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Database: UniProt
Entry: A0A0J6XX85_9ACTN
LinkDB: A0A0J6XX85_9ACTN
Original site: A0A0J6XX85_9ACTN 
ID   A0A0J6XX85_9ACTN        Unreviewed;       155 AA.
AC   A0A0J6XX85;
DT   14-OCT-2015, integrated into UniProtKB/TrEMBL.
DT   14-OCT-2015, sequence version 1.
DT   24-JAN-2024, entry version 22.
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=ACS04_02480 {ECO:0000313|EMBL:KMO99373.1};
OS   Streptomyces roseus.
OC   Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC   Streptomycetaceae; Streptomyces.
OX   NCBI_TaxID=66430 {ECO:0000313|EMBL:KMO99373.1, ECO:0000313|Proteomes:UP000035932};
RN   [1] {ECO:0000313|EMBL:KMO99373.1, ECO:0000313|Proteomes:UP000035932}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 31245 {ECO:0000313|EMBL:KMO99373.1,
RC   ECO:0000313|Proteomes:UP000035932};
RA   Cruz-Morales P., Martinez-Guerrero C., Morales-Escalante M.A.,
RA   Yanez-Guerra L.A., Kopp J.F., Feldmann J., Ramos-Aboites H.E.,
RA   Barona-Gomez F.;
RT   "Recapitulation of the evolution of biosynthetic gene clusters reveals
RT   hidden chemical diversity on bacterial genomes.";
RL   Submitted (JUN-2015) 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:KMO99373.1}.
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DR   EMBL; LFML01000010; KMO99373.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0J6XX85; -.
DR   STRING; 66430.ACS04_02480; -.
DR   PATRIC; fig|66430.4.peg.16; -.
DR   Proteomes; UP000035932; 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: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, ECO:0000313|EMBL:KMO99373.1};
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:UP000035932}.
SQ   SEQUENCE   155 AA;  16177 MW;  BD86FE88665AA8A4 CRC64;
     MQELGRTLAG LLRPGDLVLL TGELGAGKTT LTRGLGEGLG VRGAVTSPTF VIARVHPSLS
     GGPALVHVDA YRLGGGLDEM EDLDLDVSLP ESVVVVEWGD GKVEELSDDR LHVVIARAVG
     HEEVLDDVRE VSVRGIGARW SAPDALAALQ GVSAR
//
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