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Database: UniProt
Entry: A0A1I8HQR3_9PLAT
LinkDB: A0A1I8HQR3_9PLAT
Original site: A0A1I8HQR3_9PLAT 
ID   A0A1I8HQR3_9PLAT        Unreviewed;       664 AA.
AC   A0A1I8HQR3;
DT   18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT   18-JAN-2017, sequence version 1.
DT   24-JAN-2024, entry version 27.
DE   SubName: Full=Centaurin-gamma-1A {ECO:0000313|WBParaSite:maker-uti_cns_0007435-snap-gene-0.3-mRNA-1};
OS   Macrostomum lignano.
OC   Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Platyhelminthes;
OC   Rhabditophora; Macrostomorpha; Macrostomida; Macrostomidae; Macrostomum.
OX   NCBI_TaxID=282301 {ECO:0000313|Proteomes:UP000095280, ECO:0000313|WBParaSite:maker-uti_cns_0007435-snap-gene-0.3-mRNA-1};
RN   [1] {ECO:0000313|WBParaSite:maker-uti_cns_0007435-snap-gene-0.3-mRNA-1}
RP   IDENTIFICATION.
RG   WormBaseParasite;
RL   Submitted (NOV-2016) to UniProtKB.
CC   -!- SIMILARITY: Belongs to the centaurin gamma-like family.
CC       {ECO:0000256|ARBA:ARBA00005430}.
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DR   AlphaFoldDB; A0A1I8HQR3; -.
DR   WBParaSite; maker-uti_cns_0007435-snap-gene-0.3-mRNA-1; maker-uti_cns_0007435-snap-gene-0.3-mRNA-1; maker-uti_cns_0007435-snap-gene-0.3.
DR   Proteomes; UP000095280; Unplaced.
DR   GO; GO:0005096; F:GTPase activator activity; IEA:InterPro.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   Gene3D; 1.25.40.20; Ankyrin repeat-containing domain; 1.
DR   Gene3D; 1.10.220.150; Arf GTPase activating protein; 1.
DR   Gene3D; 2.30.29.30; Pleckstrin-homology domain (PH domain)/Phosphotyrosine-binding domain (PTB); 1.
DR   InterPro; IPR002110; Ankyrin_rpt.
DR   InterPro; IPR036770; Ankyrin_rpt-contain_sf.
DR   InterPro; IPR037278; ARFGAP/RecO.
DR   InterPro; IPR001164; ArfGAP_dom.
DR   InterPro; IPR038508; ArfGAP_dom_sf.
DR   InterPro; IPR011993; PH-like_dom_sf.
DR   InterPro; IPR001849; PH_domain.
DR   PANTHER; PTHR45819; CENTAURIN-GAMMA-1A; 1.
DR   PANTHER; PTHR45819:SF5; CENTAURIN-GAMMA-1A; 1.
DR   Pfam; PF13637; Ank_4; 1.
DR   Pfam; PF01412; ArfGap; 1.
DR   PRINTS; PR00405; REVINTRACTNG.
DR   SMART; SM00105; ArfGap; 1.
DR   SMART; SM00233; PH; 1.
DR   SUPFAM; SSF48403; Ankyrin repeat; 1.
DR   SUPFAM; SSF57863; ArfGap/RecO-like zinc finger; 1.
DR   SUPFAM; SSF50729; PH domain-like; 1.
DR   PROSITE; PS50297; ANK_REP_REGION; 1.
DR   PROSITE; PS50088; ANK_REPEAT; 1.
DR   PROSITE; PS50115; ARFGAP; 1.
DR   PROSITE; PS50003; PH_DOMAIN; 1.
PE   3: Inferred from homology;
KW   ANK repeat {ECO:0000256|PROSITE-ProRule:PRU00023};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833};
KW   Zinc-finger {ECO:0000256|PROSITE-ProRule:PRU00288}.
FT   DOMAIN          173..347
FT                   /note="PH"
FT                   /evidence="ECO:0000259|PROSITE:PS50003"
FT   DOMAIN          391..514
FT                   /note="Arf-GAP"
FT                   /evidence="ECO:0000259|PROSITE:PS50115"
FT   REPEAT          552..584
FT                   /note="ANK"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT   REGION          1..40
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          86..126
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          250..308
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          358..377
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          627..664
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        86..104
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        250..267
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        290..304
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        363..377
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   664 AA;  70067 MW;  922C7F167F2D0B3D CRC64;
     MAACSTARRC QTPTTAAAVA GGAGRPSPSH HHQQQQQQQH RALLGAYNLP PPGQGHASAG
     REYQHQVLLP ASLAAHQYYE PAAHSLPVQQ QASPQQLSSG KKTSDSTLWD HRPAAGDPGH
     NTSMASGQPA YYSSVAGSAA VITASASCNQ PQQQPPLGMR GSRERASYAH GVSFVSSGYL
     YKRSAGGALS RADWKKKYAA LAETGQLTYY SSLHDYMADS HGKTIDLRLT TVKVPGQTRP
     TSNGLLLKTQ LSQQQQQSAQ SSQHPQRRRA KSSGRGGGGG IGDSAKTPDD DCSVGSSSAS
     GTPAALGPPG SGFEFTIVSL DNRTWQFEAP SQAERDDWVR SIEQGILRQL QLLGRDGNPV
     KNGAGASSAS NTSPLSSASG ATAAAATASA AASVQLLRDI LGNNVCADCG RPDPDWASIN
     LGVLLCIECS GVHRNLGTHL SRVRSLNLDD WPANNVLVMR AIGNRLANSV WEACLDPASG
     VYKPNADSPR ELKEQFIRAK YERREFLPEL PYPDCPIQQQ LVDAIARSDT RQVILCLAVA
     GPAVNRAYSQ QDPRAAVHIA ATLGQLPYLQ LLLWYGADPA VRDAEGRTGH FYAAAAGKPD
     CAEFLLLAGC PPTNLMSTSM ATATNNTAST AAATNSSVSS SSRRRSSRTA SPTSPTNATM
     EIGL
//
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