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Database: UniProt
Entry: A0A150VAE6_9PEZI
LinkDB: A0A150VAE6_9PEZI
Original site: A0A150VAE6_9PEZI 
ID   A0A150VAE6_9PEZI        Unreviewed;       823 AA.
AC   A0A150VAE6;
DT   08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT   08-JUN-2016, sequence version 1.
DT   27-MAR-2024, entry version 21.
DE   RecName: Full=Potassium channel domain-containing protein {ECO:0000259|Pfam:PF07885};
GN   ORFNames=M433DRAFT_141930 {ECO:0000313|EMBL:KYG47487.1};
OS   Acidomyces richmondensis BFW.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC   Dothideomycetidae; Mycosphaerellales; Teratosphaeriaceae; Acidomyces.
OX   NCBI_TaxID=766039 {ECO:0000313|EMBL:KYG47487.1, ECO:0000313|Proteomes:UP000075602};
RN   [1] {ECO:0000313|EMBL:KYG47487.1, ECO:0000313|Proteomes:UP000075602}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BFW {ECO:0000313|EMBL:KYG47487.1,
RC   ECO:0000313|Proteomes:UP000075602};
RX   PubMed=26973616; DOI=10.3389/fmicb.2016.00238;
RA   Mosier A.C., Miller C.S., Frischkorn K.R., Ohm R.A., Li Z., LaButti K.,
RA   Lapidus A., Lipzen A., Chen C., Johnson J., Lindquist E.A., Pan C.,
RA   Hettich R.L., Grigoriev I.V., Singer S.W., Banfield J.F.;
RT   "Fungi Contribute Critical but Spatially Varying Roles in Nitrogen and
RT   Carbon Cycling in Acid Mine Drainage.";
RL   Front. Microbiol. 7:238-238(2016).
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC       pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
CC   -!- SIMILARITY: Belongs to the two pore domain potassium channel (TC
CC       1.A.1.8) family. {ECO:0000256|RuleBase:RU003857}.
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:KYG47487.1}.
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DR   EMBL; JPDO01000076; KYG47487.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A150VAE6; -.
DR   STRING; 766039.A0A150VAE6; -.
DR   Proteomes; UP000075602; Unassembled WGS sequence.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005267; F:potassium channel activity; IEA:InterPro.
DR   Gene3D; 1.10.287.70; -; 2.
DR   InterPro; IPR003280; 2pore_dom_K_chnl.
DR   InterPro; IPR013099; K_chnl_dom.
DR   PANTHER; PTHR11003:SF291; POTASSIUM CHANNEL SUBFAMILY K MEMBER 18; 1.
DR   PANTHER; PTHR11003; POTASSIUM CHANNEL, SUBFAMILY K; 1.
DR   Pfam; PF07885; Ion_trans_2; 2.
DR   PRINTS; PR01333; 2POREKCHANEL.
DR   SUPFAM; SSF81324; Voltage-gated potassium channels; 2.
PE   3: Inferred from homology;
KW   Coiled coil {ECO:0000256|SAM:Coils};
KW   Ion channel {ECO:0000256|RuleBase:RU003857};
KW   Ion transport {ECO:0000256|RuleBase:RU003857};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW   Reference proteome {ECO:0000313|Proteomes:UP000075602};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692,
KW   ECO:0000256|RuleBase:RU003857};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW   ECO:0000256|SAM:Phobius};
KW   Transport {ECO:0000256|ARBA:ARBA00022448, ECO:0000256|RuleBase:RU003857}.
FT   TRANSMEM        47..80
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        100..121
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        133..155
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        175..198
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        218..239
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        273..296
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        368..393
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        399..417
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        429..450
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          224..296
FT                   /note="Potassium channel"
FT                   /evidence="ECO:0000259|Pfam:PF07885"
FT   DOMAIN          380..454
FT                   /note="Potassium channel"
FT                   /evidence="ECO:0000259|Pfam:PF07885"
FT   REGION          1..41
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          629..663
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          696..719
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          762..823
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          529..561
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COMPBIAS        11..28
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        647..662
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        698..714
FT                   /note="Basic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        762..788
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        801..823
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   823 AA;  92469 MW;  2F84EA010D1DF4E9 CRC64;
     MSTIDPGMEE TVEQKANDLE SNLYEKDDAA EEREEESEED LREPSRWWFA STLCPLLAGT
     FGPIANGFSI CALAYVWRVY IPTGGTEEHG VPIPDPAWEL AINAISLLCA LAGNASLLLN
     MTKRLKFSIA QPITIAGFLL AGVLLIADVA AINASPTYYL TGKNAPDAHH ALSSAYYYAI
     FAAAFYMIIG GLMCLTVYGA NQGLYDKQFH LTPSQRTLMI QTMMFIVYLL LGSLVFSHIE
     GWQYLNAVYW ADVTILTVGF GDYTPTTTLA RALLFPFAIG GILILGLVIG SIRSLVLERG
     REKMAARIVE KRRKSAIQNV DERKQTIKIG WLASADFSTD PSLSPAQRRE EEFNVMRKVQ
     DIADRERGWF SLGVSVLFAL LLWLLGAFVF MHTEYTQQWT YFESVYFAYV ALLTIGYGDF
     HPDSNSGRAF FVVWSLLAVP SLTILISNMG DTIVKYFSDF SIWIGSITVL PGDKGFRATA
     EGVLERISNL VSAGAKGFTA PGLLGDAPNG HRIQHAQRMS ADEHEKRMMD QLAERLTSHL
     ENEELAEAKS AEQQGDELQR DIHFYHYVLA RELRNIQKDL NANPPKKYTW PEWEYYLKLM
     GNEDDPKDYP GQRHPDIMVP DELRIASSSG SEATVGVNGE VSKGVDKNSG ANKDDNLDSD
     AEPMRRQSTL YETPYEFPAQ SDGVVDRQTE VKEWKRLHES HKKLRPHPDR KSQRKSRRQL
     TSMDLLDWSW LSAKSPLLCM QSESEWILER LSAALERELN RQRKGYKRKP PISMSDIKRR
     KAEKQKNPTH SGTEGGGTDQ GKATNEREGK EEEGFEKAAR SAM
//
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