ID V2WXT4_MONRO Unreviewed; 1579 AA.
AC V2WXT4;
DT 22-JAN-2014, integrated into UniProtKB/TrEMBL.
DT 22-JAN-2014, sequence version 1.
DT 27-MAR-2024, entry version 46.
DE SubName: Full=Signal transducer {ECO:0000313|EMBL:ESK85040.1};
GN ORFNames=Moror_15710 {ECO:0000313|EMBL:ESK85040.1};
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:ESK85040.1, ECO:0000313|Proteomes:UP000017559};
RN [1] {ECO:0000313|EMBL:ESK85040.1, ECO:0000313|Proteomes:UP000017559}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MCA 2997 {ECO:0000313|EMBL:ESK85040.1,
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:ESK85040.1}.
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DR EMBL; AWSO01001163; ESK85040.1; -; Genomic_DNA.
DR RefSeq; XP_007855653.1; XM_007857462.1.
DR STRING; 1381753.V2WXT4; -.
DR KEGG; mrr:Moror_15710; -.
DR HOGENOM; CLU_001251_1_0_1; -.
DR OrthoDB; 5100844at2759; -.
DR Proteomes; UP000017559; Unassembled WGS sequence.
DR GO; GO:0005085; F:guanyl-nucleotide exchange factor activity; IEA:InterPro.
DR CDD; cd04435; DEP_fRom2; 1.
DR CDD; cd00160; RhoGEF; 2.
DR Gene3D; 1.20.900.10; Dbl homology (DH) domain; 2.
DR Gene3D; 2.30.29.30; Pleckstrin-homology domain (PH domain)/Phosphotyrosine-binding domain (PTB); 1.
DR InterPro; IPR001180; CNH_dom.
DR InterPro; IPR035899; DBL_dom_sf.
DR InterPro; IPR000219; DH-domain.
DR InterPro; IPR011993; PH-like_dom_sf.
DR InterPro; IPR041675; PH_5.
DR InterPro; IPR001849; PH_domain.
DR PANTHER; PTHR46572; RHO1 GDP-GTP EXCHANGE PROTEIN 1-RELATED; 1.
DR PANTHER; PTHR46572:SF1; RHO1 GUANINE NUCLEOTIDE EXCHANGE FACTOR TUS1; 1.
DR Pfam; PF00780; CNH; 1.
DR Pfam; PF15405; PH_5; 1.
DR Pfam; PF00621; RhoGEF; 2.
DR SMART; SM00036; CNH; 1.
DR SMART; SM00233; PH; 1.
DR SMART; SM00325; RhoGEF; 2.
DR SUPFAM; SSF48065; DBL homology domain (DH-domain); 2.
DR SUPFAM; SSF50729; PH domain-like; 1.
DR PROSITE; PS50219; CNH; 1.
DR PROSITE; PS50010; DH_2; 2.
DR PROSITE; PS50003; PH_DOMAIN; 1.
PE 4: Predicted;
KW Reference proteome {ECO:0000313|Proteomes:UP000017559}.
FT DOMAIN 471..699
FT /note="DH"
FT /evidence="ECO:0000259|PROSITE:PS50010"
FT DOMAIN 753..944
FT /note="DH"
FT /evidence="ECO:0000259|PROSITE:PS50010"
FT DOMAIN 979..1138
FT /note="PH"
FT /evidence="ECO:0000259|PROSITE:PS50003"
FT DOMAIN 1182..1490
FT /note="CNH"
FT /evidence="ECO:0000259|PROSITE:PS50219"
FT REGION 26..195
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 508..530
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 620..646
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 46..84
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 111..127
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 132..148
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 156..175
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 179..195
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 514..530
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1579 AA; 176471 MW; DC2AA001D2C6EEEC CRC64;
MSNVDTTLDS TLGDEQLSEL FDKVWVGYGA GPHPRSTPTP PPPNNRLSTR SRSYRPLPPT
PGQSSSTSSP ISTRQFSVES PSEDQKFGRQ LPRPVTNGSG YFVQSPMEEA PQYPFPVPPP
PPPVPQVNRS YVEDTPEYTP SPAFSSHVPD SKSPAVAVLP PTPVPPPPPL PPSRVEEWQS
PGASGSGSAS WSPPEPYANG YTNGYTNGHV NGYDDYGAGP SNIAGPSTHA HAHLERRPSK
LLSAISAGPG LFPEEGGFDD VPYQDSDYGG GSFNGSEGDE DPYLFVNYSL LSHIAVQLKD
KVPRGTHVKG SIPYPRAFTG KDIVSTIQSL IQRELAINHN ISTSDRRAAL QVARSLQSQL
FFYEVEWGGD VLQDGVEDVY MFLDDMDGPS EGGVGEKAEL PTGVVTALTK CYTPDCVEGS
ACYSPRCPKR GDTVIGPAQN GPEPVQSALR GDWLKAVPKE VLVSLPESEI NRQTIIHKLI
SKEEQYIQDL DVVETMFIRP LRQANPPIIS SLPPSPSRNS YPSLHAHTPT SDTPVDSFID
TVFSNILDLR ECNKRLLEVL YVRQREQSPV IQRIGDIFLD AATEFRIAYP IYIGGYVAAE
KRLREEAENN TQWRMFVEQS TREVQRHRKP STPGLENGPS GSQAHQVSPI RLDLKHYLNR
PIEHLQKYPV LLEAILNETV EGNPDAEYLQ EAIEAIRALQ GIAQLRTFQT SMGRGPAGKW
EWFDLVGKDI TGGGKSDPKG KAKELGIGKT ECKRQSIIFE LIKGEMGYVK DLENIDVIYV
RPLRNAEPPI IPPDRIDQFI NDVFHNFNEV YAHHRRMLEK FHEIQREEHP VIKSITAAVF
DAALNFRDAY LEYVPNYPIA EYRIDEEMAR NPAFKKFVED CTRHPEAHRL DMKNFINRPI
PRLLRYELLL KGILDETPPG HEDREDIPQV LEVIKALGKD TEPGVVSAKQ KVELWRYNSN
IVFKPGEWID MDLLDENRSL IHTGKLLRQP EGGLNGWSEL FVLLFDNYLV MTKAREKDGV
TKFYVNRRPI PLDLLTLVNF TDPPTQRGAG LLRNLRGERH NTSNNTDLNT LRPPDNTLTT
VMSNTSGVST NASTLNDARS VFPCTIHHNG RMGGAYILYA ESAQVRAEWK NKLEEAMGLR
RVVQESNKVF EIETLSTDTF LVPPLVGQNT DGAVWSGDNQ FTGKVTCSVP FNTPDGRGLV
AIGCAEGVWI GFRHDSRSMR RVLHLKMVTQ CAMLEDFGIF LVLADKSLFA YHIEALVPSS
PASQHASQTP QKLSGNKDVH FFSVGTLQGR TLVVYMKRKS MDSIFYAVEP VIDKIKEVTK
ASVGLGSRLG FRTAKSDWFR PYREFFLPSE SFDLIFLKAK IAILCTKGFE IMDLSDLQSV
TIPQKEDPRF AGLAKRCESC RPLGMFRSTE DEFLLCYNEF GLYVNKRGEP SRPNGLIEWE
GTAERVALHS PYILLFDTRF IEIRHVQTGR LAQIICGNDV HCLWDGRGTN VQPPMTPLPG
QDEEERMVQE PRVHGVMNVN EPMGMARASP RAQHVFELIP TIPLYLPGSL ASPTTNTYFP
QSYSPPHSPT FRPMTLYRS
//
