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Database: UniProt
Entry: A0A161X212_9PEZI
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ID   A0A161X212_9PEZI        Unreviewed;       783 AA.
AC   A0A161X212;
DT   06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT   06-JUL-2016, sequence version 1.
DT   24-JAN-2024, entry version 27.
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=CI238_05561 {ECO:0000313|EMBL:KZL87716.1};
OS   Colletotrichum incanum.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Hypocreomycetidae; Glomerellales; Glomerellaceae; Colletotrichum;
OC   Colletotrichum spaethianum species complex.
OX   NCBI_TaxID=1573173 {ECO:0000313|EMBL:KZL87716.1, ECO:0000313|Proteomes:UP000076584};
RN   [1] {ECO:0000313|EMBL:KZL87716.1, ECO:0000313|Proteomes:UP000076584}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MAFF 238704 {ECO:0000313|EMBL:KZL87716.1,
RC   ECO:0000313|Proteomes:UP000076584};
RA   Hacquard S., Kracher B., Hiruma K., Weinman A., Muench P., Garrido Oter R.,
RA   Ver Loren van Themaat E., Dallerey J.-F., Damm U., Henrissat B.,
RA   Lespinet O., Thon M., Kemen E., McHardy A.C., Schulze-Lefert P.,
RA   O'Connell R.J.;
RT   "Survival trade-offs in plant roots during colonization by closely related
RT   pathogenic and mutualistic fungi.";
RL   Submitted (JUN-2015) 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   -!- 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:KZL87716.1}.
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DR   EMBL; LFIW01000193; KZL87716.1; -; Genomic_DNA.
DR   STRING; 1573173.A0A161X212; -.
DR   OrthoDB; 275822at2759; -.
DR   UniPathway; UPA00375; -.
DR   Proteomes; UP000076584; 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; SFLDS00029; Radical_SAM; 1.
DR   SFLD; SFLDF00284; 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:UP000076584};
KW   S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691}.
SQ   SEQUENCE   783 AA;  88295 MW;  879845DFD8FBBC09 CRC64;
     MASSLESAGF KSILNNAHDA WQQVRIPVIL FAAFGLLVLR FYLHSTEEKG ELKAIPKVYN
     REKPETKPVD EKKDVKKDIK PSPPSPTTES KAPKSNGPKR IKGGLVKRTS SDSSNGEALA
     RKIRPLIFFS SITANTPKIA KEYAERLEKD LQKAATDTSC SFVTPEVLDL AEVDFDDYFI
     TPPKSEEDPA ELFYLFLLPS YNIDTINDTF LEHLQETHHD FRIDTAPLSS LLGYSVFGFG
     DREGWPTEDD GFCFQAKEVD KWMAKLTGRK RAFPVGMGDT KRDYSERLSE WSEGVVDVLG
     MLAKTGSLGE GLPGSGAPEE SDDESAEEDD DEVLIEDSEA KPEKLKNRKN IDDVEDLGRI
     MKSSNPEADK NSRTAAAPIA VDFTTYGKTA QKKTPTPAAK EMVPKNSPTY ASLTKQGYSI
     VGSHSGVKIC RWTKSALRGR GSCYKYSFYG INSHQCMETT PSLSCSNKCV FCWRHGTNPV
     GTTWRWVVDP PELIFDGVKA NHYNKIKMLR GVPGVRAERF AEAMRIRHCA LSLVGEPIFY
     PYINEFLGML HAERISSFLV CNAQHPDQLA ALKAVTQLYV SIDASNKESL RKIDRPLHRD
     FWERFQRCLD ILREKRFKHR TVFRLTLVKG FNVDDEVEGY AQLVEKGLPC FVEIKGVTYC
     GTSTASNAGL SMSNVPFYWE VAEFVKALEK RLNEKGLKYG IAAEHAHSCC VLLASERFYV
     DGKWHPRIDY QRFFELLEER GPDGDWKPED YMGEATPEWA TWGNGGFDPR DERVDRKGRK
     IER
//
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