ID V9EFT0_PHYPR Unreviewed; 871 AA.
AC V9EFT0;
DT 19-FEB-2014, integrated into UniProtKB/TrEMBL.
DT 19-FEB-2014, sequence version 1.
DT 24-JAN-2024, entry version 48.
DE RecName: Full=Arf-GAP with coiled-coil, ANK repeat and PH domain-containing protein {ECO:0008006|Google:ProtNLM};
GN ORFNames=F443_17012 {ECO:0000313|EMBL:ETI36907.1};
OS Phytophthora parasitica P1569.
OC Eukaryota; Sar; Stramenopiles; Oomycota; Peronosporales; Peronosporaceae;
OC Phytophthora.
OX NCBI_TaxID=1317065 {ECO:0000313|EMBL:ETI36907.1, ECO:0000313|Proteomes:UP000018721};
RN [1] {ECO:0000313|EMBL:ETI36907.1, ECO:0000313|Proteomes:UP000018721}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=P1569 {ECO:0000313|EMBL:ETI36907.1,
RC ECO:0000313|Proteomes:UP000018721};
RG The Broad Institute Genomics Platform;
RA Russ C., Tyler B., Panabieres F., Shan W., Tripathy S., Grunwald N.,
RA Machado M., Johnson C.S., Arredondo F., Hong C., Coffey M., Young S.K.,
RA Zeng Q., Gargeya S., Fitzgerald M., Abouelleil A., Alvarado L.,
RA Chapman S.B., Gainer-Dewar J., Goldberg J., Griggs A., Gujja S., Hansen M.,
RA Howarth C., Imamovic A., Ireland A., Larimer J., McCowan C., Murphy C.,
RA Pearson M., Poon T.W., Priest M., Roberts A., Saif S., Shea T., Sykes S.,
RA Wortman J., Nusbaum C., Birren B.;
RT "The Genome Sequence of Phytophthora parasitica P1569.";
RL Submitted (NOV-2013) to the EMBL/GenBank/DDBJ databases.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:ETI36907.1}.
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DR EMBL; ANIZ01002987; ETI36907.1; -; Genomic_DNA.
DR AlphaFoldDB; V9EFT0; -.
DR EnsemblProtists; ETI36907; ETI36907; F443_17012.
DR eggNOG; KOG0521; Eukaryota.
DR HOGENOM; CLU_006640_0_0_1; -.
DR OrthoDB; 1449795at2759; -.
DR Proteomes; UP000018721; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:InterPro.
DR GO; GO:0005096; F:GTPase activator activity; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR CDD; cd08204; ArfGap; 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; 2.
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; 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; PF13637; Ank_4; 1.
DR Pfam; PF01412; ArfGap; 1.
DR Pfam; PF16746; BAR_3; 1.
DR Pfam; PF00169; PH; 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; SSF103657; BAR/IMD domain-like; 1.
DR SUPFAM; SSF50729; PH domain-like; 1.
DR PROSITE; PS50088; ANK_REPEAT; 1.
DR PROSITE; PS50115; ARFGAP; 1.
DR PROSITE; PS50003; PH_DOMAIN; 1.
PE 4: Predicted;
KW ANK repeat {ECO:0000256|PROSITE-ProRule:PRU00023};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000018721};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00288}.
FT DOMAIN 520..624
FT /note="PH"
FT /evidence="ECO:0000259|PROSITE:PS50003"
FT DOMAIN 641..761
FT /note="Arf-GAP"
FT /evidence="ECO:0000259|PROSITE:PS50115"
FT REPEAT 807..839
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REGION 63..112
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 285..311
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 334..360
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 63..83
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 289..305
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 334..358
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 871 AA; 95759 MW; 67C7EEA53B31ADE3 CRC64;
MKAFSAWRGG DGGAKASNDA VSELQQVILK KDLMILSLQT QLDAYKARYG ALPAEDLDKL
LQSDAINEPQ EKRSRDLSAD RKELPPDINS TVSVTDGSDS KPIEDKKQPT PRVVVTSPRF
RASSDADEAR AKIQSRSSKN VVLDFVEDSP MFRRQLEGFE ESITGLRALL KELVAHSKEY
AAAGKHFGQE ETALADELIL RKHARAIFST SCPELGSLSE LFGEMHDTLA QVQSSRVSML
LGVESLLSRS IQQFSEKELL KEAGELRKDV TRLGEEYETL LGKLLSKSRQ PGQPANGTGT
PTGVGDSIGT LGLGSPALPM GSYNGEFTIT GTPPASAASS GSNNNILGSD SGSTNGSDKH
QRALERDVVV AHRRFELARF DLVRYMNRID CMKKFVLVEC FNSILYAQLG HFHACHELVK
SVEPSLRKRQ EMMQVSRKDF EQDELMWASQ RELLDKRLSQ DVEAVSSSYP SSESSPVAAG
SLSVDTTIAS ESFPSLDLPV EVISIDTLSS RQTVASTPGG VAKQGYLFVR NSMFPARSWK
RRWFQIHAGK LFQTTSRGGT GKHPTESSLT LVCDLLLARV RELEGSSLPF CFEVIDANRA
KLLLQAASAR DMMEWIEASR RSTESALEKQ SHRQEVHPEQ QSVIDELTEA NPCCADCGQE
PAEWVSINIG CLLCIECSGI HRSLGVHESK VRSLALDSWD MSLLTLLRDK LGNDTVNVVW
EHTIPDGWTK PTPTTSRDEK ARFIKAKYHF HGFAEPDPTL SALEDDDSIL KQELAKRFIA
GASRGDLNEL MWCLAHGVDV NVRAGEQNET ALHVSAAAGA ATCCDYLVVN GASLTLIDKR
GRLPYDAAKA GGFEDIKLTL MQKMSLEQYQ S
//