         1    410       Multifunctional CCA protein.
FT                                /FTId=PRO_1000054282.
FT   DOMAIN      228    329       HD. {ECO:0000255|PROSITE-
FT                                ProRule:PRU01175}.
FT   METAL        21     21       Magnesium. {ECO:0000255|HAMAP-
FT                                Rule:MF_01261}.
FT   METAL        23     23       Magnesium. {ECO:0000255|HAMAP-
FT                                Rule:MF_01261}.
FT   BINDING       8      8       ATP or CTP; via amide nitrogen.
FT                                {ECO:0000255|HAMAP-Rule:MF_01261}.
FT   BINDING      11     11       ATP or CTP. {ECO:0000255|HAMAP-
FT                                Rule:MF_01261}.
FT   BINDING      91     91       ATP or CTP. {ECO:0000255|HAMAP-
FT                                Rule:MF_01261}.
FT   BINDING     137    137       ATP or CTP. {ECO:0000255|HAMAP-
FT                                Rule:MF_01261}.
FT   BINDING     140    140       ATP or CTP. {ECO:0000255|HAMAP-
FT                                Rule:MF_01261}.
SQ   SEQUENCE   410 AA;  45639 MW;  738BEAF7F6D6F491 CRC64;
     MQIYKVGGAV RDRLLGRPVT DIDWVVVGAS SDEMLARGYR PVGADFPVFL HPQSGEEYAL
     ARTERKSGRG YGGFTFHASP EVTLEEDLTR RDLTINAMAE DEQGRVIDPY GGQADLEARL
     LRHVSPAFAE DPLRVLRVAR FAARYAGLGF RIAAETLALM RQLAESGELQ ALTPERSWKE
     ISRALMEPNP EVFIQVLHDC GALAELIPEV EALFGVPQPA AHHPEIDTGV HVLSVLQQCA
     RHRQPLSVRW ACLLHDLGKG LTSEADWPRH IAHEARGVPL IDAVNQRFRV PRDCQELARL
     VGEYHTHAHR ALELRPNTLL ELLQSFDVYR RPQRFEEFVA ASEMDARGRL GLEQRDYPQA
     AYLLGAAQAA RAVSVKPLVE KGLKGAELGE ALKRARLAAL KAYKEERGKA
//

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