ID A0A0L7QKI4_9HYME Unreviewed; 1338 AA.
AC A0A0L7QKI4;
DT 11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT 11-NOV-2015, sequence version 1.
DT 27-MAR-2024, entry version 40.
DE SubName: Full=Regulator of G-protein signaling loco {ECO:0000313|EMBL:KOC59139.1};
GN ORFNames=WH47_11215 {ECO:0000313|EMBL:KOC59139.1};
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:KOC59139.1, ECO:0000313|Proteomes:UP000053825};
RN [1] {ECO:0000313|EMBL:KOC59139.1, ECO:0000313|Proteomes:UP000053825}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=0110345459 {ECO:0000313|EMBL:KOC59139.1};
RA Pan H., Kapheim K.;
RT "The genome of Habropoda laboriosa.";
RL Submitted (JUL-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; KQ414940; KOC59139.1; -; Genomic_DNA.
DR STRING; 597456.A0A0L7QKI4; -.
DR Proteomes; UP000053825; Unassembled WGS sequence.
DR GO; GO:0071944; C:cell periphery; IEA:UniProt.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005096; F:GTPase activator activity; IEA:UniProtKB-KW.
DR GO; GO:0048699; P:generation of neurons; IEA:UniProt.
DR GO; GO:0051179; P:localization; IEA:UniProt.
DR GO; GO:0007165; P:signal transduction; IEA:InterPro.
DR CDD; cd00992; PDZ_signaling; 1.
DR CDD; cd01817; RBD1_RGS12_like; 1.
DR Gene3D; 1.10.196.10; -; 1.
DR Gene3D; 2.30.42.10; -; 1.
DR Gene3D; 2.30.29.30; Pleckstrin-homology domain (PH domain)/Phosphotyrosine-binding domain (PTB); 1.
DR Gene3D; 1.10.167.10; Regulator of G-protein Signalling 4, domain 2; 1.
DR InterPro; IPR003109; GoLoco_motif.
DR InterPro; IPR001478; PDZ.
DR InterPro; IPR036034; PDZ_sf.
DR InterPro; IPR011993; PH-like_dom_sf.
DR InterPro; IPR006020; PTB/PI_dom.
DR InterPro; IPR003116; RBD_dom.
DR InterPro; IPR016137; RGS.
DR InterPro; IPR046995; RGS10/12/14-like.
DR InterPro; IPR036305; RGS_sf.
DR InterPro; IPR024066; RGS_subdom1/3.
DR InterPro; IPR044926; RGS_subdomain_2.
DR InterPro; IPR029071; Ubiquitin-like_domsf.
DR PANTHER; PTHR45945; REGULATOR OF G-PROTEIN SIGNALING LOCO; 1.
DR PANTHER; PTHR45945:SF3; REGULATOR OF G-PROTEIN SIGNALING LOCO; 1.
DR Pfam; PF00595; PDZ; 1.
DR Pfam; PF00640; PID; 1.
DR Pfam; PF02196; RBD; 1.
DR Pfam; PF00615; RGS; 1.
DR PRINTS; PR01301; RGSPROTEIN.
DR SMART; SM00390; GoLoco; 1.
DR SMART; SM00228; PDZ; 1.
DR SMART; SM00462; PTB; 1.
DR SMART; SM00455; RBD; 2.
DR SMART; SM00315; RGS; 1.
DR SUPFAM; SSF50156; PDZ domain-like; 1.
DR SUPFAM; SSF50729; PH domain-like; 1.
DR SUPFAM; SSF48097; Regulator of G-protein signaling, RGS; 1.
DR SUPFAM; SSF54236; Ubiquitin-like; 2.
DR PROSITE; PS50877; GOLOCO; 1.
DR PROSITE; PS50106; PDZ; 1.
DR PROSITE; PS50898; RBD; 1.
DR PROSITE; PS50132; RGS; 1.
PE 4: Predicted;
KW GTPase activation {ECO:0000256|ARBA:ARBA00022468};
KW Reference proteome {ECO:0000313|Proteomes:UP000053825};
KW Repeat {ECO:0000256|ARBA:ARBA00022737}.
FT DOMAIN 17..94
FT /note="PDZ"
FT /evidence="ECO:0000259|PROSITE:PS50106"
FT DOMAIN 629..746
FT /note="RGS"
FT /evidence="ECO:0000259|PROSITE:PS50132"
FT DOMAIN 879..949
FT /note="RBD"
FT /evidence="ECO:0000259|PROSITE:PS50898"
FT REGION 361..393
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 454..478
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 786..813
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1066..1085
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1094..1125
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1215..1338
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 361..391
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 456..470
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 786..806
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1224..1289
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1338 AA; 148631 MW; 4129D4ABDBD9246B CRC64;
MHQNRRKKKR VNYGVRAVEV LRGMKGFGFT ISGQQPCILS CIVPGSPADI AGLRAGDYLV
SVNGHNVSKL PHDDVVQLIG RSKGTLRLQI AENYYSDSSD EEGVTTVRCK PKYIHKPRAS
NMGALQLQCR VAKVVRDLQS GAMFDATGKT PPELQGHGTY CDLHYHWDMS SPLPPPPPPA
SHKRDSEKIV HRTVVGYLGT IDIPNQLHPS CMMQVLRKCI KRLKAEKRNP TTVLLTIHVA
NIKLTNSENR IIAEYPSYRI IFCNSFSEQD KQYFGILTKS VKDKENIVSN SCHVFTIYYK
LIDHTVHSSV CNIFGFTCTK TSELNVCQEF PDSCNGLIGA IQTLYISDST ATDTNPYNEM
RRHQETASPQ PSNISTSTAH SSNSDSGIGY KDDCTSRSDK NIIQNASRRR CPASEYRDAC
EYSSKLYGNE AVDLRLTVRA VSNACWNEAN KSDMCKENSE TNSGTQKGTK RGDLPTCPLP
SASTVKQGLV SSSVGSLVSV CTTAMLHSID DSIETSDDSI IKSNRLPRVT GLGKLTGTDD
TRDKFSPKVF SGISKSLVHS FEDLNTTSMD YVRPLCQTYS DKSDNSRPWG SLQEIRNVGA
CVQDTCLHGS TELCDKSTDC KNIHTWASGF ERLLEDQKGL QTFAEFLKKE FSHENIYFWA
ACERYKDTKD VVTRRKLANQ IYQRHLSAKA AEPVNVDSHA AGQITQDLLS EAPADLFLQA
QKQVFNLMKF DSYPRFLRSD LYRRCVETGS TIIGVEDCDL NLTSSPSVKL KKSHSDAEDR
CRKSILPWNR KNRSKSKDRG ESEYNNKAPN RNETIYKSFT TMKREVEGNN NDDSISISSS
RSSLASWDLA LRQSFHKHSL SSYEGQSNET KEVRAKCTGL CRVILPDGST TVVPTSQTES
IKDVVTRLLD KRALRYSNYD VLILATDETV EAKYSSSVLA GQEVEVVPTK ILKVDLPSRR
VITVIAHKGR TLKEVLRPLL NKYGFNLDMV TVWSENHRVS MDIQAIDAPA RLIFTTNIKE
EDPEKESNTV KYTHDASNAQ PTLDEITNRV FEELLVGKGS SKYHYNDGSC KSDDQRSEGS
SSILPSKFFL RDSTMHGKKK GGKSKCNTNE KSNGGNDYAC EESGKSHPPL IAKWRNGVKL
QLPGKFDGED LYEGLKRAQR SRLEDQRGTE INFELPDFLK NKENGKPTDR NKIRRPRILP
TNCEANAKFY GSIHERKNCS SSGGHDQKTR MTVMGGGSAS KNGNADERYH VSSSASGKES
QKNGSCSRTV AALGTLDAQA DSSSAVTKSS KPPPLPPKPK NLVTGPAKTG YPVVSSKPLP
KSNRAVPFSP IEPSRKNI
//
