ID A0A1L9PSW4_ASPVE Unreviewed; 479 AA.
AC A0A1L9PSW4;
DT 15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT 15-MAR-2017, sequence version 1.
DT 27-MAR-2024, entry version 30.
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 ORFNames=ASPVEDRAFT_44147 {ECO:0000313|EMBL:OJJ04618.1};
OS Aspergillus versicolor CBS 583.65.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Nidulantes.
OX NCBI_TaxID=1036611 {ECO:0000313|EMBL:OJJ04618.1, ECO:0000313|Proteomes:UP000184073};
RN [1] {ECO:0000313|Proteomes:UP000184073}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 583.65 {ECO:0000313|Proteomes:UP000184073};
RX PubMed=28196534; DOI=10.1186/s13059-017-1151-0;
RA de Vries R.P., Riley R., Wiebenga A., Aguilar-Osorio G., Amillis S.,
RA Uchima C.A., Anderluh G., Asadollahi M., Askin M., Barry K., Battaglia E.,
RA Bayram O., Benocci T., Braus-Stromeyer S.A., Caldana C., Canovas D.,
RA Cerqueira G.C., Chen F., Chen W., Choi C., Clum A., Dos Santos R.A.,
RA Damasio A.R., Diallinas G., Emri T., Fekete E., Flipphi M., Freyberg S.,
RA Gallo A., Gournas C., Habgood R., Hainaut M., Harispe M.L., Henrissat B.,
RA Hilden K.S., Hope R., Hossain A., Karabika E., Karaffa L., Karanyi Z.,
RA Krasevec N., Kuo A., Kusch H., LaButti K., Lagendijk E.L., Lapidus A.,
RA Levasseur A., Lindquist E., Lipzen A., Logrieco A.F., MacCabe A.,
RA Maekelae M.R., Malavazi I., Melin P., Meyer V., Mielnichuk N., Miskei M.,
RA Molnar A.P., Mule G., Ngan C.Y., Orejas M., Orosz E., Ouedraogo J.P.,
RA Overkamp K.M., Park H.-S., Perrone G., Piumi F., Punt P.J., Ram A.F.,
RA Ramon A., Rauscher S., Record E., Riano-Pachon D.M., Robert V., Roehrig J.,
RA Ruller R., Salamov A., Salih N.S., Samson R.A., Sandor E., Sanguinetti M.,
RA Schuetze T., Sepcic K., Shelest E., Sherlock G., Sophianopoulou V.,
RA Squina F.M., Sun H., Susca A., Todd R.B., Tsang A., Unkles S.E.,
RA van de Wiele N., van Rossen-Uffink D., Oliveira J.V., Vesth T.C.,
RA Visser J., Yu J.-H., Zhou M., Andersen M.R., Archer D.B., Baker S.E.,
RA Benoit I., Brakhage A.A., Braus G.H., Fischer R., Frisvad J.C.,
RA Goldman G.H., Houbraken J., Oakley B., Pocsi I., Scazzocchio C.,
RA Seiboth B., vanKuyk P.A., Wortman J., Dyer P.S., Grigoriev I.V.;
RT "Comparative genomics reveals high biological diversity and specific
RT adaptations in the industrially and medically important fungal genus
RT Aspergillus.";
RL Genome Biol. 18:RESEARCH28.1-RESEARCH28.45(2017).
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-COMP:10375,
CC ChEBI:CHEBI:33019, ChEBI:CHEBI:57623, ChEBI:CHEBI:74411,
CC ChEBI:CHEBI:74415; EC=2.5.1.75;
CC Evidence={ECO:0000256|PIRNR:PIRNR039110,
CC ECO:0000256|RuleBase:RU003783};
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
CC -!- SIMILARITY: Belongs to the IPP transferase family.
CC {ECO:0000256|ARBA:ARBA00005842, ECO:0000256|PIRNR:PIRNR039110,
CC ECO:0000256|RuleBase:RU003785}.
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DR EMBL; KV878132; OJJ04618.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1L9PSW4; -.
DR STRING; 1036611.A0A1L9PSW4; -.
DR VEuPathDB; FungiDB:ASPVEDRAFT_44147; -.
DR OrthoDB; 11270at2759; -.
DR Proteomes; UP000184073; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
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-KW.
DR Gene3D; 1.10.20.140; -; 1.
DR Gene3D; 3.30.160.60; Classic Zinc Finger; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR HAMAP; MF_00185; IPP_trans; 1.
DR InterPro; IPR039657; Dimethylallyltransferase.
DR InterPro; IPR030666; IPP_transferase_euk.
DR InterPro; IPR018022; IPT.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR036236; Znf_C2H2_sf.
DR InterPro; IPR013087; Znf_C2H2_type.
DR NCBIfam; TIGR00174; miaA; 1.
DR PANTHER; PTHR11088; TRNA DIMETHYLALLYLTRANSFERASE; 1.
DR PANTHER; PTHR11088:SF95; TRNA DIMETHYLALLYLTRANSFERASE; 1.
DR Pfam; PF01715; IPPT; 1.
DR Pfam; PF12874; zf-met; 1.
DR PIRSF; PIRSF039110; IPP_transferase; 1.
DR SUPFAM; SSF57667; beta-beta-alpha zinc fingers; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 2.
DR PROSITE; PS00028; ZINC_FINGER_C2H2_1; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PIRNR:PIRNR039110};
KW Cytoplasm {ECO:0000256|PIRNR:PIRNR039110};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW ECO:0000256|PIRNR:PIRNR039110};
KW Reference proteome {ECO:0000313|Proteomes:UP000184073};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|PIRNR:PIRNR039110};
KW tRNA processing {ECO:0000256|PIRNR:PIRNR039110,
KW ECO:0000256|RuleBase:RU003783}.
FT DOMAIN 408..430
FT /note="C2H2-type"
FT /evidence="ECO:0000259|PROSITE:PS00028"
FT REGION 448..479
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 448..469
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 479 AA; 54575 MW; 66AD52320B9425F4 CRC64;
MRPLIAVVGA TGTGKSKLAV DIASRFNGEI INGDAMQMYR GLPIITNQIP IEERNGIPHH
LISCIDLEEN PWRISRFRKE CLRFVDDIHA RGKLPVLVGG THYYTQSVLF QDQLVDKESD
SSEEEVNSCP AEDIDSAVKW PILDAEPELV LQKLREVDPI MAERWHPKDT RKIRRSLEIY
FQTGKPASQV YAEQRLPNQA AERNDDATAG TGQLRFNTMI FWVHSEKSTL QERLFKRVDA
MVDQGLLSEA SRMTDYIKEN EAQGITVDQT RGVWISIGFK ELAPYFDALK DNSMTEKELE
SIRQSCIESV KIATRQYATS QIKWIRNKLW NGLAGAGMTS RLYILDSTDV EDWTASITEP
SERLVEALLK DERLPDPKSL SELARTVLDA KETQPLPSSQ GATKCITCDI CRKTMTNEEQ
WKIHMHSSAH KRVLKSLARK EERAAYLRRQ QESLENTEQH VRDSTKELDS QTLQGEVTE
//
