ID A0A3E2HF25_SCYLI Unreviewed; 1075 AA.
AC A0A3E2HF25;
DT 16-JAN-2019, integrated into UniProtKB/TrEMBL.
DT 16-JAN-2019, sequence version 1.
DT 27-MAR-2024, entry version 27.
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};
DE Flags: Fragment;
GN ORFNames=B7463_g4286 {ECO:0000313|EMBL:RFU32028.1};
OS Scytalidium lignicola (Hyphomycete).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC Leotiomycetes incertae sedis; Scytalidium.
OX NCBI_TaxID=5539 {ECO:0000313|EMBL:RFU32028.1, ECO:0000313|Proteomes:UP000258309};
RN [1] {ECO:0000313|EMBL:RFU32028.1, ECO:0000313|Proteomes:UP000258309}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 105466 {ECO:0000313|EMBL:RFU32028.1,
RC ECO:0000313|Proteomes:UP000258309};
RA Buettner E., Gebauer A.M., Hofrichter M., Liers C., Kellner H.;
RT "Draft genome sequence of Scytalidium lignicola DSM 105466, a ubiquitous
RT saprotrophic fungus.";
RL Submitted (MAY-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:RFU32028.1}.
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DR EMBL; NCSJ02000063; RFU32028.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A3E2HF25; -.
DR STRING; 5539.A0A3E2HF25; -.
DR OMA; RQWYIRN; -.
DR Proteomes; UP000258309; 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; 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; 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 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:UP000258309}.
FT DOMAIN 127..749
FT /note="Aminoacyl-tRNA synthetase class Ia"
FT /evidence="ECO:0000259|Pfam:PF00133"
FT DOMAIN 794..938
FT /note="Methionyl/Valyl/Leucyl/Isoleucyl-tRNA synthetase
FT anticodon-binding"
FT /evidence="ECO:0000259|Pfam:PF08264"
FT REGION 1..100
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 32..60
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 75..92
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:RFU32028.1"
FT NON_TER 1075
FT /evidence="ECO:0000313|EMBL:RFU32028.1"
SQ SEQUENCE 1075 AA; 121500 MW; 5D9C297C850D3770 CRC64;
MASHSASAAL TGEKIDLPTG QDANKIVTAG AGDGEKKVKS EKELERERKK AEKQAKFEQK
KAKVANAATS AAPSKNKEKK AKAEKKAEEG ALPPYVEDTP PGEKKILKSF DDPQYKAYNP
LAVESAWYAW WEKEGFFKPE FTTEGNVKPE GKFVIVEPPP NVTGNLHMGH ALPSALQDLL
IRWNRMHGKT TLLLPGCDHA GISTQSVVEN MLWRREQKTR HDLGRPKFVE RVWDWKDEYH
QKINSVLRKM GGSFDWTREA FTMDKNFTAA VTETFVTLHE QGIIYRANRL VNWCTKLNTA
LSNLEVTNKE LAGRTLLDVP GYNKKVEFGV IIHFQYPIEG SDEKIEVATT RIETMLGDTG
IAVHPDDERY KHLVGKNAVH PFIKGRLLPI VADDYVEKDF GSGAVKITPA HDHNDFALGQ
RHNLKFINIL TDDGKMNENT GPYQGNKRFD VRYTIQDDLK KAGLYVDKKD NPMTVPLCEK
SKDVIEPLLK PQWWMRMREM ADDAIRVVKN GEIKIRPETA EKSYLRWMEN INDWCLSRQL
WWGHQAPMYF AVIDGEQNDD SDGSLWFAGR TQEEAEIKAK KALAGKTFTL KRDEDVLDTW
FSSGLWPFAT LGWPNKTHDL ETLYPTSVLE TGWDILFFWV ARMIMLGLKM TGKVPFTEVY
CHSLIRDSDG RKMSKSLGNV IDPQDVIQGI ALEELHKKLL IGNLNPLEVE KATKYQKTAF
PDGIPQCGTD ALRFSLVAYT TGGGDIAFDV KVIHGYRKFC NKIYQATKYV LGKLDADFVP
RKSSEITGKE SLAEQWILHK LTAAARDVNQ ALDDREFMRS TSIIYTYCYE LFDVYIENSK
SILQDGTAEE KRSALDTLYT AIEGALTMLH PFMPFLTEEL WQRLPRRAED KTPSIVVATY
PKFDENMYNT AAEAAYDLVL GVSKGIRSLM AEYSLKDQGN VFIQTYNSAA HETVTSQMQF
IKSLSGKGLT SISVLSSSDP RPTGCVLFSV SSAAAVFLHV KGRVDIDAEI QKATKKLEKT
RAGIDKQRKI LEDPGYKEKV SPELQEVEKI KLGDLETEQN GFEEVIKQFE ALKSE
//
