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Database: UniProt
Entry: A0A2P7YYL6_9ASCO
LinkDB: A0A2P7YYL6_9ASCO
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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
//
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