ID A1CM28_ASPCL Unreviewed; 472 AA.
AC A1CM28;
DT 23-JAN-2007, integrated into UniProtKB/TrEMBL.
DT 23-JAN-2007, sequence version 1.
DT 27-MAR-2024, entry version 96.
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=ACLA_095480 {ECO:0000313|EMBL:EAW08615.1};
OS Aspergillus clavatus (strain ATCC 1007 / CBS 513.65 / DSM 816 / NCTC 3887 /
OS NRRL 1 / QM 1276 / 107).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Fumigati.
OX NCBI_TaxID=344612 {ECO:0000313|EMBL:EAW08615.1, ECO:0000313|Proteomes:UP000006701};
RN [1] {ECO:0000313|EMBL:EAW08615.1, ECO:0000313|Proteomes:UP000006701}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 1007 / CBS 513.65 / DSM 816 / NCTC 3887 / NRRL 1
RC {ECO:0000313|Proteomes:UP000006701};
RX PubMed=18404212; DOI=10.1371/journal.pgen.1000046;
RA Fedorova N.D., Khaldi N., Joardar V.S., Maiti R., Amedeo P., Anderson M.J.,
RA Crabtree J., Silva J.C., Badger J.H., Albarraq A., Angiuoli S., Bussey H.,
RA Bowyer P., Cotty P.J., Dyer P.S., Egan A., Galens K., Fraser-Liggett C.M.,
RA Haas B.J., Inman J.M., Kent R., Lemieux S., Malavazi I., Orvis J.,
RA Roemer T., Ronning C.M., Sundaram J.P., Sutton G., Turner G., Venter J.C.,
RA White O.R., Whitty B.R., Youngman P., Wolfe K.H., Goldman G.H.,
RA Wortman J.R., Jiang B., Denning D.W., Nierman W.C.;
RT "Genomic islands in the pathogenic filamentous fungus Aspergillus
RT fumigatus.";
RL PLoS Genet. 4:E1000046-E1000046(2008).
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; DS027058; EAW08615.1; -; Genomic_DNA.
DR RefSeq; XP_001270041.1; XM_001270040.1.
DR AlphaFoldDB; A1CM28; -.
DR STRING; 344612.A1CM28; -.
DR EnsemblFungi; EAW08615; EAW08615; ACLA_095480.
DR GeneID; 4702523; -.
DR KEGG; act:ACLA_095480; -.
DR VEuPathDB; FungiDB:ACLA_095480; -.
DR eggNOG; KOG1384; Eukaryota.
DR HOGENOM; CLU_032616_2_3_1; -.
DR OMA; WGLHLKS; -.
DR OrthoDB; 11270at2759; -.
DR Proteomes; UP000006701; 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:0003676; F:nucleic acid binding; IEA:InterPro.
DR GO; GO:0052381; F:tRNA dimethylallyltransferase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
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; IPR003604; Matrin/U1-like-C_Znf_C2H2.
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 SMART; SM00451; ZnF_U1; 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.
DR PROSITE; PS50157; ZINC_FINGER_C2H2_2; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PIRNR:PIRNR039110};
KW Cytoplasm {ECO:0000256|PIRNR:PIRNR039110};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00042};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW ECO:0000256|PIRNR:PIRNR039110};
KW Reference proteome {ECO:0000313|Proteomes:UP000006701};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|PIRNR:PIRNR039110};
KW tRNA processing {ECO:0000256|PIRNR:PIRNR039110,
KW ECO:0000256|RuleBase:RU003783};
KW Zinc {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-ProRule:PRU00042};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00042}.
FT DOMAIN 406..433
FT /note="C2H2-type"
FT /evidence="ECO:0000259|PROSITE:PS50157"
FT REGION 437..472
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 437..455
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 456..472
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 472 AA; 53723 MW; 144280029ADCDB63 CRC64;
MEPLIAVVGA TGTGKSQLAV DLASRFNGEI INGDAMQLYR GLPIITNQIP IEERNGIPHH
LISCIELEEE PWRIGYFKRE CLRLIKDIHA RGKLPILVGG THYYTQTVLF KDQLVEESLV
LGDNEATHFS GEFEPTSTRW PILDAPPDVL FQKLKEVDPV MASRWHPNDS RKIRRSLEIF
FQTGKPASEI YAEQKRQKDV TSTDGDMVSG MGQLRYPTMI FWVHSEKETL NGRLAKRVDN
MVQQGLMSEA KKMWTYLQDK KEQGIIVDQT RGVWVSIGFK ELAPYFESLN EGALSEAETE
TLKQSCIELV KIATRQYASS QIKWIRNKLW RALAEAGMTD RLYLLDSTNV EDWQKCVTEP
SERLVHALLN NQPLPNPKSI SDLARETLGA REAQSQTQNS SAVQTFTCDV CNRTMATEDQ
WNIHLNGHAH KRAVKGAARK AERDEYLRKR QTPADYRNQD CSSSIEQHRN PA
//
