ID A0A165R7A9_9APHY Unreviewed; 993 AA.
AC A0A165R7A9;
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=Voltage-gated potassium channel {ECO:0000313|EMBL:KZT70402.1};
GN ORFNames=DAEQUDRAFT_203974 {ECO:0000313|EMBL:KZT70402.1};
OS Daedalea quercina L-15889.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Polyporales; Daedalea.
OX NCBI_TaxID=1314783 {ECO:0000313|EMBL:KZT70402.1, ECO:0000313|Proteomes:UP000076727};
RN [1] {ECO:0000313|EMBL:KZT70402.1, ECO:0000313|Proteomes:UP000076727}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=L-15889 {ECO:0000313|EMBL:KZT70402.1,
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 two pore domain potassium channel (TC
CC 1.A.1.8) family. {ECO:0000256|RuleBase:RU003857}.
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DR EMBL; KV429051; KZT70402.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A165R7A9; -.
DR STRING; 1314783.A0A165R7A9; -.
DR OrthoDB; 5010334at2759; -.
DR Proteomes; UP000076727; 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 Ion channel {ECO:0000256|RuleBase:RU003857, ECO:0000313|EMBL:KZT70402.1};
KW Ion transport {ECO:0000256|RuleBase:RU003857};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000076727};
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 130..148
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 168..190
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 202..225
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 237..257
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 278..301
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 331..353
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 640..661
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 667..686
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 698..717
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 284..356
FT /note="Potassium channel"
FT /evidence="ECO:0000259|Pfam:PF07885"
FT DOMAIN 650..720
FT /note="Potassium channel"
FT /evidence="ECO:0000259|Pfam:PF07885"
FT REGION 22..60
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 913..993
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 917..938
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 942..964
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 993 AA; 110986 MW; 17E92D78F25C20B3 CRC64;
MGFGFLINVV LALTGRGRND FARDLEKQGH PPAGEHQGYS SPQEVTSSDD EGDHLHSPSL
MSHPLRQFAT VDSTFSGLRT PLRPSRTLTW SSTTEPHRPT LVSRLSSFFF PSPQPGETAR
YTPYYRYSPI ISGVVIPFSI LLEIPGLTER WYIQTEANQT VDTKPNPVLL DVGLGISMAC
AVFANVCLIL RFSEKWIKLT TLLCIFFLTS HDAINIACVT TFGVIHRVND GFTYGQSFWM
TLCSTIASTI TNLSLIIDYI RTRNFAHSGS GLTRKQRSLV ILVIILLMYI ALGALINSVL
LHLSYINGLY FTVVSIETIG FGDIVARDTG ARVWVCIYNV FGVITLGIVI SLCRDTVLEG
LEIGYRKRLR QLRARRHEAR RFRRWQTRWR RAIEWRLRQQ GSPVWVSDNQ RAEEQGVRFV
GLGGSTAGAG QVSWLARFVH LRRPPPEDPT RRQTKHVVGH PFGKHLNISA LSDEQLHAAA
LEAGVPLNTF VDFSPAHRVE RDAREQPHPA GGIFAGDGWP AHAATPTDAQ LGRMALMHTR
MALAISGREI YAPTPSLEHR EEVISSIIED QDAQHEAAQE QREIRMANRH RRAKEQVGHR
RGKFIAAPRW LRKYASGALS AQPYAKLKKE MADDERNANL VKLGIAWSVF FAFWFVGSAV
FSATEGWTYG IAMYFCFICF LTTGYGDYAP ATPAGRSIFV VWALFGVATM TILVAVVEDA
CSEKYRSAMH SQVFDRAVRK YRRNSADEAA EVPQAKYQLQ RVGVDRMRNV DAIRKGEINI
EPEEQSMANV QAQLEEAGQK AHKELEALPH EIIRQARTFQ DYMQFFAKGG GHDDGEHDPN
NVPRSLRQLL DEIVADENVD ERVRQEILAD DDAKHTLFIL SIERALKKMI HSADNALQAC
AERDTIMAIQ TEQRAKAPGG NKERVAKEAE HIGEDSAPAD DVDESSSSSL PSSRTESNSS
PARQACLRRL ACPRARALPP PDLQTTTIAL AEQ
//
