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Database: UniProt
Entry: A0A3P8V9G9_CYNSE
LinkDB: A0A3P8V9G9_CYNSE
Original site: A0A3P8V9G9_CYNSE 
ID   A0A3P8V9G9_CYNSE        Unreviewed;       691 AA.
AC   A0A3P8V9G9;
DT   13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT   13-FEB-2019, sequence version 1.
DT   24-JAN-2024, entry version 24.
DE   RecName: Full=tRNA 4-demethylwyosine synthase (AdoMet-dependent) {ECO:0000256|ARBA:ARBA00012821};
DE            EC=4.1.3.44 {ECO:0000256|ARBA:ARBA00012821};
OS   Cynoglossus semilaevis (Tongue sole).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC   Carangaria; Pleuronectiformes; Pleuronectoidei; Cynoglossidae;
OC   Cynoglossinae; Cynoglossus.
OX   NCBI_TaxID=244447 {ECO:0000313|Ensembl:ENSCSEP00000009075.1, ECO:0000313|Proteomes:UP000265120};
RN   [1] {ECO:0000313|Ensembl:ENSCSEP00000009075.1, ECO:0000313|Proteomes:UP000265120}
RP   NUCLEOTIDE SEQUENCE.
RX   PubMed=24487278;
RA   Chen S., Zhang G., Shao C., Huang Q., Liu G., Zhang P., Song W., An N.,
RA   Chalopin D., Volff J.N., Hong Y., Li Q., Sha Z., Zhou H., Xie M., Yu Q.,
RA   Liu Y., Xiang H., Wang N., Wu K., Yang C., Zhou Q., Liao X., Yang L.,
RA   Hu Q., Zhang J., Meng L., Jin L., Tian Y., Lian J., Yang J., Miao G.,
RA   Liu S., Liang Z., Yan F., Li Y., Sun B., Zhang H., Zhang J., Zhu Y., Du M.,
RA   Zhao Y., Schartl M., Tang Q., Wang J.;
RT   "Whole-genome sequence of a flatfish provides insights into ZW sex
RT   chromosome evolution and adaptation to a benthic lifestyle.";
RL   Nat. Genet. 46:253-260(2014).
RN   [2] {ECO:0000313|Ensembl:ENSCSEP00000009075.1}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (SEP-2023) to UniProtKB.
CC   -!- FUNCTION: Probable component of the wybutosine biosynthesis pathway.
CC       Wybutosine is a hyper modified guanosine with a tricyclic base found at
CC       the 3'-position adjacent to the anticodon of eukaryotic phenylalanine
CC       tRNA. Catalyzes the condensation of N-methylguanine with 2 carbon atoms
CC       from pyruvate to form the tricyclic 4-demethylwyosine, an intermediate
CC       in wybutosine biosynthesis. {ECO:0000256|ARBA:ARBA00025368}.
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   AlphaFoldDB; A0A3P8V9G9; -.
DR   Ensembl; ENSCSET00000009182.1; ENSCSEP00000009075.1; ENSCSEG00000005810.1.
DR   GeneTree; ENSGT00510000047059; -.
DR   UniPathway; UPA00375; -.
DR   Proteomes; UP000265120; Chromosome 4.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR   GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:InterPro.
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; IPR001094; Flavdoxin-like.
DR   InterPro; IPR008254; Flavodoxin/NO_synth.
DR   InterPro; IPR029039; Flavoprotein-like_sf.
DR   InterPro; IPR007197; rSAM.
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   PRINTS; PR00369; FLAVODOXIN.
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   Iron {ECO:0000256|ARBA:ARBA00023004};
KW   Iron-sulfur {ECO:0000256|ARBA:ARBA00023014};
KW   Membrane {ECO:0000256|SAM:Phobius};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Reference proteome {ECO:0000313|Proteomes:UP000265120};
KW   S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        12..31
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        56..76
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          109..267
FT                   /note="Flavodoxin-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50902"
FT   DOMAIN          424..661
FT                   /note="Radical SAM core"
FT                   /evidence="ECO:0000259|PROSITE:PS51918"
FT   REGION          279..338
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        279..333
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   691 AA;  78763 MW;  A9F76756680EF42E CRC64;
     MVDNCTVYCV QFAKTMIHLL CIIFLSSRVF ATDTKASQNE YSITETYFMS IWNKRLYLYT
     LAALVFGAWF LLKALWKKKS LKNVDSGVYK AVKNNEQPHT DKVVHVSGVK IFYGSQTGTA
     KVFAQELSEE VKTLGITSDV IDMKDYDPDD RLADECTSKS VCVFLVATYT DGEPTENAEW
     FCKWLEEAST DFRYGKTYLK GLRYAVFGLG NSVYVGHYNT VGKNVDKWLW MLSGMRIMTR
     GEGDCNVVKS RNGSIQADFL AWKAKFLNRL QSLAKGEKKK CSGDCKTNGS CKKKNRKEDQ
     VVEKQQQVEE KTSSEEELME SSSDEDETGG KSGSVVDMED LGNMMSSVRK VKIKEDRRGG
     DLLLNGVKKT EDEDERREMI TPALRASLTK QGYKLIGSHS GVKLCRWTKS MLRGRGGCYK
     HTFYGIESHR CMETTPSLAC ANKCVFCWRH HTNPVGTEWR WKMDPAEEIL QDAMEKHQNM
     IRQFRGVPGV KPERYEEGLV VKHCALSLVG EPIMYPEINT FLRLLHSHNI SSFLVTNAQF
     PEEIRSLVPV TQLYVSVDAS TKDSLKKIDR PLFKDFWPRF LDSLKALGEK RQRTVYRLTL
     VKAWNVEELQ AYSELIALGQ PDFIEVKAAP WRLVQSGKVD VYSDSFQATM MTPINPALDT
     PCTPFYLTYT FSLLCFLKFP FKGKNLQKIS L
//
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