ID   A0A2G5HR27_CERBT        Unreviewed;       986 AA.
AC   A0A2G5HR27;
DT   31-JAN-2018, integrated into UniProtKB/TrEMBL.
DT   31-JAN-2018, sequence version 1.
DT   24-JAN-2024, entry version 18.
DE   SubName: Full=Putative chloride channel protein UM03490-D {ECO:0000313|EMBL:PIA94989.1};
GN   ORFNames=CB0940_08937 {ECO:0000313|EMBL:PIA94989.1};
OS   Cercospora beticola (Sugarbeet leaf spot fungus).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC   Dothideomycetidae; Mycosphaerellales; Mycosphaerellaceae; Cercospora.
OX   NCBI_TaxID=122368 {ECO:0000313|EMBL:PIA94989.1, ECO:0000313|Proteomes:UP000230605};
RN   [1] {ECO:0000313|EMBL:PIA94989.1, ECO:0000313|Proteomes:UP000230605}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=09-40 {ECO:0000313|EMBL:PIA94989.1,
RC   ECO:0000313|Proteomes:UP000230605};
RA   De Jonge R., Ebert M.K., Suttle J.C., Jurick Ii W.M., Secor G.A.,
RA   Thomma B.P., Van De Peer Y., Bolton M.D.;
RT   "The cercosporin biosynthetic gene cluster was horizontally transferred to
RT   several fungal lineages and shown to be expanded in Cercospora beticola
RT   based on microsynteny with recipient genomes.";
RL   Submitted (OCT-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:PIA94989.1}.
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DR   EMBL; LKMD01000104; PIA94989.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2G5HR27; -.
DR   OrthoDB; 150430at2759; -.
DR   Proteomes; UP000230605; Chromosome 6.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005247; F:voltage-gated chloride channel activity; IEA:InterPro.
DR   CDD; cd03684; ClC_3_like; 1.
DR   Gene3D; 1.10.3080.10; Clc chloride channel; 1.
DR   InterPro; IPR046342; CBS_dom_sf.
DR   InterPro; IPR014743; Cl-channel_core.
DR   InterPro; IPR001807; Cl-channel_volt-gated.
DR   PANTHER; PTHR45711; CHLORIDE CHANNEL PROTEIN; 1.
DR   PANTHER; PTHR45711:SF3; CLC CHANNEL; 1.
DR   Pfam; PF00654; Voltage_CLC; 1.
DR   PRINTS; PR00762; CLCHANNEL.
DR   SUPFAM; SSF54631; CBS-domain pair; 1.
DR   SUPFAM; SSF81340; Clc chloride channel; 1.
PE   4: Predicted;
KW   Chloride {ECO:0000256|ARBA:ARBA00023214};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW   ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        214..241
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        298..317
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        458..482
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        533..553
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        573..590
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   REGION          1..95
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          867..921
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        33..70
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        71..85
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        885..900
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   986 AA;  108236 MW;  3E66D34CC63F89CD CRC64;
     MPKSVASHAS SNREDDDDDD YEIDEQQAEA IRNAYRNAFS NQQQQQHHYN MSAAPQSHTS
     PTATRRLASH QPSDTDIRHR HRSVQGGGGT TESSALLAPE NPALSRRDYR TVSAPSTPRY
     GFARAHSYVH SARGSRRGSF ARGLMKAINP STYRGEEDND NRRGPTSSKL RQKLYWDDRV
     WYDQFTSTDW VHDSIADAYR VKELRSRKDF RGRVWAFFDG GIGWVLVFII GCVTAAFAYL
     IDITEATIFD YKNGYCGTHW WYSKRMCCTG ASECESWMRW SGSNNTTAQD QAALWKDYGA
     FVLWCVSLAL IGCLITLQTK TTISSAISLS TLDENLAADH HDPTKSGTEG GTKSGYVSGY
     VSPTQRFQEA ARRPPVTYYP AAGSGVAEVR VILSGFVLHG YLGVRTLMCK AIGIVLSVGS
     GMSVGKEGPY VHIATCIGNI ITRFSSKYHD NDAKRREILS ASAAAGVAVA FGAPIGGVLF
     SLEEVSYYFP PKTLFRTFFC CIAAALSLKA LNPYGTNKIV LFEVRYLTDW NSFELIVFAC
     LGVLGGVLGA LFIKASRLWA KTFRKLGFIK SYPMLEVFLV ALVTGLVSFW NRFLRLPVAE
     LLFELSAPCS SFSNSGSALC PTEEQIPSTI KYLLVAFVLK AILTTVTFGI KVPAGIYVPS
     MVVGGLAGRI VGHIVQLVVL KHPDLAVFSN CHIDGNPEEC VVPGVYALVA AGATMCGVTR
     LSVTLAVILF ELTGSLEHVL PFSMGVLIAK WTADALEPLS VYDLLTDMNA YPYLDHKVRP
     VFSTDLGDIT PEPMPNRYID ISNSPFVPAK QLRFKLEYLH MAGELDGGLP ILKNGVLAGL
     IPGPDLEFAL DRIPDEEEAM CRMDAHDQAV QGSARPSTGV SAEENDSDTA REDNVGDAEQ
     AHRPRPASTI GEDSDPTDLT PYIDPAPVAL DITSPMDLVF ECFAKMGLRY ICVLHEGKYA
     GMVHKKAFVR YVKAVQDEDR YGVPAE
//