ID A0A2P1P8T8_9RICK Unreviewed; 309 AA. AC A0A2P1P8T8; DT 23-MAY-2018, integrated into UniProtKB/TrEMBL. DT 23-MAY-2018, sequence version 1. DT 11-DEC-2019, entry version 8. DE RecName: Full=tRNA dimethylallyltransferase {ECO:0000256|HAMAP-Rule:MF_00185}; DE EC=2.5.1.75 {ECO:0000256|HAMAP-Rule:MF_00185}; DE AltName: Full=Dimethylallyl diphosphate:tRNA dimethylallyltransferase {ECO:0000256|HAMAP-Rule:MF_00185}; DE Short=DMAPP:tRNA dimethylallyltransferase {ECO:0000256|HAMAP-Rule:MF_00185}; DE Short=DMATase {ECO:0000256|HAMAP-Rule:MF_00185}; DE AltName: Full=Isopentenyl-diphosphate:tRNA isopentenyltransferase {ECO:0000256|HAMAP-Rule:MF_00185}; DE Short=IPP transferase {ECO:0000256|HAMAP-Rule:MF_00185}; DE Short=IPPT {ECO:0000256|HAMAP-Rule:MF_00185}; DE Short=IPTase {ECO:0000256|HAMAP-Rule:MF_00185}; GN Name=miaA {ECO:0000256|HAMAP-Rule:MF_00185}; GN ORFNames=phytr_7380 {ECO:0000313|EMBL:AVP87676.1}; OS Candidatus Phycorickettsia trachydisci. OC Bacteria; Proteobacteria; Alphaproteobacteria; Rickettsiales; OC Rickettsiaceae; Candidatus Phycorickettsia. OX NCBI_TaxID=2115978 {ECO:0000313|EMBL:AVP87676.1, ECO:0000313|Proteomes:UP000241762}; RN [1] {ECO:0000313|EMBL:AVP87676.1, ECO:0000313|Proteomes:UP000241762} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=CCALA 838 {ECO:0000313|EMBL:AVP87676.1}; RA Yurchenko T., Sevcikova T., Pribyl P., El Karkouri K., Klimes V., RA Amaral R., Zbrankova V., Kim E., Raoult D., Santos L.M.A., Elias M.; RT "A gene transfer event suggests a long-term partnership between RT eustigmatophyte algae and a novel lineage of endosymbiotic bacteria."; RL Submitted (MAR-2018) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Catalyzes the transfer of a dimethylallyl group onto the CC adenine at position 37 in tRNAs that read codons beginning with CC uridine, leading to the formation of N6-(dimethylallyl)adenosine CC (i(6)A). {ECO:0000256|HAMAP-Rule:MF_00185, CC ECO:0000256|RuleBase:RU003784}. CC -!- CATALYTIC ACTIVITY: CC Reaction=adenosine(37) in tRNA + dimethylallyl diphosphate = CC diphosphate + N(6)-dimethylallyladenosine(37) in tRNA; CC Xref=Rhea:RHEA:26482, Rhea:RHEA-COMP:10162, Rhea:RHEA-COMP:10375, CC ChEBI:CHEBI:33019, ChEBI:CHEBI:57623, ChEBI:CHEBI:74411, CC ChEBI:CHEBI:74415; EC=2.5.1.75; Evidence={ECO:0000256|HAMAP- CC Rule:MF_00185, ECO:0000256|RuleBase:RU003783}; CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; CC Evidence={ECO:0000256|HAMAP-Rule:MF_00185}; CC -!- SUBUNIT: Monomer. {ECO:0000256|HAMAP-Rule:MF_00185}. CC -!- SIMILARITY: Belongs to the IPP transferase family. {ECO:0000256|HAMAP- CC Rule:MF_00185, ECO:0000256|RuleBase:RU003785}. CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of CC feature annotation. {ECO:0000256|HAMAP-Rule:MF_00185}. 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; CP027845; AVP87676.1; -; Genomic_DNA. DR KEGG; ptc:phytr_7380; -. DR KO; K00791; -. DR Proteomes; UP000241762; Chromosome. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule. DR GO; GO:0052381; F:tRNA dimethylallyltransferase activity; IEA:UniProtKB-UniRule. DR GO; GO:0008033; P:tRNA processing; IEA:UniProtKB-UniRule. DR HAMAP; MF_00185; IPP_trans; 1. DR InterPro; IPR039657; Dimethylallyltransferase. DR InterPro; IPR018022; IPT. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR11088; PTHR11088; 1. DR Pfam; PF01715; IPPT; 1. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR00174; miaA; 1. PE 3: Inferred from homology; KW ATP-binding {ECO:0000256|HAMAP-Rule:MF_00185, KW ECO:0000256|RuleBase:RU003785}; KW Magnesium {ECO:0000256|HAMAP-Rule:MF_00185}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00185, KW ECO:0000256|RuleBase:RU003785}; KW Transferase {ECO:0000256|HAMAP-Rule:MF_00185, KW ECO:0000256|RuleBase:RU003785, ECO:0000313|EMBL:AVP87676.1}; KW tRNA processing {ECO:0000256|HAMAP-Rule:MF_00185, KW ECO:0000256|RuleBase:RU003783}. FT NP_BIND 31..38 FT /note="ATP" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00185" FT REGION 33..38 FT /note="Substrate binding" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00185" FT SITE 121 FT /note="Interaction with substrate tRNA" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00185" FT SITE 147 FT /note="Interaction with substrate tRNA" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00185" SQ SEQUENCE 309 AA; 35684 MW; 2400B9CBD125B4F0 CRC64; MTSKAYLFEY SSLNLVIHIL KKMRKIHIIC GPTASGKSAY ALDMAQKIRA IIINADALQV YKQLKIITCC PKEEDLKITQ HFLYNHIDIF EEYNAHKYVN QVVEVLTALP DHIPTIIVGG TGMYLQFLIQ GVHRLPEIDS QIRKSVRDKI SDPIKLYKEL KEIDPLSAST LNQLDTKRIS RALEVYLQTS KSITSFYRDD NLYRPLEGCD ITTHLLLLDR KKLYENCNKR FESLIKQGAL DEAQKILPLW DNLHTSAKKA LGLKELVNYL KDEVSLDDAI KVAQQKTRNF AKRQMTWFRH QLKADHIIS //