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Database: UniProt
Entry: A0A177CGW7_9PLEO
LinkDB: A0A177CGW7_9PLEO
Original site: A0A177CGW7_9PLEO 
ID   A0A177CGW7_9PLEO        Unreviewed;       462 AA.
AC   A0A177CGW7;
DT   07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT   07-SEP-2016, sequence version 1.
DT   27-MAR-2024, entry version 23.
DE   RecName: Full=FAD-binding PCMH-type domain-containing protein {ECO:0000259|PROSITE:PS51387};
GN   ORFNames=CC84DRAFT_1088054 {ECO:0000313|EMBL:OAG06813.1};
OS   Paraphaeosphaeria sporulosa.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC   Pleosporomycetidae; Pleosporales; Massarineae; Didymosphaeriaceae;
OC   Paraphaeosphaeria.
OX   NCBI_TaxID=1460663 {ECO:0000313|EMBL:OAG06813.1, ECO:0000313|Proteomes:UP000077069};
RN   [1] {ECO:0000313|EMBL:OAG06813.1, ECO:0000313|Proteomes:UP000077069}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AP3s5-JAC2a {ECO:0000313|EMBL:OAG06813.1,
RC   ECO:0000313|Proteomes:UP000077069};
RG   DOE Joint Genome Institute;
RA   Zeiner C.A., Purvine S.O., Zink E.M., Wu S., Pasa-Tolic L., Chaput D.L.,
RA   Haridas S., Grigoriev I.V., Santelli C.M., Hansel C.M.;
RT   "Comparative analysis of secretome profiles of manganese(II)-oxidizing
RT   ascomycete fungi.";
RL   Submitted (MAY-2016) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the oxygen-dependent FAD-linked oxidoreductase
CC       family. {ECO:0000256|ARBA:ARBA00005466}.
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DR   EMBL; KV441551; OAG06813.1; -; Genomic_DNA.
DR   RefSeq; XP_018037178.1; XM_018174232.1.
DR   AlphaFoldDB; A0A177CGW7; -.
DR   STRING; 1460663.A0A177CGW7; -.
DR   GeneID; 28757718; -.
DR   InParanoid; A0A177CGW7; -.
DR   OrthoDB; 2446456at2759; -.
DR   Proteomes; UP000077069; Unassembled WGS sequence.
DR   GO; GO:0071949; F:FAD binding; IEA:InterPro.
DR   Gene3D; 3.30.465.10; -; 1.
DR   Gene3D; 3.40.462.20; -; 1.
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:SF13; DEPENDENT OXIDOREDUCTASE, PUTATIVE-RELATED; 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   Reference proteome {ECO:0000313|Proteomes:UP000077069};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..20
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           21..462
FT                   /note="FAD-binding PCMH-type domain-containing protein"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5008058186"
FT   DOMAIN          18..196
FT                   /note="FAD-binding PCMH-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51387"
SQ   SEQUENCE   462 AA;  49653 MW;  F410173A4BFDA9CF CRC64;
     MRRAAVVAAA VAALGATVSA DTCASVAATS SIQIKKQLDI GYATEQANYW STACGAMKPS
     CQLPNQGFAS IDGGPLISTR ELNEVIYDAG NGVVRVGPGN DWDDVIGALD GTGVTVVGGR
     IGDVGVGGLV LGGGLSFLST QYGWVANNVV EYEIVLANAS IVTASESHNA DLWKALKGGI
     NNYGIVTAYT FKAHPQGQIW GGNIAYTADK SAEILAAVRD FTEYYPDDKA GIIMTAELTQ
     FGVIDIWLMF LFYDGPTPPA GVFDNFTAIA HLSDDTKSRS YSDLLTHNNF GVIKTEIYTI
     ATEMIPLPSA DVGPDFLGAI YDNWRNTTES VIDAAGLIGS IALQPIPKRL ARKAMEAGGD
     MIDLDDEIDR IILEFDLSWL SPLDSARMDV ATQKFYTGSK DLVEQYQADD KLPEGYLPLF
     ANDAYYRQDY FGRLRTADFA RTVRDAVDPS GFFASRTGGW KP
//
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