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Protein

CCA tRNA nucleotidyltransferase 1, mitochondrial

Gene

Trnt1

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

Adds and repairs the conserved 3'-CCA sequence necessary for the attachment of amino acids to the 3' terminus of tRNA molecules, using CTP and ATP as substrates.By similarity

Catalytic activityi

A tRNA precursor + 2 CTP + ATP = a tRNA with a 3' CCA end + 3 diphosphate.

Cofactori

Mg2+Curated

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei77 – 771By similarity
Active sitei79 – 791By similarity
Active sitei121 – 1211By similarity

GO - Molecular functioni

  1. ATP:3'-cytidine-cytidine-tRNA adenylyltransferase activity Source: UniProtKB-EC
  2. ATP binding Source: UniProtKB-KW
  3. CTP:3'-cytidine-tRNA cytidylyltransferase activity Source: UniProtKB-EC
  4. CTP:tRNA cytidylyltransferase activity Source: UniProtKB-EC
  5. tRNA adenylyltransferase activity Source: UniProtKB
  6. tRNA binding Source: UniProtKB
  7. tRNA nucleotidyltransferase activity Source: MGI

GO - Biological processi

  1. tRNA 3'-end processing Source: UniProtKB
  2. tRNA 3'-terminal CCA addition Source: MGI
  3. tRNA processing Source: MGI
Complete GO annotation...

Keywords - Molecular functioni

Nucleotidyltransferase, Transferase

Keywords - Biological processi

tRNA processing

Keywords - Ligandi

ATP-binding, Magnesium, Nucleotide-binding, RNA-binding

Names & Taxonomyi

Protein namesi
Recommended name:
CCA tRNA nucleotidyltransferase 1, mitochondrial (EC:2.7.7.72)
Alternative name(s):
mitochondrial tRNA nucleotidyl transferase, CCA-adding
Short name:
mt CCA-adding enzyme
Short name:
mt tRNA CCA-diphosphorylase
Short name:
mt tRNA CCA-pyrophosphorylase
Short name:
mt tRNA adenylyltransferase
Gene namesi
Name:Trnt1
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589 Componenti: Chromosome 6

Organism-specific databases

MGIiMGI:1917297. Trnt1.

Subcellular locationi

Mitochondrion By similarity

GO - Cellular componenti

  1. intracellular Source: MGI
  2. mitochondrion Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Mitochondrion

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transit peptidei1 – 4141MitochondrionSequence AnalysisAdd
BLAST
Chaini42 – 434393CCA tRNA nucleotidyltransferase 1, mitochondrialPRO_0000004783Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei400 – 4001PhosphoserineBy similarity
Modified residuei402 – 4021N6-acetyllysine1 Publication

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

MaxQBiQ8K1J6.
PaxDbiQ8K1J6.
PRIDEiQ8K1J6.

PTM databases

PhosphoSiteiQ8K1J6.

Expressioni

Gene expression databases

BgeeiQ8K1J6.
CleanExiMM_TRNT1.
GenevestigatoriQ8K1J6.

Interactioni

Subunit structurei

Monomer and homodimer.By similarity

Protein-protein interaction databases

STRINGi10090.ENSMUSP00000108874.

Structurei

3D structure databases

ProteinModelPortaliQ8K1J6.
SMRiQ8K1J6. Positions 30-431.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Keywords - Domaini

Transit peptide

Phylogenomic databases

eggNOGiCOG0617.
GeneTreeiENSGT00390000009678.
HOGENOMiHOG000253345.
HOVERGENiHBG061403.
InParanoidiQ8K1J6.
KOiK00974.
OMAiFPVSGHD.
OrthoDBiEOG7CCBR5.
PhylomeDBiQ8K1J6.
TreeFamiTF313253.

Family and domain databases

InterProiIPR002646. PolA_pol_head_dom.
[Graphical view]
PfamiPF01743. PolyA_pol. 1 hit.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

This entry describes 2 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: Q8K1J6-1) [UniParc]FASTAAdd to basket

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.

« Hide

        10         20         30         40         50
MQSVLYPWHR QVLRCSWSRL CLLKRYLFTM KLQSPEFQSL FTEGLKSLTE
60 70 80 90 100
LFAKENHELR IAGGAVRDLL NGVKPQDVDF ATTATPTQMK EMFQSAGIRM
110 120 130 140 150
INNKGEKHGT ITARLHEENF EVTTLRIDVT TDGRHAEVEF TTDWQKDAER
160 170 180 190 200
RDLTINSMFL GFDGTLFDYF NGYADLKNKK VRFVGHAKQR IQEDYLRILR
210 220 230 240 250
YFRFYGRIVD RPGDHDHETL EAIAENAKGL AGISGERIWV ELKKILTGDH
260 270 280 290 300
VNHLIHLIYD LGVAPHIGLP ANANLEEFNK VSKNVEGFSP KPMTLLASLF
310 320 330 340 350
KVQDDVTKLD LRLKISKEEK NLGLFIVKNR KDLIKATDSS EPLKPYQDFV
360 370 380 390 400
IDSREPDATA RVCELLKYQG EHGLLKEMQQ WSVPPFPVSG HDIRKVGISS
410 420 430
GKEIGALLQQ LREQWKKSGY RMEKDELLSY IKKT
Length:434
Mass (Da):49,895
Last modified:October 1, 2002 - v1
Checksum:i0578FB438165838B
GO
Isoform 2 (identifier: Q8K1J6-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     204-215: FYGRIVDRPGDH → PGIVLGDLTTEK
     216-434: Missing.

Note: No experimental confirmation available.

Show »
Length:215
Mass (Da):25,018
Checksum:iB0AEFBB90317372B
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti202 – 2021F → I in BAB70663 (PubMed:11504732).Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei204 – 21512FYGRI…RPGDH → PGIVLGDLTTEK in isoform 2. 1 PublicationVSP_018616Add
BLAST
Alternative sequencei216 – 434219Missing in isoform 2. 1 PublicationVSP_018617Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB063106 mRNA. Translation: BAB70663.1.
AK011764 mRNA. Translation: BAB27827.3.
AK135791 mRNA. Translation: BAE22664.1.
AK152739 mRNA. Translation: BAE31459.1.
AK166804 mRNA. Translation: BAE39032.1.
BC031764 mRNA. Translation: AAH31764.1.
CCDSiCCDS20397.1. [Q8K1J6-1]
CCDS57443.1. [Q8K1J6-2]
RefSeqiNP_001229287.1. NM_001242358.1. [Q8K1J6-1]
NP_001229289.1. NM_001242360.1. [Q8K1J6-2]
NP_081572.1. NM_027296.3. [Q8K1J6-1]
XP_006506644.1. XM_006506581.2. [Q8K1J6-1]
UniGeneiMm.196332.

Genome annotation databases

EnsembliENSMUST00000057578; ENSMUSP00000060900; ENSMUSG00000013736. [Q8K1J6-1]
ENSMUST00000113247; ENSMUSP00000108873; ENSMUSG00000013736. [Q8K1J6-2]
ENSMUST00000113248; ENSMUSP00000108874; ENSMUSG00000013736. [Q8K1J6-1]
ENSMUST00000113249; ENSMUSP00000108875; ENSMUSG00000013736. [Q8K1J6-1]
GeneIDi70047.
KEGGimmu:70047.
UCSCiuc009dcy.2. mouse. [Q8K1J6-1]
uc029vxx.1. mouse. [Q8K1J6-2]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB063106 mRNA. Translation: BAB70663.1.
AK011764 mRNA. Translation: BAB27827.3.
AK135791 mRNA. Translation: BAE22664.1.
AK152739 mRNA. Translation: BAE31459.1.
AK166804 mRNA. Translation: BAE39032.1.
BC031764 mRNA. Translation: AAH31764.1.
CCDSiCCDS20397.1. [Q8K1J6-1]
CCDS57443.1. [Q8K1J6-2]
RefSeqiNP_001229287.1. NM_001242358.1. [Q8K1J6-1]
NP_001229289.1. NM_001242360.1. [Q8K1J6-2]
NP_081572.1. NM_027296.3. [Q8K1J6-1]
XP_006506644.1. XM_006506581.2. [Q8K1J6-1]
UniGeneiMm.196332.

3D structure databases

ProteinModelPortaliQ8K1J6.
SMRiQ8K1J6. Positions 30-431.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi10090.ENSMUSP00000108874.

PTM databases

PhosphoSiteiQ8K1J6.

Proteomic databases

MaxQBiQ8K1J6.
PaxDbiQ8K1J6.
PRIDEiQ8K1J6.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000057578; ENSMUSP00000060900; ENSMUSG00000013736. [Q8K1J6-1]
ENSMUST00000113247; ENSMUSP00000108873; ENSMUSG00000013736. [Q8K1J6-2]
ENSMUST00000113248; ENSMUSP00000108874; ENSMUSG00000013736. [Q8K1J6-1]
ENSMUST00000113249; ENSMUSP00000108875; ENSMUSG00000013736. [Q8K1J6-1]
GeneIDi70047.
KEGGimmu:70047.
UCSCiuc009dcy.2. mouse. [Q8K1J6-1]
uc029vxx.1. mouse. [Q8K1J6-2]

Organism-specific databases

CTDi51095.
MGIiMGI:1917297. Trnt1.

Phylogenomic databases

eggNOGiCOG0617.
GeneTreeiENSGT00390000009678.
HOGENOMiHOG000253345.
HOVERGENiHBG061403.
InParanoidiQ8K1J6.
KOiK00974.
OMAiFPVSGHD.
OrthoDBiEOG7CCBR5.
PhylomeDBiQ8K1J6.
TreeFamiTF313253.

Miscellaneous databases

ChiTaRSiTrnt1. mouse.
NextBioi330891.
PROiQ8K1J6.
SOURCEiSearch...

Gene expression databases

BgeeiQ8K1J6.
CleanExiMM_TRNT1.
GenevestigatoriQ8K1J6.

Family and domain databases

InterProiIPR002646. PolA_pol_head_dom.
[Graphical view]
PfamiPF01743. PolyA_pol. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Identification and characterization of mammalian mitochondrial tRNA nucleotidyltransferases."
    Nagaike T., Suzuki T., Tomari Y., Takemoto-Hori C., Negayama F., Watanabe K., Ueda T.
    J. Biol. Chem. 276:40041-40049(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
  2. "The transcriptional landscape of the mammalian genome."
    Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
    , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
    Science 309:1559-1563(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
    Strain: C57BL/6J.
    Tissue: Blastocyst, Bone marrow macrophage, Egg and Embryo.
  3. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
    Strain: FVB/N.
    Tissue: Mammary gland.
  4. "SIRT5-mediated lysine desuccinylation impacts diverse metabolic pathways."
    Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y., Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.
    Mol. Cell 50:919-930(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-402, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Embryonic fibroblast.

Entry informationi

Entry nameiTRNT1_MOUSE
AccessioniPrimary (citable) accession number: Q8K1J6
Secondary accession number(s): Q3TKW1
, Q3UX99, Q920N6, Q9CSX0
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 3, 2003
Last sequence update: October 1, 2002
Last modified: April 1, 2015
This is version 110 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.