ID A0A2V1CRS5_9HELO Unreviewed; 1100 AA.
AC A0A2V1CRS5;
DT 12-SEP-2018, integrated into UniProtKB/TrEMBL.
DT 12-SEP-2018, sequence version 1.
DT 27-MAR-2024, entry version 21.
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=DL98DRAFT_196239 {ECO:0000313|EMBL:PVH88311.1};
OS Cadophora sp. DSE1049.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC Helotiales; Helotiales incertae sedis; Cadophora.
OX NCBI_TaxID=1485229 {ECO:0000313|EMBL:PVH88311.1, ECO:0000313|Proteomes:UP000244409};
RN [1] {ECO:0000313|EMBL:PVH88311.1, ECO:0000313|Proteomes:UP000244409}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSE1049 {ECO:0000313|EMBL:PVH88311.1,
RC ECO:0000313|Proteomes:UP000244409};
RX PubMed=29679020; DOI=10.1038/s41598-018-24686-4;
RA Knapp D.G., Nemeth J.B., Barry K., Hainaut M., Henrissat B., Johnson J.,
RA Kuo A., Lim J.H.P., Lipzen A., Nolan M., Ohm R.A., Tamas L.,
RA Grigoriev I.V., Spatafora J.W., Nagy L.G., Kovacs G.M.;
RT "Comparative genomics provides insights into the lifestyle and reveals
RT functional heterogeneity of dark septate endophytic fungi.";
RL Sci. Rep. 8:6321-6321(2018).
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; KZ804110; PVH88311.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2V1CRS5; -.
DR STRING; 1485229.A0A2V1CRS5; -.
DR Proteomes; UP000244409; 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 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:UP000244409}.
FT DOMAIN 151..771
FT /note="Aminoacyl-tRNA synthetase class Ia"
FT /evidence="ECO:0000259|Pfam:PF00133"
FT DOMAIN 819..965
FT /note="Methionyl/Valyl/Leucyl/Isoleucyl-tRNA synthetase
FT anticodon-binding"
FT /evidence="ECO:0000259|Pfam:PF08264"
FT REGION 1..119
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 1039..1097
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 33..47
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 61..86
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1100 AA; 123469 MW; 6CC865C4DA4BF42D CRC64;
MATNAASHNP IGEETGPVSG KPLPVSKEIK AALADATNSS PTGTHVAGQD AGSKVGTAET
GTKVKSEKEL ERERKKAEKQ AKFDQKKAKA ATATPTTSKT KEKKANASKK ADEGVLPPYV
EDTPFGEKKI IKSFDDPQYK AYNPTAVESA WYSWWEKEGF FKPEFTADGK VKPEGSFVIV
EPPPNVTGAL HMGHALGNAL QDVMIRFNRM HGKTTLWLPG CDHAGISTQN VVENMLWRRE
GKTRHDLGRP KFVETVWDWK TEYHQKINTV LRRMGGSMDW TREAFTMNEN FSAAVTETFV
SLHEEGIIYR ENRLVNWCTK LNTSLSNLEV SNKELTGRTL LDVPGYDEKV EFGIIVHFKY
EIEGTDEKIE VATTRPETML GDTGVAVHPD DERYKHLVGK NAIHPFIPGR KMPIVADAYV
EKDFGTGAVK ITPAHDPNDF ALGSRHNLER INILTDDGFM NENAGPYVGQ KRFDVRYTIQ
EDLKKAGLYV DKKDNAMTVP LCEKSKDVIE PLLKPQWWMK MTDMAAAALD VVKSGEIKIL
PETAEKSYIR WMTDVNDWCL SRQLWWGHQA PMYFAQIDGE EHDEADGSLW FAGRTEEEAQ
AKANKALPGK KFTLKRDEDV LDTWFSSGLW PFATMGWPNK THDLETLFPT SILETGWDIL
FFWIARMIMF SLKLTGKVPF TEVYCHSLVR DSEGRKMSKS LGNVIDPQDF IEGCSLEDLH
KKLLSGNLAP NEVERATKYQ KTAFPDGIPQ CGTDALRFAL VSYSTGSGDI LFDVKVIHAY
RKFCNKIYQA TKFVLGKLPA DFVPYKTAKP TGKESLAELW ILHKMTIAAK DINVAINDRE
FQKSTSVVYQ FWYNQLCDVY IENSKAILQD GSEEEKLSAL NTLYTALEGA LTMIHPFMPF
LTEELWQRLP RRPEDKTPSI GLAKYPVYDD SLDSPDSEAA YELVLDISRG VRSLMAEYSL
KDEAKVYIQS TDTTSHSTII AQIQSIKSLS GKGVSSIDVL STTDSRPAGC VVFSVSSTTA
VFLHVKGRVD IDGEIAKAAK KLDKTKVGIE KQKKILNDEG YKEKVSKELQ EVELKKLADL
ETEAKAFEET IKQFEVLKME
//
