ID A0A091Q9I3_MERNU Unreviewed; 1182 AA.
AC A0A091Q9I3;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 27-MAR-2024, entry version 46.
DE SubName: Full=Regulator of G-protein signaling 12 {ECO:0000313|EMBL:KFQ22085.1};
DE Flags: Fragment;
GN ORFNames=N331_01727 {ECO:0000313|EMBL:KFQ22085.1};
OS Merops nubicus (Northern carmine bee-eater).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Coraciiformes; Meropidae; Merops.
OX NCBI_TaxID=57421 {ECO:0000313|EMBL:KFQ22085.1, ECO:0000313|Proteomes:UP000052967};
RN [1] {ECO:0000313|EMBL:KFQ22085.1, ECO:0000313|Proteomes:UP000052967}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BGI_N331 {ECO:0000313|EMBL:KFQ22085.1};
RA Zhang G., Li C.;
RT "Genome evolution of avian class.";
RL Submitted (APR-2014) to the EMBL/GenBank/DDBJ databases.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
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DR EMBL; KK692076; KFQ22085.1; -; Genomic_DNA.
DR RefSeq; XP_008935427.1; XM_008937179.1.
DR AlphaFoldDB; A0A091Q9I3; -.
DR GeneID; 103769932; -.
DR KEGG; mnb:103769932; -.
DR CTD; 6002; -.
DR OrthoDB; 22856at2759; -.
DR Proteomes; UP000052967; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0005096; F:GTPase activator activity; IEA:UniProtKB-KW.
DR GO; GO:0007165; P:signal transduction; IEA:InterPro.
DR CDD; cd00992; PDZ_signaling; 1.
DR CDD; cd13162; PTB_RGS12; 1.
DR CDD; cd17136; RBD1_RGS12; 1.
DR CDD; cd17138; RBD2_RGS12; 1.
DR CDD; cd08742; RGS_RGS12; 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; 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; IPR037880; RGS12_RGS.
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:SF1; REGULATOR OF G-PROTEIN SIGNALING 12; 1.
DR PANTHER; PTHR45945; 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 Pfam; PF16613; RGS12_us1; 1.
DR Pfam; PF16611; RGS12_us2; 1.
DR PRINTS; PR01301; RGSPROTEIN.
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; PS50106; PDZ; 1.
DR PROSITE; PS01179; PID; 1.
DR PROSITE; PS50898; RBD; 2.
DR PROSITE; PS50132; RGS; 1.
PE 4: Predicted;
KW GTPase activation {ECO:0000256|ARBA:ARBA00022468};
KW Reference proteome {ECO:0000313|Proteomes:UP000052967};
KW Repeat {ECO:0000256|ARBA:ARBA00022737}.
FT DOMAIN 22..99
FT /note="PDZ"
FT /evidence="ECO:0000259|PROSITE:PS50106"
FT DOMAIN 226..338
FT /note="PID"
FT /evidence="ECO:0000259|PROSITE:PS01179"
FT DOMAIN 708..825
FT /note="RGS"
FT /evidence="ECO:0000259|PROSITE:PS50132"
FT DOMAIN 957..1027
FT /note="RBD"
FT /evidence="ECO:0000259|PROSITE:PS50898"
FT DOMAIN 1029..1099
FT /note="RBD"
FT /evidence="ECO:0000259|PROSITE:PS50898"
FT REGION 541..561
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 607..644
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 832..937
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1117..1158
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 609..623
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 841..867
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 868..890
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 913..937
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1117..1147
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT NON_TER 1182
FT /evidence="ECO:0000313|EMBL:KFQ22085.1"
SQ SEQUENCE 1182 AA; 130808 MW; DDB25E88190421C2 CRC64;
MYRPGETVKR RLNMHAPPRI RSVEVARGRA GYGFTLSGQA PCVLSCVMKG SPADYVGLKA
GDQIFAVNEI NVKKASHEDV VKLIGKCSGV LHMVIAEGIS HIDSCSSDEE VGFYDGKGWL
KPKPDSKALG INRAEKVVEE MQSGGIFNMI FENPTLCAGN SDNSAPKQRS FSASAAIRFE
TGNETVSNPN LLSKEEISKV LNDDSVFRIG LEGAEDFGLD ASILNVAMIV GYLGSIELPS
TTSNLENESL QAIRGCMRRL RAEQKIHSLV MMKIMHDCIQ LCSDKSGVVA EYPAEKLAFS
AVCPDDRRFF GLVTMQTNDD ASLAQEDEGV LRTSCHVFMV DPELFHHKIH QGIARRFGLE
CTADPDTNGC LEFPTSSLPV LQFISVLYRD MGELIEGMRA RAFLDGDADA HQNNSTSSNS
DSGIGNFNQE EKNNRVLVVD LGSNPSKHIP NSMWENPVGR GQNQPSSHWN GFCHDQEGNI
PLEVIQNEKS QNASKHLSPS ARIEVPLVSS RNSVPPSKKH PAGTGSQRWL PVHVLQEWQQ
GNASDQESYT DSTDGWSSVN CGTLPPPMSK IPADRYRVDG SFAQPQLKSH KNEWSKKMFC
MQNKFVPPHS IRKSKEDKKG AKFGHPPGLN QAPPPRSSVR RSFGRSKRFS ITRSLDDLES
ATVSDGELNS TDLKDCISEN SLSSNASLPS VQSCRRLRER RVASWAVSFE RLLQDPLGVK
YFSEFLRKEF SEENILFWQA CEYFNHVPAH DKKELSYRAR EIFSKFLCSK ATTPVNIDSQ
AQLADDILNS PHPDMFKEQQ LQIFNLMKFD SYTRFLKSPL YQECILAEVE GRPLPDPQRV
PSSPTSKHSI SSEKSNISTP KKLSGKSKSG RSLNEESGEE DTEKKKRGTF FSWSRSKSLG
KSQKRKENGD YPHDSIQSNG LSYRRESQGS MSSTASLDLS EASRLPAFLP DKEKSPKYCC
INLPDGSSSK MAVKSGFSIK EVLSGLCEKH GINIAAVDLF LVGGDKPLVL HQDSSILESR
DLRLEKRTLF RLDLVPINRS VGLKAKPTKP VTEVLRPVVA KYGLNLNELV ARLNGEQEPL
DLGVPISNLD GQRVVLDEKE PTKGRVFTDK QKGASVKQSA TVTTSRNQVS TGEGRTLGKS
NSIKMKGENG KNAREVRLSK REDSIAKIGK KKCQKINLDE AE
//
