ID L8G8J3_PSED2 Unreviewed; 732 AA.
AC L8G8J3;
DT 03-APR-2013, integrated into UniProtKB/TrEMBL.
DT 03-APR-2013, sequence version 1.
DT 27-MAR-2024, entry version 60.
DE RecName: Full=Actin polymerization protein Bzz1 {ECO:0008006|Google:ProtNLM};
GN ORFNames=GMDG_04045 {ECO:0000313|EMBL:ELR09550.1};
OS Pseudogymnoascus destructans (strain ATCC MYA-4855 / 20631-21) (Bat
OS white-nose syndrome fungus) (Geomyces destructans).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC Leotiomycetes incertae sedis; Pseudeurotiaceae; Pseudogymnoascus.
OX NCBI_TaxID=658429 {ECO:0000313|EMBL:ELR09550.1, ECO:0000313|Proteomes:UP000011064};
RN [1] {ECO:0000313|Proteomes:UP000011064}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC MYA-4855 / 20631-21 {ECO:0000313|Proteomes:UP000011064};
RG The Broad Institute Genome Sequencing Platform;
RA Cuomo C.A., Blehert D.S., Lorch J.M., Young S.K., Zeng Q., Gargeya S.,
RA Fitzgerald M., Haas B., Abouelleil A., Alvarado L., Arachchi H.M.,
RA Berlin A., Brown A., Chapman S.B., Chen Z., Dunbar C., Freedman E.,
RA Gearin G., Gellesch M., Goldberg J., Griggs A., Gujja S., Heiman D.,
RA Howarth C., Larson L., Lui A., MacDonald P.J.P., Montmayeur A., Murphy C.,
RA Neiman D., Pearson M., Priest M., Roberts A., Saif S., Shea T., Shenoy N.,
RA Sisk P., Stolte C., Sykes S., Wortman J., Nusbaum C., Birren B.;
RT "The genome sequence of Geomyces destructans 20631-21.";
RL Submitted (SEP-2010) to the EMBL/GenBank/DDBJ databases.
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DR EMBL; GL573238; ELR09550.1; -; Genomic_DNA.
DR RefSeq; XP_012742464.1; XM_012887010.1.
DR AlphaFoldDB; L8G8J3; -.
DR STRING; 658429.L8G8J3; -.
DR VEuPathDB; FungiDB:GMDG_04045; -.
DR HOGENOM; CLU_015390_1_0_1; -.
DR InParanoid; L8G8J3; -.
DR OrthoDB; 4260488at2759; -.
DR Proteomes; UP000011064; 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:UP000011064};
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 575..635
FT /note="SH3"
FT /evidence="ECO:0000259|PROSITE:PS50002"
FT DOMAIN 674..732
FT /note="SH3"
FT /evidence="ECO:0000259|PROSITE:PS50002"
FT REGION 455..579
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 636..663
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 139..202
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 457..477
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 495..537
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 559..573
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 640..660
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 732 AA; 80799 MW; F4FC5570F2C702C9 CRC64;
MADVQIAPSF GAELKDAFKP VNSWVSQGIS WLDDIQQFYR ERSVIEKEYG AKLNVLAKKY
FEKKAKKSGS LSVGDTPAMT PGSLESASLT TWTTQLTTLE SRAAEHDRYG NELVQNVAEP
LRNLGLRYED IRKRHADYAD KLEKERDSTY SDLKKTKAKY DAACQEVENK RKKSESAFDY
SKAKAQNSYQ QQLLEMNNAK NTYLIAIRAM NKQKEMYYHE YVPDVLDGLQ DLNEARTAKL
NGLWSLAASL ELGMIKRSTD IINYLAQEIP RNIPTLDTMM FVRHNAAPWQ EPVNKTFEPS
PVWHDDDSMI VDEPAKVFLR NMLNKSKGQL GDLRRDVDMR RKEVEGLKRV QQAVREGKDK
RDEVVVWSQL LMAQENLHDS DHKRLNVEVE TTTITTTIGD LTIGAKNHNF KSQTFKIPTN
CDLCGERIWG LSAKGFDCRD CGYTCHSKCE MKVPAECPGE QSKDEKKKLK ASRQEDAGHG
RAPSVAGNGD MPSGLPTPLS RSNTMNSLSS GYAASANRSV TRGGPQSPTT EPQLPDRSSK
PAGTLRKARL VAPPPTSYIS ELPGSSANGA SGVRSSEPRG KMVYAYDASG EGEISVGEGD
EVTITEPDDG SGWVKVKSGF GEGLVPGSYL EMMPSPSPAL SARPASTYSN SGSSVAGSVS
KKQGPVVAPK RGARKLRYVE ALYDYTAQSD AEHNMLEGDR FVLVKKDPGD GWSEVERGGV
TKSVPASYVQ LV
//
