ID A0A164D4G5_9MICO Unreviewed; 187 AA.
AC A0A164D4G5;
DT 06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT 06-JUL-2016, 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 Name=tsaE {ECO:0000313|EMBL:KZE93164.1};
GN ORFNames=AVP42_01945 {ECO:0000313|EMBL:KZE93164.1};
OS Agromyces sp. NDB4Y10.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Microbacteriaceae;
OC Agromyces.
OX NCBI_TaxID=1775951 {ECO:0000313|EMBL:KZE93164.1, ECO:0000313|Proteomes:UP000185889};
RN [1] {ECO:0000313|EMBL:KZE93164.1, ECO:0000313|Proteomes:UP000185889}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NDB4Y10 {ECO:0000313|EMBL:KZE93164.1,
RC ECO:0000313|Proteomes:UP000185889};
RA Adelskov J., Patel B.K.;
RT "Draft genome sequence of Agromyces sp. NDB4Y10 isolated from a newly
RT drilled coal seam bore well.";
RL Submitted (JAN-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}.
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:KZE93164.1}.
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DR EMBL; LQGY01000037; KZE93164.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A164D4G5; -.
DR STRING; 1775951.AVP42_01945; -.
DR PATRIC; fig|1775951.3.peg.2012; -.
DR OrthoDB; 9800307at2; -.
DR Proteomes; UP000185889; Unassembled WGS sequence.
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: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:UP000185889}.
FT REGION 130..164
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 187 AA; 19523 MW; 485DAAF863ACC06F CRC64;
MSTRIVPDAD AMEELGRELG RQLRAGDLVV LTGPLGAGKT TLTRGIGDGL GVRGPVQSPT
FVLARTHPSL VGGAPLVHVD AYRLSGAAEL EDLDLDFDHA AVVVEWGAGL LDGVSDSWLE
VVIARRRGGV ATDGDDAEHA SDAEEDLESD EPRTVELVGH GPRWADTPYA TAVRLEAGPG
SARDAAN
//
