ID A0AAE0XLT9_9PEZI Unreviewed; 1094 AA.
AC A0AAE0XLT9;
DT 29-MAY-2024, integrated into UniProtKB/TrEMBL.
DT 29-MAY-2024, sequence version 1.
DT 28-JAN-2026, entry version 9.
DE RecName: Full=Valine--tRNA ligase, mitochondrial {ECO:0000256|ARBA:ARBA00040837};
DE EC=6.1.1.9 {ECO:0000256|ARBA:ARBA00013169};
DE AltName: Full=Valyl-tRNA synthetase {ECO:0000256|ARBA:ARBA00029936};
GN ORFNames=B0T22DRAFT_109819 {ECO:0000313|EMBL:KAK3695526.1};
OS Podospora appendiculata.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Sordariomycetidae; Sordariales; Podosporaceae; Podospora.
OX NCBI_TaxID=314037 {ECO:0000313|EMBL:KAK3695526.1, ECO:0000313|Proteomes:UP001270362};
RN [1] {ECO:0000313|EMBL:KAK3695526.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=CBS 314.62 {ECO:0000313|EMBL:KAK3695526.1};
RX PubMed=37820761;
RA Hensen N., Bonometti L., Westerberg I., Brannstrom I.O., Guillou S.,
RA Cros-Aarteil S., Calhoun S., Haridas S., Kuo A., Mondo S., Pangilinan J.,
RA Riley R., LaButti K., Andreopoulos B., Lipzen A., Chen C., Yan M., Daum C.,
RA Ng V., Clum A., Steindorff A., Ohm R.A., Martin F., Silar P., Natvig D.O.,
RA Lalanne C., Gautier V., Ament-Velasquez S.L., Kruys A., Hutchinson M.I.,
RA Powell A.J., Barry K., Miller A.N., Grigoriev I.V., Debuchy R.,
RA Gladieux P., Hiltunen Thoren M., Johannesson H.;
RT "Genome-scale phylogeny and comparative genomics of the fungal order
RT Sordariales.";
RL Mol. Phylogenet. Evol. 189:0-0(2023).
RN [2] {ECO:0000313|EMBL:KAK3695526.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=CBS 314.62 {ECO:0000313|EMBL:KAK3695526.1};
RG Lawrence Berkeley National Laboratory;
RA Haridas S., Hensen N., Bonometti L., Westerberg I., Brannstrom I.O.,
RA Guillou S., Cros-Aarteil S., Calhoun S., Kuo A., Mondo S., Pangilinan J.,
RA Riley R., Labutti K., Andreopoulos B., Lipzen A., Chen C., Yanf M.,
RA Daum C., Ng V., Clum A., Steindorff A., Ohm R., Martin F., Silar P.,
RA Natvig D., Lalanne C., Gautier V., Ament-Velasquez S.L., Kruys A.,
RA Hutchinson M.I., Powell A.J., Barry K., Miller A.N., Grigoriev I.V.,
RA Debuchy R., Gladieux P., Thoren M.H., Johannesson H.;
RL Submitted (JUN-2023) to the EMBL/GenBank/DDBJ databases.
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 Mitochondrion {ECO:0000256|ARBA:ARBA00004173}.
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:KAK3695526.1}.
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DR EMBL; JAULSO010000001; KAK3695526.1; -; Genomic_DNA.
DR AlphaFoldDB; A0AAE0XLT9; -.
DR Proteomes; UP001270362; Unassembled WGS sequence.
DR GO; GO:0005829; C:cytosol; IEA:TreeGrafter.
DR GO; GO:0005739; C:mitochondrion; IEA:UniProtKB-SubCell.
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; 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:000005; 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|SAM:Coils};
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:UP001270362}.
FT DOMAIN 146..766
FT /note="Aminoacyl-tRNA synthetase class Ia"
FT /evidence="ECO:0000259|Pfam:PF00133"
FT DOMAIN 810..957
FT /note="Methionyl/Valyl/Leucyl/Isoleucyl-tRNA synthetase
FT anticodon-binding"
FT /evidence="ECO:0000259|Pfam:PF08264"
FT REGION 46..126
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 1065..1092
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 49..62
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 65..92
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 94..109
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1094 AA; 122844 MW; 7CB2AFD33BD9EEC9 CRC64;
MPSALLRLLS SRREPILKTS STLLLDLLRP PRLLRFYSAQ HSAKMAGEAP PIAAPTAPSA
PDAPAPKKND KKEKARLDKA AKFAAKQLEK SKQPQKAEAA PKAAKAQAPA LPPFENTTPE
GEKKALHPFS DPNFSAYNPK AVEAAWYSWW EKSGFFKPET SGSAEVGTFV IPLPPPNVTG
ALHCGHALAN SLQDTLIRWH RMRGFATVWV PGCDHAGIST QSVVEKMLWK QEKKTRLDLG
RETFTDLVWK WKGDYHARIN NAQRALGGSM DWSREAFTMD ENLTRATMET FCRLHDEGLV
YRSNRLVNWC VQLNTALSGL EVENKEITGR TLLDVPGYDK KVEFGVLTYF KYPIEGSEET
IEVATTRPET MLGDTGIAVN PEDARYTHLV GKFAIHPFTS RRLPVVADSY VDLAFGTGAV
KLTPAHDQND YQLGQRHKLE FVNIFNDNGT LNDNAGPLFQ GQKRFDARYT VVQELTKLGL
YVKKEPNNMV IPLCEKSKDV IEPIMKPMWW VKMEGMAADA LRVVEEGEVK IAPESARKSY
VRWMSQINDW CISRQLWWGH QIPAYRVIFE GEDDAETDNT PWIVGRTQEE AIAKAEEKYA
PRKFRLEQDP DCLDTWFSSG LWPMAILGWP NAESSDMKKF FPTSMLETGW DILFFWVARM
IMLSLKLTGK VPFTEVYCHS LIRDSEGRKM SKSLGNVIDP LDIISGIELE QLHAKLLVGN
LKDEEVARAT KYQKTAFPSG IPECGSDALR FTLLSYTTGG GDISFDIKVM HAYRRFCNKI
WQATKYVLGK LPEDFQPSSE LGATSLSVPE KWILYRYNSA VKGVHDALEA REFSKATKIS
YQFFYDELCD VFIENSKAIL QDGTPEEQLS VQQTLYRTLD GALRLLHPMM PYITEELWQR
LPRNAKDAPP SIMLASYPSF DNELEFVSEA EDYELGLRCA GGIRSLAADY NIRADGQAYI
KASTAASLEK VKAQLPAIKT LCGKAVGELL VLGPETAEAD MPRGCAIYVI SADIAVQLQV
STQITDIDAE IKKITTKLQK TNLAIAKQQE LLAKEGFEKV SDAVLTLEKK KLADSQAAKE
NYERTMEEFS KMKI
//
