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Database: UniProt
Entry: A0A1I2IP69_9ACTN
LinkDB: A0A1I2IP69_9ACTN
Original site: A0A1I2IP69_9ACTN 
ID   A0A1I2IP69_9ACTN        Unreviewed;       149 AA.
AC   A0A1I2IP69;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   27-MAR-2024, entry version 19.
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=SAMN05421541_110235 {ECO:0000313|EMBL:SFF43500.1};
OS   Actinoplanes philippinensis.
OC   Bacteria; Actinomycetota; Actinomycetes; Micromonosporales;
OC   Micromonosporaceae; Actinoplanes.
OX   NCBI_TaxID=35752 {ECO:0000313|EMBL:SFF43500.1, ECO:0000313|Proteomes:UP000199645};
RN   [1] {ECO:0000313|EMBL:SFF43500.1, ECO:0000313|Proteomes:UP000199645}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 43019 {ECO:0000313|EMBL:SFF43500.1,
RC   ECO:0000313|Proteomes:UP000199645};
RA   de Groot N.N.;
RL   Submitted (OCT-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; FONV01000010; SFF43500.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1I2IP69; -.
DR   STRING; 35752.SAMN05421541_110235; -.
DR   OrthoDB; 9800307at2; -.
DR   Proteomes; UP000199645; 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:UP000199645}.
SQ   SEQUENCE   149 AA;  16110 MW;  FC8743BC636F7AAE CRC64;
     MKLKTVEDTR EFGRRLAGVL RAGDLVLLTG PLGAGKTALA QGIGAGLGVQ GPITSPTFVI
     ARVHRGPLPL VHADAYRLGD RPDPRAEIDD LDLDASADDA VTVVEWGVGL VEQLNDEYLQ
     VRLDRLDDDT RTVELLPHGG DWAHRLETM
//
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