ID A0A3B4H3G7_9CICH Unreviewed; 829 AA.
AC A0A3B4H3G7;
DT 05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT 05-DEC-2018, sequence version 1.
DT 27-MAR-2024, entry version 23.
DE SubName: Full=ArfGAP with GTPase domain, ankyrin repeat and PH domain 2 {ECO:0000313|Ensembl:ENSPNYP00000029735.1};
OS Pundamilia nyererei.
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Ovalentaria; Cichlomorphae; Cichliformes; Cichlidae; African cichlids;
OC Pseudocrenilabrinae; Haplochromini; Pundamilia.
OX NCBI_TaxID=303518 {ECO:0000313|Ensembl:ENSPNYP00000029735.1, ECO:0000313|Proteomes:UP000261460};
RN [1] {ECO:0000313|Ensembl:ENSPNYP00000029735.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-2023) to UniProtKB.
CC -!- SIMILARITY: Belongs to the centaurin gamma-like family.
CC {ECO:0000256|ARBA:ARBA00005430}.
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 AlphaFoldDB; A0A3B4H3G7; -.
DR STRING; 303518.ENSPNYP00000029735; -.
DR Ensembl; ENSPNYT00000030459.1; ENSPNYP00000029735.1; ENSPNYG00000022408.1.
DR GeneTree; ENSGT00940000158956; -.
DR Proteomes; UP000261460; Unplaced.
DR GO; GO:0005525; F:GTP binding; IEA:InterPro.
DR GO; GO:0005096; F:GTPase activator activity; IEA:UniProtKB-KW.
DR GO; GO:0003924; F:GTPase activity; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR CDD; cd08836; ArfGap_AGAP; 1.
DR CDD; cd04103; Centaurin_gamma; 1.
DR CDD; cd01250; PH_AGAP; 1.
DR Gene3D; 1.25.40.20; Ankyrin repeat-containing domain; 1.
DR Gene3D; 1.10.220.150; Arf GTPase activating protein; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR Gene3D; 2.30.29.30; Pleckstrin-homology domain (PH domain)/Phosphotyrosine-binding domain (PTB); 2.
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; IPR027417; P-loop_NTPase.
DR InterPro; IPR011993; PH-like_dom_sf.
DR InterPro; IPR001849; PH_domain.
DR InterPro; IPR001806; Small_GTPase.
DR PANTHER; PTHR45819:SF3; ARF-GAP WITH GTPASE, ANK REPEAT AND PH DOMAIN-CONTAINING PROTEIN 2; 1.
DR PANTHER; PTHR45819; CENTAURIN-GAMMA-1A; 1.
DR Pfam; PF12796; Ank_2; 1.
DR Pfam; PF01412; ArfGap; 1.
DR Pfam; PF00169; PH; 1.
DR Pfam; PF00071; Ras; 1.
DR PRINTS; PR00405; REVINTRACTNG.
DR SMART; SM00248; ANK; 2.
DR SMART; SM00105; ArfGap; 1.
DR SMART; SM00233; PH; 1.
DR SMART; SM00175; RAB; 1.
DR SMART; SM00173; RAS; 1.
DR SMART; SM00174; RHO; 1.
DR SUPFAM; SSF48403; Ankyrin repeat; 1.
DR SUPFAM; SSF57863; ArfGap/RecO-like zinc finger; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 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.
DR PROSITE; PS51419; RAB; 1.
DR PROSITE; PS51421; RAS; 1.
PE 3: Inferred from homology;
KW ANK repeat {ECO:0000256|ARBA:ARBA00023043, ECO:0000256|PROSITE-
KW ProRule:PRU00023}; GTPase activation {ECO:0000256|ARBA:ARBA00022468};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00288}.
FT DOMAIN 336..553
FT /note="PH"
FT /evidence="ECO:0000259|PROSITE:PS50003"
FT DOMAIN 574..698
FT /note="Arf-GAP"
FT /evidence="ECO:0000259|PROSITE:PS50115"
FT REPEAT 741..773
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REGION 242..265
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 308..332
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 397..514
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 804..829
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 311..328
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 402..416
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 427..441
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 457..487
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 804..823
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 829 AA; 89404 MW; 0D6AF5A8AAE725B5 CRC64;
VRMTSNSKTV NSAAIKAEIK RHDSLQTAIN RLAKQFERVG DQQLRSGLKV YLHSIQVNIA
NSQEWTLSRS IPELRLGVLG SLKSGKSALV NKYITGSYSA VEKPDGGRYK KEVLVDGQSH
LLLIREEAGP PDAQFSSWAD AVILVFSLEN EASFQELYQL YSQLSAFRSD IPVIVVGTQD
KISSTNPRVI EDQRARQLCI DVRHSLFYET CATYGFNVDR VFSEAAQKIV AQKKQAALQA
CKSLPNSPSH SGGSTPGSAS FPGQASNGPS IGYAYSLPST PVVSHRELRV AQGDGGGSVN
ARSLKSIPRR PSLFKNRDTD KKGGDAKGDL SSLRGVPIKQ GILWKRSGSS LNKEWKKKYV
TLSNNGTLSY HSSSSDYTQN THGKEIDLLR VTVKVPGKRP PRAVAPTGPS PAPPGAVPGV
NGLSKELPAA DSTSTATLSV VADDRSGGLS PQGGERGLQR CPSSLSTKAQ SVGTYPGSFG
GKDPSQSSPM SDRKKNRRKK SMNQKGDAAV GQAEEEENAD FIIVSFTGQT WHFEAPSMDE
RDSWVTAIES QILASLGSCE SGRNKARRSS QSEAVALQAI RNAKGNSQCV DCEAPNPTWA
SLNLGALICI ECSGIHRNLG THLSRVRSLD LDDWPGELTQ VLAAIGNHMA NSIWESCTQG
RTKPTPSATR WERESWIRAK YEQRAFVAPL VPVSGAQLPE DGVPVWLLSA VTDRDLPRLL
LLLAHSTKEQ INAPPAGLPS PPRTALHAAC QLGDVVMTQL LIWYGIDVKA KDNQGQTAMM
LATKKGSKSC IDILLQHGCP NETSPTAATP ILSRRSSTAS LGRTSSRKR
//