(data stored in SCRATCH zone)

SWISSPROT: A4ATC5_MARSH

ID   A4ATC5_MARSH            Unreviewed;       876 AA.
AC   A4ATC5;
DT   03-APR-2007, integrated into UniProtKB/TrEMBL.
DT   03-APR-2007, sequence version 1.
DT   08-MAY-2019, entry version 94.
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   OrderedLocusNames=FB2170_16461 {ECO:0000313|EMBL:EAR00695.1};
OS   Maribacter sp. (strain HTCC2170 / KCCM 42371).
OC   Bacteria; Bacteroidetes; Flavobacteriia; Flavobacteriales;
OC   Flavobacteriaceae; Maribacter.
OX   NCBI_TaxID=313603 {ECO:0000313|EMBL:EAR00695.1, ECO:0000313|Proteomes:UP000001602};
RN   [1] {ECO:0000313|EMBL:EAR00695.1, ECO:0000313|Proteomes:UP000001602}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=HTCC2170 / KCCM 42371 {ECO:0000313|Proteomes:UP000001602};
RX   PubMed=21037013; DOI=10.1128/JB.01207-10;
RA   Oh H.M., Kang I., Yang S.J., Jang Y., Vergin K.L., Giovannoni S.J.,
RA   Cho J.C.;
RT   "Complete genome sequence of strain HTCC2170, a novel member of the
RT   genus Maribacter in the family Flavobacteriaceae.";
RL   J. Bacteriol. 193:303-304(2011).
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:SAAS00889227}.
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,
CC         ChEBI:CHEBI:57762, ChEBI:CHEBI:78442, ChEBI:CHEBI:78537,
CC         ChEBI:CHEBI:456215; EC=6.1.1.9; Evidence={ECO:0000256|HAMAP-
CC         Rule:MF_02004, ECO:0000256|SAAS:SAAS01116702};
CC   -!- SUBUNIT: Monomer. {ECO:0000256|HAMAP-Rule:MF_02004,
CC       ECO:0000256|SAAS:SAAS00889229}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_02004,
CC       ECO:0000256|SAAS:SAAS00889155}.
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:SAAS00889246}.
CC   -!- CAUTION: Lacks conserved residue(s) required for the propagation
CC       of feature annotation. {ECO:0000256|HAMAP-Rule:MF_02004}.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   -----------------------------------------------------------------------
DR   EMBL; CP002157; EAR00695.1; -; Genomic_DNA.
DR   RefSeq; WP_013304498.1; NC_014472.1.
DR   STRING; 313603.FB2170_16461; -.
DR   EnsemblBacteria; EAR00695; EAR00695; FB2170_16461.
DR   KEGG; fbc:FB2170_16461; -.
DR   eggNOG; ENOG4105CA4; Bacteria.
DR   eggNOG; COG0525; LUCA.
DR   HOGENOM; HOG000020093; -.
DR   KO; K01873; -.
DR   OMA; FATKLWN; -.
DR   OrthoDB; 32262at2; -.
DR   BioCyc; MSP313603:G1GNS-71-MONOMER; -.
DR   Proteomes; UP000001602; 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; -; 1.
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   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;
DR   PRODOM; A4ATC5.
DR   SWISS-2DPAGE; A4ATC5.
KW   Aminoacyl-tRNA synthetase {ECO:0000256|HAMAP-Rule:MF_02004,
KW   ECO:0000256|RuleBase:RU363035, ECO:0000256|SAAS:SAAS00711227,
KW   ECO:0000313|EMBL:EAR00695.1};
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:SAAS00889220, ECO:0000256|SAM:Coils};
KW   Complete proteome {ECO:0000313|Proteomes:UP000001602};
KW   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_02004,
KW   ECO:0000256|SAAS:SAAS00889138};
KW   Ligase {ECO:0000256|HAMAP-Rule:MF_02004,
KW   ECO:0000256|RuleBase:RU363035, ECO:0000256|SAAS:SAAS00711254};
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};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001602}.
FT   DOMAIN       16    574       tRNA-synt_1. {ECO:0000259|Pfam:PF00133}.
FT   DOMAIN      616    756       Anticodon_1. {ECO:0000259|Pfam:PF08264}.
FT   DOMAIN      811    875       Val_tRNA-synt_C. {ECO:0000259|Pfam:
FT                                PF10458}.
FT   COILED      851    871       {ECO:0000256|SAM:Coils}.
FT   MOTIF        43     53       "HIGH" region. {ECO:0000256|HAMAP-Rule:
FT                                MF_02004}.
FT   BINDING     538    538       ATP. {ECO:0000256|HAMAP-Rule:MF_02004}.
SQ   SEQUENCE   876 AA;  101202 MW;  3A1CF0677B8B1B1C CRC64;
     MDIPSKYEPQ KVENHWYDYW TKHNYFHSTP DEREPYSIVI PPPNVTGILH MGHMLNNTIQ
     DVLIRKARLM GKNACWVPGT DHASIATEAK VVARLKEQGI DKADLSREEF LKHAWDWTHE
     YGGVILEQLK KLGCSCDWER TAFTMDDNMS ASVNKVFVDL FNKGLIYRGH RMVNWDPQAL
     TTLSDEEVIY EEKQGLLYYL SYEIEGSDEK VTIATTRPET ILGDTAICIN PNDERFKHLK
     GKKAIVPICN RVIPIIEDEY VDIEFGTGCL KVTPAHDIND KALGEKHSLE VIDIFNADAT
     LNSFGLHYQG KDRFVVRKEI KKELEEQGFL VKTENYINKV GTSERTKAVI EPRLSEQWFL
     KMEDLVKPAI KAVLDSDDIN FYPKKFENTY RHWMENIRDW NISRQLWWGQ QIPAYYYGDG
     QNDFVVAETK EEALELARAK SQNPNLKIED LKQDPDVVDT WFSSWLWPMT VFNGILEPDN
     EDISYYYPTS DLVTGPDIIF FWVARMIISG YEYRDEKPFE NVYFTGLVRD KQRRKMSKQL
     GNSPDALKLI ENYGADGVRV GLLLSSAAGN DLMFDEDLCQ QGKNFANKIW NGFRLLKGWE
     VADLPQPEAS KLGISWYKAK FNQTLVEIED HFSKYRISDA LMAIYKLVWD DYSSWLLEII
     KPAYQQPIDR KTFDEVITLF EGNLKLLHPF MPFLTEEIWQ HIAERSPEQA LVVSQWPEGK
     NVDSALINEF EFAAEVISGV RTKRKEKNIP MKEALELSIL NKERTSDAWD VVVRKLTNVS
     SIFYVEAAVE GALSFRIKSN EYFIPISGAV DLEAEIKKIQ EELKYTKGFL MSVQKKLSNE
     RFVNNAPEKV IEIERKKQSD AEAKIETLEK SLASLS
//

If you have problems or comments...

PBIL Back to PBIL home page