ID A0A1Y2VUU3_9PEZI Unreviewed; 738 AA.
AC A0A1Y2VUU3;
DT 30-AUG-2017, integrated into UniProtKB/TrEMBL.
DT 30-AUG-2017, sequence version 1.
DT 27-MAR-2024, entry version 29.
DE RecName: Full=Actin polymerization protein Bzz1 {ECO:0008006|Google:ProtNLM};
GN ORFNames=M426DRAFT_324127 {ECO:0000313|EMBL:OTB00661.1};
OS Hypoxylon sp. CI-4A.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Xylariomycetidae; Xylariales; Hypoxylaceae; Hypoxylon.
OX NCBI_TaxID=1001833 {ECO:0000313|EMBL:OTB00661.1, ECO:0000313|Proteomes:UP000242955};
RN [1] {ECO:0000313|EMBL:OTB00661.1, ECO:0000313|Proteomes:UP000242955}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CI-4A {ECO:0000313|EMBL:OTB00661.1,
RC ECO:0000313|Proteomes:UP000242955};
RX PubMed=28078400; DOI=10.1007/s00253-017-8091-1;
RA Wu W., Davis R.W., Tran-Gyamfi M.B., Kuo A., LaButti K., Mihaltcheva S.,
RA Hundley H., Chovatia M., Lindquist E., Barry K., Grigoriev I.V.,
RA Henrissat B., Gladden J.M.;
RT "Characterization of four endophytic fungi as potential consolidated
RT bioprocessing hosts for conversion of lignocellulose into advanced
RT biofuels.";
RL Appl. Microbiol. Biotechnol. 101:2603-2618(2017).
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DR EMBL; KZ111594; OTB00661.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1Y2VUU3; -.
DR STRING; 1001833.A0A1Y2VUU3; -.
DR InParanoid; A0A1Y2VUU3; -.
DR OrthoDB; 4260488at2759; -.
DR Proteomes; UP000242955; 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 Pfam; PF14604; SH3_9; 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:UP000242955};
KW SH3 domain {ECO:0000256|ARBA:ARBA00022443, ECO:0000256|PROSITE-
KW ProRule:PRU00192}; Transport {ECO:0000256|ARBA:ARBA00022448};
KW Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT DOMAIN 8..275
FT /note="F-BAR"
FT /evidence="ECO:0000259|PROSITE:PS51741"
FT DOMAIN 405..455
FT /note="Phorbol-ester/DAG-type"
FT /evidence="ECO:0000259|PROSITE:PS50081"
FT DOMAIN 571..631
FT /note="SH3"
FT /evidence="ECO:0000259|PROSITE:PS50002"
FT DOMAIN 678..738
FT /note="SH3"
FT /evidence="ECO:0000259|PROSITE:PS50002"
FT REGION 466..545
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 637..672
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 164..200
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 321..348
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 495..524
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 637..663
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 738 AA; 81829 MW; 2ED41ACB4B2AF0E6 CRC64;
MAEVEVAPTF GAELKDGFKP ANAWVANGIA WLDDIQSFYR ERSAIEKEHS AKLNALAKKY
FEKKSKKSAS LSVGDTPAMT PGSLENASLN IWTTHLTTLE SIAEEHEKYG NELITKVADP
MKYFAAKFDD LRKRHVEYAT KLEAERDSSY ADLRKVKTKY DAACQEVESK RKKTESSFDK
AKAQSQYQQQ LQDMNNVKNT YLIAINVTNK QKEKYYHEYV PEVLDSLQDL AEFRTMKLNT
LWSTAASLET TMLQQSNSLV DHLAQEITRN QPHLDCMMYI RHNMGLWQEP HDKMFEPSPV
WHDDDLMITD EVAKVFLRNV LNKSKGQLGD LRREVDKKRR EIEGVKRVKQ RIREGKENKD
EVLVVSQIFS MQEDLHQVDR KRLTAEVETS TITSAVGDVT LGAKNHNFKS QTFKIPTNCD
LCGERIWGLS AKGFDCRDCG YTCHSKCEMK VPAECPGELS KEERKKYKAE RQSAAGALLK
PSSGPPDHVA ELPDLTRSNT MTSLSSGYAA SANRSITGSA VSPRSPAEDT PPEPPGPRPS
VKKSRLMAPP PAAYISELPG SSVSVPAPSK SAERKGKMVY AFEAHGDGEV SVSEGREVTV
LQPDDGSGWA KVRVGYKEGI VPASYLEIVP EPIVPQDTGS SSINNRPAST YSNSGSSINT
TGPVKKKGPA VAPRRGAKKL KYVIALYDYA AQSDAEHSMM EGERFVLIKD DPGDGWAEVE
KGGVTKSVPA SYVAVANE
//
