ID A0A136J529_9PEZI Unreviewed; 777 AA.
AC A0A136J529;
DT 11-MAY-2016, integrated into UniProtKB/TrEMBL.
DT 11-MAY-2016, sequence version 1.
DT 24-JAN-2024, entry version 25.
DE RecName: Full=tRNA 4-demethylwyosine synthase (AdoMet-dependent) {ECO:0000256|ARBA:ARBA00012821};
DE EC=4.1.3.44 {ECO:0000256|ARBA:ARBA00012821};
GN ORFNames=Micbo1qcDRAFT_147035 {ECO:0000313|EMBL:KXJ92262.1};
OS Microdochium bolleyi.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Xylariomycetidae; Xylariales; Microdochiaceae; Microdochium.
OX NCBI_TaxID=196109 {ECO:0000313|EMBL:KXJ92262.1, ECO:0000313|Proteomes:UP000070501};
RN [1] {ECO:0000313|Proteomes:UP000070501}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=J235TASD1 {ECO:0000313|Proteomes:UP000070501};
RG DOE Joint Genome Institute;
RA David A.S., May G., Haridas S., Lim J., Wang M., Labutti K., Lipzen A.,
RA Barry K., Grigoriev I.V.;
RT "Draft genome sequence of Microdochium bolleyi, a fungal endophyte of
RT beachgrass.";
RL Submitted (FEB-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=N(1)-methylguanosine(37) in tRNA(Phe) + pyruvate + S-adenosyl-
CC L-methionine = 4-demethylwyosine(37) in tRNA(Phe) + 5'-deoxyadenosine
CC + CO2 + H2O + L-methionine; Xref=Rhea:RHEA:36347, Rhea:RHEA-
CC COMP:10164, Rhea:RHEA-COMP:10165, ChEBI:CHEBI:15361,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:16526, ChEBI:CHEBI:17319,
CC ChEBI:CHEBI:57844, ChEBI:CHEBI:59789, ChEBI:CHEBI:64315,
CC ChEBI:CHEBI:73542; EC=4.1.3.44;
CC Evidence={ECO:0000256|ARBA:ARBA00000664};
CC -!- COFACTOR:
CC Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC Evidence={ECO:0000256|ARBA:ARBA00001966};
CC -!- PATHWAY: tRNA modification; wybutosine-tRNA(Phe) biosynthesis.
CC {ECO:0000256|ARBA:ARBA00004797}.
CC -!- SIMILARITY: Belongs to the TYW1 family.
CC {ECO:0000256|ARBA:ARBA00010115}.
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; KQ964249; KXJ92262.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A136J529; -.
DR STRING; 196109.A0A136J529; -.
DR InParanoid; A0A136J529; -.
DR OrthoDB; 275822at2759; -.
DR UniPathway; UPA00375; -.
DR Proteomes; UP000070501; Unassembled WGS sequence.
DR GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW.
DR GO; GO:0010181; F:FMN binding; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0102521; F:tRNA-4-demethylwyosine synthase activity; IEA:UniProtKB-EC.
DR GO; GO:0008033; P:tRNA processing; IEA:InterPro.
DR CDD; cd01335; Radical_SAM; 1.
DR Gene3D; 3.40.50.360; -; 1.
DR Gene3D; 3.20.20.70; Aldolase class I; 1.
DR InterPro; IPR013785; Aldolase_TIM.
DR InterPro; IPR008254; Flavodoxin/NO_synth.
DR InterPro; IPR029039; Flavoprotein-like_sf.
DR InterPro; IPR007197; rSAM.
DR InterPro; IPR013917; tRNA_wybutosine-synth.
DR InterPro; IPR034556; tRNA_wybutosine-synthase.
DR PANTHER; PTHR13930; S-ADENOSYL-L-METHIONINE-DEPENDENT TRNA 4-DEMETHYLWYOSINE SYNTHASE; 1.
DR PANTHER; PTHR13930:SF0; S-ADENOSYL-L-METHIONINE-DEPENDENT TRNA 4-DEMETHYLWYOSINE SYNTHASE TYW1-RELATED; 1.
DR Pfam; PF00258; Flavodoxin_1; 1.
DR Pfam; PF04055; Radical_SAM; 1.
DR Pfam; PF08608; Wyosine_form; 1.
DR SFLD; SFLDF00284; tRNA_wybutosine-synthesizing; 1.
DR SFLD; SFLDG01071; tRNA_wybutosine-synthesizing; 1.
DR SUPFAM; SSF52218; Flavoproteins; 1.
DR SUPFAM; SSF102114; Radical SAM enzymes; 1.
DR PROSITE; PS50902; FLAVODOXIN_LIKE; 1.
DR PROSITE; PS51918; RADICAL_SAM; 1.
PE 3: Inferred from homology;
KW 4Fe-4S {ECO:0000256|ARBA:ARBA00022485};
KW Iron {ECO:0000256|ARBA:ARBA00023004};
KW Iron-sulfur {ECO:0000256|ARBA:ARBA00023014};
KW Lyase {ECO:0000256|ARBA:ARBA00023239};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000070501};
KW S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691}.
FT DOMAIN 118..292
FT /note="Flavodoxin-like"
FT /evidence="ECO:0000259|PROSITE:PS50902"
FT DOMAIN 443..691
FT /note="Radical SAM core"
FT /evidence="ECO:0000259|PROSITE:PS51918"
FT REGION 43..109
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 303..327
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 756..777
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 56..82
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 84..99
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 313..327
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 762..777
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 777 AA; 86516 MW; 5559B80E90C61AC3 CRC64;
MAGPTGSGAS GLIEAWHQHR TYTLVVATGI ACVVWLLVTR KSEHEGPKAD APKAVSSSAR
SASVAQDEKP SQVDQPLPTT AKSKEAQKEP RRIKGEVRKN NAGQNKSPVL ATSQPTQVLV
FFSSLTAGTE KRAGAYMQIL EPLLAAIQKE SQSTFLKPEL LNLAEVDYDE YFINPPKSAG
EVDVPASYFY LFILPSYNID TINDTFIEHL QETHNDFRID TAPLSGLLGY SVFGIGDREG
WPTEDEGFCF QAKEVDKWMA KLTSRKRAYP VGMADARLDY QDRLSEWTDG IKSVLEMVAR
TGSLGEGVPG SGDAVESDDE GEVDDDDGEV VFEDGSVPLR NTKRKEGRNV DDVEDLGRIM
KSSREDGTDT ARAPLAVDFT TYKSSTSKGV PAIKEMVPKN SPTYTSLTKQ GYSIVGSHSG
VKICRWTKSA LRGRGSCYKY SFYGINSHQC METTPSLSCS NKCVFCWRHG TNPVGTTWRW
KVDPPELIFD GVKAGHYQKI KMMRGVPGVR AERFAEAMRI RHCALSLVGE PIFYPYINEF
LGMLHAERIS SFLVCNAQHP DQLAALKAVT QLYVSIDASN KESLRKIDRP LHRDFWERFQ
RCLDILREKR FKQRTVFRLT LVKGFNIDDE VEGYADLVER GLPCFVEIKG VTYCGTSTSA
GAGLSMANVP FYNEVTDFVE ALTAKLQERG LGYGIAAEHA HSCCVLIASD RFNVDGKWHT
RIDYQRFFEL LEERGADGDW TPEDYMGEAT PEWATWGNGG FDPRDERVDR KGRPIAV
//
