ID A0A2P7ZQA3_9PEZI Unreviewed; 1246 AA.
AC A0A2P7ZQA3;
DT 23-MAY-2018, integrated into UniProtKB/TrEMBL.
DT 23-MAY-2018, sequence version 1.
DT 27-MAR-2024, entry version 22.
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=B9Z65_335 {ECO:0000313|EMBL:PSK50391.1};
OS Elsinoe australis.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Dothideomycetidae; Myriangiales; Elsinoaceae; Elsinoe.
OX NCBI_TaxID=40998 {ECO:0000313|EMBL:PSK50391.1, ECO:0000313|Proteomes:UP000243723};
RN [1] {ECO:0000313|EMBL:PSK50391.1, ECO:0000313|Proteomes:UP000243723}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NL1 {ECO:0000313|EMBL:PSK50391.1,
RC ECO:0000313|Proteomes:UP000243723};
RA Cheng Q.;
RT "Draft genome sequence of Elsinoe australis.";
RL Submitted (MAY-2017) 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:PSK50391.1}.
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DR EMBL; NHZQ01000138; PSK50391.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2P7ZQA3; -.
DR STRING; 40998.A0A2P7ZQA3; -.
DR Proteomes; UP000243723; 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; IPR020100; Glc-repressible_Grg1.
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; PF11034; Grg1; 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:UP000243723}.
FT DOMAIN 164..847
FT /note="Aminoacyl-tRNA synthetase class Ia"
FT /evidence="ECO:0000259|Pfam:PF00133"
FT DOMAIN 892..1026
FT /note="Methionyl/Valyl/Leucyl/Isoleucyl-tRNA synthetase
FT anticodon-binding"
FT /evidence="ECO:0000259|Pfam:PF08264"
FT REGION 35..90
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1191..1246
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 49..63
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 76..90
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1195..1219
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1220..1246
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1246 AA; 137915 MW; D76CE9A620D17DA1 CRC64;
MSAPNADKPN EGIVGQISNS VSNAANYVSE TIQGKGAEAS KEANKEQAKG NVAGQSSVSD
RVSGALGAAS DKMDQTTHES SAKANKHSNK FIDHQDTTDI HWDGITDMTG FTAPSRLLRI
AQAASGDVNW SATLNLPKIT FPPRATAEDF QTYRKRCSQE LYAWQKENRP GSDDNGSDNT
FVLHDGPPYA NGAVHVGHAV NKVLKDLIVR TNLSRGKQVH YRPGWDCHGL PIELKALRAS
GDVGLQGKSQ QNNLAGEEAK TSTALPKVDP LSIRAQARQL AQDTVKEQSE NFQSWGVMGD
WDTPYLTMNK EFEIRQLGVF KEMVAKGLIY RQNKPVHWSP SSRTALAEAE LEYDDNHKVT
TAYIKFPITK LPPILAQNGY VDPNRLTALI WTTTPWTLPA NTAIGVRSDI IYTLIELPDE
GQLLVAKDRL EALKAHFNDV PAEIIIDEIP GSALVDGSTE YVNVLSGKTS RIIDVDFVTS
TSGTGLVHLA SGHGMDDYLA LKAQGFNDVF APVDDEGKFT AEALPSDPRQ LQGLYVESKG
AKAVLEILRN RPETLPIKTH DGLSLVLATE NLTHKNPIDW RTKQPVITRA TDQWFANVGS
VQDSAIQSLE AVEFIPETGK NRLQSFLRGR SQWCISRQRS WGVPIPALYK KDTGEAVMTV
ESIEHIISII EQRGTDAWWS DAADDSAWIS SSLPPGEYVR GMDTMDVWFD SGTSWTSVDP
RQGKPIADVY VEGTDQHRGW FQSSVLTHVS SGSDSQAPAA PFGHLITHGF TLDSQGHKMS
KSLGNVVTPD EILRGVLKTP TKSSKSSKSK SAPIVLAPQT NRPSTLGPDA LRLWVASSDY
TRDITISQPS LLAIHQSLSK YRTTFKFLLG VTSDYPSPYP DENLLNDLTF ADQSLLHSLS
KTSSHIHRLQ NAYEFSRSLQ SLNAFINNDL SASYLEIAKD RLYAADPETR LHTQTILMIV
LDELLLMLAP ITPLLVEEVW HHSPAERRDN APHPLHRIYD GPFRAQDETE EESVHALEKA
VRQMRRVGDA VKGAQEEARR MGKLGSGLAC QVEVLVPQDA DEEFKALVSN LEAEGELEEV
LVVSGAEVLP REEELRRRLR EEEEGDETLG EVARGMREWR ENVAWEVERE FSCGVEGEEE
EGVKGLVKII PSVGGKCERC WKYNVLDVVE EDGEEQIPIC DRCQEVLGLV GEEGEGGQEG
EEGGEQDEDE MDEEEDEEDE PNRGGRHLRE QRKQSWRERF GIGGRR
//
