ID G0MKX8_CAEBE Unreviewed; 1074 AA.
AC G0MKX8;
DT 19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT 19-OCT-2011, sequence version 1.
DT 24-JAN-2024, entry version 65.
DE RecName: Full=Arf-GAP domain-containing protein {ECO:0000259|PROSITE:PS50115};
GN ORFNames=CAEBREN_28075 {ECO:0000313|EMBL:EGT34827.1};
OS Caenorhabditis brenneri (Nematode worm).
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=135651 {ECO:0000313|Proteomes:UP000008068};
RN [1] {ECO:0000313|Proteomes:UP000008068}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PB2801 {ECO:0000313|Proteomes:UP000008068};
RG Caenorhabditis brenneri Sequencing and Analysis Consortium;
RA Wilson R.K.;
RL Submitted (JUL-2011) to the EMBL/GenBank/DDBJ databases.
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DR EMBL; GL379799; EGT34827.1; -; Genomic_DNA.
DR AlphaFoldDB; G0MKX8; -.
DR STRING; 135651.G0MKX8; -.
DR EnsemblMetazoa; CBN28075.1; CBN28075.1; WBGene00190040.
DR eggNOG; KOG0705; Eukaryota.
DR HOGENOM; CLU_007326_1_0_1; -.
DR InParanoid; G0MKX8; -.
DR Proteomes; UP000008068; Unassembled WGS sequence.
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 GO; GO:0090630; P:activation of GTPase activity; IEA:EnsemblMetazoa.
DR GO; GO:0055059; P:asymmetric neuroblast division; IEA:EnsemblMetazoa.
DR GO; GO:0060582; P:cell fate determination involved in pattern specification; IEA:EnsemblMetazoa.
DR GO; GO:0048259; P:regulation of receptor-mediated endocytosis; IEA:EnsemblMetazoa.
DR CDD; cd08836; ArfGap_AGAP; 1.
DR CDD; cd04103; Centaurin_gamma; 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); 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; IPR027417; P-loop_NTPase.
DR InterPro; IPR011993; PH-like_dom_sf.
DR InterPro; IPR001806; Small_GTPase.
DR PANTHER; PTHR45819; CENTAURIN-GAMMA-1A; 1.
DR PANTHER; PTHR45819:SF5; CENTAURIN-GAMMA-1A; 1.
DR Pfam; PF12796; Ank_2; 1.
DR Pfam; PF01412; ArfGap; 1.
DR Pfam; PF00071; Ras; 1.
DR PRINTS; PR00405; REVINTRACTNG.
DR SMART; SM00248; ANK; 2.
DR SMART; SM00105; ArfGap; 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; PS51419; RAB; 1.
DR PROSITE; PS51421; RAS; 1.
PE 4: Predicted;
KW ANK repeat {ECO:0000256|PROSITE-ProRule:PRU00023};
KW GTPase activation {ECO:0000256|ARBA:ARBA00022468};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000008068};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00288}.
FT DOMAIN 791..911
FT /note="Arf-GAP"
FT /evidence="ECO:0000259|PROSITE:PS50115"
FT REPEAT 948..980
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REGION 98..183
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 435..454
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 463..501
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 561..599
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 646..730
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1014..1048
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1055..1074
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 98..113
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 126..143
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 162..183
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 463..481
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 648..670
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 716..730
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1074 AA; 119140 MW; 0E6F39C25E134B41 CRC64;
MPLIRNYDYY DIISAAPSTS RPPVVVPTHN NFGSSRQSSY SATPSKGRIY YGKNEYRGNA
NMTINDPTDF EETADLNAND SVVGEDKRKK KRWRDLLFPK NRHSSRKDRE NSNVNVTTRS
LSSVSFRSEK PDRSRRRESG SLSRHRYIPP PPLPMPPRRI MTSTSMGYSD DAMTSSSSHT
TTDYDDVVPV PSYVIYPASS IAHARRNHSR DAILPAILPA VYVGSSRKIM MGNGSNKIFR
SPSYHHDAFV NSHEWTLSRS ISEMRVGIVG TSQSGKTSLV HRYLTGTYTP EESPEGGRFK
KEVVIEGQSH LLLIRDEGQQ HLDVQFCQWV DAVVFVFNVC SIQSYDSIQA LAHEMSKYRN
ISDLPLILVG TKDHISEKRA RVITEDEGRQ LAAQMKRCSY FETSSTYGTN VERVFKEACC
KVIQSRVRIQ VGSAATSQVR TPTPTHSECG RKDYQDPRFI SSNSFAMPSN MRPSYPTNSA
RRNTVHHREQ PPSSRTASER SMSAMLGAPY GNRMTAGVSP SASQKSVHSI ANGCYSRSSA
ALLDSDQPSL NSYLIDSMSS GGTPVNHQSG ANQVSASTSH LPTPSSTPNT QRKNSVFPNI
FKQRSSERIK MIESLILNRS YMDKTAQGKE MDLKLATIRI TGRLHPLHSH RVTNTTGSST
DGSGTPTLKS YEPRRSDVGV GANSGDGTSG GGSDDAIKEN HRQQFSPPAM PQTVAGKKKR
ESRKVGANSK HNDEEDECFE VINNCLMRWE FCAGSLEERD EWIQAIGGEI EKSLGKEVAN
AKTNNRAVAD RPDIAALRSI PGNGRCADCE NPAAEWASIN LGIVICIECS GIHRNLGSHI
SKVRGLELDQ WPVEHLAVMQ AIGNDKANEM WEYGLTNERK PLPESSREEK ERFIDRKYVQ
KAFLKPIPTG EPVTSQLISA VLARDVMSLN VLLANGMSVD EINTTTKDGR TVLHLAASIG
SVELAQLLIW HNADARILDN NGRSCLFYAR SNGFREVFDM LVTAGLSPDY GLPQENNDYS
QMPEFSAMGS TSNREYSMSG DESYSSRRIS MAPPQVPVRR YLPQQPELDE TSVI
//