ID A0A2P7YYL6_9ASCO Unreviewed; 1053 AA.
AC A0A2P7YYL6;
DT 23-MAY-2018, integrated into UniProtKB/TrEMBL.
DT 23-MAY-2018, sequence version 1.
DT 27-MAR-2024, entry version 20.
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=C7M61_000723 {ECO:0000313|EMBL:PSK41052.1};
OS [Candida] pseudohaemulonii.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Metschnikowiaceae; Metschnikowiaceae incertae sedis;
OC Candida/Metschnikowiaceae.
OX NCBI_TaxID=418784 {ECO:0000313|EMBL:PSK41052.1, ECO:0000313|Proteomes:UP000241107};
RN [1] {ECO:0000313|EMBL:PSK41052.1, ECO:0000313|Proteomes:UP000241107}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=B12108 {ECO:0000313|EMBL:PSK41052.1,
RC ECO:0000313|Proteomes:UP000241107};
RA Munoz J.F., Gade L.G., Chow N.A., Litvintseva A.P., Loparev V.N.,
RA Cuomo C.A.;
RT "Candida pseudohaemulonii genome assembly and annotation.";
RL Submitted (MAR-2018) 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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:PSK41052.1}.
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DR EMBL; PYFQ01000001; PSK41052.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2P7YYL6; -.
DR STRING; 418784.A0A2P7YYL6; -.
DR EnsemblFungi; C7M61_000723_t1; PSK41052.1; C7M61_000723.
DR VEuPathDB; FungiDB:C7M61_000723; -.
DR OrthoDB; 5473263at2759; -.
DR Proteomes; UP000241107; Unassembled WGS sequence.
DR GO; GO:0005739; C:mitochondrion; IEA:EnsemblFungi.
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:EnsemblFungi.
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:UP000241107}.
FT DOMAIN 110..731
FT /note="Aminoacyl-tRNA synthetase class Ia"
FT /evidence="ECO:0000259|Pfam:PF00133"
FT DOMAIN 776..925
FT /note="Methionyl/Valyl/Leucyl/Isoleucyl-tRNA synthetase
FT anticodon-binding"
FT /evidence="ECO:0000259|Pfam:PF08264"
FT REGION 1..83
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 1024..1051
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 1..17
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 19..83
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1053 AA; 120013 MW; C9C182D0297621C9 CRC64;
MSEEDKVNAS SAQAQAPAAE ETKKEKTPKQ LENERKKAEK MAKFLAKKKK QEEDAKNKKP
AEKKPKKEKK VAEPVPEWKD ETKPGEKKIL ASLDDAAFKA YNPKNVESSW YAWWEKQGYF
EPELDEGKIK KEGQFTIPAP PPNVTGALHI GHALTIAIQD TLIRYNRMKG KTTLFLPGFD
HAGISTQSVV EKQVWKNEKK TRHDYGREKF VDKVWEWKEE YHARIKDQVK RLGASYDWTR
EAFTLNPDLS AAVVEAFVRL HEDGTIYRAS RLVNWSTKLN TAISNLEVEN KNISGRTLLS
VPNYDEKIEF GVLTSYSYPV VDSDEKITVA TTRPETLFGD TGVAVHPEDP RYKHLHGKFV
QHPFLDRKIP IVTDSEAVDM TFGTGAVKIT PAHDQNDYNT GKRQNLEFIN ILTDDGYLNE
NCGEWKGMKR FDARAKVIEE LKKLDLYVDQ KDNEMTIPTC SRSGDVIEPL LKPQWWVKQD
DMAKEAIKAV KSGEITITPQ SSEKEYFQWL ENIQDWCISR QLWWGHRCPV YFVNIEGKEG
DRLDNNYWVA GRSYEEALEK AEKKFPGVKF TLEQDEDVLD TWFSSGLWPI STLGWPNQSE
DLKLFAPMSM LETGWDILFF WVSRMILLCL KLTGKVPFKE VFCHSLVRDA QGRKMSKSLG
NVVDPLDVIS GISLADLHEK LKVGNLDARE IEKASAGQKQ SYPNGIPECG TDALRFALCA
YTTGGRDINL DILRVEGYRK FCNKMYQATK FVLGRLGADY KPPATQKRTG NESLVEKWIL
HRLTTATQSF TEHIEKREFS ETTSAVYNFW YDLCDVYIEN SKHLIQDGTA EQKKSAQDTL
YTCIDQGLKM IHPFMPYVTE EMWQRLPRRS GDETPSITIA QFPEYDASFD DKEAHDAYEL
VLAITKGARS LLSQYNILKN GQVYVETSDE NVRKIAKDQD HSMVSLIKGV EKIEVLEAGQ
PVPSGCALNG VNASTNVHVL VKGQIDLDSE IAKVTKKLSN VRELDGKLKD SIGKFTDKTK
PEAKEAAYKR QENFKAEIEG YEQTIAILEK LKL
//