ID A5DX19_LODEL Unreviewed; 1103 AA.
AC A5DX19;
DT 12-JUN-2007, integrated into UniProtKB/TrEMBL.
DT 12-JUN-2007, sequence version 1.
DT 27-MAR-2024, entry version 102.
DE RecName: Full=valine--tRNA ligase {ECO:0000256|ARBA:ARBA00013169};
DE EC=6.1.1.9 {ECO:0000256|ARBA:ARBA00013169};
DE AltName: Full=Valyl-tRNA synthetase {ECO:0000256|ARBA:ARBA00029936};
GN ORFNames=LELG_01906 {ECO:0000313|EMBL:EDK43727.1};
OS Lodderomyces elongisporus (strain ATCC 11503 / CBS 2605 / JCM 1781 / NBRC
OS 1676 / NRRL YB-4239) (Yeast) (Saccharomyces elongisporus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Debaryomycetaceae; Candida/Lodderomyces clade;
OC Lodderomyces.
OX NCBI_TaxID=379508 {ECO:0000313|EMBL:EDK43727.1, ECO:0000313|Proteomes:UP000001996};
RN [1] {ECO:0000313|EMBL:EDK43727.1, ECO:0000313|Proteomes:UP000001996}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 11503 / BCRC 21390 / CBS 2605 / JCM 1781 / NBRC 1676 /
RC NRRL YB-4239 {ECO:0000313|Proteomes:UP000001996};
RX PubMed=19465905; DOI=10.1038/nature08064;
RA Butler G., Rasmussen M.D., Lin M.F., Santos M.A., Sakthikumar S.,
RA Munro C.A., Rheinbay E., Grabherr M., Forche A., Reedy J.L., Agrafioti I.,
RA Arnaud M.B., Bates S., Brown A.J., Brunke S., Costanzo M.C.,
RA Fitzpatrick D.A., de Groot P.W., Harris D., Hoyer L.L., Hube B., Klis F.M.,
RA Kodira C., Lennard N., Logue M.E., Martin R., Neiman A.M., Nikolaou E.,
RA Quail M.A., Quinn J., Santos M.C., Schmitzberger F.F., Sherlock G.,
RA Shah P., Silverstein K.A., Skrzypek M.S., Soll D., Staggs R.,
RA Stansfield I., Stumpf M.P., Sudbery P.E., Srikantha T., Zeng Q., Berman J.,
RA Berriman M., Heitman J., Gow N.A., Lorenz M.C., Birren B.W., Kellis M.,
RA Cuomo C.A.;
RT "Evolution of pathogenicity and sexual reproduction in eight Candida
RT genomes.";
RL Nature 459:657-662(2009).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-valine + tRNA(Val) = AMP + diphosphate + L-valyl-
CC tRNA(Val); 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:ARBA00001624};
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; CH981525; EDK43727.1; -; Genomic_DNA.
DR RefSeq; XP_001527077.1; XM_001527027.1.
DR AlphaFoldDB; A5DX19; -.
DR STRING; 379508.A5DX19; -.
DR GeneID; 5234273; -.
DR KEGG; lel:LELG_01906; -.
DR VEuPathDB; FungiDB:LELG_01906; -.
DR eggNOG; KOG0432; Eukaryota.
DR HOGENOM; CLU_001493_0_1_1; -.
DR InParanoid; A5DX19; -.
DR OMA; LDTWMDS; -.
DR OrthoDB; 5473263at2759; -.
DR Proteomes; UP000001996; Unassembled WGS sequence.
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; cd00817; ValRS_core; 1.
DR Gene3D; 3.40.50.620; HUPs; 2.
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; 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; IPR009008; Val/Leu/Ile-tRNA-synth_edit.
DR InterPro; IPR002303; Valyl-tRNA_ligase.
DR NCBIfam; TIGR00422; valS; 1.
DR PANTHER; PTHR11946:SF109; VALINE--TRNA LIGASE; 1.
DR PANTHER; PTHR11946; VALYL-TRNA SYNTHETASES; 1.
DR Pfam; PF08264; Anticodon_1; 1.
DR Pfam; PF00133; tRNA-synt_1; 1.
DR PRINTS; PR00986; TRNASYNTHVAL.
DR SUPFAM; SSF47323; Anticodon-binding domain of a subclass of class I aminoacyl-tRNA synthetases; 1.
DR SUPFAM; SSF52374; Nucleotidylyl transferase; 1.
DR SUPFAM; SSF50677; ValRS/IleRS/LeuRS editing domain; 1.
DR PROSITE; PS00178; AA_TRNA_LIGASE_I; 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:UP000001996}.
FT DOMAIN 158..781
FT /note="Aminoacyl-tRNA synthetase class Ia"
FT /evidence="ECO:0000259|Pfam:PF00133"
FT DOMAIN 826..973
FT /note="Methionyl/Valyl/Leucyl/Isoleucyl-tRNA synthetase
FT anticodon-binding"
FT /evidence="ECO:0000259|Pfam:PF08264"
FT REGION 44..128
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 1074..1101
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 54..68
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 69..128
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1103 AA; 124844 MW; 87238E485AC51A60 CRC64;
MLLSKLLFST NLGIRRGVVP LAKNYLYPSL VLNLRRNMSD VTKPDETAQV APAAPTDASA
TNTQDGEAPR PKTAKELEKE RKKAEKLAKF NAKKAKQADS AKAKADEPKK PKKEKKKADA
TPAPEYIDKT VPGEKKVLAS LEDPAFKAYN PKNVESSWYS WWDKSGFFEP ELTEDGKIKS
EGVFSIPCPP PNVTGALHIG HALTVSIQDT LIRWNRMQGK TTLFIPGFDH AGIATQSVVE
KQIWAKEQKT RHDYGREKFV EKVWEWKEEY HSRIKNQFKK LGASYDWSRE RFTLNPDLSA
AVTEAFVRMH EDGTIYRSLR LVNWSVKLNT AISNLEVDNK NITGRTLLAV PGYDQKIEFG
TLTSFSYQVD GSDEKLTVAT TRPETIFGDT GVAVHPKDPR YKHLHGKYVL HPFLDRKLPI
VTDEEAVDME FGTGAVKITP AHDQNDYNVG KKNNLEFINI YTDDGLLNEN CGPEWQGMKR
FDARAKAIEQ LKAKGLFVDQ KDHEMVIPIC SRSGDVIEPL LKPQWYVNQQ QMAKDAIAAV
KNGEIKITPK SSEQEYFYWL ENIQDWCISR QLWWGHRCPV YFVNIEGEEH DRLDNKYWIS
GRSEEEALQK ANEKFAGKKF TLEQDEDVLD TWFSSGLWPI STLGWPNKTK DLELFSPMSM
LETGWDILFF WVTRMVLMSL KLTGKVPFKE VFCHSLVRDA QGRKMSKSLG NVIDPLDVVN
GISLQGLHDK LLTGNLDPRE LKKATEGQKI SYPNGIPECG TDALRFALCA YSTGGRDINL
DILRVEGYRK FCNKIYQATK FVLGRLGDDY VPPKSASLTG KETLVEKWIL DRLSTAAKNT
NEALEARNMG DSTNHIYNFW YDLCDVYIEN SKSLIQDGTP EQKKSAQDTL YTSIDGALRL
IHPYMPFITE EMWQRLPRRE GDDTTTISKA RYPQHNEEFD NPEAVQAYEL VLEITKGARS
LLSQYNILKN GQVFVESNNE GIYKIAAEQQ DSIVSLIKGV EKISVVKTSD EVPSGCALQA
IGPDCTVHVL VKGQIDLDAE IAKVDKKLNV AKDNKKKFDD AISKFTEKTN PSAIESAKQR
LEKVVAEIEG YEQTIAILEK LKL
//
