ID A0A165QLM9_9APHY Unreviewed; 937 AA.
AC A0A165QLM9;
DT 06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT 06-JUL-2016, sequence version 1.
DT 27-MAR-2024, entry version 17.
DE SubName: Full=DUF221-domain-containing protein {ECO:0000313|EMBL:KZT69635.1};
GN ORFNames=DAEQUDRAFT_690409 {ECO:0000313|EMBL:KZT69635.1};
OS Daedalea quercina L-15889.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Polyporales; Daedalea.
OX NCBI_TaxID=1314783 {ECO:0000313|EMBL:KZT69635.1, ECO:0000313|Proteomes:UP000076727};
RN [1] {ECO:0000313|EMBL:KZT69635.1, ECO:0000313|Proteomes:UP000076727}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=L-15889 {ECO:0000313|EMBL:KZT69635.1,
RC ECO:0000313|Proteomes:UP000076727};
RX PubMed=26659563; DOI=10.1093/molbev/msv337;
RA Nagy L.G., Riley R., Tritt A., Adam C., Daum C., Floudas D., Sun H.,
RA Yadav J.S., Pangilinan J., Larsson K.H., Matsuura K., Barry K., Labutti K.,
RA Kuo R., Ohm R.A., Bhattacharya S.S., Shirouzu T., Yoshinaga Y.,
RA Martin F.M., Grigoriev I.V., Hibbett D.S.;
RT "Comparative Genomics of Early-Diverging Mushroom-Forming Fungi Provides
RT Insights into the Origins of Lignocellulose Decay Capabilities.";
RL Mol. Biol. Evol. 33:959-970(2016).
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; KV429056; KZT69635.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A165QLM9; -.
DR STRING; 1314783.A0A165QLM9; -.
DR OrthoDB; 1330110at2759; -.
DR Proteomes; UP000076727; 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:UP000076727};
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 24..45
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 108..130
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 154..174
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 377..401
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 421..443
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 464..486
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 533..553
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 574..593
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 599..617
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 637..658
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 664..684
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 24..174
FT /note="CSC1/OSCA1-like N-terminal transmembrane"
FT /evidence="ECO:0000259|Pfam:PF13967"
FT DOMAIN 198..361
FT /note="CSC1/OSCA1-like cytosolic"
FT /evidence="ECO:0000259|Pfam:PF14703"
FT DOMAIN 373..655
FT /note="CSC1/OSCA1-like 7TM region"
FT /evidence="ECO:0000259|Pfam:PF02714"
FT REGION 813..834
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 892..937
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 937 AA; 105949 MW; E95C490D659F2357 CRC64;
MATNITQEII NEDASQRTLA PVAVGSQVAL MSVVSLATII IFNVLRPRNK IVYEPKVKYH
VGDKQPPRIS DSMFGWLPPV LHTKEPVLVE KIGLDAAIFL RFLRMLRWMF TTIVFICGAV
LIPVDIAYNI QNVPSKSRDV LSILTIRDVS GWRLWIHVAV MYTITGVVLA FVWFHWREVV
RLRREWFRSP EYMRSFYART LMVTQVPKKL QSDEGIRAIF QSVQVPYPTT SVHIGRKVGQ
LPELIEYHNN TVREFEAVLV QYLKDGKLAK ERPQKRLGGF LCFGGQKVDA INYYMAKLKR
TEEAVERSRD QFDQRQAESY GFASMAAVPY AHIVANMLRD KHPKGTTVTL APNPKDIVWT
NLNKSTAEIA RNRTIGWAFL VFVCFVNTIP LLVISVLANL ASLTAYVPFL ESWSVNSPGT
FAVVSGVLPP AVSAIFGYAL PIVMRWLTKY MGASTHSRLD RSVVARYFAF LVISQLIIFT
LIGVLFNSVT QIVEQIGEHK SFKEIIEDLH NLPGLITRTY IDQASYWLTY FPLRGFLCIF
DLAQILNLVV IFIKKNLFGR TPREIREWTQ PPEFRFAIYY PNLLLMATIG LFFAPIAPLV
AVASMVVFWI SSWVYKYQLM FVFVSQVETG GRLWNVVINR LLVGVVLMHL IMTLTIGFQF
TFGSFKWIAV IPPIFGVIGF KIYLTRTFLP AFQYYIPTDE ELQQAAVHSK RSDNLNNKLE
KRFGHPALHQ DLFTPMVHAN MTHLLPEVFD GKIGSTKTAL DDFGGTKVDA AVVGGVRIAG
IEEQDLEYDP TLYQRDRGEL DWDQRSVSSA TLIGDNGSTA HLNPAGRAAS PAPSRMTGYD
RYLASGPQPE IEMARLDYDQ QPLLHAAQAP GYYEAEMANR SMASFSQYGG SPYGTPQMEY
TPPMPPMAAS YDSHTDQGLR QAPVYRPAPQ HSNSWQS
//
