ID A0A1X2IYZ0_9FUNG Unreviewed; 507 AA.
AC A0A1X2IYZ0;
DT 05-JUL-2017, integrated into UniProtKB/TrEMBL.
DT 05-JUL-2017, sequence version 1.
DT 27-MAR-2024, entry version 17.
DE SubName: Full=Dbl homology domain-containing protein {ECO:0000313|EMBL:ORZ24510.1};
GN ORFNames=BCR42DRAFT_91970 {ECO:0000313|EMBL:ORZ24510.1};
OS Absidia repens.
OC Eukaryota; Fungi; Fungi incertae sedis; Mucoromycota; Mucoromycotina;
OC Mucoromycetes; Mucorales; Cunninghamellaceae; Absidia.
OX NCBI_TaxID=90262 {ECO:0000313|EMBL:ORZ24510.1, ECO:0000313|Proteomes:UP000193560};
RN [1] {ECO:0000313|EMBL:ORZ24510.1, ECO:0000313|Proteomes:UP000193560}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NRRL 1336 {ECO:0000313|EMBL:ORZ24510.1,
RC ECO:0000313|Proteomes:UP000193560};
RG DOE Joint Genome Institute;
RA Mondo S.J., Dannebaum R.O., Kuo R.C., Labutti K., Haridas S., Kuo A.,
RA Salamov A., Ahrendt S.R., Lipzen A., Sullivan W., Andreopoulos W.B.,
RA Clum A., Lindquist E., Daum C., Ramamoorthy G.K., Gryganskyi A., Culley D.,
RA Magnuson J.K., James T.Y., O'Malley M.A., Stajich J.E., Spatafora J.W.,
RA Visel A., Grigoriev I.V.;
RT "Pervasive Adenine N6-methylation of Active Genes in Fungi.";
RL Submitted (JUL-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:ORZ24510.1}.
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DR EMBL; MCGE01000002; ORZ24510.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1X2IYZ0; -.
DR STRING; 90262.A0A1X2IYZ0; -.
DR OrthoDB; 1358804at2759; -.
DR Proteomes; UP000193560; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:InterPro.
DR GO; GO:0005634; C:nucleus; IEA:InterPro.
DR GO; GO:0005096; F:GTPase activator activity; IEA:InterPro.
DR GO; GO:0005085; F:guanyl-nucleotide exchange factor activity; IEA:InterPro.
DR GO; GO:2000431; P:regulation of cytokinesis, actomyosin contractile ring assembly; IEA:InterPro.
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; IPR026817; Ect2.
DR InterPro; IPR011993; PH-like_dom_sf.
DR PANTHER; PTHR16777; PROTEIN ECT2; 1.
DR PANTHER; PTHR16777:SF2; PROTEIN ECT2; 1.
DR Pfam; PF00621; RhoGEF; 1.
DR SUPFAM; SSF48065; DBL homology domain (DH-domain); 1.
DR SUPFAM; SSF50729; PH domain-like; 1.
DR PROSITE; PS50010; DH_2; 1.
PE 4: Predicted;
KW Reference proteome {ECO:0000313|Proteomes:UP000193560}.
FT DOMAIN 84..255
FT /note="DH"
FT /evidence="ECO:0000259|PROSITE:PS50010"
FT REGION 389..428
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 507 AA; 58039 MW; 5930AC38719545E0 CRC64;
MNNDGEKHQY EQQLGHLLEL SSISPISDIG STSTSSSIHS ASYYTEQLMD DLSIIDDIYS
SYDHEQLTLA INNQVTYSTR NGALKEQMVQ HLIKTESQFV HDLDAFHTHF AAEMPQFQVQ
KNKLAFQTTD CDILFKPTLD LISAHQVLLD ELRQRLSIYG PTQIISDIFL QFFDHTNASY
TAYLKGFSST LLTLDRLHKT NAFIKFCESR QQSNPSLKDC GYYICIPLIR LSAYTQAVDQ
CTQLTEPAHP DYNALITISK RYKTREQQWQ SLVEDCLSHY KVYKWFRAVQ NSPALVTPTR
RLLLYSDLIH LDPDAPTDMT DHRTYILYND LLIFCKQQKD GRMFYQGIVI LDKAVLKPMD
RKIANKIRDK HQKAIKQANG SRKLSLFGIK KQQQQQPQQQ QQLKSNSSNQ TSTRTSTTSD
SSSSGSASSI YSEDSGVYGF EIFFQFVMDK NVTSYTNPIT SYGMGPVTSV ASNDSVRRHI
LLTRSLEEQT LWNEHLQRVI KSVTSSR
//