ID Q0U1J9_PHANO Unreviewed; 1687 AA.
AC Q0U1J9;
DT 05-SEP-2006, integrated into UniProtKB/TrEMBL.
DT 05-FEB-2008, sequence version 2.
DT 27-MAR-2024, entry version 78.
DE RecName: Full=FAD-binding PCMH-type domain-containing protein {ECO:0000259|PROSITE:PS51387};
GN ORFNames=SNOG_14375 {ECO:0000313|EMBL:EAT78246.2};
OS Phaeosphaeria nodorum (strain SN15 / ATCC MYA-4574 / FGSC 10173) (Glume
OS blotch fungus) (Parastagonospora nodorum).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Pleosporomycetidae; Pleosporales; Pleosporineae; Phaeosphaeriaceae;
OC Parastagonospora.
OX NCBI_TaxID=321614 {ECO:0000313|EMBL:EAT78246.2, ECO:0000313|Proteomes:UP000001055};
RN [1] {ECO:0000313|Proteomes:UP000001055}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SN15 / ATCC MYA-4574 / FGSC 10173
RC {ECO:0000313|Proteomes:UP000001055};
RX PubMed=18024570; DOI=10.1105/tpc.107.052829;
RA Hane J.K., Lowe R.G., Solomon P.S., Tan K.C., Schoch C.L., Spatafora J.W.,
RA Crous P.W., Kodira C., Birren B.W., Galagan J.E., Torriani S.F.,
RA McDonald B.A., Oliver R.P.;
RT "Dothideomycete-plant interactions illuminated by genome sequencing and EST
RT analysis of the wheat pathogen Stagonospora nodorum.";
RL Plant Cell 19:3347-3368(2007).
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000256|ARBA:ARBA00001974};
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CH445355; EAT78246.2; -; Genomic_DNA.
DR RefSeq; XP_001804563.1; XM_001804511.1.
DR EnsemblFungi; SNOT_14375; SNOT_14375; SNOG_14375.
DR GeneID; 5981487; -.
DR KEGG; pno:SNOG_14375; -.
DR VEuPathDB; FungiDB:JI435_143750; -.
DR VEuPathDB; FungiDB:JI435_308950; -.
DR eggNOG; KOG1231; Eukaryota.
DR HOGENOM; CLU_002983_0_0_1; -.
DR InParanoid; Q0U1J9; -.
DR OrthoDB; 2680039at2759; -.
DR Proteomes; UP000001055; Unassembled WGS sequence.
DR GO; GO:0005739; C:mitochondrion; IBA:GO_Central.
DR GO; GO:0004458; F:D-lactate dehydrogenase (cytochrome) activity; IBA:GO_Central.
DR GO; GO:0008720; F:D-lactate dehydrogenase activity; IBA:GO_Central.
DR GO; GO:0071949; F:FAD binding; IEA:InterPro.
DR GO; GO:0050660; F:flavin adenine dinucleotide binding; IBA:GO_Central.
DR GO; GO:1903457; P:lactate catabolic process; IBA:GO_Central.
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:UP000001055}.
FT DOMAIN 1246..1427
FT /note="FAD-binding PCMH-type"
FT /evidence="ECO:0000259|PROSITE:PS51387"
FT REGION 1..24
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 440..460
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 517..573
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 606..638
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 658..794
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 835..994
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1054..1131
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1144..1169
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 445..460
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 529..549
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 606..621
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 658..706
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 736..762
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 763..794
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 842..862
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 874..890
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 901..945
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1054..1070
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1084..1098
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1687 AA; 182586 MW; AC994661D30763FE CRC64;
MASSRSSRAP SFSSDRPSAA SSITFQMPTT VRPAPAYIAA SVASQIVTDH HNAQLREEDD
DADELENAIF SEQALSLLNA FLDHLLFAFL SSARSPSLTA VRPAISDVLK PRLAREATES
ADEELQGLLA GEDDEISAND GQPVDKWDVE KVWKRTRLRI MVYTRLGELE DEDEEKYVQQ
ERGLSMDEDE DDEAGLVSWA SAIFLTSVIE YIAEQTLLVS GSAAYARMAA KLKKVQQQVQ
DTEEASFERI VVEEPDAEKI ALNSALGRLW RTWRKRVRSP LSPISPGRGI RSVASWGSLH
RRKMSHDTID GSLRGEQEPI PERIPTETEI AANIPLPVGD NDVNEIEVPG LANTFEADSE
STGTQTPVPR NQRPSSVIML APVETFRRRA TKPRPVSMPH PPASEFTVPV FSERASDPPE
TPFETPMEYA TKRTSYMAHE QPAAVPQHTH HEEREALESP QTADAEMLAF AANTGLGFRM
STVNPIKTEV PAKTEDEPEI PSAGGYESEP KIMQSKRMSV EKTGPPGIVR TFSTRSSSRS
AQHTPVASPM LPQQADARSY LDDAETTDDE PERTAIGVAR TSDIPIRSTP TPDMAAHGGY
VEVQPRQTSI SSISARNTPS PDAKPITPDR SVARKDLHKR ELSGGAYAAA GASQLGNITS
APRQQAPPKS RGASLPSLQE AESPNARRNK TTSEASPTQT ATQRKPVQAG RDARANTLER
QAQNKSAEET KRTPHATLDG SPSSEKSAVQ RVSSTSSKKS SIHARNNGRD SEASQRSAVR
SRMSEEDRER QFESLVNAEE TVKFTLTPQT VRDFEASSPS LTVRFTVFHI HPRVNADKDN
SFGTGHLPSR SSSRSKGPVA APQKSSPSRK VVGRQLAREP RIEQESMRDF ADFIRSTGPS
PGQDKPVQPF VNISGNGPRS TNASSSSLGR KTSTRQNSTR GTEGPSASGK PRVNMEPRSP
AGLSTGNDDL IDFIRQGPPN APNGQPRIPR NVAPFRTTVD SDQFDQMLGG NNVESAYGST
ASTLDSKHST QTINSRTGLI PEPKVVQPAY SNQPQKLSGN MASNNQEPVI TRTRRRVKDP
YAIDISDEED DDEDEDQLTA LPPSTQPPGV RQESLMDFLN GMDPPSTSKP EPFVLSPETI
AAAKARANTS SSSLSSTTTG PRNGPQNYGA ISSTSVASDA HRAYKPRLQA RAPAVSEVRT
SKTATSDLAD FLRNSGPPEH VVPSQPVEEK KKNLRTVTTS VKYVNVSSFP HIALFYPSTT
QDVSILLKEC HERRIAVTAY GGGTSFGGAL SNSGGVCVSF ERMAQLLHIN ADDGDCVVQP
GLNWMHLNAL LQKSEKGTGL FFPVDPSPQA SVGGMIAMSC SGTNAYRYGT MRECVVGVTV
VLADGRVVKT KQRPRKSSAG YDLTHLIVGS EGTLGLVTEA TLRLVPLPRN LHVGIATFGA
LEGGVDVVLE VQKSGHVFEA LEVADGKQME CLNRSKLSPV NFTETPTLFF KIAGPSKQMV
ADQINIMKTL CARHKATSLE ITDDESRIAT LWGARKAMGT ALVAMKQSPT DLFIHSDCAV
PISKLPALIA GTHDLITAAT PPNSRWFCAN VGHAGDGNVH SSIICPAEDK ELAEAVIKRI
CRLALSLEGT VTGEHGVGMK LRDVLEEEVG KTGVEIMRGI KEALDPRGIL NPGKVFRLEN
GVGKAKL
//
