ID   B7ZCJ6_HUMAN            Unreviewed;       326 AA.
AC   B7ZCJ6;
DT   03-MAR-2009, integrated into UniProtKB/TrEMBL.
DT   03-MAR-2009, sequence version 1.
DT   05-FEB-2025, entry version 119.
DE   RecName: Full=Valine--tRNA ligase, mitochondrial {ECO:0000256|ARBA:ARBA00040837};
DE            EC=6.1.1.9 {ECO:0000256|ARBA:ARBA00013169};
DE   AltName: Full=Valyl-tRNA synthetase {ECO:0000256|ARBA:ARBA00029936};
DE   Flags: Fragment;
GN   Name=VARS2 {ECO:0000313|Ensembl:ENSP00000403749.1};
OS   Homo sapiens (Human).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Homo.
OX   NCBI_TaxID=9606 {ECO:0000313|Ensembl:ENSP00000403749.1, ECO:0000313|Proteomes:UP000005640};
RN   [1] {ECO:0000313|Ensembl:ENSP00000403749.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=11237011; DOI=10.1038/35057062;
RG   International Human Genome Sequencing Consortium;
RA   Lander E.S., Linton L.M., Birren B., Nusbaum C., Zody M.C., Baldwin J.,
RA   Devon K., Dewar K., Doyle M., FitzHugh W., Funke R., Gage D., Harris K.,
RA   Heaford A., Howland J., Kann L., Lehoczky J., LeVine R., McEwan P.,
RA   McKernan K., Meldrim J., Mesirov J.P., Miranda C., Morris W., Naylor J.,
RA   Raymond C., Rosetti M., Santos R., Sheridan A., Sougnez C.,
RA   Stange-Thomann N., Stojanovic N., Subramanian A., Wyman D., Rogers J.,
RA   Sulston J., Ainscough R., Beck S., Bentley D., Burton J., Clee C.,
RA   Carter N., Coulson A., Deadman R., Deloukas P., Dunham A., Dunham I.,
RA   Durbin R., French L., Grafham D., Gregory S., Hubbard T., Humphray S.,
RA   Hunt A., Jones M., Lloyd C., McMurray A., Matthews L., Mercer S., Milne S.,
RA   Mullikin J.C., Mungall A., Plumb R., Ross M., Shownkeen R., Sims S.,
RA   Waterston R.H., Wilson R.K., Hillier L.W., McPherson J.D., Marra M.A.,
RA   Mardis E.R., Fulton L.A., Chinwalla A.T., Pepin K.H., Gish W.R.,
RA   Chissoe S.L., Wendl M.C., Delehaunty K.D., Miner T.L., Delehaunty A.,
RA   Kramer J.B., Cook L.L., Fulton R.S., Johnson D.L., Minx P.J., Clifton S.W.,
RA   Hawkins T., Branscomb E., Predki P., Richardson P., Wenning S., Slezak T.,
RA   Doggett N., Cheng J.F., Olsen A., Lucas S., Elkin C., Uberbacher E.,
RA   Frazier M., Gibbs R.A., Muzny D.M., Scherer S.E., Bouck J.B.,
RA   Sodergren E.J., Worley K.C., Rives C.M., Gorrell J.H., Metzker M.L.,
RA   Naylor S.L., Kucherlapati R.S., Nelson D.L., Weinstock G.M., Sakaki Y.,
RA   Fujiyama A., Hattori M., Yada T., Toyoda A., Itoh T., Kawagoe C.,
RA   Watanabe H., Totoki Y., Taylor T., Weissenbach J., Heilig R., Saurin W.,
RA   Artiguenave F., Brottier P., Bruls T., Pelletier E., Robert C., Wincker P.,
RA   Smith D.R., Doucette-Stamm L., Rubenfield M., Weinstock K., Lee H.M.,
RA   Dubois J., Rosenthal A., Platzer M., Nyakatura G., Taudien S., Rump A.,
RA   Yang H., Yu J., Wang J., Huang G., Gu J., Hood L., Rowen L., Madan A.,
RA   Qin S., Davis R.W., Federspiel N.A., Abola A.P., Proctor M.J., Myers R.M.,
RA   Schmutz J., Dickson M., Grimwood J., Cox D.R., Olson M.V., Kaul R.,
RA   Raymond C., Shimizu N., Kawasaki K., Minoshima S., Evans G.A.,
RA   Athanasiou M., Schultz R., Roe B.A., Chen F., Pan H., Ramser J.,
RA   Lehrach H., Reinhardt R., McCombie W.R., de la Bastide M., Dedhia N.,
RA   Blocker H., Hornischer K., Nordsiek G., Agarwala R., Aravind L.,
RA   Bailey J.A., Bateman A., Batzoglou S., Birney E., Bork P., Brown D.G.,
RA   Burge C.B., Cerutti L., Chen H.C., Church D., Clamp M., Copley R.R.,
RA   Doerks T., Eddy S.R., Eichler E.E., Furey T.S., Galagan J., Gilbert J.G.,
RA   Harmon C., Hayashizaki Y., Haussler D., Hermjakob H., Hokamp K., Jang W.,
RA   Johnson L.S., Jones T.A., Kasif S., Kaspryzk A., Kennedy S., Kent W.J.,
RA   Kitts P., Koonin E.V., Korf I., Kulp D., Lancet D., Lowe T.M.,
RA   McLysaght A., Mikkelsen T., Moran J.V., Mulder N., Pollara V.J.,
RA   Ponting C.P., Schuler G., Schultz J., Slater G., Smit A.F., Stupka E.,
RA   Szustakowski J., Thierry-Mieg D., Thierry-Mieg J., Wagner L., Wallis J.,
RA   Wheeler R., Williams A., Wolf Y.I., Wolfe K.H., Yang S.P., Yeh R.F.,
RA   Collins F., Guyer M.S., Peterson J., Felsenfeld A., Wetterstrand K.A.,
RA   Patrinos A., Morgan M.J., de Jong P., Catanese J.J., Osoegawa K.,
RA   Shizuya H., Choi S., Chen Y.J.;
RT   "Initial sequencing and analysis of the human genome.";
RL   Nature 409:860-921(2001).
RN   [2] {ECO:0000313|Ensembl:ENSP00000403749.1, ECO:0000313|Proteomes:UP000005640}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=14574404; DOI=10.1038/nature02055;
RA   Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L.,
RA   Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., Gilbert J.G.,
RA   Clamp M.E., Bethel G., Milne S., Ainscough R., Almeida J.P., Ambrose K.D.,
RA   Andrews T.D., Ashwell R.I., Babbage A.K., Bagguley C.L., Bailey J.,
RA   Banerjee R., Barker D.J., Barlow K.F., Bates K., Beare D.M., Beasley H.,
RA   Beasley O., Bird C.P., Blakey S., Bray-Allen S., Brook J., Brown A.J.,
RA   Brown J.Y., Burford D.C., Burrill W., Burton J., Carder C., Carter N.P.,
RA   Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V.,
RA   Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J.,
RA   Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., Ellington A.E.,
RA   Evans K.A., Faulkner L., Francis M.D., Frankish A., Frankland J.,
RA   French L., Garner P., Garnett J., Ghori M.J., Gilby L.M., Gillson C.J.,
RA   Glithero R.J., Grafham D.V., Grant M., Gribble S., Griffiths C.,
RA   Griffiths M., Hall R., Halls K.S., Hammond S., Harley J.L., Hart E.A.,
RA   Heath P.D., Heathcott R., Holmes S.J., Howden P.J., Howe K.L., Howell G.R.,
RA   Huckle E., Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M.,
RA   Joy A.A., Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K.,
RA   Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R.,
RA   Lloyd D.M., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M.,
RA   Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., McMurray A.,
RA   Moore M.J., Mullikin J.C., Niblett D., Nickerson T., Novik K.L., Oliver K.,
RA   Overton-Larty E.K., Parker A., Patel R., Pearce A.V., Peck A.I.,
RA   Phillimore B., Phillips S., Plumb R.W., Porter K.M., Ramsey Y., Ranby S.A.,
RA   Rice C.M., Ross M.T., Searle S.M., Sehra H.K., Sheridan E., Skuce C.D.,
RA   Smith S., Smith M., Spraggon L., Squares S.L., Steward C.A., Sycamore N.,
RA   Tamlyn-Hall G., Tester J., Theaker A.J., Thomas D.W., Thorpe A., Tracey A.,
RA   Tromans A., Tubby B., Wall M., Wallis J.M., West A.P., White S.S.,
RA   Whitehead S.L., Whittaker H., Wild A., Willey D.J., Wilmer T.E., Wood J.M.,
RA   Wray P.W., Wyatt J.C., Young L., Younger R.M., Bentley D.R., Coulson A.,
RA   Durbin R., Hubbard T., Sulston J.E., Dunham I., Rogers J., Beck S.;
RT   "The DNA sequence and analysis of human chromosome 6.";
RL   Nature 425:805-811(2003).
RN   [3] {ECO:0000313|Ensembl:ENSP00000403749.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=15496913; DOI=10.1038/nature03001;
RG   International Human Genome Sequencing Consortium;
RT   "Finishing the euchromatic sequence of the human genome.";
RL   Nature 431:931-945(2004).
RN   [4] {ECO:0007829|PubMed:21269460}
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA   Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Burckstummer T.,
RA   Bennett K.L., Superti-Furga G., Colinge J.;
RT   "Initial characterization of the human central proteome.";
RL   BMC Syst. Biol. 5:17-17(2011).
RN   [5] {ECO:0000313|Ensembl:ENSP00000403749.1}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (OCT-2024) to UniProtKB.
CC   -!- FUNCTION: Catalyzes the attachment of valine to tRNA(Val) in a two-step
CC       reaction: valine is first activated by ATP to form Val-AMP and then
CC       transferred to the acceptor end of tRNA(Val).
CC       {ECO:0000256|ARBA:ARBA00043854}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=tRNA(Val) + L-valine + ATP = L-valyl-tRNA(Val) + AMP +
CC         diphosphate; Xref=Rhea:RHEA:10704, Rhea:RHEA-COMP:9672, Rhea:RHEA-
CC         COMP:9708, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:57762,
CC         ChEBI:CHEBI:78442, ChEBI:CHEBI:78537, ChEBI:CHEBI:456215; EC=6.1.1.9;
CC         Evidence={ECO:0000256|ARBA:ARBA00047552};
CC   -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000256|ARBA:ARBA00004173}.
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DR   EMBL; AL669830; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   ProteomicsDB; 7178; -.
DR   Antibodypedia; 45126; 66 antibodies from 17 providers.
DR   Ensembl; ENST00000411697.5; ENSP00000406721.1; ENSG00000223494.11.
DR   Ensembl; ENST00000425563.5; ENSP00000415752.1; ENSG00000230985.11.
DR   Ensembl; ENST00000428017.5; ENSP00000403749.1; ENSG00000137411.19.
DR   Ensembl; ENST00000431578.5; ENSP00000415560.1; ENSG00000236178.11.
DR   Ensembl; ENST00000446577.5; ENSP00000415729.1; ENSG00000234032.11.
DR   Ensembl; ENST00000452966.5; ENSP00000394190.1; ENSG00000206476.15.
DR   UCSC; uc063mxf.1; human.
DR   HGNC; HGNC:21642; VARS2.
DR   VEuPathDB; HostDB:ENSG00000137411; -.
DR   GeneTree; ENSGT00940000159890; -.
DR   HOGENOM; CLU_074007_0_0_1; -.
DR   OMA; RQWYIRN; -.
DR   OrthoDB; 629407at2759; -.
DR   ChiTaRS; VARS2; human.
DR   Proteomes; UP000005640; Chromosome 6.
DR   Bgee; ENSG00000137411; Expressed in right hemisphere of cerebellum and 96 other cell types or tissues.
DR   GO; GO:0005739; C:mitochondrion; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0004832; F:valine-tRNA ligase activity; IEA:InterPro.
DR   GO; GO:0006438; P:valyl-tRNA aminoacylation; IEA:InterPro.
DR   FunFam; 3.40.50.620:FF:000020; Valine--tRNA ligase, mitochondrial; 1.
DR   Gene3D; 3.40.50.620; HUPs; 1.
DR   InterPro; IPR001412; aa-tRNA-synth_I_CS.
DR   InterPro; IPR002300; aa-tRNA-synth_Ia.
DR   InterPro; IPR014729; Rossmann-like_a/b/a_fold.
DR   InterPro; IPR002303; Valyl-tRNA_ligase.
DR   PANTHER; PTHR11946:SF71; VALINE--TRNA LIGASE, MITOCHONDRIAL; 1.
DR   PANTHER; PTHR11946; VALYL-TRNA SYNTHETASES; 1.
DR   Pfam; PF00133; tRNA-synt_1; 1.
DR   SUPFAM; SSF52374; Nucleotidylyl transferase; 1.
DR   PROSITE; PS00178; AA_TRNA_LIGASE_I; 1.
PE   1: Evidence at protein level;
KW   Aminoacyl-tRNA synthetase {ECO:0000256|ARBA:ARBA00023146};
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW   Ligase {ECO:0000256|ARBA:ARBA00022598};
KW   Mitochondrion {ECO:0000256|ARBA:ARBA00023128};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Protein biosynthesis {ECO:0000256|ARBA:ARBA00022917};
KW   Proteomics identification {ECO:0007829|PeptideAtlas:B7ZCJ6,
KW   ECO:0007829|ProteomicsDB:B7ZCJ6};
KW   Reference proteome {ECO:0000313|Proteomes:UP000005640};
KW   Transit peptide {ECO:0000256|ARBA:ARBA00022946}.
FT   DOMAIN          113..295
FT                   /note="Aminoacyl-tRNA synthetase class Ia"
FT                   /evidence="ECO:0000259|Pfam:PF00133"
FT   REGION          25..53
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        42..53
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   NON_TER         326
FT                   /evidence="ECO:0000313|Ensembl:ENSP00000403749.1"
SQ   SEQUENCE   326 AA;  36879 MW;  DC6738B86381F55C CRC64;
     MPHLPLASFR PPFWGLRHSR GLPRFHSVST QSEPHGSPIS RRNREAKQKR LREKQATLEA
     EIAGESKSPA ESIKAWRPKE LVLYEIPTKP GEKKDVSGPL PPAYSPRYVE AAWYPWWVRE
     GFFKPEYQAR LPQATGETFS MCIPPPNVTG SLHIGHALTV AIQDALVRWH RMRGDQVLWV
     PGSDHAGIAT QAVVEKQLWK ERGVRRHELS REAFLREVWQ WKEAKGGEIC EQLRALGASL
     DWDRECFTMD VGSSVAVTEA FVRLYKAGLL YRNHQLVNWS CALRSAISDI EVENRPLPGH
     TQLRLPGCPT PVSFGLLFSV AFPVDG
//