ID K2GT89_ENTNP Unreviewed; 727 AA.
AC K2GT89;
DT 28-NOV-2012, integrated into UniProtKB/TrEMBL.
DT 28-NOV-2012, sequence version 1.
DT 27-MAR-2024, entry version 53.
DE SubName: Full=Rho guanine nucleotide exchange factor, putative {ECO:0000313|EMBL:EKE37057.1};
GN ORFNames=ENU1_210820 {ECO:0000313|EMBL:EKE37057.1};
OS Entamoeba nuttalli (strain P19) (Amoeba).
OC Eukaryota; Amoebozoa; Evosea; Archamoebae; Mastigamoebida; Entamoebidae;
OC Entamoeba.
OX NCBI_TaxID=1076696 {ECO:0000313|EMBL:EKE37057.1, ECO:0000313|Proteomes:UP000006769};
RN [1] {ECO:0000313|EMBL:EKE37057.1, ECO:0000313|Proteomes:UP000006769}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=P19 {ECO:0000313|EMBL:EKE37057.1,
RC ECO:0000313|Proteomes:UP000006769};
RA Hannick L., Karamycheva S., Lorenzi H., Caler E.;
RL Submitted (NOV-2011) to the EMBL/GenBank/DDBJ databases.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton
CC {ECO:0000256|ARBA:ARBA00004245}.
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DR EMBL; JH930173; EKE37057.1; -; Genomic_DNA.
DR RefSeq; XP_008860603.1; XM_008862381.1.
DR AlphaFoldDB; K2GT89; -.
DR EnsemblProtists; EKE37057; EKE37057; ENU1_210820.
DR GeneID; 20076783; -.
DR VEuPathDB; AmoebaDB:ENU1_210820; -.
DR OMA; IYCKKER; -.
DR OrthoDB; 10022at2759; -.
DR Proteomes; UP000006769; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-SubCell.
DR GO; GO:0005085; F:guanyl-nucleotide exchange factor activity; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0035556; P:intracellular signal transduction; IEA:InterPro.
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 Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
DR InterPro; IPR035899; DBL_dom_sf.
DR InterPro; IPR000219; DH-domain.
DR InterPro; IPR001331; GDS_CDC24_CS.
DR InterPro; IPR011993; PH-like_dom_sf.
DR InterPro; IPR001849; PH_domain.
DR InterPro; IPR000306; Znf_FYVE.
DR InterPro; IPR017455; Znf_FYVE-rel.
DR InterPro; IPR011011; Znf_FYVE_PHD.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR PANTHER; PTHR12673; FACIOGENITAL DYSPLASIA PROTEIN; 1.
DR PANTHER; PTHR12673:SF263; GRFA PROTEIN, PUTATIVE-RELATED; 1.
DR Pfam; PF01363; FYVE; 1.
DR Pfam; PF00621; RhoGEF; 1.
DR SMART; SM00064; FYVE; 1.
DR SMART; SM00233; PH; 1.
DR SMART; SM00325; RhoGEF; 1.
DR SUPFAM; SSF48065; DBL homology domain (DH-domain); 1.
DR SUPFAM; SSF57903; FYVE/PHD zinc finger; 1.
DR SUPFAM; SSF50729; PH domain-like; 1.
DR PROSITE; PS00741; DH_1; 1.
DR PROSITE; PS50010; DH_2; 1.
DR PROSITE; PS50003; PH_DOMAIN; 1.
DR PROSITE; PS50178; ZF_FYVE; 1.
PE 4: Predicted;
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW Cytoskeleton {ECO:0000256|ARBA:ARBA00023212};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00091}.
FT DOMAIN 277..464
FT /note="DH"
FT /evidence="ECO:0000259|PROSITE:PS50010"
FT DOMAIN 493..581
FT /note="PH"
FT /evidence="ECO:0000259|PROSITE:PS50003"
FT DOMAIN 604..660
FT /note="FYVE-type"
FT /evidence="ECO:0000259|PROSITE:PS50178"
FT REGION 48..70
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 87..109
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 162..240
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 175..194
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 214..238
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 727 AA; 82919 MW; CCB914C848D1F9FC CRC64;
MKKVQYDPFG DDYNTTTEYS DDVFSSLSST PSMSPVLSDI DSFCDQLTNK PLTPNQEEVF
SPKTIPRSTS ETNDFNILET QGKIVSSLSP RLDPSHNSHS PRMKKERSWR TAQIFQKEKV
LNVVGSLEGF NIEDDHIPFA EVPPKKMCLT TTPQNQVSLI NTSTSTTLSS STQSCDEETK
KKTQRDKISH ESCKEIICAK PPPKSSPSDI INQSLQREKD RSIKSKSEPY EETSDEHQQI
NEQSLIENSN TDLSIDTSTI SSSDSLTLML DKPTKSYRER ILDEFVSSEY TYVIGLKICS
KFFEEPLSKQ QKYCPPNLFS IVFKGFDDVY RINSNLLQEL NNLKNHVDGK SLDTHLGEAF
SQFIPLLNVY KTYVGNTEAQ FAALDRLESK SSFKKLCFNL QSKISVGHAL NLRSYLITPV
QRLPRYKLLL EDLIRNTPEG HCDLARLKNA LDKVMSINLN VNHSVDIQSR QQKLIELSKK
IKGIDDLIQP NRYYICDGEL TRINQKGKKI KHFYLFNDRL ISGKPGNEVI VSFDEKIVNI
MIQDDSDISF NILSPNKSFE ILCTNEEEKR DWFEKIIDAI NTENQLVPVQ QSKKAIEYAP
LWLPQSIQKC QLCGKAFSLI NRKQFCIHCG LCVCNGCYRG RFIFNGVNKR GCDRCMKKAL
AMNKIIIDDD ISKRKTIRMK SSKEDEIVLR LEGVNLTRVR SNANVAPIRP LLIKKPINEN
EAKKTDD
//
