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Database: UniProt
Entry: A0A261CF32_9PELO
LinkDB: A0A261CF32_9PELO
Original site: A0A261CF32_9PELO 
ID   A0A261CF32_9PELO        Unreviewed;       897 AA.
AC   A0A261CF32;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   08-NOV-2023, entry version 21.
DE   RecName: Full=DH domain-containing protein {ECO:0008006|Google:ProtNLM};
DE   Flags: Fragment;
GN   ORFNames=FL83_04468 {ECO:0000313|EMBL:OZG21137.1};
OS   Caenorhabditis latens.
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC   Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC   Caenorhabditis.
OX   NCBI_TaxID=1503980 {ECO:0000313|EMBL:OZG21137.1, ECO:0000313|Proteomes:UP000216463};
RN   [1] {ECO:0000313|EMBL:OZG21137.1, ECO:0000313|Proteomes:UP000216463}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PX534 {ECO:0000313|EMBL:OZG21137.1,
RC   ECO:0000313|Proteomes:UP000216463};
RA   Fierst J.L.;
RT   "Caenorhabditis latens genome sequence.";
RL   Submitted (JUL-2017) 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:OZG21137.1}.
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DR   EMBL; NIPN01000010; OZG21137.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A261CF32; -.
DR   STRING; 1503980.A0A261CF32; -.
DR   Proteomes; UP000216463; 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   CDD; cd00160; RhoGEF; 1.
DR   Gene3D; 3.40.50.10190; BRCT 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; IPR001357; BRCT_dom.
DR   InterPro; IPR036420; BRCT_dom_sf.
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   SMART; SM00292; BRCT; 2.
DR   SMART; SM00325; RhoGEF; 1.
DR   SUPFAM; SSF52113; BRCT domain; 1.
DR   SUPFAM; SSF48065; DBL homology domain (DH-domain); 1.
DR   PROSITE; PS50172; BRCT; 1.
DR   PROSITE; PS50010; DH_2; 1.
PE   4: Predicted;
KW   Reference proteome {ECO:0000313|Proteomes:UP000216463}.
FT   DOMAIN          190..276
FT                   /note="BRCT"
FT                   /evidence="ECO:0000259|PROSITE:PS50172"
FT   DOMAIN          345..543
FT                   /note="DH"
FT                   /evidence="ECO:0000259|PROSITE:PS50010"
FT   REGION          287..341
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          749..786
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          846..897
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        287..326
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        327..341
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        749..780
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        846..885
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   NON_TER         1
FT                   /evidence="ECO:0000313|EMBL:OZG21137.1"
SQ   SEQUENCE   897 AA;  102159 MW;  DE15963D46318FA8 CRC64;
     MDVSMLQSQE KRSRSMRKLA VWKGDIEEYK EIFDMINQQK EKRKIEVVPY ESLDELDSDW
     REYTFFCGDF TSDLFHTLTN AQDSGASAHL IVGPAALSHK LQTAQDFMLL RPCRPLYCEL
     MKNVTMKLST EVLNKRELVD MVHFMGGSVR KDSMTLVGVP TLRADWITES WKNRDDPYFD
     VFKQDFIDKH SLGVFEGLSL YFHGFKKNEI DDMKINFINT KGTLVDDPSE ATHVVYNPIN
     DIEPLPVSSN QVHVTQEWFW VSLHRGCCAL EDNFALPTGS LRRKLLDNSN TNSPLGKSSR
     SHNSRSLSSM RDCSGEGPSS NRTPDYIYSN DDEENVCKSP RQPSKRLRVC MEMVETEKNY
     VALLKLVVKF KQALETEISE NEFVTRTDVA MIFGKLDPIL ELHEKIYARL TAILNEAHTL
     LSAVNGNKND DKNLDFAQVW IDAKEEMMRA YPQYLNSFDT IKCLFAKHDK ENSKFHTFCK
     AKESSPEFHR LQLTDLMIKP VQRLPSVALL LNEMAKKSDS KLKCTAEQAA KVIDEVLKIA
     NKILEKNDNL ISHFSKFTAI ESIPPILVAA NRMFLRELVV SPIASTSSRL SQFSKMKLFL
     FHDVLVITKV RSEKNAMQRF ARHASLASLK AIKRKPYRYI DQIQLITMRS AFRIRAPGDF
     SKFQEAQSHV HDVFVWCLIH RDEQGGDTET VFVSTDSEEV RDFLDDIHKK IMSNCGRYFF
     QSDPFEVNDL NDAHVANLTN RYFRNLCGSK PQNGHDSQMN TTASERTSQN ELSHNETVMG
     PPKPQSRMRR ALSNAQLTIT STLGFGRNPN RNSLARISEN SSFMTSPRVS CVPAALVNMT
     SVGIPGGNCD SESTPKRGQR APLTSDTFTR TGALGRSTSM RRQPTGFSHS EKEPHRS
//
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