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Database: UniProt
Entry: A0A072PEL7_9EURO
LinkDB: A0A072PEL7_9EURO
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ID   A0A072PEL7_9EURO        Unreviewed;       628 AA.
AC   A0A072PEL7;
DT   01-OCT-2014, integrated into UniProtKB/TrEMBL.
DT   01-OCT-2014, 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};
GN   ORFNames=A1O9_09810 {ECO:0000313|EMBL:KEF54015.1};
OS   Exophiala aquamarina CBS 119918.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Chaetothyriomycetidae; Chaetothyriales; Herpotrichiellaceae; Exophiala.
OX   NCBI_TaxID=1182545 {ECO:0000313|EMBL:KEF54015.1, ECO:0000313|Proteomes:UP000027920};
RN   [1] {ECO:0000313|EMBL:KEF54015.1, ECO:0000313|Proteomes:UP000027920}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CBS 119918 {ECO:0000313|EMBL:KEF54015.1,
RC   ECO:0000313|Proteomes:UP000027920};
RG   The Broad Institute Genomics Platform;
RA   Cuomo C., de Hoog S., Gorbushina A., Walker B., Young S.K., Zeng Q.,
RA   Gargeya S., Fitzgerald M., Haas B., Abouelleil A., Allen A.W., Alvarado L.,
RA   Arachchi H.M., Berlin A.M., Chapman S.B., Gainer-Dewar J., Goldberg J.,
RA   Griggs A., Gujja S., Hansen M., Howarth C., Imamovic A., Ireland A.,
RA   Larimer J., McCowan C., Murphy C., Pearson M., Poon T.W., Priest M.,
RA   Roberts A., Saif S., Shea T., Sisk P., Sykes S., Wortman J., Nusbaum C.,
RA   Birren B.;
RT   "The Genome Sequence of Exophiala aquamarina CBS 119918.";
RL   Submitted (MAR-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:KEF54015.1}.
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DR   EMBL; AMGV01000011; KEF54015.1; -; Genomic_DNA.
DR   RefSeq; XP_013256605.1; XM_013401151.1.
DR   AlphaFoldDB; A0A072PEL7; -.
DR   STRING; 1182545.A0A072PEL7; -.
DR   GeneID; 25284718; -.
DR   VEuPathDB; FungiDB:A1O9_09810; -.
DR   HOGENOM; CLU_015599_1_0_1; -.
DR   OrthoDB; 460053at2759; -.
DR   Proteomes; UP000027920; 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   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:UP000027920}.
FT   DOMAIN          36..290
FT                   /note="tRNA(Ile)-lysidine/2-thiocytidine synthase N-
FT                   terminal"
FT                   /evidence="ECO:0000259|Pfam:PF01171"
SQ   SEQUENCE   628 AA;  70613 MW;  9009D5ACF1E6A10D CRC64;
     MTVRQSAVQV TDLLTGVKKL WETSLLKKAC SAPTRIGVCV SGGPDSMALA YLLSRIPQVD
     PSIRIEPIAF IVNHNARPGS RLEAERVGTQ LRTHGKAPMA SQDISTETPI DIESRILHMR
     WPEETNPLAL PDFEMMARYS RYQLIAQAAI REKIQHLFLG HHLDDQLETI IMRLVRNTSF
     SFLAIKGMAE TSRIPCCENI RGANESLDFP SADGHLPPDK APQQETESWP FAANYGSPVG
     ISELHGLQLH RPLLEFKKSQ LIGTCQQHKV QYVSDETNFD PTITMRNAVR YMRAKFNLPR
     ALQATSLLNL MAAAREHSRS LESRGNELAS HFQIVEFDLR VGSMIVQLPQ DLASVCERDL
     EGTSHALSSL TSVISPQPRD ATPSLVPQAR CLEFISILSS IRPQIPVSKK SGEAISTRQT
     LQGATLQIQQ TQIEQLANTP GMGPGQSRWR LSRPTMRYDE IKAVEQKFEP EFGNHEGDSS
     GAWSKWILWD HRYWIRVRSR IATDLSHVAI RNFRREDVHC IVSKGPPNWR NFKSTLREVA
     PGNMRWTLPI LTFADEISAF PTLNVRVQNS ANGRGEGGDL PAHPPVLEWE MCYKVIDKPF
     IQAQKSKIVW KNLADAYDSN QRRAFVSA
//
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