ID A0A0D9P9U9_METAN Unreviewed; 1075 AA.
AC A0A0D9P9U9;
DT 27-MAY-2015, integrated into UniProtKB/TrEMBL.
DT 27-MAY-2015, sequence version 1.
DT 27-MAR-2024, entry version 35.
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=H634G_01071 {ECO:0000313|EMBL:KJK82943.1};
OS Metarhizium anisopliae BRIP 53293.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Clavicipitaceae; Metarhizium.
OX NCBI_TaxID=1291518 {ECO:0000313|EMBL:KJK82943.1, ECO:0000313|Proteomes:UP000054544};
RN [1] {ECO:0000313|Proteomes:UP000054544}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BRIP 53293 {ECO:0000313|Proteomes:UP000054544};
RX PubMed=25102932; DOI=10.1186/1471-2164-15-660;
RA Pattemore J.A., Hane J.K., Williams A.H., Wilson B.A., Stodart B.J.,
RA Ash G.J.;
RT "The genome sequence of the biocontrol fungus Metarhizium anisopliae and
RT comparative genomics of Metarhizium species.";
RL BMC Genomics 15:660-660(2014).
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; KE384721; KJK82943.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0D9P9U9; -.
DR STRING; 1291518.A0A0D9P9U9; -.
DR Proteomes; UP000054544; 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; 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:UP000054544}.
FT DOMAIN 127..749
FT /note="Aminoacyl-tRNA synthetase class Ia"
FT /evidence="ECO:0000259|Pfam:PF00133"
FT DOMAIN 793..943
FT /note="Methionyl/Valyl/Leucyl/Isoleucyl-tRNA synthetase
FT anticodon-binding"
FT /evidence="ECO:0000259|Pfam:PF08264"
FT REGION 1..64
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 1003..1072
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 37..64
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1075 AA; 121453 MW; 5259807A79AF8434 CRC64;
MASNSARGGP VGANEGAETP QPAAQTTVPD IGAPRAADGA PKEKSEKDLE KERKKAEKAA
KIEAKKAKAA QMAANAANKE KKAKEKRIEE AVPPYVEDTP AGEKKRIRPF EDPNFKAYDP
IAVESAWYDW WEKEGFFKPE FTPDGKVKEA GSFVIVHPPP NVTGSLHMGH ALGDSLQDLM
IRWNRMNGKT TLWLPGCDHA GISTQSVVEK MLWRKEGKTR HDLGRTKFVE TVWEWKEEYH
KRINKALTHM GSSFDWSREA FTMDANLSAA VAETFVRLHE EGIIYRANRL VNWCTHLNTA
LSNLEVDNKE LTGRTLLDVP GYEKKVEFGV IVHFKYPIEG SNETVEVATT RIETMLGDTG
IAVHPNDARY KHLVGKNAMH PFIPDRKLPI VADEYVDMEF GTGAVKLTPA HDPNDFNLGQ
KHNLEFINIL TDDGLMNENA GPYKGQKRFD VRYSIQDALK EKGLYVDKKD NAMKVPLCEK
SKDVIEPRMK PQWWVRMKDL TGPALEVVRE GKIKIRPDTA ERSYFRWLED IQDWCISRQL
WWGHRCPVYF ANIEGVAKDT ADDKLWFSGR TREEAEKKAA AALPGKKFTL EQDEDVLDTW
FSSGLWPFST LGWPNKTHDL ETLYPTTVLE TGWDILFFWI ARMITLGLKM TGKIPFSEVY
CHSLVRDSEG RKMSKSLGNV IDPLDVISGI KLEDLHQKLY QGNLHPSEVE KATKYQKTAF
PDGIPQCGAD ALRFTMINAS TGGGDINLDV KVIHGYRKFC NKIFQATKYV LGSLPRDFAP
AADGVIRGKT LAERWILHKM NSAARDLNVA IADREFQKST NIIYKYWYAE LCDVYIENSK
AIIRDGTEEE RQSALQTLYT SLEWALTLIH PFMPYITEEM WQRMPRRPGD NTKSIMVSKY
PQYSPKLDDP ESESAYELVL AATKATRSLM SEYSLKENAE VFVQAYNEAA LKTCNAEVAS
IKSLSGKSVK TMHVIGPDAP RPAGCVAYPV STSVAVFLHV KGRVDMDAEI SKAQKKLEKA
KMSIQKQEKI LFDPGYIEKV SAAVREGDEQ RLADAKQEAI SFEETIKQFE QLKLE
//
