GenomeNet

Database: UniProt
Entry: W2W3W7_PHYPR
LinkDB: W2W3W7_PHYPR
Original site: W2W3W7_PHYPR 
ID   W2W3W7_PHYPR            Unreviewed;      1211 AA.
AC   W2W3W7;
DT   19-MAR-2014, integrated into UniProtKB/TrEMBL.
DT   19-MAR-2014, sequence version 1.
DT   27-MAR-2024, entry version 43.
DE   RecName: Full=FAD-binding FR-type domain-containing protein {ECO:0000259|PROSITE:PS51384};
GN   ORFNames=F441_18605 {ECO:0000313|EMBL:ETP04688.1};
OS   Phytophthora parasitica CJ01A1.
OC   Eukaryota; Sar; Stramenopiles; Oomycota; Peronosporales; Peronosporaceae;
OC   Phytophthora.
OX   NCBI_TaxID=1317063 {ECO:0000313|EMBL:ETP04688.1, ECO:0000313|Proteomes:UP000018958};
RN   [1] {ECO:0000313|EMBL:ETP04688.1, ECO:0000313|Proteomes:UP000018958}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CJ01A1 {ECO:0000313|EMBL:ETP04688.1,
RC   ECO:0000313|Proteomes:UP000018958};
RG   The Broad Institute Genomics Platform;
RA   Russ C., Tyler B., Panabieres F., Shan W., Tripathy S., Grunwald N.,
RA   Machado M., Johnson C.S., Walker B., Young S.K., Zeng Q., Gargeya S.,
RA   Fitzgerald M., Haas B., Abouelleil A., Allen A.W., Alvarado L.,
RA   Arachchi H.M., Berlin A.M., Chapman S.B., Gainer-Dewar J., Goldberg J.,
RA   Griggs A., Gujja S., Hansen M., Howarth C., Imamovic A., Ireland A.,
RA   Larimer J., McCowan C., Murphy C., Pearson M., Poon T.W., Priest M.,
RA   Roberts A., Saif S., Shea T., Sisk P., Sykes S., Wortman J., Nusbaum C.,
RA   Birren B.;
RT   "The Genome Sequence of Phytophthora parasitica CJ01A1.";
RL   Submitted (NOV-2013) to the EMBL/GenBank/DDBJ databases.
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC       pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:ETP04688.1}.
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; ANIX01003733; ETP04688.1; -; Genomic_DNA.
DR   AlphaFoldDB; W2W3W7; -.
DR   EnsemblProtists; ETP04688; ETP04688; F441_18605.
DR   Proteomes; UP000018958; Unassembled WGS sequence.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR   CDD; cd07067; HP_PGM_like; 1.
DR   CDD; cd06186; NOX_Duox_like_FAD_NADP; 1.
DR   Gene3D; 3.40.50.80; Nucleotide-binding domain of ferredoxin-NADP reductase (FNR) module; 1.
DR   Gene3D; 3.40.50.1240; Phosphoglycerate mutase-like; 1.
DR   Gene3D; 2.40.30.10; Translation factors; 1.
DR   InterPro; IPR000778; Cyt_b245_heavy_chain.
DR   InterPro; IPR011992; EF-hand-dom_pair.
DR   InterPro; IPR013112; FAD-bd_8.
DR   InterPro; IPR017927; FAD-bd_FR_type.
DR   InterPro; IPR013130; Fe3_Rdtase_TM_dom.
DR   InterPro; IPR013121; Fe_red_NAD-bd_6.
DR   InterPro; IPR039261; FNR_nucleotide-bd.
DR   InterPro; IPR013078; His_Pase_superF_clade-1.
DR   InterPro; IPR029033; His_PPase_superfam.
DR   InterPro; IPR017938; Riboflavin_synthase-like_b-brl.
DR   PANTHER; PTHR11972:SF69; METALLOREDUCTASE AIM14-RELATED; 1.
DR   PANTHER; PTHR11972; NADPH OXIDASE; 1.
DR   Pfam; PF08022; FAD_binding_8; 1.
DR   Pfam; PF01794; Ferric_reduct; 1.
DR   Pfam; PF00300; His_Phos_1; 1.
DR   Pfam; PF08030; NAD_binding_6; 1.
DR   PRINTS; PR00466; GP91PHOX.
DR   SFLD; SFLDS00052; Ferric_Reductase_Domain; 1.
DR   SFLD; SFLDG01168; Ferric_reductase_subgroup_(FRE; 1.
DR   SFLD; SFLDG01169; NADPH_oxidase_subgroup_(NOX); 1.
DR   SMART; SM00855; PGAM; 1.
DR   SUPFAM; SSF47473; EF-hand; 1.
DR   SUPFAM; SSF52343; Ferredoxin reductase-like, C-terminal NADP-linked domain; 1.
DR   SUPFAM; SSF53254; Phosphoglycerate mutase-like; 1.
DR   SUPFAM; SSF63380; Riboflavin synthase domain-like; 1.
DR   PROSITE; PS51384; FAD_FR; 1.
PE   4: Predicted;
KW   Flavoprotein {ECO:0000256|ARBA:ARBA00022630};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW   NADP {ECO:0000256|ARBA:ARBA00022857};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW   ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        673..689
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        754..777
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        808..828
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        840..861
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          873..1010
FT                   /note="FAD-binding FR-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51384"
FT   REGION          398..428
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        414..428
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1211 AA;  137253 MW;  DDD0C310B060D214 CRC64;
     MTGPHSTSSS NSPTIRAVDG FFSTIPQAEA SSELLQLFRQ FKLATSSWSE FREKLEADGT
     RNLKVVFFIR HGEGLHNEAI KLYGSERWYK ELVTSDVYRD AELTPFGIQD AKNKGPPSIK
     AEMERGMPPI ERVVVSPISR AIQTAQNFFV ENQIPDKPFV CIESCREHLG VDTCNNRRSV
     SELKAKFPAV DFSALKDEED TLWTTDYRES AEEIQTRAKE FLTELFRTIP ERHVAVVTHF
     GFIEAVCAAM LGMKIEAVLS RQHGRLDITL STSVKCRVQN VSGSLVDFAP SDDILLSGLE
     TKMVVNYASN EPQPGDSIFP RSTTTTPAST IKSEFAMLET NTPVECTHTL HQEETKELQR
     LPSALAMPRI YGPSVRQPPI DSQSKRTSFV AMLGGSGVDR HVRKPLGNSR RGHTRRAGGT
     TNRSSFLPNE SALNMSFHPS MSGASMWSRP SRQMNKAELY ELKDRLWKDS LSSAPSNAFG
     AVDCGDPHAP EQLSFFTHAF NTSRITGEGS AALGYDERSR SSMAFIPLPR ESVAMMIDAV
     RVSALDDNEK CRFLFEMFDV EHHGVLTKEG VRAFIEATFA ANGVDFVGAF DYDAVVDKVF
     GHCRQPYKMT FNEFKAIFAD VVVEADDDKS KEALGLMSSV VETQRQREIV YNNEQGGRWY
     RVKKYCRKYK PEIFWLTLYF LLMIGVFIAK ASRFPVDPAV GNCPRIAKGF AEICLVNTMF
     VLLPMCRNFV TGLRTLPVVV NHLPIDNHIE FHKVCGVVML IASVGHTAAW LAIVIYVRTV
     PLAVWEASRY HHLSFVRDEN LFDFALRIPI WTGMVMLICA GIAAPLCLAK YRRGNFNMFW
     VTHMLFIPFL VLMAFHGFAR WLAEPQAQYW ILPPVVIFLI EKRYRMTQVF GGQTKIIHVQ
     LSKESVAIFM KKPRSFGKRQ RFLPGMYMFI NVPAISKFEW HPFTISSAPE DKFLSLHIQK
     AGDWTGALYK NLEMLQREHK ASSIEDQGSP MTSPYPVVYL DGPVGAPAQD YSRYREVVLI
     GAGIGVTPFA SILRSIMHQW ESFRCPHCRH VRFPPSFQLR KIYFYWVTRE QESLTWFTNT
     MNQLSEMDTE NRLEIHNFFS SVKSEAVIAP LQALQKFIHN NEGQDIISGL NTKQQTHFGR
     PDWNTELSRV ARNHRLLEPS VNTSDEREEI GVFFCGPKPL GNIIHEQCTV LNQAKARQAP
     DVQFEFHSEN F
//
DBGET integrated database retrieval system