ID C1GZ37_PARBA Unreviewed; 753 AA.
AC C1GZ37;
DT 26-MAY-2009, integrated into UniProtKB/TrEMBL.
DT 04-FEB-2015, sequence version 2.
DT 27-MAR-2024, entry version 89.
DE RecName: Full=Actin polymerization protein Bzz1 {ECO:0008006|Google:ProtNLM};
GN ORFNames=PAAG_03781 {ECO:0000313|EMBL:EEH41860.2};
OS Paracoccidioides lutzii (strain ATCC MYA-826 / Pb01) (Paracoccidioides
OS brasiliensis).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Onygenales; Onygenales incertae sedis; Paracoccidioides.
OX NCBI_TaxID=502779 {ECO:0000313|EMBL:EEH41860.2, ECO:0000313|Proteomes:UP000002059};
RN [1] {ECO:0000313|EMBL:EEH41860.2, ECO:0000313|Proteomes:UP000002059}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC MYA-826 / Pb01 {ECO:0000313|Proteomes:UP000002059};
RX PubMed=22046142; DOI=10.1371/journal.pgen.1002345;
RA Desjardins C.A., Champion M.D., Holder J.W., Muszewska A., Goldberg J.,
RA Bailao A.M., Brigido M.M., Ferreira M.E., Garcia A.M., Grynberg M.,
RA Gujja S., Heiman D.I., Henn M.R., Kodira C.D., Leon-Narvaez H.,
RA Longo L.V.G., Ma L.-J., Malavazi I., Matsuo A.L., Morais F.V., Pereira M.,
RA Rodriguez-Brito S., Sakthikumar S., Salem-Izacc S.M., Sykes S.M.,
RA Teixeira M.M., Vallejo M.C., Walter M.E., Yandava C., Young S., Zeng Q.,
RA Zucker J., Felipe M.S., Goldman G.H., Haas B.J., McEwen J.G., Nino-Vega G.,
RA Puccia R., San-Blas G., Soares C.M., Birren B.W., Cuomo C.A.;
RT "Comparative genomic analysis of human fungal pathogens causing
RT paracoccidioidomycosis.";
RL PLoS Genet. 7:E1002345-E1002345(2011).
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DR EMBL; KN294000; EEH41860.2; -; Genomic_DNA.
DR RefSeq; XP_015702152.1; XM_015845063.1.
DR AlphaFoldDB; C1GZ37; -.
DR STRING; 502779.C1GZ37; -.
DR GeneID; 9097623; -.
DR KEGG; pbl:PAAG_03781; -.
DR VEuPathDB; FungiDB:PAAG_03781; -.
DR eggNOG; KOG3565; Eukaryota.
DR HOGENOM; CLU_015390_1_0_1; -.
DR OMA; YADGWWE; -.
DR OrthoDB; 4260488at2759; -.
DR Proteomes; UP000002059; Partially assembled 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:UP000002059};
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 589..649
FT /note="SH3"
FT /evidence="ECO:0000259|PROSITE:PS50002"
FT DOMAIN 695..753
FT /note="SH3"
FT /evidence="ECO:0000259|PROSITE:PS50002"
FT REGION 457..601
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 649..690
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 728..753
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 121..148
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 323..350
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 457..474
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 499..527
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 649..677
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 753 AA; 83471 MW; CF3A0C2C1BF49B27 CRC64;
MADVDSSVQF GSELKDAFKP INAWVSNGIG WLDEIQQFYR ERSAIEKEYA TKLTALCRKY
HERKAKKSSS LSVGDTPTLT PGSLECASLT TWSTQLTAIE AEAAERDRFG SDLVYQVAEP
LKQAAARFEE LRRNHAEYAS KLEKEQEATY SDLKKVKGRY DGTCQEVENR RKKTESAFDH
GKHKAQVAYQ QQILEMNNVK NTYLISINVT NKLKEKYYYE YVPELLNGLQ DLNETRVAKL
NSIWLLAAQL EKSTLAKSEE HISHLISEIP RNEPRLDSTM FVRHNMSNWQ DPADIQFEPS
PIWHDDATMV TDETAKIFLQ NILTRSKAQA KELKVEADKK RREVEKAKRI RQSVRDGKDK
RDEAEVVRSI FAMQEDLHLL DRKRLTAEVE TSTITSVVGD LSFGARSHNF RSQTFKIPTN
CDLCGERIWG LSAKGFDCRD CGYTCHSKCE MKVPAECPGE QNKEEKKKLK IERQEAAGSG
TAIDLPMSPN GASEPPALSR RDTMNSLSSG YAASTARSTS VVLNPQTTEA GAVEVPESLP
AATKSATKPS IGARRNRIVA PPPAQYVSAP PPPSEEAESG GRAGFSPKSN EPRGKMLYPY
DANGEDEITV GEGREVIIVE PDDGSGWMRV RAGTRSGLVP ASYVETMSTP YSSVSTSPNL
PKRPGSAYST SSASLAGSAG GKRRGPAVTP KRGAKKLQYV VALYAYEARS DAEWSMEEGD
RFVLVNRDSG NGWSDVEKGG QTKSVPANYI EEV
//
