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Database: UniProt
Entry: A0A1Z4G3D3_9CYAN
LinkDB: A0A1Z4G3D3_9CYAN
Original site: A0A1Z4G3D3_9CYAN 
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
//
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