ID A0A0A1TDG4_9HYPO Unreviewed; 426 AA.
AC A0A0A1TDG4;
DT 04-FEB-2015, integrated into UniProtKB/TrEMBL.
DT 04-FEB-2015, sequence version 1.
DT 08-NOV-2023, entry version 23.
DE RecName: Full=CrcB-like protein {ECO:0008006|Google:ProtNLM};
GN ORFNames=VHEMI08419 {ECO:0000313|EMBL:CEJ92789.1};
OS [Torrubiella] hemipterigena.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Clavicipitaceae;
OC Clavicipitaceae incertae sedis; 'Torrubiella' clade.
OX NCBI_TaxID=1531966 {ECO:0000313|EMBL:CEJ92789.1, ECO:0000313|Proteomes:UP000039046};
RN [1] {ECO:0000313|EMBL:CEJ92789.1, ECO:0000313|Proteomes:UP000039046}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Horn F., Habel A., Scharf D.H., Dworschak J., Brakhage A.A., Guthke R.,
RA Hertweck C., Linde J.;
RT "Draft Genome Sequence and Gene Annotation of the Entomopathogenic Fungus
RT Verticillium hemipterigenum.";
RL Genome Announc. 3:e01439-e01414(2015).
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; CDHN01000005; CEJ92789.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0A1TDG4; -.
DR STRING; 1531966.A0A0A1TDG4; -.
DR HOGENOM; CLU_030507_0_0_1; -.
DR OrthoDB; 162264at2759; -.
DR Proteomes; UP000039046; 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:UP000039046};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT TRANSMEM 87..107
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 113..132
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 175..196
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 224..250
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 271..289
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 295..315
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 392..413
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT REGION 1..51
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..31
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 426 AA; 46085 MW; 1A8A9319E960988E CRC64;
MDASSQHTRQ PPTMSSDSTP NAQTASGEVT AMPDSYKQPE APTPSEAVPR TNLEDLQYRD
PHHYPPNILE ASSQHTVSAL ATKIYTLSYL VLFSLFGTLA RVGLTALTSY PGAPVFTTVW
ANVGGSFIMG FLTEDRMLFR HEWGRAVYDE AIRARKDGED LSAAKKAHLA TKKTIPLYVG
LATGFCGSFT SFSTFLRDVF LAASNDLPVP GGGFTTHRNG GYSFMALLGV LVTDITLSLG
AYTMGSHLAA ATEGLLPSLP FHFTRKILDR VAVVLGWGCW LGAVFLSIFP PHDHWRGQIT
FALVFAPIGC LGRFYLAMYL NAKRPSFPLG TFAANIIGTA ILAIGWDVAH VPAGGVITCQ
VMQGLEDGLC GCLTTVSTWV AELHTLRRKH SYIYGAASVI TGFALMIIIM GGLRWSQGFH
PLLCKI
//
