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CCA_FRANO
ID   CCA_FRANO               Reviewed;          84 AA.
AC   Q47907;
DT   15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   03-AUG-2022, entry version 59.
DE   RecName: Full=CCA tRNA nucleotidyltransferase;
DE            EC=2.7.7.72;
DE   AltName: Full=CCA-adding enzyme;
DE   AltName: Full=tRNA CCA-pyrophosphorylase;
DE   AltName: Full=tRNA adenylyltransferase;
DE   Flags: Fragment;
GN   Name=cca;
OS   Francisella novicida.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Thiotrichales;
OC   Francisellaceae; Francisella.
OX   NCBI_TaxID=264;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=U112;
RX   PubMed=7881549; DOI=10.1099/13500872-140-12-3309;
RA   Mdluli K.E., Anthony L.S., Baron G.S., McDonald M.K., Myltseva S.V.,
RA   Nano F.E.;
RT   "Serum-sensitive mutation of Francisella novicida: association with an ABC
RT   transporter gene.";
RL   Microbiology 140:3309-3318(1994).
CC   -!- FUNCTION: This enzyme carries out synthesis of the tRNA CCA terminus
CC       without the direction of a template using the multiple accepting and
CC       donating subsites within its active site. {ECO:0000250}.
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   -!- SIMILARITY: Belongs to the tRNA nucleotidyltransferase/poly(A)
CC       polymerase family. {ECO:0000305}.
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DR   EMBL; L17003; AAD15236.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q47907; -.
DR   SMR; Q47907; -.
DR   STRING; 676032.FN3523_1671; -.
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:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0016437; F:tRNA cytidylyltransferase activity; IEA:UniProtKB-EC.
DR   GO; GO:0008033; P:tRNA processing; IEA:UniProtKB-KW.
DR   Gene3D; 3.30.460.10; -; 1.
DR   InterPro; IPR043519; NT_sf.
DR   InterPro; IPR002646; PolA_pol_head_dom.
DR   Pfam; PF01743; PolyA_pol; 1.
DR   SUPFAM; SSF81301; SSF81301; 1.
PE   3: Inferred from homology;
KW   ATP-binding; Magnesium; Metal-binding; Nucleotide-binding;
KW   Nucleotidyltransferase; RNA-binding; Transferase; tRNA processing.
FT   CHAIN           1..>84
FT                   /note="CCA tRNA nucleotidyltransferase"
FT                   /id="PRO_0000139088"
FT   BINDING         8
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250|UniProtKB:Q7SIB1"
FT   BINDING         8
FT                   /ligand="CTP"
FT                   /ligand_id="ChEBI:CHEBI:37563"
FT                   /evidence="ECO:0000250|UniProtKB:Q7SIB1"
FT   BINDING         11
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250|UniProtKB:Q7SIB1"
FT   BINDING         11
FT                   /ligand="CTP"
FT                   /ligand_id="ChEBI:CHEBI:37563"
FT                   /evidence="ECO:0000250|UniProtKB:Q7SIB1"
FT   BINDING         21
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250|UniProtKB:Q7SIB1"
FT   BINDING         23
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250|UniProtKB:Q7SIB1"
FT   NON_TER         84
SQ   SEQUENCE   84 AA;  9527 MW;  2C8625AF99C84095 CRC64;
     MKFYLVGGAV RDMLLGITPK DKDWVVVGAT EDEMLANGFI KIAANFPVFI HPQTKQEYAL
     ARSEKKTRNG YHGFEVNFSK YITL
 
 
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