ID A0A178DL72_9PLEO Unreviewed; 710 AA.
AC A0A178DL72;
DT 07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT 07-SEP-2016, sequence version 1.
DT 24-JAN-2024, entry version 24.
DE SubName: Full=Ferric reductase transmembrane component 4 {ECO:0000313|EMBL:OAL44596.1};
GN ORFNames=IQ07DRAFT_578208 {ECO:0000313|EMBL:OAL44596.1};
OS Pyrenochaeta sp. DS3sAY3a.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Pleosporomycetidae; Pleosporales; Pleosporineae; Cucurbitariaceae;
OC Pyrenochaeta.
OX NCBI_TaxID=765867 {ECO:0000313|EMBL:OAL44596.1, ECO:0000313|Proteomes:UP000077535};
RN [1] {ECO:0000313|EMBL:OAL44596.1, ECO:0000313|Proteomes:UP000077535}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DS3sAY3a {ECO:0000313|EMBL:OAL44596.1,
RC ECO:0000313|Proteomes:UP000077535};
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 -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
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DR EMBL; KV441661; OAL44596.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A178DL72; -.
DR STRING; 765867.A0A178DL72; -.
DR InParanoid; A0A178DL72; -.
DR OrthoDB; 2444729at2759; -.
DR Proteomes; UP000077535; 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; 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.
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:UP000077535};
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 TRANSMEM 12..32
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 44..64
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 249..269
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 289..309
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 330..349
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 364..386
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 393..413
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 425..443
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 598..616
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 292..407
FT /note="Ferric oxidoreductase"
FT /evidence="ECO:0000259|Pfam:PF01794"
FT DOMAIN 449..502
FT /note="FAD-binding 8"
FT /evidence="ECO:0000259|Pfam:PF08022"
FT REGION 514..538
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 514..528
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 710 AA; 78944 MW; 59B20AC41C548F75 CRC64;
MRGKSGMGPG NLARIYSAAL GTLKLTITWT LVRQRHGIMR TTSPMGLLGL MLSGTASALI
GYHIPMYQPN CAFACRDQFG SAHLECTSMD HAGGGHHGSS ATSPECYAQD TAWLTTLAYC
INQTCADLPK FKLEAYWAER VTKSVRGNKL EPKWTYQETL HYMEGQAPPT RELEEDEVLN
FTALYNPESW ESTRGALQHF ELAETNHSKY AIILLVLKPR LVWPSLIGTY HVRALPFSIG
NVPTLGQTWY IALFIVLNII ATAAGYHSFQ YPSNAWFADG WQEVMAYVSA RTGVLAFALA
PLTILFAGRN NILLWLTNWS HSTYLLLHRW VARVFTLQII LHSILEFMLY KRQGAVDAEQ
KEPYWIWGIV ATIACVIMVV ISTLYFRRMS YEIFLIIHII LAVFVIAGSW YHVEILFARK
WGYELWLYAA CAVWFFDRVL RVGRILKNGM RRAEVTQVTD DIVRIDVKDV RWQAIPGRHT
YAYFPTINPL RPWENHPFSI IPTALLNSRG HSVAASTSSG SQHSGDDIEK SGTVGKVGPS
ATVARTNIRS GSTAGISLYV RKSAGLTKAL NQHTSLLTLL DGPYPNNSTA GVLKTDRLVL
IAGGIGITAA LPFIGYHPNV KLYWSVKSSA QGLVTDLGDV LQSLREKDVK VGGRLNVAEI
LEREESEGWK RIGVVVCGPG GLCDDVRSSV SRRGRGGGAV WELDVEAFSW
//