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Database: UniProt
Entry: G0MKX8_CAEBE
LinkDB: G0MKX8_CAEBE
Original site: G0MKX8_CAEBE 
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
//
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