ID A0A229X102_9EURO Unreviewed; 629 AA.
AC A0A229X102;
DT 25-OCT-2017, integrated into UniProtKB/TrEMBL.
DT 25-OCT-2017, sequence version 1.
DT 27-MAR-2024, entry version 21.
DE RecName: Full=Potassium channel domain-containing protein {ECO:0000259|Pfam:PF07885};
GN ORFNames=CDV55_103886 {ECO:0000313|EMBL:RHZ52146.1}, CFD26_100872
GN {ECO:0000313|EMBL:RLL94430.1};
OS Aspergillus turcosus.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
OX NCBI_TaxID=1245748 {ECO:0000313|EMBL:RHZ52146.1, ECO:0000313|Proteomes:UP000215394};
RN [1] {ECO:0000313|Proteomes:UP000215289, ECO:0000313|Proteomes:UP000215394}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HMR AF 1038 {ECO:0000313|EMBL:RLL94430.1}, and HMR AF 23
RC {ECO:0000313|EMBL:RHZ52146.1};
RA Parent-Michaud M., Dufresne P.J., Fournier E., Martineau C., Moreira S.,
RA Perkins V., De Repentigny L., Dufresne S.F.;
RT "Draft genome sequences of two Aspergillus turcosus clinical strains
RT isolated from bronchoalveolar lavage fluid: one azole-susceptible and the
RT other azole-resistant.";
RL Submitted (AUG-2018) 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 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:RHZ52146.1}.
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DR EMBL; NKHV02000210; RHZ52146.1; -; Genomic_DNA.
DR EMBL; NIDN02000205; RLL94430.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A229X102; -.
DR STRING; 1245748.A0A229X102; -.
DR OrthoDB; 5010334at2759; -.
DR Proteomes; UP000215289; Unassembled WGS sequence.
DR Proteomes; UP000215394; 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};
KW Ion transport {ECO:0000256|RuleBase:RU003857};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000215289};
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 75..96
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 102..129
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 150..172
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 192..211
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 247..268
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 340..364
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 370..389
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 401..421
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 198..268
FT /note="Potassium channel"
FT /evidence="ECO:0000259|Pfam:PF07885"
FT DOMAIN 350..425
FT /note="Potassium channel"
FT /evidence="ECO:0000259|Pfam:PF07885"
FT REGION 470..523
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 504..523
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 629 AA; 71884 MW; 08F4F38FAD4C4660 CRC64;
MVNENSQDEG QNIIEEVPHH ALPAWWWLAS TAYPLLAGTL GPMASAFSIC SLSEEWSMEF
EAGNGQIRGI GDPDWVIVVN AISLGCAILS NFVLLWSMAR RIAFAVAQPI IIIGWYTSSL
LLTCLLCIFA ASKVQSRSDS GRRRWLTGAY YYAAFAAGLY FVLSSLLLIT VYGAYRGHYS
REFRLTTSQR SLMLQTILFL IYLLGGAAVY ARIEGWRYLD AVYWADFTLL TIGIGDFAPK
THEGRGLLFP YAVGGILILG LIVGSIRAQM LEKGRQKMAE TVTERTRRFL VREAVSDHRH
LRDVIPRLQP ERDESDRDRQ RREFQFMRRV RQIATLERKW ISLATSLAVW MMLWFLGAIA
FWLPGQNEKL TYFEALYFAY TTLFTIGYGD FRATSDWERS FFVFWTLLAV PTVTLLIANV
GDTVVRTIRD VTIYLGELTI LPGDKPIREL IKDITRLSWK ERFLSEAVAD KKPDEEDVEE
AAAAATTAAE NGDQDDQGEE EERNAIEADE HKKEESARAR GDVTAETIHH HHYLLFREVR
RMMDYATRNL HKEFDYQEWE YFLNLIAGAG DETEGEAYPK WDWTGHKSPL LGHKTEVQWL
LEALTEALER ELRKASRGYH SPEQSESDS
//
