ID A0A1V8TF80_9PEZI Unreviewed; 748 AA.
AC A0A1V8TF80;
DT 07-JUN-2017, integrated into UniProtKB/TrEMBL.
DT 07-JUN-2017, sequence version 1.
DT 27-MAR-2024, entry version 31.
DE RecName: Full=Protein BZZ1 {ECO:0008006|Google:ProtNLM};
GN ORFNames=B0A48_04255 {ECO:0000313|EMBL:OQO09901.1};
OS Rachicladosporium antarcticum.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Dothideomycetidae; Cladosporiales; Cladosporiaceae; Rachicladosporium.
OX NCBI_TaxID=1507870 {ECO:0000313|EMBL:OQO09901.1, ECO:0000313|Proteomes:UP000192596};
RN [1] {ECO:0000313|Proteomes:UP000192596}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CCFEE 5527 {ECO:0000313|Proteomes:UP000192596};
RA Coleine C., Masonjones S., Stajich J.E.;
RT "Genomes of endolithic fungi from Antarctica.";
RL Submitted (MAR-2017) to the EMBL/GenBank/DDBJ databases.
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:OQO09901.1}.
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DR EMBL; NAJO01000009; OQO09901.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1V8TF80; -.
DR STRING; 1507870.A0A1V8TF80; -.
DR InParanoid; A0A1V8TF80; -.
DR OrthoDB; 4260488at2759; -.
DR Proteomes; UP000192596; 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; PF00018; SH3_1; 1.
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:UP000192596};
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 408..458
FT /note="Phorbol-ester/DAG-type"
FT /evidence="ECO:0000259|PROSITE:PS50081"
FT DOMAIN 574..639
FT /note="SH3"
FT /evidence="ECO:0000259|PROSITE:PS50002"
FT DOMAIN 690..748
FT /note="SH3"
FT /evidence="ECO:0000259|PROSITE:PS50002"
FT REGION 481..514
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 532..577
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 617..684
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 121..148
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 492..514
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 617..667
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 748 AA; 81543 MW; 5191F010BFB6DFC7 CRC64;
MAEVDIAPNF GAELKDGFKN ANAWVGGGIQ WLDDIQAFYR ERAVIEKDYS AKLAALAKKY
FDKKLKKSSS LSVGDTPTVT PGSLESASMT TWTVQLSTLE SRAAEHERFS QQLVSGLAEP
LKNLAARYED LRKQHEGYAA KLEKERDSSY GDLKKTKGKY DSVCQEVENK RKKIESSFDH
GKTKAQGAYV QQQADMRNTK NTYLITINVT NKQKERYYYE YVPELLDALQ ALSEARTATL
NNIWSAASTM ETQTLDRSLQ LMSHLSSEIP RNNPVLDSMM FVRHNALQQW QPPSDFVFEP
SPVWLDDNSM ASDPQSRTFL MNILSKSKSS LGALRKECEA KRREVDGAKR VRQAIREGKD
KRDEVEVVRS LFVHSESLHE AERRRVTAEV EVETITAVMG DISVGMRAHR FENKTFKIPT
NCDLCSDRIW GLSAKGLSCM DCGYTCHLKC ELKVPADCPG ELDKDARKAV KAQRQVEAQN
MAAAPAGAEM ATNGNGNGTS SHRDSLPSLQ RSDTIGSMNT LSSGYAASAH RSVSGATVTS
PAETKPAPIS KGHRVMAPPP AAYRSAPDAD DSGSSEQKGK MLYAYTANGD GEISVAEGID
FAVVESDDGS GWLRIRPLSP FSSQTPGLVP TSYTELQPRP SPRPISTLSS AASNSTTSLN
STTAPRKQGP AVAPRRGKRT VSTSAGGGAL GVKYVEALYT YEPSGDGETG MNAGERLVLI
KDDEGDGWCT VRGGKGEGVV PAGWVKAV
//
