GenomeNet

Database: UniProt
Entry: A0A0U5ES86_9BACT
LinkDB: A0A0U5ES86_9BACT
Original site: A0A0U5ES86_9BACT 
ID   A0A0U5ES86_9BACT        Unreviewed;       446 AA.
AC   A0A0U5ES86;
DT   16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT   16-MAR-2016, sequence version 1.
DT   24-JAN-2024, entry version 27.
DE   RecName: Full=tRNA(Ile)-lysidine synthase {ECO:0000256|HAMAP-Rule:MF_01161};
DE            EC=6.3.4.19 {ECO:0000256|HAMAP-Rule:MF_01161};
DE   AltName: Full=tRNA(Ile)-2-lysyl-cytidine synthase {ECO:0000256|HAMAP-Rule:MF_01161};
DE   AltName: Full=tRNA(Ile)-lysidine synthetase {ECO:0000256|HAMAP-Rule:MF_01161};
GN   Name=tilS {ECO:0000256|HAMAP-Rule:MF_01161,
GN   ECO:0000313|EMBL:CUI17025.1};
GN   ORFNames=PNK_1412 {ECO:0000313|EMBL:CUI17025.1};
OS   Candidatus Protochlamydia naegleriophila.
OC   Bacteria; Chlamydiota; Chlamydiia; Parachlamydiales; Parachlamydiaceae;
OC   Candidatus Protochlamydia.
OX   NCBI_TaxID=389348 {ECO:0000313|EMBL:CUI17025.1, ECO:0000313|Proteomes:UP000069902};
RN   [1] {ECO:0000313|Proteomes:UP000069902}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=KNic {ECO:0000313|Proteomes:UP000069902};
RA   Bertelli C.;
RL   Submitted (SEP-2015) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Ligates lysine onto the cytidine present at position 34 of
CC       the AUA codon-specific tRNA(Ile) that contains the anticodon CAU, in an
CC       ATP-dependent manner. Cytidine is converted to lysidine, thus changing
CC       the amino acid specificity of the tRNA from methionine to isoleucine.
CC       {ECO:0000256|HAMAP-Rule:MF_01161}.
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, ECO:0000256|HAMAP-
CC         Rule:MF_01161};
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496,
CC       ECO:0000256|HAMAP-Rule:MF_01161}.
CC   -!- DOMAIN: The N-terminal region contains the highly conserved SGGXDS
CC       motif, predicted to be a P-loop motif involved in ATP binding.
CC       {ECO:0000256|HAMAP-Rule:MF_01161}.
CC   -!- SIMILARITY: Belongs to the tRNA(Ile)-lysidine synthase family.
CC       {ECO:0000256|HAMAP-Rule:MF_01161}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; LN879502; CUI17025.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0U5ES86; -.
DR   STRING; 389348.PNK_1412; -.
DR   KEGG; pnl:PNK_1412; -.
DR   PATRIC; fig|389348.3.peg.1581; -.
DR   InParanoid; A0A0U5ES86; -.
DR   Proteomes; UP000069902; Chromosome cPNK.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0016879; F:ligase activity, forming carbon-nitrogen bonds; IEA:UniProtKB-UniRule.
DR   GO; GO:0006400; P:tRNA modification; IEA:UniProtKB-UniRule.
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   ATP-binding {ECO:0000256|HAMAP-Rule:MF_01161};
KW   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_01161};
KW   Ligase {ECO:0000256|ARBA:ARBA00022598, ECO:0000256|HAMAP-Rule:MF_01161};
KW   Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_01161};
KW   Reference proteome {ECO:0000313|Proteomes:UP000069902};
KW   tRNA processing {ECO:0000256|HAMAP-Rule:MF_01161}.
FT   DOMAIN          19..197
FT                   /note="tRNA(Ile)-lysidine/2-thiocytidine synthase N-
FT                   terminal"
FT                   /evidence="ECO:0000259|Pfam:PF01171"
FT   BINDING         24..29
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01161"
SQ   SEQUENCE   446 AA;  51310 MW;  41769C04990EC737 CRC64;
     MLTTVVQFLK VYCGSSKPIL LGLSGGADSL SLFYCLLEGQ RQGLVTFHVA HVDHGWRTES
     GAEARALKRL VEGYQIPYHE RALNPSSLVG NLEAVCREAR QQFFYELSHQ HGFQGVMLAH
     QQDDQVETIL KRVLEGSHWS HFTGLQSETW LQGIRYLRPL LSISKKDVYV FLNDRHLVPF
     EDDTNSDERF LRARMRQTMI PQLNQTFGKR VDSALLYLSD EMQELKKYFY EKLSPYLDCI
     VRGPFGSYLN LQHVVLPFAE IKYLLRLICE KEGFPLSRFI LKRAGEAFFK NESNVILEIG
     GKGLVIDRQC LFLLPSLKES HWSDSIPLLQ EERAVANGAW KIGMQKRSFL SSQCASSWKE
     GWIGLMRVCL PLGDYHLGPP LLKACRTLHS TPIDRFWTKH KVPAFLRSYF PVIWRGDSIF
     HEFLTGRADF TLEEGDECLE VQLSRE
//
DBGET integrated database retrieval system