ID A0A1Y1XR13_9FUNG Unreviewed; 1270 AA.
AC A0A1Y1XR13;
DT 30-AUG-2017, integrated into UniProtKB/TrEMBL.
DT 30-AUG-2017, sequence version 1.
DT 27-MAR-2024, entry version 26.
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=K493DRAFT_411128 {ECO:0000313|EMBL:ORX87936.1};
OS Basidiobolus meristosporus CBS 931.73.
OC Eukaryota; Fungi; Fungi incertae sedis; Zoopagomycota;
OC Entomophthoromycotina; Basidiobolomycetes; Basidiobolales; Basidiobolaceae;
OC Basidiobolus.
OX NCBI_TaxID=1314790 {ECO:0000313|EMBL:ORX87936.1, ECO:0000313|Proteomes:UP000193498};
RN [1] {ECO:0000313|EMBL:ORX87936.1, ECO:0000313|Proteomes:UP000193498}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 931.73 {ECO:0000313|EMBL:ORX87936.1,
RC ECO:0000313|Proteomes:UP000193498};
RG DOE Joint Genome Institute;
RA Mondo S.J., Dannebaum R.O., Kuo R.C., Labutti K., Haridas S., Kuo A.,
RA Salamov A., Ahrendt S.R., Lipzen A., Sullivan W., Andreopoulos W.B.,
RA Clum A., Lindquist E., Daum C., Ramamoorthy G.K., Gryganskyi A., Culley D.,
RA Magnuson J.K., James T.Y., O'Malley M.A., Stajich J.E., Spatafora J.W.,
RA Visel A., Grigoriev I.V.;
RT "Pervasive Adenine N6-methylation of Active Genes in Fungi.";
RL Submitted (JUL-2016) 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:ORX87936.1}.
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DR EMBL; MCFE01000542; ORX87936.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1Y1XR13; -.
DR STRING; 1314790.A0A1Y1XR13; -.
DR InParanoid; A0A1Y1XR13; -.
DR OrthoDB; 5473263at2759; -.
DR Proteomes; UP000193498; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:InterPro.
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; 1.25.40.10; Tetratricopeptide repeat domain; 1.
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; IPR011990; TPR-like_helical_dom_sf.
DR InterPro; IPR019734; TPR_repeat.
DR InterPro; IPR009080; tRNAsynth_Ia_anticodon-bd.
DR InterPro; IPR037118; Val-tRNA_synth_C_sf.
DR InterPro; IPR019499; Val-tRNA_synth_tRNA-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 Pfam; PF10458; Val_tRNA-synt_C; 1.
DR PRINTS; PR00986; TRNASYNTHVAL.
DR SMART; SM00028; TPR; 3.
DR SUPFAM; SSF47323; Anticodon-binding domain of a subclass of class I aminoacyl-tRNA synthetases; 1.
DR SUPFAM; SSF52374; Nucleotidylyl transferase; 1.
DR SUPFAM; SSF48452; TPR-like; 1.
DR SUPFAM; SSF50677; ValRS/IleRS/LeuRS editing domain; 1.
DR PROSITE; PS00178; AA_TRNA_LIGASE_I; 1.
DR PROSITE; PS50005; TPR; 2.
DR PROSITE; PS50293; TPR_REGION; 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:UP000193498};
KW TPR repeat {ECO:0000256|PROSITE-ProRule:PRU00339}.
FT REPEAT 86..119
FT /note="TPR"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00339"
FT REPEAT 125..158
FT /note="TPR"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00339"
FT DOMAIN 286..924
FT /note="Aminoacyl-tRNA synthetase class Ia"
FT /evidence="ECO:0000259|Pfam:PF00133"
FT DOMAIN 978..1133
FT /note="Methionyl/Valyl/Leucyl/Isoleucyl-tRNA synthetase
FT anticodon-binding"
FT /evidence="ECO:0000259|Pfam:PF08264"
FT DOMAIN 1205..1265
FT /note="Valyl-tRNA synthetase tRNA-binding arm"
FT /evidence="ECO:0000259|Pfam:PF10458"
FT REGION 1..27
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 1202..1229
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 1270 AA; 144632 MW; 2E4D58ECA01C54E0 CRC64;
MSPKISEISD SEEEEFYESL EYADEPNTVL KETQLKEVSS EDPTVVAENS THAIPKTVAS
VEASEINIIP PTPLTEEEIE ERVQEVESYK AVGNQLFGSG EYESAVEKYN QALEICPKEK
PSLLALLHGN IAACYIKLER LEDAVSACDS ALALEPTYVK ALVRRAQANE KIGKYLALSS
ALEDYKKLLD IAPNYRRECE RALVRLPPRI EEQQEIEKAE MLEKVKDLGN RFLGMFGLST
DNFQMQKDPS TGNYSMQFKL RNYAQVSKPK RPLNGKYQPA EVEKGWYEWW EKQGYFSPTH
RHSRAGEQKI TTVLTPPPNV TGNLHIGHAL TFSVQDSLVR WRRMCGEAVS WIPGTDHAGI
GTQSVVEKQL MKQHKLTRHD LGRDKFISEV WKWKELHGNK IIEQMRKMGS SLDWKNEFFT
MDAPRTEAVT NAFIQFFKDG LLYRDTRIVN WCCHLETAIS DIEVDYETVQ GQTFLTLPGR
EDKVEVGVLH KLAYKVVDPV GDIEELVVAT TRIETILGDC ALAIHPEDPR YKTLHGKFVL
HPVLNQKIPI ICDPELVDPD FGTGVVKVTP GHDPNDYACG RRHNLPLTSI MDKTGTFNEL
CGVRKYQNKD RYIVRNEIVE DLISSGAYRG KDVNHEMRIS RCSRSGDIIE PMVQPQWFLN
CQEMAKTAIK NMDNGSMNIT PGHHKPDWYR WLENIQDWCV SRQLWWGHRI PAYRLIFNDP
EIRKVIQGSA SSNELWFVAE SKEKAVEQVS DFLNQHKISN QTDYSLEQDD DVLDTWFSSA
LLPLSALGWD GKSKSLENYP TAFIETGFDI LFFWVARMAM LSTYFSGSPP FKDIYLHAMI
RDSQGRKMSK SLGNVIDPLH VINGISLNEL RQALHSGNLA SEEIKRSESV MEKEFPDGIP
ACGTDALRFS LVSYTQQTRQ INMDISNVTS ALHFGNKLWN LCRFSFGRFD TLREYVPPIS
DSLAVPSITK LEEQPLVNKY ILSRLADTVR KTHSAMSEYQ LHQATDSIRR FVVNDLCDVY
LEFSKPTLYG KSTIEEQRSA TLILTTCLDT SLRLLHPFMP FVTEELWQNL IAHTNPESST
QPESLMVTEF PAPEKFGAFY DEQVESEMQI ILSLIHASRS LRQTQHVSIS QELPFSVWTD
QPDLLGPLRR YSSELQNFVK ATSLEIVHGQ EAEIPSDVAV STISPNLKVF VPVSALKSVG
SNSKVQGEID RIKRKMAKIT KEIEDLEDKI NKPEYEVRVP ERVKLSNSKR LAMFKEQLTS
FQTNLGLLEK
//
