ID A0A0D2K7I3_9EURO Unreviewed; 947 AA.
AC A0A0D2K7I3;
DT 29-APR-2015, integrated into UniProtKB/TrEMBL.
DT 29-APR-2015, sequence version 1.
DT 27-MAR-2024, entry version 46.
DE RecName: Full=DH domain-containing protein {ECO:0008006|Google:ProtNLM};
GN ORFNames=Z520_02076 {ECO:0000313|EMBL:KIY01938.1};
OS Fonsecaea multimorphosa CBS 102226.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Chaetothyriomycetidae; Chaetothyriales; Herpotrichiellaceae; Fonsecaea.
OX NCBI_TaxID=1442371 {ECO:0000313|EMBL:KIY01938.1, ECO:0000313|Proteomes:UP000053411};
RN [1] {ECO:0000313|EMBL:KIY01938.1, ECO:0000313|Proteomes:UP000053411}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 102226 {ECO:0000313|EMBL:KIY01938.1,
RC ECO:0000313|Proteomes:UP000053411};
RG The Broad Institute Genomics Platform;
RA Cuomo C., de Hoog S., Gorbushina A., Stielow B., Teixiera M.,
RA Abouelleil A., Chapman S.B., Priest M., Young S.K., Wortman J., Nusbaum C.,
RA Birren B.;
RT "The Genome Sequence of Fonsecaea multimorphosa CBS 102226.";
RL Submitted (JAN-2015) to the EMBL/GenBank/DDBJ databases.
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DR EMBL; KN848064; KIY01938.1; -; Genomic_DNA.
DR RefSeq; XP_016636060.1; XM_016772590.1.
DR AlphaFoldDB; A0A0D2K7I3; -.
DR STRING; 1442371.A0A0D2K7I3; -.
DR GeneID; 27707822; -.
DR VEuPathDB; FungiDB:Z520_02076; -.
DR OrthoDB; 23973at2759; -.
DR Proteomes; UP000053411; Unassembled WGS sequence.
DR GO; GO:0005085; F:guanyl-nucleotide exchange factor activity; IEA:InterPro.
DR CDD; cd00014; CH_SF; 1.
DR CDD; cd05992; PB1; 1.
DR CDD; cd13246; PH_Scd1; 1.
DR CDD; cd00160; RhoGEF; 1.
DR Gene3D; 1.10.418.10; Calponin-like domain; 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; IPR010481; Cdc24/Scd1_N.
DR InterPro; IPR033511; Cdc24/Scd1_PH_dom.
DR InterPro; IPR036872; CH_dom_sf.
DR InterPro; IPR035899; DBL_dom_sf.
DR InterPro; IPR000219; DH-domain.
DR InterPro; IPR000270; PB1_dom.
DR InterPro; IPR011993; PH-like_dom_sf.
DR InterPro; IPR001849; PH_domain.
DR PANTHER; PTHR47339; CELL DIVISION CONTROL PROTEIN 24; 1.
DR PANTHER; PTHR47339:SF1; CELL DIVISION CONTROL PROTEIN 24; 1.
DR Pfam; PF06395; CDC24; 1.
DR Pfam; PF00564; PB1; 1.
DR Pfam; PF15411; PH_10; 1.
DR Pfam; PF00621; RhoGEF; 1.
DR SMART; SM00233; PH; 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; PS50003; PH_DOMAIN; 1.
PE 4: Predicted;
KW Glycosyltransferase {ECO:0000256|ARBA:ARBA00022676};
KW Reference proteome {ECO:0000313|Proteomes:UP000053411};
KW Transferase {ECO:0000256|ARBA:ARBA00022676}.
FT DOMAIN 189..368
FT /note="DH"
FT /evidence="ECO:0000259|PROSITE:PS50010"
FT DOMAIN 398..519
FT /note="PH"
FT /evidence="ECO:0000259|PROSITE:PS50003"
FT REGION 161..186
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 548..606
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 619..838
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 560..605
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 621..635
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 643..665
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 673..718
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 760..786
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 823..838
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 947 AA; 105101 MW; FDACBFB209C950A5 CRC64;
MLASPPIMNG DHGPMLDKNN IINVRDGESL YQICIKLRRR LSGVPGFRPY LEEMEEREAD
GSTDPVSSLW QCFRSGLPLL TIYNASNPEE GDLTVDTSRP DRVGKEAAFL FIKSCMQQMN
IPAADTFTVT DLYSDNTTGF VKVTKLVNRV LDMLKLSGKL HPSTDSEDSR DGVDAGSNAP
EQTPKTMTRR QYILRELVET ERQYVHHLQN LQALKKELEE VGALTGDAIH NIFLNLNNLL
DFAQRFLIRI EQQNEMPEEQ QNWGRLFVHY RDPFRQYEPF IANQRRCEAT CQQEWDRMVA
TARSPLTQQM LANPTILNGF LLKPFQRLTK YPLLLKDLLN QIEDPTLKSD LSSAIAIIQD
VLMQADASID KETRDDALQD LQERIDDWKQ LQIGALGELL LMGTFNVMKE SAIRSDEKEY
HIYLFSRILV MCKDVNANKP KNRLANNKPA LSLRGKPKMN LKGRIYFANV TQVIPSTSPG
NYTLQISWKG ESGIETFNIK FKNDDTLQKW HNLIETQRSA CMLESKTRGI SETHLLSLQG
ANLENPYLAQ DEDEDYNRLS GTTYGGTDAN GYSEFNMSRN ASSTSLRSRS ATGGSGGSGP
QMSANRMRVP TGEIGALSLN TRGLPTASPQ EFNGGSYFSP IDRDTPPGST ISARSSSQSA
FAGYHRGTTP VSGGMHPTES HRNTAPAMAR NPNGQSGNPY LANGRSRGQS SGPGMQAPRM
RSASSPDVHP MVQQGRKYTS TEHVPTVPPI PAHMAKQMAP PNRSLNNSPS NAPPSRGGTP
HQQQFGLPSA PRPAMPGHGY SFDPHYSNDP RRPGHVPSLS QGRAFSPPVS SPSSDGDPYI
PSQLKAKVCF DENYVSMIIA SNIQFRSLAD RIDAKLARFT NHSIASGSVR LRYRDEDGDF
ILIDSDEAVH EALLDWRETH VVNSANPQNA ELLLFAHAAH GESIVNG
//
