ID A0A1V6S987_9EURO Unreviewed; 679 AA.
AC A0A1V6S987;
DT 07-JUN-2017, integrated into UniProtKB/TrEMBL.
DT 07-JUN-2017, sequence version 1.
DT 27-MAR-2024, entry version 19.
DE RecName: Full=tRNA(Ile)-lysidine synthetase {ECO:0000256|ARBA:ARBA00013267};
DE EC=6.3.4.19 {ECO:0000256|ARBA:ARBA00013267};
GN ORFNames=PENVUL_c004G10084 {ECO:0000313|EMBL:OQE10299.1};
OS Penicillium vulpinum.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Penicillium.
OX NCBI_TaxID=29845 {ECO:0000313|EMBL:OQE10299.1, ECO:0000313|Proteomes:UP000191518};
RN [1] {ECO:0000313|Proteomes:UP000191518}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=IBT 29486 {ECO:0000313|Proteomes:UP000191518};
RX PubMed=28368369; DOI=10.1038/nmicrobiol.2017.44;
RA Nielsen J.C., Grijseels S., Prigent S., Ji B., Dainat J., Nielsen K.F.,
RA Frisvad J.C., Workman M., Nielsen J.;
RT "Global analysis of biosynthetic gene clusters reveals vast potential of
RT secondary metabolite production in Penicillium species.";
RL Nat. Microbiol. 2:17044-17044(2017).
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:OQE10299.1}.
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DR EMBL; MDYP01000004; OQE10299.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1V6S987; -.
DR STRING; 29845.A0A1V6S987; -.
DR OrthoDB; 460053at2759; -.
DR Proteomes; UP000191518; 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; 2.
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:UP000191518}.
FT DOMAIN 51..204
FT /note="tRNA(Ile)-lysidine/2-thiocytidine synthase N-
FT terminal"
FT /evidence="ECO:0000259|Pfam:PF01171"
FT DOMAIN 270..315
FT /note="tRNA(Ile)-lysidine/2-thiocytidine synthase N-
FT terminal"
FT /evidence="ECO:0000259|Pfam:PF01171"
SQ SEQUENCE 679 AA; 76057 MW; E54F7F3DF63253B6 CRC64;
MAGNISISPF LFQRCFQQAW SGSRRARVNY GSTKYGTKPG DNDTVQLPRR VGIAVSGGAD
SMALAYLCKQ LERSSDIAGA ISVTAFVVDH RARSESTIEA QKVAGWLRDM DIRTHILSLD
WSEITSSQNQ SSPKSGASSP MPSAFETHAR RLRFQALGIA CHEFKLETLL LGHHQDDNIE
TTIWRLSTGA TGLGLGGIAE VARIPECHGL FGASESWSTT SIPTKPPTNP QVRVRFDNQK
HGFITFPDPN AKTDKITFNL TSNANMASPG IFICRPLLSF TKTSLLETCH KNKVPYVSDP
TNFDPTLTPR NAIRSLRTSN SLPRALESQS ILSLIRSSQT LLQRSDELSN YLLSSQCRIL
DFNPKAGSAV IQFLDTTPAS MDPQLATLSA SRMRQIQTIV LRRITELVSP FPDNHFSLRS
YESLVPNVFS GPDGSHGTGQ KRRNAFTVAG VLFQRLANEA STPGKSQDPR LGDNIWLLSR
QPFMRNRDPV TQLNVSPSGS FTQWVLWDNR YWMRLRLVPI DCDPNQLEDR LLSLPLTIRP
LHKFDIERIR KDAVNSRPQR MNKDSVVEQK IPGTFEHLKA LLSVEAPAQL RFTLPVISRE
GVIAKPGKPL GQKIWQQLAL PTLDYRLSSH STKYSSLNEV ELIHLRCRWK LKWQWMYKMI
DTEALRLMGW PVGKDAEDA
//
