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Database: UniProt
Entry: N4U6P3_FUSC1
LinkDB: N4U6P3_FUSC1
Original site: N4U6P3_FUSC1 
ID   N4U6P3_FUSC1            Unreviewed;       774 AA.
AC   N4U6P3;
DT   26-JUN-2013, integrated into UniProtKB/TrEMBL.
DT   26-JUN-2013, sequence version 1.
DT   27-MAR-2024, entry version 39.
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=FOC1_g10005166 {ECO:0000313|EMBL:ENH65635.1};
OS   Fusarium oxysporum f. sp. cubense (strain race 1) (Panama disease fungus).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Hypocreomycetidae; Hypocreales; Nectriaceae; Fusarium;
OC   Fusarium oxysporum species complex.
OX   NCBI_TaxID=1229664 {ECO:0000313|EMBL:ENH65635.1, ECO:0000313|Proteomes:UP000016928};
RN   [1] {ECO:0000313|Proteomes:UP000016928}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=race 1 {ECO:0000313|Proteomes:UP000016928};
RA   Fang X., Huang J.;
RT   "Genome sequencing and comparative transcriptomics of race 1 and race 4 of
RT   banana pathogen: Fusarium oxysporum f. sp. cubense.";
RL   Submitted (SEP-2012) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|Proteomes:UP000016928}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=race 1 {ECO:0000313|Proteomes:UP000016928};
RX   PubMed=24743270;
RA   Guo L., Han L., Yang L., Zeng H., Fan D., Zhu Y., Feng Y., Wang G.,
RA   Peng C., Jiang X., Zhou D., Ni P., Liang C., Liu L., Wang J., Mao C.,
RA   Fang X., Peng M., Huang J.;
RT   "Genome and Transcriptome Analysis of the Fungal Pathogen Fusarium
RT   oxysporum f. sp. cubense Causing Banana Vascular Wilt Disease.";
RL   PLoS ONE 9:E95543-E95543(2014).
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}.
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DR   EMBL; KB730484; ENH65635.1; -; Genomic_DNA.
DR   AlphaFoldDB; N4U6P3; -.
DR   STRING; 1229664.N4U6P3; -.
DR   VEuPathDB; FungiDB:FOC1_g10005166; -.
DR   HOGENOM; CLU_007952_1_2_1; -.
DR   OMA; FHVNGKW; -.
DR   UniPathway; UPA00375; -.
DR   Proteomes; UP000016928; 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:UP000016928};
KW   S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691}.
FT   DOMAIN          119..289
FT                   /note="Flavodoxin-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50902"
FT   DOMAIN          437..686
FT                   /note="Radical SAM core"
FT                   /evidence="ECO:0000259|PROSITE:PS51918"
FT   REGION          82..112
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          299..345
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          748..774
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        314..330
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        331..345
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        760..774
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   774 AA;  87721 MW;  C20BE3FED302AC10 CRC64;
     MDWANYSPPS RLDSFVDDLV DVWHLHRTPI LLTLCVILVA IRTYFHINGQ KTEIVAFKKV
     YEEPAKPKVV VEEKTPTIEA VEEKKNGKSQ GPRRIKGGIA RKPSKNKEEE KDLTRPVAPL
     VFFSSITTKT AKIAEAYIED FCGKLDELSK LSGRQFLKPE LRDLTEIDFD DYFLAPYKGH
     GDADLFYLFL IPSYNIDTIN DTFLEHLQET HHDFRIDTAP LSGILGYSVF GFGDSENWPT
     EADGFCFQAM EVDKWMAKLT ARKRAYPVGM GDMKSDHEER LQEWSKGVQE VIEHVARTGS
     LGEGVPGSGA AEESDVEDIA EDEDDGEVVF DDEEPKKKSK SARDLDDVED LGRLIKKDDG
     STTQKAPLAV DFTTYGSSTK KAVPQGPKEM VAKESPTYKA LTKQGYAIVG SHSGVKTCRW
     TKSALRGRGS CYKYSFYGIK SHLCMETTPS LSCSNKCVFC WRHGTNPVGT TWRWVVDPPE
     LIFEGVKKNH YQKIKMLRGV PGVRAERFAE AMQIKHCALS LVGEPIFYPY INEFLGMLHA
     ERISSFLVCN AQHPDQLAAL KVVTQLYVSI DAADKESLRK IDRPLHRDFW ERFNRCLDIL
     REKRFHHRTV FRLTLVKGFN VEEEAEGYAR LVEQGLPCFV EVKGVTYCGT STSSNAGLSM
     SNVPFYWEVC DFVKALEKRL KEKGLKYGIA AEHAHSCCIL LASERFYVDG KWHTLIDYKK
     FFELLESRGP PDEGGWTPED YMDATPTPEW ANWGNGGFNP EDERVDRKGR KIEA
//
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