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Database: UniProt
Entry: A0A2N5SM51_9BASI
LinkDB: A0A2N5SM51_9BASI
Original site: A0A2N5SM51_9BASI 
ID   A0A2N5SM51_9BASI        Unreviewed;      1687 AA.
AC   A0A2N5SM51;
DT   25-APR-2018, integrated into UniProtKB/TrEMBL.
DT   25-APR-2018, sequence version 1.
DT   13-SEP-2023, entry version 15.
DE   RecName: Full=SEC7 domain-containing protein {ECO:0008006|Google:ProtNLM};
GN   ORFNames=PCANC_22604 {ECO:0000313|EMBL:PLW14317.1};
OS   Puccinia coronata f. sp. avenae.
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Pucciniomycotina;
OC   Pucciniomycetes; Pucciniales; Pucciniaceae; Puccinia.
OX   NCBI_TaxID=200324 {ECO:0000313|EMBL:PLW14317.1, ECO:0000313|Proteomes:UP000235388};
RN   [1] {ECO:0000313|EMBL:PLW14317.1, ECO:0000313|Proteomes:UP000235388}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=12NC29 {ECO:0000313|EMBL:PLW14317.1};
RA   Miller M.E., Zhang Y., Omidvar V., Sperschneider J., Schwessinger B.,
RA   Raley C., Palmer J.M., Garnica D., Upadhyaya N., Rathjen J., Taylor J.M.,
RA   Park R.F., Dodds P.N., Hirsch C.D., Kianian S.F., Figueroa M.;
RT   "De novo assembly and phasing of dikaryotic genomes from two isolates of
RT   Puccinia coronata f. sp. avenae, the causal agent of oat crown rust.";
RL   Submitted (NOV-2017) 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:PLW14317.1}.
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DR   EMBL; PGCJ01000924; PLW14317.1; -; Genomic_DNA.
DR   STRING; 200324.A0A2N5SM51; -.
DR   Proteomes; UP000235388; 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; 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:SF373; PH AND SEC7 DOMAIN-CONTAINING PROTEIN C11E3.11C; 1.
DR   Pfam; PF15410; PH_9; 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:UP000235388}.
FT   DOMAIN          796..976
FT                   /note="SEC7"
FT                   /evidence="ECO:0000259|PROSITE:PS50190"
FT   DOMAIN          1292..1441
FT                   /note="PH"
FT                   /evidence="ECO:0000259|PROSITE:PS50003"
FT   REGION          1..323
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          342..439
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          476..496
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          534..555
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          613..803
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          957..989
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1007..1103
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1205..1227
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1339..1362
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1520..1580
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        11..39
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        81..150
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        158..313
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        344..377
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        405..431
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        613..684
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        712..733
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        734..757
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1041..1055
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1206..1227
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1520..1558
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1687 AA;  181826 MW;  E01603E377CAB8D8 CRC64;
     MRKRSGFFRR KHSTSQAQAD SNCAESPSSS SHQLPLSPTP STEPSTPRYP LLAGEPSPHH
     QHHHHYSTAL DAPPVPIIPL SYNQNLATSQ SNNNSPSMPP PLKSRVSSPS STRRGPSSTG
     HSLDLEGPNQ EASASNTSTT NPNLYQEFPP LSASQPICRG SPAESLFSPS SSRPHSPALS
     SNRQFPIPSS CSSSQPRKSS WLQSTSRALF SSSERSDLPK LPSSTGAHTL SPNSAGLSPC
     PFSQTRNAPA SHDSRSGKNR PVLTATTFLS SSSSTSLGAD GGQVGSAGGS GSASQPPIPS
     SLNSTSSSLP HLPTVAPSPA LSEEDKLRLS LERWNLDLDG VLGGGSSSMS SPTTPKASSS
     DPNDANSHAQ QDPEVTERSV NPHIIRSPPA VNQYNLMTGL PPLPPESSAS ASHSLPSLVN
     PNRTTLQTRY PPDPFDRSHS SLTRIKALDL DSMSLIPSSD LLLASAPIIS SKHNPVGDDS
     GLTSTSFSSP NLSNAGPSSL QGIVVSRASS MKEWRDLGVS PVNSARVNNL RRRGYTENNG
     RQPPKLLGSQ FPAPSRRRSI LPQISSSQPT TTRAINAESV SCTVDPMSAA PEEEDTATDD
     PFARLPPSIR LVSCSSHTSS SEQDPPNSVV TGTSSQKPYA VSSRSPSFNR GDLPQSFRSS
     GSASPAVRAH PSQASKTTHQ LRGNTGLGAK PIVESDRPLS PQIPQLQRRD LDNKTTQTKK
     ATVNEDHRSP RNHQSSPNLR SFRPSTPTDN SFISVIVSAP QLPEEGTTPG EREISMAHSQ
     PHPFPSLASS PKPDSLSDRP DSRHSLIVPG LTLEANSLRL AELFWQEDES IIKRRKLTEW
     LGSPDTAENQ LQVLTRRAFM NKFDFKDLRI DLAFRKLCTK MYLKGETQQV DRILVEFSRR
     YWEQNQSHLY VNTDMVHALS YSVLLLNTDL HVVDTTSRMS RSQFIRNTME TVYAQLSNSE
     PSQADRSKMS FSDLPRPSIT ADSAKTNYRT GGSASMVIRN RRTSFIDLGR TLPGSGPSSQ
     SSARPSMERW RDVLRNGSQP IIKASRRSHS ITSLPSDDDL PGRVSGYPSA SARTSTDHIG
     RHPSVDGGTP SSPGLVLSDG HSSSAHFYSA DNGSSAHKSD KLNKALFDKE LESLLKDIYL
     AIKGHPIAQH PAESHSQESA SYASLQRMAS RRGHYGHGAA DTMGPHKRAS LRGFGGLAAM
     LSTGNDVPGA SPNSPTPSAS TSVSSLPSGM MGYSSNAGSS VNLTNLTTPS IGFVSNLSQS
     IIREQHEEES LESGQVDDDL ARDSELALLG APWAKEGILQ RKQYWESKGK RHKDRGWAEV
     FVVIQTGVLK MFQFGQSNSS SSAGGGGAVG LPGKEAEKNS IDAGSSNAHF GVGGGNWLPN
     AQLLGAITLS HALTSVLVSG YSRERAHVFV LTLSNGASYF FQAGTEELVY EWVSTCNYWA
     ARLSKEPLTG GVSNMEYGWN QLLESDLTAT ADKKEELAEC PADREELMSI VSGHSGHSHK
     GRRLRDLLFN GLPLAGSHSP TLVTQSSRTS DLEHWSQSVT SIDSQTPPPS QSEPKSASAV
     QLDRHAGQPT APEKLSIADW TPPVPPMALS SLPEQVQFEN LKRHNAHIQV ELEKHNLLRR
     PMVNMYWNRP MYLQKAMANW EKKSQYLMAE IIKYTTYLNA LESTIALKLK ISPGSGPAPS
     CSSSVNH
//
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