ID A0A179UM72_BLAGS Unreviewed; 1050 AA.
AC A0A179UM72;
DT 07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT 07-SEP-2016, sequence version 1.
DT 27-MAR-2024, entry version 32.
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=BDBG_04279 {ECO:0000313|EMBL:OAT08319.1};
OS Blastomyces gilchristii (strain SLH14081) (Blastomyces dermatitidis).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Onygenales; Ajellomycetaceae; Blastomyces.
OX NCBI_TaxID=559298 {ECO:0000313|EMBL:OAT08319.1, ECO:0000313|Proteomes:UP000002038};
RN [1] {ECO:0000313|Proteomes:UP000002038}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SLH14081 {ECO:0000313|Proteomes:UP000002038};
RX PubMed=26439490; DOI=10.1371/journal.pgen.1005493;
RA Munoz J.F., Gauthier G.M., Desjardins C.A., Gallo J.E., Holder J.,
RA Sullivan T.D., Marty A.J., Carmen J.C., Chen Z., Ding L., Gujja S.,
RA Magrini V., Misas E., Mitreva M., Priest M., Saif S., Whiston E.A.,
RA Young S., Zeng Q., Goldman W.E., Mardis E.R., Taylor J.W., McEwen J.G.,
RA Clay O.K., Klein B.S., Cuomo C.A.;
RT "The dynamic genome and transcriptome of the human fungal pathogen
RT Blastomyces and close relative Emmonsia.";
RL PLoS Genet. 11:E1005493-E1005493(2015).
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; GG657454; OAT08319.1; -; Genomic_DNA.
DR RefSeq; XP_002625410.1; XM_002625364.1.
DR AlphaFoldDB; A0A179UM72; -.
DR STRING; 559298.A0A179UM72; -.
DR GeneID; 8504990; -.
DR KEGG; bgh:BDBG_04279; -.
DR VEuPathDB; FungiDB:BDBG_04279; -.
DR OrthoDB; 5473263at2759; -.
DR Proteomes; UP000002038; 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; 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};
KW Reference proteome {ECO:0000313|Proteomes:UP000002038}.
FT DOMAIN 102..723
FT /note="Aminoacyl-tRNA synthetase class Ia"
FT /evidence="ECO:0000259|Pfam:PF00133"
FT DOMAIN 768..919
FT /note="Methionyl/Valyl/Leucyl/Isoleucyl-tRNA synthetase
FT anticodon-binding"
FT /evidence="ECO:0000259|Pfam:PF08264"
FT REGION 1..95
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 1021..1048
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 1..24
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 38..64
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 78..95
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1050 AA; 118419 MW; 421CFBE204941777 CRC64;
MASNPAQNTP APQQAANPTP PAENETVKSV AIGAPGAQKE KSERELEKER KKAEKMKKFA
EKKAKSGSAT PTAAPKTSEK KPKVEKEKNA DAYDPHTIES GRYEWWEKQG FFKPEFGPDG
NVKEKGKFVI PIPPPNVTGD LHMGHGLTNA LQDTMIRWQR MKGKTVLWLP GYDHAGISTQ
SVVEKILWKT EGKSRHDVGR EAMTNMIWDW THKYHDSITT TLKRLGGSFD WTREAFTMDE
NLSAAVTETF VRLHEEGTIY RANRLVNWCV ALNTSLSNLE VENKELEGRT LLDVPGYQRK
VEFGVLTHFL YPIDGTDETI QVATTRPETM LGDTGIAVHP DDKRYQKYVG KFAKHPFLDR
LLPIFADNQV DPEFGTGAVK ITPAHDFNDF IRGKDNKLEF ISIMNDDGTF NANAGPFAGV
KRFDARYKVI EALKEKGLYV KWENNPMKVP MCAKSNDVIE PILKPQWWMS MKDLTGPAIK
AVESGEIIIR PETAEKSYFR WMNNINDWCL SRQLWWGHQA PAYFVQLEGE HGDDSDGNLW
VVGRTEVEAQ QKAEAKFVGK KFTLKRDPDV LDTWFSSGLW PFSTLGWPKN TPDFERLYPT
SVLETGWDIL FFWVARMIML GLKMTGKVPF TEVYCHSLIR DSEGRKMSKS LGNVVNPIDV
IEGIELQVLH DKLKHGNLAE KEIAAATRYQ KKAFPKGIPE CGTDALRFAL VSYTTGGGDI
NFDIQVIHGY RRFCNKIYQA TRYVLGKLGE DFKPQATPSK TGKESLSERW ILHKFNSAAK
LANENLESRD FSVAASVLYQ YWYSQLCDVF IENSKSLLQA DVPAEVQQSA KETLYTALEG
ALTLIHPIMP FVTEELWQRL PRRPNDDTPS IMKAAYPEYN PAFDDVAAET AYELILATSK
TIRSILSEYE VKTKSDIKIQ TYDATSYKTV SDEVHLIKSL GGKYVGEIAV LDPESQTPPP
GCVPSVVSAQ AAVYLQVSDE VRLEQEEKAK VSLAKAQEAV KRQLGIMGSA GWKEKVKPEV
RALEEKKLRD AEIEAARLEE HIKGLEKLKI
//
