ID E9GBE1_DAPPU Unreviewed; 2073 AA.
AC E9GBE1;
DT 05-APR-2011, integrated into UniProtKB/TrEMBL.
DT 05-APR-2011, sequence version 1.
DT 27-MAR-2024, entry version 62.
DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:EFX82944.1};
GN ORFNames=DAPPUDRAFT_240350 {ECO:0000313|EMBL:EFX82944.1};
OS Daphnia pulex (Water flea).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Crustacea; Branchiopoda;
OC Diplostraca; Cladocera; Anomopoda; Daphniidae; Daphnia.
OX NCBI_TaxID=6669 {ECO:0000313|EMBL:EFX82944.1, ECO:0000313|Proteomes:UP000000305};
RN [1] {ECO:0000313|EMBL:EFX82944.1, ECO:0000313|Proteomes:UP000000305}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=21292972; DOI=10.1126/science.1197761;
RA Colbourne J.K., Pfrender M.E., Gilbert D., Thomas W.K., Tucker A.,
RA Oakley T.H., Tokishita S., Aerts A., Arnold G.J., Basu M.K., Bauer D.J.,
RA Caceres C.E., Carmel L., Casola C., Choi J.H., Detter J.C., Dong Q.,
RA Dusheyko S., Eads B.D., Frohlich T., Geiler-Samerotte K.A., Gerlach D.,
RA Hatcher P., Jogdeo S., Krijgsveld J., Kriventseva E.V., Kultz D.,
RA Laforsch C., Lindquist E., Lopez J., Manak J.R., Muller J., Pangilinan J.,
RA Patwardhan R.P., Pitluck S., Pritham E.J., Rechtsteiner A., Rho M.,
RA Rogozin I.B., Sakarya O., Salamov A., Schaack S., Shapiro H., Shiga Y.,
RA Skalitzky C., Smith Z., Souvorov A., Sung W., Tang Z., Tsuchiya D., Tu H.,
RA Vos H., Wang M., Wolf Y.I., Yamagata H., Yamada T., Ye Y., Shaw J.R.,
RA Andrews J., Crease T.J., Tang H., Lucas S.M., Robertson H.M., Bork P.,
RA Koonin E.V., Zdobnov E.M., Grigoriev I.V., Lynch M., Boore J.L.;
RT "The ecoresponsive genome of Daphnia pulex.";
RL Science 331:555-561(2011).
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
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DR EMBL; GL732538; EFX82944.1; -; Genomic_DNA.
DR STRING; 6669.E9GBE1; -.
DR EnsemblMetazoa; EFX82944; EFX82944; DAPPUDRAFT_240350.
DR KEGG; dpx:DAPPUDRAFT_240350; -.
DR eggNOG; KOG3520; Eukaryota.
DR HOGENOM; CLU_001593_0_0_1; -.
DR InParanoid; E9GBE1; -.
DR PhylomeDB; E9GBE1; -.
DR Proteomes; UP000000305; Unassembled WGS sequence.
DR GO; GO:0005085; F:guanyl-nucleotide exchange factor activity; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0035023; P:regulation of Rho protein signal transduction; IBA:GO_Central.
DR CDD; cd20815; C1_p190RhoGEF-like; 1.
DR CDD; cd15789; PH_ARHGEF2_18_like; 1.
DR CDD; cd00160; RhoGEF; 1.
DR Gene3D; 3.30.60.20; -; 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; IPR046349; C1-like_sf.
DR InterPro; IPR035899; DBL_dom_sf.
DR InterPro; IPR000219; DH-domain.
DR InterPro; IPR002219; PE/DAG-bd.
DR InterPro; IPR011993; PH-like_dom_sf.
DR InterPro; IPR041020; PH_16.
DR InterPro; IPR001849; PH_domain.
DR PANTHER; PTHR13944; AGAP007712-PA; 1.
DR PANTHER; PTHR13944:SF21; CYSTS, ISOFORM C; 1.
DR Pfam; PF17838; PH_16; 1.
DR Pfam; PF00621; RhoGEF; 1.
DR SMART; SM00109; C1; 1.
DR SMART; SM00233; PH; 1.
DR SMART; SM00325; RhoGEF; 1.
DR SUPFAM; SSF57889; Cysteine-rich domain; 1.
DR SUPFAM; SSF48065; DBL homology domain (DH-domain); 1.
DR SUPFAM; SSF50729; PH domain-like; 1.
DR PROSITE; PS50010; DH_2; 1.
DR PROSITE; PS50003; PH_DOMAIN; 1.
DR PROSITE; PS50081; ZF_DAG_PE_2; 1.
PE 4: Predicted;
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Guanine-nucleotide releasing factor {ECO:0000256|ARBA:ARBA00022658};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000000305};
KW Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT DOMAIN 797..845
FT /note="Phorbol-ester/DAG-type"
FT /evidence="ECO:0000259|PROSITE:PS50081"
FT DOMAIN 1059..1248
FT /note="DH"
FT /evidence="ECO:0000259|PROSITE:PS50010"
FT DOMAIN 1289..1393
FT /note="PH"
FT /evidence="ECO:0000259|PROSITE:PS50003"
FT REGION 519..573
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 588..620
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 760..796
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 922..1013
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1568..1587
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1749..1810
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1869..1898
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1913..2046
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 1659..1732
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 557..573
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 781..796
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 922..974
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1766..1783
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1784..1808
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1869..1890
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1927..1941
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1948..1962
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1974..1989
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2029..2046
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 2073 AA; 222748 MW; 325282515EBBD8E8 CRC64;
MVPYQLQQAK GLLHCYNQMD RTSRIPMQDH LKGKSHLKNL NNFPERKLAF EQLSISTPEP
KDDSFQISST VDERIEKAWN HQTICGYIYD ESFSILSIEK KIQVLSPHFA FIGQDDPMPN
FVKYLRLITL AICGSINYGN DNHFKANACN IDVSCGDGSR GCIDRFLRSP QPVESPDDKS
RPCEYPSGFS PLCTVPTFGM AHYIEQEVYT SSEESGAEDS DEDIITDYLS PLDDNGNLDA
GASAATSSSS PGVAAINVAA IATRFYSTES PPCSLRISAA EDMEPAGAAA ADGGGGGTDD
RMISNYATAA AAAAAAAESI PIISVTQHSP AASKAFFILE TGRDRYDGED NLRQLHGIQE
SIQRMRQVSV QTLRLQRRSH PRQRMCKILA VAQSQVGRRL RYGGVGAGCN WSLSCPSLSG
SGSGGGQGGV ASGLAGHGNG NNNEADWLGA TLADWDSPTP PGMAAHYWVG GDGGPSHKAG
LANGSKRRRS WASPWEVDEM GLASAGGTCG ITYEEAGGGG ALDGVGGRTR SISLSSGDTD
NEQDAAGGGG GSGHSSRARQ AGITTSSSAL SSGELKVLAG RHSTHSLNDM GFPLIPALPT
KPRGMSKDGG GGGRDGDPSK WLSPRILTLQ KSISTPSILA VKDGSNLTAL TLSSIKNSTG
GSNSASSAAS ATMAATIGGA SVGSGASAAG MMAKETQGIL MTATAAGPTS SFPRISSYTG
LESETDDDSE LHLNHHHHHL SHDHVSSRYS LGSFVAEPGF ENDDDANSSK RRKRGSIFFR
KRKDKDKEKD KSKLKQPHQF VPVCHSNSQP CDVCSKSLTN KAALRCESCA ITVHENSCRD
QVSDCTRFKV PKSIPLGSKV SSLANLTGAG HAKLQSSHSA VGAAAFTASN ASSAGSSLYY
SVSSSSAATS AGLSATNNHV TAGSSANSSG GSTWSVAQSI GSTLPSSSNS SSTAATNTPA
SSSQTPSTPI ASPLFGNSKC GAGADKDPND PSNTPSEDQP SHATNEGDGH DTIEGVFNAA
DIKDLDLDPE LGILDEEAEA WVGTVDKKIS KKLKEKEIKR QEHIYEFIIT EKHHCLTLKV
MQKIFAEGMR REMRLSSETV DRIFPCLEEL IEYHLQFLRR LRQRQRQESI VSTIEDILRV
QFSGLLGDQL RSLYGEFCSR HQEAVSMYKE MIKEDRKFAA FARQCTLNPL CKKKGIPECI
LFVTQRITKY PLLIDPLIKT SREQPEECLK LQQVLGFVKD ILIGVNAQVA EKERKLRLIE
VYNKIDAKSA TTYKNKKFKK SDLLSSNRRL MFEGVAYLNH ARGKVQLVTV VVLSDVVFFL
QESNQKFHFV TQDNKAGVIS LQKLLVREKA GGQDTRSIYL ISSNPDEPEM YELQCQNPRE
KRIWIDTIRA AVEQCPEDEE GNVSEGEEQR KIREAQDIKT RQLIATLREK DRQLGSLLEE
KMATFCELVE LLANNEDSTS SWLLLGSDSA PPKYSHLVEQ GFQSAQAKET LSQAMTELCR
LLGLLLSSNA AANWNLSRSV SSVGERHSDT FSMPLLPKRA ETFGGFDQNG KEKGCVKKKS
ATDLTAVDST TTTTTNEQPA SWSAQTPPVL QLNGDQQAMG LELVHNVSTL LCLLSSQATA
FESLRNDFLA EIKASRSGTA LTSAPFGSSS ATLAKFQHKA SHNQRLEELR NLQDRLSKEK
AEWSRERTMQ EEHISEQRKQ LLKLQEQVRI ENTDIQQQRE NLYQKLEALR GQGILLSPNM
TIVSTAPMAS AVSPTSGGED ADATGGPSSP PPPNPPPNST SLLPSPTPSS VDLGRRKTRG
SNTAGMGSAS AGLLKRESCS NLPLPMNLIS AKNEQKAVVA ALANTLPIKQ QLPMKLAKLG
AALGSAGHAT GGNSNSGGSN NSSHGSPHGN VASPTGGGLV QQLLPLRLSE SLEHKRASPK
VPSTDPFKPK LSSSSFSPPA SKSEDFVAGH SRTGSSPASI QMLSPRHHHY HHTTTTTTAT
TTSTASAGGN MHPPKVPDKP ASLLLQQAAR GSPQLPPPPG HHQHHQAHPP PKVHDPETNQ
EIKKERKMWK DTASLLPATP SPVYQRWSTN TVM
//