ID A0A3F3PLK0_9EURO Unreviewed; 1450 AA.
AC A0A3F3PLK0;
DT 16-JAN-2019, integrated into UniProtKB/TrEMBL.
DT 16-JAN-2019, sequence version 1.
DT 22-FEB-2023, entry version 15.
DE RecName: Full=SEC7 domain-containing protein {ECO:0000259|PROSITE:PS50190};
GN ORFNames=BDQ94DRAFT_184413 {ECO:0000313|EMBL:RDH27652.1};
OS Aspergillus welwitschiae.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
OX NCBI_TaxID=1341132 {ECO:0000313|EMBL:RDH27652.1, ECO:0000313|Proteomes:UP000253729};
RN [1] {ECO:0000313|EMBL:RDH27652.1, ECO:0000313|Proteomes:UP000253729}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 139.54b {ECO:0000313|EMBL:RDH27652.1,
RC ECO:0000313|Proteomes:UP000253729};
RG DOE Joint Genome Institute;
RA Vesth T.C., Nybo J., Theobald S., Brandl J., Frisvad J.C., Nielsen K.F.,
RA Lyhne E.K., Kogle M.E., Kuo A., Riley R., Clum A., Nolan M., Lipzen A.,
RA Salamov A., Henrissat B., Wiebenga A., De vries R.P., Grigoriev I.V.,
RA Mortensen U.H., Andersen M.R., Baker S.E.;
RT "The genomes of Aspergillus section Nigri reveals drivers in fungal
RT speciation.";
RL Submitted (JUL-2018) to the EMBL/GenBank/DDBJ databases.
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DR EMBL; KZ852086; RDH27652.1; -; Genomic_DNA.
DR STRING; 1341132.A0A3F3PLK0; -.
DR OrthoDB; 1369677at2759; -.
DR Proteomes; UP000253729; 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; IPR041681; PH_9.
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:SF373; PH AND SEC7 DOMAIN-CONTAINING PROTEIN C11E3.11C; 1.
DR Pfam; PF15410; PH_9; 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:UP000253729}.
FT DOMAIN 655..881
FT /note="SEC7"
FT /evidence="ECO:0000259|PROSITE:PS50190"
FT REGION 1..65
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 128..239
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 262..688
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 870..945
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 974..1074
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1307..1336
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 51..65
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 149..186
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 194..210
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 278..320
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 344..374
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 420..439
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 495..539
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 548..579
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 622..646
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 647..669
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 671..688
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 881..897
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 910..945
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1044..1074
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1307..1331
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1450 AA; 158103 MW; 7104DE66547E85EC CRC64;
MPQQHAGRSP PRTPPSEAVN GKPTRRGNHP RPSVRETFLD DFNAADNTNE SNESCDERDP
HDLSLSPKHA ARTSIVDNML LSLDQFVAGS SVLDDYRLFN SVFETDLYGH GSPDSLAQRR
YRGHTFSSSL SSEVDGTFED GTARHASQLP RGRRSNSSSN YHSSLRRFGS TRSREGTGSR
GQLYDYRPSS TAAAGAHTAR NGSKGSASSQ VDFGPPLLRR RADSTGERRS ASFDFGTRPP
FIPFSEPVAD YGSWSFSDFD AAPTPSIPGG PSKHHPSSQG DYAGSLSLQQ SRTPVASRRN
SIKSPRANSN RKSRPENIGT ATIRSRDLDL ANLGDAGLEL PPTIPSSLDP PAPSPTISFN
KPIFPPPPEP APAKERPGFF RRVFGSKAPT FGPSDYSQSD SHSAQETDTK DIKSWRQPLK
HSGTGLNSGR DGNHQVVTKK SSFFRRRKKS VAESAPPPIV LPPELSGSRA MEIMKPEPSP
VGSLKKVMNP YIMDSNASMP DQANKPSQSR AATDDAEAKN PGTTSTHNPR GSLLTTSGPP
KAKYSLYPAV SSANNNEATF LGNSSGDEES GSKSNGQDPI APVDRQPGSR ASRDGVSSRG
SDMDSVDKDQ VFALPGGLKP QETAVSSLSP VMESFSQMSA SPTHSSDDAP EETKEIPVSD
VRKDEIVDGT SRISTPANGP GGSPRASISE MSNYYTASES AAMGPTEPKL ADLAEASPDD
IPASEPTSSD KEQAQMLFDS QDQVVGNEPA AAWLGDPDRA LVRKAYMDLF DWANLNILAA
LRSLCNRLVL KGETQQVDRV LDAFSTRWCE CNPRHSFKAS DVVHTICYSL LLLNTDLHLA
DIEQKMTKAQ FVRNTMPTIH RVAADAAPDG FFDQRDANKS KAQSQDPPSL ASNSRSATTD
DLERKTPTAD KPTNGPTKLV NRLSRTDLSA KMISDPDNDT GPLVNTPFTG TMRAWEQQVE
MVLRDFYTSI QKQKLPLHGA QGEKEPTRSS SNNLLGPHPG GLRRSPSTVS KSGSDIYPRG
RSADSRYGTA RWSSKPRSRA RLYPPSTMGS SRTSLDDQSS LWSPSASSTW SKYSSGKLTS
ASVDSFNSDY PRGDYQQSIG FANALSQAII REDSAHSIAS FEDAERNTPL LEDETLQLAG
APWAKEGSLK HKHHLDSVDK RAKDRNWNEC FAVIQQGWMR LFSFNASMKS VRQKAKQRHP
GGVVVGGGNW TENAEEIWKF LLRQTIASAL PPPGYSKSRP HVWALSLPTG AVHLFQAGTP
EIVREFVSSA NYWSARLSKE PLIGGISNME YGWSDAVINS ALISAESSRT PPSSSGARPS
IQSSIRSSID QQGVRPRLPA DRVHISDWAP PQQSMMASAL PEDEQLKALQ TYVKNVEEEL
QRHNELRPAM ILAFSPRHPN AAKALANWER KSSYLLREIV KFRTYIDSLS SALEQKKRIY
TNREESTPVE
//
