ID F4RXT1_MELLP Unreviewed; 683 AA.
AC F4RXT1;
DT 28-JUN-2011, integrated into UniProtKB/TrEMBL.
DT 28-JUN-2011, sequence version 1.
DT 27-MAR-2024, entry version 53.
DE RecName: Full=FAD-binding domain-containing protein {ECO:0008006|Google:ProtNLM};
GN ORFNames=MELLADRAFT_38407 {ECO:0000313|EMBL:EGG02844.1};
OS Melampsora larici-populina (strain 98AG31 / pathotype 3-4-7) (Poplar leaf
OS rust fungus).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Pucciniomycotina;
OC Pucciniomycetes; Pucciniales; Melampsoraceae; Melampsora.
OX NCBI_TaxID=747676 {ECO:0000313|Proteomes:UP000001072};
RN [1] {ECO:0000313|Proteomes:UP000001072}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=98AG31 / pathotype 3-4-7 {ECO:0000313|Proteomes:UP000001072};
RX PubMed=21536894; DOI=10.1073/pnas.1019315108;
RA Duplessis S., Cuomo C.A., Lin Y.-C., Aerts A., Tisserant E.,
RA Veneault-Fourrey C., Joly D.L., Hacquard S., Amselem J., Cantarel B.L.,
RA Chiu R., Coutinho P.M., Feau N., Field M., Frey P., Gelhaye E.,
RA Goldberg J., Grabherr M.G., Kodira C.D., Kohler A., Kuees U.,
RA Lindquist E.A., Lucas S.M., Mago R., Mauceli E., Morin E., Murat C.,
RA Pangilinan J.L., Park R., Pearson M., Quesneville H., Rouhier N.,
RA Sakthikumar S., Salamov A.A., Schmutz J., Selles B., Shapiro H.,
RA Tanguay P., Tuskan G.A., Henrissat B., Van de Peer Y., Rouze P.,
RA Ellis J.G., Dodds P.N., Schein J.E., Zhong S., Hamelin R.C.,
RA Grigoriev I.V., Szabo L.J., Martin F.;
RT "Obligate biotrophy features unraveled by the genomic analysis of rust
RT fungi.";
RL Proc. Natl. Acad. Sci. U.S.A. 108:9166-9171(2011).
CC -!- SIMILARITY: Belongs to the PheA/TfdB FAD monooxygenase family.
CC {ECO:0000256|ARBA:ARBA00007801}.
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DR EMBL; GL883128; EGG02844.1; -; Genomic_DNA.
DR RefSeq; XP_007413957.1; XM_007413895.1.
DR AlphaFoldDB; F4RXT1; -.
DR STRING; 747676.F4RXT1; -.
DR EnsemblFungi; EGG02844; EGG02844; MELLADRAFT_38407.
DR GeneID; 18927712; -.
DR KEGG; mlr:MELLADRAFT_38407; -.
DR VEuPathDB; FungiDB:MELLADRAFT_38407; -.
DR eggNOG; KOG3855; Eukaryota.
DR HOGENOM; CLU_009665_9_2_1; -.
DR InParanoid; F4RXT1; -.
DR OrthoDB; 1386239at2759; -.
DR Proteomes; UP000001072; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0071949; F:FAD binding; IEA:InterPro.
DR GO; GO:0016705; F:oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen; IEA:UniProt.
DR CDD; cd02979; PHOX_C; 1.
DR Gene3D; 3.40.30.20; -; 1.
DR Gene3D; 3.30.9.10; D-Amino Acid Oxidase, subunit A, domain 2; 1.
DR Gene3D; 3.50.50.60; FAD/NAD(P)-binding domain; 1.
DR InterPro; IPR002938; FAD-bd.
DR InterPro; IPR036188; FAD/NAD-bd_sf.
DR InterPro; IPR012941; Phe_hydrox_C_dim_dom.
DR InterPro; IPR038220; PHOX_C_sf.
DR InterPro; IPR036249; Thioredoxin-like_sf.
DR PANTHER; PTHR43004:SF20; 2-MONOOXYGENASE, PUTATIVE (AFU_ORTHOLOGUE AFUA_1G13660)-RELATED; 1.
DR PANTHER; PTHR43004; TRK SYSTEM POTASSIUM UPTAKE PROTEIN; 1.
DR Pfam; PF01494; FAD_binding_3; 2.
DR Pfam; PF07976; Phe_hydrox_dim; 1.
DR PRINTS; PR00420; RNGMNOXGNASE.
DR SUPFAM; SSF54373; FAD-linked reductases, C-terminal domain; 1.
DR SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 1.
DR SUPFAM; SSF52833; Thioredoxin-like; 1.
PE 3: Inferred from homology;
KW FAD {ECO:0000256|ARBA:ARBA00022827};
KW Flavoprotein {ECO:0000256|ARBA:ARBA00022630};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Reference proteome {ECO:0000313|Proteomes:UP000001072};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 12..33
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 9..125
FT /note="FAD-binding"
FT /evidence="ECO:0000259|Pfam:PF01494"
FT DOMAIN 225..422
FT /note="FAD-binding"
FT /evidence="ECO:0000259|Pfam:PF01494"
FT DOMAIN 461..637
FT /note="Phenol hydroxylase C-terminal dimerisation"
FT /evidence="ECO:0000259|Pfam:PF07976"
SQ SEQUENCE 683 AA; 76499 MW; AE7780735D772275 CRC64;
MNSDSNVSKV DVLIIGAGPA GLMAAACLTK YGINNIRIVD KRSTKIYTGQ ADGLNARSLE
IFHALGMGSE IIREINVFGE VCYWEPNESG EIKRASRSPA TLPGLSKFRS SCLHQGRIEK
HLIDKISKWS ISSNQSNDQN QKRVIVERAV CPDSIELPPI TSSPLSDEDE DHITLTLRHL
SESEAQPAQF LPSTNDGLFR SNVFDDEESS LGSTLNDLPI KESLETIQCK FVIGTDGARS
WTRNALGLKL IGESLNYFWG VLDGIPATNF PDIRMRCAVH SAENGSVMII PREKDLVRLY
IQLPQPPEGQ RPNRNDVTPE KLLEVANSIL APYTIRIPKI EWYTCYEIGQ RLADSWQWNN
RVFIAGDACH THSPKAGQGM NTSMADTFNL AWKLAHVLQK KAHPKILETY ETERSKIARE
LIIFDQKLSS LFSGKPAKDK EDESGISLEE FHEILERGKY FTSGTTVNYE NNLLVVKQTD
SNLKIKSKPD LAKKISIGTR LQSHRVVCLA DAKVYDTLEL IPADGKWKLL IFPGDIQGNE
NCKAKLEKLS NFLADDQKSP IKRFTPVGDE SDSILDCITI ASSPRISLEL EHFHQILRPL
QGQHGFGSYL KIFTDEASYR EGHGHAYEKY GINPDVGCML VVRPDQHVSL ILDLDDHLAL
SKSFFSIHTP IESCQVDFFY LFL
//
