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Database: UniProt
Entry: A0A0A1U318_ENTIV
LinkDB: A0A0A1U318_ENTIV
Original site: A0A0A1U318_ENTIV 
ID   A0A0A1U318_ENTIV        Unreviewed;      1092 AA.
AC   A0A0A1U318;
DT   04-FEB-2015, integrated into UniProtKB/TrEMBL.
DT   04-FEB-2015, sequence version 1.
DT   27-MAR-2024, entry version 39.
DE   SubName: Full=Rho/RAC guanine nucleotide exchange factor, putative {ECO:0000313|EMBL:ELP87100.1};
GN   ORFNames=EIN_495550 {ECO:0000313|EMBL:ELP87100.1};
OS   Entamoeba invadens IP1.
OC   Eukaryota; Amoebozoa; Evosea; Archamoebae; Mastigamoebida; Entamoebidae;
OC   Entamoeba.
OX   NCBI_TaxID=370355 {ECO:0000313|EMBL:ELP87100.1, ECO:0000313|Proteomes:UP000014680};
RN   [1] {ECO:0000313|EMBL:ELP87100.1, ECO:0000313|Proteomes:UP000014680}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=IP1 {ECO:0000313|EMBL:ELP87100.1,
RC   ECO:0000313|Proteomes:UP000014680};
RA   Zafar N., Inman J., Hall N., Lorenzi H., Caler E.;
RL   Submitted (OCT-2012) to the EMBL/GenBank/DDBJ databases.
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DR   EMBL; KB206864; ELP87100.1; -; Genomic_DNA.
DR   RefSeq; XP_004253871.1; XM_004253823.1.
DR   AlphaFoldDB; A0A0A1U318; -.
DR   EnsemblProtists; ELP87100; ELP87100; EIN_495550.
DR   GeneID; 14886096; -.
DR   KEGG; eiv:EIN_495550; -.
DR   VEuPathDB; AmoebaDB:EIN_495550; -.
DR   OrthoDB; 24433at2759; -.
DR   Proteomes; UP000014680; Unassembled WGS sequence.
DR   GO; GO:0005096; F:GTPase activator activity; IEA:InterPro.
DR   GO; GO:0005085; F:guanyl-nucleotide exchange factor activity; IEA:InterPro.
DR   CDD; cd00160; RhoGEF; 1.
DR   Gene3D; 1.10.220.150; Arf GTPase activating protein; 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; IPR037278; ARFGAP/RecO.
DR   InterPro; IPR001164; ArfGAP_dom.
DR   InterPro; IPR038508; ArfGAP_dom_sf.
DR   InterPro; IPR001715; CH_dom.
DR   InterPro; IPR036872; CH_dom_sf.
DR   InterPro; IPR035899; DBL_dom_sf.
DR   InterPro; IPR000219; DH-domain.
DR   InterPro; IPR011993; PH-like_dom_sf.
DR   InterPro; IPR001849; PH_domain.
DR   PANTHER; PTHR12673; FACIOGENITAL DYSPLASIA PROTEIN; 1.
DR   PANTHER; PTHR12673:SF159; RAC GUANINE NUCLEOTIDE EXCHANGE FACTOR JJ; 1.
DR   Pfam; PF01412; ArfGap; 1.
DR   Pfam; PF00307; CH; 1.
DR   Pfam; PF00621; RhoGEF; 1.
DR   SMART; SM00105; ArfGap; 1.
DR   SMART; SM00033; CH; 1.
DR   SMART; SM00233; PH; 1.
DR   SMART; SM00325; RhoGEF; 1.
DR   SUPFAM; SSF57863; ArfGap/RecO-like zinc finger; 1.
DR   SUPFAM; SSF47576; Calponin-homology domain, CH-domain; 1.
DR   SUPFAM; SSF48065; DBL homology domain (DH-domain); 1.
DR   SUPFAM; SSF50729; PH domain-like; 1.
DR   PROSITE; PS50115; ARFGAP; 1.
DR   PROSITE; PS50021; CH; 1.
DR   PROSITE; PS50010; DH_2; 1.
PE   4: Predicted;
KW   Coiled coil {ECO:0000256|SAM:Coils};
KW   Metal-binding {ECO:0000256|PROSITE-ProRule:PRU00288};
KW   Reference proteome {ECO:0000313|Proteomes:UP000014680};
KW   Zinc {ECO:0000256|PROSITE-ProRule:PRU00288};
KW   Zinc-finger {ECO:0000256|PROSITE-ProRule:PRU00288}.
FT   DOMAIN          5..109
FT                   /note="Calponin-homology (CH)"
FT                   /evidence="ECO:0000259|PROSITE:PS50021"
FT   DOMAIN          446..627
FT                   /note="DH"
FT                   /evidence="ECO:0000259|PROSITE:PS50010"
FT   DOMAIN          936..998
FT                   /note="Arf-GAP"
FT                   /evidence="ECO:0000259|PROSITE:PS50115"
FT   REGION          123..178
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          232..265
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          320..408
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          538..569
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COMPBIAS        123..159
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        160..178
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        239..260
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        352..385
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1092 AA;  122957 MW;  E7BAA81751EC3F11 CRC64;
     MSSFPDEIKE CVNWVNGQLP DEEPITDVLT GLSDGTKLIR IVAKLSGKKA LRYSLTANTP
     FQKQQNMAVL LKMTEMAYGT NVSYDAGDLA RGNEGQLLSL AFYIGQKSGT RVPKRKTLTK
     ATSIGLKNVQ PNANEQVSKN SPLRQTSDVA LNHTEKTQNK NNTNGDETDK MERSPRSPRK
     VVIDVVPALP EKRYHNISSS KTVVQTRDIK ETTDSTDDGL DIPVDVIETT LTSQGVKEKS
     QTDLEEESPI KSDMTESTEN NEEGSAHYSL YDEIEVLGKY DTFMETNKCT TPTVSESSYV
     QPIVDTSSMC TVSTGVVESE ALHQETPPSQ LEDVPPPTPT LPQRPKRMLE SSMNKLCQSS
     PSAGCKSSRE ASLSSGTSRM SFMSESGSGA KRDKIGKSPR DTISQMPEMS YDQKTYLEED
     VDIINKYCRG YLGRLKAKPT MKMLSQRRNV VLEILNTERI YVSRLKQFLE FYLAKALQIF
     PGDSILKKCE ENLRVIVGYN GNLLKELEQL QTEGKIYGEG IGKSFEKLSH FLKTYCSYIN
     STDAINEHEE KLRRTKKEFE SQMKQTQLEN KLETFNSYVI LPVQRIPRYR LLLTELLKTM
     TPQHGEYIAL DKSLQQIIEV GSAVNETKRT MEQKNIVSLV FSKFKYPTGM QQIQPDAACS
     FVRIGNMELL DREKGKLKSV TLLLFSNNVV ITKVPTTGTL HKGKLKADSI ETIVESKKSL
     TVEYVIPIGS FCVLDSADFM LGSGGLSERA PSFKIVTKDL LTFQFCTLTE SEKNSWLVDL
     DSQVALVQER ALIGIRESNK NIIESLYDAY RSQWSENTIK MPWWHSDLMG EECMIFANGY
     VATFGNAHDA FARQNIRNYF VTKYTSVAFS GQKTITLVNF ARKEKPRVVL ELNTTAEALM
     WVFLLRQSFI GFYDPNEINM ALFSCAENDL PALPPEEVVF AITENAKNRT CADCGDTAVK
     YVDMTFGCFV CSDCGRIHRY FTNKPQVCAP KILGDKSLVD LRLLIQKGND FLNEELVVGQ
     GLPTNPAEYD GDLNQYLWKK YKQEGEAPKS IIREVGKKTG TLRRDEVNKI RAKRGMERRS
     TFSVIEEDKK KK
//
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