CCA1_YEAST
ID CCA1_YEAST Reviewed; 546 AA.
AC P21269; D3DM76;
DT 01-MAY-1991, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1991, sequence version 1.
DT 03-AUG-2022, entry version 179.
DE RecName: Full=CCA tRNA nucleotidyltransferase, mitochondrial;
DE EC=2.7.7.72;
DE AltName: Full=CCA-adding enzyme;
DE AltName: Full=tRNA CCA-pyrophosphorylase;
DE AltName: Full=tRNA adenylyltransferase;
DE AltName: Full=tRNA nucleotidyltransferase;
DE Flags: Precursor;
GN Name=CCA1; Synonyms=TNT1; OrderedLocusNames=YER168C;
OS Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX NCBI_TaxID=559292;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=2204621; DOI=10.1016/s0021-9258(17)46210-7;
RA Aebi M., Kirchner G., Chen J.Y., Vijayraghavan U., Jacobson A.,
RA Martin N.C., Abelson J.;
RT "Isolation of a temperature-sensitive mutant with an altered tRNA
RT nucleotidyltransferase and cloning of the gene encoding tRNA
RT nucleotidyltransferase in the yeast Saccharomyces cerevisiae.";
RL J. Biol. Chem. 265:16216-16220(1990).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169868;
RA Dietrich F.S., Mulligan J.T., Hennessy K.M., Yelton M.A., Allen E.,
RA Araujo R., Aviles E., Berno A., Brennan T., Carpenter J., Chen E.,
RA Cherry J.M., Chung E., Duncan M., Guzman E., Hartzell G., Hunicke-Smith S.,
RA Hyman R.W., Kayser A., Komp C., Lashkari D., Lew H., Lin D., Mosedale D.,
RA Nakahara K., Namath A., Norgren R., Oefner P., Oh C., Petel F.X.,
RA Roberts D., Sehl P., Schramm S., Shogren T., Smith V., Taylor P., Wei Y.,
RA Botstein D., Davis R.W.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome V.";
RL Nature 387:78-81(1997).
RN [3]
RP GENOME REANNOTATION.
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=24374639; DOI=10.1534/g3.113.008995;
RA Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
RA Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
RA Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.;
RT "The reference genome sequence of Saccharomyces cerevisiae: Then and now.";
RL G3 (Bethesda) 4:389-398(2014).
RN [4]
RP ALTERNATIVE INITIATION, AND PROTEIN SEQUENCE OF 19-26.
RX PubMed=8175766; DOI=10.1016/s0021-9258(17)36841-2;
RA Wolfe C.L., Lou Y.-C., Hopper A.K., Martin N.C.;
RT "Interplay of heterogeneous transcriptional start sites and translational
RT selection of AUGs dictate the production of mitochondrial and
RT cytosolic/nuclear tRNA nucleotidyltransferase from the same gene in
RT yeast.";
RL J. Biol. Chem. 269:13361-13366(1994).
RN [5]
RP LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
RX PubMed=14562106; DOI=10.1038/nature02046;
RA Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N.,
RA O'Shea E.K., Weissman J.S.;
RT "Global analysis of protein expression in yeast.";
RL Nature 425:737-741(2003).
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.
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 -!- INTERACTION:
CC P21269; P00925: ENO2; NbExp=2; IntAct=EBI-4347, EBI-6475;
CC -!- SUBCELLULAR LOCATION: Cytoplasm. Nucleus.
CC -!- SUBCELLULAR LOCATION: [Isoform Mitochondrial]: Mitochondrion.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative initiation; Named isoforms=3;
CC Name=Mitochondrial;
CC IsoId=P21269-1; Sequence=Displayed;
CC Name=Cytoplasmic+nuclear 1;
CC IsoId=P21269-2; Sequence=VSP_018698;
CC Name=Cytoplasmic+nuclear 2;
CC IsoId=P21269-3; Sequence=VSP_018699;
CC -!- MISCELLANEOUS: Present with 13500 molecules/cell in log phase SD
CC medium. {ECO:0000269|PubMed:14562106}.
CC -!- MISCELLANEOUS: [Isoform Cytoplasmic+nuclear 1]: Produced by alternative
CC initiation at Met-10 of isoform Mitochondrial. {ECO:0000305}.
CC -!- MISCELLANEOUS: [Isoform Cytoplasmic+nuclear 2]: Produced by alternative
CC initiation at Met-18 of isoform Mitochondrial. {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the tRNA nucleotidyltransferase/poly(A)
CC polymerase family. {ECO:0000305}.
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DR EMBL; M59870; AAA35160.1; -; Genomic_DNA.
DR EMBL; U18922; AAB64695.1; -; Genomic_DNA.
DR EMBL; BK006939; DAA07830.1; -; Genomic_DNA.
DR PIR; S11180; S11180.
DR RefSeq; NP_011095.1; NM_001179058.1. [P21269-1]
DR AlphaFoldDB; P21269; -.
DR SMR; P21269; -.
DR BioGRID; 36921; 260.
DR DIP; DIP-2841N; -.
DR IntAct; P21269; 6.
DR MINT; P21269; -.
DR STRING; 4932.YER168C; -.
DR iPTMnet; P21269; -.
DR MaxQB; P21269; -.
DR PaxDb; P21269; -.
DR PeptideAtlas; P21269; -.
DR PRIDE; P21269; -.
DR EnsemblFungi; YER168C_mRNA; YER168C; YER168C. [P21269-1]
DR GeneID; 856915; -.
DR KEGG; sce:YER168C; -.
DR SGD; S000000970; CCA1.
DR VEuPathDB; FungiDB:YER168C; -.
DR eggNOG; KOG2159; Eukaryota.
DR GeneTree; ENSGT00390000009678; -.
DR HOGENOM; CLU_019592_2_1_1; -.
DR InParanoid; P21269; -.
DR OMA; QDIDVGI; -.
DR BioCyc; YEAST:G3O-30329-MON; -.
DR BRENDA; 2.7.7.72; 984.
DR PRO; PR:P21269; -.
DR Proteomes; UP000002311; Chromosome V.
DR RNAct; P21269; protein.
DR GO; GO:0005759; C:mitochondrial matrix; IDA:SGD.
DR GO; GO:0005739; C:mitochondrion; HDA:SGD.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0052929; F:ATP:3'-cytidine-cytidine-tRNA adenylyltransferase activity; IDA:SGD.
DR GO; GO:0052928; F:CTP:3'-cytidine-tRNA cytidylyltransferase activity; IDA:SGD.
DR GO; GO:0052927; F:CTP:tRNA cytidylyltransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0016779; F:nucleotidyltransferase activity; IBA:GO_Central.
DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
DR GO; GO:0004810; F:tRNA adenylyltransferase activity; IDA:SGD.
DR GO; GO:0016437; F:tRNA cytidylyltransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0001680; P:tRNA 3'-terminal CCA addition; IDA:SGD.
DR CDD; cd05398; NT_ClassII-CCAase; 1.
DR Gene3D; 3.30.460.10; -; 1.
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 SUPFAM; SSF81301; SSF81301; 1.
PE 1: Evidence at protein level;
KW Alternative initiation; ATP-binding; Cytoplasm; Direct protein sequencing;
KW Mitochondrion; Nucleotide-binding; Nucleotidyltransferase; Nucleus;
KW Reference proteome; RNA-binding; Transferase; Transit peptide.
FT TRANSIT 1..?
FT /note="Mitochondrion"
FT /evidence="ECO:0000255"
FT CHAIN ?..546
FT /note="CCA tRNA nucleotidyltransferase, mitochondrial"
FT /id="PRO_0000004779"
FT VAR_SEQ 1..17
FT /note="Missing (in isoform Cytoplasmic+nuclear 2)"
FT /evidence="ECO:0000305"
FT /id="VSP_018699"
FT VAR_SEQ 1..9
FT /note="Missing (in isoform Cytoplasmic+nuclear 1)"
FT /evidence="ECO:0000305"
FT /id="VSP_018698"
SQ SEQUENCE 546 AA; 62485 MW; C0B2B918596E19D5 CRC64;
MLRSTISLLM NSAAQKTMTN SNFVLNAPKI TLTKVEQNIC NLLNDYTDLY NQKYHNKPEP
LTLRITGGWV RDKLLGQGSH DLDIAINVMS GEQFATGLNE YLQQHYAKYG AKPHNIHKID
KNPEKSKHLE TATTKLFGVE VDFVNLRSEK YTELSRIPKV CFGTPEEDAL RRDATLNALF
YNIHKGEVED FTKRGLQDLK DGVLRTPLPA KQTFLDDPLR VLRLIRFASR FNFTIDPEVM
AEMGDPQINV AFNSKISRER VGVEMEKILV GPTPLLALQL IQRAHLENVI FFWHNDSSVV
KFNEENCQDM DKINHVYNDN ILNSHLKSFI ELYPMFLEKL PILREKIGRS PGFQQNFILS
AILSPMANLQ IIGNPKKKIN NLVSVTESIV KEGLKLSKND AAVIAKTVDS ICSYEEILAK
FADRSQLKKS EIGIFLRNFN GEWETAHFAS LSDAFLKIPK LETKKIELLF QNYNEFYSYI
FDNNLNNCHE LKPIVDGKQM AKLLQMKPGP WLGKINNEAI RWQFDNPTGT DQELITHLKA
ILPKYL
