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Database: UniProt
Entry: A0A1B8G5L4_9PEZI
LinkDB: A0A1B8G5L4_9PEZI
Original site: A0A1B8G5L4_9PEZI 
ID   A0A1B8G5L4_9PEZI        Unreviewed;       597 AA.
AC   A0A1B8G5L4;
DT   02-NOV-2016, integrated into UniProtKB/TrEMBL.
DT   02-NOV-2016, sequence version 1.
DT   27-MAR-2024, entry version 25.
DE   RecName: Full=tRNA(Ile)-lysidine synthetase {ECO:0000256|ARBA:ARBA00013267};
DE            EC=6.3.4.19 {ECO:0000256|ARBA:ARBA00013267};
GN   ORFNames=VE02_00022 {ECO:0000313|EMBL:OBT91135.1};
OS   Pseudogymnoascus sp. 03VT05.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC   Leotiomycetes incertae sedis; Pseudeurotiaceae; Pseudogymnoascus.
OX   NCBI_TaxID=1622148 {ECO:0000313|EMBL:OBT91135.1};
RN   [1] {ECO:0000313|EMBL:OBT91135.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=03VT05 {ECO:0000313|EMBL:OBT91135.1};
RA   Palmer J.M., Drees K.P., Foster J.T., Lindner D.L.;
RT   "Comparative genomics of Pseudogymnoascus destructans, the fungus causing
RT   white-nose syndrome of bats.";
RL   Submitted (MAR-2016) 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; KV459351; OBT91135.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1B8G5L4; -.
DR   Proteomes; UP000091872; 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; 2.
DR   SUPFAM; SSF52402; Adenine nucleotide alpha hydrolases-like; 1.
PE   3: Inferred from homology;
KW   Ligase {ECO:0000256|ARBA:ARBA00022598}.
FT   DOMAIN          52..186
FT                   /note="tRNA(Ile)-lysidine/2-thiocytidine synthase N-
FT                   terminal"
FT                   /evidence="ECO:0000259|Pfam:PF01171"
FT   DOMAIN          236..289
FT                   /note="tRNA(Ile)-lysidine/2-thiocytidine synthase N-
FT                   terminal"
FT                   /evidence="ECO:0000259|Pfam:PF01171"
SQ   SEQUENCE   597 AA;  67134 MW;  B50133291D01F62A CRC64;
     MVGILHRTGW SGRGAAAISL DRFIASLRRL NHKGLNQLTE THGKPSKPLT IGLAISGGVD
     SMALASLCSG IQNKDRFRFR AFVVDHKVRA GSGDEAHAVA KILEEKDIPT DVLKIEWPEG
     LSPKEASNFE SLARTYRFQA LGKACRDHDI QSLFLAHHRD DQAETILMRM INGHRKDGLC
     GMRLSGDIPE CRGIYGVHQS GVVDESATAS QIKFGRGVDL NKSRSLDSLD DNTSSLGMRI
     ESGGIKVYRP LLCFTKQELR DTCEANDMSW FEDKTNADPT LTMRNAIRHI YANNKLPVAL
     QKPSILALAK RLQENRDGDL ERRNKSFTQK VQILKFEPSV PYCSVYFEPL DIGHNTKSST
     EISSTEFEDA SWWLRAVIQL ISPVENIALG TLSTAVQRIY PELDSQAGHD SAPRKAFTVA
     GVMFEPAPSD MHDSLLSSHT GYSEGSTLAP QQIANRHWIV RPQPYKRGKE PRLEFKPLQG
     KDEGAYWRDN DSWKLFDGRF WIRILNLTSS NISLRPFQPE DVNKLKGTKF MEQLEQREKF
     LLPLKASKFR YVLPAIVAEV NGMEQVVGLP TLGIVAQDME KLVKYEVRYR DLDSWPN
//
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