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Database: UniProt
Entry: C7MU08_SACVD
LinkDB: C7MU08_SACVD
Original site: C7MU08_SACVD 
ID   C7MU08_SACVD            Unreviewed;       157 AA.
AC   C7MU08;
DT   13-OCT-2009, integrated into UniProtKB/TrEMBL.
DT   13-OCT-2009, sequence version 1.
DT   27-MAR-2024, entry version 62.
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   OrderedLocusNames=Svir_04610 {ECO:0000313|EMBL:ACU95536.1};
OS   Saccharomonospora viridis (strain ATCC 15386 / DSM 43017 / JCM 3036 / NBRC
OS   12207 / P101).
OC   Bacteria; Actinomycetota; Actinomycetes; Pseudonocardiales;
OC   Pseudonocardiaceae; Saccharomonospora.
OX   NCBI_TaxID=471857 {ECO:0000313|EMBL:ACU95536.1, ECO:0000313|Proteomes:UP000000841};
RN   [1] {ECO:0000313|EMBL:ACU95536.1, ECO:0000313|Proteomes:UP000000841}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 15386 / DSM 43017 / JCM 3036 / NBRC 12207 / P101
RC   {ECO:0000313|Proteomes:UP000000841};
RX   PubMed=21304650; DOI=10.4056/sigs.20263;
RA   Pati A., Sikorski J., Nolan M., Lapidus A., Copeland A.,
RA   Glavina Del Rio T., Lucas S., Chen F., Tice H., Pitluck S., Cheng J.F.,
RA   Chertkov O., Brettin T., Han C., Detter J.C., Kuske C., Bruce D.,
RA   Goodwin L., Chain P., D'haeseleer P., Chen A., Palaniappan K., Ivanova N.,
RA   Mavromatis K., Mikhailova N., Rohde M., Tindall B.J., Goker M., Bristow J.,
RA   Eisen J.A., Markowitz V., Hugenholtz P., Kyrpides N.C., Klenk H.P.;
RT   "Complete genome sequence of Saccharomonospora viridis type strain
RT   (P101).";
RL   Stand. Genomic Sci. 1:141-149(2009).
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; CP001683; ACU95536.1; -; Genomic_DNA.
DR   RefSeq; WP_012795965.1; NC_013159.1.
DR   AlphaFoldDB; C7MU08; -.
DR   STRING; 471857.Svir_04610; -.
DR   KEGG; svi:Svir_04610; -.
DR   eggNOG; COG0802; Bacteria.
DR   HOGENOM; CLU_087829_1_1_11; -.
DR   Proteomes; UP000000841; 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:UP000000841}.
SQ   SEQUENCE   157 AA;  16837 MW;  F93A126117D6B8AF CRC64;
     MRQVSAELPT PDDAMRFGRA LGELLRPGDL VLLSGPLGAG KTTMTRGIAE GMGVSGRVSS
     PTFVLARVHP AGESGVPLVH VDAYRLGGDL AQLEDLDLDT ELDRAALVVE WGEGMAEQLS
     EDYLVVRLDR RPDDVRVVTL EPHGAWVTRL AEARLAG
//
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