ID A0A364KM21_9EURO Unreviewed; 737 AA.
AC A0A364KM21;
DT 07-NOV-2018, integrated into UniProtKB/TrEMBL.
DT 07-NOV-2018, sequence version 1.
DT 27-MAR-2024, entry version 25.
DE RecName: Full=Actin polymerization protein Bzz1 {ECO:0008006|Google:ProtNLM};
GN ORFNames=BHQ10_000611 {ECO:0000313|EMBL:RAO64599.1};
OS Talaromyces amestolkiae.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Trichocomaceae; Talaromyces;
OC Talaromyces sect. Talaromyces.
OX NCBI_TaxID=1196081 {ECO:0000313|EMBL:RAO64599.1, ECO:0000313|Proteomes:UP000249363};
RN [1] {ECO:0000313|EMBL:RAO64599.1, ECO:0000313|Proteomes:UP000249363}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CIB {ECO:0000313|EMBL:RAO64599.1,
RC ECO:0000313|Proteomes:UP000249363};
RX PubMed=28649280; DOI=10.1186/s13068-017-0844-7;
RA de Eugenio L.I., Mendez-Liter J.A., Nieto-Dominguez M., Alonso L.,
RA Gil-Munoz J., Barriuso J., Prieto A., Martinez M.J.;
RT "Differential ?-glucosidase expression as a function of carbon source
RT availability in Talaromyces amestolkiae: a genomic and proteomic
RT approach.";
RL Biotechnol. Biofuels 10:161-161(2017).
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:RAO64599.1}.
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; MIKG01000001; RAO64599.1; -; Genomic_DNA.
DR STRING; 1196081.A0A364KM21; -.
DR OrthoDB; 4260488at2759; -.
DR Proteomes; UP000249363; 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:UP000249363};
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 579..639
FT /note="SH3"
FT /evidence="ECO:0000259|PROSITE:PS50002"
FT DOMAIN 679..737
FT /note="SH3"
FT /evidence="ECO:0000259|PROSITE:PS50002"
FT REGION 464..584
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 316..390
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 477..497
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 505..535
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 543..558
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 737 AA; 81632 MW; 1DD1A873C1134E44 CRC64;
MAEVNVNPQF GAELKDAXKP VNSWVSNGIA WLDDIQQFYR ERSAIEREYA SKLSALCKKY
SERKSKKISS LSVGDTPTMT PGSLESASLT TWSTQLTTVE SHAAVRDKFG LDLISHVADP
LKNISARYEE LRKSHVEYHG KLEKERESQL SELKKVKGKY DGVCQEVENR RKKTESSFDY
NKTKAQTAYQ QQLLEMSNSK NTYIINIHVA NKLKNQFYHE YVPEVLDSLG DLNETRVQKL
NSFWSLAAQL EKGASTQSTE LMTHLENEIP RNNPKLDSLM FLQHNASQSQ EPPNLTFEPS
PVWHDDDQMI TDESAKVFLR NMLMKSKSQV RELKAEAEKQ QREVESAKRI RDNVRQGKDK
RDEVDVVKAI FNLQEKLHET ERKKMTAEVE TLTILAVVGD LSLGAKNHNF RSQTFKIPTN
CDLCGERIWG LSAKGFDCVD CGYTCHSKCQ MKVPAECPGE QTKEEKKKLK AERQEQAQSA
PAVSEHAPSN GNNGTVADMP ALTRRDTMNS LSSGYAHSAH RSVSGSISSS KPSGEEPAEL
SAAPPRSSTS TTKRNRILAP PPTQYATPPV AAEAPTSKKN EQRGKMVYGY QATGDGEVTV
SEGQEILVLE PDDGSGWMRV KAGSQEGLVP SAYAELAPAP SPALTERPAS TYSNSSASLA
GSTTAKKVGP AVAPRRGAKK LQYVEALYDY EARSDAEHNM SEGDRFVLVT KDSGDGWAEV
EKGGQVKSVP ANYIQEV
//
