ID A0A420HV19_9PEZI Unreviewed; 1131 AA.
AC A0A420HV19;
DT 08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT 08-MAY-2019, sequence version 1.
DT 03-MAY-2023, entry version 14.
DE RecName: Full=ADP-ribosylation factor GTPase-activating protein {ECO:0000256|RuleBase:RU369028};
GN ORFNames=GcM3_158012 {ECO:0000313|EMBL:RKF61252.1};
OS Golovinomyces cichoracearum.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC Erysiphales; Erysiphaceae; Golovinomyces.
OX NCBI_TaxID=62708 {ECO:0000313|EMBL:RKF61252.1, ECO:0000313|Proteomes:UP000283383};
RN [1] {ECO:0000313|EMBL:RKF61252.1, ECO:0000313|Proteomes:UP000283383}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=UMSG3 {ECO:0000313|EMBL:RKF61252.1};
RX PubMed=30253736; DOI=10.1186/s12864-018-5069-z;
RA Wu Y., Ma X., Pan Z., Kale S.D., Song Y., King H., Zhang Q., Presley C.,
RA Deng X., Wei C.I., Xiao S.;
RT "Comparative genome analyses reveal sequence features reflecting distinct
RT modes of host-adaptation between dicot and monocot powdery mildew.";
RL BMC Genomics 19:705-705(2018).
CC -!- FUNCTION: GTPase-activating protein for the ADP ribosylation factor
CC family. {ECO:0000256|RuleBase:RU369028}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|RuleBase:RU369028}.
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:RKF61252.1}.
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DR EMBL; MCBQ01015828; RKF61252.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A420HV19; -.
DR STRING; 62708.A0A420HV19; -.
DR Proteomes; UP000283383; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
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; cd07608; BAR_ArfGAP_fungi; 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; IPR027267; AH/BAR_dom_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; 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; SSF57863; ArfGap/RecO-like zinc finger; 1.
DR SUPFAM; SSF103657; BAR/IMD domain-like; 1.
DR SUPFAM; SSF50729; PH domain-like; 1.
DR PROSITE; PS50115; ARFGAP; 1.
DR PROSITE; PS50003; PH_DOMAIN; 1.
PE 4: Predicted;
KW ANK repeat {ECO:0000256|RuleBase:RU369028};
KW Cytoplasm {ECO:0000256|RuleBase:RU369028};
KW GTPase activation {ECO:0000256|RuleBase:RU369028};
KW Metal-binding {ECO:0000256|RuleBase:RU369028};
KW Reference proteome {ECO:0000313|Proteomes:UP000283383};
KW Repeat {ECO:0000256|RuleBase:RU369028};
KW Zinc {ECO:0000256|RuleBase:RU369028};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00288}.
FT DOMAIN 661..767
FT /note="PH"
FT /evidence="ECO:0000259|PROSITE:PS50003"
FT DOMAIN 850..974
FT /note="Arf-GAP"
FT /evidence="ECO:0000259|PROSITE:PS50115"
FT REGION 251..288
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 529..597
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 610..638
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 263..277
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 529..551
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 552..597
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1131 AA; 126573 MW; 91E8D91E003594D9 CRC64;
MGNVSSRHDE ASALYLRDQN RLTISSLLIT NARRQTILHV VPNTFPATKF SGSREALDAR
LVEYVQDPES PPNFPTFILK LNNDDELTFK FSFIIRQTTV PESTTQLDTN INGLTYVSAS
TAKEVETLVT REFHADPNFH KNSNVQLVGD FSTGNSQSVS FDWSWKWRPP KSTEDRGGGW
RNACSFVEYD QRAHRFDTLA SFSFWVSSKK STNSSFGSIL TCATDQSSNP GHSNPTYGPF
NIVPSMNFRV PSSQTTGSHR LSGTDMRDLD DPPSPKMVTT EDHPAPEPSL QKDLIKIDVS
RQRLGKDMSE TEDGPLFRAT MKSLEQKTGN MRQRMKKVLK KAEAAHLAQI ECNEAKSAFM
EALREASLSN ANAVQPALEH YFDKIAREIL AYERQSSTNL QKIIIDPIMK VYNIDIKQAE
SKKRDFEEES KDYYAYVSRY LGQRQDSLKE KKRADSDSKY QIKRRNFELK RFDYSTFMQD
LHGGRKEQEV LSHLTKYADA QTRGYLATAK KIEELLPHLD ALSAKVQETD KEFQYQRTER
EEKRRNLEKS NPTYTEPDII IPSSTPVSSL LATSPISTAP PESELSRSDS TASQFRSTHQ
VGLVSLNTPN TGASQEFPRS PGCQYSHLSS SSSNAGNQTK FKGIRDLEEK DRSHVGEKSS
TQRKEGLLWA LSRPGSHSDP RGLNKQAWHK FWIVVDAGKV SEYNNWKQRL DLHREPIDLR
VASVREARNA ERRFCFEVIT PHYKRVYQAT SEEDMNNWIS AINNAIQSAV EGRDFRDMPS
TAPRQEPHSI RRDIGSILTG KSSSINHGSH HHCTNGGGQG VNSSVFRRTT IGARPAYSRK
GSNGFDESPD KLLQLLRDAD QSNCLCADCS SGIKTEWVSI NLGIILCIEC SGIHRSLGTH
ISKIRSLTLD LQSFTTDIVE LLLLAGNRIS NSVWEARLEP GDKPSPQATR ETRLKFITAK
YVDRIYVLPI SSKLSRYSTA DETLLTAIKR NEIQNVIYAL ALGASPNICD KSRGTHSVYL
ALAAADPAST SPASMISGSN SEKNVAFPIA EILIQNGAEI PSALPAFPLS RSACLYIEQK
SWRSSLSVDT VGSLPNSNMS LGEKQIKERE TRLQKRVSAG GRLAKAPIPE I
//
