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
//