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Database: UniProt
Entry: A0A0C9XT66_9AGAR
LinkDB: A0A0C9XT66_9AGAR
Original site: A0A0C9XT66_9AGAR 
ID   A0A0C9XT66_9AGAR        Unreviewed;       564 AA.
AC   A0A0C9XT66;
DT   29-APR-2015, integrated into UniProtKB/TrEMBL.
DT   29-APR-2015, sequence version 1.
DT   27-MAR-2024, entry version 24.
DE   RecName: Full=tRNA(Ile)-lysidine synthetase {ECO:0000256|ARBA:ARBA00013267};
DE            EC=6.3.4.19 {ECO:0000256|ARBA:ARBA00013267};
GN   ORFNames=K443DRAFT_85633 {ECO:0000313|EMBL:KIK08161.1};
OS   Laccaria amethystina LaAM-08-1.
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC   Agaricomycetidae; Agaricales; Agaricineae; Hydnangiaceae; Laccaria.
OX   NCBI_TaxID=1095629 {ECO:0000313|EMBL:KIK08161.1, ECO:0000313|Proteomes:UP000054477};
RN   [1] {ECO:0000313|EMBL:KIK08161.1, ECO:0000313|Proteomes:UP000054477}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=LaAM-08-1 {ECO:0000313|EMBL:KIK08161.1,
RC   ECO:0000313|Proteomes:UP000054477};
RG   DOE Joint Genome Institute;
RA   Kuo A., Kohler A., Nagy L.G., Floudas D., Copeland A., Barry K.W.,
RA   Cichocki N., Veneault-Fourrey C., LaButti K., Lindquist E.A., Lipzen A.,
RA   Lundell T., Morin E., Murat C., Sun H., Tunlid A., Henrissat B.,
RA   Grigoriev I.V., Hibbett D.S., Martin F., Nordberg H.P., Cantor M.N.,
RA   Hua S.X.;
RL   Submitted (APR-2014) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|Proteomes:UP000054477}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=LaAM-08-1 {ECO:0000313|Proteomes:UP000054477};
RG   DOE Joint Genome Institute;
RG   Mycorrhizal Genomics Consortium;
RA   Kohler A., Kuo A., Nagy L.G., Floudas D., Copeland A., Barry K.W.,
RA   Cichocki N., Veneault-Fourrey C., LaButti K., Lindquist E.A., Lipzen A.,
RA   Lundell T., Morin E., Murat C., Riley R., Ohm R., Sun H., Tunlid A.,
RA   Henrissat B., Grigoriev I.V., Hibbett D.S., Martin F.;
RT   "Evolutionary Origins and Diversification of the Mycorrhizal Mutualists.";
RL   Submitted (JAN-2015) 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}.
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DR   EMBL; KN838543; KIK08161.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0C9XT66; -.
DR   STRING; 1095629.A0A0C9XT66; -.
DR   HOGENOM; CLU_035256_0_0_1; -.
DR   OrthoDB; 460053at2759; -.
DR   Proteomes; UP000054477; 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:UP000054477}.
FT   DOMAIN          31..243
FT                   /note="tRNA(Ile)-lysidine/2-thiocytidine synthase N-
FT                   terminal"
FT                   /evidence="ECO:0000259|Pfam:PF01171"
SQ   SEQUENCE   564 AA;  63104 MW;  F0BD7322BD43F317 CRC64;
     MPIYGQPTAI SNVEFSHMLK KTKPPVGWSN KIAVANSGGP DSTCLLFLIN RYLLEHPSPS
     LRPRRVISFT VDHDLQKKSS DMANHCRLFA QSIGVEHITR KIPWGEGAYP PRPSPGDMFE
     RTARDARYAL LLQTLTRADA DVLAVGHHAD DQVETALMRL GMGSTQLGAG GMRACRRWGM
     GAGMNDRSLT WAGHKGMSKW IVRPLLDVGK DRILATCEQN NLEYITDPTN FQPHITIRNA
     IRRLIDGTPD LDHLNLPPDI IEKVESINKS LSSVPAPLDL TAGLESLRGA VNFFHSQLED
     VDSQVDSILK RCRLPSPPGT FLMALASVSD VKRFLLQQGM VLRILRTISF YPWGSLQSEA
     GRRQLSLKQI ITKLWNPDPF TAGIKPFVAG GGVLWKPVVF RREKIKDVTR VSDLLSDDTV
     AWLATRQPPF DKKKKLPQIA RDSPLFRDIT NLLVYGLDLW KTNNGPDYVE ILFDCRFLVS
     FRLPHIPIEI LSALMSGRGK LLLQASSRWY SPLVLYQDHG AARIVHSLVS DDFSGAHSWD
     NKSTEGKVCV DWIVVKFIRT LNAI
//
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