ID C4R5G8_KOMPG Unreviewed; 1072 AA.
AC C4R5G8;
DT 07-JUL-2009, integrated into UniProtKB/TrEMBL.
DT 07-JUL-2009, sequence version 1.
DT 27-MAR-2024, entry version 97.
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 OrderedLocusNames=PAS_chr3_0754 {ECO:0000313|EMBL:CAY70804.1};
OS Komagataella phaffii (strain GS115 / ATCC 20864) (Yeast) (Pichia pastoris).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Phaffomycetaceae; Komagataella.
OX NCBI_TaxID=644223 {ECO:0000313|EMBL:CAY70804.1, ECO:0000313|Proteomes:UP000000314};
RN [1] {ECO:0000313|EMBL:CAY70804.1, ECO:0000313|Proteomes:UP000000314}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=GS115 / ATCC 20864 {ECO:0000313|Proteomes:UP000000314};
RX PubMed=19465926; DOI=10.1038/nbt.1544;
RA De Schutter K., Lin Y.C., Tiels P., Van Hecke A., Glinka S.,
RA Weber-Lehmann J., Rouze P., Van de Peer Y., Callewaert N.;
RT "Genome sequence of the recombinant protein production host Pichia
RT pastoris.";
RL Nat. Biotechnol. 27:561-566(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; FN392321; CAY70804.1; -; Genomic_DNA.
DR RefSeq; XP_002492983.1; XM_002492938.1.
DR AlphaFoldDB; C4R5G8; -.
DR SMR; C4R5G8; -.
DR STRING; 644223.C4R5G8; -.
DR EnsemblFungi; CAY70804; CAY70804; PAS_chr3_0754.
DR GeneID; 8200447; -.
DR KEGG; ppa:PAS_chr3_0754; -.
DR eggNOG; KOG0432; Eukaryota.
DR HOGENOM; CLU_001493_0_1_1; -.
DR InParanoid; C4R5G8; -.
DR OMA; LDTWMDS; -.
DR OrthoDB; 5473263at2759; -.
DR Proteomes; UP000000314; Chromosome 3.
DR GO; GO:0005737; C:cytoplasm; 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: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; IPR010978; tRNA-bd_arm.
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; SSF46589; tRNA-binding arm; 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:UP000000314}.
FT DOMAIN 124..746
FT /note="Aminoacyl-tRNA synthetase class Ia"
FT /evidence="ECO:0000259|Pfam:PF00133"
FT DOMAIN 791..940
FT /note="Methionyl/Valyl/Leucyl/Isoleucyl-tRNA synthetase
FT anticodon-binding"
FT /evidence="ECO:0000259|Pfam:PF08264"
FT REGION 24..52
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 1008..1070
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 36..52
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1072 AA; 121673 MW; D5677DEE4D988C03 CRC64;
MRILPRGLQK YKSLVTQIHS FRSTSMSTVP ESNIPPKVKT EKELEKERKK AEKLAKFEAK
KAKQEALKKN QLANAEKKTK KEKKPVEEVS VYVDQTPKGE KKILASLEDP AFKAYNPKNV
ESSWYEWWVK EGLFEPEFGP DGKPKPAGVF SIPAPPPNIT GALHIGHALT IALQDTLIRF
YRMKGKTTLY LPGFDHAGIA TQSVVEKSLW AQEGKTRHDL GREKFIEKVW DWKDVYQNRI
RSQFEKLGAS YDFSREAFTL NPMLSKAVTE AFVRLHEDGT IYRAQRLVNW SVKLNTAISN
IEVENKIIPA KTAISVPGYE NKIEFGVLHS FAYPVVGSDE KLIVATTRPE TVFGDTGVAV
HPDDPRYKHL HGKFVQHPLL DRQIPIVTDA EAVDMEFGTG AVKITPGHDN NDYNTGKRQK
LEFINIFTDD GYLNENCGKY KGLKRFDARQ IVIDDLKALN LYEGEEPNEM TIPTCSRSGD
IIEPYLKPQW WVAQDKMAAE AIKAVKDGRI TITPKVSESE YFRWLENIQD WCISRQLWWG
HRCPVYFVNI EGEVNDENDG QYWVSGRSLE EAQEKASAKF AGKIFTLEQD EDVLDTWFSS
GLWPFSTLGW PDNTPDMKQF YPFSMLETGW DILFFWVTRM ILLGLKLTGD VPFKEVFCHS
LVRDAQGRKM SKSLGNVVDP LDVINGISLE DLHAKLLGGN LDPREVEKAK KGQKESYPSG
IPECGTDALR FALCAYTTGG RDINLDILRV EGYRKFCNKI YQATKFVLMR LGDDYKPPAT
GDLTGKESLV ERWILHKLSK ASKVVNESIE KRDFFEATNA IYQFWLYELC DVYIENSKYL
ITEGTADQKK SAQDTLFTCI DAALKLIHPF MPFLTEEMWQ RLPRREAEKS IISISKAPYP
EYNPSYDDIS SESNYEQILE ITRAARSLFA QYGITKEGKL YIESADAAAY KLASEEKHSI
VSLIKPVNDL IVIDSPEKVP EGCALQSVTP KINAHILVKG QVDLDAEILK TQNKVSKVEK
SLQALEKTLA SSNYASKASK EIQEQDQTKK QNFISELEGL NATIANLQQL KL
//
