ID SYV2_HUMAN STANDARD; PRT; 1264 AA. AC P26640; Q96E77; Q9UQM2; DT 01-AUG-1992 (Rel. 23, Created) DT 16-OCT-2001 (Rel. 40, Last sequence update) DT 01-MAY-2005 (Rel. 47, Last annotation update) DE Valyl-tRNA synthetase 2 (EC 6.1.1.9) (Valine--tRNA ligase 2) (ValRS 2) DE (G7a). GN Name=VARS2; Synonyms=G7A; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Primates; Catarrhini; Hominidae; OC Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE. RX MEDLINE=91378943; PubMed=1898367; RA Hsieh H.-L., Campbell R.D.; RT "Evidence that gene G7a in the human major histocompatibility complex RT encodes valyl-tRNA synthetase."; RL Biochem. J. 278:809-816(1991). RN [2] RP ERRATUM. RA Hsieh S.-L., Campbell R.D.; RL Biochem. J. 281:879-879(1992). RN [3] RP NUCLEOTIDE SEQUENCE. RA Rowen L., Madan A., Qin S., Shaffer T., James R., Ratcliffe A., RA Abbasi N., Dickhoff R., Loretz C., Madan A., Dors M., Young J., RA Lasky S., Hood L.; RT "Sequence of the human major histocompatibility complex class III RT region."; RL Submitted (OCT-1999) to the EMBL/GenBank/DDBJ databases. RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Shiina S., Tamiya G., Oka A., Inoko H.; RT "Homo sapiens 2,229,817bp genomic DNA of 6p21.3 HLA class I region."; RL Submitted (SEP-1999) to the EMBL/GenBank/DDBJ databases. RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=Muscle; RX MEDLINE=22388257; PubMed=12477932; DOI=10.1073/pnas.242603899; RA Strausberg R.L., Feingold E.A., Grouse L.H., Derge J.G., RA Klausner R.D., Collins F.S., Wagner L., Shenmen C.M., Schuler G.D., RA Altschul S.F., Zeeberg B., Buetow K.H., Schaefer C.F., Bhat N.K., RA Hopkins R.F., Jordan H., Moore T., Max S.I., Wang J., Hsieh F., RA Diatchenko L., Marusina K., Farmer A.A., Rubin G.M., Hong L., RA Stapleton M., Soares M.B., Bonaldo M.F., Casavant T.L., Scheetz T.E., RA Brownstein M.J., Usdin T.B., Toshiyuki S., Carninci P., Prange C., RA Raha S.S., Loquellano N.A., Peters G.J., Abramson R.D., Mullahy S.J., RA Bosak S.A., McEwan P.J., McKernan K.J., Malek J.A., Gunaratne P.H., RA Richards S., Worley K.C., Hale S., Garcia A.M., Gay L.J., Hulyk S.W., RA Villalon D.K., Muzny D.M., Sodergren E.J., Lu X., Gibbs R.A., RA Fahey J., Helton E., Ketteman M., Madan A., Rodrigues S., Sanchez A., RA Whiting M., Madan A., Young A.C., Shevchenko Y., Bouffard G.G., RA Blakesley R.W., Touchman J.W., Green E.D., Dickson M.C., RA Rodriguez A.C., Grimwood J., Schmutz J., Myers R.M., RA Butterfield Y.S.N., Krzywinski M.I., Skalska U., Smailus D.E., RA Schnerch A., Schein J.E., Jones S.J.M., Marra M.A.; RT "Generation and initial analysis of more than 15,000 full-length human RT and mouse cDNA sequences."; RL Proc. Natl. Acad. Sci. U.S.A. 99:16899-16903(2002). RN [6] RP NUCLEOTIDE SEQUENCE OF 201-1263. RX MEDLINE=93154582; PubMed=8428657; DOI=10.1016/0378-1119(93)90122-J; RA Vilalta A., Donovan D., Wood L., Vogeli G., Yang D.C.H.; RT "Cloning, sequencing and expression of a cDNA encoding mammalian RT valyl-tRNA synthetase."; RL Gene 123:181-186(1993). CC -!- CATALYTIC ACTIVITY: ATP + L-valine + tRNA(Val) = AMP + diphosphate CC + L-valyl-tRNA(Val). CC -!- ENZYME REGULATION: Can be regulated by protein kinase C-dependent CC phosphorylation. CC -!- SUBUNIT: Forms high-molecular-mass aggregates with elongation CC factor 1. CC -!- SIMILARITY: Belongs to the class-I aminoacyl-tRNA synthetase CC family. CC -!- SIMILARITY: Contains 1 GST-like domain. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; X59303; CAA41990.1; -. DR EMBL; AF134726; AAD21819.1; -. DR EMBL; AP000503; BAB63303.1; -. DR EMBL; BC012808; AAH12808.1; -. DR EMBL; M98326; AAA81332.1; -. DR PIR; S17675; S17675. DR HSSP; P96142; 1IVS. DR IntAct; P26640; -. DR Ensembl; ENSG00000096171; Homo sapiens. DR Genew; HGNC:12651; VARS2. DR H-InvDB; HIX0005731; -. DR MIM; 604137; -. DR GO; GO:0005622; C:intracellular; NAS. DR GO; GO:0004832; F:valine-tRNA ligase activity; IDA. DR GO; GO:0006414; P:translational elongation; NAS. DR InterPro; IPR010987; GST_C_like. DR InterPro; IPR004046; GST_Cterm. DR InterPro; IPR004045; GST_Nterm. DR InterPro; IPR002300; tRNA-synt_1a. DR InterPro; IPR001412; tRNA-synt_I. DR InterPro; IPR002303; tRNA-synt_val. DR InterPro; IPR010978; tRNA_binding_arm. DR InterPro; IPR009080; tRNAsyn_1a_bind. DR InterPro; IPR009008; ValRS_IleRS_edit. DR Pfam; PF00043; GST_C; 1. DR Pfam; PF02798; GST_N; 1. DR Pfam; PF00133; tRNA-synt_1; 1. DR PRINTS; PR00986; TRNASYNTHVAL. DR TIGRFAMs; TIGR00422; valS; 1. DR PROSITE; PS00178; AA_TRNA_LIGASE_I; 1. KW Aminoacyl-tRNA synthetase; ATP-binding; Ligase; Phosphorylation; KW Protein biosynthesis. FT DOMAIN 1 198 GST. FT SITE 344 354 "HIGH" region. FT SITE 862 866 "KMSKS" region. FT BINDING 865 865 ATP (By similarity). FT CONFLICT 51 51 P -> S (in Ref. 1 and 5). FT CONFLICT 331 331 A -> G (in Ref. 6). FT CONFLICT 590 590 V -> G (in Ref. 1). FT CONFLICT 620 640 ALINVPPPFLGLPRFEARKAV -> GPHQCASAFPGPAQVL FT RPGKRC (in Ref. 1). FT CONFLICT 792 792 S -> F (in Ref. 1). FT CONFLICT 1064 1064 M -> I (in Ref. 6). FT CONFLICT 1169 1169 Missing (in Ref. 6). SQ SEQUENCE 1264 AA; 140476 MW; 95CCDDBB3AB148AD CRC64; MSTLYVSPHP DAFPSLRALI AARYGEAGEG PGWGGAHPRI CLQPPPTSRT PFPPPRLPAL EQGPGGLWVW GATAVAQLLW PAGLGGPGGS RAAVLVQQWV SYADTELIPA ACGATLPALG LRSSAQDPQA VLGALGRALS PLEEWLRLHT YLAGEAPTLA DLAAVTALLL PFRYVLDPPA RRIWNNVTRW FVTCVRQPEF RAVLGEVVLY SGARPLSHQP GPEAPALPKT AAQLKKEAKK REKLEKFQQK QKIQQQQPPP GEKKPKPEKR EKRDPGVITY DLPTPPGEKK DVSGPMPDSY SPRYVEAAWY PWWEQQGFFK PEYGRPNVSA ANPRGVFMMC IPPPNVTGSL HLGHALTNAI QDSLTRWHRM RGETTLWNPG CDHAGIATQV VVEKKLWREQ GLSRHQLGRE AFLQEVWKWK EEKGDRIYHQ LKKLGSSLDW DRACFTMDPK LSAAVTEAFV RLHEEGIIYR STRLVNWSCT LNSAISDIEV DKKELTGRTL LSVPGYKEKV EFGVLVSFAY KVQGSDSDEE VVVATTRIET MLGDVAVAVH PKDTRYQHLK GKNVIHPFLS RSLPIVFDEF VDMDFGTGAV KITPAHDQND YEVGQRHGLE AISIMDSRGA LINVPPPFLG LPRFEARKAV LVALKERGLF RGIEDNPMVV PLCNRSKDVV EPLLRPQWYV RCGEMAQAAS AAVTRGDLRI LPEAHQRTWH AWMDNIREWC ISRQLWWGHR IPAYFVTVSD PAVPPGEDPD GRYWVSGRNE AEAREKAAKE FGVSPDKISL QQDEDVLDTW FSSGLFPLSI LGWPNQSEDL SVFYPGTLLE TGHDILFFWV ARMVMLGLKL TGRLPFREVY LHAIVRDAHG RKMSKSLGNV IDPLDVIYGI SLQGLHNQLL NSNLDPSEVE KAKEGQKADF PAGIPECGTD ALRFGLCAYM SQGRDINLDV NRILGYRHFC NKLWNATKFA LRGLGKGFVP SPTSQPGGHE SLVDRWIRSR LTEAVRLSNQ GFQAYDFPAV TTAQYSFWLY ELCDVYLECL KPVLNGVDQV AAECARQTLY TCLDVGLRLL SPFMPFVTEE LFQRLPRRMP QAPPSLCVTP YPEPSECSWK DPEAEAALEL ALSITRAVRS LRADYNLTRI RPDCFLEVAD EATGALASAV SGYVQALASA GVVAVLALGA PAPQGCAVAL ASDRCSIHLQ LQGLVDPARE LGKLQAKRVE AQRQAQRLRE RRAASGYPVK VPLEVQEADE AKLQQTEAEL RKVDEAIALF QKML //