SYIM_MACFA
ID SYIM_MACFA Reviewed; 993 AA.
AC Q4R646;
DT 02-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT 02-MAY-2006, sequence version 2.
DT 03-AUG-2022, entry version 89.
DE RecName: Full=Isoleucine--tRNA ligase, mitochondrial;
DE EC=6.1.1.5;
DE AltName: Full=Isoleucyl-tRNA synthetase;
DE Short=IleRS;
DE Flags: Precursor; Fragment;
GN Name=IARS2; ORFNames=QtsA-19161;
OS Macaca fascicularis (Crab-eating macaque) (Cynomolgus monkey).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC Cercopithecidae; Cercopithecinae; Macaca.
OX NCBI_TaxID=9541;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Testis;
RG International consortium for macaque cDNA sequencing and analysis;
RT "DNA sequences of macaque genes expressed in brain or testis and its
RT evolutionary implications.";
RL Submitted (JUN-2005) to the EMBL/GenBank/DDBJ databases.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-isoleucine + tRNA(Ile) = AMP + diphosphate + L-
CC isoleucyl-tRNA(Ile); Xref=Rhea:RHEA:11060, Rhea:RHEA-COMP:9666,
CC Rhea:RHEA-COMP:9695, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019,
CC ChEBI:CHEBI:58045, ChEBI:CHEBI:78442, ChEBI:CHEBI:78528,
CC ChEBI:CHEBI:456215; EC=6.1.1.5;
CC -!- SUBCELLULAR LOCATION: Mitochondrion matrix {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the class-I aminoacyl-tRNA synthetase family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAE01429.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AB169344; BAE01429.1; ALT_INIT; mRNA.
DR AlphaFoldDB; Q4R646; -.
DR SMR; Q4R646; -.
DR STRING; 9541.XP_005540946.1; -.
DR eggNOG; KOG0433; Eukaryota.
DR Proteomes; UP000233100; Unplaced.
DR GO; GO:0005759; C:mitochondrial matrix; IEA:UniProtKB-SubCell.
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; 3.40.50.620; -; 2.
DR Gene3D; 3.90.740.10; -; 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; IPR033708; Anticodon_Ile_BEm.
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; IPR014729; Rossmann-like_a/b/a_fold.
DR InterPro; IPR009080; tRNAsynth_Ia_anticodon-bd.
DR InterPro; IPR009008; Val/Leu/Ile-tRNA-synth_edit.
DR InterPro; IPR010663; Znf_FPG/IleRS.
DR Pfam; PF08264; Anticodon_1; 1.
DR Pfam; PF00133; tRNA-synt_1; 1.
DR Pfam; PF06827; zf-FPG_IleRS; 1.
DR PRINTS; PR00984; TRNASYNTHILE.
DR SUPFAM; SSF47323; SSF47323; 1.
DR SUPFAM; SSF50677; SSF50677; 1.
DR TIGRFAMs; TIGR00392; ileS; 1.
DR PROSITE; PS00178; AA_TRNA_LIGASE_I; 1.
PE 2: Evidence at transcript level;
KW Acetylation; Aminoacyl-tRNA synthetase; ATP-binding; Ligase; Mitochondrion;
KW Nucleotide-binding; Protein biosynthesis; Reference proteome;
KW Transit peptide.
FT TRANSIT <1..29
FT /note="Mitochondrion"
FT /evidence="ECO:0000255"
FT CHAIN 30..993
FT /note="Isoleucine--tRNA ligase, mitochondrial"
FT /id="PRO_0000233336"
FT MOTIF 97..107
FT /note="'HIGH' region"
FT /evidence="ECO:0000250"
FT MOTIF 645..649
FT /note="'KMSKS' region"
FT /evidence="ECO:0000250"
FT BINDING 648
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT MOD_RES 55
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q8BIJ6"
FT MOD_RES 55
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q8BIJ6"
FT MOD_RES 170
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q9NSE4"
FT MOD_RES 175
FT /note="N6-succinyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q8BIJ6"
FT MOD_RES 214
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q9NSE4"
FT MOD_RES 222
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q9NSE4"
FT MOD_RES 222
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q8BIJ6"
FT MOD_RES 460
FT /note="N6-succinyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q8BIJ6"
FT MOD_RES 481
FT /note="N6-succinyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q8BIJ6"
FT MOD_RES 706
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q8BIJ6"
FT MOD_RES 756
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q9NSE4"
FT MOD_RES 756
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q8BIJ6"
FT MOD_RES 762
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q9NSE4"
FT MOD_RES 762
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q8BIJ6"
FT NON_TER 1
SQ SEQUENCE 993 AA; 111941 MW; E8C8F0C7458F0AD2 CRC64;
SLWGTPRLPC SPGWQGATKR LLVRSVSGAS NHQPNSNTGR YRDTVLLPQT SFPMKLLGRQ
QPDKELEIQQ KCGFSELYSW QRERKVKTEF CLHDGPPYAN GDPHVGHALN KILKDIANRF
HMMSGSKVHF VPGWDCHGLP IEIKVLSELG REAQNLSAME IREKARSFAK AAIEKQKSAF
IRWGIMADWN NCYYTFDGKY EAKQLRTFYQ MYDKGLVYRS YKPVFWSPSS RTALAEAELE
YNPEHVSRSI YVKFPLLKPS PKLASLIDGS SPVSFLVWTT QPWTIPANEA VCYMPESKYA
VVKCSKSGDL YVLAADKVET VASTLETAFE TISTFSGVDL ENGTCSHPLI PDKASPLLPA
NHVTMAKGTG LVHTAPAHGM EDYGVASQHN LPMDCLVDED GVFTDVAGPE LQNKAVLEEG
TDVVIKMLQT AKNLLKEEKL VHSYPYDWRT KKPVVIRASK QWFINIADIK IAAKELLKKV
KFIPGSALNG MVEMMDRRPY WCISRQRVWG VPIPVFHHKT KDEYLINSQT IEHIVKLVEQ
HGSDVWWTLP PEQLLPKEVL SEVGGPDALE YVPGQDILDI WFDSGTSWSH VLPGPDQRAD
LYLEGKDQLG GWFQSSLLTS VATRKKAPYK TVIVHGFTLG EKGEKMSKSL GNVIHPDVVV
NGGQDQSKEP PYGADVLRWW VADSNVFTEV AIGPSVLNAA RDDISKLRNT LRFLLGNVAD
FNPETDSIPV NDMYVIDQYM LHLLQDLANK ITELYKQYDF GKVVRLLRTF YTRELSHFYF
SIIKDRLYCE KENDPRRRSC QTALVEILDV IVRSFAPILP HLAEEVFQHI PYIKEPKSVF
RTGWISTSSI WKKPGLEEAV ESVCAMRDSF LGSIPGKNAA EYKVIIVIEP GLLFEIIEML
QSEETSSTSQ LNELMMASES TLLAQEPREL TADVIELKGK FLINLEGGDI REESSYKVIV
MPTTKEKCPR CWKYTAESSD TLCPRCAEVV SGK
