ID A0A1E3PVZ7_LIPST Unreviewed; 561 AA.
AC A0A1E3PVZ7;
DT 18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT 18-JAN-2017, sequence version 1.
DT 27-MAR-2024, entry version 22.
DE RecName: Full=tRNA(Ile)-lysidine synthetase {ECO:0000256|ARBA:ARBA00013267};
DE EC=6.3.4.19 {ECO:0000256|ARBA:ARBA00013267};
GN ORFNames=LIPSTDRAFT_75858 {ECO:0000313|EMBL:ODQ69596.1};
OS Lipomyces starkeyi NRRL Y-11557.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Lipomycetaceae; Lipomyces.
OX NCBI_TaxID=675824 {ECO:0000313|EMBL:ODQ69596.1, ECO:0000313|Proteomes:UP000094385};
RN [1] {ECO:0000313|EMBL:ODQ69596.1, ECO:0000313|Proteomes:UP000094385}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NRRL Y-11557 {ECO:0000313|EMBL:ODQ69596.1,
RC ECO:0000313|Proteomes:UP000094385};
RX PubMed=27535936; DOI=10.1073/pnas.1603941113;
RA Riley R., Haridas S., Wolfe K.H., Lopes M.R., Hittinger C.T., Goeker M.,
RA Salamov A.A., Wisecaver J.H., Long T.M., Calvey C.H., Aerts A.L.,
RA Barry K.W., Choi C., Clum A., Coughlan A.Y., Deshpande S., Douglass A.P.,
RA Hanson S.J., Klenk H.-P., LaButti K.M., Lapidus A., Lindquist E.A.,
RA Lipzen A.M., Meier-Kolthoff J.P., Ohm R.A., Otillar R.P., Pangilinan J.L.,
RA Peng Y., Rokas A., Rosa C.A., Scheuner C., Sibirny A.A., Slot J.C.,
RA Stielow J.B., Sun H., Kurtzman C.P., Blackwell M., Grigoriev I.V.,
RA Jeffries T.W.;
RT "Comparative genomics of biotechnologically important yeasts.";
RL Proc. Natl. Acad. Sci. U.S.A. 113:9882-9887(2016).
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}.
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DR EMBL; KV454303; ODQ69596.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1E3PVZ7; -.
DR STRING; 675824.A0A1E3PVZ7; -.
DR OrthoDB; 460053at2759; -.
DR Proteomes; UP000094385; 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:UP000094385}.
FT DOMAIN 43..238
FT /note="tRNA(Ile)-lysidine/2-thiocytidine synthase N-
FT terminal"
FT /evidence="ECO:0000259|Pfam:PF01171"
SQ SEQUENCE 561 AA; 64543 MW; 9FF0E7981F8A222E CRC64;
MSVYDVTMRP LLAAAKNANP ITQAEFASSL LRLFDFKIPR VFGIALSGGV DSMCLAYLSD
VFARKHGTTV FAFTVDHKLR DGSFTEAKSI SNVLATQLGD THPHVRHEIL ELDWKYAEKS
SHMIERTART LRYRALAKAC VKHRIEHLLL AHNLDDQVET VMIRLLRGST SRGLAGMRRV
CWIPEGYSTY GAHHVKILRP LLLQSKVRLI ATCLKAQLQW YEDMTNHDPT YTKRNAVRYL
LSQPEKLPQA LRPETLASFC ERLSVQRRQT DLSGLRLFTQ EMDGGNITFS RSSMIAVWKM
RPEAYERRDL NSLVSFIQRL VSMVTPLDLS DISSQRYREV VTKLLDPKET TFTFMNIQWT
HTTKTVTRRK QVRRACLEAQ PNVGKLAASP FSGCNLQPHK NAKNRRFSLK VNRSALKDEE
QEAGVEHYWT LARQPIPGHN QPIAVVLIPP SGWSDWALWD GRMWFRFRWE TMKQTSPKPI
MIRPFSEMDR YTISKFGPDV ERNFNAKTRA INGRQLSTLP VLHDPEIARM IAMPTVRFYI
GTRELLCDMT PKNQDILTDR Q
//
