ID A0A2G5HJX2_CERBT Unreviewed; 488 AA.
AC A0A2G5HJX2;
DT 31-JAN-2018, integrated into UniProtKB/TrEMBL.
DT 31-JAN-2018, sequence version 1.
DT 24-JAN-2024, entry version 16.
DE SubName: Full=ADP-ribosylation factor GTPase-activating protein glo3 {ECO:0000313|EMBL:PIA92867.1};
GN ORFNames=CB0940_04729 {ECO:0000313|EMBL:PIA92867.1};
OS Cercospora beticola (Sugarbeet leaf spot fungus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Dothideomycetidae; Mycosphaerellales; Mycosphaerellaceae; Cercospora.
OX NCBI_TaxID=122368 {ECO:0000313|EMBL:PIA92867.1, ECO:0000313|Proteomes:UP000230605};
RN [1] {ECO:0000313|EMBL:PIA92867.1, ECO:0000313|Proteomes:UP000230605}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=09-40 {ECO:0000313|EMBL:PIA92867.1,
RC ECO:0000313|Proteomes:UP000230605};
RA De Jonge R., Ebert M.K., Suttle J.C., Jurick Ii W.M., Secor G.A.,
RA Thomma B.P., Van De Peer Y., Bolton M.D.;
RT "The cercosporin biosynthetic gene cluster was horizontally transferred to
RT several fungal lineages and shown to be expanded in Cercospora beticola
RT based on microsynteny with recipient genomes.";
RL Submitted (OCT-2015) 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:PIA92867.1}.
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DR EMBL; LKMD01000105; PIA92867.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2G5HJX2; -.
DR OrthoDB; 389572at2759; -.
DR Proteomes; UP000230605; Chromosome 4.
DR GO; GO:0005096; F:GTPase activator activity; IEA:InterPro.
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};
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 10..131
FT /note="Arf-GAP"
FT /evidence="ECO:0000259|PROSITE:PS50115"
FT REGION 91..110
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 123..333
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 91..108
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 123..137
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 167..188
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 249..285
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 301..317
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 488 AA; 52334 MW; 67F1F4A25BDB90D8 CRC64;
MSLAPKTESH RIFEQLKRRA PNKICFDCGG KNPTWSSVPF GIYLCLDCSA HHRNLGVHIS
FVRSTNLDQW QWDQLRRMKV GGNESAKTFF QRNGGSAALN SKDPKTKYTS NAAVKYKEEL
QRRVEADQKR NPDGIVIEEE AGDEGPESGT STPANGDDDF FSSWDKPAVK RSSNPPSRTG
TPSQAGRASP FLNPGAANGN GTARPKSPLN PTNAEDAKPA PSRAVPSAAR KTTVASKPKA
NILGAKKTKL GAKKVDAGAL DFDEAEKKAK EEEERKAKLG YDPDDVETPS EAGIAAKQPG
AETSTIHQPT PLSPGRSGSY GNPKPRERSD SEMERLGMGV RKLGFGMVGQ QKKPAAAAGA
AKIGGFGSTS RAAPVEDDSE RYARDKFGAQ KGIGSDEFFG RGAFDSNAQN EAKSRLQNFE
GQTSISSNAY FGRPEEEGPE EYGDLEGAAK DFVRKFGIQA GDDLENVSAL LGEAGSKLQG
AIRSYLNS
//