ID F2U3X4_SALR5 Unreviewed; 996 AA.
AC F2U3X4;
DT 31-MAY-2011, integrated into UniProtKB/TrEMBL.
DT 31-MAY-2011, sequence version 1.
DT 27-MAR-2024, entry version 52.
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=PTSG_02983 {ECO:0000313|EMBL:EGD82318.1};
OS Salpingoeca rosetta (strain ATCC 50818 / BSB-021).
OC Eukaryota; Choanoflagellata; Craspedida; Salpingoecidae; Salpingoeca.
OX NCBI_TaxID=946362 {ECO:0000313|Proteomes:UP000007799};
RN [1] {ECO:0000313|Proteomes:UP000007799}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 50818 {ECO:0000313|Proteomes:UP000007799};
RA Russ C., Cuomo C., Burger G., Gray M.W., Holland P.W.H., King N.,
RA Lang F.B.F., Roger A.J., Ruiz-Trillo I., Young S.K., Zeng Q., Gargeya S.,
RA Alvarado L., Berlin A., Chapman S.B., Chen Z., Freedman E., Gellesch M.,
RA Goldberg J., Griggs A., Gujja S., Heilman E., Heiman D., Howarth C.,
RA Mehta T., Neiman D., Pearson M., Roberts A., Saif S., Shea T., Shenoy N.,
RA Sisk P., Stolte C., Sykes S., White J., Yandava C., Haas B., Nusbaum C.,
RA Birren B.;
RT "Annotation of Salpingoeca rosetta.";
RL Submitted (AUG-2009) to the EMBL/GenBank/DDBJ databases.
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, ECO:0000256|RuleBase:RU363035}.
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DR EMBL; GL832960; EGD82318.1; -; Genomic_DNA.
DR RefSeq; XP_004996501.1; XM_004996444.1.
DR AlphaFoldDB; F2U3X4; -.
DR STRING; 946362.F2U3X4; -.
DR EnsemblProtists; EGD82318; EGD82318; PTSG_02983.
DR GeneID; 16077089; -.
DR KEGG; sre:PTSG_02983; -.
DR eggNOG; KOG0432; Eukaryota.
DR InParanoid; F2U3X4; -.
DR OMA; LDTWMDS; -.
DR OrthoDB; 5473263at2759; -.
DR Proteomes; UP000007799; Unassembled WGS sequence.
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; 3.40.50.620; HUPs; 2.
DR Gene3D; 3.90.740.10; Valyl/Leucyl/Isoleucyl-tRNA synthetase, editing domain; 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: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 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:UP000007799}.
FT DOMAIN 110..741
FT /note="Aminoacyl-tRNA synthetase class Ia"
FT /evidence="ECO:0000259|Pfam:PF00133"
FT DOMAIN 786..937
FT /note="Methionyl/Valyl/Leucyl/Isoleucyl-tRNA synthetase
FT anticodon-binding"
FT /evidence="ECO:0000259|Pfam:PF08264"
FT REGION 1..21
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 46..100
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 996 AA; 113601 MW; E6C34089441B740F CRC64;
MAQRVTVFGM TSAEKPSEDV QTKLAVLYPK QELSAKEKKK IQKMEKFLKK QQQKEQQAAV
AGSDSKKKDK KKKKKKAEDT FVYKPVQPGE KKNLDDMPSQ YHPDMVQRDW YEWWTKQGFF
KPEYNEGHEK IACPCEKKSY TLVIPPPNVT GSLHMGHALT NSIEDTLTRW NRQCGKRTLW
NPGCDHAGIA TQSVVEKKLW REKQLRRQDL GREKFLDLVW QWKEEKGGFI YKQIKYLGAS
CDWDREAFTM SDRCCRAVKE AFIRMHEDGI IMRKKKLINW SCHLNSAISE IEVDKVDIAG
RTLVSVPGLD EKVEVGVITS FAYKLKGGDD EIVVATTRPE TMLGDVAIAV HPEDPRYASY
VGKTALHPFI PDRELVIVAD DFVDREFGTG AVKITPAHDP NDFECGVRNN LPMITVITKD
GKIAPGCGEF SGMHRFTARR VVIERLKEKG LYRGDAENPM VIPRCSRSSD ICEPLLETQW
FVNCDGMAKT AVDAVKSGEL RLIPANQEKT WFHWLESPRD WCISRQLWWG HRIPAYFVSV
NDDAVPKGTS DDNKYWVSGH DEDEARAKAA KRFGVDPSKI TLTQDEDVLD TWFSSGIFPI
SIFGWPDNTP DLQKFYPGDL LETGYDILFF WVARMVMMCT YLTGKLPFKD VYLHPIIRDK
EGVKMSKSRG NVIDPTDVCT GITLEGLHER LAQGNLDPRE IERAKELQKR QFPQGIKECG
VDALRFTLCA LVTPGRDINL DVNRIFGYRT FCNKVYNGVK LVMSKLGPDF KPAEYGKLLG
DESELDLWML SRLSTCIRDM NKQLEEYDLV GSTTSIYNLW LYEFCNFYLE VVKPVFQDDQ
YKHRRNTVQN VMYTVAESGL RLLSIFMPFL CEELWQRLPR RKATNDLVVP ASVCVAAYPY
TPLHINEDIE KKIAILHAIV GRARSLKSSL HAPSARPKLL IRGTTAATTA VCEEYAVDVA
QLVRADVAIL PAKEAPPADF EPSPEQDEFE VFMARK
//
