ID H8MHV3_CORCM Unreviewed; 1170 AA.
AC H8MHV3;
DT 16-MAY-2012, integrated into UniProtKB/TrEMBL.
DT 16-MAY-2012, sequence version 1.
DT 24-JAN-2024, entry version 70.
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 ECO:0000313|EMBL:AFE10628.1};
GN OrderedLocusNames=COCOR_03319 {ECO:0000313|EMBL:AFE10628.1};
OS Corallococcus coralloides (strain ATCC 25202 / DSM 2259 / NBRC 100086 / M2)
OS (Myxococcus coralloides).
OC Bacteria; Myxococcota; Myxococcia; Myxococcales; Cystobacterineae;
OC Myxococcaceae; Corallococcus.
OX NCBI_TaxID=1144275 {ECO:0000313|EMBL:AFE10628.1, ECO:0000313|Proteomes:UP000007587};
RN [1] {ECO:0000313|EMBL:AFE10628.1, ECO:0000313|Proteomes:UP000007587}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 25202 / DSM 2259 / NBRC 100086 / M2
RC {ECO:0000313|Proteomes:UP000007587};
RX PubMed=22582372; DOI=10.1128/JB.00397-12;
RA Huntley S., Zhang Y., Treuner-Lange A., Kneip S., Sensen C.W.,
RA Sogaard-Andersen L.;
RT "Complete Genome Sequence of the Fruiting Myxobacterium Corallococcus
RT coralloides DSM 2259.";
RL J. Bacteriol. 194:3012-3013(2012).
RN [2] {ECO:0000313|Proteomes:UP000007587}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 25202 / DSM 2259 / NBRC 100086 / M2
RC {ECO:0000313|Proteomes:UP000007587};
RA Huntley S., Zhang Y., Treuner-Lange A., Sensen C.W., Sogaard-Andersen L.;
RT "Genome sequence of the fruiting myxobacterium Corallococcus coralloides
RT DSM 2259.";
RL Submitted (MAR-2012) 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 -!- FUNCTION: Might have a role in establishing the nucleoid structure of
CC elementary bodies. {ECO:0000256|ARBA:ARBA00002344}.
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}.
CC -!- SIMILARITY: Belongs to the histone H1/H5 family. HCT subfamily.
CC {ECO:0000256|ARBA:ARBA00008424}.
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DR EMBL; CP003389; AFE10628.1; -; Genomic_DNA.
DR RefSeq; WP_014396134.1; NC_017030.1.
DR AlphaFoldDB; H8MHV3; -.
DR STRING; 1144275.COCOR_03319; -.
DR KEGG; ccx:COCOR_03319; -.
DR eggNOG; COG0525; Bacteria.
DR HOGENOM; CLU_001493_0_2_7; -.
DR InParanoid; H8MHV3; -.
DR OMA; FATKLWN; -.
DR OrthoDB; 9810365at2; -.
DR Proteomes; UP000007587; 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:0003677; F:DNA binding; IEA:InterPro.
DR GO; GO:0030527; F:structural constituent of chromatin; IEA:InterPro.
DR GO; GO:0004832; F:valine-tRNA ligase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0030261; P:chromosome condensation; IEA:InterPro.
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 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; IPR009970; HC2.
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; PF07382; HC2; 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:UP000007587}.
FT DOMAIN 20..599
FT /note="Aminoacyl-tRNA synthetase class Ia"
FT /evidence="ECO:0000259|Pfam:PF00133"
FT DOMAIN 643..792
FT /note="Methionyl/Valyl/Leucyl/Isoleucyl-tRNA synthetase
FT anticodon-binding"
FT /evidence="ECO:0000259|Pfam:PF08264"
FT DOMAIN 851..915
FT /note="Valyl-tRNA synthetase tRNA-binding arm"
FT /evidence="ECO:0000259|Pfam:PF10458"
FT REGION 910..997
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1034..1170
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 849..876
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02004"
FT MOTIF 48..58
FT /note="'HIGH' region"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02004"
FT MOTIF 539..543
FT /note="'KMSKS' region"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02004"
FT COMPBIAS 961..984
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1064..1078
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1079..1170
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 542
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02004"
SQ SEQUENCE 1170 AA; 129550 MW; 109025503281980A CRC64;
MTDTTELSKA YEPSEVEARW YNHWLERDYF RAEAPSSKPP FSIVLPPPNV TGSLHIGHAL
TATIQDILTR WKRMSGFNAL WLPGTDHAGI ATQMVVEKEL KKTEGKSRHD LGREAFLERV
WTWKGKFGAR IGEQHRYLGA SLDWSRERFT MDEQSSAAVR EVFVRLYEEG LMYRAQKLIN
WCPSCRTALS DLEVEHEEKN GSLWHIRYPV KGTERFLTVA TTRPETLLGD TAVAVHPEDP
RYQDLIGKSV ALPLTDREIP VIADAELVNM EFGTGVVKVT PAHDFNDYQT GLRHKLPMLS
ILDEAARMTK DTGKYAGVDR TEARKQVLAD LTELGLLEKE EPHKLNVGTC QRCATVVEPR
LSPQWFIKIE PLAKPAIQAV EEGRTKFVPE SWTNTYFHWM NNIHDWCVSR QLWWGHQIPA
WYCAACTPAE ERSKDTADVI VSRTPPESCP KCGGKELTQD PDVLDTWFSS ALWPFSTLGW
PKQTADLQTF YPTSVMETGH DIIFFWVARM MMMGLHFMGD VPFRTVYLHA MVRDEKGEKM
SKTKGNVIDP LDVILGAKAD ALQPSLRNRF PQGMPAHGAD ALRFTLASLT QQGRDIKLSM
DRLGGYKAFC NKLWNASRFA LMNMGDFSLD KTPLEGRKLT LADRWILSRL QKATEETRAS
LEAFGFAEAA STLYQFLWAE FCDWYIELAK GSLYGEDAEA KDTTRAVLVT CLDRILRLMH
PFMPFITEEI WQKLPMSRPT ESICIAAYPE PETAWVDAAA EGEMAPVIAA IEGLRTLRGE
SNLPPSAKVK AVVQSPDATT RELLERWRAY LMPLAGLSEV VVGPPGAKPP QAAAFVSGNL
EIYVPLAGLV DLDAERDRLK KEIARAEQEL AALQRKLDNP NFVARAPPDV VEKDKARVTE
LQERTVKLQD HLQRIAPEPP MSETPSPLPG STESEAPEAS ESPAPETVQV PESAQVKVAA
EPRAPKDEAV NLGQELKGEI EAEEAAQEPQ AADPVVEEAL NKLREGTKEG LSAADHHDLG
VAYMSMGLVD DAMREFDRAK EGGDTREAPE GSAAPVKKAP AKKASAKKAA EKKTAVKKAA
GKKTAAKKAA VKKAPAKKAA GKKSAVKKAP AKKASAKKAA GKKTAAKKAA VKKAPAKKAS
AKKAAGKKTA AKKAVAKKTT RGKPARKTRR
//