ID F9WWH7_ZYMTI Unreviewed; 649 AA.
AC F9WWH7;
DT 19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT 19-OCT-2011, sequence version 1.
DT 27-MAR-2024, entry version 66.
DE RecName: Full=Actin polymerization protein Bzz1 {ECO:0008006|Google:ProtNLM};
DE Flags: Fragment;
GN ORFNames=MYCGRDRAFT_102352 {ECO:0000313|EMBL:EGP91202.1};
OS Zymoseptoria tritici (strain CBS 115943 / IPO323) (Speckled leaf blotch
OS fungus) (Septoria tritici).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Dothideomycetidae; Mycosphaerellales; Mycosphaerellaceae; Zymoseptoria.
OX NCBI_TaxID=336722 {ECO:0000313|EMBL:EGP91202.1, ECO:0000313|Proteomes:UP000008062};
RN [1] {ECO:0000313|EMBL:EGP91202.1, ECO:0000313|Proteomes:UP000008062}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 115943 / IPO323 {ECO:0000313|Proteomes:UP000008062};
RX PubMed=21695235; DOI=10.1371/journal.pgen.1002070;
RA Goodwin S.B., Ben M'barek S., Dhillon B., Wittenberg A.H.J., Crane C.F.,
RA Hane J.K., Foster A.J., Van der Lee T.A.J., Grimwood J., Aerts A.,
RA Antoniw J., Bailey A., Bluhm B., Bowler J., Bristow J., van der Burgt A.,
RA Canto-Canche B., Churchill A.C.L., Conde-Ferraez L., Cools H.J.,
RA Coutinho P.M., Csukai M., Dehal P., De Wit P., Donzelli B.,
RA van de Geest H.C., van Ham R.C.H.J., Hammond-Kosack K.E., Henrissat B.,
RA Kilian A., Kobayashi A.K., Koopmann E., Kourmpetis Y., Kuzniar A.,
RA Lindquist E., Lombard V., Maliepaard C., Martins N., Mehrabi R.,
RA Nap J.P.H., Ponomarenko A., Rudd J.J., Salamov A., Schmutz J.,
RA Schouten H.J., Shapiro H., Stergiopoulos I., Torriani S.F.F., Tu H.,
RA de Vries R.P., Waalwijk C., Ware S.B., Wiebenga A., Zwiers L.-H.,
RA Oliver R.P., Grigoriev I.V., Kema G.H.J.;
RT "Finished genome of the fungal wheat pathogen Mycosphaerella graminicola
RT reveals dispensome structure, chromosome plasticity, and stealth
RT pathogenesis.";
RL PLoS Genet. 7:E1002070-E1002070(2011).
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DR EMBL; CM001196; EGP91202.1; -; Genomic_DNA.
DR RefSeq; XP_003856226.1; XM_003856178.1.
DR AlphaFoldDB; F9WWH7; -.
DR STRING; 336722.F9WWH7; -.
DR EnsemblFungi; Mycgr3T102352; Mycgr3P102352; Mycgr3G102352.
DR GeneID; 13402994; -.
DR KEGG; ztr:MYCGRDRAFT_102352; -.
DR eggNOG; KOG3565; Eukaryota.
DR HOGENOM; CLU_015390_1_0_1; -.
DR InParanoid; F9WWH7; -.
DR OMA; YADGWWE; -.
DR OrthoDB; 4260488at2759; -.
DR Proteomes; UP000008062; Chromosome 1.
DR GO; GO:0030479; C:actin cortical patch; IEA:EnsemblFungi.
DR GO; GO:0106006; F:cytoskeletal protein-membrane anchor activity; IEA:EnsemblFungi.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0034314; P:Arp2/3 complex-mediated actin nucleation; IEA:EnsemblFungi.
DR GO; GO:0072583; P:clathrin-dependent endocytosis; IEA:EnsemblFungi.
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; 1.
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; 1.
DR SUPFAM; SSF103657; BAR/IMD domain-like; 1.
DR SUPFAM; SSF57889; Cysteine-rich domain; 1.
DR SUPFAM; SSF50044; SH3-domain; 1.
DR PROSITE; PS51741; F_BAR; 1.
DR PROSITE; PS50002; SH3; 1.
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:UP000008062};
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 565..628
FT /note="SH3"
FT /evidence="ECO:0000259|PROSITE:PS50002"
FT REGION 468..563
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 616..649
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 475..521
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 535..550
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT NON_TER 649
FT /evidence="ECO:0000313|EMBL:EGP91202.1"
SQ SEQUENCE 649 AA; 71203 MW; C48BC9C4C183F3C2 CRC64;
MAELEVNPQL GIELKDGFKP VNAWVGGGIA WLDDMQQFYR ERSAIEKEYS QKLSALAKKY
FEKKAKKTSG LSVGDTPTVT PGSLESASMT TWTVQLTTLE NRAAEHDRFS NQLVSSLAEP
LKHLGLKYED LRKQHAEYAS KLEKERDANY ADLRKAKSKY DSVCQEVENR RKKTESSFDH
GKAKAQTAFQ QQQGEMRNAK NLYLIAINVT NKQKERYYHE YVPELIDSLQ ALAETKTAAL
NNLWSTAASL ETQVLTRSTQ LLEHLSTEIP RNNPVLDSMM FVRHNASPWQ DPPDFAFEPS
PVWLDDDVMA SDPMSKTFLM NILVKSRAQM GDFKRESDMK RREVDGAKRV RQAIREGKDK
RDEVEVVRSQ FVHQSALHEA ERKRISAEVE VSTILAGVGD VSVGARNHTF KNQTYKIPTS
CDLCGDRLWG LNAKGMNCEE CGFTCHTKCE LKVPADCPGE LTKEQKKAVK AQRQAAAQAQ
ASAPAAAQNG HSHGSAAPGL QRSDTMGSMN TLSSGYAASA KRSVSGMTID ESGPPPAAAG
PPPINRPRVM APPPSQYLTS NGGAAEEQHG KMLYTYQANG EGEISITEGQ SFILVEPDDG
SGWIKVRPTS FGAVPGLVPS SYAELAPPAP PSKPPLGDDR PTSAAASAS
//
