ID A0A0G0H9J2_9BACT Unreviewed; 910 AA.
AC A0A0G0H9J2;
DT 22-JUL-2015, integrated into UniProtKB/TrEMBL.
DT 22-JUL-2015, sequence version 1.
DT 27-MAR-2024, entry version 41.
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=US50_C0022G0003 {ECO:0000313|EMBL:KKQ35190.1};
OS Candidatus Nomurabacteria bacterium GW2011_GWB1_37_5.
OC Bacteria; Candidatus Nomurabacteria.
OX NCBI_TaxID=1618742 {ECO:0000313|EMBL:KKQ35190.1, ECO:0000313|Proteomes:UP000033876};
RN [1] {ECO:0000313|EMBL:KKQ35190.1, ECO:0000313|Proteomes:UP000033876}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Brown C.T., Hug L.A., Thomas B.C., Sharon I., Castelle C.J., Singh A.,
RA Wilkins M.J., Williams K.H., Banfield J.F.;
RT "rRNA introns, odd ribosomes, and small enigmatic genomes across a large
RT radiation of phyla.";
RL Nature 0:0-0(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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KKQ35190.1}.
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DR EMBL; LBTF01000022; KKQ35190.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0G0H9J2; -.
DR PATRIC; fig|1618742.3.peg.440; -.
DR Proteomes; UP000033876; Unassembled WGS sequence.
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 CDD; cd07067; HP_PGM_like; 1.
DR CDD; cd00817; ValRS_core; 1.
DR Gene3D; 3.40.50.620; HUPs; 2.
DR Gene3D; 3.40.50.1240; Phosphoglycerate mutase-like; 1.
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; IPR013078; His_Pase_superF_clade-1.
DR InterPro; IPR029033; His_PPase_superfam.
DR InterPro; IPR013155; M/V/L/I-tRNA-synth_anticd-bd.
DR InterPro; IPR001345; PG/BPGM_mutase_AS.
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 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; PF00300; His_Phos_1; 1.
DR Pfam; PF00133; tRNA-synt_1; 2.
DR PRINTS; PR00986; TRNASYNTHVAL.
DR SMART; SM00855; PGAM; 1.
DR SUPFAM; SSF47323; Anticodon-binding domain of a subclass of class I aminoacyl-tRNA synthetases; 1.
DR SUPFAM; SSF52374; Nucleotidylyl transferase; 1.
DR SUPFAM; SSF53254; Phosphoglycerate mutase-like; 1.
DR SUPFAM; SSF50677; ValRS/IleRS/LeuRS editing domain; 1.
DR PROSITE; PS00178; AA_TRNA_LIGASE_I; 1.
DR PROSITE; PS00175; PG_MUTASE; 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 20..463
FT /note="Aminoacyl-tRNA synthetase class Ia"
FT /evidence="ECO:0000259|Pfam:PF00133"
FT DOMAIN 629..754
FT /note="Aminoacyl-tRNA synthetase class Ia"
FT /evidence="ECO:0000259|Pfam:PF00133"
FT DOMAIN 795..908
FT /note="Methionyl/Valyl/Leucyl/Isoleucyl-tRNA synthetase
FT anticodon-binding"
FT /evidence="ECO:0000259|Pfam:PF08264"
FT BINDING 453..460
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR613078-2"
FT BINDING 503
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR613078-2"
SQ SEQUENCE 910 AA; 104890 MW; 7E8DE6BC2593991E CRC64;
MSIDERLLKP YDPESTESRI YKLWEESGFF SPEKCIESGV TKSDAKPFTI IMPPPNVTGI
LHMGHASMLT VEDIMIRYHR MKGDRTLWLP GTDHAAIATQ SKVEKEIQKK EGKNRHDLGR
DELVRRIETF AKESHDTIVK QIKIMGSSCD WSREAFTLDE KRSLAVRTMF KQMYDDGLIY
RGHRVINWDP KGQTTVSDDE IVYEERKAKM YTFKYSKDFP ISISTTRPET KVGDTAVAVH
PDDIRYKEYV GKEYDAVFCG VPIHIKIIAD PSVEKDFGTG ALGVTPAHST ADWEMAQRHN
LPLVQVINEY AKMTVTEPSL NGKKTIEARE IIVEWLRKEG LLEKEEEISQ NISTAERTGG
IIEPLPKLQW FVAVNKEITG RGKTLKDLMR EPVASSEIKI IPEYFNKTYF NWIDNLRDWC
ISRQIWYGHR IPVWYDKDGK VHLPKEQKII LARHGESEGN VKKIYSGHQD SPLTEKGVGQ
AEIIGQSLKY GNVTKIISSD LSRAHDTAKI IKNYLNISDD IETLKDLREV DPGEFTNMPT
DGTSIMVKAF ESKEGESYEN LAERAKRVLE RIKTIKTDGS ILIVSHNSFL AALSSLIEER
LDKNSMINMR SDKPLTNTEL REYTLQIVPD PIMEQDPDTL DTWFSSALWT FSTLGWPKKT
KDLEIYHPTD VLETGYEILF FWVARMILFT EYELKTIPFH TIYLHGTIRD AQGRKMSKSL
GNGIDPMDIA AKYGADAGRM ALVIGTAPGT DIKLAEDKIK GYKHFSNKIW NITRFVIENT
NDIDYAHKPE LSINDKELLN ELNNLIHETT DDIDNYRFYL AGEKIYHYVW HRFADIIIED
SKKIFMSSHE SDKISRKWII FEILQNSLKL LHPFMPFVTE ELWQIIQKNN KTLKQENNLL
MVEKWPEQAR
//
