ID F2PKY9_TRIEC Unreviewed; 499 AA.
AC F2PKY9;
DT 31-MAY-2011, integrated into UniProtKB/TrEMBL.
DT 31-MAY-2011, sequence version 1.
DT 27-MAR-2024, entry version 42.
DE SubName: Full=FAD binding domain-containing protein {ECO:0000313|EMBL:EGE02587.1};
GN ORFNames=TEQG_01622 {ECO:0000313|EMBL:EGE02587.1};
OS Trichophyton equinum (strain ATCC MYA-4606 / CBS 127.97) (Horse ringworm
OS fungus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Onygenales; Arthrodermataceae; Trichophyton.
OX NCBI_TaxID=559882 {ECO:0000313|Proteomes:UP000009169};
RN [1] {ECO:0000313|Proteomes:UP000009169}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC MYA-4606 / CBS 127.97 {ECO:0000313|Proteomes:UP000009169};
RX PubMed=22951933; DOI=10.1128/mbio.00259-12;
RA Martinez D.A., Oliver B.G., Graeser Y., Goldberg J.M., Li W.,
RA Martinez-Rossi N.M., Monod M., Shelest E., Barton R.C., Birch E.,
RA Brakhage A.A., Chen Z., Gurr S.J., Heiman D., Heitman J., Kosti I.,
RA Rossi A., Saif S., Samalova M., Saunders C.W., Shea T., Summerbell R.C.,
RA Xu J., Young S., Zeng Q., Birren B.W., Cuomo C.A., White T.C.;
RT "Comparative genome analysis of Trichophyton rubrum and related
RT dermatophytes reveals candidate genes involved in infection.";
RL MBio 3:E259-E259(2012).
CC -!- SIMILARITY: Belongs to the oxygen-dependent FAD-linked oxidoreductase
CC family. {ECO:0000256|ARBA:ARBA00005466}.
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; DS995723; EGE02587.1; -; Genomic_DNA.
DR AlphaFoldDB; F2PKY9; -.
DR VEuPathDB; FungiDB:TEQG_01622; -.
DR eggNOG; ENOG502QQWK; Eukaryota.
DR HOGENOM; CLU_018354_4_4_1; -.
DR Proteomes; UP000009169; Unassembled WGS sequence.
DR GO; GO:0071949; F:FAD binding; IEA:InterPro.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR GO; GO:1901576; P:organic substance biosynthetic process; IEA:UniProt.
DR Gene3D; 3.30.465.10; -; 2.
DR Gene3D; 3.40.462.20; -; 1.
DR InterPro; IPR012951; BBE.
DR InterPro; IPR016166; FAD-bd_PCMH.
DR InterPro; IPR036318; FAD-bd_PCMH-like_sf.
DR InterPro; IPR016169; FAD-bd_PCMH_sub2.
DR InterPro; IPR006094; Oxid_FAD_bind_N.
DR PANTHER; PTHR13878; GULONOLACTONE OXIDASE; 1.
DR PANTHER; PTHR13878:SF91; L-GULONOLACTONE OXIDASE 3; 1.
DR Pfam; PF08031; BBE; 1.
DR Pfam; PF01565; FAD_binding_4; 1.
DR SUPFAM; SSF56176; FAD-binding/transporter-associated domain-like; 1.
DR PROSITE; PS51387; FAD_PCMH; 1.
PE 3: Inferred from homology;
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..21
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 22..499
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5003283630"
FT DOMAIN 118..302
FT /note="FAD-binding PCMH-type"
FT /evidence="ECO:0000259|PROSITE:PS51387"
SQ SEQUENCE 499 AA; 54369 MW; 69BEBFC985615E37 CRC64;
MKIPSQQVLL ALPLLASPAQ SYPGKHPRCS AGDACWPKDH VWQDFNSTIS GRLIRTFPAA
AVCHTAQYDA AACSVAKERW TDSFWRTNQT GAYSAILWEL GEKGQCFINT PKEDKCDQGI
VPYYSVSASG VKDIEKAVKF ADKHDLYLVV KNTGHDHLGR SSGSGAFSIW THNLKGKEWH
KTFKPKGAPS NVGGIPAVTL QAGEQLLDVY KAAAAEGVTF AGGSAQTVGA AGGFMTGGGV
SPFSHFYGLA VDNVLEVNLV TAQGKAKTIN QYTDPDYFYA LRGGGGSAWG VITSVTYKTH
PKPTHIRVGI AQLNVTTEDA RRVVIEKSLQ ALPDITEAGW VGYGVYATEK TNPTAFQVIF
LQPNATMENF NKTFEPMNKI GTLPVVKVNS DERDNTSVHS SFKDSRALIS FSVDWADNAS
EQEKKAAKKT SAEVSKRLAE IVGKETGTYL NEASPYEPDW QNAFWGDKYA RLLSIKRRID
PKNLFVCNRC VGTDIVLEP
//
