CCA_GEOSE
ID CCA_GEOSE Reviewed; 404 AA.
AC Q7SIB1;
DT 16-AUG-2005, integrated into UniProtKB/Swiss-Prot.
DT 15-DEC-2003, sequence version 1.
DT 03-AUG-2022, entry version 70.
DE RecName: Full=CCA-adding enzyme;
DE EC=2.7.7.72;
DE AltName: Full=CCA tRNA nucleotidyltransferase;
DE AltName: Full=tRNA CCA-pyrophosphorylase;
DE AltName: Full=tRNA adenylyl-/cytidylyl- transferase;
DE AltName: Full=tRNA nucleotidyltransferase;
DE AltName: Full=tRNA-NT;
GN Name=cca;
OS Geobacillus stearothermophilus (Bacillus stearothermophilus).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Geobacillus.
OX NCBI_TaxID=1422;
RN [1] {ECO:0007744|PDB:1MIV, ECO:0007744|PDB:1MIW, ECO:0007744|PDB:1MIY}
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS) OF
RP NATIVE PROTEIN AND COMPLEXES WITH ATP AND CTP, AND SUBUNIT.
RX PubMed=12526808; DOI=10.1016/s0092-8674(02)01115-7;
RA Li F., Xiong Y., Wang J., Cho H.D., Tomita K., Weiner A.M., Steitz T.A.;
RT "Crystal structures of the Bacillus stearothermophilus CCA-adding enzyme
RT and its complexes with ATP or CTP.";
RL Cell 111:815-824(2002).
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.
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 -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:12526808}.
CC -!- DOMAIN: The crystal structure reveals a seahorse-shaped subunit
CC consisting of four domains: head, neck, body, and tail. The head domain
CC contains the nucleotidyltransferase activity. The neck domain provides
CC a specific template for the incoming ATP or CTP, whereas the body and
CC tail domains may be involved in tRNA binding.
CC -!- MISCELLANEOUS: A single active site specifically recognizes both ATP
CC and CTP and is responsible for their addition.
CC -!- SIMILARITY: Belongs to the tRNA nucleotidyltransferase/poly(A)
CC polymerase family. Bacterial CCA-adding enzyme type 3 subfamily.
CC {ECO:0000305}.
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DR PDB; 1MIV; X-ray; 3.50 A; A/B=1-404.
DR PDB; 1MIW; X-ray; 3.00 A; A/B=1-404.
DR PDB; 1MIY; X-ray; 3.52 A; A/B=1-404.
DR PDBsum; 1MIV; -.
DR PDBsum; 1MIW; -.
DR PDBsum; 1MIY; -.
DR AlphaFoldDB; Q7SIB1; -.
DR SMR; Q7SIB1; -.
DR DrugBank; DB02431; Cytidine-5'-Triphosphate.
DR BRENDA; 2.7.7.72; 623.
DR EvolutionaryTrace; Q7SIB1; -.
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 1: Evidence at protein level;
KW 3D-structure; ATP-binding; Magnesium; Metal-binding; Nucleotide-binding;
KW Nucleotidyltransferase; RNA repair; RNA-binding; Transferase;
KW tRNA processing.
FT CHAIN 1..404
FT /note="CCA-adding enzyme"
FT /id="PRO_0000139033"
FT BINDING 27
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0007744|PDB:1MIW"
FT BINDING 27
FT /ligand="CTP"
FT /ligand_id="ChEBI:CHEBI:37563"
FT /evidence="ECO:0007744|PDB:1MIY"
FT BINDING 30
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0007744|PDB:1MIW"
FT BINDING 30
FT /ligand="CTP"
FT /ligand_id="ChEBI:CHEBI:37563"
FT /evidence="ECO:0007744|PDB:1MIY"
FT BINDING 40
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 42
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 111
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0007744|PDB:1MIW"
FT BINDING 111
FT /ligand="CTP"
FT /ligand_id="ChEBI:CHEBI:37563"
FT /evidence="ECO:0007744|PDB:1MIY"
FT BINDING 154
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0007744|PDB:1MIW"
FT BINDING 154
FT /ligand="CTP"
FT /ligand_id="ChEBI:CHEBI:37563"
FT /evidence="ECO:0007744|PDB:1MIY"
FT BINDING 157
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0007744|PDB:1MIW"
FT BINDING 157
FT /ligand="CTP"
FT /ligand_id="ChEBI:CHEBI:37563"
FT /evidence="ECO:0007744|PDB:1MIY"
FT BINDING 160
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0007744|PDB:1MIW"
FT BINDING 160
FT /ligand="CTP"
FT /ligand_id="ChEBI:CHEBI:37563"
FT /evidence="ECO:0007744|PDB:1MIY"
FT BINDING 163
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0007744|PDB:1MIW"
FT BINDING 163
FT /ligand="CTP"
FT /ligand_id="ChEBI:CHEBI:37563"
FT /evidence="ECO:0007744|PDB:1MIY"
FT SITE 112
FT /note="May assist in discriminating ATP from CTP"
FT SITE 153
FT /note="Involved in nucleotide selection"
FT /evidence="ECO:0000255"
FT HELIX 3..17
FT /evidence="ECO:0007829|PDB:1MIW"
FT STRAND 22..26
FT /evidence="ECO:0007829|PDB:1MIW"
FT HELIX 27..34
FT /evidence="ECO:0007829|PDB:1MIW"
FT STRAND 42..47
FT /evidence="ECO:0007829|PDB:1MIW"
FT HELIX 49..55
FT /evidence="ECO:0007829|PDB:1MIW"
FT STRAND 57..63
FT /evidence="ECO:0007829|PDB:1MIW"
FT HELIX 64..66
FT /evidence="ECO:0007829|PDB:1MIW"
FT STRAND 68..73
FT /evidence="ECO:0007829|PDB:1MIW"
FT STRAND 76..82
FT /evidence="ECO:0007829|PDB:1MIW"
FT STRAND 84..86
FT /evidence="ECO:0007829|PDB:1MIV"
FT STRAND 98..100
FT /evidence="ECO:0007829|PDB:1MIV"
FT HELIX 104..109
FT /evidence="ECO:0007829|PDB:1MIW"
FT STRAND 111..114
FT /evidence="ECO:0007829|PDB:1MIW"
FT HELIX 115..117
FT /evidence="ECO:0007829|PDB:1MIW"
FT STRAND 129..131
FT /evidence="ECO:0007829|PDB:1MIV"
FT HELIX 132..138
FT /evidence="ECO:0007829|PDB:1MIW"
FT STRAND 143..145
FT /evidence="ECO:0007829|PDB:1MIW"
FT HELIX 147..153
FT /evidence="ECO:0007829|PDB:1MIW"
FT HELIX 156..168
FT /evidence="ECO:0007829|PDB:1MIW"
FT HELIX 174..183
FT /evidence="ECO:0007829|PDB:1MIW"
FT HELIX 184..189
FT /evidence="ECO:0007829|PDB:1MIW"
FT HELIX 192..203
FT /evidence="ECO:0007829|PDB:1MIW"
FT STRAND 205..207
FT /evidence="ECO:0007829|PDB:1MIW"
FT HELIX 208..217
FT /evidence="ECO:0007829|PDB:1MIW"
FT TURN 219..222
FT /evidence="ECO:0007829|PDB:1MIW"
FT HELIX 231..236
FT /evidence="ECO:0007829|PDB:1MIW"
FT HELIX 237..239
FT /evidence="ECO:0007829|PDB:1MIW"
FT HELIX 242..244
FT /evidence="ECO:0007829|PDB:1MIW"
FT HELIX 248..258
FT /evidence="ECO:0007829|PDB:1MIW"
FT HELIX 264..270
FT /evidence="ECO:0007829|PDB:1MIW"
FT HELIX 275..290
FT /evidence="ECO:0007829|PDB:1MIW"
FT HELIX 294..296
FT /evidence="ECO:0007829|PDB:1MIW"
FT HELIX 299..321
FT /evidence="ECO:0007829|PDB:1MIW"
FT HELIX 326..336
FT /evidence="ECO:0007829|PDB:1MIW"
FT HELIX 344..346
FT /evidence="ECO:0007829|PDB:1MIW"
FT HELIX 351..358
FT /evidence="ECO:0007829|PDB:1MIW"
FT STRAND 362..364
FT /evidence="ECO:0007829|PDB:1MIV"
FT HELIX 365..378
FT /evidence="ECO:0007829|PDB:1MIW"
FT HELIX 386..397
FT /evidence="ECO:0007829|PDB:1MIW"
FT HELIX 399..403
FT /evidence="ECO:0007829|PDB:1MIW"
SQ SEQUENCE 404 AA; 45369 MW; DC0C8E4C47133940 CRC64;
MKPPFQEALG IIQQLKQHGY DAYFVGGAVR DLLLGRPIGD VDIATSALPE DVMAIFPKTI
DVGSKHGTVV VVHKGKAYEV TTFKTDGDYE DYRRPESVTF VRSLEEDLKR RDFTMNAIAM
DEYGTIIDPF GGREAIRRRI IRTVGEAEKR FREDALRMMR AVRFVSELGF ALAPDTEQAI
VQNAPLLAHI SVERMTMEME KLLGGPFAAR ALPLLAETGL NAYLPGLAGK EKQLRLAAAY
RWPWLAAREE RWALLCHALG VQESRPFLRA WKLPNKVVDE AGAILTALAD IPRPEAWTNE
QLFSAGLERA LSVETVRAAF TGAPPGPWHE KLRRRFASLP IKTKGELAVN GKDVIEWVGK
PAGPWVKEAL DAIWRAVVNG EVENEKERIY AWLMERNRTR EKNC
