ID A0A2H3IBN3_9EURO Unreviewed; 1366 AA.
AC A0A2H3IBN3;
DT 31-JAN-2018, integrated into UniProtKB/TrEMBL.
DT 31-JAN-2018, sequence version 1.
DT 27-MAR-2024, entry version 20.
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=PENO1_054530 {ECO:0000313|EMBL:PCG99102.1};
OS Penicillium occitanis (nom. inval.).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Penicillium.
OX NCBI_TaxID=290292 {ECO:0000313|EMBL:PCG99102.1, ECO:0000313|Proteomes:UP000218381};
RN [1] {ECO:0000313|EMBL:PCG99102.1, ECO:0000313|Proteomes:UP000218381}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CL100 {ECO:0000313|EMBL:PCG99102.1,
RC ECO:0000313|Proteomes:UP000218381};
RX PubMed=28951729; DOI=10.3389/fmicb.2017.01627;
RA Bravo-Ruiz G., Sassi A.H., Marcet-Houben M., Di Pietro A., Gargouri A.,
RA Gabaldon T., Roncero M.I.G.;
RT "Regulatory Mechanisms of a Highly Pectinolytic Mutant of Penicillium
RT occitanis and Functional Analysis of a Candidate Gene in the Plant Pathogen
RT Fusarium oxysporum.";
RL Front. Microbiol. 8:1627-1627(2017).
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:PCG99102.1}.
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DR EMBL; NPFK01000146; PCG99102.1; -; Genomic_DNA.
DR STRING; 290292.A0A2H3IBN3; -.
DR OrthoDB; 656at2759; -.
DR Proteomes; UP000218381; 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:0016491; F:oxidoreductase activity; IEA:InterPro.
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 CDD; cd08276; MDR7; 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; 3.90.180.10; Medium-chain alcohol dehydrogenases, catalytic domain; 1.
DR Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
DR Gene3D; 3.90.740.10; Valyl/Leucyl/Isoleucyl-tRNA synthetase, editing domain; 1.
DR HAMAP; MF_02002; Ile_tRNA_synth_type1; 1.
DR InterPro; IPR001412; aa-tRNA-synth_I_CS.
DR InterPro; IPR002300; aa-tRNA-synth_Ia.
DR InterPro; IPR013149; ADH-like_C.
DR InterPro; IPR013154; ADH-like_N.
DR InterPro; IPR033708; Anticodon_Ile_BEm.
DR InterPro; IPR011032; GroES-like_sf.
DR InterPro; IPR002301; Ile-tRNA-ligase.
DR InterPro; IPR023585; Ile-tRNA-ligase_type1.
DR InterPro; IPR013155; M/V/L/I-tRNA-synth_anticd-bd.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR InterPro; IPR020843; PKS_ER.
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; PF08240; ADH_N; 1.
DR Pfam; PF00107; ADH_zinc_N; 1.
DR Pfam; PF08264; Anticodon_1; 1.
DR Pfam; PF00133; tRNA-synt_1; 1.
DR PRINTS; PR00984; TRNASYNTHILE.
DR SMART; SM00829; PKS_ER; 1.
DR SUPFAM; SSF47323; Anticodon-binding domain of a subclass of class I aminoacyl-tRNA synthetases; 1.
DR SUPFAM; SSF50129; GroES-like; 1.
DR SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 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:UP000218381}.
FT DOMAIN 23..356
FT /note="Enoyl reductase (ER)"
FT /evidence="ECO:0000259|SMART:SM00829"
SQ SEQUENCE 1366 AA; 152221 MW; 3983AF57C21D870D CRC64;
MPSKYQAWRV HPNASTHDEK SIDILENLVL EEAEKPLPDP GQVLVRIHAA ALNFRDLLIT
AFSPKYPVPT IPGLSPCSDG AGSIEAMGPS KNSRWKVGDE VIFRVTNSWD DGDVSNFKGN
GLGSGDIQGT LSQYLLVDES WLVKKPSHLT WEQAASIAGA GGTAIQALFH NGISNGLDLS
GKTVLTQGTG GSSIFSAQFA VAAGARVIGT TSSDSKAELL KDLGVHEVVN YRTHPSWADE
VLKLTDGRGV DLVIDVGGSA TFEQSLKAAR FGGTVAAVGF MTEPQPSDPG LIHAIIFGAK
TIRGQMAASL EMYHELVEFM ERHKIEPVVG QVSEWTEAKD AFKALMRQSV PGKIVIKSSR
PIHHIQAHMS AATPEVLPRS TFPARVPVAD QAKYLRRCSD ELYAWQRENR PASDTFVLHD
GPPYANGELH VGHALNKILK DIINRTQLSR GKRVHYVPGW DCHGLPIELK ALQAQQKDGN
DFSKGPGSAA TIRKAARKLA EKTVREQMRE FRAWGVMGDW EGHYKTLDKK FEMNQLGIFR
EMVEKGLIYR RFKPVYWSPS TGTALAEAEL EYNENHISAA ALVRFPLVKM PEQIRNNPLV
DTEALSAVIW TTTPWTLPAN AAIAVSESLN YLIVQSSTHG QLLIAESRLS YFQDMLKEDL
QVLVPSIQGS ELCQGTTYRP LFPREEIPEQ PIIAADFVTA DSGSGLVHCA PGHGMDDYEV
CLEQGIRAFA PVNDEGLFTN EAMPHDPSFL AGKSVLDEGN TLVLQYVEST NQLLNQHKYE
HKYPYDWRSK KPIIIRATEQ WFADVANIRE SALASLEEVN FVPATGRQRL KNFVQNRTEW
CISRQRAWGV PIPALYDKTT GQAVLTKETV SHIMNVIEER GIDAWWTDSP EDPSWIPQHL
QQEGSPGYRR GTDTMDVWFD SGTSWTQVKD ESLKKERPAD IYLEGTDQHR GWFQSSLLTY
VSHQVASGKV QPSTVKAPFK HLITHGFTLD QDARKMSKSI GNIMLPEAIM NGTLLPPLKQ
KKSKGAKEQK PSGPVYDALG PDALRLWVAS SDYTRDVVIG QQVLQTVNTS LHKYRVTFKL
LLGALGDFDP AANLRQYEDL HEIDRQALMQ LTRLVETCRN AFDNFEFYRA VNALNRWTNL
EFSAFYMETL KDRLYTEAED SASRRAAQTT LFYIYTYLQE LLAPITPLLV EESWEHTPEL
VKALLEHPLQ RVARTAPNEW VDEAISNDFI DLMAANTAVK AIQESARSKK QMGSSLQSYV
HFELPDNASL DIFQRYINEL PDLFVVSSVS LSVKGSDLPG DIASAEWSYA EEFELSNSGK
KTTVHVYAPN QAKCPRCWRY VAPEPLAEEA PLCKRCDDVI NKLDGN
//
