Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

Q99J10 (CTU1_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 91. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Cytoplasmic tRNA 2-thiolation protein 1

EC=2.7.7.-
Alternative name(s):
ATP-binding domain-containing protein 3
Cytoplasmic tRNA adenylyltransferase 1
Gene names
Name:Ctu1
Synonyms:Atpbd3, Ncs6
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length420 AA.
Sequence statusComplete.
Protein existenceEvidence at transcript level

General annotation (Comments)

Function

Plays a central role in 2-thiolation of mcm5S2U at tRNA wobble positions of tRNA(Lys), tRNA(Glu) and tRNA(Gln). Directly binds tRNAs and probably acts by catalyzing adenylation of tRNAs, an intermediate required for 2-thiolation. It is unclear whether it acts as a sulfurtransferase that transfers sulfur from thiocarboxylated URM1 onto the uridine of tRNAs at wobble position By similarity. HAMAP-Rule MF_03053

Pathway

tRNA modification; 5-methoxycarbonylmethyl-2-thiouridine-tRNA biosynthesis. HAMAP-Rule MF_03053

Subunit structure

Component of a complex at least composed of URM1, CTU2/NCS2 and CTU1/ATPBD3. May form a heterodimer with CTU2/NCS2 By similarity.

Subcellular location

Cytoplasm By similarity HAMAP-Rule MF_03053.

Sequence similarities

Belongs to the TtcA family. CTU1/NCS6/ATPBD3 subfamily.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 420420Cytoplasmic tRNA 2-thiolation protein 1 HAMAP-Rule MF_03053
PRO_0000282392

Amino acid modifications

Modified residue2001Phosphoserine By similarity

Sequences

Sequence LengthMass (Da)Tools
Q99J10 [UniParc].

Last modified June 1, 2001. Version 1.
Checksum: 3DDCEDBE70D196B1

FASTA42043,823
        10         20         30         40         50         60 
MPAPTCFSCH KTRAALRRPR SGQALCGSCF CAAFEAEVLH TVLAGHLLPP GAVVAVGASG 

        70         80         90        100        110        120 
GKDSTVLAHV LRELAPRLGI TLHLVAVDEG IGGYRDAALE AVRSQAARWE LPLTIVAYED 

       130        140        150        160        170        180 
LFGGWTMDAV ARSTAGSGRS RSCCTFCGVL RRRALEEGAR LVGATHIVTG HNADDMAETV 

       190        200        210        220        230        240 
LMNFLRGDAG RLARGGVLGS TGEGCALPRC RPLQFASQKE VVLYAHFRHL RYFSEECVYA 

       250        260        270        280        290        300 
PEAFRGHARD LLKLLEAARP SAVLDLVHSA ERLALAPAAK PPPPGTCSRC GALASHKLCQ 

       310        320        330        340        350        360 
ACALLDGLNR GLPRLAIGKG RRVLQVEPPQ PGNPSLVTSD PVAPAGPCTC KQPKDKANPC 

       370        380        390        400        410        420 
GNGGDRAGAT CVSQCDLSPG NGEDRAGATC VSQRDLSLGN GGDRAGATCV SQCDLSPVAE 

« Hide

References

[1]"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. expand/collapse author list , 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(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: NOD.
[2]"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(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: NMRI.
Tissue: Mammary tumor.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AK155284 mRNA. Translation: BAE33164.1.
BC005752 mRNA. Translation: AAH05752.1.
RefSeqNP_663557.1. NM_145582.1.
UniGeneMm.26514.

3D structure databases

ProteinModelPortalQ99J10.
SMRQ99J10. Positions 4-309.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING10090.ENSMUSP00000036770.

PTM databases

PhosphoSiteQ99J10.

Proteomic databases

PaxDbQ99J10.
PRIDEQ99J10.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000038332; ENSMUSP00000036770; ENSMUSG00000038888.
GeneID233189.
KEGGmmu:233189.
UCSCuc009gnh.1. mouse.

Organism-specific databases

CTD90353.
MGIMGI:2385277. Ctu1.

Phylogenomic databases

eggNOGCOG0037.
GeneTreeENSGT00390000001041.
HOGENOMHOG000225864.
HOVERGENHBG100428.
InParanoidQ99J10.
KOK14168.
OMAICTQGED.
OrthoDBEOG7PGDRH.
PhylomeDBQ99J10.
TreeFamTF352405.

Enzyme and pathway databases

UniPathwayUPA00988.

Gene expression databases

BgeeQ99J10.
CleanExMM_ATPBD3.
GenevestigatorQ99J10.

Family and domain databases

Gene3D3.40.50.620. 1 hit.
HAMAPMF_03053. CTU1.
InterProIPR000541. Ncs6/Tuc1/Ctu1.
IPR014729. Rossmann-like_a/b/a_fold.
IPR011063. tRNA-lysidine/thiocyt_synth.
[Graphical view]
PfamPF01171. ATP_bind_3. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio381599.
PROQ99J10.
SOURCESearch...

Entry information

Entry nameCTU1_MOUSE
AccessionPrimary (citable) accession number: Q99J10
Entry history
Integrated into UniProtKB/Swiss-Prot: April 3, 2007
Last sequence update: June 1, 2001
Last modified: April 16, 2014
This is version 91 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PATHWAY comments

Index of metabolic and biosynthesis pathways

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot