ID A0A2J6TGY5_9HELO Unreviewed; 1021 AA.
AC A0A2J6TGY5;
DT 28-MAR-2018, integrated into UniProtKB/TrEMBL.
DT 28-MAR-2018, sequence version 1.
DT 27-MAR-2024, entry version 20.
DE SubName: Full=DUF221-domain-containing protein {ECO:0000313|EMBL:PMD62280.1};
GN ORFNames=K444DRAFT_585382 {ECO:0000313|EMBL:PMD62280.1};
OS Hyaloscypha bicolor E.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC Helotiales; Hyaloscyphaceae; Hyaloscypha; Hyaloscypha bicolor.
OX NCBI_TaxID=1095630 {ECO:0000313|EMBL:PMD62280.1, ECO:0000313|Proteomes:UP000235371};
RN [1] {ECO:0000313|EMBL:PMD62280.1, ECO:0000313|Proteomes:UP000235371}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=E {ECO:0000313|EMBL:PMD62280.1,
RC ECO:0000313|Proteomes:UP000235371};
RG DOE Joint Genome Institute;
RA Martino E., Morin E., Grelet G., Kuo A., Kohler A., Daghino S., Barry K.,
RA Choi C., Cichocki N., Clum A., Copeland A., Hainaut M., Haridas S.,
RA Labutti K., Lindquist E., Lipzen A., Khouja H.-R., Murat C., Ohm R.,
RA Olson A., Spatafora J., Veneault-Fourrey C., Henrissat B., Grigoriev I.,
RA Martin F., Perotto S.;
RT "A degradative enzymes factory behind the ericoid mycorrhizal symbiosis.";
RL Submitted (APR-2016) 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}.
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DR EMBL; KZ613783; PMD62280.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2J6TGY5; -.
DR InParanoid; A0A2J6TGY5; -.
DR OrthoDB; 54187at2759; -.
DR Proteomes; UP000235371; 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; 1.
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:UP000235371};
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 30..55
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 107..131
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 170..189
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 466..493
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 513..540
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 560..584
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 608..626
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 664..697
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 717..742
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 749..771
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 30..191
FT /note="CSC1/OSCA1-like N-terminal transmembrane"
FT /evidence="ECO:0000259|Pfam:PF13967"
FT DOMAIN 215..453
FT /note="CSC1/OSCA1-like cytosolic"
FT /evidence="ECO:0000259|Pfam:PF14703"
FT DOMAIN 468..739
FT /note="CSC1/OSCA1-like 7TM region"
FT /evidence="ECO:0000259|Pfam:PF02714"
FT DOMAIN 940..1017
FT /note="10TM putative phosphate transporter extracellular
FT tail"
FT /evidence="ECO:0000259|Pfam:PF12621"
FT REGION 802..826
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 860..879
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1021 AA; 115658 MW; 4CF22C72756D3AB0 CRC64;
MSGISSFIDG TINGAAGLAQ GREGTTITTF VISLAAGFIL FAVQFGTFVV IRNYLWAKRI
YQPRSFLVPV KQRIESPYNN PFKWLFTVFK IKEDPVVLGK AGMDAYFFLR FLSMCLKIFT
PMAIIIMPIL IPLNVKQGKG TNTISGVTYN ITGLDTLAWS NASPAKTSRY WAHLVMAVGV
VVWVCLMFHQ ELSHYIAKRE DFLNSLGHRL KASSTTVLIQ DIPEKLCNEE ALEELYGDFP
GGIRRIWINR DFTTLVNKDK LRKFYENLLE NTETNLLRKV ARQSHKARLR QRGESTQEAP
EQITPEVRSK VGQTLFPARP EMGPATPAAC VRDLEYDLET KAAWANFLTP KQRQTMRIPK
DRHAAAARIP LIGRLFSTKV DTIYYCRREL ARLNKEIEMD TKTPDAYPKN LSAFVQFNSQ
KAAHLTCQSV ADTSPRHMRR RMVEISPGDI NWPSLNLSWR ARYVRLVVFL VLFTILLFVF
GLISFFTGIL SRISTLSGST SWLKWIDSLP PWLISFIQGT LPPVIQVILL SGPLPILLRL
LTNRARGATT GQEGERSLQL LYFIFLIVEL FIIPTISSGL TSIVEELIRT PTSVPNILAT
NLPTAANYYF SFLILQALSL SATSILQTIR LFKFYVIGHV NTPDSVFEKL SWTNLTRTGS
NIPWYTTFAV IGLVYSTIAP LILLFMLITF SLFWVVIKNN LLYCVRTGTV DGGGLFFPSA
INQLFTGVYF MEVCLIGLFF LVRDTQGHVA CAAQGIIMAV VLVLTILYQI WLMHHLDPLF
KYAPVRLEVE SKALLADYQG ERETGSNLTN HETSETVNSE PRDEAKDRLD LSGNIASHAQ
NIEKAHAPKL STQYRPPFWE RQSSHRSQDL QAQQREDAKS AEGILARLNR PLDEARLAHL
EKKLAKTEAV RGSALLPRRK DIEAQMLDDP ISKIIMQHND ELENLDPEER DMLISVAFMH
PVLRETRPSV WIPTDELGVS DDEVRRTREL SEDVVIDNRG AYFDRRLKVQ VDKPPPDMSE
F
//
