ID A0A395M989_9HYPO Unreviewed; 1015 AA.
AC A0A395M989;
DT 05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT 05-DEC-2018, sequence version 1.
DT 27-MAR-2024, entry version 22.
DE RecName: Full=Duf221 domain protein {ECO:0008006|Google:ProtNLM};
GN ORFNames=FIE12Z_11294 {ECO:0000313|EMBL:RFN44435.1};
OS Fusarium flagelliforme.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Nectriaceae; Fusarium;
OC Fusarium incarnatum-equiseti species complex.
OX NCBI_TaxID=2675880 {ECO:0000313|EMBL:RFN44435.1, ECO:0000313|Proteomes:UP000265631};
RN [1] {ECO:0000313|EMBL:RFN44435.1, ECO:0000313|Proteomes:UP000265631}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NRRL 13405 {ECO:0000313|EMBL:RFN44435.1,
RC ECO:0000313|Proteomes:UP000265631};
RX PubMed=29649280; DOI=10.1371/journal.ppat.1006946;
RA Proctor R.H., McCormick S.P., Kim H.S., Cardoza R.E., Stanley A.M.,
RA Lindo L., Kelly A., Brown D.W., Lee T., Vaughan M.M., Alexander N.J.,
RA Busman M., Gutierrez S.;
RT "Evolution of structural diversity of trichothecenes, a family of toxins
RT produced by plant pathogenic and entomopathogenic fungi.";
RL PLoS Pathog. 14:e1006946-e1006946(2018).
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
CC -!- SIMILARITY: Belongs to the CSC1 (TC 1.A.17) family.
CC {ECO:0000256|ARBA:ARBA00007779}.
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:RFN44435.1}.
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; PXXK01000430; RFN44435.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A395M989; -.
DR Proteomes; UP000265631; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005227; F:calcium-activated cation channel activity; IEA:InterPro.
DR InterPro; IPR045122; Csc1-like.
DR InterPro; IPR003864; CSC1/OSCA1-like_7TM.
DR InterPro; IPR027815; CSC1/OSCA1-like_cyt.
DR InterPro; IPR032880; Csc1/OSCA1-like_N.
DR PANTHER; PTHR13018:SF154; DOMAIN PROTEIN, PUTATIVE (AFU_ORTHOLOGUE AFUA_3G11660)-RELATED; 1.
DR PANTHER; PTHR13018; PROBABLE MEMBRANE PROTEIN DUF221-RELATED; 1.
DR Pfam; PF14703; PHM7_cyt; 1.
DR Pfam; PF02714; RSN1_7TM; 1.
DR Pfam; PF13967; RSN1_TM; 1.
PE 3: Inferred from homology;
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000265631};
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:ARBA00022448}.
FT TRANSMEM 33..54
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 118..136
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 163..185
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 394..416
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 436..460
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 481..505
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 600..627
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 658..677
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 683..702
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 33..183
FT /note="CSC1/OSCA1-like N-terminal transmembrane"
FT /evidence="ECO:0000259|Pfam:PF13967"
FT DOMAIN 207..376
FT /note="CSC1/OSCA1-like cytosolic"
FT /evidence="ECO:0000259|Pfam:PF14703"
FT DOMAIN 387..672
FT /note="CSC1/OSCA1-like 7TM region"
FT /evidence="ECO:0000259|Pfam:PF02714"
FT REGION 835..877
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 898..1015
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 898..970
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1015 AA; 113774 MW; B9141BF0BDB1DB55 CRC64;
MDHLHGRNPQ NAGEQLLELL QRPFSGQLAA ASLYSALATS LPITIGIAIV FSILRPYHQA
IYAPKLKHAD EKHVPPPIGK APWSWITTLW RTNEDMLVPL IGMDATVFLR FVRMCRNMFL
TLCVTGIGIL LPVNIAKWNE YKGEKNTNWV IGITPLNTYA PAIWSQVVIA WCFNFIIMGF
LWFNYRKVLQ LRRKYFETED YQKSLHSRTL MVFDIPKKGC SDEGIARIID QIAPNSSFAR
TAVARNVKEL PALIEQHDHA VRKLEKILAK YLKDPSNVPV ARPMCRPSKK DRSYGTYPKG
QKVDAIEYYT QRIRDLEVHI KEVRASVDKR GSMPYGFASY ADIAEAHGIA YACRKKKPVG
ATVRLAPRPN DIIWENMPLY SSTRGRRRWV NNMWITVLTF LWIVPNLGIA IFLVNLQNLG
SVWPAFMTEL AAHPKIWGAI QGIAAPAIMS LTYLVLPMIF RRLSVKAGDQ TKTGRERHVL
AKLYFFFVFN NLIIFSIFSV IWQFVASVVA DTTGAKKEDV WESIKNNNIA AGLFEALCNN
SVFWVTYLLQ RQLGAAIDLA QAWPLVQAFF LKKFSSPTPR ELIELTAPPP FEYASYYNYF
LYYATVTMCF AGIQPLVLPA TALYFLIDSW LKKYLLLYRF VTKTESGGMF WRVIFNRFIF
ATILSNLVVM LTCWVRGNFG THIEFFCVVP LPFIMIIFKI YCNYAFNDKI TYYNTQDVTK
SPENGVDPKE NRMRSERLAN RFGHPALYRP LITPMVHSKA QNLLPAIYKG RLSDGRDVDS
GDMMTVSGYS DMVMLDPMQG GKPGKAANSF PGFEFVNDTQ MDFEYYKNRA EFAENHGGGE
IYGRPGEIGR PGTPGSMDGS DFSRPGTPVG RTGSPAAFAG GAAQQQRLMS LASNVSGDTS
YQSYRPGGNA GFTQQTTLGQ EPPARGRSPL YSQNNGSSSG LGLIQNAAAP AYSSNLSTPG
RMTPVQSPGP SVSAMGGGPQ GYSGLAQHAP EAEPSYDYFR GNNNNRPRRN PGEGW
//
