(data stored in ACNUC6288 zone)

SWISSPROT: Q6BLT1_DEBHA

ID   Q6BLT1_DEBHA            Unreviewed;       475 AA.
AC   Q6BLT1;
DT   16-AUG-2004, integrated into UniProtKB/TrEMBL.
DT   04-NOV-2008, sequence version 2.
DT   08-MAY-2019, entry version 101.
DE   RecName: Full=tRNA dimethylallyltransferase {ECO:0000256|PIRNR:PIRNR039110, ECO:0000256|RuleBase:RU003783};
DE            EC=2.5.1.75 {ECO:0000256|PIRNR:PIRNR039110, ECO:0000256|RuleBase:RU003783};
GN   OrderedLocusNames=DEHA2F10934g {ECO:0000313|EMBL:CAG89185.2};
OS   Debaryomyces hansenii (strain ATCC 36239 / CBS 767 / JCM 1990 / NBRC
OS   0083 / IGC 2968) (Yeast) (Torulaspora hansenii).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina;
OC   Saccharomycetes; Saccharomycetales; Debaryomycetaceae; Debaryomyces.
OX   NCBI_TaxID=284592 {ECO:0000313|EMBL:CAG89185.2, ECO:0000313|Proteomes:UP000000599};
RN   [1] {ECO:0000313|EMBL:CAG89185.2, ECO:0000313|Proteomes:UP000000599}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 36239 / CBS 767 / JCM 1990 / NBRC 0083 / IGC 2968
RC   {ECO:0000313|Proteomes:UP000000599};
RX   PubMed=15229592; DOI=10.1038/nature02579;
RG   Genolevures;
RA   Dujon B., Sherman D., Fischer G., Durrens P., Casaregola S.,
RA   Lafontaine I., de Montigny J., Marck C., Neuveglise C., Talla E.,
RA   Goffard N., Frangeul L., Aigle M., Anthouard V., Babour A., Barbe V.,
RA   Barnay S., Blanchin S., Beckerich J.M., Beyne E., Bleykasten C.,
RA   Boisrame A., Boyer J., Cattolico L., Confanioleri F., de Daruvar A.,
RA   Despons L., Fabre E., Fairhead C., Ferry-Dumazet H., Groppi A.,
RA   Hantraye F., Hennequin C., Jauniaux N., Joyet P., Kachouri R.,
RA   Kerrest A., Koszul R., Lemaire M., Lesur I., Ma L., Muller H.,
RA   Nicaud J.M., Nikolski M., Oztas S., Ozier-Kalogeropoulos O.,
RA   Pellenz S., Potier S., Richard G.F., Straub M.L., Suleau A.,
RA   Swennene D., Tekaia F., Wesolowski-Louvel M., Westhof E., Wirth B.,
RA   Zeniou-Meyer M., Zivanovic I., Bolotin-Fukuhara M., Thierry A.,
RA   Bouchier C., Caudron B., Scarpelli C., Gaillardin C., Weissenbach J.,
RA   Wincker P., Souciet J.L.;
RT   "Genome evolution in yeasts.";
RL   Nature 430:35-44(2004).
CC   -!- FUNCTION: Catalyzes the transfer of a dimethylallyl group onto the
CC       adenine at position 37. {ECO:0000256|PIRNR:PIRNR039110}.
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-
CC         COMP:10375, ChEBI:CHEBI:33019, ChEBI:CHEBI:57623,
CC         ChEBI:CHEBI:74411, ChEBI:CHEBI:74415; EC=2.5.1.75;
CC         Evidence={ECO:0000256|PIRNR:PIRNR039110,
CC         ECO:0000256|RuleBase:RU003783};
CC   -!- SIMILARITY: Belongs to the IPP transferase family.
CC       {ECO:0000256|PIRNR:PIRNR039110, ECO:0000256|RuleBase:RU003785}.
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DR   EMBL; CR382138; CAG89185.2; -; Genomic_DNA.
DR   RefSeq; XP_460840.2; XM_460840.1.
DR   STRING; 4959.XP_460840.2; -.
DR   EnsemblFungi; CAG89185; CAG89185; DEHA2F10934g.
DR   GeneID; 2903575; -.
DR   KEGG; dha:DEHA2F10934g; -.
DR   HOGENOM; HOG000039995; -.
DR   InParanoid; Q6BLT1; -.
DR   KO; K00791; -.
DR   OMA; CQHHMIS; -.
DR   OrthoDB; 1003231at2759; -.
DR   Proteomes; UP000000599; Chromosome F.
DR   GO; GO:0005829; C:cytosol; IEA:EnsemblFungi.
DR   GO; GO:0005739; C:mitochondrion; IEA:EnsemblFungi.
DR   GO; GO:0005730; C:nucleolus; IEA:EnsemblFungi.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0004003; F:ATP-dependent DNA helicase activity; IEA:InterPro.
DR   GO; GO:0003677; F:DNA binding; IEA:InterPro.
DR   GO; GO:0000049; F:tRNA binding; IEA:EnsemblFungi.
DR   GO; GO:0052381; F:tRNA dimethylallyltransferase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0006260; P:DNA replication; IEA:InterPro.
DR   GO; GO:0061587; P:transfer RNA gene-mediated silencing; IEA:EnsemblFungi.
DR   GO; GO:0006400; P:tRNA modification; IEA:EnsemblFungi.
DR   HAMAP; MF_00185; IPP_trans; 1.
DR   InterPro; IPR039657; Dimethylallyltransferase.
DR   InterPro; IPR001177; DNA_helicase_E1_C_Papillomavir.
DR   InterPro; IPR030666; IPP_transferase_euk.
DR   InterPro; IPR018022; IPT.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   PANTHER; PTHR11088; PTHR11088; 1.
DR   Pfam; PF01715; IPPT; 1.
DR   Pfam; PF00519; PPV_E1_C; 1.
DR   PIRSF; PIRSF039110; IPP_transferase; 1.
DR   SUPFAM; SSF52540; SSF52540; 2.
DR   TIGRFAMs; TIGR00174; miaA; 1.
PE   3: Inferred from homology;
DR   PRODOM; Q6BLT1.
DR   SWISS-2DPAGE; Q6BLT1.
KW   ATP-binding {ECO:0000256|PIRNR:PIRNR039110,
KW   ECO:0000256|RuleBase:RU003785};
KW   Complete proteome {ECO:0000313|Proteomes:UP000000599};
KW   Cytoplasm {ECO:0000256|PIRNR:PIRNR039110};
KW   Nucleotide-binding {ECO:0000256|PIRNR:PIRNR039110,
KW   ECO:0000256|RuleBase:RU003785};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000599};
KW   Transferase {ECO:0000256|PIRNR:PIRNR039110,
KW   ECO:0000256|RuleBase:RU003785};
KW   tRNA processing {ECO:0000256|PIRNR:PIRNR039110,
KW   ECO:0000256|RuleBase:RU003783}.
FT   DOMAIN        2     49       PPV_E1_C. {ECO:0000259|Pfam:PF00519}.
SQ   SEQUENCE   475 AA;  55248 MW;  3E287C5E133F7859 CRC64;
     MIIRYLRYFK NLMMTTPKKN IVTIVGTTGV GKSQFSIELA KAINGEIINA DSMQVYKRLD
     IITNKHPVEE REGITHHVMD HVNWNEEYFI HRFSKEANNA IEDIHNRGKI PIIIGGTHYY
     LQNLLFKNKT VGESSSSSKL TKELTNEDIE LLDGPVNEIF NKLQQIDPII AEKFHPEDKR
     KLRRALEIYI TTGQKPSEIY HEQKLDELED TSLKYNTLLF WVYSDPDILK DRLDKRVDRM
     MEIGALNEIN ELYGVYKSQV QVPDCTTGIW QVIGFKEFLP WLEFAGSSNK QEASRLFNEG
     IDRMKIRTRQ YAKYQVKWIK KLLAVELNKE TRFNFKYGGK LYLLDATDLG SWDEKVREVG
     LNIASQFLTT GPTSVTHPEA PAHLQDIFPS NSFLDNFNSN KKLGSEKNWK HYECSVCKDK
     QGKNLIAVGE ESWQIHLKSR RHKRQLGSGE RKRKHEQMIN QYKQKTPTEE DNSSI
//

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