ID   SYV_PROMP               Reviewed;         918 AA.
AC   Q7UZI3;
DT   07-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2003, sequence version 1.
DT   03-AUG-2022, entry version 105.
DE   RecName: Full=Valine--tRNA ligase {ECO:0000255|HAMAP-Rule:MF_02004};
DE            EC=6.1.1.9 {ECO:0000255|HAMAP-Rule:MF_02004};
DE   AltName: Full=Valyl-tRNA synthetase {ECO:0000255|HAMAP-Rule:MF_02004};
DE            Short=ValRS {ECO:0000255|HAMAP-Rule:MF_02004};
GN   Name=valS {ECO:0000255|HAMAP-Rule:MF_02004}; OrderedLocusNames=PMM1682;
OS   Prochlorococcus marinus subsp. pastoris (strain CCMP1986 / NIES-2087 /
OS   MED4).
OC   Bacteria; Cyanobacteria; Synechococcales; Prochlorococcaceae;
OC   Prochlorococcus.
OX   NCBI_TaxID=59919;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CCMP1986 / NIES-2087 / MED4;
RX   PubMed=12917642; DOI=10.1038/nature01947;
RA   Rocap G., Larimer F.W., Lamerdin J.E., Malfatti S., Chain P., Ahlgren N.A.,
RA   Arellano A., Coleman M., Hauser L., Hess W.R., Johnson Z.I., Land M.L.,
RA   Lindell D., Post A.F., Regala W., Shah M., Shaw S.L., Steglich C.,
RA   Sullivan M.B., Ting C.S., Tolonen A., Webb E.A., Zinser E.R.,
RA   Chisholm S.W.;
RT   "Genome divergence in two Prochlorococcus ecotypes reflects oceanic niche
RT   differentiation.";
RL   Nature 424:1042-1047(2003).
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:0000255|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:0000255|HAMAP-Rule:MF_02004};
CC   -!- SUBUNIT: Monomer. {ECO:0000255|HAMAP-Rule:MF_02004}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|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:0000255|HAMAP-Rule:MF_02004}.
CC   -!- DOMAIN: The C-terminal coiled-coil domain is crucial for aminoacylation
CC       activity. {ECO:0000255|HAMAP-Rule:MF_02004}.
CC   -!- SIMILARITY: Belongs to the class-I aminoacyl-tRNA synthetase family.
CC       ValS type 1 subfamily. {ECO:0000255|HAMAP-Rule:MF_02004}.
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DR   EMBL; BX548174; CAE20141.1; -; Genomic_DNA.
DR   RefSeq; WP_011133309.1; NC_005072.1.
DR   AlphaFoldDB; Q7UZI3; -.
DR   SMR; Q7UZI3; -.
DR   STRING; 59919.PMM1682; -.
DR   EnsemblBacteria; CAE20141; CAE20141; PMM1682.
DR   KEGG; pmm:PMM1682; -.
DR   eggNOG; COG0525; Bacteria.
DR   HOGENOM; CLU_001493_0_2_3; -.
DR   OMA; FATKLWN; -.
DR   OrthoDB; 32262at2; -.
DR   Proteomes; UP000001026; 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; 1.10.287.380; -; 1.
DR   Gene3D; 3.40.50.620; -; 2.
DR   Gene3D; 3.90.740.10; -; 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; PTHR11946; 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; 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; ATP-binding; Coiled coil; Cytoplasm; Ligase;
KW   Nucleotide-binding; Protein biosynthesis.
FT   CHAIN           1..918
FT                   /note="Valine--tRNA ligase"
FT                   /id="PRO_0000224533"
FT   COILED          849..883
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_02004"
FT   MOTIF           50..60
FT                   /note="'HIGH' region"
FT   MOTIF           548..552
FT                   /note="'KMSKS' region"
FT   BINDING         551
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_02004"
SQ   SEQUENCE   918 AA;  106312 MW;  C8257ECC0732A66A CRC64;
     MNESNDELTL NNYLPSQVEQ KWQKRWDSLR AFSPNPSDNG DPFCIVIPPP NVTGSLHMGH
     AFNTALIDVI IRFQRLLGKN VLCLPGTDHA SIAVQTILEK QLKTEGKNSE DIGREEFLKR
     AWIWKEQSGG KIISQLKRIG YSVDWERERF TLDEKLNEAV VEAFNILHEK KLIYRGEYLV
     NWCPASQSAV SDLEVEMQEV NGYLWHFKYP LISDQGQILD KYLEVATTRP ETLLGDTALA
     VNPNDERYKK YIDKKVKVPF VDREIPVISD IHVDKDFGTG CVKVTPAHDP NDFAIGKRNN
     LKQINIMNKD GTLNINAGKF QDLDRFDARK KIIKELDTLG LLTKIENYKN TVPFSDRGKV
     PIEPLLSTQW FLKMDNISSS CLKELDSKKP TFIPQRWEKV YKDWLDNIND WCISRQLWWG
     HQIPAWYVLK QSEDSIDQNT PYVVARNEKE ALSKATKEFG SNLQLIRDKD VLDTWFSSGL
     WPFSTLGWPN INDADFKKWY PNSVLITGFD IIFFWVARMT MMGKTFTNNI PFKDVYIHGL
     VRDENNKKMS KSSGNGIDPL LLIDKYGSDA LRFALLREVA GAGQDIRLDY DRKENTSSTV
     EASRNFANKL WNATKFVLIN KTFSENCSLN ESDEKNLELS DKWILSKLNQ LNTKVSNLLI
     EYKLGESAKL LYEFAWNDFC DWYVEFAKQK FNNKETHNRK ISEKILIKVL TDVLVMMHPF
     MPHITEELWH KLQIKPEQIL LSLQKWPVLE KKYINSQIDK SFHELFEIIR LIRNLRVELG
     LKPSQLVPVY LISDNVELTN FLKTLIVDIK TFTKSSEVII CKSKDIDKNN FAQSFSGIIG
     DLEVYLPFND FVNLEALKDR LTKDLKKVNS DIETLNKRIS NKNFIDKAPK EIVDECFAKL
     KEGNLQSEII NKKLKLLK