ID S8B8U8_DACHA Unreviewed; 1451 AA.
AC S8B8U8;
DT 16-OCT-2013, integrated into UniProtKB/TrEMBL.
DT 16-OCT-2013, sequence version 1.
DT 27-MAR-2024, entry version 50.
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=H072_11146 {ECO:0000313|EMBL:EPS35468.1};
OS Dactylellina haptotyla (strain CBS 200.50) (Nematode-trapping fungus)
OS (Monacrosporium haptotylum).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Orbiliomycetes;
OC Orbiliales; Orbiliaceae; Dactylellina.
OX NCBI_TaxID=1284197 {ECO:0000313|EMBL:EPS35468.1, ECO:0000313|Proteomes:UP000015100};
RN [1] {ECO:0000313|EMBL:EPS35468.1, ECO:0000313|Proteomes:UP000015100}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 200.50 {ECO:0000313|EMBL:EPS35468.1,
RC ECO:0000313|Proteomes:UP000015100};
RX PubMed=24244185;
RA Meerupati T., Andersson K.M., Friman E., Kumar D., Tunlid A., Ahren D.;
RT "Genomic mechanisms accounting for the adaptation to parasitism in
RT nematode-trapping fungi.";
RL PLoS Genet. 9:E1003909-E1003909(2013).
RN [2] {ECO:0000313|Proteomes:UP000015100}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 200.50 {ECO:0000313|Proteomes:UP000015100};
RA Ahren D.G.;
RT "Genomic mechanisms accounting for the adaptation to parasitism in
RT nematode-trapping fungi.";
RL Submitted (APR-2013) 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 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}.
CC -!- SIMILARITY: Belongs to the peptidase C13 family.
CC {ECO:0000256|ARBA:ARBA00009941}.
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:EPS35468.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AQGS01001130; EPS35468.1; -; Genomic_DNA.
DR RefSeq; XP_011116516.1; XM_011118214.1.
DR STRING; 1284197.S8B8U8; -.
DR eggNOG; KOG0434; Eukaryota.
DR eggNOG; KOG1349; Eukaryota.
DR HOGENOM; CLU_001493_1_0_1; -.
DR OMA; LLTYWNT; -.
DR OrthoDB; 656at2759; -.
DR UniPathway; UPA00196; -.
DR Proteomes; UP000015100; Unassembled WGS sequence.
DR GO; GO:0042765; C:GPI-anchor transamidase complex; IEA:InterPro.
DR GO; GO:0002161; F:aminoacyl-tRNA editing activity; IEA:InterPro.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0003923; F:GPI-anchor transamidase activity; IEA:InterPro.
DR GO; GO:0004822; F:isoleucine-tRNA ligase activity; IEA:UniProtKB-EC.
DR GO; GO:0000049; F:tRNA binding; IEA:InterPro.
DR GO; GO:0016255; P:attachment of GPI anchor to protein; IEA:InterPro.
DR GO; GO:0006428; P:isoleucyl-tRNA aminoacylation; IEA:InterPro.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR CDD; cd07961; Anticodon_Ia_Ile_ABEc; 1.
DR CDD; cd00818; IleRS_core; 1.
DR Gene3D; 3.40.50.1460; -; 1.
DR Gene3D; 3.40.50.620; HUPs; 2.
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; IPR028361; GPI_transamidase.
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; IPR001096; Peptidase_C13.
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; PF01650; Peptidase_C13; 1.
DR Pfam; PF00133; tRNA-synt_1; 1.
DR PIRSF; PIRSF500138; GPI8; 1.
DR PIRSF; PIRSF019663; Legumain; 1.
DR PRINTS; PR00776; HEMOGLOBNASE.
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 Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Ligase {ECO:0000256|ARBA:ARBA00022598, ECO:0000256|RuleBase:RU363035};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW ECO:0000256|RuleBase:RU363035}; Protease {ECO:0000256|ARBA:ARBA00022670};
KW Protein biosynthesis {ECO:0000256|ARBA:ARBA00022917,
KW ECO:0000256|RuleBase:RU363035};
KW Reference proteome {ECO:0000313|Proteomes:UP000015100};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 1425..1445
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 13..634
FT /note="Aminoacyl-tRNA synthetase class Ia"
FT /evidence="ECO:0000259|Pfam:PF00133"
FT DOMAIN 690..845
FT /note="Methionyl/Valyl/Leucyl/Isoleucyl-tRNA synthetase
FT anticodon-binding"
FT /evidence="ECO:0000259|Pfam:PF08264"
FT ACT_SITE 1206
FT /evidence="ECO:0000256|PIRSR:PIRSR019663-1"
FT ACT_SITE 1248
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PIRSR:PIRSR019663-1"
SQ SEQUENCE 1451 AA; 166381 MW; 4607397A7A7B3D6F CRC64;
MASINFSKEE ERILAFWQEI DAFRTSVKLS EGRKPFTFYD GPPFATGLPH YGHLLASTIK
DIVPRYAHMR GHYVERRFGW DTHGLPVEHE IDKKLGITGK EDVMKMGIKA YNAECRAIVM
RYAEEWEKTI GRLGRWIDFQ NDYKTLKPEF METVWWVFKQ LFDKEQVYRG YRVMPYSTAC
TTPLSNFEAQ QNYKDVQDPA VVVTFPLLDD PETSLLAWTT TPWTLPSHTG IAAHPDFEYI
KIFDEKTGHH YILLEACLKT LYKDPKKAKF KIVDKLKGKD MLGWKYEPLF PYFYDQFKEH
GFQVLNATYV TQDSGVGLVH QAPAFGEEDY NVAFESGVIN DKRLPPNPVD EAGKFTAEVT
DFAGMYVKDA DKKIIKHLKE KGRLIVESTI MHSYPFCWRS DTPLLYKAMP AWFVKIPTIV
PKMLENIETM HWVPGAIKDK RFSSWIANAR DWNISRNRYW GTPLPIWVSE DYEEMVCIGS
VAELEELSGV KGIKDLHRDS IDHITIPSKK GKGDLKRIEE VFDCWFESGS MPYASKHYPF
ENKDSFEKAF PADFIAEGLD QTRGWFYTLV VLGTHLFGIS PFKNCIVNGI VLAEDGKKMS
KRLKNYPDPT LVMDTYGADP LRLYVINSPV VRAEPLRFKE AGVKEVVSKV LLPLWNSYNF
FAGQALLFKK IHGEDFIFHL EGGGSKNVMD RWILASTSSF LDYVNKEMAA YRLYTVVPRI
LEMIDNMTNW YIRFNRKRLK GEYGKEDTLH ALNSLFEVLF TLVRGMAPFT PFITDNLYQR
LLPHIPKEML PEDHRSVHFL SYPEVREELF DPAVERQVGR MQKVIELGRV CREHKTIGLK
VPLKTLVVIH PDTEYLSDVE SLQSYIKEEL NIRELVLSSD EDKYGVKYSL QADWPTLGKK
LKKDVQRVKK ALPSLSSADC KAFIANKEIT VDGIKLVEED LRVFRDVDPE SPYCKDHATN
TDQDVLVILD VALHPELQGE GLGREIINRV QKLRKKAGLV ATDDVKMVFK MKEDPIGLAE
VFEEQSAAIE KVLRRKVEQD EGATGEVVAE EDQEIQVMKL SAWGGLALVS SLFSAPACLA
HSQHTSNWAV LVSTSRFWFN YRHLANVLSM YRTVKRLGIP DSQIILMLSD DVACNPRNTF
PGTVYNNADR AIDLYGDNIE VDYRGYEVTV ENFIRLLTDR VPPDTPRSKR LLTDDRSNIF
IYMTGHGGNE FLKFQDAEEI SAFDIADAFQ QMFEKKRYNE MLFMIDTCQA NTMYSKFYSP
NILATGSSEL DQSSYSHHAD NDVGVAVIDR YTYFNLEYLE THVKNASSKH TLADLFSSYD
PVKIASTPGI RTDLFRRDLK EVLITDFLGN VQSVEVDGDG MRLDEDLLSL ARGAGYNISE
AEWKEAMKGT RDLYEQEKEK IAATAREQKT WSGPARVHKD GETDFWRNVM SAGAVAVCFL
GYWLFSFVDK V
//
