ID A0A093Y6Q0_TALMA Unreviewed; 633 AA.
AC A0A093Y6Q0;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 27-MAR-2024, entry version 31.
DE RecName: Full=tRNA(Ile)-lysidine synthetase {ECO:0000256|ARBA:ARBA00013267};
DE EC=6.3.4.19 {ECO:0000256|ARBA:ARBA00013267};
GN ORFNames=GQ26_0010330 {ECO:0000313|EMBL:KFX53158.1};
OS Talaromyces marneffei PM1.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Trichocomaceae; Talaromyces;
OC Talaromyces sect. Talaromyces.
OX NCBI_TaxID=1077442 {ECO:0000313|EMBL:KFX53158.1, ECO:0000313|Proteomes:UP000029285};
RN [1] {ECO:0000313|EMBL:KFX53158.1, ECO:0000313|Proteomes:UP000029285}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PM1 {ECO:0000313|EMBL:KFX53158.1,
RC ECO:0000313|Proteomes:UP000029285};
RX PubMed=25330172; DOI=10.1371/journal.pgen.1004662;
RA Yang E., Wang G., Cai J., Woo P.C., Lau S.K., Yuen K.-Y., Chow W.-N.,
RA Lin X.;
RT "Signature Gene Expression Reveals Novel Clues to the Molecular Mechanisms
RT of Dimorphic Transition in Penicillium marneffei.";
RL PLoS Genet. 10:e1004662-e1004662(2014).
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:KFX53158.1}.
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DR EMBL; JPOX01000001; KFX53158.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A093Y6Q0; -.
DR eggNOG; ENOG502RZPD; Eukaryota.
DR HOGENOM; CLU_015599_1_0_1; -.
DR Proteomes; UP000029285; 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}.
FT DOMAIN 45..280
FT /note="tRNA(Ile)-lysidine/2-thiocytidine synthase N-
FT terminal"
FT /evidence="ECO:0000259|Pfam:PF01171"
FT REGION 465..485
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 633 AA; 72275 MW; F9A724D97A19C5E7 CRC64;
MALPFKYGIS APVSTQQFFK SFREAWTNIL PRYQRAPVNH IPRRIGIAVS GGPDSMALAY
LCRQLQITRP ELNLDVKAFV VDHKFREEST EEAHMVTKWL SNLDIQSEVL TLDWLPGESP
KKQMAFETLA RTKRYQALGI ACLENRLNTL LIGHHLDDNV ETGLLRMTPT AQLEGLAGIA
PVARIPECHG LWGVSESGSI ETIRGRQRSF EFDLKEGKMT HFSTVDWKFD MTTGGVLLCR
PLLPFYKSSI LETCREAKVP YVTDPTNSDP TLTIRNTIRN LLASDKLPRA LRPASMSTFL
ANNRVSLLDI MSETDKLLRD CQLLKFYPNT STMEVMFPTL PIHSSDAQNY RILAAALRRI
VNIITPRPEV KNQALRLYER FAHEIFTGQQ RNDFTVAGVH FRLQESPNNK DTGVLFDNIW
HISRTPFMAG TEPILEIDNL SDEWSTPVLW DNRYWFQFRF NRESASDPND PLKAGSADGA
ERPSALSAEE LASLQSLNPR ITIRPLEKKD MAFVNFYLKT MKRNYEFAKW APRNSRFTIP
VITTSTLLPT TENQNNKKRK KRRISILKIR GNVPQEGYIG LPTLNLMDMD VDGEIGFKVQ
CRWSYKNVDT EALKMMGWLA EDQKKVAGYH GHF
//
