ID H3B5X3_LATCH Unreviewed; 1201 AA.
AC H3B5X3;
DT 18-APR-2012, integrated into UniProtKB/TrEMBL.
DT 18-APR-2012, sequence version 1.
DT 27-MAR-2024, entry version 64.
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 Name=VARS1 {ECO:0000313|Ensembl:ENSLACP00000017294.1};
OS Latimeria chalumnae (Coelacanth).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Coelacanthiformes; Coelacanthidae; Latimeria.
OX NCBI_TaxID=7897 {ECO:0000313|Ensembl:ENSLACP00000017294.1, ECO:0000313|Proteomes:UP000008672};
RN [1] {ECO:0000313|Proteomes:UP000008672}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Wild caught {ECO:0000313|Proteomes:UP000008672};
RA Di Palma F., Alfoldi J., Johnson J., Berlin A., Gnerre S., Jaffe D.,
RA MacCallum I., Young S., Walker B.J., Lander E., Lindblad-Toh K.;
RT "The draft genome of Latimeria chalumnae.";
RL Submitted (AUG-2011) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSLACP00000017294.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
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}.
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DR EMBL; AFYH01090914; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AFYH01090915; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AFYH01090916; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AFYH01090917; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AFYH01090918; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AFYH01090919; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR AlphaFoldDB; H3B5X3; -.
DR STRING; 7897.ENSLACP00000017294; -.
DR Ensembl; ENSLACT00000017421.1; ENSLACP00000017294.1; ENSLACG00000015232.1.
DR eggNOG; KOG0432; Eukaryota.
DR eggNOG; KOG0867; Eukaryota.
DR GeneTree; ENSGT00940000157775; -.
DR HOGENOM; CLU_001493_0_1_1; -.
DR InParanoid; H3B5X3; -.
DR OMA; LDTWMDS; -.
DR TreeFam; TF300648; -.
DR Proteomes; UP000008672; Unassembled WGS sequence.
DR Bgee; ENSLACG00000015232; Expressed in muscle tissue and 4 other cell types or tissues.
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; 1.20.1050.10; -; 1.
DR Gene3D; 3.40.50.620; HUPs; 2.
DR Gene3D; 3.90.740.10; Valyl/Leucyl/Isoleucyl-tRNA synthetase, editing domain; 1.
DR InterPro; IPR002300; aa-tRNA-synth_Ia.
DR InterPro; IPR033705; Anticodon_Ia_Val.
DR InterPro; IPR010987; Glutathione-S-Trfase_C-like.
DR InterPro; IPR036282; Glutathione-S-Trfase_C_sf.
DR InterPro; IPR004046; GST_C.
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; PF00043; GST_C; 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; SSF47616; GST C-terminal domain-like; 1.
DR SUPFAM; SSF52374; Nucleotidylyl transferase; 1.
DR SUPFAM; SSF50677; ValRS/IleRS/LeuRS editing domain; 1.
DR PROSITE; PS50405; GST_CTER; 1.
PE 3: Inferred from homology;
KW Aminoacyl-tRNA synthetase {ECO:0000256|ARBA:ARBA00023146};
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Ligase {ECO:0000256|ARBA:ARBA00022598};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Protein biosynthesis {ECO:0000256|ARBA:ARBA00022917};
KW Reference proteome {ECO:0000313|Proteomes:UP000008672}.
FT DOMAIN 78..210
FT /note="GST C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS50405"
FT REGION 211..278
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 108..138
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 232..278
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1201 AA; 135621 MW; 20EF5C3DC3D5EA99 CRC64;
MPTLYLSPHP DDFRNLRILI AAQYGGSGSG DVKIVEAAAA GAACATKLPQ LETESDGTLT
GTGAIAYFLA SDQLRGSSAK EVTLVQQWVN FADNEAIQAA CGWAFPVLGV MKANKQALER
AQQELKKLLQ VLDDYLKLRT YLVGERITLA DIAVSCSLLL PYKYVLEPAL RKSYVNVNRW
FLTCVNQPQF RKVLGEVKLC ENVEQAASKP VITQEQQAAS GPAAPEEGEP KQKTAAQVKK
EAKKKEKLEK FQQKQDKMKQ QKQPQNEKKP KAEKKEKKEL GVITYEIPTP PGDKKDVFCP
MPDSYSPQYV EAAWYPWWEK QGFFKPEFGP PPTNCFRKEV LTLMMIPPPS RFLNETLRRR
HRMRGEMTLW NPGCDHAGIA TQVVVEKKLW REQRKTRHDL GRDGFIQQVW NWKNEKGDRI
YHQLRKLGSS LDWDRACFTM DSKLSYAVQE AFVRLHEDGV IYRSTRLVNW SCTLNSAISD
IEAQVDKKEL TGRTLLPVPG YAEKVEFGVL VSFAYKIEGS GIFCADEEVV VATTRIETML
GDTAVAVHPE DARYQHLKGK NIVHPFCARK MPVVFDDFVD MSFGTEPEGA VKITPAHDHN
DYEVGLRHGL EFVNIIDDNG VLINVPVPFL VRTPCFTGVC VRDGGSWVFE SSSSGVQRGG
SRSKDIVEPL MKPQWYVRCD EMARQAADTV RSGELRIIPE FHHKTWFNWL DNIRDWCVSR
QLWWGHRVPA YFVTVNDPSV PPGEDTDGKY WISGRSEEEA RMKATKVFGV SPEKISLRQD
EDVLDTWFSS AIFPFSIFGW PNETEDLKVF YPGTLLETGH DILFFWVARM VMFGLKLMGQ
LPFKEVYLHA VVRDAHGRKM SKSLGNVIDP LDVISGITLE GLHLQLQDSN LDPAETERAK
QGQKSDYPNG IPECGTDALR FALCAYTCQG RDINLDVNRI LGYRHFCNKL WNATKFAIRG
LGEDFRPESS AQLCGQESLV DRWILSRLCH AVQLCDAGFR SYDFPAITTA VYNFWLYELC
DIYLECLKPV FAGMDESTIR AARSTLYTCL DVGLRLLSPL MPFVSEELFQ RLPRRSADTP
PSISVTPYPD TAEYCWRDEQ VDRNVEFTMS IIRTIRSLRA DYNLTKTKAD CYLKCLDEET
AAVVTCYCAY IQTLSSSLSV TALVEGEPPA GCAVAIASDK CTVNIMLKVG ANISLSRYSI
L
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