ID A0A0M8MYU9_9BASI Unreviewed; 1034 AA.
AC A0A0M8MYU9;
DT 09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT 09-DEC-2015, sequence version 1.
DT 27-MAR-2024, entry version 33.
DE RecName: Full=isoleucine--tRNA ligase {ECO:0000256|ARBA:ARBA00013165};
DE EC=6.1.1.5 {ECO:0000256|ARBA:ARBA00013165};
DE AltName: Full=Isoleucyl-tRNA synthetase {ECO:0000256|ARBA:ARBA00032665};
GN ORFNames=Malapachy_3580 {ECO:0000313|EMBL:KOS16470.1};
OS Malassezia pachydermatis.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Ustilaginomycotina;
OC Malasseziomycetes; Malasseziales; Malasseziaceae; Malassezia.
OX NCBI_TaxID=77020 {ECO:0000313|EMBL:KOS16470.1, ECO:0000313|Proteomes:UP000037751};
RN [1] {ECO:0000313|EMBL:KOS16470.1, ECO:0000313|Proteomes:UP000037751}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 1879 {ECO:0000313|EMBL:KOS16470.1,
RC ECO:0000313|Proteomes:UP000037751};
RA Triana S., Ohm R., Gonzalez A., DeCock H., Restrepo S., Celis A.;
RT "Draft Genome Sequence of Malassezia furfur CBS1878 and Malassezia
RT pachydermatis CBS1879.";
RL Submitted (JUL-2015) to the EMBL/GenBank/DDBJ databases.
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:KOS16470.1}.
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DR EMBL; LGAV01000001; KOS16470.1; -; Genomic_DNA.
DR RefSeq; XP_017994102.1; XM_018138046.1.
DR AlphaFoldDB; A0A0M8MYU9; -.
DR STRING; 77020.A0A0M8MYU9; -.
DR GeneID; 28729922; -.
DR VEuPathDB; FungiDB:Malapachy_3580; -.
DR OrthoDB; 656at2759; -.
DR Proteomes; UP000037751; 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:0004822; F:isoleucine-tRNA ligase activity; IEA:UniProtKB-EC.
DR GO; GO:0000049; F:tRNA binding; IEA:InterPro.
DR GO; GO:0006428; P:isoleucyl-tRNA aminoacylation; IEA:InterPro.
DR CDD; cd07960; Anticodon_Ia_Ile_BEm; 1.
DR Gene3D; 1.10.730.20; -; 1.
DR Gene3D; 3.40.50.620; HUPs; 2.
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; IPR033708; Anticodon_Ile_BEm.
DR InterPro; IPR002301; Ile-tRNA-ligase.
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 NCBIfam; TIGR00392; ileS; 1.
DR PANTHER; PTHR42765:SF1; ISOLEUCINE--TRNA LIGASE, MITOCHONDRIAL; 1.
DR PANTHER; PTHR42765; SOLEUCYL-TRNA SYNTHETASE; 1.
DR Pfam; PF08264; Anticodon_1; 1.
DR Pfam; PF00133; tRNA-synt_1; 1.
DR PRINTS; PR00984; TRNASYNTHILE.
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:UP000037751}.
FT DOMAIN 75..732
FT /note="Aminoacyl-tRNA synthetase class Ia"
FT /evidence="ECO:0000259|Pfam:PF00133"
FT DOMAIN 778..938
FT /note="Methionyl/Valyl/Leucyl/Isoleucyl-tRNA synthetase
FT anticodon-binding"
FT /evidence="ECO:0000259|Pfam:PF08264"
SQ SEQUENCE 1034 AA; 116728 MW; 96D1B70EE6FBF924 CRC64;
MDVPRRMMRL RWLSRRTEAL YISPLRTLGA SYATAAKKGG KKEQGKYQAT LRLPQTPFSL
RAFAKDREPR FRKATTENLY EWQRRHLGGD QRDFVLHDGP PYANGSLHMG HALNKILKDI
ILRFQVLQGR RVHYMPGWDC HGLPIEIKAV AEARAQGQTS MTPTQIRDTA RKVALRELDN
QREMFKQFGI MTDWSDSNCY RTLSFSYELA QLRLFAKCVE RGLIYERFRP VYWSPSTQTA
LAEAEIEYDE HVSHSVYLRF RLEPSTSLRT LLGTLAEEPI SMVVWTTTPW SLFGNMALTI
KADAVYSIVR TSTNELLLVA QDLVSSLSSV SLGRDTKAPR THLGALDEVL TLPGTALVGS
TYRYPFMAPD AVRYITAADF VTTESGTGIV HSAPAHGQED YEAWRDSGCL ESYGITSPVD
HRGAFAFDSK HGATPAIQDD IQSLEGLLAL EEGTKKVLEL LDKYGILLGE QLYTHSYPID
WRTKKPILTR ATAQWFADLS QTLPDTNAAL RDVHFVPPTG EHRLHSLVSR RSEWCISRQR
AWGVPIPVVY DAETHTPLVS VDNVEHIIDV MASHGSTDAW WTLDAEAFVA PAHRVPGKSW
YIKGDTLDVW FDSGSSWAVL QQALGEPLCT SEPCADVYLE GSDQHRGWFQ SSLLTRVAVC
GHGTKAPYAN LVTHGFVVDE SGRKMSKSIG NVIAPEAFLQ GDPKKPKEFP ALGTDVLRWW
VAKADYTKDI PISTLIMKHV SDEVRKLRNT ARFMLANLND LPRESIPPLS PSTASLMDRY
TMHELYKLER TCREAYRQFD FAQVTRSLLE FATKTLSSLY LDIVKDPLYA GSEADRQGIL
YVLDHVLHTM TTLLAPILPH LAEDIAWYRR GAQADPTPAE METMPSFFQQ GWRPVDVVWH
DPALEAQAQA LLRMRSDIFV LMTHCQKAGH IKASSETAVD IYLPSSHPLW AVCEAHQAQL
PDLFQVSHVR LFPEEAAFHA HLRADRWSQS LTIHNTPIQL RMQASPQHKC PRCWKYHSDQ
PETLCARCDA VLSP
//
