ID G6FV55_9CYAN Unreviewed; 1000 AA.
AC G6FV55;
DT 25-JAN-2012, integrated into UniProtKB/TrEMBL.
DT 25-JAN-2012, sequence version 1.
DT 18-JUN-2025, entry version 72.
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 ORFNames=FJSC11DRAFT_2752 {ECO:0000313|EMBL:EHC12110.1};
OS Fischerella thermalis JSC-11.
OC Bacteria; Bacillati; Cyanobacteriota; Cyanophyceae; Nostocales;
OC Hapalosiphonaceae; Fischerella.
OX NCBI_TaxID=741277 {ECO:0000313|EMBL:EHC12110.1, ECO:0000313|Proteomes:UP000004344};
RN [1] {ECO:0000313|EMBL:EHC12110.1, ECO:0000313|Proteomes:UP000004344}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JSC-11 {ECO:0000313|EMBL:EHC12110.1,
RC ECO:0000313|Proteomes:UP000004344};
RG US DOE Joint Genome Institute (JGI-PGF);
RA Lucas S., Han J., Lapidus A., Cheng J.-F., Goodwin L., Pitluck S.,
RA Peters L., Land M.L., Hauser L., Sarkisova S., Bryant D.A., Brown I.,
RA Woyke T.J.;
RT "The draft genome of Fischerella sp. JSC-11.";
RL Submitted (SEP-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=tRNA(Val) + L-valine + ATP = L-valyl-tRNA(Val) + AMP +
CC diphosphate; 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:ARBA00047552, ECO:0000256|HAMAP-
CC Rule:MF_02004};
CC -!- SUBUNIT: Monomer. {ECO:0000256|ARBA:ARBA00011245, ECO:0000256|HAMAP-
CC Rule:MF_02004}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496,
CC ECO:0000256|HAMAP-Rule:MF_02004}. Membrane
CC {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein
CC {ECO:0000256|ARBA:ARBA00004141}.
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|ARBA:ARBA00060830,
CC ECO:0000256|HAMAP-Rule:MF_02004}.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|HAMAP-Rule:MF_02004}.
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:EHC12110.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AGIZ01000008; EHC12110.1; -; Genomic_DNA.
DR RefSeq; WP_009457475.1; NZ_AGIZ01000008.1.
DR AlphaFoldDB; G6FV55; -.
DR PATRIC; fig|741277.3.peg.2326; -.
DR Proteomes; UP000004344; Unassembled WGS sequence.
DR GO; GO:0005829; C:cytosol; IEA:TreeGrafter.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0002161; F:aminoacyl-tRNA deacylase 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 FunFam; 1.10.287.380:FF:000001; Valine--tRNA ligase; 1.
DR FunFam; 3.40.50.620:FF:000032; Valine--tRNA ligase; 1.
DR FunFam; 3.40.50.620:FF:000098; Valine--tRNA ligase; 1.
DR FunFam; 3.90.740.10:FF:000005; Valine--tRNA ligase, mitochondrial; 1.
DR Gene3D; 3.40.50.620; HUPs; 2.
DR Gene3D; 1.10.730.10; Isoleucyl-tRNA Synthetase, Domain 1; 1.
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; IPR025564; CAAD_dom.
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; NF004349; PRK05729.1; 1.
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; PF14159; CAAD; 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};
KW Coiled coil {ECO:0000256|ARBA:ARBA00023054, ECO:0000256|HAMAP-
KW 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:UP000004344}.
FT DOMAIN 20..582
FT /note="Aminoacyl-tRNA synthetase class Ia"
FT /evidence="ECO:0000259|Pfam:PF00133"
FT DOMAIN 633..784
FT /note="Methionyl/Valyl/Leucyl/Isoleucyl-tRNA synthetase
FT anticodon-binding"
FT /evidence="ECO:0000259|Pfam:PF08264"
FT DOMAIN 828..897
FT /note="Cyanobacterial aminoacyl-tRNA synthetase CAAD"
FT /evidence="ECO:0000259|Pfam:PF14159"
FT DOMAIN 935..1000
FT /note="Valyl-tRNA synthetase tRNA-binding arm"
FT /evidence="ECO:0000259|Pfam:PF10458"
FT COILED 940..995
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02004"
FT MOTIF 49..59
FT /note="'HIGH' region"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02004"
FT BINDING 545
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02004"
SQ SEQUENCE 1000 AA; 113672 MW; 7AF8A9019F6057E6 CRC64;
MTATITNLPD RYDPFTTEAK WQKFWEENQT YKADPHAGGE PYCIVIPPPN VTGSLHMGHA
FDNSLIDTLV RYHRMKGDNA LYLPGTDHAS IAVHTMLEKQ LKVEGKTRYE LGREKFLERA
WQWKRESGGT IVNQLRRLGV SVDWSRERFT LDAGLSKAVL EAFNRLYEEG LIYRGKYLVN
WCPESQSAVS DLEVDAKEVD GHLWHFRYPL SDGSGYVEVA TTRPETMLGD TAVAVNPNDE
RYQHLIGKTI TLPIMNREIP IIGDELVDPT FGTGCVKVTP AHDPNDFEMG KRHSLPFINI
MNKDGSLNEN AGEFQGQDRF VARKNVVARL EADGFLVKVE DYKHSVPYSE RGKVPVEPLL
STQWFVKIRP LADRALEFLD EKNSPRFVPQ RWTKVYRDWL VKLKDWCISR QLWWGHQIPA
WYAVSETGGE ITENTPFVVA RSETEARERL KSQFGENVKV EQDPDVLDTW FSSGLWPFST
LGWPEQTPDL ATYYPTSTLV TGFDIIFFWV ARMTMMAGHF TGQMPFKDVY IHGLVLDENG
QKQSKTKGNG IDPLILIEKY GTDALRYTMI KEVAGAGQDI RMDYNRKTDE SPSVEASRNF
ANKLWNAARF VMMNLDGQTP QQLGEPNPTE LSDRWILSRY HRVVQQTRNY LDNYGLGEAA
KGLYEFIWGD FCDWYIELVK SRLQKNADPI SRRVAQQTLA YVLEGILKLL SPFMPHITEE
IWHTLTQQGA ETKQSLSRQL YPEAQTNFID SELEEQFELL IATIRTIRNL RAEADVKPGA
RVNVNLQTDS KKERQILTAG QSYIQDLAKV ENLTITGGES QQPTEKPRIG WENIAVTIAL
IYFFRLGLAI ADAVDDIPLL GSFFEVIGFG YATWFVGQNI LSAEARQKFW QQLFKPSAEQ
MASSEVSPQP QAPEKAIAGV VGTVQVLLPL AGVVDIDAYV AKLQKRLTKL EGEIKSLSGR
LSNPKFVEQA PPNVVRETRD ALAEAQKQAE ILRDRLRQLA
//
