ID M3DBB4_SPHMS Unreviewed; 459 AA.
AC M3DBB4;
DT 01-MAY-2013, integrated into UniProtKB/TrEMBL.
DT 01-MAY-2013, sequence version 1.
DT 27-MAR-2024, entry version 55.
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=SEPMUDRAFT_38605 {ECO:0000313|EMBL:EMF15350.1};
OS Sphaerulina musiva (strain SO2202) (Poplar stem canker fungus) (Septoria
OS musiva).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Dothideomycetidae; Mycosphaerellales; Mycosphaerellaceae; Sphaerulina.
OX NCBI_TaxID=692275 {ECO:0000313|EMBL:EMF15350.1, ECO:0000313|Proteomes:UP000016931};
RN [1] {ECO:0000313|EMBL:EMF15350.1, ECO:0000313|Proteomes:UP000016931}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SO2202 {ECO:0000313|EMBL:EMF15350.1,
RC ECO:0000313|Proteomes:UP000016931};
RX PubMed=23236275; DOI=10.1371/journal.ppat.1003037;
RA Ohm R.A., Feau N., Henrissat B., Schoch C.L., Horwitz B.A., Barry K.W.,
RA Condon B.J., Copeland A.C., Dhillon B., Glaser F., Hesse C.N., Kosti I.,
RA LaButti K., Lindquist E.A., Lucas S., Salamov A.A., Bradshaw R.E.,
RA Ciuffetti L., Hamelin R.C., Kema G.H.J., Lawrence C., Scott J.A.,
RA Spatafora J.W., Turgeon B.G., de Wit P.J.G.M., Zhong S., Goodwin S.B.,
RA Grigoriev I.V.;
RT "Diverse lifestyles and strategies of plant pathogenesis encoded in the
RT genomes of eighteen Dothideomycetes fungi.";
RL PLoS Pathog. 8:E1003037-E1003037(2012).
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 -!- SIMILARITY: Belongs to the IPP transferase family.
CC {ECO:0000256|ARBA:ARBA00005842, ECO:0000256|PIRNR:PIRNR039110,
CC ECO:0000256|RuleBase:RU003785}.
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; KB456261; EMF15350.1; -; Genomic_DNA.
DR RefSeq; XP_016763471.1; XM_016908711.1.
DR AlphaFoldDB; M3DBB4; -.
DR STRING; 692275.M3DBB4; -.
DR GeneID; 27905848; -.
DR eggNOG; KOG1384; Eukaryota.
DR HOGENOM; CLU_032616_2_3_1; -.
DR OMA; WGLHLKS; -.
DR OrthoDB; 11270at2759; -.
DR Proteomes; UP000016931; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
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; IPR022755; Znf_C2H2_jaz.
DR InterPro; IPR036236; Znf_C2H2_sf.
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; PF12171; zf-C2H2_jaz; 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.
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:ARBA00022723};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW ECO:0000256|PIRNR:PIRNR039110};
KW Reference proteome {ECO:0000313|Proteomes:UP000016931};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|PIRNR:PIRNR039110};
KW tRNA processing {ECO:0000256|PIRNR:PIRNR039110,
KW ECO:0000256|RuleBase:RU003783}; Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771}.
FT DOMAIN 403..427
FT /note="Zinc finger double-stranded RNA binding"
FT /evidence="ECO:0000259|Pfam:PF12171"
FT REGION 418..459
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 459 AA; 52175 MW; 0989178C14C1D88E CRC64;
MTRTPPKQPL VAVIGATGTG KSQLAVEIAK RYNGEIINGD AMQLYAGLPI LTNKITPDEQ
EGIPHHLLGC IALHEQTWVV GTFIRHALKT IEEIRARGKL PILVGGTHYY TQSLLFYDRL
AEDEEEREQR EFIVDTSDKW PILKEPTDVL LKELNRIDPV MADRWHPNDR RKIQRSLEIY
LQTGKRASDI YAEQRARKEE VGAEEAGEPK MRFPALLIWV HCEAAVLRER LDKRVDKMLA
NGLLDEVNTL DRFARDQETQ GTRVDDGKGI WVSIGYREFR DYVRKLHTSV DEQQTLEKLK
AIALEATQAS TRQYAKRQVR WIRIKLVNAL MQANASHQMY LLNGSDVSRF EETVVDPALQ
LTGQYLRAED MPAPSTLSTV AAEQLQPKRD DLAGAPEAWV KQYCSVCDTT SVTPTQWQQH
ISSKSHKKRV SKARQAESRT AGLYRDPSGN EAKSDEVLQ
//
