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Database: UniProt
Entry: E2AEJ4_CAMFO
LinkDB: E2AEJ4_CAMFO
Original site: E2AEJ4_CAMFO 
ID   E2AEJ4_CAMFO            Unreviewed;       826 AA.
AC   E2AEJ4;
DT   30-NOV-2010, integrated into UniProtKB/TrEMBL.
DT   30-NOV-2010, sequence version 1.
DT   27-MAR-2024, entry version 71.
DE   SubName: Full=Rho GTPase-activating protein 26 {ECO:0000313|EMBL:EFN68151.1};
GN   ORFNames=EAG_05540 {ECO:0000313|EMBL:EFN68151.1};
OS   Camponotus floridanus (Florida carpenter ant).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Hymenoptera; Apocrita; Aculeata; Formicoidea;
OC   Formicidae; Formicinae; Camponotus.
OX   NCBI_TaxID=104421 {ECO:0000313|Proteomes:UP000000311};
RN   [1] {ECO:0000313|EMBL:EFN68151.1, ECO:0000313|Proteomes:UP000000311}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C129 {ECO:0000313|Proteomes:UP000000311};
RX   PubMed=20798317; DOI=10.1126/science.1192428;
RA   Bonasio R., Zhang G., Ye C., Mutti N.S., Fang X., Qin N., Donahue G.,
RA   Yang P., Li Q., Li C., Zhang P., Huang Z., Berger S.L., Reinberg D.,
RA   Wang J., Liebig J.;
RT   "Genomic comparison of the ants Camponotus floridanus and Harpegnathos
RT   saltator.";
RL   Science 329:1068-1071(2010).
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DR   EMBL; GL438862; EFN68151.1; -; Genomic_DNA.
DR   RefSeq; XP_011256719.1; XM_011258417.1.
DR   AlphaFoldDB; E2AEJ4; -.
DR   STRING; 104421.E2AEJ4; -.
DR   EnsemblMetazoa; XM_011258417.2; XP_011256719.1; LOC105251540.
DR   GeneID; 105251540; -.
DR   KEGG; cfo:105251540; -.
DR   InParanoid; E2AEJ4; -.
DR   OMA; CASQERY; -.
DR   OrthoDB; 5395569at2759; -.
DR   Proteomes; UP000000311; Unassembled WGS sequence.
DR   GO; GO:0005737; C:cytoplasm; IEA:InterPro.
DR   GO; GO:0005096; F:GTPase activator activity; IEA:UniProtKB-KW.
DR   GO; GO:0007165; P:signal transduction; IEA:InterPro.
DR   CDD; cd01249; BAR-PH_GRAF_family; 1.
DR   CDD; cd07602; BAR_RhoGAP_OPHN1-like; 1.
DR   CDD; cd11882; SH3_GRAF-like; 1.
DR   Gene3D; 1.20.1270.60; Arfaptin homology (AH) domain/BAR domain; 1.
DR   Gene3D; 2.30.29.30; Pleckstrin-homology domain (PH domain)/Phosphotyrosine-binding domain (PTB); 1.
DR   Gene3D; 1.10.555.10; Rho GTPase activation protein; 1.
DR   Gene3D; 2.30.30.40; SH3 Domains; 1.
DR   InterPro; IPR027267; AH/BAR_dom_sf.
DR   InterPro; IPR004148; BAR_dom.
DR   InterPro; IPR047234; GRAF_fam.
DR   InterPro; IPR011993; PH-like_dom_sf.
DR   InterPro; IPR001849; PH_domain.
DR   InterPro; IPR047225; PH_GRAF.
DR   InterPro; IPR008936; Rho_GTPase_activation_prot.
DR   InterPro; IPR000198; RhoGAP_dom.
DR   InterPro; IPR036028; SH3-like_dom_sf.
DR   InterPro; IPR001452; SH3_domain.
DR   PANTHER; PTHR12552; OLIGOPHRENIN 1; 1.
DR   PANTHER; PTHR12552:SF1; RHO GTPASE-ACTIVATING PROTEIN GRAF; 1.
DR   Pfam; PF16746; BAR_3; 1.
DR   Pfam; PF00169; PH; 1.
DR   Pfam; PF00620; RhoGAP; 1.
DR   Pfam; PF14604; SH3_9; 1.
DR   SMART; SM00233; PH; 1.
DR   SMART; SM00324; RhoGAP; 1.
DR   SMART; SM00326; SH3; 1.
DR   SUPFAM; SSF103657; BAR/IMD domain-like; 1.
DR   SUPFAM; SSF48350; GTPase activation domain, GAP; 1.
DR   SUPFAM; SSF50729; PH domain-like; 1.
DR   SUPFAM; SSF50044; SH3-domain; 1.
DR   PROSITE; PS50003; PH_DOMAIN; 1.
DR   PROSITE; PS50238; RHOGAP; 1.
DR   PROSITE; PS50002; SH3; 1.
PE   4: Predicted;
KW   Coiled coil {ECO:0000256|SAM:Coils};
KW   GTPase activation {ECO:0000256|ARBA:ARBA00022468};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000311};
KW   SH3 domain {ECO:0000256|ARBA:ARBA00022443, ECO:0000256|PROSITE-
KW   ProRule:PRU00192}.
FT   DOMAIN          270..374
FT                   /note="PH"
FT                   /evidence="ECO:0000259|PROSITE:PS50003"
FT   DOMAIN          388..573
FT                   /note="Rho-GAP"
FT                   /evidence="ECO:0000259|PROSITE:PS50238"
FT   DOMAIN          767..826
FT                   /note="SH3"
FT                   /evidence="ECO:0000259|PROSITE:PS50002"
FT   REGION          644..673
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          700..720
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          24..58
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COMPBIAS        656..670
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        700..714
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   826 AA;  93999 MW;  68A46A49DFE60957 CRC64;
     MGVGLKPLEF TDCLTDSPYF RENLHYHERE LEKTSQQIKR LVKEVKDLLL AAKNLSRAQR
     AFSKTLQNFS FECIGESQTE DETHISQSLK EFGKLIASIE DERDRMLERA YDQIILPLEN
     FRKVHIGGVK DGKKKFEKQT IKFCQSQERY LNLSTKKQDN VLQEADATLE MAERHFSQAS
     LEYVFLLQEV QERKKFEFVE TLLGFMFGWL TFYHQGHEVA KDFKPYMTEL QLKIQKTREN
     FLATRDKTES LMNKMKDMKK STVESGLNKL HSREGYLFLM ERKAFGTTWT KQYCTYQKDK
     KEFTMIPYNQ LTGKFSSKET FTLASCIRRM SDTIEKRFCF DITAIDRPNV TYTFQALSEE
     DRKLWMDAMD GKEPTFPRLG SSVKSEDMTL DENGFAFVSK CIAALEDRGL EEQGLYRVVG
     VASKVTKLLT MGLDKRKVEK LNLNDRFEWE SKTITSALKT YLRTLSEPLM TFRYYNSFIT
     AAKQETKETR INDIHNLVYR LPKTNFNMLI LLITHLCTVA KKSDKNLMTV GNLAVCFGPT
     LLRPEEETVA SIMDIKFYNI VVEILIENCE RIIAGPPPDS SRITAVQAVV PNKSQCAKME
     EGPTSSGNGT AFLRYPLHTA VAVTPATSSH AHLVTRSYYD GQPLTVVNKP PPTVDERNNG
     DYEDLDNTSH RIPSYLDSRG GRIKLTNANL MYHSADKVLS GGNTSSSSES IASDPHPFTG
     ELPVKQKRGT MISVHGYPTA YPQRSNSSIC PINTSPNSGR SSPGQMPGIW RVRTLYACMA
     ENDGELSFEP NQIITNVKAS LEPGWLEGTL NGKTGLVPKN YVEQLP
//
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