ID A0A2R7YZD4_9ACTN Unreviewed; 295 AA.
AC A0A2R7YZD4;
DT 20-JUN-2018, integrated into UniProtKB/TrEMBL.
DT 20-JUN-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=C7S10_06640 {ECO:0000313|EMBL:PUA81740.1};
OS Nocardioides currus.
OC Bacteria; Actinomycetota; Actinomycetes; Propionibacteriales;
OC Nocardioidaceae; Nocardioides.
OX NCBI_TaxID=2133958 {ECO:0000313|EMBL:PUA81740.1, ECO:0000313|Proteomes:UP000244867};
RN [1] {ECO:0000313|EMBL:PUA81740.1, ECO:0000313|Proteomes:UP000244867}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=IB-3 {ECO:0000313|EMBL:PUA81740.1,
RC ECO:0000313|Proteomes:UP000244867};
RA Keele B.F.;
RL Submitted (MAR-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:PUA81740.1}.
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DR EMBL; PYXZ01000002; PUA81740.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2R7YZD4; -.
DR OrthoDB; 9800307at2; -.
DR Proteomes; UP000244867; 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:UP000244867};
KW Transferase {ECO:0000313|EMBL:PUA81740.1}.
FT DOMAIN 3..146
FT /note="N-acetyltransferase"
FT /evidence="ECO:0000259|PROSITE:PS51186"
SQ SEQUENCE 295 AA; 31462 MW; F73C172AE4E64451 CRC64;
MSLDVRRVGP ESAVPVLEVI RTAFAARPVL DPPTDALSET EESVAVELAA YGGLLATLDG
EPVGALLFRP GPEAMLLRRF GVTPAAQGTG VAGALVRTAV ESTLGEPALA VLAREELPET
IAFWEKHGFV EVERASPYVE LRRDLPSSWE VVDAEAMRDL GERLAHSVRA GDVVLLSGEL
GAGKTTLSQG FGRGLGVRGP INSPTFVIAR VHPSLVGGPD LVHVDAYRLG GIEELDDLDL
DTSLDSAVTI VEWGAGLAHV LTESRVEVEI TRALGHETDD DELDPRVVHV RRPRD
//
