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Database: UniProt
Entry: A0A077ELP4_9FLAO
LinkDB: A0A077ELP4_9FLAO
Original site: A0A077ELP4_9FLAO 
ID   A0A077ELP4_9FLAO        Unreviewed;       871 AA.
AC   A0A077ELP4;
DT   29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT   29-OCT-2014, sequence version 1.
DT   24-JAN-2024, entry version 62.
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=BD94_3354 {ECO:0000313|EMBL:AIL47129.1};
OS   Elizabethkingia anophelis NUHP1.
OC   Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales; Weeksellaceae;
OC   Elizabethkingia.
OX   NCBI_TaxID=1338011 {ECO:0000313|EMBL:AIL47129.1, ECO:0000313|Proteomes:UP000028933};
RN   [1] {ECO:0000313|EMBL:AIL47129.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NUHP1 {ECO:0000313|EMBL:AIL47129.1};
RX   PubMed=24012265; DOI=10.1016/S0140-6736(13)61858-9;
RA   Teo J., Tan S.Y., Tay M., Ding Y., Kjelleberg S., Givskov M., Lin R.T.,
RA   Yang L.;
RT   "First case of E anophelis outbreak in an intensive-care unit.";
RL   Lancet 382:855-856(2013).
RN   [2] {ECO:0000313|EMBL:AIL47129.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=NUHP1 {ECO:0000313|EMBL:AIL47129.1};
RX   PubMed=26019164; DOI=10.1093/gbe/evv101;
RA   Li Y., Liu Y., Chew S.C., Tay M., Salido M.M., Teo J., Lauro F.M.,
RA   Givskov M., Yang L.;
RT   "Complete Genome Sequence and Transcriptomic Analysis of the Novel Pathogen
RT   Elizabethkingia anophelis in Response to Oxidative Stress.";
RL   Genome Biol. Evol. 7:1676-1685(2015).
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}.
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DR   EMBL; CP007547; AIL47129.1; -; Genomic_DNA.
DR   RefSeq; WP_024565999.1; NZ_CP007547.1.
DR   AlphaFoldDB; A0A077ELP4; -.
DR   STRING; 1338011.BD94_3354; -.
DR   KEGG; eao:BD94_3354; -.
DR   eggNOG; COG0525; Bacteria.
DR   HOGENOM; CLU_001493_0_2_10; -.
DR   Proteomes; UP000028933; 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: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; 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:SF109; VALYL-TRNA SYNTHETASE; 1.
DR   PANTHER; PTHR11946; VALYL-TRNA SYNTHETASES; 1.
DR   Pfam; PF08264; Anticodon_1; 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          15..572
FT                   /note="Aminoacyl-tRNA synthetase class Ia"
FT                   /evidence="ECO:0000259|Pfam:PF00133"
FT   DOMAIN          615..757
FT                   /note="Methionyl/Valyl/Leucyl/Isoleucyl-tRNA synthetase
FT                   anticodon-binding"
FT                   /evidence="ECO:0000259|Pfam:PF08264"
FT   DOMAIN          807..871
FT                   /note="Valyl-tRNA synthetase tRNA-binding arm"
FT                   /evidence="ECO:0000259|Pfam:PF10458"
FT   MOTIF           43..53
FT                   /note="'HIGH' region"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_02004"
FT   MOTIF           534..538
FT                   /note="'KMSKS' region"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_02004"
FT   BINDING         537
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_02004"
SQ   SEQUENCE   871 AA;  100734 MW;  93BF41F3CAA7F8C9 CRC64;
     MEISDKYNPQ QAEQKWYQYW QENKFFHSEP DEREPYTVVI PPPNVTGILH MGHMLNNTLQ
     DVLVRRARMR GYNACWVPGT DHASIATEAK VVAKLKAEGI SKQDIGREKF LEHAWDWTHQ
     YGGTILEQLK KLGCSCDWDR TRFTMEDDLS KAVIKVFVDL YNKGLVYRGY KMVNWDPEAK
     TNISDEEVIY KEQNGKLYFL KYQIVGSDEF LTVATTRPET IFGDTAVCIN PNDERYTHLK
     GKKVIVPIVG REVPIIEDDY VDIEFGTGAL KITPAHDIND YEIGQRHQLE IIDSMDDNAV
     LNENGKHYQG KDRFTVRKEI AKELEEKGLL LKSEDYLNKV GTSERTGAVI EPKISVQWFL
     KMSELAKPAL DVVMDDEVKF YPEKFKNTYR HWMENVHDWN ISRQLWWGHR IPAYYYASGE
     NDFVVAETIE AALELAKQKT GNAELTTDNL RQDEDALDTW FSAWLWPMSV FDGITAPDNK
     DINYYYPTSD LVTGPDIIFF WVARMIMAGL EFKNQVPFKN VYFTGIVRDK QRRKMSKSLG
     NSPDPIELMD KYGSDGVRVG ILLSSAAGND LMFDEDLMLQ GRNFATKIWN AFKLTQSWKK
     EDKEISEENA QAIEWFEAEF NKTVAAINDQ FEKFRISDAL HLLYKLVWDD FCSWYLEIVK
     PNFGEAISQQ VYDKTIEFFG NLMKFLHPFM PFLTEEIWQA IAERQTSEAL IITQQNKETA
     FNADILKNFE QTKDIVSGVR NYRQSKGISP REEVEVYTNV SQFENEAVIK KLANVSEIHY
     AQKTDKPSFT FLVGAVECSI PLSENLDLGE EKTKTEEELK YLKGFLISVE KKLSNEKFMA
     GAPQQVVDNE LKKQKDAQDK ITLLEEKLKT L
//
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