ID A0A0A7I551_9BIFI Unreviewed; 910 AA.
AC A0A0A7I551;
DT 04-MAR-2015, integrated into UniProtKB/TrEMBL.
DT 04-MAR-2015, sequence version 1.
DT 27-MAR-2024, entry version 51.
DE RecName: Full=Valine--tRNA ligase {ECO:0000256|HAMAP-Rule:MF_02005};
DE EC=6.1.1.9 {ECO:0000256|HAMAP-Rule:MF_02005};
DE AltName: Full=Valyl-tRNA synthetase {ECO:0000256|HAMAP-Rule:MF_02005};
DE Short=ValRS {ECO:0000256|HAMAP-Rule:MF_02005};
GN Name=valS {ECO:0000256|HAMAP-Rule:MF_02005,
GN ECO:0000313|EMBL:AIZ15156.1};
GN ORFNames=AH68_09065 {ECO:0000313|EMBL:AIZ15156.1};
OS Bifidobacterium catenulatum PV20-2.
OC Bacteria; Actinomycetota; Actinomycetes; Bifidobacteriales;
OC Bifidobacteriaceae; Bifidobacterium.
OX NCBI_TaxID=1447716 {ECO:0000313|EMBL:AIZ15156.1, ECO:0000313|Proteomes:UP000030625};
RN [1] {ECO:0000313|EMBL:AIZ15156.1, ECO:0000313|Proteomes:UP000030625}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PV20-2 {ECO:0000313|EMBL:AIZ15156.1,
RC ECO:0000313|Proteomes:UP000030625};
RX PubMed=25614572;
RA Vazquez-Gutierrez P., Lacroix C., Chassard C., Klumpp J., Jans C.,
RA Stevens M.J.;
RT "Complete and Assembled Genome Sequence of Bifidobacterium kashiwanohense
RT PV20-2, Isolated from the Feces of an Anemic Kenyan Infant.";
RL Genome Announc. 3:0-0(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_02005}.
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_02005};
CC -!- SUBUNIT: Monomer. {ECO:0000256|HAMAP-Rule:MF_02005}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_02005}.
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_02005}.
CC -!- SIMILARITY: Belongs to the class-I aminoacyl-tRNA synthetase family.
CC ValS type 2 subfamily. {ECO:0000256|HAMAP-Rule:MF_02005}.
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DR EMBL; CP007456; AIZ15156.1; -; Genomic_DNA.
DR RefSeq; WP_039199287.1; NZ_CP007456.1.
DR AlphaFoldDB; A0A0A7I551; -.
DR STRING; 1447716.AH68_09065; -.
DR KEGG; bka:AH68_09065; -.
DR HOGENOM; CLU_001493_0_2_11; -.
DR OrthoDB; 9810365at2; -.
DR Proteomes; UP000030625; 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 Gene3D; 3.40.50.620; HUPs; 2.
DR HAMAP; MF_02005; Val_tRNA_synth_type2; 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; IPR009080; tRNAsynth_Ia_anticodon-bd.
DR InterPro; IPR009008; Val/Leu/Ile-tRNA-synth_edit.
DR InterPro; IPR022874; Valine-tRNA_ligase_type_2.
DR InterPro; IPR002303; Valyl-tRNA_ligase.
DR InterPro; IPR048044; Valyl-tRNA_ligase_actino.
DR NCBIfam; NF000540; alt_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; PF00133; tRNA-synt_1; 2.
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; 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_02005};
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|HAMAP-
KW Rule:MF_02005};
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490, ECO:0000256|HAMAP-Rule:MF_02005};
KW Ligase {ECO:0000256|ARBA:ARBA00022598, ECO:0000256|HAMAP-Rule:MF_02005};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP-
KW Rule:MF_02005};
KW Protein biosynthesis {ECO:0000256|ARBA:ARBA00022917, ECO:0000256|HAMAP-
KW Rule:MF_02005}.
FT DOMAIN 31..114
FT /note="Aminoacyl-tRNA synthetase class Ia"
FT /evidence="ECO:0000259|Pfam:PF00133"
FT DOMAIN 138..635
FT /note="Aminoacyl-tRNA synthetase class Ia"
FT /evidence="ECO:0000259|Pfam:PF00133"
FT DOMAIN 690..846
FT /note="Methionyl/Valyl/Leucyl/Isoleucyl-tRNA synthetase
FT anticodon-binding"
FT /evidence="ECO:0000259|Pfam:PF08264"
FT REGION 878..910
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 58..68
FT /note="'HIGH' region"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02005"
FT MOTIF 600..604
FT /note="'KMSKS' region"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02005"
FT BINDING 603
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02005"
SQ SEQUENCE 910 AA; 102232 MW; 050359F79DCE16DB CRC64;
MTESQDNTIN ANLTPLPDKV GVDGLEDKWR GVWDENEVYK FQGTRDRKAV YSIDTPPPTV
SGHLHVGHVF SYTHTDVIAR FKRMNGYDVF YPMGWDDNGL PTERRVQNYY GVRVDTSLKY
DPDFVPPFEG TDGKKIDAKD QVPISRKNFI ELCEKLTAQD EKQFEALWRS LGLSIDWTQT
YHTIGEHPQR VAQKAFLRNL ARGEAYQKDA PGLWDVTFQT AVAQAELESR EYPGFYHKVA
FRFEDGTPIY IETTRPELLA ACGALIAHPD DERYKQYFGQ YVYSPLFHVK VPILAHKAAE
MDKGAGIAMC CTFGDVTDVE WWRDLNLPLR SIIQRNGRIV MDTPDWIEDE EGKRIFQETA
GKTTFSARKV IVDALRESGD LDGEPTPTKR MANFYEKGDK PLEIVTSRQW YLKNGGTDQQ
LNAELIERGR ELNFHPDFMR VRYENWVNGL NGDWLISRQR FFGVPFPLWY PVNEDGTADY
DHPIVPSEDR LPIDPTDDVP EGYSEDQRDV PGGFTAEPDI MDTWATSSLT PQIVTRWEEP
GEENQAIFNA TFPMDLRPQG QDIIRTWLFS TVDRAHLENK CLPWANATLS GWILDPDHKK
MSKSKGNVVV PDKPIKQFGA DAVRYWAAAA RLGLDATYDE GQMKIGRRLA IKLLNATKFA
LAIGREDENH HVGAPATANW NPADVTEPLD RAAMAKMALV VREATESLNN YEHSKALEVI
ENYFWQFCDD YIELVKNRAY GTADATGRVP SEKAVKSART ALGLGLDAFA RLLAPYLPYA
TEEVWSWMHE GEGSVHHAAW PKAETYDAAA AAVSPELLTH AGEALAALRG IKSKAKVSMK
TPILSVQLGV SDEARKSIES ALGDIAEAGR VVGRISFTSP AASEGEDEAA TDVTIVESEL
GEPPAKKPKK
//
