ID A0A177QFT8_9PLAN Unreviewed; 1082 AA.
AC A0A177QFT8;
DT 07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT 07-SEP-2016, sequence version 1.
DT 27-MAR-2024, entry version 30.
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=AYO44_11715 {ECO:0000313|EMBL:OAI46239.1};
OS Planctomycetaceae bacterium SCGC AG-212-F19.
OC Bacteria; Planctomycetota; Planctomycetia; Planctomycetales;
OC Planctomycetaceae.
OX NCBI_TaxID=1799658 {ECO:0000313|EMBL:OAI46239.1, ECO:0000313|Proteomes:UP000186541};
RN [1] {ECO:0000313|Proteomes:UP000186541}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SCGC AG-212-F19 {ECO:0000313|Proteomes:UP000186541};
RA Choi J., Stepanauskas R., Howe A.;
RL Submitted (FEB-2016) 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}.
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:OAI46239.1}.
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DR EMBL; LSTD01000287; OAI46239.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A177QFT8; -.
DR Proteomes; UP000186541; Unassembled WGS sequence.
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 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 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 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:UP000186541}.
FT DOMAIN 18..485
FT /note="Aminoacyl-tRNA synthetase class Ia"
FT /evidence="ECO:0000259|Pfam:PF00133"
FT DOMAIN 561..681
FT /note="Aminoacyl-tRNA synthetase class Ia"
FT /evidence="ECO:0000259|Pfam:PF00133"
FT DOMAIN 800..957
FT /note="Methionyl/Valyl/Leucyl/Isoleucyl-tRNA synthetase
FT anticodon-binding"
FT /evidence="ECO:0000259|Pfam:PF08264"
FT DOMAIN 1017..1080
FT /note="Valyl-tRNA synthetase tRNA-binding arm"
FT /evidence="ECO:0000259|Pfam:PF10458"
FT REGION 1033..1059
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 243..278
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02004"
FT MOTIF 46..56
FT /note="'HIGH' region"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02004"
FT COMPBIAS 1038..1059
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 646
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02004"
SQ SEQUENCE 1082 AA; 123379 MW; F72462FD2726085A CRC64;
MAMDLPKTYD PHEAQQRWLA FWEQHGYWHS RPDPNRKPFT IVIPPPNVTG ALHMGHALNN
TLQDVLIRYH RAKGDNTLWM PGTDHAGIAT QAVVEKRVLA EEGKTRHDLG REELVRRIWK
WKDEYEKRIL GQLRELGASL DWARTRFTLD EVCARAVRQT FFNLFSDGLI YRGKRLVNWD
AFLQTSVADD EVDNVEQEAE FSYFRYPFAD GKSHEGLDHV LIATTRPETM LGDTAVAVHP
DPRRELDKRT QELQAKLAKA DEKEKKEIQE RLKRLALRQD EMLPHLENLA ALARAGTMLE
LPLVGRKISL IADFYADPEK GTGAVKITPA HDFNDYQVGD RHPETGEPIN ILHPDGRIND
EGQGRFRGEN FSYVGLDRFE ARKRVAADLD RLGLLDRVEK ITNTIPISDR SKTPIEPYLS
DQWFVKMADL AQSAIDAVNN GRVQFFPERY AQMYLEWLGQ KRDWCISRQL WWGHQIPVWS
IACADTKALD EVRGVLASHP KIAERVGQGS VAFQVQLDEE VQKLLKKGAT PPADRPYGFV
QICLRDDEQT DIIGLLKPYN PQRDPDVLDT WFSSALWPHS TLGWPEPTPE LKYYYPTSVL
VTSRDIITLW VARMVITGLY NCKAVPFRHV YIHPKILDGF GETMSKSKGN GVDPLDIISV
YGTDALRFVM VHLATETQDS RLPVGNICPH CGTLLPMKRE HMYMQTRKVI CPAEPVSPDD
PKKKIKCGKP FRPGGPWPAP DPELPTARQG SEKFEMGRNF ANKLWNAARF QLTKPPDKDR
APLDGYQPEA IRIAELPIED RWILSRLASV TAEITAAMES YHFSDAARLI YDFFWSEFCD
WYVEMSKGRL TDPAARPLTQ RMLVGVLDAS LRLVQPIMPF VAESIWQYLN EVAFERGLPN
PEPAAESVVI APWPAFPAAW KDPAMEQRIA RMQELIRFVR EVRNRYMLDA KTSLDVFVRC
NETIAADFRM LAPFVAQLSG VRQLEAGPQV TKPPQAATHV LADSESYVSL QGLIDPAAES
KRLEKQLAEK KKHLQSTQAK LNNESFRKNA PPEVVQQQVQ QVADLENQIK TIEENLRELG
QR
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