ID A0A3N4I0Y8_ASCIM Unreviewed; 1064 AA.
AC A0A3N4I0Y8;
DT 13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT 13-FEB-2019, 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=BJ508DRAFT_363002 {ECO:0000313|EMBL:RPA79772.1};
OS Ascobolus immersus RN42.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Pezizomycetes;
OC Pezizales; Ascobolaceae; Ascobolus.
OX NCBI_TaxID=1160509 {ECO:0000313|EMBL:RPA79772.1, ECO:0000313|Proteomes:UP000275078};
RN [1] {ECO:0000313|EMBL:RPA79772.1, ECO:0000313|Proteomes:UP000275078}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=RN42 {ECO:0000313|EMBL:RPA79772.1,
RC ECO:0000313|Proteomes:UP000275078};
RX PubMed=30420746; DOI=10.1038/s41559-018-0710-4;
RA Murat C., Payen T., Noel B., Kuo A., Morin E., Chen J., Kohler A.,
RA Krizsan K., Balestrini R., Da Silva C., Montanini B., Hainaut M.,
RA Levati E., Barry K.W., Belfiori B., Cichocki N., Clum A., Dockter R.B.,
RA Fauchery L., Guy J., Iotti M., Le Tacon F., Lindquist E.A., Lipzen A.,
RA Malagnac F., Mello A., Molinier V., Miyauchi S., Poulain J., Riccioni C.,
RA Rubini A., Sitrit Y., Splivallo R., Traeger S., Wang M., Zifcakova L.,
RA Wipf D., Zambonelli A., Paolocci F., Nowrousian M., Ottonello S.,
RA Baldrian P., Spatafora J.W., Henrissat B., Nagy L.G., Aury J.M.,
RA Wincker P., Grigoriev I.V., Bonfante P., Martin F.M.;
RT "Pezizomycetes genomes reveal the molecular basis of ectomycorrhizal
RT truffle lifestyle.";
RL Nat. Ecol. Evol. 2:1956-1965(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; ML119695; RPA79772.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A3N4I0Y8; -.
DR STRING; 1160509.A0A3N4I0Y8; -.
DR Proteomes; UP000275078; 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:UP000275078}.
FT DOMAIN 117..738
FT /note="Aminoacyl-tRNA synthetase class Ia"
FT /evidence="ECO:0000259|Pfam:PF00133"
FT DOMAIN 783..928
FT /note="Methionyl/Valyl/Leucyl/Isoleucyl-tRNA synthetase
FT anticodon-binding"
FT /evidence="ECO:0000259|Pfam:PF08264"
FT REGION 1..70
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 993..1062
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 31..70
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1064 AA; 120101 MW; FBCEF277F4159AC0 CRC64;
MADSTAPPTD IPEKKAPTGE EVPVEAGGAG VKVKSEKELE KERKKAEKAK KFAEKQAKVT
KDAGKAEKKE KKVKEVKVEE VLPPYVEETP AGEKKILKPL DDAYHKAYSP QVVESAWYSW
WEKEGFFKPE FTPDGKTKPE GSFVIPIPPP NVTGALHVGH ALANVLQDSL IRWNRMQGKT
TLFLPGCDHA GISTQSVVEK MLWKLEKKTR YDLGREEFVK RAWEWKEDYH ERITRALKRM
GGSYDWSREA FTLDENLSEA VAHTFVTLHE EGIIYRANRL VNWCVQLNTA ISNLEVDNKE
IEGRTLLDVP GYSKKVEFGV ITHFKYQIEG SDETIEVATT RPETMLGDTG IAVHPDDKRY
QHLIGKFAIH PIVDRKMPIV ADTYVEMDFG TGAVKITPAH DHNDFALGKR HNLEFINIMN
DDGTFNANAG PYEGHKRFDV RYSVVDELTK KGLFVKKEDN KMVIPLCAKS KDVIEPIMKP
QWWMSMKNMA EEAIKVVKDG TVKIRPESAE KSYFKWLEGI QDWCLSRQLW WGHRCPVYFV
RFEEDAGQSD DNELWVSGKT EAEAREKAEK KFPGKKFTLE QDPDVLDTWF SSGLWPFSTL
GWPKQTKDLE NLYPTSLLET GWDILFFWVA RMIMLGIKMT GKVPFTEVYC HQLVRDSEGR
KMSKSLGNVI DPLDVIEGIT FEKLNGKLLI GNLDPKELAT ATKFQKTTFP DGIPECGTDA
LRFCLAQYNT GGGDIQFDVK VMHGHRKFCN KIYQATKYVL GKLGNDYVPP AKAGKTGKES
LAERWILHKM NTCAKDIDRA LSDREFSKAT QIIYAYWYNN LCDVYIENSK SLISSGNAEE
AKSAIDTLYT ALEGALLMIH PFMPFLTEEL WQRLPRRPED KTPSVCVAKY PVYTAELDDA
ASEEAYELLL DITKGLRSLT AEYAIKGEGK AFVQAFDDAS FKTATAEAQS IQALAGKGIG
SVEILDASAP TPDGCVVSSV SSKASVFLHV KGRVDVDAEI KKADSKLKKA QESIKKQEKL
LKDKNFLTKA TDDLKEAEQK KLEDLEAVVR GVEETVKELQ KLRI
//
