ID A0A0S4IIS8_BODSA Unreviewed; 1358 AA.
AC A0A0S4IIS8;
DT 17-FEB-2016, integrated into UniProtKB/TrEMBL.
DT 17-FEB-2016, sequence version 1.
DT 27-MAR-2024, entry version 35.
DE SubName: Full=Potassium channel protein, putative {ECO:0000313|EMBL:CUE73028.1};
GN ORFNames=BSAL_54745 {ECO:0000313|EMBL:CUE73028.1};
OS Bodo saltans (Flagellated protozoan).
OC Eukaryota; Discoba; Euglenozoa; Kinetoplastea; Metakinetoplastina;
OC Eubodonida; Bodonidae; Bodo.
OX NCBI_TaxID=75058 {ECO:0000313|EMBL:CUE73028.1, ECO:0000313|Proteomes:UP000051952};
RN [1] {ECO:0000313|Proteomes:UP000051952}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Lake Konstanz {ECO:0000313|Proteomes:UP000051952};
RG Pathogen Informatics;
RL Submitted (SEP-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
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DR EMBL; CYKH01000142; CUE73028.1; -; Genomic_DNA.
DR VEuPathDB; TriTrypDB:BSAL_54745; -.
DR OrthoDB; 2953470at2759; -.
DR Proteomes; UP000051952; Unassembled WGS sequence.
DR GO; GO:0034702; C:monoatomic ion channel complex; IEA:UniProtKB-KW.
DR GO; GO:0005267; F:potassium channel activity; IEA:UniProtKB-KW.
DR Gene3D; 1.10.287.70; -; 1.
DR Gene3D; 1.20.120.350; Voltage-gated potassium channels. Chain C; 1.
DR InterPro; IPR005821; Ion_trans_dom.
DR InterPro; IPR027359; Volt_channel_dom_sf.
DR PANTHER; PTHR11537:SF254; POTASSIUM VOLTAGE-GATED CHANNEL PROTEIN SHAKER; 1.
DR PANTHER; PTHR11537; VOLTAGE-GATED POTASSIUM CHANNEL; 1.
DR Pfam; PF00520; Ion_trans; 1.
DR PRINTS; PR00169; KCHANNEL.
DR SUPFAM; SSF81324; Voltage-gated potassium channels; 1.
PE 4: Predicted;
KW Ion channel {ECO:0000256|ARBA:ARBA00023303, ECO:0000313|EMBL:CUE73028.1};
KW Ion transport {ECO:0000256|ARBA:ARBA00023065};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Potassium {ECO:0000256|ARBA:ARBA00022958};
KW Potassium channel {ECO:0000256|ARBA:ARBA00022826};
KW Potassium transport {ECO:0000256|ARBA:ARBA00022538};
KW Reference proteome {ECO:0000313|Proteomes:UP000051952};
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 212..235
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 247..270
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 354..374
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 218..548
FT /note="Ion transport"
FT /evidence="ECO:0000259|Pfam:PF00520"
FT REGION 1..51
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 436..470
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 553..622
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 722..761
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 900..932
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1101..1122
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1270..1331
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 22..51
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 437..468
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 553..572
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 917..932
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1104..1122
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1276..1296
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1309..1331
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1358 AA; 148391 MW; 21CEFF7F7E1F1566 CRC64;
MASSSQGLWT PPPIPLEEAL GRSAIRRGDV GVGDEGSEAA RGLSPRRRRE SAISVLDPAN
VRREVGRMRR QSSSSLLRRS SSFSSRREDV PAYNAASILG GDSEVGNPRF DSFKSSSTPS
LDSEDRFFLR EARVTKDILH HLTEDDDGGF DDTLFLSCQG FLKAHHVAVG ARRDLRKKVQ
DRALRIAERK RMTTFWARTL QMLDDPRSSF HAFMVFVTVA TLVVASTITT IISTLPAYNP
IVKSEYLILW NLVDLALGLA FTAETGLRFL SSVFDTTMPT SKWQNGYRFF TKPSNLIDLV
SIAPSYVQLV VSPSSRVITG TLRTVRLLRL FKILRFYKPV RMLQKALKFA GKGLVAPMLF
LITILVFISA GAYFSEDGEY DPSVHKFLID NDPVCVFEPS YFLTLLQRVP DYVAPTPAPT
AFSNVTGVPT PVPSSLPPGV NWESSSTGSS SSNSVGFDQS QASHGTEKVP DASNLGPVIN
HLDCPVSQSN FINIIQCTWW GVSTMSTTGF GDMVTVTGIG RVLSVFGILA GIILNAMPIA
VIDASFVTTL QTEEDQETRE EARRKRDDAN VKLAGVDGNN PDDNGGVQRV SETSIGAPPP
HFRLDDDDRR SAKSASSTMQ QQQLDTSLLA AEGGNASFFA RSALLEQEAH DRQLLDEMTP
RTQAELLLLH LQLLSKAQVI DLANPSDVVL YLLDTLLEAS VTNTAAELAM WHNKQFQHVW
GSGGGAAAHD GAEDSNEQQN NNSKKMEQRH HHHHHHHHHD EMAWCPPTIV SLPIWVAKTQ
TNIAREAQVA GLLVHNPLGE QREVFAERLL LTQPLRLPVG WDPSGGPLWG TGGDEEDSDE
VDMGARHKKK TSSTLNFFTA APELSTTSVN VLDRSLLLKF RRSRREAIAR SVLLPSRLPA
AAGTEGGAGR ARGITSARHK PSSSPLAPTT TASSRFQPLD FSAILDEHCW IVLHQAWGRT
SHLLVPRRPP AVVTSASHSG YSWEEECNTV QLLRFQPHSN SWEIVVPFLT ENKISATTTA
VAATLHQFRS RVSVPCNIMS SGAATALCGA REQLQLSRGT TLSTRNNCEI ARQLLTQFRR
RSHFDTLVAL DKQLAASRMT YRAQRQAKEQ EEAKKARSAK AKKDAETRDL LDALSSEKKE
AYALLQRLDL DIGSAASSSD RLSLLALAST AADKLERERA AERSITMKRF AQMTRVCSEE
QSPRYLLQPG DVILLSGGSS LSSHNLTSSA IPAEGSGSSY GHSLAAVARR VAGLLPAHDE
MMSFAASRVD EQTTRRHGLP QTATNNFSSR RNSTGLVGSP RVGELPVPKT AVSSSSQQLG
ASPRISGGES ASFVTPWPSL DELSPLLGNT LLYVYNGS
//
