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Reviewed, UniProtKB/Swiss-Prot Q3U2A8 (SYVM_MOUSE)

Last modified June 16, 2009. Version 43. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

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Names and origin

Protein namesRecommended name:
    Valyl-tRNA synthetase, mitochondrial
    EC=6.1.1.9
Alternative name(s):
    Valine--tRNA ligase
      Short name=ValRS
Gene names
Name: Vars2
Synonyms: Kiaa1885, Vars2l
OrganismMus musculus (Mouse)
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus

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Protein attributes

Sequence length1060 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at transcript level.

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General annotation (Comments)

Catalytic activity

ATP + L-valine + tRNA(Val) = AMP + diphosphate + L-valyl-tRNA(Val).

Subcellular location

Mitochondrion Potential.

Sequence similarities

Belongs to the class-I aminoacyl-tRNA synthetase family.

Sequence caution

The sequence BAD32566.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.

The sequence BAD32566.1 differs from that shown. Reason: Miscellaneous discrepancy. The sequence differs from that shown because it seems to be derived from a pre-mRNA.

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Ontologies

Keywords
   Biological processProtein biosynthesis
   Cellular componentMitochondrion
   DomainTransit peptide
   LigandATP-binding
Nucleotide-binding
   Molecular functionAminoacyl-tRNA synthetase
Ligase
Gene Ontology (GO)
   Biological processvalyl-tRNA aminoacylation

Inferred from electronic annotation. Source: InterPro

   Cellular componentmitochondrion

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular functionATP binding

Inferred from electronic annotation. Source: UniProtKB-KW

valine-tRNA ligase activity

Inferred from electronic annotation. Source: EC

Complete GO annotation...

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Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Transit peptide1 – 1515Mitochondrion Potential
Chain16 – 10601045Valyl-tRNA synthetase, mitochondrial
PRO_0000338002

Regions

Motif146 – 15611"HIGH" region
Motif659 – 6635"KMSKS" region

Sites

Binding site6621ATP By similarity

Experimental info

Sequence conflict571A → V in BAD32566. Ref.1
Sequence conflict571A → V in BAC87668. Ref.3
Sequence conflict3271E → L in BAD32566. Ref.1
Sequence conflict3271E → L in BAC87668. Ref.3
Sequence conflict3661R → H in BAD32566. Ref.1
Sequence conflict3661R → H in BAC87668. Ref.3
Sequence conflict3831Q → R in BAC87668. Ref.3
Sequence conflict4041I → M in BAD32566. Ref.1
Sequence conflict4041I → M in BAC87668. Ref.3
Sequence conflict4081H → R in BAC87668. Ref.3
Sequence conflict4491Q → R in BAD32566. Ref.1
Sequence conflict4491Q → R in BAC87668. Ref.3
Sequence conflict4901R → L in BAC29932. Ref.2
Sequence conflict4901R → L in AAH57036. Ref.4
Sequence conflict6091H → R in BAD32566. Ref.1
Sequence conflict6091H → R in BAC87668. Ref.3
Sequence conflict8891A → T in BAC29932. Ref.2
Sequence conflict8891A → T in AAH57036. Ref.4
Sequence conflict8961R → H in BAC87668. Ref.3
Sequence conflict9441Missing in BAC87668. Ref.3
Sequence conflict9751A → T in BAC29932. Ref.2
Sequence conflict9751A → T in AAH57036. Ref.4
Sequence conflict10191V → M in BAC29932. Ref.2
Sequence conflict10191V → M in BAC87668. Ref.3
Sequence conflict10191V → M in AAH57036. Ref.4

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Sequences

Sequence LengthMass (Da)Tools
Q3U2A8-1 [UniParc].

Last modified October 11, 2005. Version 1.
Checksum: 090ACFD330E78D84

FASTA1,060118,380
        10         20         30         40         50         60 
MPHLPLASFR PPLWGLRPSW GLSRPQALCT QPEPHGSPVS RRNREAKQKR LREKQAALEA 

        70         80         90        100        110        120 
GLAEKSKIPA VPTKAWSHKE VVLYEIPTGP GEKKDVSGPL PPAYSPQYVE AAWYQWWVRE 

       130        140        150        160        170        180 
GFFKPEYQAR LPQATGETFS MCIPPPNVTG SLHIGHALTV AIQDALVRWH RMRGDRVLWI 

       190        200        210        220        230        240 
PGSDHAGIAT QAVVEKQLWK EQRVRRHELS REDFLRAVWQ WKHEKGGEIY EQLCALGASL 

       250        260        270        280        290        300 
DWDRECFTMD AGSSAAVTEA FVRLYNSGLL YRNRQLVNWS CTLRSAISDI EVESRPLPGR 

       310        320        330        340        350        360 
TVLQLPGCPT PVSFGLLASV AFPVDGEPDT EIVVGTTRPE TLPGDVAVAV HPDDPRYTHL 

       370        380        390        400        410        420 
HGRQLRHPLT GQLLPLITDT TVQPHVGTGA VKVTPAHSPI DAEIGTRHGL TPLSVIAEDG 

       430        440        450        460        470        480 
TMTSLCGDWL QGLHRFVARE KIMCTLREQG LFRGLQEHPM VLPICSRSGD VVEYLLKSQW 

       490        500        510        520        530        540 
FVRCQEMGDR AAKAVESGAL ELWPSFHQKS WQHWFAHIGD WCVSRQLWWG HQIPAYRVIG 

       550        560        570        580        590        600 
ENAEDDRKEC WVVGRSEAEA RAVAAKRTGR PEAELTLERD PDVLDTWFSS ALFPFSALGW 

       610        620        630        640        650        660 
PRETPDLAHF YPLTLLETGS DLLMFWVGRM VMLGTQLTGQ LPFSKVLLHS MVRDRQGRKM 

       670        680        690        700        710        720 
SKSLGNVLDP RDIISGQELQ VLQAKLRDGN LDPGELAVAA AAQKKDFPYG IPECGTDALR 

       730        740        750        760        770        780 
FALCSHGILG GDLHLSVSEV LNYRHFCNKL WNALRFVLRA LGDNFVPQPA EEVTPSSPMD 

       790        800        810        820        830        840 
AWILSRLAFA ASECERGFLS RELSLVTHTL YHFWLHNLCD VYLEAVKPVL SSVPRPPGPP 

       850        860        870        880        890        900 
QVLFSCADVG LRLLAPLMPF LAEELWQRLP PRPGGPLAPS ICVAPYPSAR SLEFWRQPEL 

       910        920        930        940        950        960 
ERCFSRVQEV VQALRALRAT YQLTKARPQV LLQCSDPGEQ GLVQPFLEPL GILSHCGAVG 

       970        980        990       1000       1010       1020 
FLSPGAAAPS GWALAPLGDT MKIYMELQGL VDPQSQLPRL TARRQKLQKQ LDDLLNRTVS 

      1030       1040       1050       1060 
EGLAERQQRI SSLHLELSKL DQAASYLQQL MDEAPSAREL

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References

[1]"Prediction of the coding sequences of mouse homologues of KIAA gene: IV. The complete nucleotide sequences of 500 mouse KIAA-homologous cDNAs identified by screening of terminal sequences of cDNA clones randomly sampled from size-fractionated libraries."
Okazaki N., Kikuno R., Ohara R., Inamoto S., Koseki H., Hiraoka S., Saga Y., Seino S., Nishimura M., Kaisho T., Hoshino K., Kitamura H., Nagase T., Ohara O., Koga H.
DNA Res. 11:205-218(2004) [PubMed: 15368895] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
[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. 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: 16141072] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: NOD.
[3]"NEDO cDNA sequencing project."
Kanehori K., Ishibashi T., Chiba Y., Fujimori K., Hiraoka S., Tanai H., Watanabe S., Ishida S., Ono Y., Hotuta T., Watanabe M., Sugiyama T., Irie R., Otsuki T., Sato H., Ota T., Wakamatsu A., Ishii S. expand/collapse author list , Yamamoto J., Isono Y., Kawai-Hio Y., Saito K., Nishikawa T., Kimura K., Matsuo K., Nakamura Y., Sekine M., Kikuchi H., Kanda K., Wagatsuma M., Takahashi-Fujii A., Oshima A., Sugiyama A., Kawakami B., Suzuki Y., Sugano S., Nagahari K., Masuho Y., Nagai K., Isogai T.
Submitted (JUL-2003) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
[4]"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: 15489334] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 395-1060.
Strain: C57BL/6.
Tissue: Brain.

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Cross-references

Sequence databases

AK173288 Transcribed RNA. Translation: BAD32566.1. Sequence problems.
AK038117 mRNA. Translation: BAC29932.1. Different initiation.
AK155386 mRNA. Translation: BAE33234.1.
AK129008 mRNA. Translation: BAC87668.1.
BC057036 mRNA. Translation: AAH57036.2.
IPIIPI00222180.
RefSeqNP_780346.3.
UniGeneMm.32002

3D structure databases

ModBaseSearch...

Genome annotation databases

EnsemblENSMUSG00000038838. Mus musculus. [Contig view]
GeneID68915.
KEGGmmu:68915.

Organism-specific databases

MGIMGI:1916165. Vars2.
RougeSearch...

Phylogenomic databases

HOVERGENQ3U2A8.

Gene expression databases

ArrayExpressQ3U2A8.
BgeeQ3U2A8.
CleanExMM_VARS2.

Family and domain databases

InterProIPR001412. aa-tRNA-synth_I_CS.
IPR002300. aa-tRNA-synth_Ia.
IPR014729. Rossmann-like_a/b/a_fold.
IPR013155. V/L/I-tRNA-synth_anticodon-bd.
IPR002303. Val-tRNA_synth_Ia.
IPR019754. Val-tRNA_synth_Ia_N.
[Graphical view]
Gene3DG3DSA:3.40.50.620. Rossmann-like_a/b/a_fold. 1 hit.
PANTHERPTHR11946:SF5. tRNA-synt_val. 1 hit.
PfamPF08264. Anticodon_1. 1 hit.
PF00133. tRNA-synt_1. 1 hit.
[Graphical view]
PRINTSPR00986. TRNASYNTHVAL.
TIGRFAMsTIGR00422. valS. 1 hit.
PROSITEPS00178. AA_TRNA_LIGASE_I. 1 hit.
[Graphical view]
ProtoNetSearch...

Other Resources

NextBio328167.
SOURCESearch...

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Entry information

Entry nameSYVM_MOUSE
AccessionPrimary (citable) accession number: Q3U2A8
Secondary accession number(s): Q69Z78 expand/collapse secondary AC list , Q6PGG3, Q6ZQL7, Q8BIN9
Entry history
Integrated into UniProtKB/Swiss-Prot: June 10, 2008
Last sequence update: October 11, 2005
Last modified: June 16, 2009
This is version 43 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHPI (Human Proteome Initiative)

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Relevant documents

Aminoacyl-tRNA synthetases

List of aminoacyl-tRNA synthetase entries

MGD cross-references

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

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents