CCA1_CANGA
ID CCA1_CANGA Reviewed; 531 AA.
AC Q9P4S5; Q6FKG1;
DT 10-JAN-2003, integrated into UniProtKB/Swiss-Prot.
DT 31-AUG-2004, sequence version 2.
DT 25-MAY-2022, entry version 107.
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; OrderedLocusNames=CAGL0L11858g;
OS Candida glabrata (strain ATCC 2001 / CBS 138 / JCM 3761 / NBRC 0622 / NRRL
OS Y-65) (Yeast) (Torulopsis glabrata).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Nakaseomyces;
OC Nakaseomyces/Candida clade.
OX NCBI_TaxID=284593;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], CHARACTERIZATION, AND MUTAGENESIS.
RC STRAIN=ATCC 2001 / CBS 138 / JCM 3761 / NBRC 0622 / NRRL Y-65;
RX PubMed=12478587; DOI=10.1002/yea.926;
RA Hanic-Joyce P.J., Joyce P.B.M.;
RT "Characterization of a gene encoding tRNA nucleotidyltransferase from
RT Candida glabrata.";
RL Yeast 19:1399-1411(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 2001 / CBS 138 / JCM 3761 / NBRC 0622 / NRRL Y-65;
RX PubMed=15229592; DOI=10.1038/nature02579;
RA Dujon B., Sherman D., Fischer G., Durrens P., Casaregola S., Lafontaine I.,
RA de Montigny J., Marck C., Neuveglise C., Talla E., Goffard N., Frangeul L.,
RA Aigle M., Anthouard V., Babour A., Barbe V., Barnay S., Blanchin S.,
RA Beckerich J.-M., Beyne E., Bleykasten C., Boisrame A., Boyer J.,
RA Cattolico L., Confanioleri F., de Daruvar A., Despons L., Fabre E.,
RA Fairhead C., Ferry-Dumazet H., Groppi A., Hantraye F., Hennequin C.,
RA Jauniaux N., Joyet P., Kachouri R., Kerrest A., Koszul R., Lemaire M.,
RA Lesur I., Ma L., Muller H., Nicaud J.-M., Nikolski M., Oztas S.,
RA Ozier-Kalogeropoulos O., Pellenz S., Potier S., Richard G.-F.,
RA Straub M.-L., Suleau A., Swennen D., Tekaia F., Wesolowski-Louvel M.,
RA Westhof E., Wirth B., Zeniou-Meyer M., Zivanovic Y., Bolotin-Fukuhara M.,
RA Thierry A., Bouchier C., Caudron B., Scarpelli C., Gaillardin C.,
RA Weissenbach J., Wincker P., Souciet J.-L.;
RT "Genome evolution in yeasts.";
RL Nature 430:35-44(2004).
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 -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000250}. Cytoplasm
CC {ECO:0000250}. Nucleus {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative initiation; Named isoforms=2;
CC Name=Mitochondrial;
CC IsoId=Q9P4S5-1; Sequence=Displayed;
CC Name=Cytoplasmic+nuclear;
CC IsoId=Q9P4S5-2; Sequence=VSP_018697;
CC -!- SIMILARITY: Belongs to the tRNA nucleotidyltransferase/poly(A)
CC polymerase family. {ECO:0000305}.
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DR EMBL; AF098803; AAF78448.1; -; Genomic_DNA.
DR EMBL; CR380958; CAG62257.1; -; Genomic_DNA.
DR RefSeq; XP_449283.1; XM_449283.1.
DR AlphaFoldDB; Q9P4S5; -.
DR STRING; 5478.XP_449283.1; -.
DR EnsemblFungi; CAG62257; CAG62257; CAGL0L11858g.
DR GeneID; 2890947; -.
DR KEGG; cgr:CAGL0L11858g; -.
DR CGD; CAL0135620; CCA1.
DR VEuPathDB; FungiDB:CAGL0L11858g; -.
DR eggNOG; KOG2159; Eukaryota.
DR HOGENOM; CLU_019592_2_1_1; -.
DR InParanoid; Q9P4S5; -.
DR OMA; QDIDVGI; -.
DR Proteomes; UP000002428; Chromosome L.
DR GO; GO:0005759; C:mitochondrial matrix; IGI:CGD.
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; 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:0004810; F:tRNA adenylyltransferase activity; IGI:CGD.
DR GO; GO:0000049; F:tRNA binding; IEA:EnsemblFungi.
DR GO; GO:0016437; F:tRNA cytidylyltransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0001680; P:tRNA 3'-terminal CCA addition; IGI:CGD.
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; Mitochondrion;
KW Nucleotide-binding; Nucleotidyltransferase; Nucleus; Reference proteome;
KW RNA-binding; Transferase; Transit peptide.
FT TRANSIT 1..?
FT /note="Mitochondrion"
FT /evidence="ECO:0000255"
FT CHAIN ?..531
FT /note="CCA tRNA nucleotidyltransferase, mitochondrial"
FT /id="PRO_0000004778"
FT VAR_SEQ 1..10
FT /note="Missing (in isoform Cytoplasmic+nuclear)"
FT /evidence="ECO:0000305"
FT /id="VSP_018697"
FT MUTAGEN 65
FT /note="D->A: Eliminates incorporation of CTP and ATP."
FT /evidence="ECO:0000269|PubMed:12478587"
FT MUTAGEN 67
FT /note="D->A: Eliminates incorporation of CTP and ATP."
FT /evidence="ECO:0000269|PubMed:12478587"
FT MUTAGEN 67
FT /note="D->E: Lethal."
FT /evidence="ECO:0000269|PubMed:12478587"
FT CONFLICT 80
FT /note="T -> N (in Ref. 1; AAF78448)"
FT /evidence="ECO:0000305"
FT CONFLICT 358
FT /note="A -> R (in Ref. 1; AAF78448)"
FT /evidence="ECO:0000305"
FT CONFLICT 389
FT /note="V -> D (in Ref. 1; AAF78448)"
FT /evidence="ECO:0000305"
FT CONFLICT 496
FT /note="L -> I (in Ref. 1; AAF78448)"
FT /evidence="ECO:0000305"
FT CONFLICT 521
FT /note="F -> L (in Ref. 1; AAF78448)"
FT /evidence="ECO:0000305"
FT CONFLICT 531
FT /note="Q -> QCYMSAIYRFQIY (in Ref. 1; AAF78448)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 531 AA; 62022 MW; E52AAF0DE6959EE3 CRC64;
MFKAIRRVFT MIPRIQLTEK ETRICNLLKD YTAHYNSLHY GQEPLTLRIT GGWVRDKLLG
QGSHDLDIAI NIMSGEEFAT GLNGYLLEHF DKYGVKPHSI HKIDKNPEKS KHLETATTKL
FDVEVDFVNL RSEEYTEDSR IPTTQFGTPE EDALRRDATL NALFYNIQQD AVEDFTKRGW
QDLQDGVLRT PLPARQTFLD DPLRVLRLIR FASRFNFNIE AGVLKEMHDP EINEAFNNKI
SRERIGVEME KILVGPNPIL GLKLIQRTHL ENVIFLWHGD QSVIEYNRKN WPQTKDVEDI
YKKGIFNHHL KNFIHHYKDF LSRYLKLRQA IETKDKSFQQ NFLLASILIP MADLKIIALP
KKKLNNTLPV SESIVREGLK FNKASSIVVA RCVENIAAYN SMVEKYLQSG DLKRSEVGTF
LRELRGDWEI VHYVSLMDQY LKYISRKDNV VNIIDKYDRF WNYIQEQNLQ DSDKMVPIID
GKRMVKILET KPGPWLGKIN DEVILWQFDH PQGTEQELIS FIKSILPNYL Q
