ID A0A1Z4G3D3_9CYAN Unreviewed; 1001 AA.
AC A0A1Z4G3D3;
DT 27-SEP-2017, integrated into UniProtKB/TrEMBL.
DT 27-SEP-2017, sequence version 1.
DT 24-JAN-2024, entry version 25.
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=NIES2098_51240 {ECO:0000313|EMBL:BAY11938.1};
OS Calothrix sp. NIES-2098.
OC Bacteria; Cyanobacteriota; Cyanophyceae; Nostocales; Calotrichaceae;
OC Calothrix.
OX NCBI_TaxID=1954171 {ECO:0000313|EMBL:BAY11938.1, ECO:0000313|Proteomes:UP000218444};
RN [1] {ECO:0000313|EMBL:BAY11938.1, ECO:0000313|Proteomes:UP000218444}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NIES-2098 {ECO:0000313|EMBL:BAY11938.1,
RC ECO:0000313|Proteomes:UP000218444};
RA Hirose Y., Shimura Y., Fujisawa T., Nakamura Y., Kawachi M.;
RT "Genome sequencing of cyanobaciteial culture collection at National
RT Institute for Environmental Studies (NIES).";
RL Submitted (JUN-2017) 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 Membrane {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|HAMAP-Rule:MF_02004}.
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DR EMBL; AP018172; BAY11938.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1Z4G3D3; -.
DR KEGG; caln:NIES2098_51240; -.
DR OrthoDB; 9810365at2; -.
DR Proteomes; UP000218444; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0016020; C:membrane; 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; 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; 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}; 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}.
FT DOMAIN 20..580
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 827..896
FT /note="Cyanobacterial aminoacyl-tRNA synthetase CAAD"
FT /evidence="ECO:0000259|Pfam:PF14159"
FT DOMAIN 936..1000
FT /note="Valyl-tRNA synthetase tRNA-binding arm"
FT /evidence="ECO:0000259|Pfam:PF10458"
FT COILED 934..1001
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 MOTIF 542..546
FT /note="'KMSKS' 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 1001 AA; 113201 MW; 6A8F5D37BB08AC7C CRC64;
MTATTLNLPS LYDPFSTEAK WQKFWEENQV YKADPNHGGE PYCVVIPPPN VTGSLHMGHA
FESALIDVLV RYHRMRGRNT LWLPGTDHAS IAVHTMLEKQ LKTEGKTRYE LGREQFLDRA
KQWKAESGGF IVNQLRRLGV SVDWSRERFT LDEGLSQAVV EAFTRLYAEG LIYRGEYLVN
WCPASQSAVS DVEVENQEVN GNLWHFRYPL TDGSGYVEVA TTRPETMLGD TGVAVNPSDE
RYKHLIGKTV TLPITQREIP IIGDEFVDPT FGTGCVKVTP AHDPNDFEMG KRHNLPFINI
LNKDGTINSN GGEFQGQDRF VARKNVIARL EADGFLVKVE DYKHTVPYSD RGKVPIEPLL
STQWFVKIRP LADRALEFLD QKNSPEFVPH RWTKVYRDWL VKLKDWCISR QLWWGHQIPA
WYAVSETGGQ ITDTTPFVVA KSADEAWEKA KSQFGENVQL EQDPDVLDTW FSSGLWPFST
LGWPQQTQDL ATYYPTNTLV TGFDIIFFWV ARMTMMAGHF TGQMPFKDVY IHGLVLDEKG
QKMSKTKGNG IDPLLLIDKY GTDALRYTLV KEVVGAGQDI RLEYDRKKDE SPSVEASRNF
ANKLWNAARF VMMNLDGQTP QQLGQPLATE LSDRWILSRY HQVVKQTINY IDNYGLGEAA
KGLYEFIWGD FCDWYIELVK SRLQKDADPA SRRVAQQTLA HVLEGILKLL HPFMPHITEE
IWQTLTQQPA TSPQTLSLQP YPQVDSNSIN PEIETQFELL IETIRTIRNL RAEAEIKPGA
KVTVNFQSEN PTERQILTVG QAYIKDLAKV ETLTIADKSN KATVTSKKPL RGLKTIGLII
VAIVFTRLAY TVGNAIDDVP LFGTFFEIVG FGYATWFTSR YLLSAQARQQ LWAKFFPPTL
DKHQPEIEPQ PEPAENAIAG VVGTVQVVIP LKGVVDIEAV RAKLEKSLSK AETEAQSLSA
RLSNANFVDK APKDVVQSAR DALAEAQKQA EILRDRLRGL V
//