ID   SYV_PROMA               Reviewed;         933 AA.
AC   Q7V9I9;
DT   07-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2003, sequence version 1.
DT   03-AUG-2022, entry version 104.
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=Pro_1844;
OS   Prochlorococcus marinus (strain SARG / CCMP1375 / SS120).
OC   Bacteria; Cyanobacteria; Synechococcales; Prochlorococcaceae;
OC   Prochlorococcus.
OX   NCBI_TaxID=167539;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SARG / CCMP1375 / SS120;
RX   PubMed=12917486; DOI=10.1073/pnas.1733211100;
RA   Dufresne A., Salanoubat M., Partensky F., Artiguenave F., Axmann I.M.,
RA   Barbe V., Duprat S., Galperin M.Y., Koonin E.V., Le Gall F., Makarova K.S.,
RA   Ostrowski M., Oztas S., Robert C., Rogozin I.B., Scanlan D.J.,
RA   Tandeau de Marsac N., Weissenbach J., Wincker P., Wolf Y.I., Hess W.R.;
RT   "Genome sequence of the cyanobacterium Prochlorococcus marinus SS120, a
RT   nearly minimal oxyphototrophic genome.";
RL   Proc. Natl. Acad. Sci. U.S.A. 100:10020-10025(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; AE017126; AAQ00888.1; -; Genomic_DNA.
DR   RefSeq; NP_876235.1; NC_005042.1.
DR   RefSeq; WP_011125993.1; NC_005042.1.
DR   AlphaFoldDB; Q7V9I9; -.
DR   SMR; Q7V9I9; -.
DR   STRING; 167539.Pro_1844; -.
DR   EnsemblBacteria; AAQ00888; AAQ00888; Pro_1844.
DR   GeneID; 54201173; -.
DR   KEGG; pma:Pro_1844; -.
DR   PATRIC; fig|167539.5.peg.1946; -.
DR   eggNOG; COG0525; Bacteria.
DR   HOGENOM; CLU_001493_0_2_3; -.
DR   OMA; FATKLWN; -.
DR   OrthoDB; 32262at2; -.
DR   Proteomes; UP000001420; 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; Reference proteome.
FT   CHAIN           1..933
FT                   /note="Valine--tRNA ligase"
FT                   /id="PRO_0000224530"
FT   COILED          807..833
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_02004"
FT   COILED          864..933
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_02004"
FT   MOTIF           58..68
FT                   /note="'HIGH' region"
FT   MOTIF           556..560
FT                   /note="'KMSKS' region"
FT   BINDING         559
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_02004"
SQ   SEQUENCE   933 AA;  106253 MW;  B8488F8B3B321BB7 CRC64;
     MVDQPDSENL DHAVDALSKR YDPLGTECRW QKIWEEEGAF HPDPNDEGEP FSVVIPPPNV
     TGSLHMGHAF NTALIDTIVR FQRLQGKNVL CLPGTDHASI AVQTILEKQL KKEGLTRDEL
     GRSAFLERAW AWKSESGGRI VEQLRRLGYS VDWKRERFTM DTRLSKAVSE AFVRLHQQGL
     IYRGEYLVNW CPASSSAVSD LEVETKEVDG YLWHFQYPLS KINDSNGIRF LEVATTRPET
     MLGDVAVAVN PSDSRYSNIV GQTLTLPFLG REIPVIADDH VDMDFGTGCV KVTPAHDPND
     FAIGQRHNLR QITVMNKDGT MNAEAGPFEG LDRFEARKAV VKALEQKGLL TKVEPYRHSV
     PFSDRGKVPI EPLLSTQWFV RMEPMAERCR SHLGKDEPRF YPDRWAKVYR DWLTGIRDWC
     ISRQLWWGHR IPAWFVVSET NNELTDDTPY IVALSEKDAL LEAQKKYGTD AVLRQDEDVL
     DTWFSSGLWP FSTLGWPDKT NADLSRWYPT NTLVTGFDII FFWVARMTMM AGAFTGKMPF
     ADVYIHGLVR DEQNRKMSKS AGNGIDPLLL IDRYGTDALR FALVKEVAGA GQDIRIDYDR
     AKDTSATVEA ARNFANKLWN ATRFALINLG DTTFKETFDE LEHNRLELSD QWILSKLSKV
     NNETAKRYKK YALGEAAKGL YEFAWNDFCD WYLELIKRRL NLGESPSEAD LSNRKKSQIV
     MFKVLRELLV MMHPLMPHLT EELWHGVTGF SNKKLLALQS WPALDKDLID EDLELSFSEL
     FGAIRLVRNL RAEAGLKPSQ RAPVRFVTKN QNLLNLLKKA TQDIQALTRA NKVEILHPRE
     IFEESSGRSL AGVSGELEVL LPIEGLVDLQ ALRNRLQKDL SKAENELSIL SKRLDNPSFV
     QKAPEKVIEE CRLKLSDAEA QAELVRQRLL GLK