ID K1XH75_MARBU Unreviewed; 757 AA.
AC K1XH75;
DT 28-NOV-2012, integrated into UniProtKB/TrEMBL.
DT 28-NOV-2012, sequence version 1.
DT 27-MAR-2024, entry version 47.
DE SubName: Full=Ferric reductase like transmembrane component {ECO:0000313|EMBL:EKD20113.1};
GN ORFNames=MBM_02065 {ECO:0000313|EMBL:EKD20113.1};
OS Marssonina brunnea f. sp. multigermtubi (strain MB_m1) (Marssonina leaf
OS spot fungus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC Helotiales; Drepanopezizaceae; Drepanopeziza.
OX NCBI_TaxID=1072389 {ECO:0000313|EMBL:EKD20113.1, ECO:0000313|Proteomes:UP000006753};
RN [1] {ECO:0000313|EMBL:EKD20113.1, ECO:0000313|Proteomes:UP000006753}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MB_m1 {ECO:0000313|EMBL:EKD20113.1,
RC ECO:0000313|Proteomes:UP000006753};
RX PubMed=22876864; DOI=10.1186/1471-2164-13-382;
RA Zhu S., Cao Y.-Z., Jiang C., Tan B.-Y., Wang Z., Feng S., Zhang L.,
RA Su X.-H., Brejova B., Vinar T., Xu M., Wang M.-X., Zhang S.-G.,
RA Huang M.-R., Wu R., Zhou Y.;
RT "Sequencing the genome of Marssonina brunnea reveals fungus-poplar co-
RT evolution.";
RL BMC Genomics 13:382-382(2012).
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
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DR EMBL; JH921430; EKD20113.1; -; Genomic_DNA.
DR RefSeq; XP_007289954.1; XM_007289892.1.
DR AlphaFoldDB; K1XH75; -.
DR GeneID; 18758000; -.
DR KEGG; mbe:MBM_02065; -.
DR eggNOG; KOG0039; Eukaryota.
DR HOGENOM; CLU_010365_2_0_1; -.
DR InParanoid; K1XH75; -.
DR OMA; GHQWGYE; -.
DR OrthoDB; 2444729at2759; -.
DR Proteomes; UP000006753; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR GO; GO:0006811; P:monoatomic ion transport; IEA:UniProtKB-KW.
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 InterPro; IPR013112; FAD-bd_8.
DR InterPro; IPR017927; FAD-bd_FR_type.
DR InterPro; IPR013130; Fe3_Rdtase_TM_dom.
DR InterPro; IPR039261; FNR_nucleotide-bd.
DR PANTHER; PTHR32361:SF9; FERRIC REDUCTASE TRANSMEMBRANE COMPONENT 3-RELATED; 1.
DR PANTHER; PTHR32361; FERRIC/CUPRIC REDUCTASE TRANSMEMBRANE COMPONENT; 1.
DR Pfam; PF08022; FAD_binding_8; 1.
DR Pfam; PF01794; Ferric_reduct; 1.
DR SFLD; SFLDS00052; Ferric_Reductase_Domain; 1.
DR SFLD; SFLDG01168; Ferric_reductase_subgroup_(FRE; 1.
DR SUPFAM; SSF52343; Ferredoxin reductase-like, C-terminal NADP-linked domain; 1.
DR PROSITE; PS51384; FAD_FR; 1.
PE 4: Predicted;
KW Ion transport {ECO:0000256|ARBA:ARBA00023065};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Reference proteome {ECO:0000313|Proteomes:UP000006753};
KW Signal {ECO:0000256|SAM:SignalP};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}; Transport {ECO:0000256|ARBA:ARBA00023065}.
FT SIGNAL 1..20
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 21..757
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5003855116"
FT TRANSMEM 181..202
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 239..259
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 324..346
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 361..383
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 390..410
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 445..623
FT /note="FAD-binding FR-type"
FT /evidence="ECO:0000259|PROSITE:PS51384"
FT REGION 510..582
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 510..527
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 528..542
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 545..579
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 757 AA; 83622 MW; 78EDDCDFA09CCE2C CRC64;
MYHLVPSLLL LLWQTAGASA GGIIGYGITM YKPVCAYACS DALSSLYLNC TTFMSHDSMD
MAGMKLKKRM DMGSEMMGMT SDECYATDRV WQETLAYCMK DRCGTIDGVS EERIAKAYSK
LSNSDAVYSE VLPAERPATE LDADAEWLNV TSLVNSKLYF DNRQTRSEFE YQETMHARLS
IVVYVLTVGI ALVVGYFARF GLARLVPVAV SKHLVLPALF NGRHQAPLPG NLGYAPSRLL
SFLIFLYVLL NIIFSAVPYK SVAPNAESTW FTAKKNEIAT YVANRTGVLS FANLGIAILF
AGRLNPLILL SGLSQNACLT FHRWAARVST AQAIVHSIIY TVTYFWDGGK QAYYDEVKKA
YYWWGIVATV LMSLGLAFSI LPLRKAQYEI FLVAHVIMAI MVLIGCWYHI ELRFGTSWGY
EVWLYICIAF WSFDRLARFG LARYRNMWGT TTQAVAELTP GGHFIKLTVY PGKKWTFGPG
QHAFLFFPST GRFWENHPFS IAAWDHGSSS SSSSSPSSQV TEEAASSPQQ RDPEKDADME
ISHAPAGNDS SSTSSSSLPT KTRPATHATA TTTYTGDGRP SITFLIRPHK GMTSTIQREL
AALPTPTHFP LSLEGPHGHA ADLSRADAIL CIAGGIGITA LTAYTQHFVE ARRRQAMAAR
RLVLAWSYRE RELAPVVRAL LPADAEALGV VFVWRCTTEG ERVDVPALVQ SEAQAAKRLA
VLVSASGGLA DEVRRWVVEC EGVAGTRIQL HEESFTW
//
