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Database: UniProt
Entry: A0A437A3A3_9PEZI
LinkDB: A0A437A3A3_9PEZI
Original site: A0A437A3A3_9PEZI 
ID   A0A437A3A3_9PEZI        Unreviewed;      1513 AA.
AC   A0A437A3A3;
DT   08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT   08-MAY-2019, sequence version 1.
DT   13-SEP-2023, entry version 15.
DE   RecName: Full=SEC7 domain-containing protein {ECO:0008006|Google:ProtNLM};
GN   ORFNames=DFL_003950 {ECO:0000313|EMBL:RVD85633.1};
OS   Arthrobotrys flagrans.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Orbiliomycetes;
OC   Orbiliales; Orbiliaceae; Arthrobotrys.
OX   NCBI_TaxID=97331 {ECO:0000313|EMBL:RVD85633.1, ECO:0000313|Proteomes:UP000283090};
RN   [1] {ECO:0000313|EMBL:RVD85633.1, ECO:0000313|Proteomes:UP000283090}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CBS H-5679 {ECO:0000313|EMBL:RVD85633.1,
RC   ECO:0000313|Proteomes:UP000283090};
RA   Youssar L., Wernet V., Hensel N., Hildebrandt H.-G., Fischer R.;
RT   "Intercellular communication is required for trap formation in the
RT   nematode-trapping fungus Duddingtonia flagrans.";
RL   Submitted (JAN-2019) 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:RVD85633.1}.
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DR   EMBL; SAEB01000006; RVD85633.1; -; Genomic_DNA.
DR   STRING; 97331.A0A437A3A3; -.
DR   VEuPathDB; FungiDB:DFL_003950; -.
DR   Proteomes; UP000283090; 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   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; GUANYL-NUCLEOTIDE EXCHANGE FACTOR; 1.
DR   PANTHER; PTHR10663:SF328; MIP16918P; 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   Reference proteome {ECO:0000313|Proteomes:UP000283090}.
FT   DOMAIN          407..627
FT                   /note="SEC7"
FT                   /evidence="ECO:0000259|PROSITE:PS50190"
FT   DOMAIN          751..881
FT                   /note="PH"
FT                   /evidence="ECO:0000259|PROSITE:PS50003"
FT   REGION          1..131
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          159..276
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          289..350
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          371..465
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1007..1039
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1060..1085
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1122..1145
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1172..1282
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1300..1399
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1473..1513
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        25..48
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        55..79
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        80..95
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        159..191
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        199..214
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        221..235
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        250..276
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        312..340
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        371..438
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1016..1039
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1172..1229
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1237..1270
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1355..1376
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1513 AA;  165651 MW;  2A4D261E74B759E0 CRC64;
     MTGLSWRLRP ANSRKDGSLR RQSVDVGTLF RQQESNASTT NVNESEAAAA APQEQLPTPK
     STTTTATQET ASRVSTSTIR PRPRKSEERT RSNRFSILKF RNASDPALGS KARAHEEIPP
     LPDPPRTPTI ITTAPTFDIA AAPPLPQTKS AGDIAELRTS SATGSRTNLS ATLTTASAST
     SREQSVSPAP RPSSAPRRES SRKNIGSNPS GRASRVTFDE PERTYPNNGS TQSFAPPPYD
     EHGLPIPQPR LSESSRSEAS SADMVVTTTT TTHTVSTTST FFRFSRRKKD TPLFPLPPKV
     SHMEPRVSTD AIGGGASSSN VSIRSRPSNT LSSAPPTPRQ VPTSDGMPIP ATSALAASVL
     GTMGGSATLA RANSTASNHS LRSTTSSPLA PQTRYNRARS STAGSMDRSP ADSTRTSMAV
     GRNSFSRLFS SRSRQNSEAH LPGMPARTTS PAPYLARAST SHPNSMAVSR EKLIIPERLD
     DDTPDQYLRK LEEAVNKSVV ASLLSKTDDA FHVEVLKQYM GTFNFYRDPM DMALRKLLME
     VELPKETQQI DRVLQAFADR YHECNPLIYS SSENAYFIAF SLLILHTDVF NKNNKHKMQK
     PDYVKNTSGE GITSDILEYF YDNISYTPFI HVEDDLDING EKILSHMPRR NILTKANTDL
     KKAREPVDPY TLIIDNKMDI LRPSLSDVLM VDDPYSYLGT THTMNMKELH ESFFRSSVLQ
     IVSARSRPDA FLNPATAQNP QDASPGVVEI KVTKIGLLWR KDPKKKKTRS PWQEWGALLT
     GSQLYFFKNV SWVKNLMSQY EQHVKAGNVG IIPCVFTPPL PEFNPDSMLS TDDTVALLDR
     TYKKHKNAFM FVRHGGFQEY FLADNETEMN DWLSKLNYAA AFRTAGVRMR GVTASGEVSI
     VSGRIDPQLA AQIAAARRQV IDRKIHDSNM KLKDALDQLA MLLRNAHHLK LLTPIQAKTR
     DAVILAAGSL NAKLQWVRVD IWRLRCHRDI LELDLEEERR SAKDKLRRLT LLQTPPETPA
     RGSKSPSLAD SPLSAKSTPT QATINASFNK PLFENEIVRQ STRTTTVSRT ASQSTARPST
     LGSHQGWEIG QLPFELRRGS VVGDITGDID LSQLGEPYMT NTESREYVSV TTSSSNEEIP
     RRLSNGSVIS QQAIAQAIKP GGDPESEFLE QITAKDEKGK EVEDSASHRE KKDKEKEKEK
     EKEKEKEKEK DRKEEKEKDK VRRSLHRTLR EGSQVIQLPH HRSRKGKDGN PQGEKADGEI
     DGEKKESEGL ARGAGSFTVH GKKASVITFG SDWHTIPAED RLKRHRSAAS TSVPAAAPGT
     VGDRVLDASS VGKVTVTETS AVDSSDDEDG GSGSAAASIS RSQLSRGSSS VSGRLAVVNP
     DNEGEETGTT GEKEVNDGEI SIMTASAVTD DDASNFIPDA LASPALSDAT VTHFGDTRRS
     LTTASYEAEA VVVEIAKESD EKKIEEVVVL INSQGNSGDD LPTTADDILA RPEPSVSVGA
     SLDAGKPDEE PEK
//
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