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Database: UniProt
Entry: E9C1W6_CAPO3
LinkDB: E9C1W6_CAPO3
Original site: E9C1W6_CAPO3 
ID   E9C1W6_CAPO3            Unreviewed;      1173 AA.
AC   E9C1W6;
DT   05-APR-2011, integrated into UniProtKB/TrEMBL.
DT   05-APR-2011, sequence version 1.
DT   27-MAR-2024, entry version 69.
DE   SubName: Full=Cytohesin-4 {ECO:0000313|EMBL:KJE91175.1};
GN   ORFNames=CAOG_002349 {ECO:0000313|EMBL:KJE91175.1};
OS   Capsaspora owczarzaki (strain ATCC 30864).
OC   Eukaryota; Filasterea; Capsaspora.
OX   NCBI_TaxID=595528 {ECO:0000313|EMBL:KJE91175.1, ECO:0000313|Proteomes:UP000008743};
RN   [1] {ECO:0000313|Proteomes:UP000008743}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=ATCC 30864 {ECO:0000313|Proteomes:UP000008743};
RA   Russ C., Cuomo C., Burger G., Gray M.W., Holland P.W.H., King N.,
RA   Lang F.B.F., Roger A.J., Ruiz-Trillo I., Young S.K., Zeng Q., Gargeya S.,
RA   Alvarado L., Berlin A., Chapman S.B., Chen Z., Freedman E., Gellesch M.,
RA   Goldberg J., Griggs A., Gujja S., Heilman E., Heiman D., Howarth C.,
RA   Mehta T., Neiman D., Pearson M., Roberts A., Saif S., Shea T., Shenoy N.,
RA   Sisk P., Stolte C., Sykes S., White J., Yandava C., Haas B., Nusbaum C.,
RA   Birren B.;
RT   "The Genome Sequence of Capsaspora owczarzaki ATCC 30864.";
RL   Submitted (FEB-2011) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the BRAG family.
CC       {ECO:0000256|ARBA:ARBA00006248}.
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DR   EMBL; KE346362; KJE91175.1; -; Genomic_DNA.
DR   RefSeq; XP_004349099.1; XM_004349049.2.
DR   RefSeq; XP_011270158.1; XM_011271856.1.
DR   AlphaFoldDB; E9C1W6; -.
DR   STRING; 595528.E9C1W6; -.
DR   EnsemblProtists; KJE91175; KJE91175; CAOG_002349.
DR   GeneID; 14900417; -.
DR   eggNOG; KOG0931; Eukaryota.
DR   InParanoid; E9C1W6; -.
DR   OrthoDB; 204547at2759; -.
DR   PhylomeDB; E9C1W6; -.
DR   Proteomes; UP000008743; Unassembled WGS sequence.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005085; F:guanyl-nucleotide exchange factor activity; IEA:InterPro.
DR   GO; GO:0035556; P:intracellular signal transduction; IEA:InterPro.
DR   GO; GO:0032012; P:regulation of ARF protein signal transduction; IEA:InterPro.
DR   CDD; cd00171; Sec7; 1.
DR   Gene3D; 1.10.220.20; -; 1.
DR   Gene3D; 1.10.1000.11; Arf Nucleotide-binding Site Opener,domain 2; 1.
DR   Gene3D; 2.30.29.30; Pleckstrin-homology domain (PH domain)/Phosphotyrosine-binding domain (PTB); 1.
DR   Gene3D; 1.10.10.10; Winged helix-like DNA-binding domain superfamily/Winged helix DNA-binding domain; 1.
DR   InterPro; IPR000591; DEP_dom.
DR   InterPro; IPR000048; IQ_motif_EF-hand-BS.
DR   InterPro; IPR033742; IQSEC_PH.
DR   InterPro; IPR011993; PH-like_dom_sf.
DR   InterPro; IPR023394; Sec7_C_sf.
DR   InterPro; IPR000904; Sec7_dom.
DR   InterPro; IPR035999; Sec7_dom_sf.
DR   InterPro; IPR036388; WH-like_DNA-bd_sf.
DR   InterPro; IPR036390; WH_DNA-bd_sf.
DR   PANTHER; PTHR10663; GUANYL-NUCLEOTIDE EXCHANGE FACTOR; 1.
DR   PANTHER; PTHR10663:SF406; MIP16918P; 1.
DR   Pfam; PF00612; IQ; 1.
DR   Pfam; PF16453; IQ_SEC7_PH; 1.
DR   Pfam; PF01369; Sec7; 1.
DR   SMART; SM00049; DEP; 1.
DR   SMART; SM00222; Sec7; 1.
DR   SUPFAM; SSF50729; PH domain-like; 1.
DR   SUPFAM; SSF48425; Sec7 domain; 1.
DR   SUPFAM; SSF46785; Winged helix' DNA-binding domain; 1.
DR   PROSITE; PS50186; DEP; 1.
DR   PROSITE; PS50096; IQ; 1.
DR   PROSITE; PS50190; SEC7; 1.
PE   3: Inferred from homology;
KW   Reference proteome {ECO:0000313|Proteomes:UP000008743}.
FT   DOMAIN          107..184
FT                   /note="DEP"
FT                   /evidence="ECO:0000259|PROSITE:PS50186"
FT   DOMAIN          649..836
FT                   /note="SEC7"
FT                   /evidence="ECO:0000259|PROSITE:PS50190"
FT   REGION          38..86
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          189..230
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          242..266
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          284..334
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          477..556
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          575..643
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          920..942
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1030..1062
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1074..1173
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        38..58
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        207..221
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        242..263
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        485..499
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        506..556
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        577..631
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1031..1057
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1083..1114
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1126..1173
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1173 AA;  126219 MW;  17DAC3CDA0B0A48F CRC64;
     MQDEVTQLKA RVAELEAERE SMAARIASLE TENARLTLQV AASPSSSAPE QASARATDGD
     TPAQFMDESD CEPDSTEPAA PSSDEEQLNL AELAARATEL YELCHTPETG PLVADRTTKS
     GVAMPRTFVA RELVSVLVKS GVAATRAQAV TLGRRLQSRS LIWHPASHNT VTFRDRTLLF
     RFAVDATETD EQHKAHDQPK QQQQQEQQQE HEQEQEHEQQ AAAASEHASS LTQRAVFTIG
     GVTESESGDN PSSKSSSNLN LSLPPHPLEA ERSVSVTELH ELLSPTRIEV QPPSLAPPSP
     TRRHTSDPDL SMTLGDEALA SPSEKPGGLQ LPTATRRRAN TLTGRNSTHF ENIELSGDLQ
     ELVRQGTLKR YLGGEHFEKA AITIQRFYRH HKLRTRFRDV VRRGLANSHS PAATVRTLTL
     TGSLHSSLST SHESLPMVVD ITPMSARPSM ATALSPFLPS AGDTSSLVDN VSLTDNVSLA
     DSDDDSSPSP HRSQAGDEDR GLVRSPSGSS LASQSSEALG AATESTDSGA ASPVPAKSAG
     VSPSSSTNLS ASNSRPTMCQ RLLAQLRPLS FGPGHTLAVS SPGSDSSFDS FRSSGSGGSF
     DSSTDASETS SLSVEGGLST PRTSKGSGTV APGTPAPSVP GQIDISHRTV SEDHAKTRQV
     RIAIHKFNCD SKKGMLYLID KGFVLEKPRH VAFFLMRQPG LSKAMIGEYL GENKEFNLQV
     LDCFSSMVEM SGKTFDEALR AYLSSFRLPG EAQKIDRMMN TFAQRYTQAN PEAFATVDAA
     YVLAYSTVML NTDVHNPSVK HKMTQSDFVK NNRGINNNAD FPRVFLEGIY DRIASNEILA
     GEDHVKEVER IAGNIVGNVP LLAIPQRHFV RMANFVEVLD VSQRIPKGKH IRTLYLFNDM
     LLITKPSRST LTVPAHQIAP KPADKQAKGA PAPAPSSSAA HASNAVRTVS VPRFLFRNSF
     PLLGLQIRLM TPTKYHNELF ELQDFHGTPL ILLKAEKPQE KLDFLSVLQD MIEENAEIDA
     ERLAEMEKAL VTKSPSSSST HNAPFSTSSS PHGSSNALVD SDLKRAADVR SSKRFRMPFM
     ANNKRTSLGS ASTMGLPPPS TTSLAPSTHS ETSVSLNDAD EKRSIVTSRS GGSLASSVST
     ESTSSGAASN GSQTRSSEAI ATSTAPSPAT VQT
//
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