GenomeNet

Database: UniProt
Entry: A0A1D9E135_9MICO
LinkDB: A0A1D9E135_9MICO
Original site: A0A1D9E135_9MICO 
ID   A0A1D9E135_9MICO        Unreviewed;       142 AA.
AC   A0A1D9E135;
DT   18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT   18-JAN-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=A4Z71_05775 {ECO:0000313|EMBL:AOY56756.1};
OS   Candidatus Rhodoluna planktonica.
OC   Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Microbacteriaceae;
OC   Luna cluster; Luna-1 subcluster; Rhodoluna.
OX   NCBI_TaxID=535712 {ECO:0000313|EMBL:AOY56756.1, ECO:0000313|Proteomes:UP000243784};
RN   [1] {ECO:0000313|EMBL:AOY56756.1, ECO:0000313|Proteomes:UP000243784}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MWH-Dar1 {ECO:0000313|EMBL:AOY56756.1,
RC   ECO:0000313|Proteomes:UP000243784};
RX   PubMed=27659506; DOI=10.1016/j.bbabio.2016.09.006;
RA   Nakamura S., Kikukawa T., Tamogami J., Kamiya M., Aizawa T., Hahn M.W.,
RA   Ihara K., Kamo N., Demura M.;
RT   "Photochemical characterization of actinorhodopsin and its functional
RT   existence in the natural host.";
RL   Biochim. Biophys. Acta 1857:1900-1908(2016).
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; CP015208; AOY56756.1; -; Genomic_DNA.
DR   RefSeq; WP_070955274.1; NZ_CP015208.1.
DR   AlphaFoldDB; A0A1D9E135; -.
DR   STRING; 535712.A4Z71_05775; -.
DR   KEGG; rpla:A4Z71_05775; -.
DR   OrthoDB; 9800307at2; -.
DR   Proteomes; UP000243784; 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: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:UP000243784}.
SQ   SEQUENCE   142 AA;  15491 MW;  552BA2ECC46E99C6 CRC64;
     MHELGVQLAR QLRAGDLVVL TGPLGAGKTT FTRGVGEGLN TIGTVSSPTF VIARTHKRSD
     GGPVLVHVDA YRLGSPAELD DLDIDFDHSI TLVEWGRGFT DGLVDQWLDI EIDRDHTGAT
     ETRMVRLIGN GSRWQEMQVK IA
//
DBGET integrated database retrieval system