ID A0A0A2KIS9_PENIT Unreviewed; 1056 AA.
AC A0A0A2KIS9;
DT 04-FEB-2015, integrated into UniProtKB/TrEMBL.
DT 04-FEB-2015, sequence version 1.
DT 27-MAR-2024, entry version 44.
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=PITC_064220 {ECO:0000313|EMBL:KGO67659.1};
OS Penicillium italicum (Blue mold).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Penicillium.
OX NCBI_TaxID=40296 {ECO:0000313|EMBL:KGO67659.1, ECO:0000313|Proteomes:UP000030104};
RN [1] {ECO:0000313|EMBL:KGO67659.1, ECO:0000313|Proteomes:UP000030104}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PHI-1 {ECO:0000313|EMBL:KGO67659.1,
RC ECO:0000313|Proteomes:UP000030104};
RX PubMed=25338147; DOI=10.1094/MPMI-09-14-0261-FI;
RA Ballester A.R., Marcet-Houben M., Levin E., Sela N., Selma-Lazaro C.,
RA Carmona L., Wisniewski M., Droby S., Gonzalez-Candelas L., Gabaldon T.;
RT "Genome, transcriptome, and functional analyses of Penicillium expansum
RT provide new insights into secondary metabolism and pathogenicity.";
RL Mol. Plant Microbe Interact. 28:232-248(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}.
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:KGO67659.1}.
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; JQGA01001270; KGO67659.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0A2KIS9; -.
DR STRING; 40296.A0A0A2KIS9; -.
DR HOGENOM; CLU_001493_0_1_1; -.
DR OMA; LDTWMDS; -.
DR OrthoDB; 5473263at2759; -.
DR PhylomeDB; A0A0A2KIS9; -.
DR Proteomes; UP000030104; 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:UP000030104}.
FT DOMAIN 107..728
FT /note="Aminoacyl-tRNA synthetase class Ia"
FT /evidence="ECO:0000259|Pfam:PF00133"
FT DOMAIN 773..921
FT /note="Methionyl/Valyl/Leucyl/Isoleucyl-tRNA synthetase
FT anticodon-binding"
FT /evidence="ECO:0000259|Pfam:PF08264"
FT REGION 1..93
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 984..1056
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 1..33
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 44..71
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 79..93
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1056 AA; 119119 MW; F89336E46640D33E CRC64;
MAQNSASQNP TGEPTAPVTS ATPQITDAAN PQGQQGGPAG APKVKTEKEL ERDRKKAEKN
KKFEEKQAAK AKAAASKAAA PKVEKKAKPE KDKTADAYDP IAIEAGRLEW WEERDLFKPE
FGPDGKVKPE GSFVIPIPPP NVTGSLHMGH ALTNALQDTM IRWQRMKGKT TLWLPGMDHA
GISTQSVVEK MLWKKEKKTR HDIGREAMVN LIWDWKDEYH KNIKNALRRL GGSFDWSREA
FTMDPNLSAA VTETFVRLHE EGIIYRANRL VNWCVALNTS LSNLEVENKE IEGRTLLDVP
GYDKKVEFGV LTHFCYEIDG STERIEIATT RPETMVGDTG IAVHPDDKRY QHLIGKSARH
PFLDRLLPIV ADPEVEPEFG TGAVKITPAH DFNDFNRGKA HNLEFISVMN DDGTFNKHAG
PYAGMKRFDA RYKVIEDLKE KGLYVKWEHN PMKVPRCAKS NDVIEPIMKP QWWMKMESLV
QPAIDAVENG DIIIRPESAE KSYFRWMRNL NDWCLSRQLW WGHQAPAYFV KIEGEDGDDS
DGNLWVTGRT EEDARKKAEE KFPGKKFSLV RDPDVLDTWF SSGLWPFSTL GWPTKTHDFE
NLYPTSVLET GWDILFFWVA RMIMLGLKMT GQVPFREVYC HSLIRDSDGR KMSKSLGNVI
DPLDVMEGIQ LQTLHDKLQL GNIAEKEIAA ATRYQKKAFP KGIPECGADA LRFALVSYTT
GGGDIAFDIQ VIHGYRKFCN KIYQATKFVL GKLGDDFKPQ AGVKKTGNES LSERWILHKF
NIAAKEMNEV LEQREFSSSA QISYQYWYSQ LCDVFLENSK SLLADEASAE TKESAKQTLY
TALEGALTLI HPIMPFVTEH LWQRLPRRAG DETISIMKAK YPEYLAEFDD PAAAKAYELI
LNTSKAIRSI LSQYDVKTQG DIIIQTYDAT SQKTVSGEMN TIKSLGGKTL GELSHLGPEN
KNPPSGCVVA AVGSEAAVYL RVSKEVALEQ EEKAKASLEK ARETVRRSQG IINGPGWKEK
VKAEVREQEE KRLRDAEGEA ARLEEQVKEF EKLRLE
//
