ID A0A1J9S1L3_9PEZI Unreviewed; 481 AA.
AC A0A1J9S1L3;
DT 15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT 15-FEB-2017, sequence version 1.
DT 27-MAR-2024, entry version 24.
DE SubName: Full=Arf gtpase-activating protein {ECO:0000313|EMBL:OJD38835.1};
GN ORFNames=BKCO1_3000266 {ECO:0000313|EMBL:OJD38835.1};
OS Diplodia corticola.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Dothideomycetes incertae sedis; Botryosphaeriales; Botryosphaeriaceae;
OC Diplodia.
OX NCBI_TaxID=236234 {ECO:0000313|EMBL:OJD38835.1, ECO:0000313|Proteomes:UP000183809};
RN [1] {ECO:0000313|EMBL:OJD38835.1, ECO:0000313|Proteomes:UP000183809}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 112549 {ECO:0000313|EMBL:OJD38835.1,
RC ECO:0000313|Proteomes:UP000183809};
RA Fernandes I., De Jonge R., Van De Peer Y., Devreese B., Alves A.,
RA Esteves A.C.;
RT "Proteomics and genomics reveal pathogen-plant mechanisms compatible with a
RT hemibiotrophic lifestyle of Diplodia corticola.";
RL Submitted (OCT-2016) 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:OJD38835.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; MNUE01000003; OJD38835.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1J9S1L3; -.
DR STRING; 236234.A0A1J9S1L3; -.
DR OrthoDB; 389572at2759; -.
DR Proteomes; UP000183809; Unassembled WGS sequence.
DR GO; GO:0005096; F:GTPase activator activity; IEA:UniProtKB-KW.
DR CDD; cd08831; ArfGap_ArfGap2_3_like; 1.
DR Gene3D; 1.10.220.150; Arf GTPase activating protein; 1.
DR InterPro; IPR037278; ARFGAP/RecO.
DR InterPro; IPR001164; ArfGAP_dom.
DR InterPro; IPR038508; ArfGAP_dom_sf.
DR PANTHER; PTHR45686:SF4; ADP-RIBOSYLATION FACTOR GTPASE ACTIVATING PROTEIN 3, ISOFORM H; 1.
DR PANTHER; PTHR45686; ADP-RIBOSYLATION FACTOR GTPASE ACTIVATING PROTEIN 3, ISOFORM H-RELATED; 1.
DR Pfam; PF01412; ArfGap; 1.
DR PRINTS; PR00405; REVINTRACTNG.
DR SMART; SM00105; ArfGap; 1.
DR SUPFAM; SSF57863; ArfGap/RecO-like zinc finger; 1.
DR PROSITE; PS50115; ARFGAP; 1.
PE 4: Predicted;
KW GTPase activation {ECO:0000256|ARBA:ARBA00022468};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00288}; Reference proteome {ECO:0000313|Proteomes:UP000183809};
KW Zinc {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-ProRule:PRU00288};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00288}.
FT DOMAIN 9..130
FT /note="Arf-GAP"
FT /evidence="ECO:0000259|PROSITE:PS50115"
FT REGION 131..237
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 291..329
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 342..378
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 417..437
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 140..154
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 164..209
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 305..323
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 481 AA; 51209 MW; B34A6460BDD9C076 CRC64;
MAATKQESQK IFEKLKTKPA NKICFDCGAK NPTWSSVPFG IYLCLDCSAN HRNMGVHISF
VRSTNLDIWQ WDQLRLMKVG GNESATKYFQ TNGGTAALNS KDPKAKYSSN AATKYKEELA
RRVTLDKKQF PEEVTITDVP DVETSGSNTP AGDEDDFFSS WDKPTIKRPS NPPSRTGTPA
SGSRTASPFL NASSNGNGTA RSKSPLSAGA DSTPAAPRAV PASAIRSKTT TTAKPKANIL
GAKKKGLGAK KVVASGGDGL DFEEMERKAK EEAERIEKLG YDAEAERAAA EEAAKAKEAE
SRANIVSPTP VSPRGGFGST SKERNSGDVE RLGMGVARLG FGQVGSSKPA AAPKKMGGFG
STSRAVDDDS ERFARQKFGT QKGISSDEFF GRGSFDPSAQ NEAKTRLQGF EGATSISSNA
YFGRPEEDGP AGDDYGDLEN AAKDFVRKFG ITAGDDLDNL SNLLGEGATR LQGAIRNYLN
S
//
