ID A0A151J0G8_9HYME Unreviewed; 1620 AA.
AC A0A151J0G8;
DT 08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT 08-JUN-2016, sequence version 1.
DT 24-JAN-2024, entry version 26.
DE SubName: Full=Pleckstrin homology domain-containing family G member 1 {ECO:0000313|EMBL:KYN14961.1};
GN ORFNames=ALC57_12822 {ECO:0000313|EMBL:KYN14961.1};
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:KYN14961.1, ECO:0000313|Proteomes:UP000078492};
RN [1] {ECO:0000313|EMBL:KYN14961.1, ECO:0000313|Proteomes:UP000078492}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Tcor2-1 {ECO:0000313|EMBL:KYN14961.1};
RC TISSUE=Whole body {ECO:0000313|EMBL:KYN14961.1};
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; KQ980634; KYN14961.1; -; Genomic_DNA.
DR STRING; 471704.A0A151J0G8; -.
DR Proteomes; UP000078492; Unassembled WGS sequence.
DR GO; GO:0003677; F:DNA binding; IEA:InterPro.
DR GO; GO:0005085; F:guanyl-nucleotide exchange factor activity; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR CDD; cd13243; PH_PLEKHG1_G2_G3; 1.
DR CDD; cd00160; RhoGEF; 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; IPR035899; DBL_dom_sf.
DR InterPro; IPR000219; DH-domain.
DR InterPro; IPR011993; PH-like_dom_sf.
DR InterPro; IPR001849; PH_domain.
DR InterPro; IPR043324; PH_PLEKHG1_G2_G3.
DR InterPro; IPR003656; Znf_BED.
DR PANTHER; PTHR45924; FI17866P1; 1.
DR PANTHER; PTHR45924:SF2; FI17866P1; 1.
DR Pfam; PF00621; RhoGEF; 1.
DR Pfam; PF02892; zf-BED; 2.
DR SMART; SM00233; PH; 1.
DR SMART; SM00325; RhoGEF; 1.
DR SMART; SM00614; ZnF_BED; 2.
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.
PE 4: Predicted;
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000078492};
KW Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT DOMAIN 467..654
FT /note="DH"
FT /evidence="ECO:0000259|PROSITE:PS50010"
FT DOMAIN 678..778
FT /note="PH"
FT /evidence="ECO:0000259|PROSITE:PS50003"
FT REGION 345..400
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 803..870
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 935..964
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1160..1184
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1226..1267
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1353..1378
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1419..1464
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 379..400
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 806..851
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 939..955
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1160..1177
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1230..1254
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1433..1464
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1620 AA; 183874 MW; 01D2DF4EC647B4DE CRC64;
MAEQGATYFR DVFPVRRWIR KHYTKIRGRN TANCNHCSKQ IGIRRLFYLH DHLVKAHSNE
LTEDEKKDKL LHWVWDYFTI KDTHHATCNI CGKKLKYYTT NLYLRRHLKN VHGHTANCNH
CLKQIGIRPL ILLFNHLVQV HSNELTEGEK EDKLLHWVWD HFTIKDTQNA TCNICGSELK
RDLMRNLSQH LKNVHGILPP CTDDMDNVSS DANPDTTIKE DQLHSATLTK ICTSTDLVPQ
LLGMFDELAR RSDGYDGDRV VLPSSCGISA VLQKRLSMVP VAHRSSVFGQ LCTNGDLAKP
MYQDMLKTKE QEDEYDEVVA DASNNAMLET IIPVIMLEQE GNGETIEETT GKPMYERRET
NGLTTPLRYK RRRNGGRPLS GSSIASSTSS SSCSNQGNTS AANPYLASVE SLADTCASSQ
GSADSGVVTV SEASCRILND DNGQRRNSAE EDPLCHRPRY CDPHRNPVER VLLEIVDTEA
IYVEHLRQII QGYLIFWRDN PPSFSRRLRL GDLFSNIEDI FEFNREFLWE IEKCGLDPVC
VANTFIKRNS GFKVYTEYCT NYPRTVSVLT DLMGQEETAS SFHERQEALR HQLPLGSFLL
KPVQRILKYH LLLENLSKEY GADCDLRENE AEGRSAIEAA LAAMTGIAKH INAMKRRHEH
AVRVQEIQSL LYGWLGPDLT TSGELVAEGR FRMRGAKAPR HAFLFDRMLL LTKKKEDSLL
IYKAHIMCSN LMLIESIPGE PLSFHVIPFD NPRLQYTLQA RNLEQKREWT LQIKRVILEN
YNAVIPSHAR QLVLQLGQTQ QEDDALTDKG SAKKHSAPPE YLEKRKQERE RRRSETSLKQ
KFMRGVRKSD TTMEDSPTSS CKNDNEDINV SREPTFSRSD VRASKVRDRF TGWRRKSEPG
FQSYVCLNHL DEEQKEATTS DAQSTTVEIA EEATEICTKE ENQTTLNSSS PAEAKDNNEQ
HAKPAQTVEE IVSHILMQNQ EFQKLLEKQQ TNSIINVRQQ RFNKRISTDT SDESDSENAN
YVTSSISHNN NNNRLGRVRA LHRERLIRTN NAWNLLSSAP ARENQQPLQL LYDNLKTTQK
STETLAHNGR TNQLYERQAF KRQSIVTESK VIKTALRIRE NSTSTGNEET VISPAKCMLN
HRTVERKEIN SIVMTERIEK DGSERCNDER SDANDAGDAE SKGFGNYDNL QHVWEGLQTI
KGDADGNDSP TQPAVWLTKL CEGLPTSPPK SGSLPRSFQI SPNSQPTSVT KSRFLQRDGK
PMSERPFTIA SDKPAEINLE DMERYASTCQ PEGRIAKFPM PTVSTSSSTT IFRSVFKAGS
RLQGRLRNTM STETLECNDE VERTRYFRSL SSGVKYPKKR TKQTKQHARE PSSDVEELMG
CSNDQRIPQL YYKQGSSSLG ARIAQSDYAD PTILFAESKR AQSSSVDINQ SKNTAESERR
DCEEETGSNK DTEHHESETD SFYEKSFETI ENYADVDEAF RDSAIFSDVD EAYVMRQSTP
VTIAKMTTME TAAAIAKTKI APPVPAKKKQ EMSSIKYKPN VAQKPDYLKI KSLLARGHPA
GNSETRVTTR LVNVTHQPLD SSSNNYKRNI EMDRDDVSAG QSQAGWVRKI VGQLQGHVET
//
