ID A0A166QWB5_9AGAM Unreviewed; 1005 AA.
AC A0A166QWB5;
DT 06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT 06-JUL-2016, sequence version 1.
DT 27-MAR-2024, entry version 21.
DE SubName: Full=DUF221-domain-containing protein {ECO:0000313|EMBL:KZP27629.1};
GN ORFNames=FIBSPDRAFT_780851 {ECO:0000313|EMBL:KZP27629.1};
OS Fibularhizoctonia sp. CBS 109695.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Agaricomycetidae; Atheliales; Atheliaceae; Fibularhizoctonia.
OX NCBI_TaxID=436010 {ECO:0000313|EMBL:KZP27629.1, ECO:0000313|Proteomes:UP000076532};
RN [1] {ECO:0000313|EMBL:KZP27629.1, ECO:0000313|Proteomes:UP000076532}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 109695 {ECO:0000313|EMBL:KZP27629.1,
RC ECO:0000313|Proteomes:UP000076532};
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; KV417508; KZP27629.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A166QWB5; -.
DR OrthoDB; 1330110at2759; -.
DR Proteomes; UP000076532; 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:UP000076532};
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 25..46
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 110..131
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 151..175
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 378..401
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 421..441
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 468..490
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 536..554
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 575..594
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 600..618
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 639..662
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 668..687
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 24..175
FT /note="CSC1/OSCA1-like N-terminal transmembrane"
FT /evidence="ECO:0000259|Pfam:PF13967"
FT DOMAIN 199..362
FT /note="CSC1/OSCA1-like cytosolic"
FT /evidence="ECO:0000259|Pfam:PF14703"
FT DOMAIN 373..656
FT /note="CSC1/OSCA1-like 7TM region"
FT /evidence="ECO:0000259|Pfam:PF02714"
FT REGION 856..875
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 887..1005
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 856..872
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 903..931
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 964..991
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1005 AA; 113051 MW; AEEDBF78348BE728 CRC64;
MAANNISSII DANIDLRKQM APKAVVSQVA LMTAISIITV IAFNVLRPSN KVIYEPKVKY
HVGEKHPPRI SDSTFGWIPP LLHTKEAELV DKIGLDAVTF LRFLKMFRSL FSSIAFALCA
VLIPINITYN LKNVDINDRD DLSILTIRDV QGYTLAAHVA MSYVITGLVM FFVYINWVQM
VRLRRAWFRS PEYAKSFYAR TLAVMQVPKK FQSDEGIRAI FETHKVPYPT TSVHINRRVG
QLPELIEFHN EAVRELERIL VRYLRGGKIA KERPTIRIGG FMGMGGRKID AIEFYTAKLK
RTEGAIEIYR DQVDARKAEN YGFASMASVP QAHTVANLLK NKHPKGTNIT LAPNPKDIIW
ENMDKTHGEL MRKRFTGFLY LAIIAFFNTV PLFIISVLAN LNALQDAVPF IKQWADNSPE
TFAVVSGVLP PAVSGFFGFF LPRVVRWLSQ YQGALTQSKL DRDVVGRYYS FLVISQLIVF
TLIGVIFNLV RNLIAETNEK ESFAEIWHKL GSLPKTINTT YIDQASYWLT YFPLRGFLVF
FDLAQILNLV WTSFKTHMFG RTPRDIREWT KPVDFEFAIY YTNILFMGTV ALVFAPLAPL
VVAAAAVVFW ISSWVYKYQL MYVCTSKVES GGRLWNVMVN RLLVAVVMMQ LLFMLTIGLQ
GIGGFKSFFW VSTAPPIFII LGFKMFLNRK FNNAFYYYVP NEQELSQAPT HSERADAKGN
RLGKRFGHPA LHMDLFTPML HTKMMALLPD VYKGRIQQDQ ARLGEYGGQK VEAQVISSGI
KFAAVDQRDL EFDPQLYARD RGEQDWDARS MASTDMLGSD TASLAPSKSV FYANGNGRSS
PAPPLPQSTV YNQYLAQGPG HRSNQSDIEL SRIGPSTDHL PLLAQQGYFD GALPPPGAPY
QQQRGSPGGS PQTQYPPAHG SPQSQYPPAR GSPQAQYPPA PADMYRSESD GYREAPIHRP
YPHARQQSNL SSLQSTPIHS RNQSQYSQIP GGGPPNMAGR GVFKG
//