ID A6REA0_AJECN Unreviewed; 1506 AA.
AC A6REA0;
DT 21-AUG-2007, integrated into UniProtKB/TrEMBL.
DT 21-AUG-2007, sequence version 1.
DT 27-MAR-2024, entry version 83.
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=HCAG_07965 {ECO:0000313|EMBL:EDN04299.1};
OS Ajellomyces capsulatus (strain NAm1 / WU24) (Darling's disease fungus)
OS (Histoplasma capsulatum).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Onygenales; Ajellomycetaceae; Histoplasma.
OX NCBI_TaxID=2059318 {ECO:0000313|EMBL:EDN04299.1, ECO:0000313|Proteomes:UP000009297};
RN [1] {ECO:0000313|Proteomes:UP000009297}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NAm1 / WU24 {ECO:0000313|Proteomes:UP000009297};
RX PubMed=19717792; DOI=10.1101/gr.087551.108;
RA Sharpton T.J., Stajich J.E., Rounsley S.D., Gardner M.J., Wortman J.R.,
RA Jordar V.S., Maiti R., Kodira C.D., Neafsey D.E., Zeng Q., Hung C.-Y.,
RA McMahan C., Muszewska A., Grynberg M., Mandel M.A., Kellner E.M.,
RA Barker B.M., Galgiani J.N., Orbach M.J., Kirkland T.N., Cole G.T.,
RA Henn M.R., Birren B.W., Taylor J.W.;
RT "Comparative genomic analyses of the human fungal pathogens Coccidioides
RT and their relatives.";
RL Genome Res. 19:1722-1731(2009).
CC -!- SIMILARITY: Belongs to the class-I aminoacyl-tRNA synthetase family.
CC {ECO:0000256|ARBA:ARBA00005594}.
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DR EMBL; CH476664; EDN04299.1; -; Genomic_DNA.
DR STRING; 339724.A6REA0; -.
DR VEuPathDB; FungiDB:HCAG_07965; -.
DR HOGENOM; CLU_001493_3_0_1; -.
DR OMA; YHDHKST; -.
DR OrthoDB; 656at2759; -.
DR Proteomes; UP000009297; 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; 1.10.10.830; Ile-tRNA synthetase CP2 domain-like; 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; IPR033708; Anticodon_Ile_BEm.
DR InterPro; IPR002301; Ile-tRNA-ligase.
DR InterPro; IPR013155; M/V/L/I-tRNA-synth_anticd-bd.
DR InterPro; IPR005373; PHAF1.
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 PANTHER; PTHR42765:SF1; ISOLEUCINE--TRNA LIGASE, MITOCHONDRIAL; 1.
DR PANTHER; PTHR42765; SOLEUCYL-TRNA SYNTHETASE; 1.
DR Pfam; PF08264; Anticodon_1; 1.
DR Pfam; PF03676; PHAF1; 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 ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Ligase {ECO:0000256|ARBA:ARBA00022598};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Protein biosynthesis {ECO:0000256|ARBA:ARBA00022917};
KW Reference proteome {ECO:0000313|Proteomes:UP000009297}.
FT DOMAIN 547..1187
FT /note="Aminoacyl-tRNA synthetase class Ia"
FT /evidence="ECO:0000259|Pfam:PF00133"
FT DOMAIN 1231..1387
FT /note="Methionyl/Valyl/Leucyl/Isoleucyl-tRNA synthetase
FT anticodon-binding"
FT /evidence="ECO:0000259|Pfam:PF08264"
FT REGION 268..322
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 275..322
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1506 AA; 167700 MW; 2E5CCB1C81BB4826 CRC64;
MTTSRNMTPA QIFPGRGIGF LTLGASLHHT ITRLKAHPHT YPSIDLSYSS TNPIHSPILL
SLPENGLRLR FDGPDQRLRL IEVLDFTKIP LTYKSHEVLK AAKPTEQPPQ LGPSFRHIYN
RMFGPSYPGE FIPGSSGSKY GTYVLSYPGI AFSFPLLQSA WSEQCDFVSL MSSAAASSAT
SMAVFQGSSW ADGRSNMLTR QPQYPRSTAL AGKNRESVAD EIEEVKIHGA GRIEFFRRSG
PSIWISLSET TPQDLVAEFG PPDAIYRKND RRISIHGTQT LGNTNLRRTS PSPGRTADPT
DMDPLSETSV TDDSDGENSP TFQHNRATLA TECFYNYFDH GFDAFISHPT VSGPPFPGSS
HPETSTISPP PQLAVTKILL HGNVPGSYPF NRHRRSRWVL NIDSAREPLT SETQYGQLSD
ELKRIWKGSY SSASEEMALQ RGMVLNRGWG DSPGSSVELL GGWEDSSASK AWTGSVNDGG
QTLGNTELFG FPAFDAQAEI CCNNRNMPEL PQSLARSWSS TLKLPKSTFP PRVSLTDQVK
YLERCTHDLY SWQQRHRPNE NRFVLHDGPP YANGDLHVGH ALNKILKDII CRVQLAAGKR
VDYVPGWDCH GLPIELKALQ TQKGLGRLEA GRNGNGGAAA IRRAARQLAE KTALEQMKGF
HKWAVMADWK NAWKTMDKSF EKRQLDVFLK MVEKGLIHRR FKPVYWSPSS RTALAEAELE
YKEDHKSTAG LVKFPLVSMP SKLRDMLPSN TTEISAVIWT TTPWTLPANA AIAVSRTLEY
SIVKSEKHGY LVVGSSRREY IQTLLQGEEV TVIGSPILGC ELVSESTYLP LFKDGSVPQP
VIAADFVTAD SGSGLVHCAP GHGMEDYEVC QAHGIASHTP VDDAGLFTDA AMPLNPSMLS
GKSVLGDGNR EVLRYVESKG QLLAKHTYEH KYPYDWRSKL PVIALEDVQF IPSMGKSRLE
SFIKSRSEWC ISRQRAWGVP IPALYNRETG EEILTKESVS HILKVIDERG IDAWWTDDEN
DPTWIAASIR ETSSGAAYKR GTDTMDVWFD SGSSWTQVKT PASVEGYAAD VYLEGTDQHR
GWFQSSLLTY IAYNLGLGGK TGISRAPFKT LITHGFTLDK DSRKMSKSIG NVISPDQILD
GTLLPPLKLK RMKGEEKKPT APVFDALGTD ALRLWVASSD YTKDIVISQP VLKTVHTNLH
KYRVTFKLLL GSLQDFDPSC TVPHESLRII DKIALLQLRK LINICQDAYS SFEFYRAITA
INKWANLDFS AFYIESLKDR LYADCPNSLS RRAAQTTLCH IYYHFQNLLA PLLPNLVEES
WEHTPELIKT KFDPPLHRIM TKPPPEWQND ELEEIFPLLM AINTAVKTMQ ENARNRKEMG
SSLQTFVHIS VSCSAAGASI FEKFGYELQD LFVVSSVTVG YNNAALPPEI EAAEWKYSSD
FEFPGGSARG HVWIYTPQAI KCGRCWRYAV PLEPKQDDPL CQRCIDVVGE LPRVNHELTG
AASTSN
//
