ID M2WUG0_GALSU Unreviewed; 1039 AA.
AC M2WUG0;
DT 01-MAY-2013, integrated into UniProtKB/TrEMBL.
DT 01-MAY-2013, sequence version 1.
DT 27-MAR-2024, entry version 45.
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=Gasu_48650 {ECO:0000313|EMBL:EME27570.1};
OS Galdieria sulphuraria (Red alga).
OC Eukaryota; Rhodophyta; Bangiophyceae; Galdieriales; Galdieriaceae;
OC Galdieria.
OX NCBI_TaxID=130081 {ECO:0000313|EMBL:EME27570.1, ECO:0000313|Proteomes:UP000030680};
RN [1] {ECO:0000313|Proteomes:UP000030680}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=074W {ECO:0000313|Proteomes:UP000030680};
RX PubMed=23471408; DOI=10.1126/science.1231707;
RA Schonknecht G., Chen W.H., Ternes C.M., Barbier G.G., Shrestha R.P.,
RA Stanke M., Brautigam A., Baker B.J., Banfield J.F., Garavito R.M., Carr K.,
RA Wilkerson C., Rensing S.A., Gagneul D., Dickenson N.E., Oesterhelt C.,
RA Lercher M.J., Weber A.P.;
RT "Gene transfer from bacteria and archaea facilitated evolution of an
RT extremophilic eukaryote.";
RL Science 339:1207-1210(2013).
CC -!- SIMILARITY: Belongs to the class-I aminoacyl-tRNA synthetase family.
CC {ECO:0000256|ARBA:ARBA00005594, ECO:0000256|RuleBase:RU363035}.
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DR EMBL; KB454530; EME27570.1; -; Genomic_DNA.
DR RefSeq; XP_005704090.1; XM_005704033.1.
DR AlphaFoldDB; M2WUG0; -.
DR STRING; 130081.M2WUG0; -.
DR EnsemblPlants; EME27570; EME27570; Gasu_48650.
DR GeneID; 17086465; -.
DR Gramene; EME27570; EME27570; Gasu_48650.
DR KEGG; gsl:Gasu_48650; -.
DR eggNOG; KOG0433; Eukaryota.
DR OMA; HCWRCKT; -.
DR OrthoDB; 656at2759; -.
DR Proteomes; UP000030680; 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 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 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 Pfam; PF06827; zf-FPG_IleRS; 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:UP000030680}.
FT DOMAIN 101..724
FT /note="Aminoacyl-tRNA synthetase class Ia"
FT /evidence="ECO:0000259|Pfam:PF00133"
FT DOMAIN 771..924
FT /note="Methionyl/Valyl/Leucyl/Isoleucyl-tRNA synthetase
FT anticodon-binding"
FT /evidence="ECO:0000259|Pfam:PF08264"
FT DOMAIN 1003..1032
FT /note="Zinc finger FPG/IleRS-type"
FT /evidence="ECO:0000259|Pfam:PF06827"
SQ SEQUENCE 1039 AA; 120773 MW; D3E1CAB58BCF7076 CRC64;
MFWTDESLLM TSNFCYVLFP VGRQFPTVSG CRCTNNRWKL RKWTVQVRKV FRSHRNVLLC
TLQTERESDR DFWKQFYKNS INLPKTRFEQ RANAAVKELE IQKFWEDHLI YEKVLEANQH
KTFVLHDGPP YANGTLHVGH ALNKILKDII CRYHLLRGFY ACFIPGWDCH GLPIELKVWQ
SIPKENHDKV SVIELRRRAA EFARNTIEEQ KSSFKRFGIW GFWSRPYLTM SPEYEAAQIQ
VFGELFLRGF IYRARKPVHW SPSSKTALAE AELEYSEDHI STAIYVSFRI AHVNSLLGDL
PISSNSLELV IWTTTPWTLP ANEAVAVNPH MTYSLIEVAR LNRFLIVAKD CLKRVREKLK
LEWQDCRQVL EWTGESLVGI KYYHPIIKDK ICRVVRGGNY ITSESGTGLV HTAPGHGEED
FVVGKRENLP ISCPVDENGM FTKEAGEVLF GHSVLGQGNK LVLELVENMN LLLAKECYRH
KYPYDWRTKE PTIYRTTEQW FASLENFRKE VLDSIDQVTW IPESKKNLIR CMVMERSDWC
ISRQRAWGVP IPVFYDVSNG NIPVLDEEIL EHISHIIKEK GSDAWFYMSE EELLPAKHKN
RHLVKGMDTM DVWFDSGCSW AALESKGYLK IPADLYLEGG DQHRGWFQSS LLTCVATKGR
APYLKAITHG FVLDEKGVKM SKSVGNVIDP QVVVNGGNNQ KKDPAYGADV LRLWVASVDY
RNEVLIGPQI IRQVADIYRK IRNTLRFMVG NLYDFRKDVN AIPLAELPQL DIYMLTVFNK
FKKSVESAYE RYDFTSIYQA IQRLCITELS NFYLDISKDR LYVSLPDDYR RRSCQTVLHM
ILEDLVRIVA PLIPHTAEDL WQCFEFRRDA CLSVFQSGWL SNEKVPLGHY PDTFWENVRL
LRDDVNKCLE KAREEQLIGS SLEGRVGIYF NSKDDEKHIS FCHHLRQLSN SSNQVDQLEY
LFLVSQVEFM ESKESLYRVY SYARDSVHSQ LDCYSIGVSK ALGHKCFRCW NFSTSVQQNE
KHPELCHRCI SVVDRLLSK
//
