ID C0NWK1_AJECG Unreviewed; 576 AA.
AC C0NWK1;
DT 05-MAY-2009, integrated into UniProtKB/TrEMBL.
DT 05-MAY-2009, sequence version 1.
DT 24-JAN-2024, entry version 49.
DE RecName: Full=Chromosome condensation protein {ECO:0008006|Google:ProtNLM};
GN ORFNames=HCBG_07531 {ECO:0000313|EMBL:EEH04306.1};
OS Ajellomyces capsulatus (strain G186AR / H82 / ATCC MYA-2454 / RMSCC 2432)
OS (Darling's disease fungus) (Histoplasma capsulatum).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Onygenales; Ajellomycetaceae; Histoplasma.
OX NCBI_TaxID=447093 {ECO:0000313|EMBL:EEH04306.1, ECO:0000313|Proteomes:UP000001631};
RN [1] {ECO:0000313|Proteomes:UP000001631}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=G186AR / H82 / ATCC MYA-2454 / RMSCC 2432
RC {ECO:0000313|Proteomes:UP000001631};
RA Champion M., Cuomo C.A., Ma L.-J., Henn M.R., Sil A., Goldman B.,
RA Young S.K., Kodira C.D., Zeng Q., Koehrsen M., Alvarado L., Berlin A.,
RA Borenstein D., Chen Z., Engels R., Freedman E., Gellesch M., Goldberg J.,
RA Griggs A., Gujja S., Heiman D., Hepburn T., Howarth C., Jen D., Larson L.,
RA Lewis B., Mehta T., Park D., Pearson M., Roberts A., Saif S., Shea T.,
RA Shenoy N., Sisk P., Stolte C., Sykes S., Walk T., White J., Yandava C.,
RA Klein B., McEwen J.G., Puccia R., Goldman G.H., Felipe M.S., Nino-Vega G.,
RA San-Blas G., Taylor J., Mendoza L., Galagan J.E., Nusbaum C., Birren B.W.;
RT "The genome sequence of Ajellomyces capsulatus strain G186AR.";
RL Submitted (FEB-2009) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Fluoride channel required for the rapid expulsion of
CC cytoplasmic fluoride. {ECO:0000256|ARBA:ARBA00002598}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=fluoride(in) = fluoride(out); Xref=Rhea:RHEA:76159,
CC ChEBI:CHEBI:17051; Evidence={ECO:0000256|ARBA:ARBA00035585};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:76160;
CC Evidence={ECO:0000256|ARBA:ARBA00035585};
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
CC -!- SIMILARITY: Belongs to the fluoride channel Fluc/FEX (TC 1.A.43)
CC family. {ECO:0000256|ARBA:ARBA00035120}.
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DR EMBL; GG663374; EEH04306.1; -; Genomic_DNA.
DR AlphaFoldDB; C0NWK1; -.
DR STRING; 447093.C0NWK1; -.
DR VEuPathDB; FungiDB:I7I50_08020; -.
DR HOGENOM; CLU_030507_0_0_1; -.
DR InParanoid; C0NWK1; -.
DR OrthoDB; 162264at2759; -.
DR Proteomes; UP000001631; Unassembled WGS sequence.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-KW.
DR GO; GO:1903425; F:fluoride transmembrane transporter activity; IEA:UniProt.
DR InterPro; IPR003691; FluC.
DR PANTHER; PTHR28259; FLUORIDE EXPORT PROTEIN 1-RELATED; 1.
DR PANTHER; PTHR28259:SF1; FLUORIDE EXPORT PROTEIN 1-RELATED; 1.
DR Pfam; PF02537; CRCB; 2.
PE 3: Inferred from homology;
KW Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000001631};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT TRANSMEM 145..169
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 175..196
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 297..325
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 345..373
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 394..412
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 424..444
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 456..478
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 484..506
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 553..575
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT REGION 1..66
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 211..287
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..31
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 38..57
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 236..250
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 251..275
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 576 AA; 63458 MW; ABAEF6B2A0B6853B CRC64;
MDDEKSSVHF RHSHSGQEAL AEARGDPELT RGPSLEEAQS GWREERRRLE EGRVADLTES
ALPDTLEDAE AELQREHIRE ATFRRDLERN GPLTEFAVPP PVERVSSWRG DWAALESAES
RVTTPPPTVE RVAGIEARLS DYATLLYTIS YLVFFSILGA LARIGLQWLT SYPGAPLITA
VTWANVGGCL LMGFLAEDRK LFREEWGQWK RKHPGHESSA PNGHISNPSS HAHLPHPMKQ
LRRRYSRSHT RQQHPPSERQ SRVSEHNDVD SPKEEPVTPP MEPAQSLKIH KSIKKTIPLY
IGLTTGFCGS LTSFSSFMLD VFLALANDLP TPGHPESPVP RNGGYSFMAV LAIIIYTLSL
SIGALILGSH LAIFMDKYTP VIPYIFSRRY VDPFISFLAM GSWLGAVFLA IWPPDRSLGV
REHWRGSAMF AVVFAPLGCL FRFYVSLLLN SRIPKFPLGT FTANIFGTLV LAMCYDLQRS
TNVLAVPVSS FSPASAAVAA AAVSVSRLTG CQVLQGIMDG FCGCTTTVST WVAELDSLDH
EHAYVYGLVT TGVALGLLVV IIGSVQWTVG FGLAVC
//
