ID M2VZK8_GALSU Unreviewed; 1056 AA.
AC M2VZK8;
DT 01-MAY-2013, integrated into UniProtKB/TrEMBL.
DT 01-MAY-2013, sequence version 1.
DT 13-SEP-2023, entry version 42.
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_38250 {ECO:0000313|EMBL:EME28776.1};
OS Galdieria sulphuraria (Red alga).
OC Eukaryota; Rhodophyta; Bangiophyceae; Galdieriales; Galdieriaceae;
OC Galdieria.
OX NCBI_TaxID=130081 {ECO:0000313|EMBL:EME28776.1, 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 -!- 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 Evidence={ECO:0000256|ARBA:ARBA00000114};
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; KB454516; EME28776.1; -; Genomic_DNA.
DR RefSeq; XP_005705296.1; XM_005705239.1.
DR AlphaFoldDB; M2VZK8; -.
DR EnsemblPlants; EME28776; EME28776; Gasu_38250.
DR GeneID; 17087627; -.
DR Gramene; EME28776; EME28776; Gasu_38250.
DR KEGG; gsl:Gasu_38250; -.
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; cd07961; Anticodon_Ia_Ile_ABEc; 1.
DR CDD; cd00818; IleRS_core; 1.
DR Gene3D; 3.40.50.620; HUPs; 2.
DR Gene3D; 3.90.740.10; Valyl/Leucyl/Isoleucyl-tRNA synthetase, editing domain; 1.
DR HAMAP; MF_02003; Ile_tRNA_synth_type2; 1.
DR InterPro; IPR001412; aa-tRNA-synth_I_CS.
DR InterPro; IPR002300; aa-tRNA-synth_Ia.
DR InterPro; IPR033709; Anticodon_Ile_ABEc.
DR InterPro; IPR002301; Ile-tRNA-ligase.
DR InterPro; IPR023586; Ile-tRNA-ligase_type2.
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; PTHR42780:SF1; ISOLEUCINE--TRNA LIGASE, CYTOPLASMIC; 1.
DR PANTHER; PTHR42780; SOLEUCYL-TRNA SYNTHETASE; 1.
DR Pfam; PF08264; Anticodon_1; 1.
DR Pfam; PF19302; DUF5915; 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:UP000030680}.
FT DOMAIN 22..655
FT /note="Aminoacyl-tRNA synthetase class Ia"
FT /evidence="ECO:0000259|Pfam:PF00133"
FT DOMAIN 712..864
FT /note="Methionyl/Valyl/Leucyl/Isoleucyl-tRNA synthetase
FT anticodon-binding"
FT /evidence="ECO:0000259|Pfam:PF08264"
SQ SEQUENCE 1056 AA; 122428 MW; A421393627B29260 CRC64;
MSKRDALDEV PERVSFPEEE RKILQFWEEK SAFHTSMDMS KGRQTFSFYD GPPFATGLPH
YGNILAGTIK DVVTRYAYQT GHDVPRRFGW DCHGLPVEHE IDKKLGVKCR EDVLRLGIDK
YNAECRSIVL RYASEWETIV KRLGRWIDFK NDYKTLDMTY MESVWWVFKQ LYLKGLVYRG
FRVMPYSTAL NTPMSNFEAN LNYKEISDPS VIVSFPLLTD PNTCLLAWTT TPWTLPSNLS
LCVHPDLDYV TVEDTIQGKK YIFAEGRKEE CLKALRRDSK KASSEVLRIT SRCKGTDLKG
LQYQPLFEYF YERFKDKAFL VLVDEYVTSD TGTGIVHQAP AFGEDDFRVC SNAGIISYND
EVPCPIDDNG RFIQPVTDFC GLHVKEADKS IIQFIKSLNR LITNERIVHS YPFCWRSETP
LIYRAVPSWF VRVESFRNRL TENNKKSSWV PEAVQFNRFG NWLENARDWN VSRNRYWGTP
IPIWMSDDKQ EIVVIGSEEE LRQLAGLQEK LTDLHRDSID HITIQSKSGK VLRRVDEVFD
CWFESGSMPY ASIHYPFEPD SEAVFRSTFP AVFVAEGLDQ TRGWFYTLMV LSTALFDKPA
FQHCIVNGLI LAEDGKKMSK RLKNYPDPIQ VTESHGADAL RLYLINSPVV RAETLRFKES
GVREVVRDVI LPWYNAYRFF VQNVKQYELE MDEEFGAIEL DLLSKSNVNE MDHWIESSLA
SLVLYVRKEM EAYHLYNVVP RLLGFIDSLT NWYVRLNRPR LKGNSGKKEW KTSLTVLGDV
LIVFCRLMAP FAPFTSEMIF QNLKKVAPLD SFADSVHYLM IPEPRLHSID QKFEQTVSYI
QQVILLGRIA RDRRNVPLKQ PLRKLVIIHR DAQVLEAIRQ LESYIVLELN VKQLVYTTEE
KQYVLLRADA DGRALGSKLG KDFAKIRSAI QQLSSDDIFE LEQSGKLDIE GHCILLEQVK
VIRQVKKDIT MLQEEYEMVA SNDTSGLLIF MDMKQDENLY EEGIARELIN RVQKLRKKAG
LLPRDEIEVF VDTDDVLLRR YMTLSLKCVC SCNILT
//
