ID A0A288GSH7_9BACT Unreviewed; 807 AA.
AC A0A288GSH7;
DT 20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT 20-DEC-2017, sequence version 1.
DT 27-MAR-2024, entry version 20.
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=valS {ECO:0000313|EMBL:AKH32517.1};
GN ORFNames=XF24_00152 {ECO:0000313|EMBL:AKH32517.1};
OS candidate division SR1 bacterium Aalborg_AAW-1.
OC Bacteria; Candidatus Absconditabacteria.
OX NCBI_TaxID=1643353 {ECO:0000313|EMBL:AKH32517.1, ECO:0000313|Proteomes:UP000217286};
RN [1] {ECO:0000313|EMBL:AKH32517.1, ECO:0000313|Proteomes:UP000217286}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Aalborg_AAW-1 {ECO:0000313|EMBL:AKH32517.1};
RX PubMed=26067967;
RA Dueholm M.S., Albertsen M., Stokholm-Bjerregaard M., McIlroy S.J.,
RA Karst S.M., Nielsen P.H.;
RT "Complete Genome Sequence of the Bacterium Aalborg_AAW-1, Representing a
RT Novel Family within the Candidate Phylum SR1.";
RL Genome Announc. 3:e00624-15(2015).
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|RuleBase:RU363035}.
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DR EMBL; CP011268; AKH32517.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A288GSH7; -.
DR STRING; 1643353.XF24_00152; -.
DR KEGG; srg:XF24_00152; -.
DR Proteomes; UP000217286; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
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 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: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 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 Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
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}.
FT DOMAIN 13..572
FT /note="Aminoacyl-tRNA synthetase class Ia"
FT /evidence="ECO:0000259|Pfam:PF00133"
FT DOMAIN 615..764
FT /note="Methionyl/Valyl/Leucyl/Isoleucyl-tRNA synthetase
FT anticodon-binding"
FT /evidence="ECO:0000259|Pfam:PF08264"
SQ SEQUENCE 807 AA; 92469 MW; 86FBB7B597F6343A CRC64;
MANYSIHDRE SHRQQFWIDN NTYKFDPTDT SRPLYTIDTP PPTVSGTLHI GHIFSYTQAE
IIARYKRMTG HNVYYPVGYD DNGIPTEILV QKELGDQAKL TGTAVRDMDR KTFVNACLDI
TAQYRDEYKA LWQSVGMSFD RDMTYSTISP MVQKIAQERF AELYKKGAIV RKEFPALWDW
ANQTTIAQAE TEEKEEDAFF NDVRFDVEGG EHIIIATTRP ELMPACVAVF VNPEDSRYTH
MLGKFAITPF GHKVPILADE KAKMDKGTGA VMCCSYGDET DIYWIMTHKL EPRIIVGRDG
RIHNSGVEEI ENLKPKQARE AIIPILEEKG NLIKRTPIRQ GIMYSERGKV PVEIIPVTQW
FINIIPIKDQ LITYANEMNF LPTHMQKRYD DWVENLQWDW NISRSRSFGI PLPVWYSKIT
GEVILPDTDQ YPIDPLTESP KNLPAGHTLD DIIREEMVLD TWFTSGISID VNKEIMKKNG
VQDIPATFDL RPQAHDIIRT WLLYTVVQSH YARETKPFDH VMISGHVLAG KGEKISKSKG
NAKFGPKELL EQFGADAVRY RAASGQLGKD IVFEETELKN GQRLITKLWN ACQFVKIHIE
SSNQELETND LYPTDQRILS RLNETVAKVT KAYDNYEVGL AKIAFEEFFW RDFCDNYLEL
IKNRLYKPEL YTNGEELKVS AQYALSQCFW TILRLIAPII PHVTEELYQD IFKSQYGLHS
IHQATIPAIQ SIKSIILDDI ITIISDVRGY KTSHKLSLGS ELQKIVISGP QSLLDSIQPY
EIDILGVTKS NSIEYNIADN YSIDIVA
//
