ID S8CJT7_9LAMI Unreviewed; 598 AA.
AC S8CJT7;
DT 16-OCT-2013, integrated into UniProtKB/TrEMBL.
DT 16-OCT-2013, sequence version 1.
DT 27-MAR-2024, entry version 28.
DE RecName: Full=tRNA(Ile)-lysidine synthetase {ECO:0000256|ARBA:ARBA00013267};
DE EC=6.3.4.19 {ECO:0000256|ARBA:ARBA00013267};
DE Flags: Fragment;
GN ORFNames=M569_07840 {ECO:0000313|EMBL:EPS66935.1};
OS Genlisea aurea.
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC asterids; lamiids; Lamiales; Lentibulariaceae; Genlisea.
OX NCBI_TaxID=192259 {ECO:0000313|EMBL:EPS66935.1, ECO:0000313|Proteomes:UP000015453};
RN [1] {ECO:0000313|EMBL:EPS66935.1, ECO:0000313|Proteomes:UP000015453}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=23855885;
RA Leushkin E.V., Sutormin R.A., Nabieva E.R., Penin A.A., Kondrashov A.S.,
RA Logacheva M.D.;
RT "The miniature genome of a carnivorous plant Genlisea aurea contains a low
RT number of genes and short non-coding sequences.";
RL BMC Genomics 14:476-476(2013).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + cytidine(34) in tRNA(Ile2) + L-lysine = AMP +
CC diphosphate + H(+) + lysidine(34) in tRNA(Ile2);
CC Xref=Rhea:RHEA:43744, Rhea:RHEA-COMP:10625, Rhea:RHEA-COMP:10670,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:32551,
CC ChEBI:CHEBI:33019, ChEBI:CHEBI:82748, ChEBI:CHEBI:83665,
CC ChEBI:CHEBI:456215; EC=6.3.4.19;
CC Evidence={ECO:0000256|ARBA:ARBA00000047};
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
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:EPS66935.1}.
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DR EMBL; AUSU01003393; EPS66935.1; -; Genomic_DNA.
DR AlphaFoldDB; S8CJT7; -.
DR OrthoDB; 460053at2759; -.
DR Proteomes; UP000015453; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR GO; GO:0016879; F:ligase activity, forming carbon-nitrogen bonds; IEA:InterPro.
DR GO; GO:0006400; P:tRNA modification; IEA:UniProt.
DR CDD; cd01992; PP-ATPase; 1.
DR Gene3D; 3.40.50.620; HUPs; 1.
DR HAMAP; MF_01161; tRNA_Ile_lys_synt; 1.
DR InterPro; IPR014729; Rossmann-like_a/b/a_fold.
DR InterPro; IPR011063; TilS/TtcA_N.
DR InterPro; IPR012094; tRNA_Ile_lys_synt.
DR InterPro; IPR012795; tRNA_Ile_lys_synt_N.
DR NCBIfam; TIGR02432; lysidine_TilS_N; 1.
DR PANTHER; PTHR43033; TRNA(ILE)-LYSIDINE SYNTHASE-RELATED; 1.
DR PANTHER; PTHR43033:SF1; TRNA(ILE)-LYSIDINE SYNTHASE-RELATED; 1.
DR Pfam; PF01171; ATP_bind_3; 1.
DR SUPFAM; SSF52402; Adenine nucleotide alpha hydrolases-like; 1.
PE 3: Inferred from homology;
KW Ligase {ECO:0000256|ARBA:ARBA00022598};
KW Reference proteome {ECO:0000313|Proteomes:UP000015453}.
FT DOMAIN 51..257
FT /note="tRNA(Ile)-lysidine/2-thiocytidine synthase N-
FT terminal"
FT /evidence="ECO:0000259|Pfam:PF01171"
FT REGION 463..487
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:EPS66935.1"
FT NON_TER 598
FT /evidence="ECO:0000313|EMBL:EPS66935.1"
SQ SEQUENCE 598 AA; 66927 MW; E984A038A1EBDEF6 CRC64;
VSPIPGILSW LGRFSSRTRC LRFIRRRCRS SYEDRFSRRM SMAGLKPHHR IAIAVSGGPD
SVALCILTAG WKCGNHDAST SLRSNPVDGL LAVVVDHGLR NESAEEAHIV SGRITDMGIK
CEVARCQWSE GRPKVGHLQE AARNKRYDIL QSICLREKFG VLLVAHHSDD QAELFILRLS
RNSGVLGLAG MPFVSEIFPE CPDLCEEGSK THGILLVRPL LDFTKEDLYD ICRIFGRQWV
EDPTNVSPLF ARNRIRMSLK NLSSADKAEL SKVISECRKI RLDVEKRCQA LLSDTVEIVH
HGYAVVDLQL LLTMEVDDIC LARFIVLLLQ FISQRHRPIR GNALKVLLSY FRTTPCKTCL
AAAGCYLRPA PGSKGSKLLV CCCVDACLPP TTKPFSPRNG LNSEESEQII AESNGNLDRS
TPDDTRLSFE FSESGESVLR KSLMLGILSA STHEAVISIQ KEETESFKSR NGETGEDNKR
KHLDPEKKPL LLRGGEAGLY WMNRFAVEWK CSKKYRCCDC LVSNDVVDVI LREMRDVDWI
YVYDLAEKRE KKNGIAEAEA AVISAERAAV QRLKSIPVCV RRCMPVLVDE DGVLLSIP
//
