ID A0A0L1JCK3_ASPNO Unreviewed; 1168 AA.
AC A0A0L1JCK3;
DT 11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT 11-NOV-2015, sequence version 1.
DT 27-MAR-2024, entry version 25.
DE RecName: Full=DUF221 domain protein {ECO:0008006|Google:ProtNLM};
GN ORFNames=ANOM_002241 {ECO:0000313|EMBL:KNG89489.1};
OS Aspergillus nomiae NRRL 13137.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
OX NCBI_TaxID=1509407 {ECO:0000313|EMBL:KNG89489.1, ECO:0000313|Proteomes:UP000037505};
RN [1] {ECO:0000313|EMBL:KNG89489.1, ECO:0000313|Proteomes:UP000037505}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NRRL 13137 {ECO:0000313|EMBL:KNG89489.1,
RC ECO:0000313|Proteomes:UP000037505};
RA Moore M.G., Shannon B.M., Brian M.M.;
RT "The Genome of the Aflatoxigenic Filamentous Fungus Aspergillus nomius.";
RL Submitted (JUN-2014) to the EMBL/GenBank/DDBJ databases.
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:KNG89489.1}.
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DR EMBL; JNOM01000030; KNG89489.1; -; Genomic_DNA.
DR RefSeq; XP_015410412.1; XM_015547498.1.
DR AlphaFoldDB; A0A0L1JCK3; -.
DR GeneID; 26804045; -.
DR OrthoDB; 54187at2759; -.
DR Proteomes; UP000037505; 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:UP000037505};
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 27..48
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 108..127
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 168..187
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 629..654
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 674..699
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 720..748
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 768..796
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 842..860
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 881..901
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 913..932
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 27..189
FT /note="CSC1/OSCA1-like N-terminal transmembrane"
FT /evidence="ECO:0000259|Pfam:PF13967"
FT DOMAIN 213..287
FT /note="CSC1/OSCA1-like cytosolic"
FT /evidence="ECO:0000259|Pfam:PF14703"
FT DOMAIN 539..616
FT /note="CSC1/OSCA1-like cytosolic"
FT /evidence="ECO:0000259|Pfam:PF14703"
FT DOMAIN 627..899
FT /note="CSC1/OSCA1-like 7TM region"
FT /evidence="ECO:0000259|Pfam:PF02714"
FT DOMAIN 1087..1159
FT /note="10TM putative phosphate transporter extracellular
FT tail"
FT /evidence="ECO:0000259|Pfam:PF12621"
FT REGION 290..310
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 390..511
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1012..1047
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 412..426
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 427..443
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 464..511
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1019..1047
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1168 AA; 131649 MW; FEF7FA308D4357B5 CRC64;
MAQDLGSALE HAGGTGQKSA GIPINTFLAS LATAIVIFAV QFLLFLLLKS KLTRIYQPRT
YLVPDRERTE PSPPGLFRWV VPVFRTSSTE FIQKCGLDAY FFLRYLRMLL KIFVPLGCII
LPVLLPLNKA GGKDQHYKNG TESGNTWNVT GLDQLAWGNV TPENTSRYWG HLIMAIITIV
YVCAVFYDEL RNYIRLRQAY LTSPQHRLRA SATTVLVTAI PERWLTVDAL ASLFDVFPGG
VRNIWINRNF DDLNEKVKLR DALALKLEAA ETDLVIKCKK AQLKQAKAEA KKSGVKARKT
AKEEQRDTDR KASLMAMDAG ISSGDPHQAH TLAEVLHHDG SQDQTEPGKR RRLNPFDPAM
EAAGAVGHGV GKLGKSVLEG FKKVEGGIDG KLARSGGFVP DSSVAPQDGS RSSEHRQSES
DSMDVADRSQ ARTNATDSGV TGATGSKPKR PFWKATGSSN SKLSHRSEPD EFPLTQRESI
SIDEERKDAP TEKEKNNRDK RRTRTEGEQL EGEEYPVAYN EDFDNEDFGE PLWKNISDQR
TVDTVDYCRK EVARLNLEIE VDQQTPEKFP LMNSAFIQFN HQVAAHMACQ AVSHHVPKQM
APRIVEISPD DVIWDNMSIR WWERYLRTFG ILTIVCAMVV GWAFPVAFTG LLSQLSYLEE
AFTWLRWISK LPEWFISAVQ GILPALFLAI LMAVLPLILR FLCRTQGIHT GMAVELTVQN
YYFAFLFVQL FLVVAISSSF STIISNVANV TSWPQLLAEN IPLSSNYFFS YMILQAMSVS
AGALVQVVNL ASWFILGPLL DTTARTKWAR TTNLNQMQWG TFFPVYTTLA SIGLIYCVIS
PLILVFNVIT FGLFWFVYRY NTLYVTKFRF DTGGLLFPKA INQLFTGIYF MELCLIGLFF
LVRDVQGTVA CKGQAICMIV VLVLTVGYQI LLNEAFGPLI RYLPITLEDE AVRRDEEFER
AQRARLGLLQ DDELNADRGQ LSDHEEHRGP QTDQATHDIE LKDIEASMEL RTEFQDRRPS
LGPTRQSWAD RSSRSRSKYF GANSDSSVPT VQRIREKVVA DAEAQGPPTN QVAPALFAGI
HDELEDLTPE ERDQLVQRAF QHDALRAKRP VIWIPRDDLG VSDDEVYRTQ RFSKHIWISN
EYQALDGKCR TVFSRSPPDF SEVDLIQL
//
