ID R0GSX2_9BRAS Unreviewed; 824 AA.
AC R0GSX2;
DT 26-JUN-2013, integrated into UniProtKB/TrEMBL.
DT 26-JUN-2013, sequence version 1.
DT 24-JAN-2024, entry version 55.
DE RecName: Full=ADP-ribosylation factor GTPase-activating protein AGD3 {ECO:0008006|Google:ProtNLM};
GN ORFNames=CARUB_v10000234mg {ECO:0000313|EMBL:EOA19969.1};
OS Capsella rubella.
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Camelineae; Capsella.
OX NCBI_TaxID=81985 {ECO:0000313|EMBL:EOA19969.1, ECO:0000313|Proteomes:UP000029121};
RN [1] {ECO:0000313|Proteomes:UP000029121}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Monte Gargano {ECO:0000313|Proteomes:UP000029121};
RX PubMed=23749190; DOI=10.1038/ng.2669;
RA Slotte T., Hazzouri K.M., Agren J.A., Koenig D., Maumus F., Guo Y.L.,
RA Steige K., Platts A.E., Escobar J.S., Newman L.K., Wang W., Mandakova T.,
RA Vello E., Smith L.M., Henz S.R., Steffen J., Takuno S., Brandvain Y.,
RA Coop G., Andolfatto P., Hu T.T., Blanchette M., Clark R.M., Quesneville H.,
RA Nordborg M., Gaut B.S., Lysak M.A., Jenkins J., Grimwood J., Chapman J.,
RA Prochnik S., Shu S., Rokhsar D., Schmutz J., Weigel D., Wright S.I.;
RT "The Capsella rubella genome and the genomic consequences of rapid mating
RT system evolution.";
RL Nat. Genet. 45:831-835(2013).
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DR EMBL; KB870810; EOA19969.1; -; Genomic_DNA.
DR RefSeq; XP_006287071.1; XM_006287009.1.
DR AlphaFoldDB; R0GSX2; -.
DR STRING; 81985.R0GSX2; -.
DR eggNOG; KOG0521; Eukaryota.
DR Proteomes; UP000029121; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:InterPro.
DR GO; GO:0005096; F:GTPase activator activity; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR CDD; cd08204; ArfGap; 1.
DR CDD; cd07606; BAR_SFC_plant; 1.
DR CDD; cd13250; PH_ACAP; 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; 1.20.1270.60; Arfaptin homology (AH) domain/BAR domain; 1.
DR Gene3D; 2.30.29.30; Pleckstrin-homology domain (PH domain)/Phosphotyrosine-binding domain (PTB); 1.
DR InterPro; IPR045258; ACAP1/2/3-like.
DR InterPro; IPR035670; AGD1/2/3/4_BAR_plant.
DR InterPro; IPR027267; AH/BAR_dom_sf.
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; IPR004148; BAR_dom.
DR InterPro; IPR011993; PH-like_dom_sf.
DR InterPro; IPR001849; PH_domain.
DR PANTHER; PTHR23180:SF160; ADP-RIBOSYLATION FACTOR GTPASE-ACTIVATING PROTEIN EFFECTOR PROTEIN 1; 1.
DR PANTHER; PTHR23180; CENTAURIN/ARF; 1.
DR Pfam; PF12796; Ank_2; 1.
DR Pfam; PF01412; ArfGap; 1.
DR Pfam; PF16746; BAR_3; 1.
DR Pfam; PF00169; PH; 1.
DR PRINTS; PR00405; REVINTRACTNG.
DR SMART; SM00248; ANK; 3.
DR SMART; SM00105; ArfGap; 1.
DR SMART; SM00721; BAR; 1.
DR SMART; SM00233; PH; 1.
DR SUPFAM; SSF48403; Ankyrin repeat; 1.
DR SUPFAM; SSF57863; ArfGap/RecO-like zinc finger; 1.
DR SUPFAM; SSF103657; BAR/IMD domain-like; 1.
DR SUPFAM; SSF50729; PH domain-like; 1.
DR PROSITE; PS50297; ANK_REP_REGION; 2.
DR PROSITE; PS50088; ANK_REPEAT; 2.
DR PROSITE; PS50115; ARFGAP; 1.
DR PROSITE; PS50003; PH_DOMAIN; 1.
PE 4: Predicted;
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 Reference proteome {ECO:0000313|Proteomes:UP000029121};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00288}.
FT DOMAIN 287..425
FT /note="PH"
FT /evidence="ECO:0000259|PROSITE:PS50003"
FT DOMAIN 496..638
FT /note="Arf-GAP"
FT /evidence="ECO:0000259|PROSITE:PS50115"
FT REPEAT 725..757
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REPEAT 758..790
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REGION 244..263
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 434..462
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 248..263
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 446..460
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 824 AA; 92162 MW; B739314E007CBC58 CRC64;
MHFTKLDDSP MFRKQLQSME ESAEVLRERS LKFYKGCRKY TAYDGDIAFA SALETFGGGH
NDPISVAFGG PVMTKFTIAL REIGTYKEVL RSQVEHILND RLLQFSNMDL HEVKEARKRF
DKASLTYDQA REKFLSLRKG TRSDVAAALE QELHTSRSMF EQARFNLVTA LSNVEAKKRF
EFLEAVSGTM DAHLRYFKQG YELLHQMEPY INQVLTYAQQ SRERSNYEQA ALNEKMQEYK
RQVDRESRIG SNGSNGSPNG DGIQAIGRSS HKMIDAVMQS AARGKVQTIR QGYLSKRSSN
LRGDWKRRFF VLDSRGMLYY YRKQCSKPSG SGSQLSGQRN SSELGSGLLS RWLSSNSHGH
GGVHDEKSVA RHTVNLLTST IKVDADQSDL RFCFRIISPT KNYTLQAESA LDQMDWIEKI
TGVIASLLSS QVPEQRLPGS PMGSGHHRSA SESSSYESSE YDHPTNEEFV CERSFLGYHE
RQSRNFQPQR SIRKGEKPID ALRKVCGNDK CADCGAPEPD WASLNLGVLV CIECSGVHRN
LGVHISKVRS LTLDVKVWEP SVISLFQALG NTYANTVWEE LLHSRSAFHV DPGLTGSDKS
RVMVTGKPSY GDMISIKEKY IQAKYAEKLF VRRSRDCDFP QSIAQQMWDA VCGNDKKAVY
RLIVNGDADV NFVYDQSSSS SSLTLSRVIL VPERPKREDV LLRLRNELLD RTSGSSSNIS
PEGSGCSSLL HCACEKADIG MAELLLQYGA NVNASDSSGQ TPLHCCIFRG KAAIARLLLS
RGANPEAMSV EGKTPLDIAA ESKFTDPEVL ALLSDTNGYN HRQC
//
