ID E9EYV3_METRA Unreviewed; 1436 AA.
AC E9EYV3;
DT 05-APR-2011, integrated into UniProtKB/TrEMBL.
DT 04-MAR-2015, sequence version 2.
DT 27-MAR-2024, entry version 52.
DE SubName: Full=Ferric-chelate reductase {ECO:0000313|EMBL:EFY99144.2};
GN ORFNames=MAA_05202 {ECO:0000313|EMBL:EFY99144.2};
OS Metarhizium robertsii (strain ARSEF 23 / ATCC MYA-3075) (Metarhizium
OS anisopliae (strain ARSEF 23)).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Clavicipitaceae; Metarhizium.
OX NCBI_TaxID=655844 {ECO:0000313|EMBL:EFY99144.2, ECO:0000313|Proteomes:UP000002498};
RN [1] {ECO:0000313|EMBL:EFY99144.2, ECO:0000313|Proteomes:UP000002498}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ARSEF 23 / ATCC MYA-3075 {ECO:0000313|Proteomes:UP000002498};
RX PubMed=21253567; DOI=10.1371/journal.pgen.1001264;
RA Gao Q., Jin K., Ying S.H., Zhang Y., Xiao G., Shang Y., Duan Z., Hu X.,
RA Xie X.Q., Zhou G., Peng G., Luo Z., Huang W., Wang B., Fang W., Wang S.,
RA Zhong Y., Ma L.J., St Leger R.J., Zhao G.P., Pei Y., Feng M.G., Xia Y.,
RA Wang C.;
RT "Genome sequencing and comparative transcriptomics of the model
RT entomopathogenic fungi Metarhizium anisopliae and M. acridum.";
RL PLoS Genet. 7:E1001264-E1001264(2011).
RN [2] {ECO:0000313|EMBL:EFY99144.2, ECO:0000313|Proteomes:UP000002498}
RP GENOME REANNOTATION.
RC STRAIN=ARSEF 23 / ATCC MYA-3075 {ECO:0000313|Proteomes:UP000002498};
RX PubMed=25368161; DOI=10.1073/pnas.1412662111;
RA Hu X., Xiao G., Zheng P., Shang Y., Su Y., Zhang X., Liu X., Zhan S.,
RA St Leger R.J., Wang C.;
RT "Trajectory and genomic determinants of fungal-pathogen speciation and host
RT adaptation.";
RL Proc. Natl. Acad. Sci. U.S.A. 111:16796-16801(2014).
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 -!- 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:EFY99144.2}.
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; ADNJ02000002; EFY99144.2; -; Genomic_DNA.
DR RefSeq; XP_007821391.2; XM_007823200.2.
DR GeneID; 19259488; -.
DR KEGG; maj:MAA_05202; -.
DR HOGENOM; CLU_248849_0_0_1; -.
DR OrthoDB; 2049651at2759; -.
DR Proteomes; UP000002498; 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:0000041; P:transition metal ion transport; IEA:UniProt.
DR CDD; cd06186; NOX_Duox_like_FAD_NADP; 2.
DR Gene3D; 3.40.50.80; Nucleotide-binding domain of ferredoxin-NADP reductase (FNR) module; 2.
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 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; 2.
DR Pfam; PF08030; NAD_binding_6; 1.
DR SFLD; SFLDS00052; Ferric_Reductase_Domain; 2.
DR SFLD; SFLDG01168; Ferric_reductase_subgroup_(FRE; 2.
DR SUPFAM; SSF52343; Ferredoxin reductase-like, C-terminal NADP-linked domain; 2.
DR PROSITE; PS51384; FAD_FR; 1.
PE 3: Inferred from homology;
KW Electron transport {ECO:0000256|ARBA:ARBA00022982};
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 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..21
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 22..1436
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5003235743"
FT TRANSMEM 216..237
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 283..304
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 324..341
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 362..384
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 396..418
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 425..446
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 452..468
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 874..904
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 951..971
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 991..1009
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1030..1051
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1066..1089
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1096..1119
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 1132..1287
FT /note="FAD-binding FR-type"
FT /evidence="ECO:0000259|PROSITE:PS51384"
FT REGION 133..177
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 159..175
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1436 AA; 159962 MW; D98487AD685B4363 CRC64;
MASKWIACGL VLQAGLAAAD GTGMVGLGKT MYNPPCAFAC RASISSCPLL CTPKGEDAET
PPECFTTDQA FMRTLALCIS MYCSQFDHPS LAKIEDYWES HLASSTVAKF EWKPAMSYGE
ALRLAKIDEQ NAVGRSQTSA GGGDHHGHKR QLLPRHGGSH GSGDEHDEMD HVDSPLPVIK
PRAPLNVTSV VAQKDWTKSY NGAKGFEINE AGHAKYTLVL LLVALFAPVV LSLVRFVPGL
SRSRTWQWVS SMLVEPPAWG KSHREPVSPY TGGGLMPTRG QALYILLISV LNTVFLVAPY
AALFPQTSFP SVESMEISTI GNRAGVLAMG NMVALFVFSA RNNVLLWLTD WPYDTFILLH
RWLGYWTILL AVIHSLMLFG YYVAEGMYED EAAKLYWTWG IVATVCGAAL WPSSLLVVRQ
KAYELFLCTH QVLVVFFVVG YYYHIWERYR HNWGYEIWVF VAIAVWLLER SARLLRVGLA
GLKTAVVSPV EGSDGDYVRV DIEDTFAEGV AYLYFPTLSW RFWENHPFSI ASSFSAHATD
AGGSLEKLHV TDVEKTARTS TRSAEVEVEA KADSPSTTAS TVTTRPSGKT RVTIAVRVRS
SMTARLAARV SAAGGPIRIP VFLEGSYHSS AGSQLSRCTR ILCIAGGVGV SAVLPILRQH
GNRPARLCWG IRNDSLRSVF RDEISGLSAT VDVETHVGSR MDVGSILREE LTAPCGSEDR
GPIGVVVCGP PGMADDVRNT ICTLGRSATN ALAPVRFSDA EVLPAKSRVE MCRSQRAVTS
MYLCLDMFCE QDARAAEVAA LNETCVGADM DALPPISIIS NYTPGDIERL RHIRLGETFA
PNATVKEVVV PAFELYKAWF DTLDAYRYVT HHHFLYGFSM ILFWLAVLAI GVGNRIILGC
IRFLKTYRLY RSRRSETATW VKSRIVIPAT FGYRCATEVW CGTIPPRIQS LTIAAFAIMN
LAFSIFGYKI TPVNLYFSTP TRQWLRYVSD RTGIISFANF PIIWLFGMRN NFAIWLTGWD
FGTYNNFHRW VARIATLQAV VHSLGYTVLI LKEGGWTYFA WWWTQMFWLA GEVATVLMCA
LMACSIYWLR RQKYELFLVL HIGMSIFILV TMLGHVSIFN GHYDAFFWVP VFIWVFDRVL
RILRIIFFNP TIKPTVATAT YNLSTNIVRL HVPCHFRAHK VRPGTYYYLS VIDDKRFWES
HPFTVASVSD SHLPGKPFGE QAPLLESDVI CAEEQEMAKP NSKFLTFLIR PYDSFTARLK
DLASEDSPQP ASIRVLVDGP YGHSQPLHLF DHVLFVVGGS GVVVPMSYLK VLTGRNKQTT
STHIHWAIRE PEFAAEVLSN DMAEALGDAS FAIDLYFSAE TERNIGANMP PKASRHYRRP
NAAAIILAAA EDAGERTLAV VACGPAKMAD DARRAVTEAL DIFPCQMEYF EESFRW
//
