ID C9S6B5_VERA1 Unreviewed; 696 AA.
AC C9S6B5;
DT 24-NOV-2009, integrated into UniProtKB/TrEMBL.
DT 24-NOV-2009, sequence version 1.
DT 27-MAR-2024, entry version 78.
DE SubName: Full=BZZ1 {ECO:0000313|EMBL:EEY14427.1};
GN ORFNames=VDBG_00535 {ECO:0000313|EMBL:EEY14427.1};
OS Verticillium alfalfae (strain VaMs.102 / ATCC MYA-4576 / FGSC 10136)
OS (Verticillium wilt of alfalfa) (Verticillium albo-atrum).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Glomerellales; Plectosphaerellaceae; Verticillium.
OX NCBI_TaxID=526221 {ECO:0000313|Proteomes:UP000008698};
RN [1] {ECO:0000313|Proteomes:UP000008698}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=VaMs.102 / ATCC MYA-4576 / FGSC 10136
RC {ECO:0000313|Proteomes:UP000008698};
RX PubMed=21829347; DOI=10.1371/journal.ppat.1002137;
RA Klosterman S.J., Subbarao K.V., Kang S., Veronese P., Gold S.E.,
RA Thomma B.P.H.J., Chen Z., Henrissat B., Lee Y.-H., Park J.,
RA Garcia-Pedrajas M.D., Barbara D.J., Anchieta A., de Jonge R., Santhanam P.,
RA Maruthachalam K., Atallah Z., Amyotte S.G., Paz Z., Inderbitzin P.,
RA Hayes R.J., Heiman D.I., Young S., Zeng Q., Engels R., Galagan J.,
RA Cuomo C.A., Dobinson K.F., Ma L.-J.;
RT "Comparative genomics yields insights into niche adaptation of plant
RT vascular wilt pathogens.";
RL PLoS Pathog. 7:E1002137-E1002137(2011).
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DR EMBL; DS985214; EEY14427.1; -; Genomic_DNA.
DR RefSeq; XP_003008853.1; XM_003008807.1.
DR AlphaFoldDB; C9S6B5; -.
DR STRING; 526221.C9S6B5; -.
DR GeneID; 9529208; -.
DR KEGG; val:VDBG_00535; -.
DR eggNOG; KOG3565; Eukaryota.
DR HOGENOM; CLU_015390_1_0_1; -.
DR OMA; YADGWWE; -.
DR OrthoDB; 4260488at2759; -.
DR Proteomes; UP000008698; 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; 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; FCH AND DOUBLE SH3 DOMAINS PROTEIN; 1.
DR PANTHER; PTHR15735:SF20; PROTEIN NERVOUS WRECK; 1.
DR Pfam; PF00130; C1_1; 1.
DR Pfam; PF00611; FCH; 1.
DR Pfam; PF14604; SH3_9; 2.
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; 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:UP000008698};
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 349..402
FT /note="Phorbol-ester/DAG-type"
FT /evidence="ECO:0000259|PROSITE:PS50081"
FT DOMAIN 530..590
FT /note="SH3"
FT /evidence="ECO:0000259|PROSITE:PS50002"
FT DOMAIN 638..696
FT /note="SH3"
FT /evidence="ECO:0000259|PROSITE:PS50002"
FT REGION 399..500
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 512..533
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 602..630
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 139..184
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 402..418
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 425..471
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 519..533
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 603..620
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 696 AA; 76522 MW; 0C63B385018094E1 CRC64;
MAEVDALPTF GAELKDGFKP ANAWVGHGIT WLEDIQQFYR ERSAIEKEYS GKLNALAKKY
FEKKNKKTAA LSVGDTPTMT PGSLESASLT TWTTQLTTLE NRADQHDRYA NNLVSQVAEP
LRFLGTRFEE LRKRHADFAA KLEAERDAQY ADLRKVKAKY DASCQEVESK RKKAESSYDK
AKAQSSYQQH IYDMNNVKNT YLIAINVTNK QKEQYYHEYI PEVMDSLQDL SEFRTVKLNG
LWTVASQLEA GLLQQGHGLM ETLTSEITRN QPHLDSMMYM QHNVGTWQEP ADKTFEPSPV
WHDDDLMVVD EFAKVFLRNV LGKSKGQLGD LRREVDKKRR EVEGVKTLKQ RVRSGAEKKD
EIPTNCDLCG ERIWGLSAKG FDCRDCGYTC HSKCEMKVPA DCPGEQTKED RKKLKAERQG
AANALLKPSN GTSGHTAELP SLSRTNTMNS LSSGYAHSAQ RSVSGSISGP RSPIDETPPP
VEPTSPRPTT AAASTVSTAT VRKNRIMAPP PTAYVSELPG SAPNGSSSSA DHQSGKMLYG
FEASGDGELS VAEGREVILL EPDDGSGWLK VRAGYKEGLV PATYVEIMAA PTPAPVIAQH
TGASGRPDST YSNSGSSVGT AGMAKKKGPA VAPRRGAKKL KYVEAIYEYT AQSDTEHSMV
EGERFVLIKE DPGDGWAEVE KGGQIKSVPA SYVQVV
//
