ID W6ML79_9ASCO Unreviewed; 765 AA.
AC W6ML79;
DT 16-APR-2014, integrated into UniProtKB/TrEMBL.
DT 16-APR-2014, sequence version 1.
DT 13-SEP-2023, entry version 46.
DE RecName: Full=DH domain-containing protein {ECO:0008006|Google:ProtNLM};
GN ORFNames=KUCA_T00002832001 {ECO:0000313|EMBL:CDK26858.1};
OS Kuraishia capsulata CBS 1993.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetales incertae sedis; Kuraishia.
OX NCBI_TaxID=1382522 {ECO:0000313|EMBL:CDK26858.1};
RN [1] {ECO:0000313|EMBL:CDK26858.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=CBS 1993 {ECO:0000313|EMBL:CDK26858.1};
RA Genoscope - CEA;
RL Submitted (DEC-2013) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:CDK26858.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=CBS 1993 {ECO:0000313|EMBL:CDK26858.1};
RA Morales L., Noel B., Porcel B., Marcet-Houben M., Hullo M-F., Sacerdot C.,
RA Tekaia F., Leh-Louis V., Despons L., Khanna V., Aury J-M., Barbe V.,
RA Couloux A., Labadie K., Pelletier E., Souciet J-L., Boekhout T.,
RA Gabaldon T., Wincker P., Dujon B.;
RT "Complete DNA sequence of /Kuraishia capsulata/ illustrates novel genomic
RT features among budding yeasts (/Saccharomycotina/).";
RL Submitted (FEB-2014) to the EMBL/GenBank/DDBJ databases.
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DR EMBL; HG793127; CDK26858.1; -; Genomic_DNA.
DR AlphaFoldDB; W6ML79; -.
DR STRING; 1382522.W6ML79; -.
DR HOGENOM; CLU_007879_0_0_1; -.
DR OrthoDB; 23973at2759; -.
DR GO; GO:0005085; F:guanyl-nucleotide exchange factor activity; IEA:InterPro.
DR GO; GO:0035556; P:intracellular signal transduction; 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; IPR010481; Cdc24/Scd1_N.
DR InterPro; IPR035899; DBL_dom_sf.
DR InterPro; IPR000219; DH-domain.
DR InterPro; IPR001331; GDS_CDC24_CS.
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; PF06395; CDC24; 1.
DR Pfam; PF00564; PB1; 1.
DR Pfam; PF15411; PH_10; 1.
DR Pfam; PF00621; RhoGEF; 1.
DR SMART; SM00666; PB1; 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; PS00741; DH_1; 1.
DR PROSITE; PS50010; DH_2; 1.
DR PROSITE; PS51745; PB1; 1.
PE 4: Predicted;
FT DOMAIN 235..410
FT /note="DH"
FT /evidence="ECO:0000259|PROSITE:PS50010"
FT DOMAIN 674..765
FT /note="PB1"
FT /evidence="ECO:0000259|PROSITE:PS51745"
FT REGION 1..23
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 580..622
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 608..622
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 765 AA; 86033 MW; 030EA278E98C921A CRC64;
MSHMPGLKSA TSFSSSSSLA RTPSGPMVAA GLIMNKRADV NESLYYICQR LIAKLEKVPG
MKAYLNLAFS SAEECSEQQA MLLSQRPASS SSHHNSTSSL DSEISVRSKW DRTMLTFSAG
MLPAQINYDP VTPVWRLFQQ GVPLCLIFNS LKPEHSIPLV SSDDLKVCKM NVYRFLSCCK
QYLDIRDEDL FPITSVFADD TNNLLKVIKV VNSVLDLDPR FTAPEIEETY KVTDARSKVV
KELVESERKF VQDLETLLRY RDDVMKRELI SSEDLGILFP NLPEIVDFQR RFLVGLECNA
SVPEKYQRIG SVFLHAGVQG FKIYDPWSLL QTQAIDVIAR EAGNLKRSSS LIDASYELQS
FLIKPVQRLC KYPLLLQQLL KLTDSSWPNY NELEASLESS KEVAHNVNEA QRKSENVQLV
KDLQERVVDW RGHGLLNVGE LLFSNTVVVK DLLSDGPSSE KEVHCYMFEK IIYFFKEMAP
KNKILSARKK SSASLTSSSG SLNGSQSNLY LNGRVFISNI NVITSNDAGS FGGPGRYLTI
RWKGTKERGG CVIKFRSEEQ LVRWEAALKR LTKDQELDMP KVRNRDNSGS SEGEYLPKFP
PVVDSPMGSA RSSASSIQDS FKMPHVRQKS EVSLLSYGAP GPYSDEKKNR SVSSPATLVG
SLAHHVASVE LREQVNIKLT YKNENVHLSV QPHVVFADLL TTFLNKLRLT IGDDLKADDT
LKLKYRDEDD DLIQFRSDDD WTVARDMLNQ IADEESRILN IVVTV
//