ID A0A2C5Y652_9HYPO Unreviewed; 647 AA.
AC A0A2C5Y652;
DT 20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT 20-DEC-2017, sequence version 1.
DT 27-MAR-2024, entry version 18.
DE RecName: Full=tRNA(Ile)-lysidine synthetase {ECO:0000256|ARBA:ARBA00013267};
DE EC=6.3.4.19 {ECO:0000256|ARBA:ARBA00013267};
GN ORFNames=CDD81_6254 {ECO:0000313|EMBL:PHH63103.1};
OS Ophiocordyceps australis.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Ophiocordycipitaceae; Ophiocordyceps.
OX NCBI_TaxID=1399860 {ECO:0000313|EMBL:PHH63103.1, ECO:0000313|Proteomes:UP000226192};
RN [1] {ECO:0000313|EMBL:PHH63103.1, ECO:0000313|Proteomes:UP000226192}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Map64 {ECO:0000313|EMBL:PHH63103.1,
RC ECO:0000313|Proteomes:UP000226192};
RA De Bekker C., Evans H.C., Brachmann A., Hughes D.P.;
RT "Ant-infecting Ophiocordyceps genomes reveal a high diversity of potential
RT behavioral manipulation genes and a possible major role for enterotoxins.";
RL Submitted (JUN-2017) 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:PHH63103.1}.
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DR EMBL; NJET01000056; PHH63103.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2C5Y652; -.
DR STRING; 1399860.A0A2C5Y652; -.
DR OrthoDB; 460053at2759; -.
DR Proteomes; UP000226192; 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:UP000226192}.
FT DOMAIN 48..278
FT /note="tRNA(Ile)-lysidine/2-thiocytidine synthase N-
FT terminal"
FT /evidence="ECO:0000259|Pfam:PF01171"
FT REGION 538..565
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 647 AA; 73085 MW; C5B44B0B25D8E7BB CRC64;
MTAPAHALFR NSCSKPISLT EFREALTACR PTIHSAPPTR PPSRVQAIAL AVSGGVDSMA
MAWLVSSTIY AYPGINIAGN PIYGAAGIVI DHGLRPNSAQ EASRVALALR KLCITPHVKS
IDLSSASPGP RSAIEGLARK MRFRKLGLTC LDLQVFSLLL AHHSDDQYET ALMRLTLGHS
YRGLQGITAA NTIPECYDLY GIGKSGLFPS RPISRPLSRH RKILSPLKCE LGGVTIYRPL
LEFDKDRLMA TCEANKVPWF QDETNFDQTL TLRNAIRHMV QNHKLPQALQ KPAIDAMCRR
VKAKVVHEDK EAERWLKHHR VIRHFDSNGG TLLVTFPPRR KRWGQRRRLF AKARLQKRRV
IATIMIRKLI DFVTPVLQLK PLIDLHVAVD WLFPELRHGP PAEVSGFTIS GVYFGNHGAD
TWLLTRRPFP NSLPLPETCL HTGDIARDKS VPWKQVKSRE VSAPVLWDGR FWIKVQSQKP
MHIRVLPLLP EHLETFRAPM PYGLRQLLKE RLKKCAPGKV RFTLPGIYCS TKEEAKEQTG
AEEQIEAKQQ SEGDEETKVE EHTKAEQLVK TQRQTISTLR LLALPSLGIH TRHAESLISY
KAMYKALDYV LLKSCEDQTE KPVSHHRRFI SASKKIRDRR LAASRNK
//
