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CCA_BLOPB
ID   CCA_BLOPB               Reviewed;         408 AA.
AC   Q493X4;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   13-SEP-2005, sequence version 1.
DT   03-AUG-2022, entry version 88.
DE   RecName: Full=CCA-adding enzyme {ECO:0000255|HAMAP-Rule:MF_01262};
DE            EC=2.7.7.72 {ECO:0000255|HAMAP-Rule:MF_01262};
DE   AltName: Full=CCA tRNA nucleotidyltransferase {ECO:0000255|HAMAP-Rule:MF_01262};
DE   AltName: Full=tRNA CCA-pyrophosphorylase {ECO:0000255|HAMAP-Rule:MF_01262};
DE   AltName: Full=tRNA adenylyl-/cytidylyl- transferase {ECO:0000255|HAMAP-Rule:MF_01262};
DE   AltName: Full=tRNA nucleotidyltransferase {ECO:0000255|HAMAP-Rule:MF_01262};
DE   AltName: Full=tRNA-NT {ECO:0000255|HAMAP-Rule:MF_01262};
GN   Name=cca {ECO:0000255|HAMAP-Rule:MF_01262}; OrderedLocusNames=BPEN_064;
OS   Blochmannia pennsylvanicus (strain BPEN).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; ant endosymbionts; Candidatus Blochmannia.
OX   NCBI_TaxID=291272;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BPEN;
RX   PubMed=16077009; DOI=10.1101/gr.3771305;
RA   Degnan P.H., Lazarus A.B., Wernegreen J.J.;
RT   "Genome sequence of Blochmannia pennsylvanicus indicates parallel
RT   evolutionary trends among bacterial mutualists of insects.";
RL   Genome Res. 15:1023-1033(2005).
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. {ECO:0000255|HAMAP-Rule:MF_01262}.
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_01262};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_01262};
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_01262}.
CC   -!- SIMILARITY: Belongs to the tRNA nucleotidyltransferase/poly(A)
CC       polymerase family. Bacterial CCA-adding enzyme type 2 subfamily.
CC       {ECO:0000255|HAMAP-Rule:MF_01262}.
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DR   EMBL; CP000016; AAZ40710.1; -; Genomic_DNA.
DR   RefSeq; WP_011282616.1; NC_007292.1.
DR   AlphaFoldDB; Q493X4; -.
DR   SMR; Q493X4; -.
DR   STRING; 291272.BPEN_064; -.
DR   EnsemblBacteria; AAZ40710; AAZ40710; BPEN_064.
DR   KEGG; bpn:BPEN_064; -.
DR   eggNOG; COG0617; Bacteria.
DR   HOGENOM; CLU_015961_1_1_6; -.
DR   OMA; GWTFHGH; -.
DR   BioCyc; CBLO291272:BPEN_RS00310-MON; -.
DR   Proteomes; UP000007794; 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:0000287; F:magnesium ion binding; 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; cd05398; NT_ClassII-CCAase; 1.
DR   Gene3D; 3.30.460.10; -; 1.
DR   HAMAP; MF_01262; CCA_bact_type2; 1.
DR   InterPro; IPR012006; CCA_bact.
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; 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; Magnesium; Metal-binding; Nucleotide-binding;
KW   Nucleotidyltransferase; RNA repair; RNA-binding; Transferase;
KW   tRNA processing.
FT   CHAIN           1..408
FT                   /note="CCA-adding enzyme"
FT                   /id="PRO_1000054314"
FT   DOMAIN          226..329
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_01262"
FT   BINDING         8
FT                   /ligand="CTP"
FT                   /ligand_id="ChEBI:CHEBI:37563"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01262"
FT   BINDING         11
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01262"
FT   BINDING         11
FT                   /ligand="CTP"
FT                   /ligand_id="ChEBI:CHEBI:37563"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01262"
FT   BINDING         21
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01262"
FT   BINDING         23
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01262"
FT   BINDING         91
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01262"
FT   BINDING         91
FT                   /ligand="CTP"
FT                   /ligand_id="ChEBI:CHEBI:37563"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01262"
FT   BINDING         137
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01262"
FT   BINDING         137
FT                   /ligand="CTP"
FT                   /ligand_id="ChEBI:CHEBI:37563"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01262"
FT   BINDING         140
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01262"
FT   BINDING         140
FT                   /ligand="CTP"
FT                   /ligand_id="ChEBI:CHEBI:37563"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01262"
SQ   SEQUENCE   408 AA;  47442 MW;  54C5EDA653982A08 CRC64;
     MEKYLVGGAV RDALLKLPVQ EKDWVVVGSS PQEMLNIGYE QVGKDFPVFL HPESHEEYAL
     ARTERKSGQG YTGFICHTAP SITIEEDLYR RDLTINAMAY DSHGNLIDPY HGQRDIKLRL
     LRHVSHTFHE DPLRVLRVAR FAARFAHMNF AIAPETLILM KQMIHELLSL SPERIWTETK
     KALITDNPQV YFTVLRHCGA LKILFPELDA LFDIPTPTQY CTKINTGYYT MTTLSKAAYL
     TDDISVRFSV LCRDLGKGIP LNKINKNTKH HDHRKLGITL IHNLCNRFKI PHEIRNFSKI
     TSEYHDYLYN VKILKPEMLM TLFHVFDCWR RPNRIDQIIL VSQSDPIRWK NYNNYSLNQE
     NLLRTAFTVT KKISTVDIIK DGFTGSNISR ELYARRLHAL NSWKNKQI
 
 
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