ID A0A6A6BTD5_9PEZI Unreviewed; 1040 AA.
AC A0A6A6BTD5;
DT 17-JUN-2020, integrated into UniProtKB/TrEMBL.
DT 17-JUN-2020, sequence version 1.
DT 28-JAN-2026, entry version 19.
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=K452DRAFT_294091 {ECO:0000313|EMBL:KAF2146525.1};
OS Aplosporella prunicola CBS 121167.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Dothideomycetes incertae sedis; Botryosphaeriales; Aplosporellaceae;
OC Aplosporella.
OX NCBI_TaxID=1176127 {ECO:0000313|EMBL:KAF2146525.1, ECO:0000313|Proteomes:UP000799438};
RN [1] {ECO:0000313|EMBL:KAF2146525.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=CBS 121167 {ECO:0000313|EMBL:KAF2146525.1};
RA Haridas S., Albert R., Binder M., Bloem J., Labutti K., Salamov A.,
RA Andreopoulos B., Baker S., Barry K., Bills G., Bluhm B., Cannon C.,
RA Castanera R., Culley D., Daum C., Ezra D., Gonzalez J., Henrissat B.,
RA Kuo A., Liang C., Lipzen A., Lutzoni F., Magnuson J., Mondo S., Nolan M.,
RA Ohm R., Pangilinan J., Park H.-J., Ramirez L., Alfaro M., Sun H., Tritt A.,
RA Yoshinaga Y., Zwiers L.-H., Turgeon B., Goodwin S., Spatafora J., Crous P.,
RA Grigoriev I.;
RT "101 Dothideomycetes genomes: a test case for predicting lifestyles and
RT emergence of pathogens.";
RL Stud. Mycol. 0:0-0(2020).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=tRNA(Val) + L-valine + ATP = L-valyl-tRNA(Val) + AMP +
CC diphosphate; 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:ARBA00047552};
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
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; ML995475; KAF2146525.1; -; Genomic_DNA.
DR RefSeq; XP_033402234.1; XM_033541659.1.
DR AlphaFoldDB; A0A6A6BTD5; -.
DR GeneID; 54299156; -.
DR OrthoDB; 629407at2759; -.
DR Proteomes; UP000799438; Unassembled WGS sequence.
DR GO; GO:0005829; C:cytosol; IEA:TreeGrafter.
DR GO; GO:0002161; F:aminoacyl-tRNA deacylase 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 FunFam; 3.90.740.10:FF:000010; Valine--tRNA ligase; 1.
DR FunFam; 1.10.730.10:FF:000009; Valine--tRNA ligase, mitochondrial; 1.
DR FunFam; 3.40.50.620:FF:000020; Valine--tRNA ligase, mitochondrial; 1.
DR FunFam; 3.40.50.620:FF:000078; Valine--tRNA ligase, mitochondrial; 1.
DR FunFam; 3.90.740.10:FF:000008; Valine--tRNA ligase, mitochondrial; 1.
DR Gene3D; 3.40.50.620; HUPs; 2.
DR Gene3D; 1.10.730.10; Isoleucyl-tRNA Synthetase, Domain 1; 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; IPR009080; tRNAsynth_Ia_anticodon-bd.
DR InterPro; IPR009008; Val/Leu/Ile-tRNA-synth_edit.
DR InterPro; IPR002303; Valyl-tRNA_ligase.
DR NCBIfam; NF004349; PRK05729.1; 1.
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|ARBA:ARBA00023054};
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
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:UP000799438}.
FT DOMAIN 146..767
FT /note="Aminoacyl-tRNA synthetase class Ia"
FT /evidence="ECO:0000259|Pfam:PF00133"
FT DOMAIN 812..951
FT /note="Methionyl/Valyl/Leucyl/Isoleucyl-tRNA synthetase
FT anticodon-binding"
FT /evidence="ECO:0000259|Pfam:PF08264"
FT REGION 1..85
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 48..85
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1040 AA; 117349 MW; 7DD8F6417ACCD8F9 CRC64;
MALNHASHNI PGEKTGPATG PPPPVSSEAA SAIVDASQKD AMGQHAPGQD EAKPVAAEGE
NKPKTEKELK KEREKAEKAK KFQEKQAKKA QLAANTVKNA SKKKVVGTEA MKPYVEETPK
GQKKILKSLD DEYHKAYIPS VVESAWYDWW EKEGYFEPEF GPDGNVKPAG YFVIPEPPPN
VTGALHCGHA LANALQDTMI RWERMRGKTV LYLPGCDHAG ISTQSVVEKM LWRKEQKTRH
DLGRPAMVQR IWDWKGEYHQ RINNVLRRMG GSFDWSREAF TMDDNLSKAV TETFVRLHEE
GLIYRSNRLV NWCTTLRTAL SNLEVDNKEI EGRTLLDVPG YDRKVEFGVI THFKYPIEGT
EETIEVATTR PETMLGDSGI AVHPNDERYK HLVGKKAKHP FVDRLLPIVA DTYVDPEFGT
GAVKITPAHD PNDFSLGQRH NLEFINVFTD DGLLNQNSGQ FQGQKRFDVR YSVVEELTKL
NLYVKKENNP MKIPLCQRTK DVIEPIVKPQ WWMRMKSLAE PAIAAARNGD IKIRPATAEA
DYFRWLENIQ DWCLSRQLWW GHQAPAYFVE VEGETNSDSD DQYWIVGRTE EEAKEKAAKK
FAGKKFTLRR DEDVLDTWFS SGLWPFSTLG WPNETPDMAK LYPTSVLETG WDILFFWVAR
MIMLGIKLTG QIPFKEVYCH SLIRDSEGRK MSKSLGNVID PVDIMEGIQL EQLHQKLLEG
NLDPKELKTA SKYQQTAFPQ GIPECGADAL RFSLVQYTTG GGDIAFDVKV MHAYRRFCNK
IYQATKYVLG KIDADYVPQK TADKTGKESL AERWILHKLS IASKEINQAL TDREFAKSTQ
IAWHYFHDDL CDVFIEYTKP IIQDGTPEAK RSAIDTLYTA LEGGLTMLHP YMPFLTEELW
QRLARRPGDS TPTIMRAAYP QHRPDFDDAA AEASYELILE AAASARSIIA QHKLVGAKAA
VRLGKADEVA AKAVDDVKTL AGKGLGDVML VKEGEEGPQG WQRGESEKTG GVVWIEVPSR
PLSKEGEVKE LEKKTGELKV
//
