ID A0A0L7QYC3_9HYME Unreviewed; 1071 AA.
AC A0A0L7QYC3;
DT 11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT 11-NOV-2015, sequence version 1.
DT 08-NOV-2023, entry version 38.
DE SubName: Full=Ras GTPase-activating protein 3 {ECO:0000313|EMBL:KOC63546.1};
GN ORFNames=WH47_02942 {ECO:0000313|EMBL:KOC63546.1};
OS Habropoda laboriosa.
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Hymenoptera; Apocrita; Aculeata; Apoidea;
OC Anthophila; Apidae; Habropoda.
OX NCBI_TaxID=597456 {ECO:0000313|EMBL:KOC63546.1, ECO:0000313|Proteomes:UP000053825};
RN [1] {ECO:0000313|EMBL:KOC63546.1, ECO:0000313|Proteomes:UP000053825}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=0110345459 {ECO:0000313|EMBL:KOC63546.1};
RA Pan H., Kapheim K.;
RT "The genome of Habropoda laboriosa.";
RL Submitted (JUL-2015) to the EMBL/GenBank/DDBJ databases.
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DR EMBL; KQ414695; KOC63546.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0L7QYC3; -.
DR STRING; 597456.A0A0L7QYC3; -.
DR EnsemblMetazoa; XM_017936458.1; XP_017791947.1; LOC108573965.
DR Proteomes; UP000053825; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0005096; F:GTPase activator activity; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0035556; P:intracellular signal transduction; IEA:InterPro.
DR CDD; cd04010; C2B_RasA3; 1.
DR CDD; cd01244; PH_GAP1-like; 1.
DR CDD; cd05128; RasGAP_GAP1_like; 1.
DR Gene3D; 2.60.40.150; C2 domain; 2.
DR Gene3D; 2.30.29.30; Pleckstrin-homology domain (PH domain)/Phosphotyrosine-binding domain (PTB); 1.
DR InterPro; IPR000008; C2_dom.
DR InterPro; IPR035892; C2_domain_sf.
DR InterPro; IPR011993; PH-like_dom_sf.
DR InterPro; IPR001849; PH_domain.
DR InterPro; IPR039360; Ras_GTPase.
DR InterPro; IPR023152; RasGAP_CS.
DR InterPro; IPR001936; RasGAP_dom.
DR InterPro; IPR008936; Rho_GTPase_activation_prot.
DR InterPro; IPR001562; Znf_Btk_motif.
DR PANTHER; PTHR10194:SF60; GTPASE-ACTIVATING PROTEIN; 1.
DR PANTHER; PTHR10194; RAS GTPASE-ACTIVATING PROTEINS; 1.
DR Pfam; PF00779; BTK; 1.
DR Pfam; PF00168; C2; 2.
DR Pfam; PF00169; PH; 1.
DR Pfam; PF00616; RasGAP; 2.
DR SMART; SM00107; BTK; 1.
DR SMART; SM00239; C2; 2.
DR SMART; SM00233; PH; 1.
DR SMART; SM00323; RasGAP; 1.
DR SUPFAM; SSF49562; C2 domain (Calcium/lipid-binding domain, CaLB); 2.
DR SUPFAM; SSF48350; GTPase activation domain, GAP; 1.
DR SUPFAM; SSF50729; PH domain-like; 1.
DR PROSITE; PS50004; C2; 2.
DR PROSITE; PS50003; PH_DOMAIN; 1.
DR PROSITE; PS00509; RAS_GTPASE_ACTIV_1; 1.
DR PROSITE; PS50018; RAS_GTPASE_ACTIV_2; 1.
DR PROSITE; PS51113; ZF_BTK; 1.
PE 4: Predicted;
KW GTPase activation {ECO:0000256|ARBA:ARBA00022468};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000053825};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00432}.
FT TRANSMEM 935..953
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 1..61
FT /note="C2"
FT /evidence="ECO:0000259|PROSITE:PS50004"
FT DOMAIN 74..212
FT /note="C2"
FT /evidence="ECO:0000259|PROSITE:PS50004"
FT DOMAIN 289..483
FT /note="Ras-GAP"
FT /evidence="ECO:0000259|PROSITE:PS50018"
FT DOMAIN 544..645
FT /note="PH"
FT /evidence="ECO:0000259|PROSITE:PS50003"
FT REGION 986..1048
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 986..1026
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1071 AA; 122245 MW; 9C14B9A8D95AC73A CRC64;
MERTLNPFFG EEFQFEVPRK FRYLGIYVYD RDRHLRQDKI LGKVAIKRED LATYHNKEHW
FPLRPVDADS EVQGKAHLEL ALQPQIGHVP TKLTVRVIEC SELTIKNGGC DPFATITVIY
SNGKQVLKRT KIKKKTVSPY FNETFIFEPE ITESKEKDIS HYPLEHGEVG EVVVGLWHAS
PGMGEQPAFL GEVRVTLRGL QKQPTSTTTA WYFLQPRAVK HRPNKISNSS TSPGTLPGLG
SLRLKIHYTT DHVFPSAMYD RLRNLLLQSV NIQPITSSAV YILGEIVASK MEAAQPLVRV
LVHYGQLVSV MQALASHEIS KLTDPTTIFR GNTLVSKMMD EGMRLAGLHY LHNTLRPAME
QVFLEKKPCE IDPTRVKDAN TIQTNLTNLK EYVERVFSAI TTSGVRCPPL MCEMFWCLRE
LAATHFPKNK EVRYSVISGF IFLRFFAPAI LGPRLFDITT EQIDSQTNRT LTLISKTIQS
LGNLVSCRGG AGSVCKEEYM ECVYREFYTE KHIQAVKQFL ELISTSSNSA IAKQRTSTQQ
EQPIVLKEGV MIKRAQGRKR FGRKNFKQRY FRLTTQDLTY SKTKGKEPLC TIPLEEILAV
EKLQEDSFKM KNMFQIIQSQ RALYVQAGNC VEEKEWIDIL TKICRTNSNR LEKYHPSAYI
NGYWLCCKAI AEIAPGCSEV SPGVEAGLRM VLDPDRDLQR IHSLIFTNMP RLETLMSACE
CQAVYGANDM CIIPGGGSPI EDVPSCFKTL TALREAAYAL QHEHRAYLRR LARDTKYGSK
QAPIGDDNYL HLAARVGFES QLTKRAYEVD NLNQHYVETD HCYNSGFSRR IEDQRSYNET
FRKCLDSDSI RSLLVTHEIN MSDTLPRKFN SYDHTKILNE CTVTKFRDDK PDISYEEDNV
IPPPTTGNVN ENLTDNITIH VYKENSTGGH WCARIIFFVV LALLVGLIGV VIFEHRGTTD
INTPLKSSRW AFIFDGWVDD SFLLSDEESH GNEPEEHETH DETEEIERDG NKLDETTELE
IIETKVSTEE ETEEENEISN EYTGQQEKTI IENELNEEES ELFQSEEGIK V
//
