ID A0A135UL97_9PEZI Unreviewed; 1128 AA.
AC A0A135UL97;
DT 06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT 06-JUL-2016, sequence version 1.
DT 24-JAN-2024, entry version 31.
DE RecName: Full=ADP-ribosylation factor GTPase-activating protein {ECO:0000256|RuleBase:RU369028};
GN ORFNames=CSAL01_02332 {ECO:0000313|EMBL:KXH61135.1};
OS Colletotrichum salicis.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Glomerellales; Glomerellaceae; Colletotrichum;
OC Colletotrichum acutatum species complex.
OX NCBI_TaxID=1209931 {ECO:0000313|EMBL:KXH61135.1, ECO:0000313|Proteomes:UP000070121};
RN [1] {ECO:0000313|EMBL:KXH61135.1, ECO:0000313|Proteomes:UP000070121}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 607.94 {ECO:0000313|EMBL:KXH61135.1,
RC ECO:0000313|Proteomes:UP000070121};
RA Baroncelli R., Thon M.R.;
RT "The genome sequence of Colletotrichum salicis CBS 607.94.";
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:KXH61135.1}.
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DR EMBL; JFFI01001317; KXH61135.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A135UL97; -.
DR STRING; 1209931.A0A135UL97; -.
DR OrthoDB; 1449795at2759; -.
DR Proteomes; UP000070121; 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:UP000070121};
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 665..772
FT /note="PH"
FT /evidence="ECO:0000259|PROSITE:PS50003"
FT DOMAIN 848..972
FT /note="Arf-GAP"
FT /evidence="ECO:0000259|PROSITE:PS50115"
FT REGION 538..643
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 802..825
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1080..1128
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 538..562
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 578..641
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 803..825
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1083..1098
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1128 AA; 125016 MW; AC9F3FDA53DC9E07 CRC64;
MGIVSSKPDD GATLYLRDQN RRATSRPLLP LPYPLLALSL CLALSISSLV ISNPRRRSSV
NIVPNSFPAT RVSASRPLGD GSPIEFVQDT EVVTSPGGVP NFILKLNQDD ELVFTFTFVI
RQGQQFVTNG GADTVATTDT QISGLTYVYA STPREVENLV TREFHADPNL HKNSNVELVG
DFATGGTPSV SFEWTWKWKP PKSIEDRGGG WRNSCSFVEY DPRAHCLHTL ASFSYWVSNP
VYPLSHPNSP SPPFLLTAPP KIRVASSQSV DSRISHAELD EPLSPLPGNT SSTTILPVPQ
SASEPIKVDV ACPKPTDDVL VPDDGPVFRA TIKSLEQKTG NMRTQMKRVL KMAKQAHEAQ
QEANKNFSEF IDTLREASST NANAVQPAIE HYFDKIAREI LAYERTNTVN LKRIVIDPLD
KFYTVDIKQA ESKKRDFEEE SKDYYAYVSR YLGQRHDSVK AKKLAESDSK YQTKRRNFEL
KRFDYSSFMQ DLHGGRKEQE VLSHLTRYAD AQTKSFLEAA KKIDTLLPQL EALSSEVQEA
DKEYQYQRRE REEKRRLLEK SNQPYNEPDP VPVPGTSSGP VAGSNGNAYV SDSDLGRADS
TGSQLKVAMS SGSNPSLSMA SPELSRSPGS LGNSSVGSPA QASKFKGIRD LEEKDYGQSS
GASSTQRKEG LLWSLSKGGS NHVDPRNLNK QGWHKFWIVL DQGKLSEYSN WKQRLDLHND
PIDLRMASVR EARNAERRFC FEVITPQFKR VYQATSEEDM NSWITSINNA LQSAVEGRIM
RDKSAPSDSG YIKRDIGSIL TGKSPSVGHN SHHHSHANSN NAPVRRITVG ARPSTHRSTS
SSFDENPDKL LQLLRDNDQG NCWCADCGSG TKVEWVSINL AIILCIECSG IHRSLGTHIS
KVRSLTLDIN SFTSDIVELL LLVGNRVSNM IWESKLEPGF KPTPQATREM RLRFITAKYV
DRAYVEPISA TLSRYPNPDD TLLAAIKKNE IQQVIYALAL RASPNVTDRS RGTHAVFLAL
AAADPASPSP TPGQPPETDR TVPFPVAEML LQNGAEVPLT MPAFPLSRSA QMYIEEKRGR
STGFSNDSVG SLPGNLSPNE KLQRERDARL QKRVSAGGRL AKSPIPER
//
