ID A0A0R0M027_9MICR Unreviewed; 1081 AA.
AC A0A0R0M027;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 13-SEP-2023, entry version 33.
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=M153_11200017358 {ECO:0000313|EMBL:KRH94914.1};
OS Pseudoloma neurophilia.
OC Eukaryota; Fungi; Fungi incertae sedis; Microsporidia; Pseudoloma.
OX NCBI_TaxID=146866 {ECO:0000313|EMBL:KRH94914.1, ECO:0000313|Proteomes:UP000051530};
RN [1] {ECO:0000313|EMBL:KRH94914.1, ECO:0000313|Proteomes:UP000051530}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MK1 {ECO:0000313|EMBL:KRH94914.1,
RC ECO:0000313|Proteomes:UP000051530};
RA Ndikumana S., Pelin A., Sanders J., Corradi N.;
RT "The genome of Pseudoloma neurophilia, a relevant intracellular parasite of
RT the zebrafish.";
RL Submitted (JUL-2015) 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 -!- 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:KRH94914.1}.
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DR EMBL; LGUB01000018; KRH94914.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0R0M027; -.
DR VEuPathDB; MicrosporidiaDB:M153_11200017358; -.
DR Proteomes; UP000051530; 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:0006428; P:isoleucyl-tRNA aminoacylation; IEA:InterPro.
DR CDD; cd00818; IleRS_core; 1.
DR Gene3D; 3.40.50.620; HUPs; 2.
DR InterPro; IPR001412; aa-tRNA-synth_I_CS.
DR InterPro; IPR002300; aa-tRNA-synth_Ia.
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; 2.
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:UP000051530}.
FT DOMAIN 14..578
FT /note="Aminoacyl-tRNA synthetase class Ia"
FT /evidence="ECO:0000259|Pfam:PF00133"
FT DOMAIN 599..685
FT /note="Aminoacyl-tRNA synthetase class Ia"
FT /evidence="ECO:0000259|Pfam:PF00133"
FT DOMAIN 735..882
FT /note="Methionyl/Valyl/Leucyl/Isoleucyl-tRNA synthetase
FT anticodon-binding"
FT /evidence="ECO:0000259|Pfam:PF08264"
SQ SEQUENCE 1081 AA; 125731 MW; 318AA9786B79E36B CRC64;
MTTEKFSFPK TEEKILQLWN NHKCFEKQNE IIADRPQFVF HDGPPFATGL PHYGHILSGT
IKDTVTRYAI QQGYSCSRRF GWDCHGLPVE YEIDKANNIT TRKQVIEEIG IANYNQMCKS
IVQKYTDQWE QIVKRMARWV DFKNGYRTMD KSFMESIWYT FSKIYDFGRV YRGFRVMAYS
TACSTPLSNF EANQNYKEVS DPSVVVKFTL KDSSAISDKF VPYSEKESTF DKKALTKPVS
LLIWTTTPWT LPANLGCCVS SEFEYILVLS DKGDEFFILL EERLSAYKQL KNCKVVAKIK
GSDLVGLKYT PIFNDYKDAH PELFQVLNNP NVDPTAGTGI IPNSPAFGEE DYNLFLASGL
LKESDLVPCP LDDKGIFFET EFKGEYFKDA DKLVIQRLKE KNLLICRSDI VHRYPFCWRS
DTPLIYKLVP NWFIKLSDFQ ENLVEVNDRI NWIPNNIKSR FSNWLGAARD WSISRNRFWG
TPIPIWTDDK FETKLVIRSI EQLETLGYRL KDGKKEKVIV TDLHREFIDD ILIDYEGKTL
SRIDEVFDCW FESGSMPYAQ DHWPFSNKNK HVENQMADLS VKNKSNPLED KFASVVPPAP
ADFIAEGLDQ TRGWFYTLHV ISSLLYDRPS YKNIICFGIV LASDGKKMSK RLKNYPDPME
IAKQLGVDSL RFYLISSPVV EAENLKFKTQ GVEEVFKNLL LNWLNCLYFY SETTSHEKTG
VQDEKDLSNV TNVFDKWILN EFSLFCQKIQ KSMVKYDLSS VLPASLQFIE NLSNWYIRMN
RDRIRSENDV LFYILKRFSI CMAPFTPYFA EYSWMFMNDT LHFLDEFLEE TGNTEFDSVH
YQLFPKTMPL FECNFSATKK IIEGIRSLRE QSAISLKTPL NVCKVISDAP LDYSDAIIKE
ECNILNLENA KSQDFQFNLK IKPNFNKIKK SHSDENIKSR ITEINKIKDK VPDHIPNEEI
FVEKTLVFEE KDHVHTTIEL KDDGNSQFIS LILDLRIDDN LLNLKTAREL NAFIQKLRKD
CGLSKSDQIE LSIADPELEN IYKLKYTLIK RSVTNNKMLK TENFEFNGRN VQIGLFESII
Q
//
