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Database: UniProt
Entry: A0A3F3Q889_9EURO
LinkDB: A0A3F3Q889_9EURO
Original site: A0A3F3Q889_9EURO 
ID   A0A3F3Q889_9EURO        Unreviewed;       743 AA.
AC   A0A3F3Q889;
DT   16-JAN-2019, integrated into UniProtKB/TrEMBL.
DT   16-JAN-2019, sequence version 1.
DT   27-MAR-2024, entry version 22.
DE   SubName: Full=FCH-domain-containing protein {ECO:0000313|EMBL:RDH35012.1};
GN   ORFNames=BDQ94DRAFT_140087 {ECO:0000313|EMBL:RDH35012.1};
OS   Aspergillus welwitschiae.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
OX   NCBI_TaxID=1341132 {ECO:0000313|EMBL:RDH35012.1, ECO:0000313|Proteomes:UP000253729};
RN   [1] {ECO:0000313|EMBL:RDH35012.1, ECO:0000313|Proteomes:UP000253729}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CBS 139.54b {ECO:0000313|EMBL:RDH35012.1,
RC   ECO:0000313|Proteomes:UP000253729};
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 (JUL-2018) to the EMBL/GenBank/DDBJ databases.
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DR   EMBL; KZ852041; RDH35012.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A3F3Q889; -.
DR   STRING; 1341132.A0A3F3Q889; -.
DR   OrthoDB; 4260488at2759; -.
DR   Proteomes; UP000253729; Unassembled WGS sequence.
DR   GO; GO:0030864; C:cortical actin cytoskeleton; IEA:UniProt.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0030036; P:actin cytoskeleton organization; IEA:UniProt.
DR   CDD; cd20824; C1_SpBZZ1-like; 1.
DR   CDD; cd11912; SH3_Bzz1_1; 1.
DR   Gene3D; 3.30.60.20; -; 1.
DR   Gene3D; 1.20.1270.60; Arfaptin homology (AH) domain/BAR domain; 1.
DR   Gene3D; 2.30.30.40; SH3 Domains; 2.
DR   InterPro; IPR027267; AH/BAR_dom_sf.
DR   InterPro; IPR035459; Bzz1_SH3_1.
DR   InterPro; IPR046349; C1-like_sf.
DR   InterPro; IPR020454; DAG/PE-bd.
DR   InterPro; IPR031160; F_BAR.
DR   InterPro; IPR001060; FCH_dom.
DR   InterPro; IPR002219; PE/DAG-bd.
DR   InterPro; IPR036028; SH3-like_dom_sf.
DR   InterPro; IPR001452; SH3_domain.
DR   PANTHER; PTHR15735:SF12; CDC42-INTERACTING PROTEIN 4, ISOFORM B; 1.
DR   PANTHER; PTHR15735; FCH AND DOUBLE SH3 DOMAINS PROTEIN; 1.
DR   Pfam; PF00130; C1_1; 1.
DR   Pfam; PF00611; FCH; 1.
DR   Pfam; PF14604; SH3_9; 2.
DR   PRINTS; PR00008; DAGPEDOMAIN.
DR   SMART; SM00109; C1; 1.
DR   SMART; SM00055; FCH; 1.
DR   SMART; SM00326; SH3; 2.
DR   SUPFAM; SSF103657; BAR/IMD domain-like; 1.
DR   SUPFAM; SSF57889; Cysteine-rich domain; 1.
DR   SUPFAM; SSF50044; SH3-domain; 2.
DR   PROSITE; PS51741; F_BAR; 1.
DR   PROSITE; PS50002; SH3; 2.
DR   PROSITE; PS00479; ZF_DAG_PE_1; 1.
DR   PROSITE; PS50081; ZF_DAG_PE_2; 1.
PE   4: Predicted;
KW   Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW   Coiled coil {ECO:0000256|ARBA:ARBA00023054, ECO:0000256|PROSITE-
KW   ProRule:PRU01077}; Membrane {ECO:0000256|ARBA:ARBA00022475};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Reference proteome {ECO:0000313|Proteomes:UP000253729};
KW   SH3 domain {ECO:0000256|ARBA:ARBA00022443, ECO:0000256|PROSITE-
KW   ProRule:PRU00192}; Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT   DOMAIN          8..277
FT                   /note="F-BAR"
FT                   /evidence="ECO:0000259|PROSITE:PS51741"
FT   DOMAIN          407..457
FT                   /note="Phorbol-ester/DAG-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50081"
FT   DOMAIN          575..635
FT                   /note="SH3"
FT                   /evidence="ECO:0000259|PROSITE:PS50002"
FT   DOMAIN          685..743
FT                   /note="SH3"
FT                   /evidence="ECO:0000259|PROSITE:PS50002"
FT   REGION          457..575
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          634..677
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          323..350
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COMPBIAS        457..474
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        483..534
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        561..575
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        647..665
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   743 AA;  82222 MW;  6FCCE2DDE382DF16 CRC64;
     MATPDVAPHF GAELKDSFKP VNNWVSNGIG WLDEIQQFYR ERSAIEKEYA AKLTALCKKY
     YDRKAKKISS LSVGDTPSMT PGSLESASLT TWSTQLSAVE AHATERDHFG NDLLVHVAEP
     LKQAANQYEE LRKCHVDFHA KLEKERDSSY SDLKKAKGKY DGACQEVEAR RKKMESSFDH
     SKPKAQAAYQ QQILEMNNVK NTYLISINVT NKMKERFYHE YVPELLDGLQ DLNETRVTKL
     NSLWTMAAQL EKNYLSKSMD HMANLINEIP RNVPHLDSLM FLRHNVTQSQ EPANLAFEPS
     PIWHDDDALI TDEAAKVFLR NLLSKSKTQV RELRVEADSK RREVENARRV RENIRQGTDK
     RNEVEVVRAI FFQQESLHEV DRRRLTAEVE TSTIMAAVGD LSLGARNHNF KSQTFKIPTN
     CDLCGERIWG LSAKGFDCRD CGYTCHSKCE MKVPAECPGE QTKEEKKKLK AERQEQANTA
     PAPLDLEPTT SSSTAPSLTR KDTMNSLSSG YAVSANRSMS NATQSPTTTA AELPTPVAET
     KPAPARKNRI LAPPPAQYIS GPPANDSTPA LSSKANEQHG KMLYAYQAGG ADEVTVQEGD
     DVVILEPDDG SGWMRVRFGS EEGLVPASYV EAGPAPSPVP SASPGFTADR PGSTYSNSSA
     SLTGGGGAGG NKRVGPAVAP RRGAKKLQYV EALYDYEARS DMEWSMVEGD RFVLVNRDGG
     DGWADVERGG VTKSVPANYI QEV
//
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