ID U4L5D9_PYROM Unreviewed; 480 AA.
AC U4L5D9;
DT 11-DEC-2013, integrated into UniProtKB/TrEMBL.
DT 11-DEC-2013, sequence version 1.
DT 27-MAR-2024, entry version 52.
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=PCON_10952 {ECO:0000313|EMBL:CCX11358.1};
OS Pyronema omphalodes (strain CBS 100304) (Pyronema confluens).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Pezizomycetes;
OC Pezizales; Pyronemataceae; Pyronema.
OX NCBI_TaxID=1076935 {ECO:0000313|EMBL:CCX11358.1};
RN [1] {ECO:0000313|EMBL:CCX11358.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS100304 {ECO:0000313|EMBL:CCX11358.1};
RC TISSUE=Vegetative mycelium {ECO:0000313|EMBL:CCX11358.1};
RX PubMed=24068976; DOI=10.1371/journal.pgen.1003820;
RA Traeger S., Altegoer F., Freitag M., Gabaldon T., Kempken F., Kumar A.,
RA Marcet-Houben M., Poggeler S., Stajich J.E., Nowrousian M.;
RT "The genome and development-dependent transcriptomes of Pyronema confluens:
RT a window into fungal evolution.";
RL PLoS Genet. 9:E1003820-E1003820(2013).
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}.
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DR EMBL; HF935612; CCX11358.1; -; Genomic_DNA.
DR AlphaFoldDB; U4L5D9; -.
DR STRING; 1076935.U4L5D9; -.
DR eggNOG; KOG1384; Eukaryota.
DR OMA; WGLHLKS; -.
DR OrthoDB; 11270at2759; -.
DR Proteomes; UP000018144; 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: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.
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};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW ECO:0000256|PIRNR:PIRNR039110};
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:ARBA00022771};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771}.
FT DOMAIN 432..454
FT /note="C2H2-type"
FT /evidence="ECO:0000259|PROSITE:PS00028"
SQ SEQUENCE 480 AA; 54920 MW; EC67C845A9BAB0F1 CRC64;
MNFLLRLLRL PTQKKMPPPP PLISVIGATG TGKSQLAVEL ALKFNGEVIN ADAMQLYKGL
PIITNKITDG ERKGVPHHLL GFLDTRDKWE VGRFIKECEK TIEDIRKRGK LPVLVGGTHY
YVQSLLYPHT IPAEESTQQQ DDEHSLPPVP ENLAEQYPIL DAPTPALYED LQRVDPVIAA
RWHPNDRRKI RRSLEIYYST GCKQTASEIY AAQRAAKQQP ELSDEEKQSK HRNLIFWVHA
ETEPLRQRLN GRVGKMINAG MWEEIEEMEK LYDELTKEGK VDLNSGIWQS IGFKEFVPYL
ELRKNPAAEE KELEKLRLRA VEDMKTATRR YAKIQVKWIR IKFINALLAD AKASGAPETL
AYPGNMFLVD STDVPNYDTN VVAPAINITK AFLDSSPLPD PLSLSALAKE NLTPHRDYDI
STRPDLWASN TCEHCEVTFT NMPDWQQHLK SGKHKKRMES VRKRKEVQEF LAKREQGKEK
//
