ID A0A0C9YMA0_9AGAR Unreviewed; 1721 AA.
AC A0A0C9YMA0;
DT 29-APR-2015, integrated into UniProtKB/TrEMBL.
DT 29-APR-2015, sequence version 1.
DT 27-MAR-2024, entry version 28.
DE RecName: Full=SEC7 domain-containing protein {ECO:0000259|PROSITE:PS50190};
GN ORFNames=K443DRAFT_671608 {ECO:0000313|EMBL:KIK09108.1};
OS Laccaria amethystina LaAM-08-1.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Agaricomycetidae; Agaricales; Agaricineae; Hydnangiaceae; Laccaria.
OX NCBI_TaxID=1095629 {ECO:0000313|EMBL:KIK09108.1, ECO:0000313|Proteomes:UP000054477};
RN [1] {ECO:0000313|EMBL:KIK09108.1, ECO:0000313|Proteomes:UP000054477}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LaAM-08-1 {ECO:0000313|EMBL:KIK09108.1,
RC ECO:0000313|Proteomes:UP000054477};
RG DOE Joint Genome Institute;
RA Kuo A., Kohler A., Nagy L.G., Floudas D., Copeland A., Barry K.W.,
RA Cichocki N., Veneault-Fourrey C., LaButti K., Lindquist E.A., Lipzen A.,
RA Lundell T., Morin E., Murat C., Sun H., Tunlid A., Henrissat B.,
RA Grigoriev I.V., Hibbett D.S., Martin F., Nordberg H.P., Cantor M.N.,
RA Hua S.X.;
RL Submitted (APR-2014) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Proteomes:UP000054477}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LaAM-08-1 {ECO:0000313|Proteomes:UP000054477};
RG DOE Joint Genome Institute;
RG Mycorrhizal Genomics Consortium;
RA Kohler A., Kuo A., Nagy L.G., Floudas D., Copeland A., Barry K.W.,
RA Cichocki N., Veneault-Fourrey C., LaButti K., Lindquist E.A., Lipzen A.,
RA Lundell T., Morin E., Murat C., Riley R., Ohm R., Sun H., Tunlid A.,
RA Henrissat B., Grigoriev I.V., Hibbett D.S., Martin F.;
RT "Evolutionary Origins and Diversification of the Mycorrhizal Mutualists.";
RL Submitted (JAN-2015) to the EMBL/GenBank/DDBJ databases.
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DR EMBL; KN838539; KIK09108.1; -; Genomic_DNA.
DR STRING; 1095629.A0A0C9YMA0; -.
DR HOGENOM; CLU_001294_0_0_1; -.
DR OrthoDB; 1332300at2759; -.
DR Proteomes; UP000054477; 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; 1.10.220.20; -; 1.
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; IPR023394; Sec7_C_sf.
DR InterPro; IPR000904; Sec7_dom.
DR InterPro; IPR035999; Sec7_dom_sf.
DR PANTHER; PTHR10663:SF388; GOLGI-SPECIFIC BREFELDIN A-RESISTANCE GUANINE NUCLEOTIDE EXCHANGE FACTOR 1; 1.
DR PANTHER; PTHR10663; GUANYL-NUCLEOTIDE EXCHANGE FACTOR; 1.
DR Pfam; PF01369; Sec7; 1.
DR SMART; SM00222; Sec7; 1.
DR SUPFAM; SSF50729; PH domain-like; 1.
DR SUPFAM; SSF48425; Sec7 domain; 1.
DR PROSITE; PS50190; SEC7; 1.
PE 4: Predicted;
KW Reference proteome {ECO:0000313|Proteomes:UP000054477}.
FT DOMAIN 1203..1395
FT /note="SEC7"
FT /evidence="ECO:0000259|PROSITE:PS50190"
FT REGION 25..170
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 197..221
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 235..532
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 547..614
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 668..800
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 822..906
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 918..958
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 974..1088
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1595..1620
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1641..1670
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 25..42
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 60..104
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 204..221
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 332..355
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 375..398
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 409..424
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 443..499
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 506..521
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 553..578
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 677..691
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 692..725
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 726..741
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 742..783
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 839..905
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 927..958
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 977..991
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1055..1086
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1721 AA; 188353 MW; 0CF5CFFE957A253F CRC64;
MADQEPQPTR AEQRMLAVAK LKRAASVPRL KDGRRPPMHV EAVSEGEKPL VNGVASEEVE
EEVQEAKISH SEAEKLASDT EQGQPDDDKN VDPDSPHPNE NTPEAEMEVD VEEERPFSPG
LNTRSKRRSR SRSRSRGSKD FKGKAKGTQS PIPQVAGDSS PDEGPPLLHP IALPILTPLL
SPIPSHFALL QQSRLLRSPT PASPEPSLFY PGTSPPTPIP LPTLEALQRG LIRSNSAGST
AAGRRMAMHK LTGGTETYDS SPPPTPPPLP GKLGRNNTVA GGERIAARQF MLSRLGGRLN
KEFEEQQTSG TEDRGAPSPT PRHRRRRSRR GSAQASVNNA NAQISDSEPV TTSPNTPLVP
QTPLPLPLDA FANLRAQSAT PNQANSSRNQ SNERAMEPPP SLPQTEPETE PPEPRRRSVL
VEEEDDVEDR IPSLPLPVNN TLPGTPPQWY SPHIASLRTP QFSNPPSNGS SDSVSGTGVL
PVYLSQRSPS RNGPFPTSPF TTPLKEEKPS GDEDEEQVLY PAESRPRTPY VSNMEFDREI
SWVASPVPEI RMPIDDEEDE EGEEVEVHQE DPDDQYVEYE DPPLSASSST GFSPQDPEAF
DDISPRMSTS SKSIVVESEN SLDAIPPHHL PTSPSLAALS QTASFTLASD VSMSPQTYPA
RLSIASRIQS DRSPLNGDFT DWEDRFTSAE PSTKRNVESS SPSTWDKLKS TFTRTGSSSG
RRSRTNSIVT RERRDHTDSS ISRESGASLN SGRTDKGETI LFQHQPQQQP LMQSPSASAS
ILSLSHAAPR GGASPIPPVA SGDMAKYQNA KLFPFPGMKQ LQEQRRVAKG GYPASASSPD
VSMAYSGQED VQTPPISQSL NLNSSLNPES GELSSTGSGP PSASHIDVFT IPPSSPQNGS
SLNLKLPMTL PGVKQWLSKN NKKKTFPHHQ SLSPSASTSF SPPPIELQNS FNSNKKASLT
DLLRGKETEL GTDWEDIGIT PTSTKTNTLL GKRLNGPELR ERGQEVPSVN GAPYHTDTEK
TPKAKKIMPP VVARSSEPRH LSPDDQPPQR PVSGTPYPSS SLSDYPNHST SESESTSSSF
SHPGSQGSAV LERLEENLTR GSRNPMLSTA VDDPPRKLLL SSPVLQVVDP NTVKDRFLFL
FSDILVIAKP VSHDQDNFMD AYKPSPPDRK YVVKSVVLLR NLRFFPDRTE SQSRTGSHSP
VPRNPLVRSF VHNFSKDPDH AIATLFSKSN IPDDPQLLGQ LLFKTVDLDR ACLGDYLSRR
TSKIVLKTYL DSFGFAGLRI DIALKVLLQS LHVSPKSTQS HGASEYLLDF FAVRWYEANA
KSVAYDKDMA IRLVRGLVQL NDLLHDGIAD EAGKSDHIKR NITSRDFVDA FRRTDVRYLV
SDEFLEEAYD SIRSERLCQA RYPSPTSRAD LQITTKRHLP ARLTYKIQSE PIILRIPHVD
PSFSIQLYGQ DLVFDPPVLT FAKSSEASFR VMGTSLGSKT VTLCRSGPNA VNYAGLPISH
TVVVERAFMR NTFQLAFSNH TGAKRRYMFS VDDPLIRHQW AVSLKRQIDN ATAAAEPSTG
SLTPVAPKFL QAAESVAFKV LQEILIGTSL PSNPSSIKGP LHRHNISSQS SHGSVNGGLT
VDYRGSPQSL AALVRSKSRS KVYHRHGAGK NELDLSNNSK SRNPLEHAGG DAFENSVVYD
QSVRIEGNVW SGRDLQIQCQ QNSSIPLVLT FLQVDSQDIT P
//
