ID A0A0V1HX88_9BILA Unreviewed; 1155 AA.
AC A0A0V1HX88;
DT 16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT 16-MAR-2016, sequence version 1.
DT 27-MAR-2024, entry version 32.
DE RecName: Full=BK channel {ECO:0000256|ARBA:ARBA00029579};
GN Name=slo-1 {ECO:0000313|EMBL:KRZ14991.1};
GN ORFNames=T11_2224 {ECO:0000313|EMBL:KRZ14991.1};
OS Trichinella zimbabwensis.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Enoplea; Dorylaimia;
OC Trichinellida; Trichinellidae; Trichinella.
OX NCBI_TaxID=268475 {ECO:0000313|EMBL:KRZ14991.1, ECO:0000313|Proteomes:UP000055024};
RN [1] {ECO:0000313|EMBL:KRZ14991.1, ECO:0000313|Proteomes:UP000055024}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ISS1029 {ECO:0000313|EMBL:KRZ14991.1};
RA Korhonen P.K., Edoardo P., Giuseppe L.R., Gasser R.B.;
RT "Evolution of Trichinella species and genotypes.";
RL Submitted (JAN-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
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:KRZ14991.1}.
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DR EMBL; JYDP01000020; KRZ14991.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0V1HX88; -.
DR Proteomes; UP000055024; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005216; F:monoatomic ion channel activity; IEA:InterPro.
DR GO; GO:0006813; P:potassium ion transport; IEA:InterPro.
DR Gene3D; 1.10.287.70; -; 1.
DR Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 2.
DR Gene3D; 1.20.120.350; Voltage-gated potassium channels. Chain C; 1.
DR InterPro; IPR005821; Ion_trans_dom.
DR InterPro; IPR003929; K_chnl_BK_asu.
DR InterPro; IPR047871; K_chnl_Slo-like.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR InterPro; IPR048735; Slowpoke-like_C.
DR InterPro; IPR027359; Volt_channel_dom_sf.
DR PANTHER; PTHR10027; CALCIUM-ACTIVATED POTASSIUM CHANNEL ALPHA CHAIN; 1.
DR PANTHER; PTHR10027:SF33; CALCIUM-ACTIVATED POTASSIUM CHANNEL SUBUNIT ALPHA-1; 1.
DR Pfam; PF03493; BK_channel_a; 1.
DR Pfam; PF00520; Ion_trans; 1.
DR Pfam; PF21014; Slowpoke_C; 1.
DR PRINTS; PR01449; BKCHANNELA.
DR PRINTS; PR00169; KCHANNEL.
DR SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
DR SUPFAM; SSF81324; Voltage-gated potassium channels; 1.
PE 4: Predicted;
KW Calcium {ECO:0000256|ARBA:ARBA00022837};
KW Ion channel {ECO:0000256|ARBA:ARBA00023303, ECO:0000313|EMBL:KRZ14991.1};
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:UP000055024};
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 57..82
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 167..187
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 208..226
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 232..255
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 296..317
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 333..352
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 359..380
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 168..391
FT /note="Ion transport"
FT /evidence="ECO:0000259|Pfam:PF00520"
FT DOMAIN 542..630
FT /note="Calcium-activated potassium channel BK alpha
FT subunit"
FT /evidence="ECO:0000259|Pfam:PF03493"
FT DOMAIN 1021..1140
FT /note="Ca2+-activated K+ channel Slowpoke-like C-terminal"
FT /evidence="ECO:0000259|Pfam:PF21014"
SQ SEQUENCE 1155 AA; 130693 MW; 82D01BF84F8296AA CRC64;
MAGRMPVGAG VVADHQKGSG GSWHQHQLSY ASSCNSTTPY DYYPMTEEER RCLEQRYYWC
FLLSSIVTFC LSMLLVVTWR ILTYICFSTS AVDEAYRVKY DALAEPEHPG KDAIVNGTSQ
IDAINEKSAM VAQPVVDRAE GSQVGWMTEA KDWAGELISG QSTTGRILVV LVFVLSIGSL
IIYFYDASHP NFQVETCISW SHSPSQQIDL AFNIFFLIYF FIRFVAATDK VWFLLEVYSF
IDYFTIPPSF VAIYLERTWL GKLFHRLRFL RALRLMTVPD ILQYLNVLKT SSSIRLAQLV
SIFVSVSLTG AGFIHLLENS GDPFQNFQNP QRITYWECVY FLVVTMGTVG YGDICCKTLL
GRFFMVFFIL GGLAMFASYV PEIADLIGSR QKYGGEYKAE NGKRHIVVCG YITYESVTHF
LQDFLHEDRD DVDVEVVFLH RVPPDLELEG LFKRHFTKVE FFQGTVMDSI DLSRVKVHKA
DACLILANKY SSDPDAEDAA NIMRVISLKN YSPEIRVIVQ LMQYHNKAYL LNIPSWNWRT
GDDVVCLAEL KLGIIAQSCL APGFSTMMAN LFAMRSFKTS MSTPGWLNDY LRGAGMEIYT
ESLSHSFVGM TFPETAELMF TRLKLLLLAI EIKDDESLEC NIIINPESNV IIKVNTQGFF
IAQSADEVKR AFYYCQKCHD DVLDVNLIKK CKCRNLTLFR KGVRHVILAN RTAKVLSPNE
RSQRSSLDDR NKGNLIEGTS EIDLKSSLRE AGLPLKVGLS DPHDGSGDPW QRIDEEDMKY
DSTGMFHWCK ARPIEDIILD REQASVTLLH NHVVLCLFAD RHSPLIGLRN FVMPLRASNY
HYHELKQVVI VGDVEYLRRE WKMIQNLPKI IILNGNPLSR ADLRAVNINM CDMCVIISAR
IPNPNEDPTL TDKEAILASL NIKAMNFDEC SPNLTAAMSG NILVNSRSPS MMLCSNPIRS
GTEILMLTEL VNDSNVQFLD QDDEDDPNTE LYLTQPFTCG KAFAISVLDS LMSTTYFNDS
ALTLIRTLVT GGATPELEGI LAEGGDLRGA PSTSQLLRKR DRCRIAQYGI NDDGPFAGLN
IQDNYTYGRL FIKVLRERRM LCIGLYRLQE PPPATSGKRF VITSPPENMK LMITDRIFVL
EPFDHGIPYE PAKKR
//
