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Database: UniProt
Entry: A0A177BU02_9PLEO
LinkDB: A0A177BU02_9PLEO
Original site: A0A177BU02_9PLEO 
ID   A0A177BU02_9PLEO        Unreviewed;      1764 AA.
AC   A0A177BU02;
DT   07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT   07-SEP-2016, sequence version 1.
DT   27-MAR-2024, entry version 27.
DE   RecName: Full=FAD-binding PCMH-type domain-containing protein {ECO:0000259|PROSITE:PS51387};
GN   ORFNames=CC84DRAFT_1223652 {ECO:0000313|EMBL:OAF98655.1};
OS   Paraphaeosphaeria sporulosa.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC   Pleosporomycetidae; Pleosporales; Massarineae; Didymosphaeriaceae;
OC   Paraphaeosphaeria.
OX   NCBI_TaxID=1460663 {ECO:0000313|EMBL:OAF98655.1, ECO:0000313|Proteomes:UP000077069};
RN   [1] {ECO:0000313|EMBL:OAF98655.1, ECO:0000313|Proteomes:UP000077069}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AP3s5-JAC2a {ECO:0000313|EMBL:OAF98655.1,
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   -!- COFACTOR:
CC       Name=FAD; Xref=ChEBI:CHEBI:57692;
CC         Evidence={ECO:0000256|ARBA:ARBA00001974};
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DR   EMBL; KV441565; OAF98655.1; -; Genomic_DNA.
DR   RefSeq; XP_018029021.1; XM_018183510.1.
DR   STRING; 1460663.A0A177BU02; -.
DR   GeneID; 28766996; -.
DR   InParanoid; A0A177BU02; -.
DR   OrthoDB; 2680039at2759; -.
DR   Proteomes; UP000077069; Unassembled WGS sequence.
DR   GO; GO:0003824; F:catalytic activity; IEA:InterPro.
DR   GO; GO:0071949; F:FAD binding; IEA:InterPro.
DR   Gene3D; 3.30.465.10; -; 1.
DR   Gene3D; 3.30.70.2740; -; 1.
DR   InterPro; IPR004113; FAD-bd_oxidored_4_C.
DR   InterPro; IPR016166; FAD-bd_PCMH.
DR   InterPro; IPR036318; FAD-bd_PCMH-like_sf.
DR   InterPro; IPR016169; FAD-bd_PCMH_sub2.
DR   InterPro; IPR016164; FAD-linked_Oxase-like_C.
DR   InterPro; IPR006094; Oxid_FAD_bind_N.
DR   InterPro; IPR016171; Vanillyl_alc_oxidase_C-sub2.
DR   PANTHER; PTHR11748; D-LACTATE DEHYDROGENASE; 1.
DR   PANTHER; PTHR11748:SF116; D-LACTATE DEHYDROGENASE (CYTOCHROME) (AFU_ORTHOLOGUE AFUA_7G02560); 1.
DR   Pfam; PF02913; FAD-oxidase_C; 1.
DR   Pfam; PF01565; FAD_binding_4; 1.
DR   SUPFAM; SSF56176; FAD-binding/transporter-associated domain-like; 1.
DR   SUPFAM; SSF55103; FAD-linked oxidases, C-terminal domain; 1.
DR   PROSITE; PS51387; FAD_PCMH; 1.
PE   4: Predicted;
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW   Reference proteome {ECO:0000313|Proteomes:UP000077069}.
FT   DOMAIN          1323..1500
FT                   /note="FAD-binding PCMH-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51387"
FT   REGION          1..32
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          410..458
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          490..1148
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1182..1278
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1298..1321
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        7..32
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        516..532
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        549..575
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        662..676
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        695..722
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        762..812
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        816..835
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        883..913
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        917..931
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        955..991
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1060..1114
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1193..1231
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1764 AA;  190596 MW;  23DB448DE60476D9 CRC64;
     MQHQRSRSDA GDVSSPRSSR APSFSSDRPS LAGSVTFQMP SSVRPAPAYI AASVASQIVT
     DNHNAQLRED TAVSVNEEPG AGLSNALFSE QALSLLNAFL DHLLFAFLST ARSPSLTAIR
     PAIIDVLKPR LAREAMATAD EELAGLLAGE DDEEFPAQQK NEGEPWDVEK VWKRTRLRIM
     VYTRLGELED EDEERYVQQE RGLSMDESDD EEAGLVSWAS AIFLTSIVEH VAEQTLLISG
     QAAFTRLSAR MRKMAQQSPD SEEQQLERLI VEDFDVEKVA LNSALGRLWR TWRKRVRSPI
     TPLSPRGIHS MSSYTSLHRR HLSHDTDHGS MIDGVPEVPE YKPTETEIAA NIPLPIGDND
     IREIEVPGLA RTFEEDESSG AETPVTRPQR PTSVIMLAPA ELLRNRVAKE RPLSVPPPQR
     KSLVLPVFSE QESEEEADDL PFETPMEAME PTSDDDSYIH DERQEDMHHD NEENGDHEAD
     ADMVAFAAST GMGFGMTPPG GPIRTEKKST LGKEEDSADT PTQSNYNGDS RVFVSKRMSL
     EKTGPPGIVR TYSTRSSSLR SQNRSQPNSP GMTPNMEARS FLEDDNSEDD TPGPEAIGVA
     HTSNIPIPSP SPSAEVNGAE KALGHAKHPS HGGYVEVLPR QIAPTAIHVR STPTPDGTRG
     PSEIPDARKE VQRRDVPQPY VHVPQPRPRE FTPPGTRLSS LQETEAWQSK QQQHQPSIPV
     KSARRGSPSE GSGRYTSPQR AREPIVAVAE RPAHLKSIEG SPRSRSGPTD GPADTKTSLK
     RVSSSSSSTA GRSVGTSILH SGRESSTSLD GRPRGLSGRM SEEDRQREFD SLVRSDETVK
     VTLTPQNMRD MDEAAVVRRE SPKPSPKPAK SSVTVYPRVN ADKDSQFGSQ HLPTRTSPRS
     NGPTPSSSSK GSMKKPLARE PQVRGDSMRD FADFIRSTGP APGDEKPVQR FALSGTGAKP
     NNGSSSSIGG LGRKLSTRQT SSHSHSSSLA GDGPSAKPRI HMEPRSPAGQ RSGNDDLIDF
     IRQGPPNSNN GQPRIPRSVA PFRTTVDSDQ FDHMLDNGNV ESAYGSQVST VSKQSSQTSN
     SKTGLIPKQS VTQPAYSNTP QQLSGSMSNV EPQITRTRRR IKDPYAIDSD DEDDDLLTAL
     PTSNKPVHRE ESMMDFLNSM EPTSNSPPQA FMLSPETIAA AKARAAAGKG GANGHSHTNS
     LTSSISAPRN GTNSRAGPSQ AHISTSVASN PPRGGYKPKL QARGAASEPR AGRSATNDLA
     DFLRNSGPPE PPAPAPGATI RREENNIAAL IQDIQNASPS TAYSTNTADL TPTSSTSHSY
     APPEQISKAV FYPKTTEDTS VILKACHRRR IAVTAYSGGT SLPGALTNSR GGVCVHFGGM
     DKVIGVSEGD LDVRVQPGIG WVELNEYLAP KGLFFPVDPA PGAKIGGMVA MSCSGTNAYR
     YGTMKEWVIS LTVVLSDGTI VTTRRRPRKS SAGYDLTHLI IGSEGTLALV TEAVLKITPL
     PQNLHVGKAT FPSLQQGVSS VKQILQSGNL LEAIELADKP SIVSINHSKL AKEHLEETPT
     LFVKFAGSKE TVSSQIAFVM KTCKENGGLA FEASSDKQRI DVIWGARKCL GNALVTMKKI
     PTDLFISTDA AVPISAMATL IEETNEIIAK RPYDTSKWFC ANVGHVGDGN VHTAIVCPVE
     DKEKAEQVLV EVQRLALTLE GTITGEHGVG LKLRDMLVEE VGEAGVGVMR AVKRALDPRG
     ILNPDKVFRL EAEKGTIGGR LEKL
//
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