ID   A0A087QDV7_LACGS        Unreviewed;       879 AA.
AC   A0A087QDV7;
DT   29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT   29-OCT-2014, sequence version 1.
DT   27-SEP-2017, 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=HMPREF5175_00651 {ECO:0000313|EMBL:KFL97810.1};
OS   Lactobacillus gasseri SV-16A-US.
OC   Bacteria; Firmicutes; Bacilli; Lactobacillales; Lactobacillaceae;
OC   Lactobacillus.
OX   NCBI_TaxID=575604 {ECO:0000313|EMBL:KFL97810.1, ECO:0000313|Proteomes:UP000030761};
RN   [1] {ECO:0000313|EMBL:KFL97810.1, ECO:0000313|Proteomes:UP000030761}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SV-16A-US {ECO:0000313|EMBL:KFL97810.1,
RC   ECO:0000313|Proteomes:UP000030761};
RG   The Broad Institute Genome Sequencing Platform;
RA   Ward D., Earl A., Feldgarden M., Gevers D., Young S.K., Zeng Q.,
RA   Koehrsen M., Alvarado L., Berlin A., Bochicchio J., Borenstein D.,
RA   Chapman S.B., Chen Z., Engels R., Freedman E., Gellesch M.,
RA   Goldberg J., Griggs A., Gujja S., Heilman E., Heiman D., Hepburn T.,
RA   Howarth C., Jen D., Larson L., Mehta T., Park D., Pearson M.,
RA   Roberts A., Saif S., Shea T., Shenoy N., Sisk P., Stolte C., Sykes S.,
RA   Thomson T., Walk T., White J., Yandava C., Liu Y., Xu Q., Haas B.,
RA   Nusbaum C., Birren B.;
RT   "The Genome Sequence of Lactobacillus gasseri strain SV-16A-US.";
RL   Submitted (MAR-2010) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Catalyzes the attachment of valine to tRNA(Val). As
CC       ValRS can inadvertently accommodate and process structurally
CC       similar amino acids such as threonine, to avoid such errors, it
CC       has a "posttransfer" editing activity that hydrolyzes mischarged
CC       Thr-tRNA(Val) in a tRNA-dependent manner. {ECO:0000256|HAMAP-
CC       Rule:MF_02004, ECO:0000256|SAAS:SAAS00711212}.
CC   -!- CATALYTIC ACTIVITY: ATP + L-valine + tRNA(Val) = AMP + diphosphate
CC       + L-valyl-tRNA(Val). {ECO:0000256|HAMAP-Rule:MF_02004,
CC       ECO:0000256|SAAS:SAAS00711221}.
CC   -!- SUBUNIT: Monomer. {ECO:0000256|HAMAP-Rule:MF_02004,
CC       ECO:0000256|SAAS:SAAS00711188}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_02004,
CC       ECO:0000256|SAAS:SAAS00711246}.
CC   -!- DOMAIN: The C-terminal coiled-coil domain is crucial for
CC       aminoacylation activity. {ECO:0000256|HAMAP-Rule:MF_02004}.
CC   -!- DOMAIN: ValRS has two distinct active sites: one for
CC       aminoacylation and one for editing. The misactivated threonine is
CC       translocated from the active site to the editing site.
CC       {ECO:0000256|HAMAP-Rule:MF_02004}.
CC   -!- SIMILARITY: Belongs to the class-I aminoacyl-tRNA synthetase
CC       family. ValS type 1 subfamily. {ECO:0000256|HAMAP-Rule:MF_02004,
CC       ECO:0000256|SAAS:SAAS00711216}.
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DR   EMBL; KN050674; KFL97810.1; -; Genomic_DNA.
DR   RefSeq; WP_003647090.1; NZ_KN050674.1.
DR   ProteinModelPortal; A0A087QDV7; -.
DR   EnsemblBacteria; KFL97810; KFL97810; HMPREF5175_00651.
DR   GeneID; 29638530; -.
DR   Proteomes; UP000030761; 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; 1.10.287.380; -; 1.
DR   Gene3D; 1.10.730.10; -; 1.
DR   Gene3D; 3.40.50.620; -; 2.
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; IPR019499; Val-tRNA_synth_tRNA-bd.
DR   InterPro; IPR009008; Val/Leu/Ile-tRNA-synth_edit.
DR   InterPro; IPR002303; Valyl-tRNA_ligase.
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; SSF46589; SSF46589; 1.
DR   SUPFAM; SSF47323; SSF47323; 1.
DR   SUPFAM; SSF50677; SSF50677; 1.
DR   TIGRFAMs; TIGR00422; valS; 1.
DR   PROSITE; PS00178; AA_TRNA_LIGASE_I; 1.
PE   3: Inferred from homology;
KW   Aminoacyl-tRNA synthetase {ECO:0000256|HAMAP-Rule:MF_02004,
KW   ECO:0000256|RuleBase:RU363035, ECO:0000256|SAAS:SAAS00711227};
KW   ATP-binding {ECO:0000256|HAMAP-Rule:MF_02004,
KW   ECO:0000256|RuleBase:RU363035, ECO:0000256|SAAS:SAAS00711241};
KW   Coiled coil {ECO:0000256|HAMAP-Rule:MF_02004,
KW   ECO:0000256|SAAS:SAAS00711237};
KW   Complete proteome {ECO:0000313|Proteomes:UP000030761};
KW   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_02004,
KW   ECO:0000256|SAAS:SAAS00711219};
KW   Ligase {ECO:0000256|HAMAP-Rule:MF_02004,
KW   ECO:0000256|RuleBase:RU363035, ECO:0000256|SAAS:SAAS00711254,
KW   ECO:0000313|EMBL:KFL97810.1};
KW   Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_02004,
KW   ECO:0000256|RuleBase:RU363035, ECO:0000256|SAAS:SAAS00711287};
KW   Protein biosynthesis {ECO:0000256|HAMAP-Rule:MF_02004,
KW   ECO:0000256|RuleBase:RU363035, ECO:0000256|SAAS:SAAS00711230}.
FT   DOMAIN       17    560       tRNA-synt_1. {ECO:0000259|Pfam:PF00133}.
FT   DOMAIN      605    752       Anticodon_1. {ECO:0000259|Pfam:PF08264}.
FT   DOMAIN      811    876       Val_tRNA-synt_C. {ECO:0000259|Pfam:
FT                                PF10458}.
FT   COILED      809    839       {ECO:0000256|HAMAP-Rule:MF_02004}.
FT   COILED      851    878       {ECO:0000256|HAMAP-Rule:MF_02004}.
FT   MOTIF        45     55       "HIGH" region. {ECO:0000256|HAMAP-Rule:
FT                                MF_02004}.
FT   MOTIF       521    525       "KMSKS" region. {ECO:0000256|HAMAP-Rule:
FT                                MF_02004}.
FT   BINDING     524    524       ATP. {ECO:0000256|HAMAP-Rule:MF_02004}.
SQ   SEQUENCE   879 AA;  101535 MW;  31CFFAAF25493EC8 CRC64;
     MTDLAPKYNP NEVEKGRYQE WLDEDLFKPS GDKKAHPYSI VIPPPNVTGK LHLGHAWDTA
     IQDTLIRFKR MEGYDTLYLP GMDHAGIATQ AKVEAKLRKQ GKDRHQMGRE AFVKQVWDWK
     DEYANIIKGQ WAKMGLSLDY SRERFTLDKG LSKAVRKVFV QLYNEGLIYR GEYIINWDPE
     LQTALSDIEV IHKDDKGAFY HIKYPFVDGS GFVEIATTRP ETMFGDTAVA VAPGDERYKD
     IVGKELVLPL VGRHIPIIED QHVDPEFGTG LVKITPAHDP NDFQVGNRHN LERINVMNDD
     GTMNEEAGKY AGMDRFEARE ALVKDLKKEG YLIKVEPIVH SVGHSERSGV QVEPRLSKQW
     FVKMKPLAEE VLKNQKTDGK VNFVPERFEG TLNHWMEDVH DWVISRQLWW GHRIPAWYNK
     KTGETYVGEE APKDIENWEQ DPDVLDTWFS SALWPFSTLG WPDTDNPDFK RYFPTNTLVT
     GYDIIFFWVS RMIFQGLHFT KKRPFKDVVL HGLMRDEQGR KMSKSLGNGV DPMDVVDKYG
     ADALRWFLLN GTAPGQDTRY DPKKLAAAWN FINKIWNASR FVIMNLPEDA KPAHMPDTTK
     FDLADSWIFD RLNHTVSEVT RLFDEYKFGE AGRELYNFIW NDFCDWYIEI SKVALNGDDE
     ELKARKQENL IWILDQILRL MHPIMPFVTE KLWLSMPHEG KSIMTAKYPE THAEFENKQA
     DSDMAFLIEV IKAVRNIRME VNAPMSSQID IMIQLDDEAN KHILDDNAEY VENFLHPKDL
     QVAADIEAPK LAKTAVIPGA QIFVPLTELV NVDDELKKME KEEKRLEEEV QRAEKKLANQ
     GFVAHAPEAV VNKEKEKKAD YESQLAGVRE RMKELKESK
//