ID A0A0C7N868_9SACH Unreviewed; 1102 AA.
AC A0A0C7N868;
DT 29-APR-2015, integrated into UniProtKB/TrEMBL.
DT 29-APR-2015, sequence version 1.
DT 27-MAR-2024, entry version 39.
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=LALA0_S03e06172g {ECO:0000313|EMBL:CEP61585.1};
OS Lachancea lanzarotensis.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Lachancea.
OX NCBI_TaxID=1245769 {ECO:0000313|EMBL:CEP61585.1, ECO:0000313|Proteomes:UP000054304};
RN [1] {ECO:0000313|EMBL:CEP61585.1, ECO:0000313|Proteomes:UP000054304}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 12615 {ECO:0000313|EMBL:CEP61585.1,
RC ECO:0000313|Proteomes:UP000054304};
RA Neuveglise Cecile;
RL Submitted (DEC-2014) to the EMBL/GenBank/DDBJ databases.
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; LN736362; CEP61585.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0C7N868; -.
DR STRING; 1245769.A0A0C7N868; -.
DR HOGENOM; CLU_001493_0_1_1; -.
DR OrthoDB; 5473263at2759; -.
DR Proteomes; UP000054304; 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; 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; 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: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:UP000054304}.
FT DOMAIN 155..778
FT /note="Aminoacyl-tRNA synthetase class Ia"
FT /evidence="ECO:0000259|Pfam:PF00133"
FT DOMAIN 823..969
FT /note="Methionyl/Valyl/Leucyl/Isoleucyl-tRNA synthetase
FT anticodon-binding"
FT /evidence="ECO:0000259|Pfam:PF08264"
FT REGION 94..116
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 1038..1100
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 1102 AA; 124919 MW; 95C55B215A291687 CRC64;
MRRSLIQVSR QCFSFPARTV YTGFTLSARD TPERRLHSSK FRTMSSDQTL PLVDPKTGEI
IINPLKEDGS EKNAKEIEKE RKKAEKLLKF AAKQAKKSEA ASKQSSAPKK EKKKKEVEVI
PEFVDKTVAG DKKILVSLDD PALKAYNPVN VESSWYDWWV KSGFFEPEFT KDGQIKPEGV
FSIPAPPPNV TGALHIGHGL TIAIQDSLIR YNRMKGKTVL FLPGFDHAGI ATQSVVEKQV
WAKEQKTRHD YGREAFVDKI WEWKEEYHKK IKNQINKLGS SYDWSREAFT LSPQLSKSVT
EAFVKLHEEG VIYRASRLVN WSVKLNTAIS NLEVENKDIK AKTMLSVPGY DEKIEFGVLT
SFAYPVVGSD EKLIVATTRP ETIFGDTGVA VHPEDPRYKH LHGKFVQHPF VDREIPIVCD
NEAVDMAFGT GAVKITPAHD QNDYNTGKRH DLEFINILTD SGLLNDECGP EWAGMKRFDA
RSKVIEALKE KGLYVGQEGN EMTIPTCSRS GDVIEPLLKP QWWVSQGDMA KEAIKAVKDG
RITITPKSSE AEYFHWLENI QDWCISRQLW WGHRCPVYFV EVEGEDHDGL DGEYWVSGRT
AEEAQEKASK KFPNVKFTLK QDEDVLDTWF SSGLWPFSTL GWPDQTADLS RFYPFSMLET
GWDILFFWVS RMILLGLKLT GEIPFNEVFC HSLVRDAQGR KMSKSLGNVI DPLDVVTGIK
LEDLHAKLLA GNLDPREIEK AKNGQRESYP NGIPQCGTDA LRFALCAYTT GGRDINLDIM
RVEGYRKFCN KIYQATKFAL MRLGDDYQPP AQEKLSGQES LVEKWILNKM THYARSVNEA
LDKRDFLTST SGIYEFWYLI CDVYIENSKY LITEGSEVEQ KSAKDTLYIL IDNALKLIHP
FMPFISEEMW QRLPKRSSET SPTIVKASYP VYRKDYDNEK AGKEYELILD AIKEARSLLA
QYGILKNGKV FIESSNSEFL ETALQQKDSI VSLIKAIDEV NVVKASSEIP EGAVLQAVTP
EINVHVLVKG HVDIDAEILK TQSKLEKAQK TKENIDKTIN SPDYEAKANE QAKATNNTRL
QNTTAEIEGL EATIANLERL KL
//
