ID K1WHG9_MARBU Unreviewed; 595 AA.
AC K1WHG9;
DT 28-NOV-2012, integrated into UniProtKB/TrEMBL.
DT 28-NOV-2012, sequence version 1.
DT 27-MAR-2024, entry version 44.
DE RecName: Full=tRNA(Ile)-lysidine synthetase {ECO:0000256|ARBA:ARBA00013267};
DE EC=6.3.4.19 {ECO:0000256|ARBA:ARBA00013267};
GN ORFNames=MBM_09592 {ECO:0000313|EMBL:EKD12271.1};
OS Marssonina brunnea f. sp. multigermtubi (strain MB_m1) (Marssonina leaf
OS spot fungus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC Helotiales; Drepanopezizaceae; Drepanopeziza.
OX NCBI_TaxID=1072389 {ECO:0000313|EMBL:EKD12271.1, ECO:0000313|Proteomes:UP000006753};
RN [1] {ECO:0000313|EMBL:EKD12271.1, ECO:0000313|Proteomes:UP000006753}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MB_m1 {ECO:0000313|EMBL:EKD12271.1,
RC ECO:0000313|Proteomes:UP000006753};
RX PubMed=22876864; DOI=10.1186/1471-2164-13-382;
RA Zhu S., Cao Y.-Z., Jiang C., Tan B.-Y., Wang Z., Feng S., Zhang L.,
RA Su X.-H., Brejova B., Vinar T., Xu M., Wang M.-X., Zhang S.-G.,
RA Huang M.-R., Wu R., Zhou Y.;
RT "Sequencing the genome of Marssonina brunnea reveals fungus-poplar co-
RT evolution.";
RL BMC Genomics 13:382-382(2012).
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; JH921460; EKD12271.1; -; Genomic_DNA.
DR RefSeq; XP_007297481.1; XM_007297419.1.
DR AlphaFoldDB; K1WHG9; -.
DR STRING; 1072389.K1WHG9; -.
DR GeneID; 18765527; -.
DR KEGG; mbe:MBM_09592; -.
DR eggNOG; ENOG502RZPD; Eukaryota.
DR HOGENOM; CLU_015599_1_0_1; -.
DR InParanoid; K1WHG9; -.
DR OMA; ARIPECH; -.
DR OrthoDB; 460053at2759; -.
DR Proteomes; UP000006753; 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:UP000006753}.
FT DOMAIN 44..291
FT /note="tRNA(Ile)-lysidine/2-thiocytidine synthase N-
FT terminal"
FT /evidence="ECO:0000259|Pfam:PF01171"
FT REGION 214..238
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 595 AA; 66129 MW; 77239E520D22DEB3 CRC64;
MKATRFLQNA IPSKVSQITV EGFANAVLKV WRPSNDPRQT ATIGLAISGG VDSMALAFLC
SRLKELKTAA ADQPDPKHDI LSSVKFQAFV VDHGVRRGSD LEAQAVSKLL ERQGIPTDVL
KIQWPEDATL KLNFESLARK YRFRTLGQAC SERGIGSLFL AHHEDDQAET VMMRLVAGHR
SKGLMGIKEH SEIPECYGIH GVHESGGIDD PRMRWSEGPP ASAPEVEDHE RGTLASRPQL
LTENGGVRVY RPLLAFSKQQ LTATCQGNSV EWFEDHTNRD QTLTKRNAIR HMFATHSLPS
ALTKPSLLSL SLKIRAKETQ RQATITSLLT QCKITHLDLR TGTAKVQFPD LSLSTHPQAT
SGQTAAELLK RIAMLVSPEQ HIELSSLHGA VAHLFPELLP GATRPPPATP VAPPPAFTVC
GVYFQRVGAT TVSGGEATRK PRWLVSRQPY PSRAKEKDAR RYHVKFPPAD GGVWSPWRLW
DGRYWIRVQN RSSRTLLVRP LLPSEWPDVA LRLGDDHSAR VKRICREKAT GARWTVLAVV
ARLHDGREVV VALPTFGLDL NLYAIEGWDS VKWEIRYKKI DIAGLRISDE KGEVE
//
