ID A0A1B7NP31_9EURO Unreviewed; 1007 AA.
AC A0A1B7NP31;
DT 02-NOV-2016, integrated into UniProtKB/TrEMBL.
DT 02-NOV-2016, sequence version 1.
DT 27-MAR-2024, entry version 30.
DE RecName: Full=Chloride channel protein {ECO:0000256|RuleBase:RU361221};
GN ORFNames=ACJ72_07297 {ECO:0000313|EMBL:OAX78397.1};
OS Emergomyces africanus.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Onygenales; Ajellomycetaceae; Emergomyces.
OX NCBI_TaxID=1955775 {ECO:0000313|EMBL:OAX78397.1, ECO:0000313|Proteomes:UP000091918};
RN [1] {ECO:0000313|EMBL:OAX78397.1, ECO:0000313|Proteomes:UP000091918}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 136260 {ECO:0000313|EMBL:OAX78397.1,
RC ECO:0000313|Proteomes:UP000091918};
RA Cuomo C.A., Schwartz I.S., Kenyon C., de Hoog G.S., Govender N.P.,
RA Botha A., Moreno L., de Vries M., Munoz J.F., Stielow J.B.;
RT "Emmonsia species relationships and genome sequence.";
RL Submitted (JUL-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141,
CC ECO:0000256|RuleBase:RU361221}; Multi-pass membrane protein
CC {ECO:0000256|ARBA:ARBA00004141, ECO:0000256|RuleBase:RU361221}.
CC -!- SIMILARITY: Belongs to the chloride channel (TC 2.A.49) family.
CC {ECO:0000256|RuleBase:RU361221}.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|RuleBase:RU361221}.
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:OAX78397.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; LGUA01001551; OAX78397.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1B7NP31; -.
DR OrthoDB; 150430at2759; -.
DR Proteomes; UP000091918; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0043227; C:membrane-bounded organelle; IEA:UniProt.
DR GO; GO:0046982; F:protein heterodimerization activity; IEA:InterPro.
DR GO; GO:0005247; F:voltage-gated chloride channel activity; IEA:UniProtKB-UniRule.
DR CDD; cd03684; ClC_3_like; 1.
DR Gene3D; 3.10.580.20; -; 1.
DR Gene3D; 3.90.1280.20; -; 1.
DR Gene3D; 1.10.3080.10; Clc chloride channel; 1.
DR Gene3D; 1.10.20.10; Histone, subunit A; 1.
DR InterPro; IPR003958; CBFA_NFYB_domain.
DR InterPro; IPR000644; CBS_dom.
DR InterPro; IPR046342; CBS_dom_sf.
DR InterPro; IPR014743; Cl-channel_core.
DR InterPro; IPR001807; Cl-channel_volt-gated.
DR InterPro; IPR009072; Histone-fold.
DR PANTHER; PTHR45711:SF9; ANION_PROTON EXCHANGE TRANSPORTER GEF1; 1.
DR PANTHER; PTHR45711; CHLORIDE CHANNEL PROTEIN; 1.
DR Pfam; PF00808; CBFD_NFYB_HMF; 1.
DR Pfam; PF00571; CBS; 2.
DR Pfam; PF00654; Voltage_CLC; 1.
DR PRINTS; PR00762; CLCHANNEL.
DR SMART; SM00116; CBS; 2.
DR SUPFAM; SSF54631; CBS-domain pair; 1.
DR SUPFAM; SSF81340; Clc chloride channel; 1.
DR SUPFAM; SSF47113; Histone-fold; 1.
DR PROSITE; PS51371; CBS; 2.
PE 3: Inferred from homology;
KW CBS domain {ECO:0000256|PROSITE-ProRule:PRU00703};
KW Chloride {ECO:0000256|ARBA:ARBA00023214, ECO:0000256|RuleBase:RU361221};
KW Ion transport {ECO:0000256|RuleBase:RU361221};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|RuleBase:RU361221};
KW Reference proteome {ECO:0000313|Proteomes:UP000091918};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692,
KW ECO:0000256|RuleBase:RU361221};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|RuleBase:RU361221}; Transport {ECO:0000256|RuleBase:RU361221}.
FT TRANSMEM 272..293
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361221"
FT TRANSMEM 305..325
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361221"
FT TRANSMEM 374..398
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361221"
FT TRANSMEM 410..430
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361221"
FT TRANSMEM 451..468
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361221"
FT TRANSMEM 488..508
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361221"
FT TRANSMEM 539..560
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361221"
FT TRANSMEM 566..590
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361221"
FT DOMAIN 689..749
FT /note="CBS"
FT /evidence="ECO:0000259|PROSITE:PS51371"
FT DOMAIN 841..900
FT /note="CBS"
FT /evidence="ECO:0000259|PROSITE:PS51371"
FT REGION 147..196
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 760..821
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 955..992
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 148..182
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 760..798
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 799..821
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 958..976
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1007 AA; 111412 MW; 79BB1B952C2C0079 CRC64;
MPSNTSAVPP PQEVSGRSAL PLTRIKKIIH LDEDIAQCSS NAAFVIAVAT EMFIRYLAEQ
GHNVLKSERK PRRTIQYKDL GLHQLFITRS TGTGTSYLTT PKLLTVDKAH SPLPIEDDNL
HPCVAGVMNP PGASISAQPF RHAQRRLSVH PPNNSRPRST SATFSLHSHR SPADNVNVHT
PSIETPLEGG PRTTIPSTIR DEINEINEIK RYEDFTTIDW VQDAVHEQAR RRAKRRSGSR
FWDQEGTLGW RRKSASRCSE WRPWSSIAPL NYIAYFIFAV LFAFSSAVLV NSFAPYAAGS
GISEIKVIIA GFIMKGFLSA RTLIIKSLTL PLSIASGLSV GKEGPSVHFA VCTGNVISRW
FDKYKRNAAK TREILTATAG AGVAVAFGSP IGGVLFSLEE MASYFPLKTL WRSYFCALVA
TGVLAAMNPF RTGQLVMFQV KYDRTWHPFE LIFFVLLGVF GGLYGAFVMK WNLRSQAFRK
KYLSRHPIIE ATVLAGATAL ICYPNMFLRI NMTEMMEILF RECEGAHDYN GICNTNNRWS
MVISLAIATI IRVLLVIISY GCKVPAGIFV PSMAIGASFG RMVGILVQAL HESFPDSKFF
ATCEPDVPCI TPGTYAFLGA GAALSGIMHL TVSVTVIMFE LTGALTYILT LSDSFGKGGI
ADRMIWFNGF PFLDSKEDHI FNVPVSHAMT SKPVVLTATD FPVSKAEKLL RQHKYQGFPI
VEDLTHKTVI GFIGRTELQY AINRAKRDGL LSPNAKCRFT TSPSSTSYRH RSVPSTNSLA
LKIPPSTQQT FGSNSSSSSR SEDHHHLHNT DLSPDDQRPS RTFDDIASST GIRTIDFSQY
VDLAPLTVHP RLPLETVMEI FKKMGPRVIL VEHRGRLSGL VTIKDCLKYQ FKVEAQEHAV
TSDGIGDSSH GNGNGNGNGG LGEGIIEQKA WEFIQWATEK VAFWRRMGRG RRGLLMQSSS
EGERDRDGRE GSGWDGELMH SRSSPDIVDG TEELEGFVEL EERGDER
//
