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Database: UniProt
Entry: A0A914KPG5_MELIC
LinkDB: A0A914KPG5_MELIC
Original site: A0A914KPG5_MELIC 
ID   A0A914KPG5_MELIC        Unreviewed;       595 AA.
AC   A0A914KPG5;
DT   22-FEB-2023, integrated into UniProtKB/TrEMBL.
DT   22-FEB-2023, sequence version 1.
DT   02-APR-2025, entry version 8.
DE   SubName: Full=Uncharacterized protein {ECO:0000313|WBParaSite:Minc3s00065g03316};
OS   Meloidogyne incognita (Southern root-knot nematode).
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC   Tylenchina; Tylenchomorpha; Tylenchoidea; Meloidogynidae; Meloidogyninae;
OC   Meloidogyne; Meloidogyne incognita group.
OX   NCBI_TaxID=6306 {ECO:0000313|Proteomes:UP000887563, ECO:0000313|WBParaSite:Minc3s00065g03316};
RN   [1] {ECO:0000313|WBParaSite:Minc3s00065g03316}
RP   IDENTIFICATION.
RG   WormBaseParasite;
RL   Submitted (NOV-2022) to UniProtKB.
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DR   WBParaSite; Minc3s00065g03316; Minc3s00065g03316; Minc3s00065g03316.
DR   Proteomes; UP000887563; Unplaced.
DR   GO; GO:0005737; C:cytoplasm; IEA:TreeGrafter.
DR   GO; GO:0043005; C:neuron projection; IEA:TreeGrafter.
DR   GO; GO:0005096; F:GTPase activator activity; IEA:TreeGrafter.
DR   GO; GO:0007186; P:G protein-coupled receptor signaling pathway; IEA:InterPro.
DR   GO; GO:0035556; P:intracellular signal transduction; IEA:InterPro.
DR   GO; GO:0009968; P:negative regulation of signal transduction; IEA:UniProtKB-KW.
DR   GO; GO:0008277; P:regulation of G protein-coupled receptor signaling pathway; IEA:InterPro.
DR   CDD; cd04450; DEP_RGS7-like; 1.
DR   FunFam; 1.10.10.10:FF:000162; Regulator of G-protein signaling 6; 1.
DR   FunFam; 1.10.1240.60:FF:000001; Regulator of G-protein signaling 6; 1.
DR   Gene3D; 1.10.1240.60; -; 1.
DR   Gene3D; 1.10.167.10; Regulator of G-protein Signalling 4, domain 2; 1.
DR   Gene3D; 1.10.10.10; Winged helix-like DNA-binding domain superfamily/Winged helix DNA-binding domain; 1.
DR   InterPro; IPR000591; DEP_dom.
DR   InterPro; IPR015898; G-protein_gamma-like_dom.
DR   InterPro; IPR036284; GGL_sf.
DR   InterPro; IPR016137; RGS.
DR   InterPro; IPR047016; RGS6/7/9/11.
DR   InterPro; IPR047017; RGS6/7/9/11_DHEX_sf.
DR   InterPro; IPR040759; RGS_DHEX.
DR   InterPro; IPR036305; RGS_sf.
DR   InterPro; IPR044926; RGS_subdomain_2.
DR   InterPro; IPR036388; WH-like_DNA-bd_sf.
DR   InterPro; IPR036390; WH_DNA-bd_sf.
DR   PANTHER; PTHR45746; LP21163P; 1.
DR   PANTHER; PTHR45746:SF6; LP21163P; 1.
DR   Pfam; PF00610; DEP; 1.
DR   Pfam; PF00631; G-gamma; 1.
DR   Pfam; PF00615; RGS; 1.
DR   Pfam; PF18148; RGS_DHEX; 1.
DR   PRINTS; PR01301; RGSPROTEIN.
DR   SMART; SM00049; DEP; 1.
DR   SMART; SM01224; G_gamma; 1.
DR   SMART; SM00224; GGL; 1.
DR   SMART; SM00315; RGS; 1.
DR   SUPFAM; SSF48097; Regulator of G-protein signaling, RGS; 1.
DR   SUPFAM; SSF48670; Transducin (heterotrimeric G protein), gamma chain; 1.
DR   SUPFAM; SSF46785; Winged helix' DNA-binding domain; 1.
DR   PROSITE; PS50186; DEP; 1.
DR   PROSITE; PS50132; RGS; 1.
PE   4: Predicted;
KW   Reference proteome {ECO:0000313|Proteomes:UP000887563};
KW   Signal transduction inhibitor {ECO:0000256|ARBA:ARBA00022700}.
FT   DOMAIN          42..118
FT                   /note="DEP"
FT                   /evidence="ECO:0000259|PROSITE:PS50186"
FT   DOMAIN          364..480
FT                   /note="RGS"
FT                   /evidence="ECO:0000259|PROSITE:PS50132"
FT   REGION          498..595
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        503..524
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        529..538
FT                   /note="Low complexity"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        550..572
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        586..595
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   595 AA;  69060 MW;  18F3465182923356 CRC64;
     MASSNCTNTT SCSTSFAEEK HPHPNMLIYR KMEKLINQML HSEDGIKIKT VKSFLSKIVS
     VFSGQDLIVW LIAHIDVFDE IDANHLLHLF ASHGYIFQVD DHVITMKGGD TSFYRFQTPY
     FWPSNCWEPE NMDYAVYLCK RTMQNKAHLE LEDFEAENLA KLQKMLSRKW EFVFMQAEAQ
     YKVDKKRDRI ERQILDSQER AFWDLHRPVP GCVNTTEVDI RKLSRSGRSK QSTCNTLVIQ
     MEDSESQLNN SNNLKTPNIR EVRFYQKPGR RRYTQIKDYL KIEISELQTR LSKNVLKTSK
     LAESYLQYYG HRVSFDAFIV QLGSATDPFQ GQPNPWISDT VDFWQHDKIT GDISTRRLKL
     WEESFEELLI DPVGRETLQK FLDKEYSGEN LRFWMEVQKL RKCSCRMVPV LVTEIYNEFI
     DSNAQSPVNI DCKVMEIIDE NLKNNPNRWS FDEAADHIFC LMKNDSYQRF LRSDLYRDLL
     NISGKKYSFS TLISRKASRK TPSKTTTNQQ SLDNPQFPLN TLNTCKGLRG SSGSRSGSFV
     GIEREKRTKC QPNSFDSSTL TMTKNNVNSS NRGIRRDSSS CSSSSVAAQQ RSNNN
//
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