UniProt: A0A1W0E8H0

Database: UniProt
Entry: A0A1W0E8H0_9MICR

LinkDB:  A0A1W0E8H0_9MICR 
Original site:  A0A1W0E8H0_9MICR

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Ontology (3)   
   GO (3)   
Chemical reaction (1)   
   KEGG ENZYME (1)   
DNA sequence (1)   
   EMBL (1)   
Protein domain (8)   
   InterPro (5)   
   Pfam (2)   
   PROSITE (1)   
Literature (1)   
   PubMed (1)   
All databases (14)   

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ID   A0A1W0E8H0_9MICR        Unreviewed;       854 AA.
AC   A0A1W0E8H0;
DT   07-JUN-2017, integrated into UniProtKB/TrEMBL.
DT   07-JUN-2017, sequence version 1.
DT   24-JAN-2024, entry version 20.
DE   RecName: Full=leucine--tRNA ligase {ECO:0000256|ARBA:ARBA00013164};
DE            EC=6.1.1.4 {ECO:0000256|ARBA:ARBA00013164};
DE   AltName: Full=Leucyl-tRNA synthetase {ECO:0000256|ARBA:ARBA00030520};
GN   ORFNames=EHP00_579 {ECO:0000313|EMBL:OQS55516.1};
OS   Ecytonucleospora hepatopenaei.
OC   Eukaryota; Fungi; Fungi incertae sedis; Microsporidia; Enterocytozoonidae;
OC   Ecytonucleospora.
OX   NCBI_TaxID=646526 {ECO:0000313|EMBL:OQS55516.1, ECO:0000313|Proteomes:UP000192758};
RN   [1] {ECO:0000313|EMBL:OQS55516.1, ECO:0000313|Proteomes:UP000192758}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=TH1 {ECO:0000313|EMBL:OQS55516.1,
RC   ECO:0000313|Proteomes:UP000192758};
RX   PubMed=28345194; DOI=10.1111/1462-2920.13734;
RA   Wiredu Boakye D., Jaroenlak P., Prachumwat A., Williams T.A., Bateman K.S.,
RA   Itsathitphaisarn O., Sritunyalucksana K., Paszkiewicz K.H., Moore K.A.,
RA   Stentiford G.D., Williams B.A.;
RT   "Decay of the glycolytic pathway and adaptation to intranuclear parasitism
RT   within Enterocytozoonidae microsporidia.";
RL   Environ. Microbiol. 19:2077-2089(2017).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + L-leucine + tRNA(Leu) = AMP + diphosphate + L-leucyl-
CC         tRNA(Leu); Xref=Rhea:RHEA:11688, Rhea:RHEA-COMP:9613, Rhea:RHEA-
CC         COMP:9622, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:57427,
CC         ChEBI:CHEBI:78442, ChEBI:CHEBI:78494, ChEBI:CHEBI:456215; EC=6.1.1.4;
CC         Evidence={ECO:0000256|ARBA:ARBA00001372};
CC   -!- SIMILARITY: Belongs to the class-I aminoacyl-tRNA synthetase family.
CC       {ECO:0000256|ARBA:ARBA00005594, ECO:0000256|RuleBase:RU363035}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:OQS55516.1}.
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DR   EMBL; MNPJ01000007; OQS55516.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1W0E8H0; -.
DR   STRING; 646526.A0A1W0E8H0; -.
DR   VEuPathDB; MicrosporidiaDB:EHP00_579; -.
DR   Proteomes; UP000192758; Unassembled WGS sequence.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0004823; F:leucine-tRNA ligase activity; IEA:InterPro.
DR   GO; GO:0006429; P:leucyl-tRNA aminoacylation; IEA:InterPro.
DR   CDD; cd00812; LeuRS_core; 1.
DR   Gene3D; 3.40.50.620; HUPs; 2.
DR   InterPro; IPR001412; aa-tRNA-synth_I_CS.
DR   InterPro; IPR002300; aa-tRNA-synth_Ia.
DR   InterPro; IPR004493; Leu-tRNA-synth_Ia_arc/euk.
DR   InterPro; IPR015413; Methionyl/Leucyl_tRNA_Synth.
DR   InterPro; IPR014729; Rossmann-like_a/b/a_fold.
DR   PANTHER; PTHR45794:SF1; LEUCINE--TRNA LIGASE, CYTOPLASMIC; 1.
DR   PANTHER; PTHR45794; LEUCYL-TRNA SYNTHETASE; 1.
DR   Pfam; PF00133; tRNA-synt_1; 1.
DR   Pfam; PF09334; tRNA-synt_1g; 1.
DR   SUPFAM; SSF52374; Nucleotidylyl transferase; 1.
DR   PROSITE; PS00178; AA_TRNA_LIGASE_I; 1.
PE   3: Inferred from homology;
KW   Aminoacyl-tRNA synthetase {ECO:0000256|ARBA:ARBA00023146,
KW   ECO:0000256|RuleBase:RU363035};
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|RuleBase:RU363035};
KW   Ligase {ECO:0000256|ARBA:ARBA00022598, ECO:0000256|RuleBase:RU363035};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW   ECO:0000256|RuleBase:RU363035};
KW   Protein biosynthesis {ECO:0000256|ARBA:ARBA00022917,
KW   ECO:0000256|RuleBase:RU363035};
KW   Reference proteome {ECO:0000313|Proteomes:UP000192758}.
FT   DOMAIN          34..93
FT                   /note="Methionyl/Leucyl tRNA synthetase"
FT                   /evidence="ECO:0000259|Pfam:PF09334"
FT   DOMAIN          138..589
FT                   /note="Aminoacyl-tRNA synthetase class Ia"
FT                   /evidence="ECO:0000259|Pfam:PF00133"
SQ   SEQUENCE   854 AA;  99754 MW;  80DD3143FF81F59A CRC64;
     MSEENSKLHF LNEIEQKGNL ETRKVKINEN LPKYFITFPY PYMNGKLHLG HLYSISKADI
     LAYFKEMTGY NVLFPFAFHC TGMPIAASAQ KLQSELNGEN VDVSIISILN SFGFELSCQD
     KSKCDQDECI CKFVDPFKWC RTFPKYCKAS LQKFDACIDW RRSFITTNVN PYYDSFVLWQ
     FKILKKKGFI NFGKRYSIFC PIDRQACLDH DRRKGEGVKP VVCVLKILKN NVLVRIKNLD
     FKYDSDSQII TTNSIVWCKI KINDIEYVLE EFYYLNIKEQ IKNVVFITNV NIKDVYENVS
     FIDVDLPYSK LKLNNDKNDK NTSIKEFVDN FKNEKLELVE KEGFIFLQIP EDKVISRSGG
     LCVVSLMDQW FLDYKNEEWK ILARKCLERM EMSTDTREKL EFAVEWINKW GFSRNFGLGT
     VYFDDKSALI DSLSDSTIYM AFYTVKHLFF SDLEGKNEIL KKEELSFELW DYVFMQTNVC
     PEFKYQETNE IVKNARKQFG YFYPVDLRVS GKDLINNHLT FFIMNHVAIF DEKYWPRRIF
     TNGHLMLNSA KMSKSEGNFL TVDDALKKFG TSATRMCLLA CGDTNEDANF VESMANSFVL
     KLYTITKTVL ALKQNDTSLL FTSLDNFLIS SIKLNKEKVF NAYESIVFRD VLKYGFYENL
     NAIETYELFS EEGSDTQNLK GWAYYEMLSM LYPVIPSLSR HLKTCLQIFS DFVPSGFSSM
     QKHVDGILYI KEILRKCMLA KGKSLEIIVV KKYADWKENC ISIINSLIAK KDNDIKKKVL
     SECSEHIKIN KKKGSVFCMD YYKNPEKYVL NFNEFEYLNE YKNLLVRESG KTIKITCLDK
     HEKSEPGNPF ILSE
//

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