ID A0A010R817_9PEZI Unreviewed; 1105 AA.
AC A0A010R817;
DT 11-JUN-2014, integrated into UniProtKB/TrEMBL.
DT 11-JUN-2014, sequence version 1.
DT 24-JAN-2024, entry version 47.
DE RecName: Full=ADP-ribosylation factor GTPase-activating protein {ECO:0000256|RuleBase:RU369028};
GN ORFNames=CFIO01_10247 {ECO:0000313|EMBL:EXF76341.1};
OS Colletotrichum fioriniae PJ7.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Glomerellales; Glomerellaceae; Colletotrichum;
OC Colletotrichum acutatum species complex.
OX NCBI_TaxID=1445577 {ECO:0000313|EMBL:EXF76341.1, ECO:0000313|Proteomes:UP000020467};
RN [1] {ECO:0000313|EMBL:EXF76341.1, ECO:0000313|Proteomes:UP000020467}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PJ7 {ECO:0000313|EMBL:EXF76341.1,
RC ECO:0000313|Proteomes:UP000020467};
RA Baroncelli R., Thon M.R.;
RT "The genome sequence of Colletotrichum fioriniae PJ7.";
RL Submitted (FEB-2014) to the EMBL/GenBank/DDBJ databases.
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:EXF76341.1}.
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DR EMBL; JARH01000854; EXF76341.1; -; Genomic_DNA.
DR RefSeq; XP_007600032.1; XM_007599970.1.
DR AlphaFoldDB; A0A010R817; -.
DR STRING; 1445577.A0A010R817; -.
DR KEGG; cfj:CFIO01_10247; -.
DR eggNOG; KOG0521; Eukaryota.
DR HOGENOM; CLU_002728_0_0_1; -.
DR OrthoDB; 1449795at2759; -.
DR Proteomes; UP000020467; 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 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:UP000020467};
KW Repeat {ECO:0000256|RuleBase:RU369028};
KW Transport {ECO:0000256|ARBA:ARBA00022448};
KW Zinc {ECO:0000256|RuleBase:RU369028};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00288}.
FT DOMAIN 643..750
FT /note="PH"
FT /evidence="ECO:0000259|PROSITE:PS50003"
FT DOMAIN 825..949
FT /note="Arf-GAP"
FT /evidence="ECO:0000259|PROSITE:PS50115"
FT REGION 519..621
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 781..803
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1058..1105
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 519..540
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 555..619
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 781..802
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1060..1075
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1105 AA; 122419 MW; D25FFFD1708D128D CRC64;
MGIVSSKPDD GATLYLRDQN RLSISSLVIS NPRRRSAVNI VPNAFPATRV SASRPLGDGS
PIEFVQDTEV VTSPGGVPNF ILKLNQDDEL VFTFTFVIRQ GQQFVTNGGA DAVATTDTQI
SGLTYVYAST PREVENLVTR EFHADPNLHK NSNVELVGDF ATGGTPSVSF EWTWKWKPPK
SIEDRGGGWR NSCSFVEYDP RAHCLHTLAS FSYWVSNPVL PLSHPNSPSP PFLLTAPPKI
RVASSQSVDS RISHAELDEP LSPLPGNTSS TTILPVPQSA SEPIKVDVAC PKPTDDVLVP
DDGPVFRATI KSLEQKTGNM RTQMKRVLKM AKQAHEAQQE ANKNFSEFID TLREASSTNA
NAVQPAIEHY FDKIAREILA YERTNTVNLK RIVIDPLDKF YTVDIKQAES KKRDFEEESK
DYYAYVSRYL GQRHDSVKAK KLAESDSKYQ TKRRNFELKR FDYSSFMQDL HGGRKEQEVL
SHLTRYADAQ TKSFLEAAKK IDTLLPQLEA LSSEVQEADK EYQYQRRERE EKRRLLEKSN
QPYNEPDPIP VPGTSSGPVA SSNGNAYVSD SDLGRADSTG SQLKVAMSSG SNPSLSMASP
ELSRSPGSLG NSSVGSPAQA SKFKGIRDLE EKDYGQSSGA SSTQRKEGLL WSLSKGGSNH
VDPRNLNKQG WHKFWIVLDQ GKLSEYSNWK QRLDLHNDPI DLRMASVREA RNAERRFCFE
VITPQFKRVY QATSEEDMNS WITSINNALQ SAVEGRIMRD KSAPSDSGYI KRDIGSILTG
KSPSVGHNSH HSHANSNSAP VRRITVGARP STHRSTSSSF DENPDKLLQL LRDNDQGNCW
CADCGSGTKV EWVSINLAII LCIECSGIHR SLGTHISKVR SLTLDINSFT SDIVELLLLV
GNRVSNMIWE AKLEPGYKPT PQATREMRLR FITAKYVDRA YVEPISATLS RYPNPDDTLL
AAIKKNEIQQ VIYALALRAS PNVTDRSRGT HAVFLALAAA DPASPSPTPG QPPETDRTVP
FPVAEMLLQN GAEVPLTMPA FPLSRSAQLY IEEKRGRSTG FTNDSVGSLP GNLSPNEKLQ
RERDARLQKR VSAGGRLAKS PIPER
//
