(data stored in SCRATCH3701 zone)

SWISSPROT: D5E9P8_METMS

ID   D5E9P8_METMS            Unreviewed;       865 AA.
AC   D5E9P8;
DT   15-JUN-2010, integrated into UniProtKB/TrEMBL.
DT   15-JUN-2010, sequence version 1.
DT   11-DEC-2019, entry version 63.
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   OrderedLocusNames=Mmah_0367 {ECO:0000313|EMBL:ADE35899.1};
OS   Methanohalophilus mahii (strain ATCC 35705 / DSM 5219 / SLP).
OC   Archaea; Euryarchaeota; Stenosarchaea group; Methanomicrobia;
OC   Methanosarcinales; Methanosarcinaceae; Methanohalophilus.
OX   NCBI_TaxID=547558 {ECO:0000313|EMBL:ADE35899.1, ECO:0000313|Proteomes:UP000001059};
RN   [1] {ECO:0000313|EMBL:ADE35899.1, ECO:0000313|Proteomes:UP000001059}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 35705 / DSM 5219 / SLP
RC   {ECO:0000313|Proteomes:UP000001059};
RG   US DOE Joint Genome Institute (JGI-PGF);
RA   Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA   Bruce D., Goodwin L., Pitluck S., Kyrpides N., Mavromatis K., Ivanova N.,
RA   Lykidis A., Saunders E., Brettin T., Detter J.C., Han C., Land M.,
RA   Hauser L., Markowitz V., Cheng J.-F., Hugenholtz P., Woyke T., Wu D.,
RA   Spring S., Schneider S., Schroeder M., Klenk H.-P., Eisen J.A.;
RT   "The complete genome of Methanohalophilus mahii DSM 5219.";
RL   Submitted (MAR-2010) to the EMBL/GenBank/DDBJ databases.
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|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; CP001994; ADE35899.1; -; Genomic_DNA.
DR   RefSeq; WP_013036842.1; NC_014002.1.
DR   EnsemblBacteria; ADE35899; ADE35899; Mmah_0367.
DR   GeneID; 8982501; -.
DR   KEGG; mmh:Mmah_0367; -.
DR   eggNOG; arCOG00808; Archaea.
DR   eggNOG; COG0525; LUCA.
DR   HOGENOM; HOG000020095; -.
DR   KO; K01873; -.
DR   OMA; FATKLWN; -.
DR   OrthoDB; 4914at2157; -.
DR   BioCyc; MMAH547558:G1GHT-364-MONOMER; -.
DR   Proteomes; UP000001059; 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; -; 1.
DR   Gene3D; 3.90.740.10; -; 1.
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   Pfam; PF08264; Anticodon_1; 1.
DR   Pfam; PF00133; tRNA-synt_1; 1.
DR   PRINTS; PR00986; TRNASYNTHVAL.
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;
DR   PRODOM; D5E9P8.
DR   SWISS-2DPAGE; D5E9P8.
KW   Aminoacyl-tRNA synthetase {ECO:0000256|HAMAP-Rule:MF_02005,
KW   ECO:0000256|RuleBase:RU363035, ECO:0000313|EMBL:ADE35899.1};
KW   ATP-binding {ECO:0000256|HAMAP-Rule:MF_02005,
KW   ECO:0000256|RuleBase:RU363035};
KW   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_02005};
KW   Ligase {ECO:0000256|HAMAP-Rule:MF_02005, ECO:0000256|RuleBase:RU363035,
KW   ECO:0000313|EMBL:ADE35899.1};
KW   Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_02005,
KW   ECO:0000256|RuleBase:RU363035};
KW   Protein biosynthesis {ECO:0000256|HAMAP-Rule:MF_02005,
KW   ECO:0000256|RuleBase:RU363035};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001059}.
FT   DOMAIN          16..556
FT                   /note="tRNA-synt_1"
FT                   /evidence="ECO:0000259|Pfam:PF00133"
FT   DOMAIN          602..746
FT                   /note="Anticodon_1"
FT                   /evidence="ECO:0000259|Pfam:PF08264"
FT   MOTIF           44..54
FT                   /note="'HIGH' region"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_02005"
FT   MOTIF           518..522
FT                   /note="'KMSKS' region"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_02005"
FT   BINDING         521
FT                   /note="ATP"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_02005"
SQ   SEQUENCE   865 AA;  99594 MW;  8F7CE8726F2D84C9 CRC64;
     MTIPKEYNPQ EVEKKWQNAW DMSMYHFDWE DENKPQYIID TPPPYPTGNF HIGNSLNWCY
     IDFVARYKRM QGFNVMFPQG WDCHGLPTEV KVEEIHGITK NQVPRAEFRK LCEELTLGNI
     EKMRQTMRML GFSVDWSNEF ITMKPEYFVK TQRSFVQMQK QGRIYQADHP VNWCPRCETA
     IAFAEVEYEA RDTKLNYLSF DKVRIATTRP ELLAACVAVA INPEDERYKE NIGENVKVPL
     FDHEVPVIAD KEVDPEFGTG VVMICTFGDK QDVRWWIEHN LPLRKAIDRN GFMTGIAGKY
     EGMKSSECKD AIIQDLKEQG YLYDQDSLDQ NVGMCWRCNT PIEILSERQW FVKIENDKIL
     ATANEINWIP DYMKIRLENW TNTMEWDWCI SRQRIFATPI PVWYCKQCGK SLIAEEEWLP
     LDPTQTKPPT PCECGSTDFE AEEDVLDTWM DSSLTALHVT GWLTDHEMRS PAQLRPQGHD
     IIRTWAFYSI LRSKALQDSR PWDSIMINGM VLGEDGHKMS KSRGNIISPE EVVDQYSSDA
     FRQWAAIGGS TGSDVMFRWK DVVSGSRYFN KMWSIFRFSM SHLEELLPEI PEVATSSLGT
     VDRWLLSKLN RLIISVTENM DNYQFDEAYK SIRGFAWETL ADNYIELVKA RLYGEDETSK
     KAARYTLYTT LETLTRMLAP FAPFFAEEVY SHISTGSVHQ TKWPSSNREI IDETAEKQGE
     IIKDLASSIR RYKSDCGMAL NAPLKKIEIY SVMDDVTDLE GATNSAVEVI EGKPEFEHVP
     VDVKPNMGII GPKFRKQAGS IIATLKSMDA SRVAQMKESR SIDIEVDGEK INLEPESVEI
     IKEVTSAGRT VDVLEVSDVM AVILR
//

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