(data stored in ACNUC7421 zone)

SWISSPROT: CCA_EDWI9

ID   CCA_EDWI9               Reviewed;         414 AA.
AC   C5BHG5;
DT   22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT   28-JUL-2009, sequence version 1.
DT   07-JUN-2017, entry version 49.
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=NT01EI_0531;
OS   Edwardsiella ictaluri (strain 93-146).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Hafniaceae; Edwardsiella.
OX   NCBI_TaxID=634503;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=93-146;
RA   Williams M.L., Gillaspy A.F., Dyer D.W., Thune R.L., Waldbieser G.C.,
RA   Schuster S.C., Gipson J., Zaitshik J., Landry C., Lawrence M.L.;
RT   "Complete genome sequence of Edwardsiella ictaluri 93-146.";
RL   Submitted (MAR-2009) to the EMBL/GenBank/DDBJ databases.
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; CP001600; ACR67764.1; -; Genomic_DNA.
DR   RefSeq; WP_015869964.1; NC_012779.2.
DR   ProteinModelPortal; C5BHG5; -.
DR   STRING; 634503.NT01EI_0531; -.
DR   EnsemblBacteria; ACR67764; ACR67764; NT01EI_0531.
DR   GeneID; 7961556; -.
DR   KEGG; eic:NT01EI_0531; -.
DR   PATRIC; fig|634503.3.peg.481; -.
DR   eggNOG; ENOG4105D4J; Bacteria.
DR   eggNOG; COG0617; LUCA.
DR   HOGENOM; HOG000007368; -.
DR   KO; K00974; -.
DR   OMA; GWTFHGH; -.
DR   OrthoDB; POG091H055X; -.
DR   Proteomes; UP000001485; 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; C5BHG5.
DR   SWISS-2DPAGE; C5BHG5.
KW   ATP-binding; Complete proteome; Hydrolase; Magnesium; Metal-binding;
KW   Multifunctional enzyme; Nickel; Nucleotide-binding;
KW   Nucleotidyltransferase; Reference proteome; RNA repair; RNA-binding;
KW   Transferase; tRNA processing.
FT   CHAIN         1    414       Multifunctional CCA protein.
FT                                /FTId=PRO_1000214131.
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   414 AA;  46364 MW;  ACF5F0AC830B472A CRC64;
     MKTYLVGGAV RDKYLQLPTQ DRDWVVVGAA PQTLLAQGYQ QVGKDFPVFL HPRSKEEYAL
     ARTERKAGQG YTGFSTYFAP DVTLEQDLLR RDLTINAMAE DDEGQLIDPY GGLQDLQQRQ
     LRHVSEAFVE DPLRVLRVAR FAARFAPLGF EVAAPTLALM QQMSQQGELA HLTPERVWLE
     TEKALSGPVP QVYFQVLRDC GALAVLFPEI DRLFGVPAPA QWHPEIDTGI HTLLTLAMAS
     HLSDDVAVRF AALTHDVGKG LTNPNFWPHH HGHGPAGVRL VREMCQRLRT PNPVRDLALL
     VAEYHDLIHT VERLRPATLL KLLDTIDVWR RPQRLQQMIL CSEADARGRT GLEDQPYPQA
     GYLRAAYHQA AQVAVCNVIT DGFQGAAIRE ELQTRRLQAL KSWKAAQEAA LNAE
//

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