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Database: UniProt
Entry: A0A0F0I0S8_ASPPU
LinkDB: A0A0F0I0S8_ASPPU
Original site: A0A0F0I0S8_ASPPU 
ID   A0A0F0I0S8_ASPPU        Unreviewed;      1404 AA.
AC   A0A0F0I0S8;
DT   24-JUN-2015, integrated into UniProtKB/TrEMBL.
DT   24-JUN-2015, sequence version 1.
DT   27-MAR-2024, entry version 29.
DE   SubName: Full=Sec7 domain protein {ECO:0000313|EMBL:KJK61374.1};
GN   ORFNames=P875_00042318 {ECO:0000313|EMBL:KJK61374.1};
OS   Aspergillus parasiticus (strain ATCC 56775 / NRRL 5862 / SRRC 143 / SU-1).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
OX   NCBI_TaxID=1403190 {ECO:0000313|EMBL:KJK61374.1, ECO:0000313|Proteomes:UP000033540};
RN   [1] {ECO:0000313|EMBL:KJK61374.1, ECO:0000313|Proteomes:UP000033540}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 56775 / NRRL 5862 / SRRC 143 / SU-1
RC   {ECO:0000313|Proteomes:UP000033540};
RA   Yu J., Fedorova N., Yin Y., Losada L., Zafar N., Taujale R., Ehrlich K.C.,
RA   Bhatnagar D., Cleveland T.E., Bennett J.W., Nierman W.C.;
RT   "Draft genome sequence of Aspergillus parasiticus SU-1.";
RL   Submitted (FEB-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:KJK61374.1}.
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DR   EMBL; JZEE01000675; KJK61374.1; -; Genomic_DNA.
DR   STRING; 1403190.A0A0F0I0S8; -.
DR   Proteomes; UP000033540; Unassembled WGS sequence.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
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   CDD; cd00171; Sec7; 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; 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; PF01369; Sec7; 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   Glycosyltransferase {ECO:0000256|ARBA:ARBA00022676};
KW   Reference proteome {ECO:0000313|Proteomes:UP000033540};
KW   Transferase {ECO:0000256|ARBA:ARBA00022676}.
FT   DOMAIN          449..602
FT                   /note="SEC7"
FT                   /evidence="ECO:0000259|PROSITE:PS50190"
FT   DOMAIN          724..852
FT                   /note="PH"
FT                   /evidence="ECO:0000259|PROSITE:PS50003"
FT   REGION          1..97
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          121..457
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          869..902
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1000..1067
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1084..1320
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1363..1404
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          912..946
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COMPBIAS        11..25
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        26..56
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        82..97
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        188..242
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        249..263
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        293..307
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        327..430
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        875..891
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1005..1026
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1094..1127
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1185..1202
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1218..1256
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1262..1276
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1279..1299
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1370..1404
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1404 AA;  154591 MW;  F00371089263AE58 CRC64;
     MYWKGLRIGT SDGNEPKRRS LVEPQSVSRH SEQIPRPTLS TTNLAPRRSE SAPRSPTLTG
     PDADHHADTA GPELAGSHSH TPPGKVRNTG LSVSDGSHWR FNRFSFMRLR HASDPQLSKS
     YAKGEEDIPP VPSLPPPTII TTAPTSHELD QPVKRKTKFK LFPDSKTPSV EELPTQRAPK
     HDQSEKPGHT AQGSTASQAA YPVLSASLSN SEEPGRLSTT SIRSNRDQPN DSQRSSVTDA
     RFSESSRSDR SAGDSNPRSA SPREGASGNK RFRMPRLKRH RSPLFPLPPK PTGNGHAQSS
     ALSKSAAGDC TPKSDISEDP NEDHISPLPS PTRSSGGLTS SRPPLLRNDS ATSAHSARST
     PSNKSRAMPT SRTRSSTLDS LANAQDNGHP SPHLISGRTS TSTSGRKSFG DIFNIPQRFR
     QNSDSPVGRS GSPGSKGPGT PGSKISLITY PERQEDDTPA TYLTRLEESI PRSAIAGVLA
     QSNDDFYKTA LRKYMRGFSF FGDPIDMAIR KLLMEVELPK ETQQIDRFLQ SFADRYHECN
     PGIFASTDQA YFIAFSILIL HTDVFNKNNK RKMQKPDYVK NTRGEGISED ILECFYENIS
     YTPFIHIEDA VSNGRHFARP RRPLLKATST DHLVRATREP VDPYTLILDG KLDSLRPSLK
     DVMNLEDTYR CDGTDGPADI DGLHRAFSKS DVLQIVSLRS RPDMYMPSSI DNPADSNPGL
     VDIKIAKVGL LWRKDPKKKR ARSPWQEWGA LLTFSQLYLF KDVAWVKSLM AQHENHQREG
     RRRAVVFKPP LTEFKPDGIM STEDAVALLD LGYRKHKHAF VFVRHSALEE VFLANTEADM
     NDWLAKLNYA ATFRTAGVRT QGMIATDYEA QRNRMSRRGS TQSSRSHLSM DKEPPSPNPD
     TDVAEELVTA RRQLIRQKIR EANEKLSDAE RQLDDLLRNA RHLQVLTPVH SRAREHVIMA
     AGRMAAKLKW VRQDIWRTKC YKEVLVRDMG EALDEEKPIA EQKLHLQMPT TTVTSQPENL
     DGAVTDKVTS PTEDDPSPHA ESSGPHSVYK TLPSQPASPD GRRPSIPASF ASLEVASRIG
     RQLSIDNTEE RAKSCSPHPA SSLQREASVL SAASKVDVSS LGSRASKITA PGSMDETEER
     LLRETGLLDV SSSPQARKHS SATNDSEVDQ KPDDAQGAFQ GERTSRIRRS LHRTLRDSPS
     GHHLHYPRKK KSRDSGFSMV TSDDNQKPQQ GEGLSRKSTN FTVHGKKASI VTFGSEWQNM
     PPEERLKLRK PTPSDEPRAS NPELASSAGS ITSESLYPGS PHPLRSGSIA TKGSARDEPW
     GSAEAAGVLY REDKAKSDAA IGLVPELSEP DAALVPPVLT LDEPSAVSNE GVPPHSTRGD
     NDSLVENNTP QGMSPSPPEQ AVNA
//
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