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
//