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Database: UniProt
Entry: S3DL65_GLAL2
LinkDB: S3DL65_GLAL2
Original site: S3DL65_GLAL2 
ID   S3DL65_GLAL2            Unreviewed;       732 AA.
AC   S3DL65;
DT   18-SEP-2013, integrated into UniProtKB/TrEMBL.
DT   18-SEP-2013, sequence version 1.
DT   24-JAN-2024, entry version 53.
DE   SubName: Full=Cysteine-rich {ECO:0000313|EMBL:EPE27273.1};
GN   ORFNames=GLAREA_03188 {ECO:0000313|EMBL:EPE27273.1};
OS   Glarea lozoyensis (strain ATCC 20868 / MF5171).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC   Helotiales; Helotiaceae; Glarea.
OX   NCBI_TaxID=1116229 {ECO:0000313|EMBL:EPE27273.1, ECO:0000313|Proteomes:UP000016922};
RN   [1] {ECO:0000313|EMBL:EPE27273.1, ECO:0000313|Proteomes:UP000016922}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 20868 / MF5171 {ECO:0000313|Proteomes:UP000016922};
RX   PubMed=23688303; DOI=10.1186/1471-2164-14-339;
RA   Chen L., Yue Q., Zhang X., Xiang M., Wang C., Li S., Che Y.,
RA   Ortiz-Lopez F.J., Bills G.F., Liu X., An Z.;
RT   "Genomics-driven discovery of the pneumocandin biosynthetic gene cluster in
RT   the fungus Glarea lozoyensis.";
RL   BMC Genomics 14:339-339(2013).
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DR   EMBL; KE145370; EPE27273.1; -; Genomic_DNA.
DR   RefSeq; XP_008086463.1; XM_008088272.1.
DR   AlphaFoldDB; S3DL65; -.
DR   STRING; 1116229.S3DL65; -.
DR   GeneID; 19462243; -.
DR   KEGG; glz:GLAREA_03188; -.
DR   eggNOG; KOG3565; Eukaryota.
DR   HOGENOM; CLU_015390_1_0_1; -.
DR   OrthoDB; 4260488at2759; -.
DR   Proteomes; UP000016922; 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; FCH AND DOUBLE SH3 DOMAINS PROTEIN; 1.
DR   PANTHER; PTHR15735:SF21; PROTEIN NERVOUS WRECK; 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   Coiled coil {ECO:0000256|ARBA:ARBA00023054, ECO:0000256|PROSITE-
KW   ProRule:PRU01077}; Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Reference proteome {ECO:0000313|Proteomes:UP000016922};
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          577..636
FT                   /note="SH3"
FT                   /evidence="ECO:0000259|PROSITE:PS50002"
FT   DOMAIN          674..732
FT                   /note="SH3"
FT                   /evidence="ECO:0000259|PROSITE:PS50002"
FT   REGION          457..580
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          323..350
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COMPBIAS        457..475
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        477..524
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   732 AA;  80989 MW;  CF5654BD43EA947C CRC64;
     MADVDIAPNF GLELKDGFKP VNAWVSNGIT WLDDIQQFYR ERSAIEKEYS AKLNTLAKKY
     YEKKAKKSSS LSVGDTPALT PGSLESASLT TWTTQLTTLE SRAAEHDRYG GELISQLADP
     LKHIATRFEE LRKRHADFAA KLEAERDGTY ADLRKTKGKY DATCQEVENK RKKAESAFDY
     SKSKAQNAYQ QQILEMHNVK NTYLIAINVT NKQKERYYHE YVPDLLDSLQ DLSESRTAKL
     NGIWALAAQL ELGMLKRSTD FVNHLAQEIP RNQPVLDSMM FVRHNAAGWQ EPPNKQFEPS
     PVWHDDGAMM VDDTAKVFLR NVLSKSKGQL GELRREVDKK RREVEGAKRV KQQIREGKDK
     RDEVEVVKAI FALQENLHEV DHKRLTAEVE TITITEAVGD VTLGAKSHNF KSQTFKIPTN
     CDLCGERIWG LSAKGFDCRD CGYTCHSKCE MKVPAECPGE QTKEERKKLK AERQEAANSL
     KSPTHQPGDS VAELPTMSRT NTMNSLSSGY AASAHRSVSG SGPRSPADET PPERPTSAKP
     SISGPTTLRK NRVVAPPPST YVSELPGSAP NGSGAASSDP KGKMLYAYDA NGDGEVTVAE
     GKEVTILEPD DGGWTKVKVG YKEGLVPTAY IEILPMATLA PRPSSIYSNS GSSMSSSIQG
     KKQGPVVAPR RGAKKLKYVE ALYEYSAQSD AEHSMTEGER FVLIKEDPGD GWAEVERNGV
     TKSVPANYVQ AV
//
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