(data stored in SCRATCH9089 zone)

SWISSPROT: CCA_PASMU

ID   CCA_PASMU               Reviewed;         420 AA.
AC   Q9CP21;
DT   16-AUG-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2001, sequence version 1.
DT   11-DEC-2019, entry version 101.
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}; OrderedLocusNames=PM0247;
OS   Pasteurella multocida (strain Pm70).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales;
OC   Pasteurellaceae; Pasteurella.
OX   NCBI_TaxID=272843;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Pm70;
RX   PubMed=11248100; DOI=10.1073/pnas.051634598;
RA   May B.J., Zhang Q., Li L.L., Paustian M.L., Whittam T.S., Kapur V.;
RT   "Complete genomic sequence of Pasteurella multocida Pm70.";
RL   Proc. Natl. Acad. Sci. U.S.A. 98:3460-3465(2001).
CC   -!- FUNCTION: Catalyzes the addition and repair of the essential 3'-
CC       terminal CCA sequence in tRNAs without using a nucleic acid template.
CC       Adds these three nucleotides in the order of C, C, and A to the tRNA
CC       nucleotide-73, using CTP and ATP as substrates and producing inorganic
CC       pyrophosphate. Also shows phosphatase, 2'-nucleotidase and 2',3'-cyclic
CC       phosphodiesterase activities. These phosphohydrolase activities are
CC       probably involved in the repair of the tRNA 3'-CCA terminus degraded by
CC       intracellular RNases. {ECO:0000255|HAMAP-Rule:MF_01261}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a tRNA precursor + ATP + 2 CTP = a tRNA with a 3' CCA end + 3
CC         diphosphate; Xref=Rhea:RHEA:14433, Rhea:RHEA-COMP:10465, Rhea:RHEA-
CC         COMP:10468, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:37563,
CC         ChEBI:CHEBI:74896, ChEBI:CHEBI:83071; EC=2.7.7.72;
CC         Evidence={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 associated
CC       with both phosphodiesterase and phosphatase activities.
CC       {ECO:0000255|HAMAP-Rule:MF_01261}.
CC   -!- MISCELLANEOUS: A single active site specifically recognizes both ATP
CC       and CTP and is responsible for their addition. {ECO:0000255|HAMAP-
CC       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; AE004439; AAK02331.1; -; Genomic_DNA.
DR   SMR; Q9CP21; -.
DR   EnsemblBacteria; AAK02331; AAK02331; PM0247.
DR   KEGG; pmu:PM0247; -.
DR   eggNOG; ENOG4105D4J; Bacteria.
DR   eggNOG; COG0617; LUCA.
DR   HOGENOM; HOG000007368; -.
DR   KO; K00974; -.
DR   OMA; GWTFHGH; -.
DR   Proteomes; UP000000809; Chromosome.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
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:0004112; F:cyclic-nucleotide phosphodiesterase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0016791; F:phosphatase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0000049; F:tRNA binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0016437; F:tRNA cytidylyltransferase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0042245; P:RNA repair; IEA:UniProtKB-KW.
DR   GO; GO:0001680; P:tRNA 3'-terminal CCA addition; IEA:UniProtKB-UniRule.
DR   CDD; cd00077; HDc; 1.
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; IPR003607; HD/PDEase_dom.
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   SMART; SM00471; HDc; 1.
DR   PROSITE; PS51831; HD; 1.
PE   3: Inferred from homology;
DR   PRODOM; Q9CP21.
DR   SWISS-2DPAGE; Q9CP21.
KW   ATP-binding; Hydrolase; Magnesium; Metal-binding; Multifunctional enzyme;
KW   Nickel; Nucleotide-binding; Nucleotidyltransferase; Reference proteome;
KW   RNA repair; RNA-binding; Transferase; tRNA processing.
FT   CHAIN           1..420
FT                   /note="Multifunctional CCA protein"
FT                   /id="PRO_0000138990"
FT   DOMAIN          228..334
FT                   /note="HD"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01175"
FT   METAL           21
FT                   /note="Magnesium"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01261"
FT   METAL           23
FT                   /note="Magnesium"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01261"
FT   BINDING         8
FT                   /note="ATP or CTP; via amide nitrogen"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01261"
FT   BINDING         11
FT                   /note="ATP or CTP"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01261"
FT   BINDING         91
FT                   /note="ATP or CTP"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01261"
FT   BINDING         137
FT                   /note="ATP or CTP"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01261"
FT   BINDING         140
FT                   /note="ATP or CTP"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01261"
SQ   SEQUENCE   420 AA;  48089 MW;  6F65F89C79B2F402 CRC64;
     MKIYLVGGAV RDQLLNLVVK DRDWVVVGAT PDDLLSQGYQ QVGKDFPVFL HPQTKEEYAL
     ARTERKAGSG YTGFICDFSP TISLEQDLSR RDLTINALAQ DLDGKIYDFY GGLTDLKQRL
     LRHVSPAFAE DPLRVLRVAR FAARYHALGF TIASETRELM QQLSQSGELS NLTAERVWLE
     TEKALLEPHP EVYFQTLQEV GALQVLFPEL AALQGVPNPA KYHPEIDTFV HTMLVLQQAV
     LLTENTDSDK SAVRFAAICH DLGKALTPKE ILPHHYGHEK AGVMPTRRLC QRFKLPHAIQ
     DFAELCCEYH SHIHKAFELR AETILKLFNR LDVWRKPERF KALLLVCIAD TRGRTGFEQV
     DYPQREFLWQ LYQSALQVNV QDIIQQGFQQ QAIRDELNRR RIIAIKQTRA EILPRFTNPC
//

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