位置:首页 > 蛋白库 > CCA_BAUCH
CCA_BAUCH
ID   CCA_BAUCH               Reviewed;         412 AA.
AC   Q1LSL7;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   30-MAY-2006, sequence version 1.
DT   03-AUG-2022, entry version 83.
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=BCI_0622;
OS   Baumannia cicadellinicola subsp. Homalodisca coagulata.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Candidatus Baumannia.
OX   NCBI_TaxID=374463;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=16729848; DOI=10.1371/journal.pbio.0040188;
RA   Wu D., Daugherty S.C., Van Aken S.E., Pai G.H., Watkins K.L., Khouri H.,
RA   Tallon L.J., Zaborsky J.M., Dunbar H.E., Tran P.L., Moran N.A., Eisen J.A.;
RT   "Metabolic complementarity and genomics of the dual bacterial symbiosis of
RT   sharpshooters.";
RL   PLoS Biol. 4:1079-1092(2006).
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}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; CP000238; ABF14019.1; -; Genomic_DNA.
DR   RefSeq; WP_011520780.1; NC_007984.1.
DR   AlphaFoldDB; Q1LSL7; -.
DR   SMR; Q1LSL7; -.
DR   STRING; 374463.BCI_0622; -.
DR   EnsemblBacteria; ABF14019; ABF14019; BCI_0622.
DR   KEGG; bci:BCI_0622; -.
DR   HOGENOM; CLU_015961_1_1_6; -.
DR   OMA; GWTFHGH; -.
DR   OrthoDB; 2018439at2; -.
DR   Proteomes; UP000002427; 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   Gene3D; 3.30.460.10; -; 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; IPR043519; NT_sf.
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   SUPFAM; SSF81301; SSF81301; 1.
DR   PROSITE; PS51831; HD; 1.
PE   3: Inferred from homology;
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..412
FT                   /note="Multifunctional CCA protein"
FT                   /id="PRO_1000054249"
FT   DOMAIN          227..328
FT                   /note="HD"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01175"
FT   BINDING         8
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01261"
FT   BINDING         8
FT                   /ligand="CTP"
FT                   /ligand_id="ChEBI:CHEBI:37563"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01261"
FT   BINDING         11
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01261"
FT   BINDING         11
FT                   /ligand="CTP"
FT                   /ligand_id="ChEBI:CHEBI:37563"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01261"
FT   BINDING         21
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01261"
FT   BINDING         23
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01261"
FT   BINDING         92
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01261"
FT   BINDING         92
FT                   /ligand="CTP"
FT                   /ligand_id="ChEBI:CHEBI:37563"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01261"
FT   BINDING         138
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01261"
FT   BINDING         138
FT                   /ligand="CTP"
FT                   /ligand_id="ChEBI:CHEBI:37563"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01261"
FT   BINDING         141
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01261"
FT   BINDING         141
FT                   /ligand="CTP"
FT                   /ligand_id="ChEBI:CHEBI:37563"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01261"
SQ   SEQUENCE   412 AA;  47235 MW;  3CEDBB6DB9D14326 CRC64;
     MKKYLVGGAV RDRLLQIPVK ERDWVVIGTT LQDMLKAGYQ QVGKDFPVFL HPKSHEEYAL
     ARIEKKSATG GYTGFTYKAS SEITLEEDLK RRDLTINAIA CDENGSLIDP YNGQRDLNQR
     WLRHVSEAFC EDPLRVLRVA RFAAQLAYLN FRIVPETRLM MQHMISELPL LSPERIWKET
     EKALATRDPQ IYFQVLRDCG ALKTLFPEID ALFGVPAPAK WHPEIDTGIH TMMTVAMAAR
     LSDSIAVRFA SLCHDIGKGL TPRDHWPSHH GHGPAGIPLV QSLCQRLRVP NSIRNLAIIV
     TEYHDLLHYA VKLKPKTLIK LFYAIDVWRR PERLEQIIII SEADARGRAG YENHFYKPGQ
     FIREAYRIAS SIMPCQVISH NLTGNKIGEK LRQYRQQAIA TWKQQNYESK QQ
 
 
维奥蛋白资源库 - 中文蛋白资源 CopyRight © 2010-2024