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Database: UniProt
Entry: A0A195EMC3_9HYME
LinkDB: A0A195EMC3_9HYME
Original site: A0A195EMC3_9HYME 
ID   A0A195EMC3_9HYME        Unreviewed;      1259 AA.
AC   A0A195EMC3;
DT   05-OCT-2016, integrated into UniProtKB/TrEMBL.
DT   05-OCT-2016, sequence version 1.
DT   24-JAN-2024, entry version 29.
DE   SubName: Full=Protein ECT2 {ECO:0000313|EMBL:KYN29276.1};
GN   ORFNames=ALC57_01399 {ECO:0000313|EMBL:KYN29276.1};
OS   Trachymyrmex cornetzi.
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Hymenoptera; Apocrita; Aculeata; Formicoidea;
OC   Formicidae; Myrmicinae; Trachymyrmex.
OX   NCBI_TaxID=471704 {ECO:0000313|EMBL:KYN29276.1, ECO:0000313|Proteomes:UP000078492};
RN   [1] {ECO:0000313|EMBL:KYN29276.1, ECO:0000313|Proteomes:UP000078492}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Tcor2-1 {ECO:0000313|EMBL:KYN29276.1};
RC   TISSUE=Whole body {ECO:0000313|EMBL:KYN29276.1};
RA   Nygaard S., Hu H., Boomsma J., Zhang G.;
RT   "Trachymyrmex cornetzi WGS genome.";
RL   Submitted (SEP-2015) to the EMBL/GenBank/DDBJ databases.
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DR   EMBL; KQ978691; KYN29276.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A195EMC3; -.
DR   STRING; 471704.A0A195EMC3; -.
DR   Proteomes; UP000078492; Unassembled WGS sequence.
DR   GO; GO:0005737; C:cytoplasm; IEA:InterPro.
DR   GO; GO:0005634; C:nucleus; IEA:InterPro.
DR   GO; GO:0005096; F:GTPase activator activity; IEA:InterPro.
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:2000431; P:regulation of cytokinesis, actomyosin contractile ring assembly; IEA:InterPro.
DR   CDD; cd01229; PH_Ect2; 1.
DR   CDD; cd00160; RhoGEF; 1.
DR   Gene3D; 3.40.50.10190; BRCT domain; 3.
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; IPR001357; BRCT_dom.
DR   InterPro; IPR036420; BRCT_dom_sf.
DR   InterPro; IPR035899; DBL_dom_sf.
DR   InterPro; IPR000219; DH-domain.
DR   InterPro; IPR026817; Ect2.
DR   InterPro; IPR049396; ECT2_BRCT0.
DR   InterPro; IPR049395; ECT2_PH.
DR   InterPro; IPR001331; GDS_CDC24_CS.
DR   InterPro; IPR011993; PH-like_dom_sf.
DR   PANTHER; PTHR16777; PROTEIN ECT2; 1.
DR   PANTHER; PTHR16777:SF2; PROTEIN ECT2; 1.
DR   Pfam; PF00533; BRCT; 1.
DR   Pfam; PF21243; ECT2_BRCT0; 1.
DR   Pfam; PF21242; ECT2_PH; 1.
DR   Pfam; PF12738; PTCB-BRCT; 1.
DR   Pfam; PF00621; RhoGEF; 1.
DR   SMART; SM00292; BRCT; 2.
DR   SMART; SM00325; RhoGEF; 1.
DR   SUPFAM; SSF52113; BRCT domain; 2.
DR   SUPFAM; SSF48065; DBL homology domain (DH-domain); 1.
DR   SUPFAM; SSF50729; PH domain-like; 1.
DR   PROSITE; PS50172; BRCT; 1.
DR   PROSITE; PS00741; DH_1; 1.
DR   PROSITE; PS50010; DH_2; 1.
PE   4: Predicted;
KW   Reference proteome {ECO:0000313|Proteomes:UP000078492}.
FT   DOMAIN          115..188
FT                   /note="BRCT"
FT                   /evidence="ECO:0000259|PROSITE:PS50172"
FT   DOMAIN          779..969
FT                   /note="DH"
FT                   /evidence="ECO:0000259|PROSITE:PS50010"
FT   REGION          1221..1259
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1259 AA;  142409 MW;  C87DE19E45034A35 CRC64;
     MEERSVHSSI GDINSAEATK TLIIPRKKRI CLVGTTCNDP ALNVAAQQFK VPVLKSETGT
     EYVEDTTYNT YFILKQFEGS EYDALCKSAH RVLGPTALLQ LAEKKEPLPS IKRPMYTQAM
     VGTIVVFSGF RAREDELRKL ANMILNMGGS IRKEMGIKVT HLIANHCSGE KYRYADTFGL
     PIMSIEWVIA LWNAKDDIST YANNEELIAT YKLKPFYGAK VCFSGFPEEE KKHMCEILEQ
     QGGEPTEIDD PNCTHVVVDI SGLFYKRANV DLYLKNTSNN PPSLTYIKPT LSLYPYSNAI
     FNTTKTDYSI ISNYLSSKNN SLISYTHDVE YNNQWNDLVS IYNISQDSAI SMNDNCVNLQ
     NSIIKSGNLY HSFTEQSDSG IDITRSSNSS STIFMSNKYS VPTPPTIINN KNIKFYISES
     SLFDNGVSFY ENSSNFPDKP DDLKSLPSYE KNNEYNPCSS TMSNSTLSLK YRKNIHYVQN
     NTSKSKIKRY IKWRKTNSCP FIHKMATLEK YKFMKTRSYP NILEHNEEQY SDTFLHNALG
     ERNKHLSKSH TSFFSKINHF SFCPIFSDSK KDISTSSYYC PSEKTLFKKK CTSLSKSFPM
     PTKISNTKHN LQNTSIFDGK SNNVSSAPHD LKTECTDLKT QDRSLLVVVD ESNVNVLPNL
     VSVSAFIVKT GWFWTSVQNE AAADEKEYLF EHYLEKVLSP TATGRRDSQQ IVSQNVTLSK
     HPCWLGGPLS NLLQNGADSP ASVSGSFLDC TASPDKQLLD EVESVATEHL PIVKENLSQR
     HKVFLELVET EANYVGILNT IMTLFKLPLE NLIGKSGKEL LNSTEVKIIF GNFPPIYDVH
     KQLLEALHCS AAHWTEDISI GEIFLKFEPD LVKAYPPYVN FFENTKQMLE ECDQNKPRFH
     AFLKNCQTIP ECGRQSLKEL LIKPIQRLPS ISLLLSDILK HTDKSNPDYS ALEASISCIK
     KVMTYINEDK RKTERQLAMF DIFNEIDNCP PHLVSSHRSF ISKCDVMEVT ERLSGRGDHL
     VLFLFTDTLE ICKKRSKAFN SLKSPNTING LQSIKLSQGK PYKHIKMLSL STIRKVVDIR
     ETDECHKVFT LVVRGTQELK ETFFSFIITD EEVNKTNYLQ TLCRQMALAV RVADADTLLI
     RYDWHQLEVG TSDVASGTLK KTIKFASRTR ARVGRAFSFN KTPSKLNRAM STIMSPFGVT
     QNLPPTNQQI AQMRLGSCNN ISELDNGGSS SPNREDVLVA PMSDQPTRKA LSMASLRRL
//
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