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Database: UniProt
Entry: B6K6X9_SCHJY
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ID   B6K6X9_SCHJY            Unreviewed;       658 AA.
AC   B6K6X9;
DT   16-DEC-2008, integrated into UniProtKB/TrEMBL.
DT   16-OCT-2013, sequence version 2.
DT   27-MAR-2024, entry version 85.
DE   SubName: Full=Diacylglycerol binding protein Bzz1 {ECO:0000313|EMBL:EEB09283.2};
GN   Name=bzz1 {ECO:0000313|JaponicusDB:SJAG_04479};
GN   ORFNames=SJAG_04479 {ECO:0000313|EMBL:EEB09283.2};
OS   Schizosaccharomyces japonicus (strain yFS275 / FY16936) (Fission yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina;
OC   Schizosaccharomycetes; Schizosaccharomycetales; Schizosaccharomycetaceae;
OC   Schizosaccharomyces.
OX   NCBI_TaxID=402676 {ECO:0000313|EMBL:EEB09283.2, ECO:0000313|Proteomes:UP000001744};
RN   [1] {ECO:0000313|EMBL:EEB09283.2, ECO:0000313|Proteomes:UP000001744}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=yFS275 / FY16936 {ECO:0000313|Proteomes:UP000001744};
RX   PubMed=21511999; DOI=10.1126/science.1203357;
RA   Rhind N., Chen Z., Yassour M., Thompson D.A., Haas B.J., Habib N.,
RA   Wapinski I., Roy S., Lin M.F., Heiman D.I., Young S.K., Furuya K., Guo Y.,
RA   Pidoux A., Chen H.M., Robbertse B., Goldberg J.M., Aoki K., Bayne E.H.,
RA   Berlin A.M., Desjardins C.A., Dobbs E., Dukaj L., Fan L., FitzGerald M.G.,
RA   French C., Gujja S., Hansen K., Keifenheim D., Levin J.Z., Mosher R.A.,
RA   Mueller C.A., Pfiffner J., Priest M., Russ C., Smialowska A., Swoboda P.,
RA   Sykes S.M., Vaughn M., Vengrova S., Yoder R., Zeng Q., Allshire R.,
RA   Baulcombe D., Birren B.W., Brown W., Ekwall K., Kellis M., Leatherwood J.,
RA   Levin H., Margalit H., Martienssen R., Nieduszynski C.A., Spatafora J.W.,
RA   Friedman N., Dalgaard J.Z., Baumann P., Niki H., Regev A., Nusbaum C.;
RT   "Comparative functional genomics of the fission yeasts.";
RL   Science 332:930-936(2011).
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DR   EMBL; KE651168; EEB09283.2; -; Genomic_DNA.
DR   RefSeq; XP_002175576.2; XM_002175540.2.
DR   AlphaFoldDB; B6K6X9; -.
DR   STRING; 402676.B6K6X9; -.
DR   EnsemblFungi; EEB09283; EEB09283; SJAG_04479.
DR   GeneID; 7051839; -.
DR   JaponicusDB; SJAG_04479; bzz1.
DR   VEuPathDB; FungiDB:SJAG_04479; -.
DR   eggNOG; KOG3565; Eukaryota.
DR   HOGENOM; CLU_015390_1_0_1; -.
DR   OMA; TPMMEEP; -.
DR   OrthoDB; 4260488at2759; -.
DR   Proteomes; UP000001744; Unassembled WGS sequence.
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   GO; GO:0030833; P:regulation of actin filament polymerization; IBA:GO_Central.
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   PRINTS; PR00452; SH3DOMAIN.
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   Coiled coil {ECO:0000256|ARBA:ARBA00023054, ECO:0000256|PROSITE-
KW   ProRule:PRU01077}; Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001744};
KW   SH3 domain {ECO:0000256|ARBA:ARBA00022443, ECO:0000256|PROSITE-
KW   ProRule:PRU00192}; Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT   DOMAIN          6..272
FT                   /note="F-BAR"
FT                   /evidence="ECO:0000259|PROSITE:PS51741"
FT   DOMAIN          398..448
FT                   /note="Phorbol-ester/DAG-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50081"
FT   DOMAIN          535..595
FT                   /note="SH3"
FT                   /evidence="ECO:0000259|PROSITE:PS50002"
FT   DOMAIN          600..658
FT                   /note="SH3"
FT                   /evidence="ECO:0000259|PROSITE:PS50002"
FT   REGION          471..494
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          508..534
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        471..487
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   658 AA;  73890 MW;  0FF607450CBD0116 CRC64;
     MSVESVSISA YIKDDYKTVD SWVQNGVKWL EELHQFYKER SLIEKEYSQK LASLAKKYFE
     KKNKRSSSLS IGDSPTSSAG SLECASLTTW TKILDGLTEE ARRIQNFSND LGSQISDQFL
     NLQGQAESMR RNQHGYYNSL LDERERIDAG VKKAKQDYYS SCEVLESARQ KKDKLGDDKS
     KRGYQDALTE MNNKKNGYVL TITEFNAHTK LYFSKLLPDV VDSLQQVNEF RVQKMNSLWK
     HSLHLEKSCY SDLSQKTDEL NNEINLNSPN LDTVMFVKHN QKNWTPPNDL PFEPSPIWHD
     TDSIATYDTN INYLRNMLIQ NRKDFETAAA SYESVMEESN KLEKAHSKSL LELPHAVVLK
     MAEVEQLKAR FQTRMHDLQS RIDLILNTAG ALDEGTQPHD FRHTSFALPT NCDYCKSTIW
     GLSKHGCVCK RCNYHCHARC EMKVPPECGK AEPLVSISRN ASLRRSNVGS ISSTNYANTT
     RSVENHGAGS MRNEEVDDFG NIAVSRATTN TSESQPSPFG DSSQTPADAA ATSAAENETV
     QVLYDYVGTT DDDLNVKEGQ MVVILQPDDG TGWVRARSGS AEGLVPASYL DLPGQASVAQ
     DESYVRALYD YTAQTDLEIS LQAGDVIRVI QRDSGNGWSE GELDGRIGQF PANYVEDI
//
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