ID A0A1V6QHF2_9EURO Unreviewed; 1067 AA.
AC A0A1V6QHF2;
DT 07-JUN-2017, integrated into UniProtKB/TrEMBL.
DT 07-JUN-2017, sequence version 1.
DT 27-MAR-2024, entry version 30.
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=PENANT_c003G03871 {ECO:0000313|EMBL:OQD88643.1};
OS Penicillium antarcticum.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Penicillium.
OX NCBI_TaxID=416450 {ECO:0000313|EMBL:OQD88643.1, ECO:0000313|Proteomes:UP000191672};
RN [1] {ECO:0000313|Proteomes:UP000191672}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=IBT 31811 {ECO:0000313|Proteomes:UP000191672};
RX PubMed=28368369; DOI=10.1038/nmicrobiol.2017.44;
RA Nielsen J.C., Grijseels S., Prigent S., Ji B., Dainat J., Nielsen K.F.,
RA Frisvad J.C., Workman M., Nielsen J.;
RT "Global analysis of biosynthetic gene clusters reveals vast potential of
RT secondary metabolite production in Penicillium species.";
RL Nat. Microbiol. 2:17044-17044(2017).
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:OQD88643.1}.
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DR EMBL; MDYN01000003; OQD88643.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1V6QHF2; -.
DR STRING; 416450.A0A1V6QHF2; -.
DR OrthoDB; 5473263at2759; -.
DR Proteomes; UP000191672; 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:UP000191672}.
FT DOMAIN 118..739
FT /note="Aminoacyl-tRNA synthetase class Ia"
FT /evidence="ECO:0000259|Pfam:PF00133"
FT DOMAIN 784..932
FT /note="Methionyl/Valyl/Leucyl/Isoleucyl-tRNA synthetase
FT anticodon-binding"
FT /evidence="ECO:0000259|Pfam:PF08264"
FT REGION 1..107
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 992..1064
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 51..82
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 89..107
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1067 AA; 120465 MW; 2D3F3DFDA0E44C37 CRC64;
MAQNSASQNP TGEPTAPLTS PPPQVDEQTR ANIADAAAKD PQGQHQGGDA APKVKTEKEL
EKERKKAEKD KKFKEKQAAK AAKAAATKDA APKAEKKAKP EKEKTTDAYD PQVIEAGRLD
WWEERDLFKP EFGPDGKVKP EGSFVIPIPP PNVTGSLHMG HALTNALQDT MIRWQRMKGK
TTLWLPGMDH AGISTQSVVE KMLWKKEKKT RHDIGREAMV GLIWDWKDEY HKNIKNALRR
VGGSFDWSRE AFTMDPNLSA AVTETFVRLH EEGIIYRANR LVNWCVHLNT SLSNLEVENK
EIEGRTLLDV PGYDKKVEFG VLTHFCYEID GGKERIEIAT TRPETMMGDT GIAVHPDDKR
YQHLIGKNAR HPFLDRLLPI VADKEVEPEF GTGAVKITPA HDFNDFNRGK AHNLEFISVM
NDDGTFNKNA GPFAGMKRFD ARYKVIDALK ERGLYVKWEH NPMKVPRCSK SNDVIEPILK
PQWWMKMESL AKPAIEAVEN GDIIIRPESA EKSYFRWMRN LNDWCLSRQL WWGHQAPAYF
VKIEGEDGDD SDGNLWVTGR TEEDARKKAE EKFPGKKFSL VRDPDVLDTW FSSGLWPFST
LGWPRQTHDF ENLYPTSVLE TGWDILFFWV ARMIMLGIKM TGKIPFKEVY CHSLIRDSEG
RKMSKSLGNV IDPLDVMEGI ELQTLHDKLQ LGNIADKEIA TATKYQKKAF PKGIPECGAD
ALRFALVSYT TGGGDIAFDI QVIHAYRKFC NKIYQATKFV LGKLGDDFKP QAAVKKTGHE
SLSERWILHK FNAAAKEINE ALEQREFSQT AQISYQYWYA QLCDVFLENS KYLLSTDASP
ETQESAKQTL YTALDGALTM IHPIMPFVTE HLWQRLPRRA GDETISIMKA KYPEYIAEFD
DPAAATAYEL ILNSSKAIRS ILAQYDVKTQ GDIIIQTYDA TSEKTISEQM TTIKSLGGKT
LGELSHLGPD NKNPPSGCVV APVGAEAAVY LRVSKEVALE QEEKAKAALE KALATVRKSQ
GIMNGPGWKD KVKAEVREAE EKRLRDADSD AARLEEQIKE FEKLRLE
//
