ID V2Z316_MONRO Unreviewed; 1324 AA.
AC V2Z316;
DT 22-JAN-2014, integrated into UniProtKB/TrEMBL.
DT 22-JAN-2014, sequence version 1.
DT 27-MAR-2024, entry version 40.
DE SubName: Full=Sec7 domain protein {ECO:0000313|EMBL:ESK98359.1};
GN ORFNames=Moror_109 {ECO:0000313|EMBL:ESK98359.1};
OS Moniliophthora roreri (strain MCA 2997) (Cocoa frosty pod rot fungus)
OS (Crinipellis roreri).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Agaricomycetidae; Agaricales; Marasmiineae; Marasmiaceae; Moniliophthora.
OX NCBI_TaxID=1381753 {ECO:0000313|EMBL:ESK98359.1, ECO:0000313|Proteomes:UP000017559};
RN [1] {ECO:0000313|EMBL:ESK98359.1, ECO:0000313|Proteomes:UP000017559}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MCA 2997 {ECO:0000313|EMBL:ESK98359.1,
RC ECO:0000313|Proteomes:UP000017559};
RX PubMed=24571091; DOI=10.1186/1471-2164-15-164;
RA Meinhardt L.W., Costa G.G.L., Thomazella D.P.T., Teixeira P.J.P.L.,
RA Carazzolle M.F., Schuster S.C., Carlson J.E., Guiltinan M.J.,
RA Mieczkowski P., Farmer A., Ramaraj T., Crozier J., Davis R.E., Shao J.,
RA Melnick R.L., Pereira G.A.G., Bailey B.A.;
RT "Genome and secretome analysis of the hemibiotrophic fungal pathogen,
RT Moniliophthora roreri, which causes frosty pod rot disease of cacao:
RT mechanisms of the biotrophic and necrotrophic phases.";
RL BMC Genomics 15:164-164(2014).
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:ESK98359.1}.
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DR EMBL; AWSO01000002; ESK98359.1; -; Genomic_DNA.
DR RefSeq; XP_007842294.1; XM_007844103.1.
DR STRING; 1381753.V2Z316; -.
DR KEGG; mrr:Moror_109; -.
DR HOGENOM; CLU_003769_0_0_1; -.
DR OrthoDB; 4248238at2759; -.
DR Proteomes; UP000017559; 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; 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:SF402; ARF GUANINE NUCLEOTIDE EXCHANGE FACTOR SYT1; 1.
DR PANTHER; PTHR10663; GUANYL-NUCLEOTIDE EXCHANGE FACTOR; 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:UP000017559}.
FT DOMAIN 439..622
FT /note="SEC7"
FT /evidence="ECO:0000259|PROSITE:PS50190"
FT DOMAIN 772..889
FT /note="PH"
FT /evidence="ECO:0000259|PROSITE:PS50003"
FT REGION 1..30
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 68..157
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 189..293
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 316..395
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 442..476
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1001..1037
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1144..1194
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1251..1298
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 68..99
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 107..125
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 140..157
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 189..228
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 250..265
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 274..291
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 316..334
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 455..469
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1144..1164
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1173..1194
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1251..1296
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1324 AA; 145807 MW; F979F46F91A7076F CRC64;
MVPQSSSSAK PHNFSHHNHP VHSPPSYQEN DISPIIFSET VTTTEVVTTT TTQTITHFFS
FPLWRKRTPT SSLSSRPTFG SSLTLEDSMP QTGSSSLRVD KELPPTPPQE NHNSAETSLS
PSRRTSLDEI ADESRRPSLF PRSESPSRKV STSSRPSSTV ALAQAALGIG LPHVLSHAST
SSASEKNTIT FSSSLPSTPS GSSPSATANR RTSKWRALST TGPSEQLEPG SRRSRGLSLG
PASFLNLKGS ESRDKGKEKE VVSPPKQLVR KASFWSRKKN SSSSEPSRDP PETLVLQQDL
SVPSLPTITP ISPFYVDISS PSADQQSSRG QHSRGLSRSH SDRASNSRYS PKLPAESDVP
HRKRRPPRRP STADILNRPP TTRFLSDARP VTASPLSTPT AELEMQFSDQ QEQQHNSAFL
RPRSQTNPPF LHRLSLNIFS SSPSQTLPAS PSLTTPPIRQ TPPKPSIDIP KPQIDEESPE
GYLNRLRLAV SKSEIAGILA STVDPFHVSA LKSYISQFDF SEDPLDVALR RLLMDVGLPR
ETQQIDRVME AFASRYYQSH ISLFTSEDHP YILAFSLIML HTDAFNKSNK RKMTKADYIK
NTRLPGVAPE VLDCFYDNIV FAPFIFVEDP LDVNGQRGLM IDGTPSKTVS PIGTTPSLPT
NGSGSLILGK RSKVDPYYLI SNNLLEPLRI EVEELVPLTD PYTYKGTMGP WDERELLKSF
SQPSVIEVAD FSRANPVLFS LSVAGGPPSP LVSALGSPAV ERAQVPEPIV LKITKVGILN
RKDDYLEGGK KAASRRWRPW SVILTGSQLL LFRDPSWADI VLSSSVSTQA FKPDELLSVK
DSIAVFDRSY TKHECTFRFV LPDGRHILWG ASTEEDMNEW ISRINYASAF KSTGVRMRPL
GMSGRDVQLT GVAAATSHLH DLQHASQSQH MVKNWDNDAS HALMGMLSGD SAMVTPGKKP
PRRITTTSTN ADVDVPEAPE IDGADQFIAT FDQVKADLAA GRCASPDGSP RPDEQSPSFF
SEPPSLPVSP ESVLNNQQLP SRSRVVLSKV KTLEDRITAT QTQLDTDMRF VRNIAVLTPF
QRATRERLVI AVQKIAKQVV QMRLDIARLS CHRDVLFQDL AAEAQDWSRA KKIALRAATE
TLQGQRPRTS LSIPRMTLSY HDSDVSGSPP IPIPETSYAT SQNSLHRPES TADSFQSFHS
ALDFGPEWPS SDDIDAPDLL NQSHIMDSTL HGSISGGVFQ AGTTAEDGML KRTSEDGEDG
SPLPRESEDS QPRSHEKFHT AHETNEEEEA EEWNKTRCAQ RVSLVRLPSV LGFEKHRTNS
TINE
//
