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Database: UniProt
Entry: G0SFZ5_CHATD
LinkDB: G0SFZ5_CHATD
Original site: G0SFZ5_CHATD 
ID   G0SFZ5_CHATD            Unreviewed;       478 AA.
AC   G0SFZ5;
DT   19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT   19-OCT-2011, sequence version 1.
DT   24-JAN-2024, entry version 42.
DE   RecName: Full=FAD-binding PCMH-type domain-containing protein {ECO:0000259|PROSITE:PS51387};
GN   ORFNames=CTHT_0072700 {ECO:0000313|EMBL:EGS17910.1};
OS   Chaetomium thermophilum (strain DSM 1495 / CBS 144.50 / IMI 039719)
OS   (Thermochaetoides thermophila).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Sordariomycetidae; Sordariales; Chaetomiaceae; Thermochaetoides.
OX   NCBI_TaxID=759272 {ECO:0000313|Proteomes:UP000008066};
RN   [1] {ECO:0000313|EMBL:EGS17910.1, ECO:0000313|Proteomes:UP000008066}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 1495 / CBS 144.50 / IMI 039719
RC   {ECO:0000313|Proteomes:UP000008066};
RX   PubMed=21784248; DOI=10.1016/j.cell.2011.06.039;
RA   Amlacher S., Sarges P., Flemming D., van Noort V., Kunze R., Devos D.P.,
RA   Arumugam M., Bork P., Hurt E.;
RT   "Insight into structure and assembly of the nuclear pore complex by
RT   utilizing the genome of a eukaryotic thermophile.";
RL   Cell 146:277-289(2011).
CC   -!- SIMILARITY: Belongs to the oxygen-dependent FAD-linked oxidoreductase
CC       family. {ECO:0000256|ARBA:ARBA00005466}.
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DR   EMBL; GL988047; EGS17910.1; -; Genomic_DNA.
DR   RefSeq; XP_006697528.1; XM_006697465.1.
DR   AlphaFoldDB; G0SFZ5; -.
DR   SMR; G0SFZ5; -.
DR   STRING; 759272.G0SFZ5; -.
DR   GeneID; 18261308; -.
DR   KEGG; cthr:CTHT_0072700; -.
DR   eggNOG; ENOG502SJ3M; Eukaryota.
DR   HOGENOM; CLU_018354_0_1_1; -.
DR   OMA; GICECVG; -.
DR   OrthoDB; 1068078at2759; -.
DR   Proteomes; UP000008066; Unassembled WGS sequence.
DR   GO; GO:0071949; F:FAD binding; IEA:InterPro.
DR   GO; GO:0016491; F:oxidoreductase activity; IEA:InterPro.
DR   Gene3D; 3.30.465.10; -; 1.
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; PTHR42973; BINDING OXIDOREDUCTASE, PUTATIVE (AFU_ORTHOLOGUE AFUA_1G17690)-RELATED; 1.
DR   PANTHER; PTHR42973:SF9; FAD-BINDING PCMH-TYPE DOMAIN-CONTAINING PROTEIN-RELATED; 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   Reference proteome {ECO:0000313|Proteomes:UP000008066};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..18
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           19..478
FT                   /note="FAD-binding PCMH-type domain-containing protein"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5003409200"
FT   DOMAIN          65..253
FT                   /note="FAD-binding PCMH-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51387"
SQ   SEQUENCE   478 AA;  53433 MW;  E9C23A9F18E1A9D9 CRC64;
     MKLIHTLLDL LTPITVIAHK GDHTPKTIDF ASLSLLLSPS SSITFPKASS LNPLLRWSFN
     INVNYPALPR AVVSPATEAD VVATIKFSNK HEIPFLVQGG GHATSASLKE FKEGVLISMK
     KFDKLEIKPG RKTALIGVGL KVNDVVHGLW KEGLQTTTGI CACAGAVGPA LGGGHGFLQG
     QYGLAADEIV RNEDLFWAIR GAGHNFGVIT EMEYKVHEVE EGKKTWAVQA FVFTGSVEHV
     EELYKVAEEL RKKQPKEMVP IIAFQFMYNG PQSDFVAYTK PLADFTPIAT FSNVTDYPGL
     MTFIGTHLEG PLCPEKSTAV LHAADVDYYD VPAIRNVWEL FNEMVTTVPG LAGSYMMLEG
     YSVQAMQAVP EESTAYPHRK QDFLLAPILL WVNGNKTLDE LGEKWGIKLK QASWSKFRPR
     SYINYAAVDE SLETLYGEQW RLKKLRRIKE TYDPENHFRF FSPIIRREKP EKTRKEEL
//
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