ID W6Z3H5_COCMI Unreviewed; 1091 AA.
AC W6Z3H5;
DT 16-APR-2014, integrated into UniProtKB/TrEMBL.
DT 16-APR-2014, sequence version 1.
DT 27-MAR-2024, entry version 50.
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=COCMIDRAFT_98522 {ECO:0000313|EMBL:EUC44278.1};
OS Bipolaris oryzae ATCC 44560.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Pleosporomycetidae; Pleosporales; Pleosporineae; Pleosporaceae; Bipolaris.
OX NCBI_TaxID=930090 {ECO:0000313|EMBL:EUC44278.1};
RN [1] {ECO:0000313|EMBL:EUC44278.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 44560 {ECO:0000313|EMBL:EUC44278.1};
RX PubMed=23357949; DOI=10.1371/journal.pgen.1003233;
RA Condon B.J., Leng Y., Wu D., Bushley K.E., Ohm R.A., Otillar R., Martin J.,
RA Schackwitz W., Grimwood J., MohdZainudin N., Xue C., Wang R., Manning V.A.,
RA Dhillon B., Tu Z.J., Steffenson B.J., Salamov A., Sun H., Lowry S.,
RA LaButti K., Han J., Copeland A., Lindquist E., Barry K., Schmutz J.,
RA Baker S.E., Ciuffetti L.M., Grigoriev I.V., Zhong S., Turgeon B.G.;
RT "Comparative genome structure, secondary metabolite, and effector coding
RT capacity across Cochliobolus pathogens.";
RL PLoS Genet. 9:E1003233-E1003233(2013).
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 ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; KI964007; EUC44278.1; -; Genomic_DNA.
DR RefSeq; XP_007689193.1; XM_007691003.1.
DR AlphaFoldDB; W6Z3H5; -.
DR STRING; 930090.W6Z3H5; -.
DR GeneID; 19129280; -.
DR KEGG; bor:COCMIDRAFT_98522; -.
DR eggNOG; KOG0432; Eukaryota.
DR HOGENOM; CLU_001493_0_1_1; -.
DR OrthoDB; 5473263at2759; -.
DR Proteomes; UP000054032; 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; 2.170.220.10; -; 1.
DR Gene3D; 3.40.50.620; HUPs; 2.
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; 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}.
FT DOMAIN 143..763
FT /note="Aminoacyl-tRNA synthetase class Ia"
FT /evidence="ECO:0000259|Pfam:PF00133"
FT DOMAIN 808..955
FT /note="Methionyl/Valyl/Leucyl/Isoleucyl-tRNA synthetase
FT anticodon-binding"
FT /evidence="ECO:0000259|Pfam:PF08264"
FT REGION 1..123
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 1020..1088
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 1..17
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 45..81
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 91..123
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1091 AA; 123206 MW; E68235A2960B0D2A CRC64;
MALNASSHNT TGDKTAPNTA PPPELSGEAK KDILGAAETE ATGQHAPGRE NEKGVEKKEK
TAKELEKERK KAEKDAKFKA KKAAAAGAAK DAPAKEKKKK GKEEEQLPEY VEQTPKGEKK
RLQSLDGPYT KAYIPKVVES AWDAWWDAQG FFKPQFAEDG NVKAPGHFVI PIPPPNVTGK
LHCGHALATS LQDVLIRWHR MRGYTTLYLP GCDHAGIATQ SVVEKMLKRR ENKTRYDLGR
QKFLERTMEW KQEYHQHLTN TLRRMGGSFD WTREAFTMDE NLSKAVTETF VRLHEDGLIY
RSNRLVNWCT ALNTALSTLE VDNKDLAGPT KLSVPGYERM VEFGVLTHFK YAIDGTDQFI
EIATTRPETM LGDSGIAVHP KDDRYKHLVG KKAKHPFIDR LMPIVADEYV DPEFGTGAVK
LTPAHDPNDF NLGKKHNLEF INILNDNGTM NKNAGRFEGE KRFDVRYTVV DALKKEGLFV
KTEPNPMKVP ICSRSGDVIE PIMKPQWWMK MESLAKPAIE AVEKGDIKIR PATSEKIYMH
WMNNVQDWCL SRQLWWGHQI PAYFVQIEGA EGDRNEDELW ITGRTEEEAR AKAEKKFPGK
KFTLSRDEDV LDTWFSSGLW PFSTLGWPNQ TADLEKLFPT SVLETGWDIL FFWVARMIFL
SLYLTGKVPF KEVYCHSLIR DSEGRKMSKS LGNVVDPVDI MDGITLQKLH DQLRAGNLDP
KELTKAEKYQ KTAFPQGIPE CGADALRMAL VGYTTGGGDI SFDVNVIHGY RRFCNKIYQA
TKYVIGRLGE SFTPQEKAGK SGKESLPERY ILHNLNAAAK KINDHLEARE FSLATQVAYK
YFYVYLCDTY IENSKAIFDE GSEEQKESAK QTLYTAIEGG LNMIHPFMPF LTEELWQRLP
RRQGDKTPSI CIAPFPQYSQ ELEDETANAE YELLVDSAKG LRSMTAEYGI KDSASTYIQA
LDDSTHSILS SSTSLPSIKS LAGKTVSEIK ILSPSETAPS GCAVYTIGTS ATAYLDVKGR
IELDKEITKA QDRLTKANET ITRQKKIMDN DWEEKVSDVV KEQEREKLKA AELEAKNWEA
SIAQFEKMKI E
//
