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Database: UniProt
Entry: A0A1J7JG11_9PEZI
LinkDB: A0A1J7JG11_9PEZI
Original site: A0A1J7JG11_9PEZI 
ID   A0A1J7JG11_9PEZI        Unreviewed;      1520 AA.
AC   A0A1J7JG11;
DT   15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT   15-FEB-2017, sequence version 1.
DT   28-JUN-2023, entry version 21.
DE   RecName: Full=SEC7 domain-containing protein {ECO:0000259|PROSITE:PS50190};
GN   ORFNames=CONLIGDRAFT_601103 {ECO:0000313|EMBL:OIW26546.1};
OS   Coniochaeta ligniaria NRRL 30616.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Sordariomycetidae; Coniochaetales; Coniochaetaceae; Coniochaeta.
OX   NCBI_TaxID=1408157 {ECO:0000313|EMBL:OIW26546.1, ECO:0000313|Proteomes:UP000182658};
RN   [1] {ECO:0000313|EMBL:OIW26546.1, ECO:0000313|Proteomes:UP000182658}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NRRL 30616 {ECO:0000313|EMBL:OIW26546.1,
RC   ECO:0000313|Proteomes:UP000182658};
RG   DOE Joint Genome Institute;
RA   Jimenez D.J., Hector R.E., Riley R., Sun H., Grigoriev I.V.,
RA   Van Elsas J.D., Nichols N.N.;
RT   "Draft genome sequence of Coniochaeta ligniaria NRRL30616, a
RT   lignocellulolytic fungus for bioabatement of inhibitors in plant biomass
RT   hydrolysates.";
RL   Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
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DR   EMBL; KV875100; OIW26546.1; -; Genomic_DNA.
DR   STRING; 1408157.A0A1J7JG11; -.
DR   InParanoid; A0A1J7JG11; -.
DR   OrthoDB; 1369677at2759; -.
DR   Proteomes; UP000182658; 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:UP000182658}.
FT   DOMAIN          703..866
FT                   /note="SEC7"
FT                   /evidence="ECO:0000259|PROSITE:PS50190"
FT   REGION          1..51
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          74..192
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          267..298
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          365..439
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          476..661
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          690..713
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          857..921
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          986..1047
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1332..1379
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1491..1520
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        24..40
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        96..114
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        123..192
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        365..419
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        485..505
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        518..534
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        556..583
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        584..603
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        619..637
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        871..885
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        987..1047
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1338..1355
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1520 AA;  164369 MW;  6EC9D1851BD7F891 CRC64;
     MPTNPSRDAR DLETFLDSLT PIDTSNKEND RPREPPQPNY RDSHDLSLSP RQVTRDSLVT
     NMLLSLDQFS MGQTSAPFGS SRAPFDDPTA FSSFGGDDGG RSTTFNSKSG RPAGHGYSYS
     SDFEGGDDSS RISSQPSRGR RSNSSSGFQS SLGRINSMRE VSHQRGSPPT TRPLHSRSGR
     GSKSSSTNSI DPGYAQVLSS QRWAQGFGAR SSSFDYGHGR ASTATGAQPP QWHIEFSNTF
     FNDELDAAPT PTVPGGPRRL AAVPSLPVLP VSEPPTSPAK GPVLERKRSS RSSKSAIVGR
     KADTKFNTAR NAPPLPTFDL DSAPAPHVGY EKSKEVLSPV TTATATPAKD KPGFFRRMFG
     SSKNNLTSTT QSSSSAFISS TSVDTSGSRT PQHLNSMKSQ STPPSRESHH STAHGLQKKT
     SSFFRRRKHS VSDAEPPPLP LPPLVLPTVK LPVAKAGPEL LSAKPEPSPI TSLRRAMDPF
     MHSNPNTPEV ATPGSFPSPL QQELAPEKSS DVAPMLSPKL EKNDEYRRRT TRGFSPDYEP
     SPKALIRAVE TESGDGRTAK PTQTDTPTRR APDPPSMTRS GSFFHDNSDD ESSPRRRSSR
     AAQGEGGDRG LQVDSQAGDK RSPRLSTKGS EASISAGDGS KSKHGLLLLP SSPTKSDEAR
     SSLALPIEGV LASGPASPTD TLYQSAHSLP SVKVDSAEPS PQLKSSKSID EPDFVVGDPT
     EDDMQKAQKI YDGNEDFIQR DRAAAWMGEE GPVRQRTLRA YMDLYDFQDK SVVTSLRQMC
     NRLVLRAETQ QVDRILVAFA KRWCDCNPNH GFKATDVIHT ICYSIMLLNT DLHMADIEQK
     MTRSQFVKNT MTTLRQAVGD SGPETFDRPS ILPSKGQNLQ VEGENRNSVE QDRPSGFRAS
     FMPPPRPDSA LGTSSNTTHD SCGPLVKAPF DGPRRAWETQ VEIVLKDIYT SIRDERLPLF
     GAEAIPTPHS GGGLSVMGML KRSPSVLSKA PSESVSSLRG RISENPRASA SRWTSKSRSR
     QRGFGNGGFS SSRTSFEDGN SIWSPTESSA TWSRYSLGRT QASMSMDSFG TGHSRGDYQQ
     SIGFANALSQ AIIREDNDLF PTSSAGDEVK PAQLLEDESL ELAGSPWVKE GMVVHKHHLD
     GIDKKAKDRT WTEVFAVIQK GQMSLFSFTP NKSLRHKKSR LAGGTLPKNT VVGGGNWQEN
     ATNLGTFALK QTLASTLPPP GYSKGRPHVW ALSLPTGAVH LFQVGTPENS IEFVNAANYW
     SARLSTHPLV GGISNVEYGW SEAIINNILV QAIDESASSL NNRPGTGISA SIKGHSRPGS
     AANAASIMSA AGGGGRRMSI RSQSSVRSHS FDFPRPGSGS SGALGMTMTG GSASRHGKLP
     GDRIHIAEWT PPAQSLRAST ASEAEQLRIL ENYVRSVEEE LQAHNGLRSP MLLAFTPRGG
     NAARAMSNWQ KKSQYLLREI GKYRNYVDAL KQAEVRRGEV YEERERARRA AAGEVASLSG
     EEDEHEDEGV AAAETTEVAA
//
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