ID A0A093XXS4_9PEZI Unreviewed; 486 AA.
AC A0A093XXS4;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 27-MAR-2024, entry version 44.
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=V490_02751 {ECO:0000313|EMBL:KFX97525.1};
OS Pseudogymnoascus sp. VKM F-3557.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC Leotiomycetes incertae sedis; Pseudeurotiaceae; Pseudogymnoascus.
OX NCBI_TaxID=1437433 {ECO:0000313|EMBL:KFX97525.1, ECO:0000313|Proteomes:UP000029320};
RN [1] {ECO:0000313|EMBL:KFX97525.1, ECO:0000313|Proteomes:UP000029320}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=VKM F-3557 {ECO:0000313|EMBL:KFX97525.1,
RC ECO:0000313|Proteomes:UP000029320};
RA Leushkin E.V., Logacheva M.D., Penin A.A., Sutormin R.A., Gerasimov E.S.,
RA Kochkina G.A., Ivanushkina N.E., Vasilenko O.V., Kondrashov A.S.,
RA Ozerskaya S.M.;
RT "Population genomics of a fungus Geomyces pannorum provides evidence of
RT horizontal gene transfer but not of sexual reproduction.";
RL Submitted (JUL-2014) to the EMBL/GenBank/DDBJ databases.
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 -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KFX97525.1}.
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DR EMBL; JPJS01000742; KFX97525.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A093XXS4; -.
DR STRING; 1437433.A0A093XXS4; -.
DR HOGENOM; CLU_032616_2_3_1; -.
DR Proteomes; UP000029320; 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: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; IPR000014; PAS.
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; PS50112; PAS; 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:UP000029320};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|PIRNR:PIRNR039110};
KW tRNA processing {ECO:0000256|PIRNR:PIRNR039110,
KW ECO:0000256|RuleBase:RU003783}.
FT DOMAIN 147..189
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT REGION 123..144
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 195..218
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 123..140
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 486 AA; 54484 MW; 033C66594BABBA38 CRC64;
MPRKPPHKPV VIVLGATGTG KSQLAVDLAL RYNGEIINGD AMQMYTGLPI VTNKITPAEQ
QGVPHHLIGN VSLQEEPWHV GVFKREAEGI IEEIRSRGRL PILVGGTHYY TQSLLFDDNL
VEDTDEKSQP PQDGGTENDE SLRKYPILGA STEEILAKLR EVDPVMADRW HPNDRRRIQR
SLEIYLTQGQ KASDVYAKQR ERKSAPKQDT ASANIEEPDR TIPLESTLLF WVHAGQEVLK
SRLDARVDKM VENGLIEEVQ SLQKLQEAET AASQPPDLTR GIWVSIGFKE FAPYLSTTMD
PAATEKDKSK ALALSIEQTK SATRQYAKRQ VRWIRLKLLI ALKKAGSLHN LYLMDGSDVA
NFQRDVSGQA IKVCGDFLNG LELPPPTEMS PAAAEFLTLS RDFDFGDRPD LWIRQTCEVC
NVTAVTEANW NFHLQSRGHR GKLRKLNRPP RVPRQLQTEA MEDGTQAQAM PTTLENGTAS
KILRFK
//
