ID H0UUX4_CAVPO Unreviewed; 1213 AA.
AC H0UUX4;
DT 22-FEB-2012, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 2.
DT 27-MAR-2024, entry version 68.
DE RecName: Full=Valine--tRNA ligase {ECO:0000256|ARBA:ARBA00024407};
DE EC=6.1.1.9 {ECO:0000256|ARBA:ARBA00013169};
DE AltName: Full=Valyl-tRNA synthetase {ECO:0000256|ARBA:ARBA00029936};
GN Name=VARS1 {ECO:0000313|Ensembl:ENSCPOP00000000783.3};
OS Cavia porcellus (Guinea pig).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Hystricomorpha; Caviidae;
OC Cavia.
OX NCBI_TaxID=10141 {ECO:0000313|Ensembl:ENSCPOP00000000783.3, ECO:0000313|Proteomes:UP000005447};
RN [1] {ECO:0000313|Proteomes:UP000005447}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=2N {ECO:0000313|Proteomes:UP000005447};
RX PubMed=21993624; DOI=10.1038/nature10530;
RA Lindblad-Toh K., Garber M., Zuk O., Lin M.F., Parker B.J., Washietl S.,
RA Kheradpour P., Ernst J., Jordan G., Mauceli E., Ward L.D., Lowe C.B.,
RA Holloway A.K., Clamp M., Gnerre S., Alfoldi J., Beal K., Chang J.,
RA Clawson H., Cuff J., Di Palma F., Fitzgerald S., Flicek P., Guttman M.,
RA Hubisz M.J., Jaffe D.B., Jungreis I., Kent W.J., Kostka D., Lara M.,
RA Martins A.L., Massingham T., Moltke I., Raney B.J., Rasmussen M.D.,
RA Robinson J., Stark A., Vilella A.J., Wen J., Xie X., Zody M.C., Baldwin J.,
RA Bloom T., Chin C.W., Heiman D., Nicol R., Nusbaum C., Young S.,
RA Wilkinson J., Worley K.C., Kovar C.L., Muzny D.M., Gibbs R.A., Cree A.,
RA Dihn H.H., Fowler G., Jhangiani S., Joshi V., Lee S., Lewis L.R.,
RA Nazareth L.V., Okwuonu G., Santibanez J., Warren W.C., Mardis E.R.,
RA Weinstock G.M., Wilson R.K., Delehaunty K., Dooling D., Fronik C.,
RA Fulton L., Fulton B., Graves T., Minx P., Sodergren E., Birney E.,
RA Margulies E.H., Herrero J., Green E.D., Haussler D., Siepel A., Goldman N.,
RA Pollard K.S., Pedersen J.S., Lander E.S., Kellis M.;
RT "A high-resolution map of human evolutionary constraint using 29 mammals.";
RL Nature 478:476-482(2011).
RN [2] {ECO:0000313|Ensembl:ENSCPOP00000000783.3}
RP IDENTIFICATION.
RC STRAIN=2N {ECO:0000313|Ensembl:ENSCPOP00000000783.3};
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- SIMILARITY: Belongs to the class-I aminoacyl-tRNA synthetase family.
CC {ECO:0000256|ARBA:ARBA00005594, ECO:0000256|RuleBase:RU363035}.
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DR EMBL; AAKN02021589; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR AlphaFoldDB; H0UUX4; -.
DR Ensembl; ENSCPOT00000000876.3; ENSCPOP00000000783.3; ENSCPOG00000000870.4.
DR VEuPathDB; HostDB:ENSCPOG00000000870; -.
DR GeneTree; ENSGT00940000157775; -.
DR HOGENOM; CLU_001493_0_1_1; -.
DR TreeFam; TF300648; -.
DR Proteomes; UP000005447; Unassembled WGS sequence.
DR Bgee; ENSCPOG00000000870; Expressed in testis and 13 other cell types or tissues.
DR GO; GO:0002161; F:aminoacyl-tRNA editing activity; IEA:InterPro.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004832; F:valine-tRNA ligase activity; IEA:UniProtKB-EC.
DR GO; GO:0006438; P:valyl-tRNA aminoacylation; IEA:InterPro.
DR CDD; cd07962; Anticodon_Ia_Val; 1.
DR CDD; cd22249; UDM1_RNF168_RNF169-like; 1.
DR CDD; cd00817; ValRS_core; 1.
DR Gene3D; 1.20.1050.10; -; 1.
DR Gene3D; 3.40.50.620; HUPs; 2.
DR Gene3D; 1.10.287.380; Valyl-tRNA synthetase, C-terminal domain; 1.
DR Gene3D; 3.90.740.10; Valyl/Leucyl/Isoleucyl-tRNA synthetase, editing domain; 1.
DR HAMAP; MF_02004; Val_tRNA_synth_type1; 1.
DR InterPro; IPR001412; aa-tRNA-synth_I_CS.
DR InterPro; IPR002300; aa-tRNA-synth_Ia.
DR InterPro; IPR033705; Anticodon_Ia_Val.
DR InterPro; IPR010987; Glutathione-S-Trfase_C-like.
DR InterPro; IPR036282; Glutathione-S-Trfase_C_sf.
DR InterPro; IPR004046; GST_C.
DR InterPro; IPR013155; M/V/L/I-tRNA-synth_anticd-bd.
DR InterPro; IPR014729; Rossmann-like_a/b/a_fold.
DR InterPro; IPR009080; tRNAsynth_Ia_anticodon-bd.
DR InterPro; IPR037118; Val-tRNA_synth_C_sf.
DR InterPro; IPR009008; Val/Leu/Ile-tRNA-synth_edit.
DR InterPro; IPR002303; Valyl-tRNA_ligase.
DR NCBIfam; TIGR00422; valS; 1.
DR PANTHER; PTHR11946:SF115; VALINE--TRNA LIGASE; 1.
DR PANTHER; PTHR11946; VALYL-TRNA SYNTHETASES; 1.
DR Pfam; PF08264; Anticodon_1; 1.
DR Pfam; PF00043; GST_C; 1.
DR Pfam; PF00133; tRNA-synt_1; 2.
DR PRINTS; PR00986; TRNASYNTHVAL.
DR SUPFAM; SSF47323; Anticodon-binding domain of a subclass of class I aminoacyl-tRNA synthetases; 1.
DR SUPFAM; SSF47616; GST C-terminal domain-like; 1.
DR SUPFAM; SSF52374; Nucleotidylyl transferase; 1.
DR SUPFAM; SSF50677; ValRS/IleRS/LeuRS editing domain; 1.
DR PROSITE; PS00178; AA_TRNA_LIGASE_I; 1.
DR PROSITE; PS50405; GST_CTER; 1.
PE 3: Inferred from homology;
KW Aminoacyl-tRNA synthetase {ECO:0000256|ARBA:ARBA00023146,
KW ECO:0000256|RuleBase:RU363035};
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|RuleBase:RU363035};
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Ligase {ECO:0000256|ARBA:ARBA00022598, ECO:0000256|RuleBase:RU363035};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW ECO:0000256|RuleBase:RU363035};
KW Protein biosynthesis {ECO:0000256|ARBA:ARBA00022917,
KW ECO:0000256|RuleBase:RU363035};
KW Reference proteome {ECO:0000313|Proteomes:UP000005447}.
FT DOMAIN 89..224
FT /note="GST C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS50405"
FT COILED 1150..1212
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 1213 AA; 133543 MW; 79F9837CD5A91E2B CRC64;
MSILYVSPAP RCLPSLRALI AARYGEAGAG PGWGGAHPRI CLQPPPASRA PFPPPRLPAL
EQGPGGLWVW GAAAVAQLLW PAGLGGPGGS QEAVLVQQWV SYADTELIPA ACGATLPALG
LRSPAQDPQA ALGALGKALQ PLEEWLRLHT YLAGNAPSLA DLAAVTALLL PFRYVLDPSA
RQIWGSVTRW FSACVQQPEF RAVLGEVVLC SGTRSPCQQS EPPLSKRALC RAPQKRPKAE
KKEKRDLGVI TYDLPTPPGE KKDVSGPMPD SYSPQYVEAA WYPWWEQQGF FKPEYGRPSV
STPNPRGIFM MCIPPPNVTG SLHLGHALTN AIQDSLTRWH RMRGETTLWN PGCDHAGIAT
QVVVEKKLWR ERGLSRHQLG REAFLQEVWK WKEEHPGAKL SAAVTEAFVR LHEEGVIYRS
TRLVNWSCAL NSAISDIEVD KKELTGRTLL SVPGYKEKVE FGVLVSFAYK VQDSDSDEEV
VVATTRIETM LGDVAVAVHP EDARYQHLKG KRVTHPFVSR SLPIVFDHFV DMEFGTGAVK
ITPAHDQNDY EVGQRHGLEA ISIMDVHGAL VNVPPPFLGL PRFEARKAVL AALKERGLFR
GVRDNPMVVP LCNRSKDVVE PLLRPQWYVR CGEMAQAASA AVTRGDLRIL PEAHQRTWHS
WMDNIRDWCI SRQLWWGHRI PAYFITVNDS AVPPGEDPDS RYWVSGRSEA EALEKAAAEF
GVSPDKISLK QDEDVLDTWF SSGLFPFSIL GWPSQSEDLS VFYPGTLLET GHDILFFWVA
RMVMLGLKLT GKLPFREVYL HAIVRDAHGR KMSKSLGNVI DPLDVIHGVS LQGLHDQLLN
SNLDPSEVEK AKEGQKADFP AGIPECGTDA LRFGLCAYTS QGRDINLDVN RILGYRHFCN
KLWNATKFAL RGLGQGFVPS PTSTPAGRGS LVDRWILSRL AEAVRLSSEG FQAYDFPAVT
TAQYSFWLYE LCDVYLECLK PVLSGSDQEV AECARQTLYT CLDVGLRLLS PFMPFVTEEL
FQRLPRRSPQ APASLCVTPY PEPAECSWKD PEAEAALELA LSISRAVRSL RADYGLTRTR
PDCFLEVADE ATGAVASAVS GYVQALASAG VVAVLALGAP APQGCAVALA SDRCSIHLQL
QGLVDPAREL SKLQAKQAEA QRQAQRLQER RSASGYAVKV PLEVQEADEA KLRQTEAELK
KVDEAIALFQ KML
//
