ID A0A0P9F1M0_RHOGW Unreviewed; 852 AA.
AC A0A0P9F1M0;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 27-MAR-2024, entry version 29.
DE RecName: Full=FAD-binding FR-type domain-containing protein {ECO:0000259|PROSITE:PS51384};
GN ORFNames=RHOBADRAFT_54724 {ECO:0000313|EMBL:KPV73505.1};
OS Rhodotorula graminis (strain WP1).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Pucciniomycotina;
OC Microbotryomycetes; Sporidiobolales; Sporidiobolaceae; Rhodotorula.
OX NCBI_TaxID=578459 {ECO:0000313|EMBL:KPV73505.1, ECO:0000313|Proteomes:UP000053890};
RN [1] {ECO:0000313|EMBL:KPV73505.1, ECO:0000313|Proteomes:UP000053890}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=WP1 {ECO:0000313|EMBL:KPV73505.1,
RC ECO:0000313|Proteomes:UP000053890};
RX PubMed=26441909; DOI=10.3389/fmicb.2015.00978;
RA Firrincieli A., Otillar R., Salamov A., Schmutz J., Khan Z., Redman R.S.,
RA Fleck N.D., Lindquist E., Grigoriev I.V., Doty S.L.;
RT "Genome sequence of the plant growth promoting endophytic yeast Rhodotorula
RT graminis WP1.";
RL Front. Microbiol. 6:978-978(2015).
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000256|ARBA:ARBA00001974};
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
CC -!- SIMILARITY: Belongs to the ferric reductase (FRE) family.
CC {ECO:0000256|ARBA:ARBA00006278}.
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; KQ474082; KPV73505.1; -; Genomic_DNA.
DR RefSeq; XP_018269554.1; XM_018417469.1.
DR AlphaFoldDB; A0A0P9F1M0; -.
DR STRING; 578459.A0A0P9F1M0; -.
DR GeneID; 28977917; -.
DR OMA; LNYVHRW; -.
DR OrthoDB; 1385919at2759; -.
DR Proteomes; UP000053890; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0000293; F:ferric-chelate reductase activity; IEA:UniProt.
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; 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 PANTHER; PTHR32361:SF9; FERRIC REDUCTASE TRANSMEMBRANE COMPONENT 3-RELATED; 1.
DR PANTHER; PTHR32361; FERRIC/CUPRIC REDUCTASE TRANSMEMBRANE COMPONENT; 1.
DR Pfam; PF01794; Ferric_reduct; 1.
DR Pfam; PF08030; NAD_binding_6; 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 3: Inferred from homology;
KW Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
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:UP000053890};
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 32..53
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 108..129
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 149..169
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 181..199
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 219..235
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 256..271
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 305..490
FT /note="FAD-binding FR-type"
FT /evidence="ECO:0000259|PROSITE:PS51384"
FT REGION 83..102
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 588..619
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 685..706
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 83..99
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 590..604
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 852 AA; 90381 MW; 52996668D2FB2F51 CRC64;
MSVCYDSIGI PVPCAGWNVY DSYVTDPRYQ RYFTIAWTSA FAVAFIVNAP ALVRTLATGD
WRRALGSSAG LFGVHEGHAR RGYVPLGRDD KKRPEPHSST SGLARRPYLA LAAVVRSASL
LTLPLPAFFA RLSSRTTPSC HPTRTYAPFS LGRLAVALLI PAFLVATLLP ESQLRANPNR
FGFLAIACIP LVFVLSAKNG PASWLLGRGW TAVNFLHRWL ARAIVLLVLL HFYFWTIQYS
GAAQTAFLAG EKERRGIAAL AFLLLLTLSS LPPMRRFSYP VFFTLHHCGL VGFLVFLHRH
TVYARAYSTW PVVAIYTLDV LGRLLSLRVR VAECDALEGG MTRVALPGLR AGWRGGQHLS
VRLFFVPPPL EHAPGTSRTR RLVRDAAHAL RCAVRPFEAH PLSIASAPAG LAADEGERGV
ELYARSCGPR TWSDDLHRHV AASSALAATA KAVGRSAASP QQQRVEAQRS ASSVRMLCLI
EGPYGGLPAY SSPVGLLEQT ESLVLVAGGS GMSFVLGVLD ELVGRRLRAK GGARGGRVDV
VWVVRQRAHV AWFAERLRAV LAAAEGSPLR VVLKVYVTCD DALATAVDAS APAPSSSPSS
SSSAGAAAPP PPPPLLPELA TLSYSRPSLR TLVHDALDRA LAPCGTCYPV CRCGELAGAG
GECANDEEEC VGGCGGVASA RELLDRREGE EEKGEGGEEK EERRGEVVPT LARQGGCCGS
QSAASRARDA TAVDEIVELP SAVPSSCCGP SSSTSFPPAR APPSCGCCCA RTTGGGCCTG
VTEGPASAAD VDADERDRVE GRPLRVRTGG MGFVVCGPGN MVAELRNAVA TIPLAKQARV
GGITVHVEQY SV
//
