ID M3INX1_CANMX Unreviewed; 321 AA.
AC M3INX1;
DT 01-MAY-2013, integrated into UniProtKB/TrEMBL.
DT 01-MAY-2013, sequence version 1.
DT 27-MAR-2024, entry version 32.
DE RecName: Full=tRNA(Ile)-lysidine synthetase {ECO:0000256|ARBA:ARBA00013267};
DE EC=6.3.4.19 {ECO:0000256|ARBA:ARBA00013267};
GN ORFNames=G210_1405 {ECO:0000313|EMBL:EMG48091.1};
OS Candida maltosa (strain Xu316) (Yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Debaryomycetaceae; Candida/Lodderomyces clade; Candida.
OX NCBI_TaxID=1245528 {ECO:0000313|EMBL:EMG48091.1, ECO:0000313|Proteomes:UP000011777};
RN [1] {ECO:0000313|EMBL:EMG48091.1, ECO:0000313|Proteomes:UP000011777}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Xu316 {ECO:0000313|Proteomes:UP000011777};
RA Yu J., Wang Q., Geng X., Bao W., He P., Cai J.;
RT "Genome sequence of Candida maltosa Xu316, a potential industrial strain
RT for xylitol and ethanol production.";
RL Submitted (FEB-2013) to the EMBL/GenBank/DDBJ databases.
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:EMG48091.1}.
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DR EMBL; AOGT01001261; EMG48091.1; -; Genomic_DNA.
DR AlphaFoldDB; M3INX1; -.
DR STRING; 1245528.M3INX1; -.
DR eggNOG; ENOG502QQNE; Eukaryota.
DR HOGENOM; CLU_865985_0_0_1; -.
DR OMA; EQSHASC; -.
DR OrthoDB; 460053at2759; -.
DR Proteomes; UP000011777; 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:UP000011777}.
FT DOMAIN 23..222
FT /note="tRNA(Ile)-lysidine/2-thiocytidine synthase N-
FT terminal"
FT /evidence="ECO:0000259|Pfam:PF01171"
SQ SEQUENCE 321 AA; 37365 MW; 6788206452553FB5 CRC64;
MIINDTLFEH GLNSLFRSRL PTKVAVALSG GPDSMLLTWL LHKHKINHNA FDIYAITIDH
KYRRESRREA LRVHDYVKNW ELKHIIKELD YDEGTDPTSL KNFEEVARTK RYEAFAEVCY
QESIPAIFVG HHKDDQLETF IQRLQGNSTI FGLAGTRRIS ALPVAKDLPP QADNHPQLRV
VRPFYNYDKQ DIFDTCAVND LQFVNDPTNL DINLTRRNYL RHMIGDILPE KAKPNSPYEI
IDRPSLEQSH ASCLEFATLF EEKAHNLSMY LQENNLIETY PSMGSMKIEF PRVCFDPETT
VVTFARWQVR NIQNDHDEFS V
//
