ID A0A1G2VNR3_9BACT Unreviewed; 849 AA.
AC A0A1G2VNR3;
DT 15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT 15-FEB-2017, sequence version 1.
DT 27-MAR-2024, entry version 31.
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=A3J67_04245 {ECO:0000313|EMBL:OHB23274.1};
OS Parcubacteria group bacterium RIFCSPHIGHO2_02_FULL_48_10b.
OC Bacteria.
OX NCBI_TaxID=1817741 {ECO:0000313|EMBL:OHB23274.1, ECO:0000313|Proteomes:UP000177975};
RN [1] {ECO:0000313|EMBL:OHB23274.1, ECO:0000313|Proteomes:UP000177975}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=27774985; DOI=10.1038/ncomms13219;
RA Anantharaman K., Brown C.T., Hug L.A., Sharon I., Castelle C.J.,
RA Probst A.J., Thomas B.C., Singh A., Wilkins M.J., Karaoz U., Brodie E.L.,
RA Williams K.H., Hubbard S.S., Banfield J.F.;
RT "Thousands of microbial genomes shed light on interconnected biogeochemical
RT processes in an aquifer system.";
RL Nat. Commun. 7:13219-13219(2016).
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:OHB23274.1}.
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DR EMBL; MHXF01000026; OHB23274.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1G2VNR3; -.
DR Proteomes; UP000177975; 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; cd00817; ValRS_core; 1.
DR Gene3D; 3.40.50.620; HUPs; 2.
DR Gene3D; 2.30.130.30; Hypothetical protein; 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; 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 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; 2.
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 15..440
FT /note="Aminoacyl-tRNA synthetase class Ia"
FT /evidence="ECO:0000259|Pfam:PF00133"
FT DOMAIN 578..702
FT /note="Aminoacyl-tRNA synthetase class Ia"
FT /evidence="ECO:0000259|Pfam:PF00133"
FT DOMAIN 753..833
FT /note="Methionyl/Valyl/Leucyl/Isoleucyl-tRNA synthetase
FT anticodon-binding"
FT /evidence="ECO:0000259|Pfam:PF08264"
SQ SEQUENCE 849 AA; 98316 MW; 5A8997EB4F50C2DB CRC64;
MLDKAYDPKN VEREIYARWE KSGYFNPDKL PKRGNRETGK RRNKPYVILM PLPNVTGSLH
IGHVLDQTIQ DLLTRWHRMR GFRALWLPGT DHAGIATQNV VEKELRKQGV SRFGLGREKF
IEKTWEWKQK YGAVIENQER LLGNSCDWSR NRFTMDPAYA EAVKNAFTHY YNKGLIYRGK
RVVNWCTRCG TSLSELEIEY KEEKARLYYI RYPIENESGN YIVVATTRPE TMLGDCAVAV
HSKDARYTGY VGKNVLLPIH DRLIPIITDK GVEQDFGTGA VKVTPSHDML DAEIAERHTL
PFLDIINERG RMTAHAGELF EDLKTDECRE RVTGMLREKN LIEKEEEYSH NLAICYRCGG
ALEPQRSNQW FVRMRERPRG QKTQMSLREM AYKAVQSGKV KILPKNYEKP YFAWLKDIKD
WCVSRQIWWG HRIPAWYCGL AEARLPVMGF NERIVPQVLG GKKTKTHRVR DHRLNVGDKV
AFENSQTKAL FGYGIITEIE QTRVADLVPM TDPSHGTLYK TTKDIITAFK RYNPDRKVTL
DTIVITYTYS FTPITEKHSR EGCGNILVSS EKPKKCPACG GTNLTQTPDV LDTWFSSALW
PFAARSKRDL EQYYPTDVLV TARDILNLWV ARMIFSGTEF KQQPPFHTVL IHGTVLTKEG
KRMSKSLGTG VDPLMLIEQY GTDALRFAVI WQSMGQQDIR WSEEALIAGK KFANKLWNAS
RFVLMRLDGK KATKKELGST LLKFPARDKN ASTIYREYKR MVQSMEKDIA AYRLGHALHR
LYDFFWHRFC DRAIEEFKDK EGIDAKLFLL ALLVEQLKIL HPFMPFATEY IYSFIPITDK
NLLMVEQIN
//
