ID A0A0D0A0X4_9AGAM Unreviewed; 1679 AA.
AC A0A0D0A0X4;
DT 29-APR-2015, integrated into UniProtKB/TrEMBL.
DT 29-APR-2015, sequence version 1.
DT 27-MAR-2024, entry version 27.
DE RecName: Full=SEC7 domain-containing protein {ECO:0000259|PROSITE:PS50190};
GN ORFNames=PISMIDRAFT_91862 {ECO:0000313|EMBL:KIK28052.1};
OS Pisolithus microcarpus 441.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Agaricomycetidae; Boletales; Sclerodermatineae; Pisolithaceae; Pisolithus.
OX NCBI_TaxID=765257 {ECO:0000313|EMBL:KIK28052.1, ECO:0000313|Proteomes:UP000054018};
RN [1] {ECO:0000313|EMBL:KIK28052.1, ECO:0000313|Proteomes:UP000054018}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=441 {ECO:0000313|EMBL:KIK28052.1,
RC ECO:0000313|Proteomes:UP000054018};
RG DOE Joint Genome Institute;
RA Kuo A., Kohler A., Costa M.D., Nagy L.G., Floudas D., Copeland A.,
RA Barry K.W., Cichocki N., Veneault-Fourrey C., LaButti K., Lindquist E.A.,
RA Lipzen A., 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:UP000054018}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=441 {ECO:0000313|Proteomes:UP000054018};
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; KN833694; KIK28052.1; -; Genomic_DNA.
DR STRING; 765257.A0A0D0A0X4; -.
DR HOGENOM; CLU_001294_0_0_1; -.
DR OrthoDB; 1332300at2759; -.
DR Proteomes; UP000054018; 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 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:UP000054018}.
FT DOMAIN 1154..1353
FT /note="SEC7"
FT /evidence="ECO:0000259|PROSITE:PS50190"
FT REGION 1..146
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 222..242
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 262..486
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 501..751
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 764..874
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 891..912
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 932..1046
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1571..1637
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 23..52
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 114..128
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 129..145
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 262..279
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 294..367
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 368..384
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 392..408
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 415..429
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 440..462
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 513..530
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 531..552
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 574..623
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 667..696
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 712..738
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 778..816
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 826..872
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 891..911
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 958..991
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 992..1015
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1016..1046
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1573..1597
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1679 AA; 182775 MW; 303ADA2CE064E385 CRC64;
MENDAASVAE QRANAVAKLR RAASLPRMKD GRRPPMRVEA VSDGEKFQTE ELQSEVVEPP
QAELPTSTEA NPEAVSERKP GTPEPSAAAR KRRPRSRSRS RGSKDFKGKF KPQSPTPISV
TPSNDSSPDD SSPSPPPPPP SVLAPIPSHL AVTSASRLLI SQNFLSPGTP LYSGTSSPAP
IMPTLDAIQR GLIRSNSVAA RMQAWQKLTG NIDPQDGTFL SPSASPQPVL GKLGRNNTVS
GGERSAARLK LFTTLNERIK EADVEGTSGG EDRERVVQAP SKRRRRRSAR HSAGATNRAP
TTDESSGVPT STSSPAVTPA PLPSTLSNES TVIEPARTAS ETPIPAQPLT INLNETITGS
REATPVRSDP PSQRKRRSVL VEPDDDVVPP HCTYPGLPPT PKHPSPAASP RIPHSSDAPS
RTSSPSTPGA VGVPVYLSAT QRPPSRQDAF PSSPFTTPHM EISISSRDEE EDVESENPEE
VVYTAENLRR SPYHDAFNRE ISWIADPVPE STLPVYDEDE DDDEAQLMHD VVQEEDDQQP
PESPREEFEP QTETSSPRQS SDSKDLVVEQ ELSPEPALSN TSPAPSPLAV TPNTTSALRS
SDESDSSQPA YPQRLSVASR IQCDRSPLNA EFDLDNPVSA PPETPLKRDG SITGTWGRIM
GALTRSASSG GRRSRTNSLA TRERQNTDSG INRESGGSLA SPKVDKHESI ASAHPPSQSV
MQSPSASASM QSLALQTPPR GGVSPIPPVS SADLAKYKDA KLFPFPGMKK LEEQRRNRGL
SVSSSTPDFV QSLPTTENDI PVPSSSNNTP SNSPDIKRDR TLSHQASDTH LLSKFKNLSS
PPLSTSASTS SRDQFGGQTP TTPQSAASVS VKLPTNREGV RKWLSKFGQS TPSLVTSSMT
STSQTRPAFS KKPSISDLLR WRKENDITSD WEEINSEKAR TPTSTSGGTF LGKPISGEFS
PVSTNGSFIN EDTQKTPRAS KIAKSSDSFS SSPAPLPPPS LPSPFVSPPP ELASSATPEP
WSSLSDYPPP TTSESSSNTS SQYSDYPAKG AAVMERLNEM ISRGPRSPTW PTTIDDPPRR
LILAAPVLQV VNANTVKDRF LMLFSDLLII AKPVVQEPDA LLELTKPNPS DRKFIVKNVI
LLRNLCFSGD REDPQSRSIP QNTLVQPFVE QFSGNPDRAI MSLFNKCGQH EDPVALAQLL
FRTPDIDRAQ LGDYLSKRSS RAVLKNYLDA FGFTGVRVDK ALRIFLQTIH ISTQASYGTS
AFDTVLDSFA SRWYEANASH VAYDKDLAYR FTRAIVQLNE VLHGAITSEP GPTGYARRNV
TARDFLDAFR RQDPRSLLSD DLIGDVYDSI RRERLCQARH PSNSTPADIA ITFKRPLPPR
LTYRVQSEPV VVRIPQPDPN FAIELFGQDL TFEPPILTFA KSPEVSFRIT GTSFGLRTVT
MLRCGPNALL YTGLPPSFSI SVERAFMRNT FQVAFLNHAN IKRRYMFSFA DPLVRHEWTT
SLKRLTETAI CTRPATGIKG SLPLAQDNFN HAIGSIAFRV LQETLIGPEV VVVQTSTSKL
KDAIKRLAAP SYPRNGSQVS ASHQDARGLS SDLVRSKSRS RTYYRHGPGK LELDSTSLTL
AQPSNPGADH EDEPVMQSRR GDRIWSGKDL EVFCRQNSSI AQVLELILPM TPEAVTQSS
//
