SYVM_DICDI
ID SYVM_DICDI Reviewed; 1051 AA.
AC Q54I78;
DT 08-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT 19-JAN-2010, sequence version 2.
DT 03-AUG-2022, entry version 111.
DE RecName: Full=Probable valine--tRNA ligase, mitochondrial;
DE EC=6.1.1.9;
DE AltName: Full=Valyl-tRNA synthetase;
DE Short=ValRS;
DE Flags: Precursor;
GN Name=valS2; ORFNames=DDB_G0288939;
OS Dictyostelium discoideum (Slime mold).
OC Eukaryota; Amoebozoa; Evosea; Eumycetozoa; Dictyostelia; Dictyosteliales;
OC Dictyosteliaceae; Dictyostelium.
OX NCBI_TaxID=44689;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AX4;
RX PubMed=15875012; DOI=10.1038/nature03481;
RA Eichinger L., Pachebat J.A., Gloeckner G., Rajandream M.A., Sucgang R.,
RA Berriman M., Song J., Olsen R., Szafranski K., Xu Q., Tunggal B.,
RA Kummerfeld S., Madera M., Konfortov B.A., Rivero F., Bankier A.T.,
RA Lehmann R., Hamlin N., Davies R., Gaudet P., Fey P., Pilcher K., Chen G.,
RA Saunders D., Sodergren E.J., Davis P., Kerhornou A., Nie X., Hall N.,
RA Anjard C., Hemphill L., Bason N., Farbrother P., Desany B., Just E.,
RA Morio T., Rost R., Churcher C.M., Cooper J., Haydock S., van Driessche N.,
RA Cronin A., Goodhead I., Muzny D.M., Mourier T., Pain A., Lu M., Harper D.,
RA Lindsay R., Hauser H., James K.D., Quiles M., Madan Babu M., Saito T.,
RA Buchrieser C., Wardroper A., Felder M., Thangavelu M., Johnson D.,
RA Knights A., Loulseged H., Mungall K.L., Oliver K., Price C., Quail M.A.,
RA Urushihara H., Hernandez J., Rabbinowitsch E., Steffen D., Sanders M.,
RA Ma J., Kohara Y., Sharp S., Simmonds M.N., Spiegler S., Tivey A.,
RA Sugano S., White B., Walker D., Woodward J.R., Winckler T., Tanaka Y.,
RA Shaulsky G., Schleicher M., Weinstock G.M., Rosenthal A., Cox E.C.,
RA Chisholm R.L., Gibbs R.A., Loomis W.F., Platzer M., Kay R.R.,
RA Williams J.G., Dear P.H., Noegel A.A., Barrell B.G., Kuspa A.;
RT "The genome of the social amoeba Dictyostelium discoideum.";
RL Nature 435:43-57(2005).
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 -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the class-I aminoacyl-tRNA synthetase family.
CC {ECO:0000305}.
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DR EMBL; AAFI02000126; EAL62993.2; -; Genomic_DNA.
DR RefSeq; XP_636501.2; XM_631409.2.
DR AlphaFoldDB; Q54I78; -.
DR SMR; Q54I78; -.
DR STRING; 44689.DDB0304686; -.
DR PaxDb; Q54I78; -.
DR PRIDE; Q54I78; -.
DR EnsemblProtists; EAL62993; EAL62993; DDB_G0288939.
DR GeneID; 8626884; -.
DR KEGG; ddi:DDB_G0288939; -.
DR dictyBase; DDB_G0288939; valS2.
DR eggNOG; KOG0432; Eukaryota.
DR HOGENOM; CLU_001493_0_0_1; -.
DR InParanoid; Q54I78; -.
DR OMA; RQWYIRN; -.
DR PhylomeDB; Q54I78; -.
DR PRO; PR:Q54I78; -.
DR Proteomes; UP000002195; Chromosome 5.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0005739; C:mitochondrion; IEA:UniProtKB-SubCell.
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; ISS:dictyBase.
DR GO; GO:0006438; P:valyl-tRNA aminoacylation; ISS:dictyBase.
DR CDD; cd07962; Anticodon_Ia_Val; 1.
DR Gene3D; 3.40.50.620; -; 2.
DR Gene3D; 3.90.740.10; -; 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 PANTHER; PTHR11946; PTHR11946; 1.
DR Pfam; PF08264; Anticodon_1; 1.
DR Pfam; PF00133; tRNA-synt_1; 1.
DR PRINTS; PR00986; TRNASYNTHVAL.
DR SUPFAM; SSF47323; SSF47323; 1.
DR SUPFAM; SSF50677; SSF50677; 1.
DR TIGRFAMs; TIGR00422; valS; 1.
DR PROSITE; PS00178; AA_TRNA_LIGASE_I; 1.
PE 3: Inferred from homology;
KW Aminoacyl-tRNA synthetase; ATP-binding; Coiled coil; Ligase; Mitochondrion;
KW Nucleotide-binding; Protein biosynthesis; Reference proteome;
KW Transit peptide.
FT TRANSIT 1..20
FT /note="Mitochondrion"
FT /evidence="ECO:0000255"
FT CHAIN 21..1051
FT /note="Probable valine--tRNA ligase, mitochondrial"
FT /id="PRO_0000327761"
FT COILED 972..1019
FT /evidence="ECO:0000255"
FT MOTIF 71..81
FT /note="'HIGH' region"
FT /evidence="ECO:0000250"
FT MOTIF 606..610
FT /note="'KMSKS' region"
FT /evidence="ECO:0000250"
FT BINDING 609
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
SQ SEQUENCE 1051 AA; 121425 MW; 9631791BD20CB26C CRC64;
MNKLLFLSKK SSTSNLYRFY SRAPINESSI KSSFDPKVVE EFKYKYWQDS GLFKPKSNNG
GEKFSMVLPP PNVTGSLHIG HSLTTTIQDS LIRYNRMMGK EVLWVPGLDH SGIATQVAVE
KELQVKQGKT RFDLGREKFL EQVFQWTDQY SSNINNQLKI TGSSLDWSRS VFTLDEQRND
AVQTAFIRMF EMGLIYRSTR LVNWCPYLQS VISDIEVDHK VIEKPTMLKL KSRKKSVEVG
AIHNIAYMME DPMLAPLIVS TTRPETIFGD TGLAIHPLDE RYKDYHGKFA IHPFNHERIP
IVLDDILVNR EMGTGVVKIT PAHDFNDYQC GQRHSLPIVN ILNSNGTLNE NSTAEFEGVD
RLDARSMVIE KLEQMGLYRE KLAHPQTLSI CSRSGDLLEP VLKPQWYVKC KDMADKSIEF
VESGEIKIIP ESFRADWSRW LTNIQDWCIS RQLWWGNPIP AYRVIMIDKV TNEDLDIHLT
ETERLKQEKW VVGKNEKEAR ENVFKTYGIA NAGEYRLEKD QDVLDTWFSS GLFPISSMGW
PTATKNSDND NDFSRFLPLD VMETGSDILF FWVARMVMMC STLNNGEVPF KTILLHPMIR
DSQGRKMSKS LGNVIDPLHV INGISLQDLK ENLSKSNLSQ QEKVTATKGL EKEFPQGIPQ
CGTDSLRFSL AQYPINGKDI NLDISKIIGN RLFCNKLWNA SKFVFNYLVN LNNLSINLYY
NNNNNEKDQQ QPFNYLESTT LIDKWILLKL SKLVEIVNES YKSNNLSIAA QSLYSFFQYD
FCDIYIECIK ADLSKPILSK QNEHSSLVLA SVLDSYLRML HPFMPFITED LWQRLPKSKQ
QLEIANSIEI DDSLSIMISD YPNPSYKYHQ LFKNQEIEIE KQVNLFLDTL KLIRSQKVSL
GINEKTKLII KLQIIGDDQI LIKSSFNQLK DSFEKLLNSN LIIDENNNND NNNNNDNNDL
TNISINKFTI SKELQISIEF DKEINNQLNQ KLINPNQSND KKILKLENFI KQLQDEIDNP
DFKQRVPEKV QNIKIEKLNQ YKIELKEIYK K
