CCA_LACGA
ID CCA_LACGA Reviewed; 398 AA.
AC Q043S5;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 14-NOV-2006, sequence version 1.
DT 03-AUG-2022, entry version 89.
DE RecName: Full=CCA-adding enzyme {ECO:0000255|HAMAP-Rule:MF_01263};
DE EC=2.7.7.72 {ECO:0000255|HAMAP-Rule:MF_01263};
DE AltName: Full=CCA tRNA nucleotidyltransferase {ECO:0000255|HAMAP-Rule:MF_01263};
DE AltName: Full=tRNA CCA-pyrophosphorylase {ECO:0000255|HAMAP-Rule:MF_01263};
DE AltName: Full=tRNA adenylyl-/cytidylyl- transferase {ECO:0000255|HAMAP-Rule:MF_01263};
DE AltName: Full=tRNA nucleotidyltransferase {ECO:0000255|HAMAP-Rule:MF_01263};
DE AltName: Full=tRNA-NT {ECO:0000255|HAMAP-Rule:MF_01263};
GN Name=cca {ECO:0000255|HAMAP-Rule:MF_01263}; OrderedLocusNames=LGAS_0908;
OS Lactobacillus gasseri (strain ATCC 33323 / DSM 20243 / BCRC 14619 / CIP
OS 102991 / JCM 1131 / KCTC 3163 / NCIMB 11718 / NCTC 13722 / AM63).
OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Lactobacillaceae;
OC Lactobacillus.
OX NCBI_TaxID=324831;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 33323 / DSM 20243 / BCRC 14619 / CIP 102991 / JCM 1131 / KCTC
RC 3163 / NCIMB 11718 / NCTC 13722 / AM63;
RX PubMed=17030793; DOI=10.1073/pnas.0607117103;
RA Makarova K.S., Slesarev A., Wolf Y.I., Sorokin A., Mirkin B., Koonin E.V.,
RA Pavlov A., Pavlova N., Karamychev V., Polouchine N., Shakhova V.,
RA Grigoriev I., Lou Y., Rohksar D., Lucas S., Huang K., Goodstein D.M.,
RA Hawkins T., Plengvidhya V., Welker D., Hughes J., Goh Y., Benson A.,
RA Baldwin K., Lee J.-H., Diaz-Muniz I., Dosti B., Smeianov V., Wechter W.,
RA Barabote R., Lorca G., Altermann E., Barrangou R., Ganesan B., Xie Y.,
RA Rawsthorne H., Tamir D., Parker C., Breidt F., Broadbent J.R., Hutkins R.,
RA O'Sullivan D., Steele J., Unlu G., Saier M.H. Jr., Klaenhammer T.,
RA Richardson P., Kozyavkin S., Weimer B.C., Mills D.A.;
RT "Comparative genomics of the lactic acid bacteria.";
RL Proc. Natl. Acad. Sci. U.S.A. 103:15611-15616(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. {ECO:0000255|HAMAP-Rule:MF_01263}.
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_01263};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_01263};
CC -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_01263}.
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_01263}.
CC -!- SIMILARITY: Belongs to the tRNA nucleotidyltransferase/poly(A)
CC polymerase family. Bacterial CCA-adding enzyme type 3 subfamily.
CC {ECO:0000255|HAMAP-Rule:MF_01263}.
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DR EMBL; CP000413; ABJ60297.1; -; Genomic_DNA.
DR RefSeq; WP_003647382.1; NZ_WBMG01000014.1.
DR AlphaFoldDB; Q043S5; -.
DR SMR; Q043S5; -.
DR GeneID; 66468925; -.
DR KEGG; lga:LGAS_0908; -.
DR HOGENOM; CLU_015961_3_0_9; -.
DR OMA; MRAVRFM; -.
DR OrthoDB; 2018439at2; -.
DR BioCyc; LGAS324831:G1G6Y-902-MON; -.
DR Proteomes; UP000000664; 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_01263; CCA_bact_type3; 1.
DR InterPro; IPR032810; CCA-adding_enz_C.
DR InterPro; IPR023068; CCA-adding_enz_firmicutes.
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 Pfam; PF13735; tRNA_NucTran2_2; 1.
DR SUPFAM; SSF81301; SSF81301; 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..398
FT /note="CCA-adding enzyme"
FT /id="PRO_1000054325"
FT BINDING 32
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01263"
FT BINDING 32
FT /ligand="CTP"
FT /ligand_id="ChEBI:CHEBI:37563"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01263"
FT BINDING 35
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01263"
FT BINDING 35
FT /ligand="CTP"
FT /ligand_id="ChEBI:CHEBI:37563"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01263"
FT BINDING 45
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01263"
FT BINDING 47
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01263"
FT BINDING 116
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01263"
FT BINDING 116
FT /ligand="CTP"
FT /ligand_id="ChEBI:CHEBI:37563"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01263"
FT BINDING 159
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01263"
FT BINDING 159
FT /ligand="CTP"
FT /ligand_id="ChEBI:CHEBI:37563"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01263"
FT BINDING 162
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01263"
FT BINDING 162
FT /ligand="CTP"
FT /ligand_id="ChEBI:CHEBI:37563"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01263"
FT BINDING 165
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01263"
FT BINDING 165
FT /ligand="CTP"
FT /ligand_id="ChEBI:CHEBI:37563"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01263"
FT BINDING 168
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01263"
FT BINDING 168
FT /ligand="CTP"
FT /ligand_id="ChEBI:CHEBI:37563"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01263"
SQ SEQUENCE 398 AA; 44736 MW; 60403FD7A7DB209D CRC64;
MKITNLPEVF TAALPVLKRI NEAGYEAYFV GGSVRDLLLN RHIHDVDIAT SAYPMEIKQI
FKKTIDTGIK HGTVTVLYEG ESYEITTFRT ESGYQDFRRP DHVTFVQNLS EDLKRRDFTI
NALAMGVDGN VIDHFDGLGD LDKHLIRAVG KAENRFHEDA LRMMRAVRFM SQLQFTLEPE
TERAISDNHE LLSKISVERI RDEFVKMGIA PGSQKAFQIF LDTGLSEEVP GFKGKKDNLA
LYPQLNFSPT TEANLWALMI ILLKLPNEKI PSFMRMWKNS NAMERQVADI VTFFDLVSSR
APSNYDLYQA GLETIASTID LAHILGQPIN GSALVDRYEA LPIKNNHDLV IDGHFLLKNG
VPAGPRVGLL LEEIKKAVLE GVISNNEAAI TEFLSLNN
