GenomeNet

Database: UniProt
Entry: A0A285VIH2_9MICO
LinkDB: A0A285VIH2_9MICO
Original site: A0A285VIH2_9MICO 
ID   A0A285VIH2_9MICO        Unreviewed;       160 AA.
AC   A0A285VIH2;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, 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=SAMN05421879_102208 {ECO:0000313|EMBL:SOC53850.1};
OS   Ornithinimicrobium cerasi.
OC   Bacteria; Actinomycetota; Actinomycetes; Micrococcales;
OC   Ornithinimicrobiaceae; Ornithinimicrobium.
OX   NCBI_TaxID=2248773 {ECO:0000313|EMBL:SOC53850.1, ECO:0000313|Proteomes:UP000219688};
RN   [1] {ECO:0000313|Proteomes:UP000219688}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=USBA17B2 {ECO:0000313|Proteomes:UP000219688};
RA   Varghese N., Submissions S.;
RL   Submitted (AUG-2017) 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   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; OBQK01000002; SOC53850.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A285VIH2; -.
DR   STRING; 1122622.GCA_000421185_02733; -.
DR   Proteomes; UP000219688; 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:UP000219688}.
SQ   SEQUENCE   160 AA;  17010 MW;  BCA632CE91A3AA22 CRC64;
     MSEPLRLDLP TSEDTRALGA RLGAVLRAGD LVVLTGDLGA GKTTLTQGLA EGLGVRGPIT
     SPTFVIARVH PSLVGGPALV HVDAYRLGGE AELDDLDLDT SLEESVTVVE WGHGLAEHLA
     EELLELELQR SGTEDGDQQS RTATLRSVGD RWEDLRVLLP
//
DBGET integrated database retrieval system