ID A0A2I2FRS6_9EURO Unreviewed; 746 AA.
AC A0A2I2FRS6;
DT 28-FEB-2018, integrated into UniProtKB/TrEMBL.
DT 28-FEB-2018, sequence version 1.
DT 27-MAR-2024, entry version 26.
DE SubName: Full=Putative actin polymerization protein Bzz1 {ECO:0000313|EMBL:PLB43334.1};
GN ORFNames=P170DRAFT_514582 {ECO:0000313|EMBL:PLB43334.1};
OS Aspergillus steynii IBT 23096.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Circumdati.
OX NCBI_TaxID=1392250 {ECO:0000313|EMBL:PLB43334.1, ECO:0000313|Proteomes:UP000234275};
RN [1] {ECO:0000313|EMBL:PLB43334.1, ECO:0000313|Proteomes:UP000234275}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=IBT 23096 {ECO:0000313|EMBL:PLB43334.1,
RC ECO:0000313|Proteomes:UP000234275};
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 -!- 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:PLB43334.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; MSFO01000011; PLB43334.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2I2FRS6; -.
DR STRING; 1392250.A0A2I2FRS6; -.
DR VEuPathDB; FungiDB:P170DRAFT_514582; -.
DR OrthoDB; 4260488at2759; -.
DR Proteomes; UP000234275; 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 PRINTS; PR00499; P67PHOX.
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:UP000234275};
KW SH3 domain {ECO:0000256|ARBA:ARBA00022443, ECO:0000256|PROSITE-
KW ProRule:PRU00192}; Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT DOMAIN 7..276
FT /note="F-BAR"
FT /evidence="ECO:0000259|PROSITE:PS51741"
FT DOMAIN 406..456
FT /note="Phorbol-ester/DAG-type"
FT /evidence="ECO:0000259|PROSITE:PS50081"
FT DOMAIN 582..641
FT /note="SH3"
FT /evidence="ECO:0000259|PROSITE:PS50002"
FT DOMAIN 688..746
FT /note="SH3"
FT /evidence="ECO:0000259|PROSITE:PS50002"
FT REGION 454..501
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 518..588
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 322..349
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 457..473
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 528..549
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 746 AA; 81956 MW; EA8878A8BCF054E7 CRC64;
MAAEAAPHFG AELKDAFKPV NNWVFNGISW LDEIQQFYRE RSAIEKEYAA KLSGLCKKYY
DRKAKKISTL SVGDTPSMTP GSLESASLTT WTTQLTAVES HASERDQFAN DLVAQVAEPL
KQAATQYEEL RKCHVDFHAK LEKERDSSYS DLKKAKGKYD GACQEVEAKR KKMESSFDHG
KAKAQTAYQQ QILEMNNVKN TYLISINVTN KMKERFYHEY VPELLDGLQD LNETRVTKLN
TLWSHAALLE KNSLSNSVNH MANLINEIPR NQPHLDSLMF LRHNVTQSQE PPSLGFEPSP
IWHDDEALIT DESAKVFLRN VLSNSKTQVR ELRVEADQKR RTVENAKRIR INIQKGTDKR
NEVEVVRSIF FLQEGLHEVD RKRLTAEVET STIISVVGDL SLGAKNHNFK SQTFKIPTNC
DLCGERIWGL SAKGFDCRDC GYTCHSKCQM KVPAECPGEQ SKEEKKKLKA ERQEQAGATP
ALDLEPSASP SAAPSLTRKD TMNSLSSGYA VSANRSLSNA ASLPPPAELA APASPAPTPP
TPASPAPAPV QETKPAAKRN RVLAPPPAQY ISPPPVDPTP KSGEQRGKML YPYQAGGADE
VTVNEGDDVV IVEPDDGGWM RVRAGASEGL VPTSYVELAP APSPASASPG FTDRPGSVYS
NSSASLAGSS GAAAKRVGPA VAPRRGAKKV QYVEAMYDYE ARSDMEWNMV EGDRFVLVSR
DGGDGWADVE RGGVTKSVPA NYIQEV
//
