ID A0A087STM0_AUXPR Unreviewed; 927 AA.
AC A0A087STM0;
DT 29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 29-OCT-2014, sequence version 1.
DT 13-SEP-2023, entry version 40.
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=F751_3691 {ECO:0000313|EMBL:KFM29074.1};
OS Auxenochlorella protothecoides (Green microalga) (Chlorella
OS protothecoides).
OC Eukaryota; Viridiplantae; Chlorophyta; core chlorophytes; Trebouxiophyceae;
OC Chlorellales; Chlorellaceae; Auxenochlorella.
OX NCBI_TaxID=3075 {ECO:0000313|EMBL:KFM29074.1, ECO:0000313|Proteomes:UP000028924};
RN [1] {ECO:0000313|EMBL:KFM29074.1, ECO:0000313|Proteomes:UP000028924}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=0710 {ECO:0000313|EMBL:KFM29074.1,
RC ECO:0000313|Proteomes:UP000028924};
RX PubMed=25012212; DOI=10.1186/1471-2164-15-582;
RA Gao C., Wang Y., Shen Y., Yan D., He X., Dai J., Wu Q.;
RT "Oil accumulation mechanisms of the oleaginous microalga Chlorella
RT protothecoides revealed through its genome, transcriptomes, and
RT proteomes.";
RL BMC Genomics 15:582-582(2014).
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; KL662186; KFM29074.1; -; Genomic_DNA.
DR RefSeq; XP_011402123.1; XM_011403821.1.
DR AlphaFoldDB; A0A087STM0; -.
DR STRING; 3075.A0A087STM0; -.
DR GeneID; 23615082; -.
DR KEGG; apro:F751_3691; -.
DR eggNOG; KOG0432; Eukaryota.
DR OrthoDB; 5473263at2759; -.
DR Proteomes; UP000028924; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:InterPro.
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:0009791; P:post-embryonic development; IEA:UniProt.
DR GO; GO:0048608; P:reproductive structure development; IEA:UniProt.
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; 1.10.287.380; Valyl-tRNA synthetase, C-terminal domain; 1.
DR Gene3D; 3.90.740.10; Valyl/Leucyl/Isoleucyl-tRNA synthetase, editing domain; 2.
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; IPR010978; tRNA-bd_arm.
DR InterPro; IPR009080; tRNAsynth_Ia_anticodon-bd.
DR InterPro; IPR037118; Val-tRNA_synth_C_sf.
DR InterPro; IPR019499; Val-tRNA_synth_tRNA-bd.
DR InterPro; IPR009008; Val/Leu/Ile-tRNA-synth_edit.
DR InterPro; IPR002303; Valyl-tRNA_ligase.
DR NCBIfam; TIGR00422; valS; 1.
DR PANTHER; PTHR11946:SF93; VALINE--TRNA LIGASE, CHLOROPLASTIC/MITOCHONDRIAL 2; 1.
DR PANTHER; PTHR11946; VALYL-TRNA SYNTHETASES; 1.
DR Pfam; PF08264; Anticodon_1; 1.
DR Pfam; PF00133; tRNA-synt_1; 1.
DR Pfam; PF10458; Val_tRNA-synt_C; 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; SSF46589; tRNA-binding arm; 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 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:UP000028924}.
FT DOMAIN 34..598
FT /note="Aminoacyl-tRNA synthetase class Ia"
FT /evidence="ECO:0000259|Pfam:PF00133"
FT DOMAIN 645..790
FT /note="Methionyl/Valyl/Leucyl/Isoleucyl-tRNA synthetase
FT anticodon-binding"
FT /evidence="ECO:0000259|Pfam:PF08264"
FT DOMAIN 858..922
FT /note="Valyl-tRNA synthetase tRNA-binding arm"
FT /evidence="ECO:0000259|Pfam:PF10458"
FT REGION 1..23
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 856..925
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 927 AA; 102797 MW; 104068F9E7D20DC8 CRC64;
MCTCSHTTLP PPAPGTRSKV ELPKSFDPVA SEEKIYSWWE SSGHFEPAAP TPGEAPFTMA
MPPPNVTGKL HMGHAMFVTL QDVLARYNRL RGRPVLWLPG TDHAGIATQK QLAAEGLTRE
GLGRAEFERR VWAWKAACGG DITRQLRRLG ASCDWGRERF TLDEGLSEAV VEAFARLHER
GLVYRGAYMV NWSPGLRTAV SDLEVEYAEE AGTLYYFKYP LAGGAEGEYL PIATTRPETI
LGDTAVAVHP KDERYRHLIG RQAQVPLTDR RIPIIADEYV DPEFGTGALK ITPGHDVNDY
EIGKRHKLAI INIMDDDGRL NAAAGAFAGV DRFEARTQVW QGLEAAGLAL RTEAHTSRVP
RAQRGGEVVE PLVREQWFIK MEGLAGPALK ALDEGKLSIV PERFERVYRH WLSNIKDWCI
SRQLWWGHRL PVWYVYESEE AAAEGPLPGQ RYVVARCPDV AALLAEEEYG KSAVLRQEGD
VLDTWFSSGL WPFSTLGWPH RDAADLKRFY PTSVLETGHD ILFFWVARMV MMGLELTGKV
PFHTIYLHGL VRDEVGRKMS KSLGNVVDPV ETCEKYGADA LRFTLCTGTA PGQDVNLSLD
RVNHARNFTN KLWNAGKFVS DKEWAALAEV NFADPASRAE LGLAERWVLL ALDDTAAAMT
AALERYDFGE AGRLLYEFVW SEFADWYVEI AKTRLYSSDA SLAAKTREVL VYAYTSLLSL
AHPFTPFITE ELWSAFPPAI HSPALIVGRW PETSGYDRDD LAAAQFAALQ AAVRAVRNSR
AEYGVEPGRR IPATVRAGDP ALRAALQQES AAIALLARLD PGQLEFRDFE GPCNSSDHVQ
LVVSDGVEVD LPMAGLFDVD KELARLRKQQ ERLEKERAAL EARLARPGFA DKAPTAVVAE
VRGALAEAGQ QLAAVQAKIQ ALELQRG
//