GenomeNet

Database: UniProt
Entry: S3E0Z8_GLAL2
LinkDB: S3E0Z8_GLAL2
Original site: S3E0Z8_GLAL2 
ID   S3E0Z8_GLAL2            Unreviewed;       946 AA.
AC   S3E0Z8;
DT   18-SEP-2013, integrated into UniProtKB/TrEMBL.
DT   18-SEP-2013, sequence version 1.
DT   27-MAR-2024, entry version 43.
DE   SubName: Full=DBL homology (DH-domain) {ECO:0000313|EMBL:EPE32188.1};
GN   ORFNames=GLAREA_07321 {ECO:0000313|EMBL:EPE32188.1};
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:EPE32188.1, ECO:0000313|Proteomes:UP000016922};
RN   [1] {ECO:0000313|EMBL:EPE32188.1, 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; KE145359; EPE32188.1; -; Genomic_DNA.
DR   RefSeq; XP_008080200.1; XM_008082009.1.
DR   AlphaFoldDB; S3E0Z8; -.
DR   STRING; 1116229.S3E0Z8; -.
DR   GeneID; 19466374; -.
DR   KEGG; glz:GLAREA_07321; -.
DR   eggNOG; KOG3519; Eukaryota.
DR   HOGENOM; CLU_007879_0_0_1; -.
DR   OMA; QPIYPRQ; -.
DR   OrthoDB; 23973at2759; -.
DR   Proteomes; UP000016922; Unassembled WGS sequence.
DR   GO; GO:0005085; F:guanyl-nucleotide exchange factor activity; IEA:InterPro.
DR   CDD; cd05992; PB1; 1.
DR   CDD; cd00160; RhoGEF; 1.
DR   Gene3D; 1.20.900.10; Dbl homology (DH) domain; 1.
DR   Gene3D; 2.30.29.30; Pleckstrin-homology domain (PH domain)/Phosphotyrosine-binding domain (PTB); 1.
DR   InterPro; IPR035899; DBL_dom_sf.
DR   InterPro; IPR000219; DH-domain.
DR   InterPro; IPR000270; PB1_dom.
DR   InterPro; IPR011993; PH-like_dom_sf.
DR   PANTHER; PTHR47339; CELL DIVISION CONTROL PROTEIN 24; 1.
DR   PANTHER; PTHR47339:SF1; CELL DIVISION CONTROL PROTEIN 24; 1.
DR   Pfam; PF00564; PB1; 1.
DR   Pfam; PF15411; PH_10; 1.
DR   Pfam; PF00621; RhoGEF; 1.
DR   SMART; SM00325; RhoGEF; 1.
DR   SUPFAM; SSF54277; CAD & PB1 domains; 1.
DR   SUPFAM; SSF48065; DBL homology domain (DH-domain); 1.
DR   SUPFAM; SSF50729; PH domain-like; 1.
DR   PROSITE; PS50010; DH_2; 1.
DR   PROSITE; PS51745; PB1; 1.
PE   4: Predicted;
KW   Coiled coil {ECO:0000256|SAM:Coils};
KW   Reference proteome {ECO:0000313|Proteomes:UP000016922}.
FT   DOMAIN          81..256
FT                   /note="DH"
FT                   /evidence="ECO:0000259|PROSITE:PS50010"
FT   DOMAIN          846..944
FT                   /note="PB1"
FT                   /evidence="ECO:0000259|PROSITE:PS51745"
FT   REGION          442..461
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          561..623
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          637..841
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          236..279
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COMPBIAS        576..609
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        652..682
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        694..747
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        779..837
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   946 AA;  105755 MW;  A70E0AFD2CD37CE3 CRC64;
     MFQHAMSRFS VSSPDLQSEL AIQQTAVKNK FRRLKKNVRK QVTQVVNKVL DNSEARGLLV
     ASTTNVPLTS APLPSGAQKS YRDYVVAELV DTERKYVQDL ENLHELKKKI EQKGVIPGDV
     VHDIFLNINA ILDFQRRFLI KIETTNSQPD DQQAWGLPFT NYEESFNIYR PFIANQRKAA
     DIAKRDFDKI VLADHPVVVD FNTLDGFLLK PMQRLVKYPM LLKDLRDKTN ADDATKEDLT
     AGIEAANRVL KEANDAVDQE LLREAREDME SRVEDWKNHQ IEQFGDLLLY GHFPVVNGKS
     DGQKEVRTLT SPLSSSNVQK FASLRLFRDS TTRKALDSTE RQNISSLEQS AEDAQSEALL
     ALDQKSHGND QRQLTNDDTF LFNMLFDQFS GCDPETGAPI FAKRFADSMG ITAPTYEQYT
     IYLFERILLC CKEINPNKSK DKVMGIQKDK KDKNKSKEPN KNAKLQLKGR IFMTNVTDVI
     ALGKQGSYTV QIFWKGDPGV ENFIIRFSNE DAMKKWHAGV DGQRKLHAQA ISAGFSPEGG
     PPTDFAWMRD QTAAMINPYA QHEDDDDEDD YRAQNSMYPG QMNQGMPRNG SSTSLRSRST
     TSDSSQSLAG IARAPPPRFP MGFANQPLSI QTQINPAQSP GQRMGDSYFS PVAETPATSR
     SSTQSNMFPF PRQGTPQGSW EEHNRYTAPA MPRAPSRGSQ TPSDAYGMNG RTPQRPSLPA
     MASQSSQASA NLQRSRSHST PDINVQNGVR RLPNGAVSGP VPAVPGIPAH LHPAYDAGIP
     RSQNNSPNGL PMRSNTQSPG TQRERMGTPT QYPNGPSHYS RSNISHRPDT SESRTMSPPL
     GEAALPTQLK VKVNCDQQYI TLVVAFNITY QSLIDRIDAK IGRFSNNAIA KGTMRLRYRD
     EDGDFVTIES DDDIQIAFQE WREAQKAQYH AGLLGEIELF CISVEN
//
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