ID D4ATB2_ARTBC Unreviewed; 1127 AA.
AC D4ATB2;
DT 18-MAY-2010, integrated into UniProtKB/TrEMBL.
DT 18-MAY-2010, sequence version 1.
DT 24-JAN-2024, entry version 71.
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=ARB_07476 {ECO:0000313|EMBL:EFE33531.1};
OS Arthroderma benhamiae (strain ATCC MYA-4681 / CBS 112371) (Trichophyton
OS mentagrophytes).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Onygenales; Arthrodermataceae; Trichophyton.
OX NCBI_TaxID=663331 {ECO:0000313|EMBL:EFE33531.1, ECO:0000313|Proteomes:UP000008866};
RN [1] {ECO:0000313|Proteomes:UP000008866}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC MYA-4681 / CBS 112371 {ECO:0000313|Proteomes:UP000008866};
RX PubMed=21247460; DOI=10.1186/gb-2011-12-1-r7;
RA Burmester A., Shelest E., Gloeckner G., Heddergott C., Schindler S.,
RA Staib P., Heidel A., Felder M., Petzold A., Szafranski K., Feuermann M.,
RA Pedruzzi I., Priebe S., Groth M., Winkler R., Li W., Kniemeyer O.,
RA Schroeckh V., Hertweck C., Hube B., White T.C., Platzer M., Guthke R.,
RA Heitman J., Woestemeyer J., Zipfel P.F., Monod M., Brakhage A.A.;
RT "Comparative and functional genomics provide insights into the
RT pathogenicity of dermatophytic fungi.";
RL Genome Biol. 12:R7.1-R7.16(2011).
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:EFE33531.1}.
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; ABSU01000009; EFE33531.1; -; Genomic_DNA.
DR RefSeq; XP_003014171.1; XM_003014125.1.
DR AlphaFoldDB; D4ATB2; -.
DR STRING; 663331.D4ATB2; -.
DR GeneID; 9521589; -.
DR KEGG; abe:ARB_07476; -.
DR eggNOG; KOG0437; Eukaryota.
DR HOGENOM; CLU_004174_1_1_1; -.
DR OMA; KFIEWQF; -.
DR OrthoDB; 5472610at2759; -.
DR Proteomes; UP000008866; Unassembled WGS sequence.
DR GO; GO:0002161; F:aminoacyl-tRNA editing activity; IEA:InterPro.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004823; F:leucine-tRNA ligase activity; IEA:UniProtKB-EC.
DR GO; GO:0006429; P:leucyl-tRNA aminoacylation; IEA:InterPro.
DR CDD; cd07959; Anticodon_Ia_Leu_AEc; 1.
DR Gene3D; 3.40.50.620; HUPs; 1.
DR Gene3D; 3.90.740.10; Valyl/Leucyl/Isoleucyl-tRNA synthetase, editing domain; 1.
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; IPR013155; M/V/L/I-tRNA-synth_anticd-bd.
DR InterPro; IPR015413; Methionyl/Leucyl_tRNA_Synth.
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 NCBIfam; TIGR00395; leuS_arch; 1.
DR PANTHER; PTHR45794:SF1; LEUCINE--TRNA LIGASE, CYTOPLASMIC; 1.
DR PANTHER; PTHR45794; LEUCYL-TRNA SYNTHETASE; 1.
DR Pfam; PF08264; Anticodon_1; 1.
DR Pfam; PF00133; tRNA-synt_1; 1.
DR Pfam; PF09334; tRNA-synt_1g; 1.
DR SUPFAM; SSF47323; Anticodon-binding domain of a subclass of class I aminoacyl-tRNA synthetases; 1.
DR SUPFAM; SSF52374; Nucleotidylyl transferase; 1.
DR SUPFAM; SSF50677; ValRS/IleRS/LeuRS editing domain; 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:UP000008866}.
FT DOMAIN 67..137
FT /note="Aminoacyl-tRNA synthetase class Ia"
FT /evidence="ECO:0000259|Pfam:PF00133"
FT DOMAIN 716..802
FT /note="Methionyl/Leucyl tRNA synthetase"
FT /evidence="ECO:0000259|Pfam:PF09334"
FT DOMAIN 837..934
FT /note="Methionyl/Valyl/Leucyl/Isoleucyl-tRNA synthetase
FT anticodon-binding"
FT /evidence="ECO:0000259|Pfam:PF08264"
SQ SEQUENCE 1127 AA; 127028 MW; CE3CEAE34727B709 CRC64;
MAASVSAAAA VALDSSKNTL KLENTEKRDT LIALEKKYQA VWKEKKVFEV DAPSLSEIPA
QSMTSAELHE KYPKFFGTMA FPYMNGTPHA GHSFTASKIE FMTGVARLEG KRALFPLGFH
CTGMPIRACA DKLVDDIKKF GKYFENYKEE EEVDAIPAPT QEIAKEDLSK FSGKKSKAAS
KAVKLKYQFQ IMMALGIPLE EVHKFADPEH WLQHFPPLWI RDLDSMGARV DWRRQMVTTD
VNPYFDSFVR WQMIRLHEMG KILYGSRYTI YSPKDGQPCM DHDRLDGEGV GPQEYTAMKL
KVKEWSPKAK EIVQGKIEED ANVYFVPATL RPETMYGQTC CFVGPAISYG IFKVKEKEYY
VVTKRAAWNM AFQGIFFDVN NLPKSQDELP PVVEAPGSAL IGTLVDAPLS FHKEGVRILP
METVSANKGT GVVSCVPSDS PDDFATISDL AKKADYYGIQ KEWAELEIHP LIETPTYGNL
TAPALVKQLK INSPKDTVQL AQAKDLAYTE GFYKGKMLVG EFKGEPVQTA KEKVRNSLIK
SGDAFPFADP MGKVTSRSGD DCVVAYLGQW FLNYGENDPE WQSTTLKYVT DDLNTYSEET
RHGFEKNLDW LNRWACARTY GLGSKLPWDP QFLVESLSDS TIYQCYYTIS HLLHADRYGK
EPGKLGIKPE QITNDIWDYI FARRELDDDL VQKSGISKES LLTLRREFEY WYPLDVRISG
KDLIQNHLTF FLYVHIALFP REYWPRGVRA NGHLLLNGEK MSKSTGNFLT LRDAVDKYGA
DATRIAFADA GDAIEDANFD ETVANSNILR MYTLKEWIEE TVADKSLRTG PTDAFLDKVF
DNEMNALARE ARKHYADTNF KLALKSALYD FTSAKDFYRE VATASGIGMH RDLILRYVEL
QALLISPIAP HWAEHMWLDV LKKTDSIQNA RFADVPEPVP GLSAALVYIR STTSNITSSE
AAFIKRISKG KNVKFDPRNP KKITIFVSRK FPAWQDKYIE LVREAFDAVN LTIDDKGLNA
KVGKLGEMKK AMPYVQTLKK RLIQGNEKPE DVFSREMPFD EVQVLHDITG NLKKVTGAKE
VEIIAVEEGG NAGTNFEGIR KEGLSPVAQS AVPGQPSFNF ENIEAAA
//
