ID F2LW48_HIPMA Unreviewed; 873 AA.
AC F2LW48;
DT 31-MAY-2011, integrated into UniProtKB/TrEMBL.
DT 31-MAY-2011, sequence version 1.
DT 27-MAR-2024, entry version 74.
DE RecName: Full=Valine--tRNA ligase {ECO:0000256|HAMAP-Rule:MF_02004};
DE EC=6.1.1.9 {ECO:0000256|HAMAP-Rule:MF_02004};
DE AltName: Full=Valyl-tRNA synthetase {ECO:0000256|HAMAP-Rule:MF_02004};
DE Short=ValRS {ECO:0000256|HAMAP-Rule:MF_02004};
GN Name=valS {ECO:0000256|HAMAP-Rule:MF_02004};
GN OrderedLocusNames=Hipma_1016 {ECO:0000313|EMBL:AEA33982.1};
OS Hippea maritima (strain ATCC 700847 / DSM 10411 / MH2).
OC Bacteria; Campylobacterota; Desulfurellia; Desulfurellales; Hippeaceae;
OC Hippea.
OX NCBI_TaxID=760142 {ECO:0000313|EMBL:AEA33982.1, ECO:0000313|Proteomes:UP000008139};
RN [1] {ECO:0000313|EMBL:AEA33982.1, ECO:0000313|Proteomes:UP000008139}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700847 / DSM 10411 / MH2
RC {ECO:0000313|Proteomes:UP000008139};
RX PubMed=21886857;
RA Huntemann M., Lu M., Nolan M., Lapidus A., Lucas S., Hammon N.,
RA Deshpande S., Cheng J.F., Tapia R., Han C., Goodwin L., Pitluck S.,
RA Liolios K., Pagani I., Ivanova N., Ovchinikova G., Pati A., Chen A.,
RA Palaniappan K., Land M., Hauser L., Jeffries C.D., Detter J.C.,
RA Brambilla E.M., Rohde M., Spring S., Goker M., Woyke T., Bristow J.,
RA Eisen J.A., Markowitz V., Hugenholtz P., Kyrpides N.C., Klenk H.P.,
RA Mavromatis K.;
RT "Complete genome sequence of the thermophilic sulfur-reducer Hippea
RT maritima type strain (MH(2)).";
RL Stand. Genomic Sci. 4:303-311(2011).
RN [2] {ECO:0000313|Proteomes:UP000008139}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700847 / DSM 10411 / MH2
RC {ECO:0000313|Proteomes:UP000008139};
RG US DOE Joint Genome Institute (JGI-PGF);
RA Lucas S., Copeland A., Lapidus A., Bruce D., Goodwin L., Pitluck S.,
RA Peters L., Kyrpides N., Mavromatis K., Pagani I., Ivanova N.,
RA Mikhailova N., Lu M., Detter J.C., Tapia R., Han C., Land M., Hauser L.,
RA Markowitz V., Cheng J.-F., Hugenholtz P., Woyke T., Wu D., Spring S.,
RA Schroeder M., Brambilla E., Klenk H.-P., Eisen J.A.;
RT "The complete genome of Hippea maritima DSM 10411.";
RL Submitted (MAR-2011) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Catalyzes the attachment of valine to tRNA(Val). As ValRS can
CC inadvertently accommodate and process structurally similar amino acids
CC such as threonine, to avoid such errors, it has a 'posttransfer'
CC editing activity that hydrolyzes mischarged Thr-tRNA(Val) in a tRNA-
CC dependent manner. {ECO:0000256|HAMAP-Rule:MF_02004}.
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, ECO:0000256|HAMAP-
CC Rule:MF_02004};
CC -!- SUBUNIT: Monomer. {ECO:0000256|HAMAP-Rule:MF_02004}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_02004}.
CC -!- DOMAIN: The C-terminal coiled-coil domain is crucial for aminoacylation
CC activity. {ECO:0000256|HAMAP-Rule:MF_02004}.
CC -!- DOMAIN: ValRS has two distinct active sites: one for aminoacylation and
CC one for editing. The misactivated threonine is translocated from the
CC active site to the editing site. {ECO:0000256|HAMAP-Rule:MF_02004}.
CC -!- SIMILARITY: Belongs to the class-I aminoacyl-tRNA synthetase family.
CC ValS type 1 subfamily. {ECO:0000256|HAMAP-Rule:MF_02004}.
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DR EMBL; CP002606; AEA33982.1; -; Genomic_DNA.
DR RefSeq; WP_013682021.1; NC_015318.1.
DR AlphaFoldDB; F2LW48; -.
DR STRING; 760142.Hipma_1016; -.
DR KEGG; hmr:Hipma_1016; -.
DR eggNOG; COG0525; Bacteria.
DR HOGENOM; CLU_001493_0_2_7; -.
DR InParanoid; F2LW48; -.
DR OrthoDB; 9810365at2; -.
DR Proteomes; UP000008139; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0002161; F:aminoacyl-tRNA editing activity; IEA:InterPro.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0004832; F:valine-tRNA ligase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0006438; P:valyl-tRNA aminoacylation; IEA:UniProtKB-UniRule.
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; 1.
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|HAMAP-Rule:MF_02004};
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|HAMAP-
KW Rule:MF_02004}; Coiled coil {ECO:0000256|HAMAP-Rule:MF_02004};
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490, ECO:0000256|HAMAP-Rule:MF_02004};
KW Ligase {ECO:0000256|ARBA:ARBA00022598, ECO:0000256|HAMAP-Rule:MF_02004};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP-
KW Rule:MF_02004};
KW Protein biosynthesis {ECO:0000256|ARBA:ARBA00022917, ECO:0000256|HAMAP-
KW Rule:MF_02004}; Reference proteome {ECO:0000313|Proteomes:UP000008139}.
FT DOMAIN 13..561
FT /note="Aminoacyl-tRNA synthetase class Ia"
FT /evidence="ECO:0000259|Pfam:PF00133"
FT DOMAIN 604..747
FT /note="Methionyl/Valyl/Leucyl/Isoleucyl-tRNA synthetase
FT anticodon-binding"
FT /evidence="ECO:0000259|Pfam:PF08264"
FT DOMAIN 804..869
FT /note="Valyl-tRNA synthetase tRNA-binding arm"
FT /evidence="ECO:0000259|Pfam:PF10458"
FT COILED 802..829
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02004"
FT MOTIF 42..52
FT /note="'HIGH' region"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02004"
FT MOTIF 521..525
FT /note="'KMSKS' region"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02004"
FT BINDING 524
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02004"
SQ SEQUENCE 873 AA; 101714 MW; 2E2E97C766870F24 CRC64;
MDETKYSPSF ETKWYEFWEK NGYFQPANKE GKENFSIVIP PPNVTGALHI GHALNGTLQD
IMVRYKRMKG YNVLWVPGTD HAGIATQNMV EKDLASKGIK KEDLGREKFV EKVWEWKEKY
GNRIINQIKR LGLSCDWSRL RFTMDEQLSK AVRKVFVQLY KEGLIYKDKY IINWCPRCHT
ALSDLEVEHK DETGKLYYIE YPFEDGSGGV VVATTRPETM FGDTAVAVNP NDERYKDVIG
KNVVLPIKDK LIPIIADEYV DMEFGTGVVK ITPAHDPNDF EVGRRHNLDI VVAIDDYGKM
TDEALHFKGM DRFECRSKLV AELEGKGFIK NVAEIKHAVG QCYRCHTTIE PYVSEQWFVK
TKPLAEPAIE AVKNGDTRFV PKNWEKTYFE WMYNIKDWCI SRQLWWGHRI PVWKCEDCGK
YTVSEDEPKA CEHCGSDKLV QEEDVLDTWF SSALWPMSTL GWPNQTDDLK RFYPTSLLVT
GFDIIFFWVA RMMMMGLHFM KDVPFRDVYI HALVRDQYGQ KMSKTKGNVI DPLEVVEKYG
ADSMRFTLAI LAAQGRDIKL SEDKIEGYKR FMNKIWNAYR FIKINTEGME LKEKPKKLSP
ASIWIKSRLA KTIRKVEQSL SEYKFNEAAS AIYQFIWHEF CDYYIEMSKV HMDDEFSYSI
KFTLLEVFEA TLRLLHPFTP FITEELWQKL PNKKGDSIII AEYPEYKESM ISEDIEAAMD
IVLDTIRSIR NLRSENNIQP SKKIKVYMKV EDEKTQSIII NFKNYVYALA GVDNLIMTNK
PDEECIVQST IYGDIFLPVE GNIDVKKEVE RLTKLIKKQE KSLSFLNSKL NNQAFLEKAP
KELIEQKKAE FEDVSRLYQK TKSRLEQLKG LVE
//
