P21269 (CCA1_YEAST) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
CCA tRNA nucleotidyltransferase, mitochondrial
EC=2.7.7.72

Alternative name(s):
CCA-adding enzyme
tRNA CCA-pyrophosphorylase
tRNA adenylyltransferase
tRNA nucleotidyltransferase

Gene names

Name:	CCA1
Synonyms:	TNT1
Ordered Locus Names:	YER168C

Organism

Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)

Taxonomic identifier

559292 [NCBI]

Taxonomic lineage

Eukaryota › Fungi › Dikarya › Ascomycota › Saccharomycotina › Saccharomycetes › Saccharomycetales › Saccharomycetaceae › Saccharomyces

Protein attributes

Sequence length	546 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	This enzyme carries out synthesis of the tRNA CCA terminus without the direction of a template using the multiple accepting and donating subsites within its active site.
Catalytic activity	A tRNA precursor + 2 CTP + ATP = a tRNA with a 3' CCA end + 3 diphosphate.
Subcellular location	Cytoplasm. Nucleus. Isoform Mitochondrial: Mitochondrion.
Miscellaneous	Present with 13500 molecules/cell in log phase SD medium. Ref.5
Sequence similarities	Belongs to the tRNA nucleotidyltransferase/poly(A) polymerase family.

Ontologies

Keywords
Cellular component	Cytoplasm Mitochondrion Nucleus
Coding sequence diversity	Alternative initiation
Domain	Transit peptide
Ligand	ATP-binding Nucleotide-binding RNA-binding
Molecular function	Nucleotidyltransferase Transferase
PTM	Phosphoprotein
Technical term	Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological process	tRNA 3'-terminal CCA addition Inferred from direct assay. Source: SGD
Cellular component	mitochondrial matrix Inferred from direct assay. Source: SGD nucleus Non-traceable author statement Ref.4. Source: SGD
Molecular function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW RNA binding Inferred from electronic annotation. Source: UniProtKB-KW tRNA adenylyltransferase activity Inferred from direct assay. Source: SGD
Complete GO annotation...

Alternative products

This entry describes 3 isoforms produced by alternative initiation. [Align] [Select]

Isoform Mitochondrial (identifier: P21269-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

Isoform Cytoplasmic+nuclear 1 (identifier: P21269-2)

The sequence of this isoform differs from the canonical sequence as follows:
     1-9: Missing.

Note: Produced by alternative initiation at Met-10 of isoform Mitochondrial.

Isoform Cytoplasmic+nuclear 2 (identifier: P21269-3)

The sequence of this isoform differs from the canonical sequence as follows:
     1-17: Missing.

Note: Produced by alternative initiation at Met-18 of isoform Mitochondrial.

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Transit peptide	1 – ?		Mitochondrion Potential
	Chain	? – 546		CCA tRNA nucleotidyltransferase, mitochondrial		PRO_0000004779
Amino acid modifications
	Modified residue	21	1	Phosphoserine Ref.6
Natural variations
	Alternative sequence	1 – 17	17	Missing in isoform Cytoplasmic+nuclear 2.		VSP_018699
	Alternative sequence	1 – 9	9	Missing in isoform Cytoplasmic+nuclear 1.		VSP_018698

Sequences

	Sequence		Length	Mass (Da)
	Isoform Mitochondrial [UniParc]. Last modified May 1, 1991. Version 1. Checksum: C0B2B918596E19D5	FASTA	546	62,485
	10 20 30 40 50 60 MLRSTISLLM NSAAQKTMTN SNFVLNAPKI TLTKVEQNIC NLLNDYTDLY NQKYHNKPEP 70 80 90 100 110 120 LTLRITGGWV RDKLLGQGSH DLDIAINVMS GEQFATGLNE YLQQHYAKYG AKPHNIHKID 130 140 150 160 170 180 KNPEKSKHLE TATTKLFGVE VDFVNLRSEK YTELSRIPKV CFGTPEEDAL RRDATLNALF 190 200 210 220 230 240 YNIHKGEVED FTKRGLQDLK DGVLRTPLPA KQTFLDDPLR VLRLIRFASR FNFTIDPEVM 250 260 270 280 290 300 AEMGDPQINV AFNSKISRER VGVEMEKILV GPTPLLALQL IQRAHLENVI FFWHNDSSVV 310 320 330 340 350 360 KFNEENCQDM DKINHVYNDN ILNSHLKSFI ELYPMFLEKL PILREKIGRS PGFQQNFILS 370 380 390 400 410 420 AILSPMANLQ IIGNPKKKIN NLVSVTESIV KEGLKLSKND AAVIAKTVDS ICSYEEILAK 430 440 450 460 470 480 FADRSQLKKS EIGIFLRNFN GEWETAHFAS LSDAFLKIPK LETKKIELLF QNYNEFYSYI 490 500 510 520 530 540 FDNNLNNCHE LKPIVDGKQM AKLLQMKPGP WLGKINNEAI RWQFDNPTGT DQELITHLKA ILPKYL
	Isoform Cytoplasmic+nuclear 1 [UniParc]. Checksum: DAB9685770C77A61	FASTA	537	61,470
	10 20 30 40 50 60 MNSAAQKTMT NSNFVLNAPK ITLTKVEQNI CNLLNDYTDL YNQKYHNKPE PLTLRITGGW 70 80 90 100 110 120 VRDKLLGQGS HDLDIAINVM SGEQFATGLN EYLQQHYAKY GAKPHNIHKI DKNPEKSKHL 130 140 150 160 170 180 ETATTKLFGV EVDFVNLRSE KYTELSRIPK VCFGTPEEDA LRRDATLNAL FYNIHKGEVE 190 200 210 220 230 240 DFTKRGLQDL KDGVLRTPLP AKQTFLDDPL RVLRLIRFAS RFNFTIDPEV MAEMGDPQIN 250 260 270 280 290 300 VAFNSKISRE RVGVEMEKIL VGPTPLLALQ LIQRAHLENV IFFWHNDSSV VKFNEENCQD 310 320 330 340 350 360 MDKINHVYND NILNSHLKSF IELYPMFLEK LPILREKIGR SPGFQQNFIL SAILSPMANL 370 380 390 400 410 420 QIIGNPKKKI NNLVSVTESI VKEGLKLSKN DAAVIAKTVD SICSYEEILA KFADRSQLKK 430 440 450 460 470 480 SEIGIFLRNF NGEWETAHFA SLSDAFLKIP KLETKKIELL FQNYNEFYSY IFDNNLNNCH 490 500 510 520 530 ELKPIVDGKQ MAKLLQMKPG PWLGKINNEA IRWQFDNPTG TDQELITHLK AILPKYL
	Isoform Cytoplasmic+nuclear 2 [UniParc]. Checksum: 9479675DBCB98814	FASTA	529	60,638
	10 20 30 40 50 60 MTNSNFVLNA PKITLTKVEQ NICNLLNDYT DLYNQKYHNK PEPLTLRITG GWVRDKLLGQ 70 80 90 100 110 120 GSHDLDIAIN VMSGEQFATG LNEYLQQHYA KYGAKPHNIH KIDKNPEKSK HLETATTKLF 130 140 150 160 170 180 GVEVDFVNLR SEKYTELSRI PKVCFGTPEE DALRRDATLN ALFYNIHKGE VEDFTKRGLQ 190 200 210 220 230 240 DLKDGVLRTP LPAKQTFLDD PLRVLRLIRF ASRFNFTIDP EVMAEMGDPQ INVAFNSKIS 250 260 270 280 290 300 RERVGVEMEK ILVGPTPLLA LQLIQRAHLE NVIFFWHNDS SVVKFNEENC QDMDKINHVY 310 320 330 340 350 360 NDNILNSHLK SFIELYPMFL EKLPILREKI GRSPGFQQNF ILSAILSPMA NLQIIGNPKK 370 380 390 400 410 420 KINNLVSVTE SIVKEGLKLS KNDAAVIAKT VDSICSYEEI LAKFADRSQL KKSEIGIFLR 430 440 450 460 470 480 NFNGEWETAH FASLSDAFLK IPKLETKKIE LLFQNYNEFY SYIFDNNLNN CHELKPIVDG 490 500 510 520 KQMAKLLQMK PGPWLGKINN EAIRWQFDNP TGTDQELITH LKAILPKYL

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Isolation of a temperature-sensitive mutant with an altered tRNA nucleotidyltransferase and cloning of the gene encoding tRNA nucleotidyltransferase in the yeast Saccharomyces cerevisiae." Aebi M., Kirchner G., Chen J.Y., Vijayraghavan U., Jacobson A., Martin N.C., Abelson J. J. Biol. Chem. 265:16216-16220(1990) [PubMed: 2204621] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]	"The nucleotide sequence of Saccharomyces cerevisiae chromosome V." Dietrich F.S., Mulligan J.T., Hennessy K.M., Yelton M.A., Allen E., Araujo R., Aviles E., Berno A., Brennan T., Carpenter J., Chen E., Cherry J.M., Chung E., Duncan M., Guzman E., Hartzell G., Hunicke-Smith S., Hyman R.W. , Kayser A., Komp C., Lashkari D., Lew H., Lin D., Mosedale D., Nakahara K., Namath A., Norgren R., Oefner P., Oh C., Petel F.X., Roberts D., Sehl P., Schramm S., Shogren T., Smith V., Taylor P., Wei Y., Botstein D., Davis R.W. Nature 387:78-81(1997) [PubMed: 9169868] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 204511 / S288c / AB972.
[3]	Saccharomyces Genome Database Submitted (DEC-2009) to the EMBL/GenBank/DDBJ databases Cited for: GENOME REANNOTATION. Strain: ATCC 204508 / S288c.
[4]	"Interplay of heterogeneous transcriptional start sites and translational selection of AUGs dictate the production of mitochondrial and cytosolic/nuclear tRNA nucleotidyltransferase from the same gene in yeast." Wolfe C.L., Lou Y.-C., Hopper A.K., Martin N.C. J. Biol. Chem. 269:13361-13366(1994) [PubMed: 8175766] [Abstract] Cited for: ALTERNATIVE INITIATION, PROTEIN SEQUENCE OF 19-26.
[5]	"Global analysis of protein expression in yeast." Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N., O'Shea E.K., Weissman J.S. Nature 425:737-741(2003) [PubMed: 14562106] [Abstract] Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
[6]	"A multidimensional chromatography technology for in-depth phosphoproteome analysis." Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H. Mol. Cell. Proteomics 7:1389-1396(2008) [PubMed: 18407956] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-21, MASS SPECTROMETRY.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	M59870 Genomic DNA. Translation: AAA35160.1. U18922 Genomic DNA. Translation: AAB64695.1. BK006939 Genomic DNA. Translation: DAA07830.1.
PIR	S11180.
RefSeq	NP_011095.1. NM_001179058.1.
3D structure databases
ProteinModelPortal	P21269.
ModBase	Search...
Protein-protein interaction databases
DIP	DIP-2841N.
IntAct	P21269. 8 interactions.
MINT	MINT-633371.
STRING	P21269.
Proteomic databases
PeptideAtlas	P21269.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblFungi	YER168C; YER168C; YER168C.
GeneID	856915.
KEGG	sce:YER168C.
NMPDR	fig|4932.3.peg.2181.
Organism-specific databases
CYGD	YER168c.
SGD	S000000970. CCA1.
Phylogenomic databases
eggNOG	fuNOG05478.
HOGENOM	HBG619392.
OMA	TCTTKLF.
OrthoDB	EOG4MKRQX.
Gene expression databases
ArrayExpress	P21269.
Genevestigator	P21269.
GermOnline	YER168C. Saccharomyces cerevisiae.
Family and domain databases
InterPro	IPR002646. PolA_pol_head_dom. [Graphical view]
KO	K00974.
Pfam	PF01743. PolyA_pol. 1 hit. [Graphical view]
ProtoNet	Search...
Other
NextBio	983365.

Entry information

Entry name

CCA1_YEAST

Accession

Primary (citable) accession number: P21269
Secondary accession number(s): D3DM76

Entry history

Integrated into UniProtKB/Swiss-Prot:	May 1, 1991
Last sequence update:	May 1, 1991
Last modified:	December 14, 2011
This is version 110 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Fungal Protein Annotation Program