ID A0A1L2ZRA5_9MICC Unreviewed; 192 AA.
AC A0A1L2ZRA5;
DT 15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT 15-MAR-2017, sequence version 1.
DT 27-MAR-2024, entry version 25.
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=BHE16_11650 {ECO:0000313|EMBL:APF41531.1};
OS Neomicrococcus aestuarii.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Micrococcaceae;
OC Neomicrococcus.
OX NCBI_TaxID=556325 {ECO:0000313|EMBL:APF41531.1, ECO:0000313|Proteomes:UP000183530};
RN [1] {ECO:0000313|EMBL:APF41531.1, ECO:0000313|Proteomes:UP000183530}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=B18 {ECO:0000313|EMBL:APF41531.1,
RC ECO:0000313|Proteomes:UP000183530};
RA Luo Y.;
RT "Genome sequencing of Zhihengliuella aestuarii B18 antagonistic to
RT Plasmodiophora brassicae.";
RL Submitted (NOV-2016) 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}.
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DR EMBL; CP018135; APF41531.1; -; Genomic_DNA.
DR RefSeq; WP_071895001.1; NZ_CP018135.1.
DR AlphaFoldDB; A0A1L2ZRA5; -.
DR STRING; 556325.BHE16_11650; -.
DR KEGG; nae:BHE16_11650; -.
DR OrthoDB; 9800307at2; -.
DR Proteomes; UP000183530; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0016740; F:transferase activity; IEA:UniProtKB-KW.
DR GO; GO:0002949; P:tRNA threonylcarbamoyladenosine modification; IEA:InterPro.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
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; PF02367; TsaE; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
PE 3: Inferred from homology;
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:UP000183530};
KW Transferase {ECO:0000313|EMBL:APF41531.1}.
FT REGION 1..21
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 192 AA; 20479 MW; 2F2EFB8ACABFEE62 CRC64;
MTNIQTEKSS TDEPSTEQWS QELTAETAED MHALGVQLGK LLVSGDVLIL TGPLGAGKTT
LTQGIGEGLG VRSGIISPTF VLARVHPSER TDASDAPALI HVDAYRLNSA EELTDLDIDS
QLESGVVVVE WGRGKAEQLS DSYLDIELVR PEVELDATVE GEILSFEDDA AEPARAVSIR
AVGPAWATRR LG
//
