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Database: UniProt
Entry: M3A2J5_PSEFD
LinkDB: M3A2J5_PSEFD
Original site: M3A2J5_PSEFD 
ID   M3A2J5_PSEFD            Unreviewed;      1181 AA.
AC   M3A2J5;
DT   01-MAY-2013, integrated into UniProtKB/TrEMBL.
DT   01-MAY-2013, sequence version 1.
DT   27-MAR-2024, entry version 42.
DE   RecName: Full=DUF221-domain-containing protein {ECO:0008006|Google:ProtNLM};
DE   Flags: Fragment;
GN   ORFNames=MYCFIDRAFT_114224 {ECO:0000313|EMBL:EME85399.1};
OS   Pseudocercospora fijiensis (strain CIRAD86) (Black leaf streak disease
OS   fungus) (Mycosphaerella fijiensis).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC   Dothideomycetidae; Mycosphaerellales; Mycosphaerellaceae; Pseudocercospora.
OX   NCBI_TaxID=383855 {ECO:0000313|EMBL:EME85399.1, ECO:0000313|Proteomes:UP000016932};
RN   [1] {ECO:0000313|EMBL:EME85399.1, ECO:0000313|Proteomes:UP000016932}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CIRAD86 {ECO:0000313|EMBL:EME85399.1,
RC   ECO:0000313|Proteomes:UP000016932};
RX   PubMed=23236275; DOI=10.1371/journal.ppat.1003037;
RA   Ohm R.A., Feau N., Henrissat B., Schoch C.L., Horwitz B.A., Barry K.W.,
RA   Condon B.J., Copeland A.C., Dhillon B., Glaser F., Hesse C.N., Kosti I.,
RA   LaButti K., Lindquist E.A., Lucas S., Salamov A.A., Bradshaw R.E.,
RA   Ciuffetti L., Hamelin R.C., Kema G.H.J., Lawrence C., Scott J.A.,
RA   Spatafora J.W., Turgeon B.G., de Wit P.J.G.M., Zhong S., Goodwin S.B.,
RA   Grigoriev I.V.;
RT   "Diverse lifestyles and strategies of plant pathogenesis encoded in the
RT   genomes of eighteen Dothideomycetes fungi.";
RL   PLoS Pathog. 8:E1003037-E1003037(2012).
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}.
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DR   EMBL; KB446556; EME85399.1; -; Genomic_DNA.
DR   RefSeq; XP_007923021.1; XM_007924830.1.
DR   AlphaFoldDB; M3A2J5; -.
DR   GeneID; 19330246; -.
DR   KEGG; pfj:MYCFIDRAFT_114224; -.
DR   eggNOG; KOG1134; Eukaryota.
DR   HOGENOM; CLU_002458_2_0_1; -.
DR   OrthoDB; 54187at2759; -.
DR   Proteomes; UP000016932; 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   InterPro; IPR022257; PHM7_ext.
DR   PANTHER; PTHR13018; PROBABLE MEMBRANE PROTEIN DUF221-RELATED; 1.
DR   PANTHER; PTHR13018:SF20; SPORULATION-SPECIFIC PROTEIN 75; 1.
DR   Pfam; PF14703; PHM7_cyt; 2.
DR   Pfam; PF12621; PHM7_ext; 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:UP000016932};
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        16..37
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        97..116
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        143..162
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        637..659
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        681..706
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        727..755
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        775..804
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        824..844
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        850..871
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        883..907
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        919..938
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          16..164
FT                   /note="CSC1/OSCA1-like N-terminal transmembrane"
FT                   /evidence="ECO:0000259|Pfam:PF13967"
FT   DOMAIN          188..266
FT                   /note="CSC1/OSCA1-like cytosolic"
FT                   /evidence="ECO:0000259|Pfam:PF14703"
FT   DOMAIN          514..623
FT                   /note="CSC1/OSCA1-like cytosolic"
FT                   /evidence="ECO:0000259|Pfam:PF14703"
FT   DOMAIN          637..907
FT                   /note="CSC1/OSCA1-like 7TM region"
FT                   /evidence="ECO:0000259|Pfam:PF02714"
FT   DOMAIN          1085..1172
FT                   /note="10TM putative phosphate transporter extracellular
FT                   tail"
FT                   /evidence="ECO:0000259|Pfam:PF12621"
FT   REGION          260..336
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          402..507
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1012..1050
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        260..290
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        304..331
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        447..477
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        485..507
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1016..1038
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   NON_TER         1
FT                   /evidence="ECO:0000313|EMBL:EME85399.1"
FT   NON_TER         1181
FT                   /evidence="ECO:0000313|EMBL:EME85399.1"
SQ   SEQUENCE   1181 AA;  133989 MW;  DA18471110BDAF08 CRC64;
     GSGQASQREG QTVNTLAASL VSAFASLGIQ VLVFMLLRLR LSRIYRPKSY LVPERERVAA
     PPGGLVGWLY PLFTTTNLGL IQKCGLDAYF FLRFLRMLLK IFFPATLLAL PILLPVNHNG
     GGTAKGLDKY SISNIAPKNS DRLWAHLFLG IIFILWTFYV VFKELRGYIR VRQAFLTSPQ
     HRIRASATTV LVTGIPRKWL TMEALSGLYD VFPGGIRNIW INRNFDDLND KVKYRDKIAR
     NLEDAETVLI KNCRKKHIEA EQKKAKEDGK KKSKKEKLQD EAEEDAAAER MAQSEGVSAG
     ENHELSQDLK DTLKEEEQHQ ADSDKRRRNP LGLVGDSVNA VGHGFKDVGK GISKFGDRVV
     GGVDNGFHKA GDDLNIATRR ANAGGGFSLD DDLTLDVRDV HTTRPAGDTR PKSSLQIEEP
     AHHKGNRKSW NIFKNNDESL AMHSPQPHTA EDDDEFPLHG DAEQKEPEAK DKQKSKSFMQ
     KLAFWKKNND EEDEDKDEYP NAIDKKWDED QDEEPYWRRY LEPKDRETIR LPLFCPTWFP
     SIPLIGKKVD RIYHLRRELA RLNLEIEEDQ KDIEKFPYMN SAFIQFNHQV AAHMCCQSLS
     HHIPQHMAPR LVEISPEDVI WDNMSVKWWE RYLRTGLILL ISAGLILLFA IPVAFTSLLN
     KVSQLASYIS WLEWLTTLPD VVISIIQGVL PPVLLSLILL LVPIIFRLLI KQQGVPTGND
     RERGVQSWYF AFLFIQVFLV VTISGGLIAI FQALADNPTS IVTEVASNIP TASNYFFSYL
     TVQALSNSAS ALLQLGSLFG WFILAPILDS TARQKWTRQT SLQYVTWGTF FPPFTNFAVI
     GIIYSIVSPL ILVFMIFIFA LFWIVYRYNV LFVYQFKHDT GGLLFPVAIN QLFTGIYFLE
     IAMIGYFFTL QYKGEVVCLP QAIIMIVMLV LTVVFQWLTN MSFKPLFQYL PITLEDEAVI
     RDEQFAKAQE SKFAPLNESG NDERDVQDML EDREHAEEDA DRAAIDEEKR AIAQRRSHTP
     GSTHSPDARR TSGSAHSARP GSHWAKKSEA KPVWGTELWK KAAPEAKTDA EAQHTVGDVL
     FSGYADELED LTPDERDLLV RYAFQHSALR ARRPVVWIPR DQLGVSDDEI KRAKKMSTVS
     IDGQNRTNIW MSNEGTALDG KGRVVFRRSP PDFSNVDLIA L
//
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