ID V2XPC2_MONRO Unreviewed; 394 AA.
AC V2XPC2;
DT 22-JAN-2014, integrated into UniProtKB/TrEMBL.
DT 22-JAN-2014, sequence version 1.
DT 22-FEB-2023, entry version 40.
DE SubName: Full=Stromal membrane-associated protein {ECO:0000313|EMBL:ESK95597.1};
GN ORFNames=Moror_12622 {ECO:0000313|EMBL:ESK95597.1};
OS Moniliophthora roreri (strain MCA 2997) (Cocoa frosty pod rot fungus)
OS (Crinipellis roreri).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Agaricomycetidae; Agaricales; Marasmiineae; Marasmiaceae; Moniliophthora.
OX NCBI_TaxID=1381753 {ECO:0000313|EMBL:ESK95597.1, ECO:0000313|Proteomes:UP000017559};
RN [1] {ECO:0000313|EMBL:ESK95597.1, ECO:0000313|Proteomes:UP000017559}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MCA 2997 {ECO:0000313|EMBL:ESK95597.1,
RC ECO:0000313|Proteomes:UP000017559};
RX PubMed=24571091; DOI=10.1186/1471-2164-15-164;
RA Meinhardt L.W., Costa G.G.L., Thomazella D.P.T., Teixeira P.J.P.L.,
RA Carazzolle M.F., Schuster S.C., Carlson J.E., Guiltinan M.J.,
RA Mieczkowski P., Farmer A., Ramaraj T., Crozier J., Davis R.E., Shao J.,
RA Melnick R.L., Pereira G.A.G., Bailey B.A.;
RT "Genome and secretome analysis of the hemibiotrophic fungal pathogen,
RT Moniliophthora roreri, which causes frosty pod rot disease of cacao:
RT mechanisms of the biotrophic and necrotrophic phases.";
RL BMC Genomics 15:164-164(2014).
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:ESK95597.1}.
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DR EMBL; AWSO01000073; ESK95597.1; -; Genomic_DNA.
DR RefSeq; XP_007845097.1; XM_007846906.1.
DR AlphaFoldDB; V2XPC2; -.
DR STRING; 1381753.V2XPC2; -.
DR KEGG; mrr:Moror_12622; -.
DR HOGENOM; CLU_023062_3_0_1; -.
DR OrthoDB; 1022106at2759; -.
DR Proteomes; UP000017559; Unassembled WGS sequence.
DR GO; GO:0005096; F:GTPase activator activity; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:InterPro.
DR CDD; cd08839; ArfGap_SMAP; 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 InterPro; IPR044732; ArfGAP_SMAP1-like.
DR PANTHER; PTHR45705; FI20236P1; 1.
DR PANTHER; PTHR45705:SF1; FI20236P1; 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 Metal-binding {ECO:0000256|PROSITE-ProRule:PRU00288};
KW Reference proteome {ECO:0000313|Proteomes:UP000017559};
KW Zinc {ECO:0000256|PROSITE-ProRule:PRU00288};
KW Zinc-finger {ECO:0000256|PROSITE-ProRule:PRU00288}.
FT DOMAIN 13..121
FT /note="Arf-GAP"
FT /evidence="ECO:0000259|PROSITE:PS50115"
FT REGION 121..179
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 192..250
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 332..376
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 157..179
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 200..215
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 236..250
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 394 AA; 41855 MW; E8BB7DFE9ECB3BF8 CRC64;
MSRPDKATTE RHAKVLRELV KQPDNKVCAD CKRNDPRWAS WNLGVFLCIR CSGIHRGMGT
HISKVKSVDL DKWTPEQMES IQKWGNRLAN LYWEAHLKAG HIPPDHKMES FIRSKYESRR
WAMEGPPPSN PSVLDGKQSA PPPAAAELPT QQPPPRSTHT PTNSLSSRNP APPVTTRQPQ
GHQLLSAGLV NQHHPRAPAP SSAQPAPPAA AAAAPTPPKA PENDLFSLDF HAPASVSPSP
GNTSPTGQVP KKDVKQDILS LFSTPAAPHP AMQSGFGQFG GMAAQTSPWA AAPASNHTAP
TQSTSMMGNT GVGMWGVNSG WGAAAPPAQP NVWANPTAPS PPTTQQPNLF ASSNDMWGGG
SLGGAQQDPF GSFSTAAPAQ KKDDVFGDIW GGFK
//
