ID A0A317VG54_ASPEC Unreviewed; 874 AA.
AC A0A317VG54;
DT 10-OCT-2018, integrated into UniProtKB/TrEMBL.
DT 10-OCT-2018, sequence version 1.
DT 24-JAN-2024, entry version 16.
DE RecName: Full=Chloride channel protein {ECO:0000256|RuleBase:RU361221};
GN ORFNames=BO83DRAFT_339038 {ECO:0000313|EMBL:PWY71912.1};
OS Aspergillus eucalypticola (strain CBS 122712 / IBT 29274).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
OX NCBI_TaxID=1448314 {ECO:0000313|EMBL:PWY71912.1, ECO:0000313|Proteomes:UP000246171};
RN [1] {ECO:0000313|EMBL:PWY71912.1, ECO:0000313|Proteomes:UP000246171}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 122712 {ECO:0000313|EMBL:PWY71912.1,
RC ECO:0000313|Proteomes:UP000246171};
RG DOE Joint Genome Institute;
RA Vesth T.C., Nybo J., Theobald S., Brandl J., Frisvad J.C., Nielsen K.F.,
RA Lyhne E.K., Kogle M.E., Kuo A., Riley R., Clum A., Nolan M., Lipzen A.,
RA Salamov A., Henrissat B., Wiebenga A., De Vries R.P., Grigoriev I.V.,
RA Mortensen U.H., Andersen M.R., Baker S.E.;
RT "The genomes of Aspergillus section Nigri reveals drivers in fungal
RT speciation.";
RL Submitted (DEC-2016) 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:PWY71912.1}.
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DR EMBL; MSFU01000014; PWY71912.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A317VG54; -.
DR VEuPathDB; FungiDB:BO83DRAFT_339038; -.
DR OrthoDB; 150430at2759; -.
DR Proteomes; UP000246171; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005247; F:voltage-gated chloride channel activity; IEA:UniProtKB-UniRule.
DR CDD; cd04591; CBS_pair_voltage-gated_CLC_euk_bac; 1.
DR CDD; cd03684; ClC_3_like; 1.
DR Gene3D; 3.10.580.20; -; 1.
DR Gene3D; 1.10.3080.10; Clc chloride channel; 1.
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 PANTHER; PTHR45711; CHLORIDE CHANNEL PROTEIN; 1.
DR PANTHER; PTHR45711:SF6; CHLORIDE CHANNEL PROTEIN; 1.
DR Pfam; PF00571; CBS; 1.
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 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 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 173..191
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361221"
FT TRANSMEM 255..279
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361221"
FT TRANSMEM 357..381
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361221"
FT TRANSMEM 434..455
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361221"
FT TRANSMEM 467..486
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361221"
FT TRANSMEM 526..545
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361221"
FT TRANSMEM 551..567
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361221"
FT TRANSMEM 621..644
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361221"
FT DOMAIN 687..749
FT /note="CBS"
FT /evidence="ECO:0000259|PROSITE:PS51371"
FT DOMAIN 779..837
FT /note="CBS"
FT /evidence="ECO:0000259|PROSITE:PS51371"
FT REGION 1..85
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 91..110
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..36
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 62..85
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 874 AA; 96211 MW; 1AAE8EED2F664A56 CRC64;
MSMSRPGPQS EAQSSLIQPY SDDEPAQDSS SLDPQHPDVP LSGGLREPLS FKRKQRQHSR
SKFRFPNFFS NSSAEPATST GLGSWFRNEQ RSDDAQPLGE PINGNGNGNL AHKDSGFLDW
YVEGPGRRVG YDNLTAIDWI FEYTKERQRK RLLYASGQGV VGYLRKLLDA SNVWIVLIAT
GVLVGIIAAG IDVASDWLAD LKTGYCKAGP GGGRFYLNRS FCCWGHDDIS DCLDWTPWRK
ALGVSSRGGG YALEYTFYIL YSVFFAICAC ILVRTYAIYA RHSGIPEIKT VLGGFVIRHF
MGPWTLAIKS LGLCLSVASG MWLGKEGPLI HVACCCASVM MKPFHSLNHN EARKREVLSA
AAAAGVSVAF GAPIGGVLFS LEQLSYYFPD KTMWQSFVCA MVASVTLHAL NPFRTGNIVL
YQVKYTREWH RFEMIPFVIL GIVGGLYGAF LIRLNMKIAT WRRSRNWARP IIEVAVVALL
SALINFPNLF MRAQNSELVH SLFAECGTGT VTDDPFGLCK TGASSAGTIA LLLMAALLGF
FLASLTFGLD IPAGIILPSV AIGALYGRGM GMTFRMWQEA YPGFFLFGKC EPDVPCVTPG
IYAIIGAASA LGGATRMTVS IVVIMFELTG ALTYVIPIMI AVMLSKWCGD IFGKRGIYES
WIQLNEYPFL DHRDDTTPPD VPAHKVMTTV DDMTVITAVG HTIDSLRGLL LTTSYRGFPV
VTDTSNPILL GYISRNELTY ALKYSTKPSD NELSGATQVF FSHQPFADPA ETLDLRPWMD
QTPITLNSNT TFLIVLRMFQ RLGLRYVLLA DKGVLQGLLT KKDVWSVVSG PDAYKDESLR
ERTFNPGTMA EEVGLLDSDD RTSLASTIER RQSL
//