ID A0A1G4ATC7_9PEZI Unreviewed; 1528 AA.
AC A0A1G4ATC7;
DT 15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT 15-FEB-2017, sequence version 1.
DT 27-MAR-2024, entry version 19.
DE SubName: Full=Sec7 domain-containing protein {ECO:0000313|EMBL:OHE92429.1};
GN ORFNames=CORC01_12290 {ECO:0000313|EMBL:OHE92429.1};
OS Colletotrichum orchidophilum.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Glomerellales; Glomerellaceae; Colletotrichum.
OX NCBI_TaxID=1209926 {ECO:0000313|EMBL:OHE92429.1, ECO:0000313|Proteomes:UP000176998};
RN [1] {ECO:0000313|EMBL:OHE92429.1, ECO:0000313|Proteomes:UP000176998}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=IMI 309357 {ECO:0000313|EMBL:OHE92429.1,
RC ECO:0000313|Proteomes:UP000176998};
RA Capua I., De Benedictis P., Joannis T., Lombin L.H., Cattoli G.;
RL Submitted (SEP-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:OHE92429.1}.
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DR EMBL; MJBS01000148; OHE92429.1; -; Genomic_DNA.
DR STRING; 1209926.A0A1G4ATC7; -.
DR OrthoDB; 4248238at2759; -.
DR Proteomes; UP000176998; Unassembled WGS sequence.
DR GO; GO:0005085; F:guanyl-nucleotide exchange factor activity; IEA:InterPro.
DR GO; GO:0032012; P:regulation of ARF protein signal transduction; IEA:InterPro.
DR Gene3D; 1.10.1000.11; Arf Nucleotide-binding Site Opener,domain 2; 1.
DR Gene3D; 2.30.29.30; Pleckstrin-homology domain (PH domain)/Phosphotyrosine-binding domain (PTB); 1.
DR InterPro; IPR011993; PH-like_dom_sf.
DR InterPro; IPR001849; PH_domain.
DR InterPro; IPR023394; Sec7_C_sf.
DR InterPro; IPR000904; Sec7_dom.
DR InterPro; IPR035999; Sec7_dom_sf.
DR PANTHER; PTHR10663:SF402; ARF GUANINE NUCLEOTIDE EXCHANGE FACTOR SYT1; 1.
DR PANTHER; PTHR10663; GUANYL-NUCLEOTIDE EXCHANGE FACTOR; 1.
DR Pfam; PF00169; PH; 1.
DR Pfam; PF01369; Sec7; 1.
DR SMART; SM00233; PH; 1.
DR SMART; SM00222; Sec7; 1.
DR SUPFAM; SSF50729; PH domain-like; 1.
DR SUPFAM; SSF48425; Sec7 domain; 1.
DR PROSITE; PS50003; PH_DOMAIN; 1.
DR PROSITE; PS50190; SEC7; 1.
PE 4: Predicted;
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Reference proteome {ECO:0000313|Proteomes:UP000176998}.
FT DOMAIN 509..677
FT /note="SEC7"
FT /evidence="ECO:0000259|PROSITE:PS50190"
FT DOMAIN 805..935
FT /note="PH"
FT /evidence="ECO:0000259|PROSITE:PS50003"
FT REGION 1..475
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 489..516
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1081..1325
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1341..1528
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 998..1025
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 108..122
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 145..170
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 216..266
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 287..326
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 357..456
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1081..1096
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1104..1211
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1212..1227
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1267..1294
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1302..1320
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1466..1500
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1528 AA; 168983 MW; 69D0D6EA47A8FEF3 CRC64;
MPFLRRRGNM VSETDMRRHT ILETETAPQL PPLPQHFPPQ RPQSHHQQQD QLPPPPPSPS
RPQSQQHKKQ KLDDQPKAIP ELKLPFLPPP PLSQLEQGQE QEQEHQGEQP RLSVSISIQE
PLPTSLAVPG PSDADNGALS QRNPDDQETR PDTPPIQEET PKHRRFSILR FRNASDSQLS
VRAKQQAEKP PPIPRPPEII TTAPTADFQV PQKKQSRMRL ADRFRRSGEI PRHSEDGGGR
AMTWKSSRRK TGLDEMESRN RPTLVTFEEP DRPASSRAPT NGEHHDVPNL SLPSNRASES
SRSDVSSGEH LYVTNATGNS PPVPSGSNFF RLPRRKPKTA APMFDLSHLP QKGKPSIGTD
NPATSSSSLG GPQPTAISTS REGTPRPQQG SRPQSSHSMR ANSVASSAHE QSAKPSASPA
TALFKPGSTN SGQSSPTRAR LQRRGRSSTL SSLGRESTDG HLDPGNGRAS TSVGRKSFGD
LFGLNRLRQN SDLGQGRQGS LTPATPGSNT SKNNSLQIAR EAIPLPDRLE DETPVKYLAR
IEEILSRGVI ASALSKGSDP FSIAVLRSYM RRFSFFEYPM DMAIRKLLME AELPKETQQI
DRCLQAFANR YHECNPGIYA SPDQAYFVAF SLLILHTDVF NKNNKHKMQQ PDYLKNTKGE
GVSDSVLSCF YDNITYTPFI HVEDDLDLNS DRLLANRAKR KTIFPGGTPE ATARRSNREP
LDPYTLIIDG KLDILRPSLK DVMELEDHYN YLGTAKDLNV KELQRTFFRT GVLQIVSARS
RPDAFRDDKG SSNPAEAAQG VVDIKITKVG LLWRKDVKKK KTRSPWQEWG AILTGAQLYF
FRNTTWIKNL MHQYESHVKQ GFDGEPITFK PPLPEFKPDG YLPTKEAVAL VDSTYKKHKN
AFKYAQPSGY VEEVLLADNE EEMNDWLAKL NYAAAFTTSG VRMRGVVGGN YEGQSRRGIR
RLGSSASAQV IQTPTGDVSI VRGKIDHKEA ESIHAQRRQT MMDAVAKADE EIALKEQELE
GHLRNARHLQ ILSPIQGKTR DQILSAAAHM DVKIKWTRMD MWKSMCHRDV LLKDLAEEQS
LRGLTPTTTP NGREPRETSP SSRERPSIPD AVSSNSVGRR RRRSSAAVST NQPLRTPQAE
PDSPVTEAYQ TPPTSATFSP HKYQNSWDSK LSKSTEHAQR QRPGSSSSQS SGEPTFYSPQ
QHSTQKKGNT AEQPADNDRH DDVDANERAL LQQAGLLESG SRGRIPPPER KRTGSFSEPG
DASESRDTPG SIDKQDKTKI RRSLQRTLRE SAGHLSHHRS RKGKDVISSG GADETSREDV
LTRGSGSFVV HGKKASVINF GSELQQLTPE ERMRQRKQDE PASPVSIAED YHDALNSSLE
PKERRGSAAS ASTATARSFR ELHRKYSSAH ASKAPIFGGR LSVPSDGESE AAVSFSEGRR
TPLPPIENES GDEAENEIAA DSPHVASPRP TTSPQLIISP QPISAALATP LATPSEPTTP
LEAQVDEEGE RGAEMQRLPS PPVQAVKA
//
