ID A0A367YT71_9ACTN Unreviewed; 340 AA.
AC A0A367YT71;
DT 07-NOV-2018, integrated into UniProtKB/TrEMBL.
DT 07-NOV-2018, sequence version 1.
DT 27-MAR-2024, entry version 21.
DE RecName: Full=tRNA threonylcarbamoyladenosine biosynthesis protein TsaE {ECO:0000256|ARBA:ARBA00019010};
DE AltName: Full=t(6)A37 threonylcarbamoyladenosine biosynthesis protein TsaE {ECO:0000256|ARBA:ARBA00032441};
GN ORFNames=DT076_13120 {ECO:0000313|EMBL:RCK69008.1};
OS Desertihabitans brevis.
OC Bacteria; Actinomycetota; Actinomycetes; Propionibacteriales;
OC Propionibacteriaceae; Desertihabitans.
OX NCBI_TaxID=2268447 {ECO:0000313|EMBL:RCK69008.1, ECO:0000313|Proteomes:UP000252770};
RN [1] {ECO:0000313|EMBL:RCK69008.1, ECO:0000313|Proteomes:UP000252770}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=16Sb5-5 {ECO:0000313|EMBL:RCK69008.1,
RC ECO:0000313|Proteomes:UP000252770};
RA Liu S.;
RT "Desertimonas flava gen. nov. sp. nov.";
RL Submitted (JUL-2018) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Required for the formation of a threonylcarbamoyl group on
CC adenosine at position 37 (t(6)A37) in tRNAs that read codons beginning
CC with adenine. Is involved in the transfer of the threonylcarbamoyl
CC moiety of threonylcarbamoyl-AMP (TC-AMP) to the N6 group of A37,
CC together with TsaD and TsaB. TsaE seems to play an indirect role in the
CC t(6)A biosynthesis pathway, possibly in regulating the core enzymatic
CC function of TsaD. {ECO:0000256|ARBA:ARBA00024908}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
CC -!- SIMILARITY: Belongs to the TsaE family.
CC {ECO:0000256|ARBA:ARBA00007599}.
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:RCK69008.1}.
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DR EMBL; QOUI01000008; RCK69008.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A367YT71; -.
DR Proteomes; UP000252770; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0016747; F:acyltransferase activity, transferring groups other than amino-acyl groups; IEA:InterPro.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0002949; P:tRNA threonylcarbamoyladenosine modification; IEA:InterPro.
DR CDD; cd04301; NAT_SF; 1.
DR Gene3D; 3.40.630.30; -; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR InterPro; IPR016181; Acyl_CoA_acyltransferase.
DR InterPro; IPR000182; GNAT_dom.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR003442; T6A_TsaE.
DR NCBIfam; TIGR00150; T6A_YjeE; 1.
DR PANTHER; PTHR33540; TRNA THREONYLCARBAMOYLADENOSINE BIOSYNTHESIS PROTEIN TSAE; 1.
DR PANTHER; PTHR33540:SF2; TRNA THREONYLCARBAMOYLADENOSINE BIOSYNTHESIS PROTEIN TSAE; 1.
DR Pfam; PF13508; Acetyltransf_7; 1.
DR Pfam; PF02367; TsaE; 1.
DR SUPFAM; SSF55729; Acyl-CoA N-acyltransferases (Nat); 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR PROSITE; PS51186; GNAT; 1.
PE 3: Inferred from homology;
KW Acyltransferase {ECO:0000256|ARBA:ARBA00023315};
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP000252770};
KW Transferase {ECO:0000313|EMBL:RCK69008.1}.
FT DOMAIN 22..173
FT /note="N-acetyltransferase"
FT /evidence="ECO:0000259|PROSITE:PS51186"
SQ SEQUENCE 340 AA; 36413 MW; BA623D0FDAB0051F CRC64;
MTAEPALTVT GQPASEALGP EWELWLASAE DAEPIAAVVR AAFAARPPVD PPAPGVRETA
GNIAALLAEG TGVTAWVADR LVGVILLTPA GPVEDPWSSA FLQRVSVHPD VQQHGIAGAM
VEAVQRLASD RGSTEVRLFV RAEFPGLQQW WRRHGYRVVE RRDHGVVLAR RVPVRVEVPR
AEDMHALGVR LAALLRPGDV VLADGPLGAG KTTLTQGLGE GLGVGDPVIS PTFVLSRVHR
PTGGRPGLVH VDAYRLGSPE EVDDLDLDSS AEHSVTVVEW GRGRAEQLSD DRLEIEILRT
TDADATDRTR PDSRTVVITP VGDRWDGVDL QSLDPQGGER
//
