ID M3WDF9_FELCA Unreviewed; 1062 AA.
AC M3WDF9;
DT 01-MAY-2013, integrated into UniProtKB/TrEMBL.
DT 28-FEB-2018, sequence version 2.
DT 27-MAR-2024, entry version 66.
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 Name=VARS2 {ECO:0000313|Ensembl:ENSFCAP00000009778.4,
GN ECO:0000313|VGNC:VGNC:66920};
OS Felis catus (Cat) (Felis silvestris catus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Carnivora; Feliformia; Felidae; Felinae; Felis.
OX NCBI_TaxID=9685 {ECO:0000313|Ensembl:ENSFCAP00000009778.4, ECO:0000313|Proteomes:UP000011712};
RN [1] {ECO:0000313|Ensembl:ENSFCAP00000009778.4, ECO:0000313|Proteomes:UP000011712}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Abyssinian {ECO:0000313|Ensembl:ENSFCAP00000009778.4,
RC ECO:0000313|Proteomes:UP000011712};
RX PubMed=17975172; DOI=10.1101/gr.6380007;
RA Pontius J.U., Mullikin J.C., Smith D.R., Lindblad-Toh K., Gnerre S.,
RA Clamp M., Chang J., Stephens R., Neelam B., Volfovsky N., Schaffer A.A.,
RA Agarwala R., Narfstrom K., Murphy W.J., Giger U., Roca A.L., Antunes A.,
RA Menotti-Raymond M., Yuhki N., Pecon-Slattery J., Johnson W.E., Bourque G.,
RA Tesler G., O'Brien S.J.;
RT "Initial sequence and comparative analysis of the cat genome.";
RL Genome Res. 17:1675-1689(2007).
RN [2] {ECO:0000313|Ensembl:ENSFCAP00000009778.4, ECO:0000313|Proteomes:UP000011712}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Abyssinian {ECO:0000313|Ensembl:ENSFCAP00000009778.4,
RC ECO:0000313|Proteomes:UP000011712};
RA Hillier L.W., Warren W., Obrien S., Wilson R.K.;
RT "Sequence assembly of the Felis catus genome version 6.2.";
RL Submitted (SEP-2011) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|Ensembl:ENSFCAP00000009778.4}
RP IDENTIFICATION.
RC STRAIN=breed Abyssinian {ECO:0000313|Ensembl:ENSFCAP00000009778.4};
RG Ensembl;
RL Submitted (SEP-2023) to UniProtKB.
CC -!- FUNCTION: Catalyzes the attachment of valine to tRNA(Val) in a two-step
CC reaction: valine is first activated by ATP to form Val-AMP and then
CC transferred to the acceptor end of tRNA(Val).
CC {ECO:0000256|ARBA:ARBA00043854}.
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 -!- SUBCELLULAR LOCATION: 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}.
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DR EMBL; AANG04003411; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR RefSeq; XP_006931595.1; XM_006931533.3.
DR AlphaFoldDB; M3WDF9; -.
DR STRING; 9685.ENSFCAP00000009778; -.
DR PaxDb; 9685-ENSFCAP00000009778; -.
DR Ensembl; ENSFCAT00000010534.6; ENSFCAP00000009778.4; ENSFCAG00000010531.6.
DR GeneID; 101100208; -.
DR CTD; 57176; -.
DR VGNC; VGNC:66920; VARS2.
DR eggNOG; KOG0432; Eukaryota.
DR GeneTree; ENSGT00940000159890; -.
DR HOGENOM; CLU_001493_0_2_1; -.
DR InParanoid; M3WDF9; -.
DR OMA; RQWYIRN; -.
DR OrthoDB; 5473263at2759; -.
DR Proteomes; UP000011712; Chromosome B2.
DR Bgee; ENSFCAG00000010531; Expressed in liver and 11 other cell types or tissues.
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; IBA:GO_Central.
DR GO; GO:0006438; P:valyl-tRNA aminoacylation; IBA:GO_Central.
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:SF71; VALINE--TRNA LIGASE, MITOCHONDRIAL; 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 Ligase {ECO:0000256|ARBA:ARBA00022598, ECO:0000256|RuleBase:RU363035};
KW Mitochondrion {ECO:0000256|ARBA:ARBA00023128};
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:UP000011712};
KW Transit peptide {ECO:0000256|ARBA:ARBA00022946}.
FT DOMAIN 113..735
FT /note="Aminoacyl-tRNA synthetase class Ia"
FT /evidence="ECO:0000259|Pfam:PF00133"
FT DOMAIN 780..928
FT /note="Methionyl/Valyl/Leucyl/Isoleucyl-tRNA synthetase
FT anticodon-binding"
FT /evidence="ECO:0000259|Pfam:PF08264"
FT REGION 25..74
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1062 AA; 118698 MW; F02B8DB4FFE253F5 CRC64;
MPHMPLASFR SPLWGLRPSQ VFPRSYPLST QSKPHGSSLS RRNHEAKKKR QREKQAALEA
GVARKSKSPA ESSKSWTPKE VVVYEIPTKR GEKKDVSRVL PPAYSPRYVE AAWYSWWVRE
GFFKPEYQTR LPQATGETFS MCIPPPNVTG SLHIGHALTV AIQDALVRWH RMCGDEVLWV
PGSDHAGIAT QAVVEKQLWK EQGVRRHELS REDFLREVWK WKEEKGGEIC EQLQALGASL
DWDRECFTMD ADSSVAVTEA FVRLYEAGLL YRNQQLVNWS CALRSAISDI EVESRPLPGR
TELRLPGCPI PVSFGLLVSV AFPVDGEPDT EIVVGTTRPE TLPGDVAVAV HPDDSRYTHL
HGRQLRHPLT GQLLPLVTDS AVQPHMGTGA VKVTPAHSLA DAELGARHGL SPLSVIAEDG
TMTSLCGDWL QGLHRFVARE KIMSALRERG LFRGLQNHPM VLPICSRSGD VVEYLLKSQW
FVRCREMGDR AAQAVESGAL ELSPSFHQKN WQHWFSHIGD WCISRQLWWG HQIPAYLVVE
EQTKGDREDC WVVGRTEAEA RKIASELTGR PAAELILQRD PDVLDTWFSS ALFPFAALGW
PQETPDLTRF YPLSLLETGS DLLFFWVGRM VMLGTQLTGQ LPFSKVLLHS MVRDRQGRKM
SKSLGNVLDP RDIISGVELQ VLQEKLRDGN LDSTELAIAA AAQRKDFPHG IPECGTDALR
FTLCSHGALG GDLHLSVSEV LSSRHFCNKI WNALRFILNA LGEKFVPQPA EELSPSSPMD
AWILSRLAHT ARECGRGFLA QELSLVTHAL HHFWLHNLCD VYLEAVKPVL LYSPRPQGPP
QVLFSCADIG LRLLAPLMPF LAEELWQRLP PRPGGSSAPS ISVAPYPTAC SLEHWHQPEL
EQRFSRVQEA VQALRALRAT YQLTKARPRV LLQSSEPEEQ GLFEAFLEPL GTLGHCGAVG
FLPPGVLAPS GWAQAPLNDT IQVYMELQGL VDPQTHLSLL AARRHKLQKQ LDGLMAWTPS
DGETETKRQQ RLSSLELELS KLDKAASHLR QLMDACPSPR EL
//
