ID M3D5G6_SPHMS Unreviewed; 1630 AA.
AC M3D5G6;
DT 01-MAY-2013, integrated into UniProtKB/TrEMBL.
DT 01-MAY-2013, sequence version 1.
DT 27-MAR-2024, entry version 49.
DE RecName: Full=SEC7 domain-containing protein {ECO:0008006|Google:ProtNLM};
GN ORFNames=SEPMUDRAFT_148510 {ECO:0000313|EMBL:EMF13129.1};
OS Sphaerulina musiva (strain SO2202) (Poplar stem canker fungus) (Septoria
OS musiva).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Dothideomycetidae; Mycosphaerellales; Mycosphaerellaceae; Sphaerulina.
OX NCBI_TaxID=692275 {ECO:0000313|EMBL:EMF13129.1, ECO:0000313|Proteomes:UP000016931};
RN [1] {ECO:0000313|EMBL:EMF13129.1, ECO:0000313|Proteomes:UP000016931}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SO2202 {ECO:0000313|EMBL:EMF13129.1,
RC ECO:0000313|Proteomes:UP000016931};
RX PubMed=23236275; DOI=10.1371/journal.ppat.1003037;
RA Ohm R.A., Feau N., Henrissat B., Schoch C.L., Horwitz B.A., Barry K.W.,
RA Condon B.J., Copeland A.C., Dhillon B., Glaser F., Hesse C.N., Kosti I.,
RA LaButti K., Lindquist E.A., Lucas S., Salamov A.A., Bradshaw R.E.,
RA Ciuffetti L., Hamelin R.C., Kema G.H.J., Lawrence C., Scott J.A.,
RA Spatafora J.W., Turgeon B.G., de Wit P.J.G.M., Zhong S., Goodwin S.B.,
RA Grigoriev I.V.;
RT "Diverse lifestyles and strategies of plant pathogenesis encoded in the
RT genomes of eighteen Dothideomycetes fungi.";
RL PLoS Pathog. 8:E1003037-E1003037(2012).
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DR EMBL; KB456263; EMF13129.1; -; Genomic_DNA.
DR RefSeq; XP_016761250.1; XM_016904967.1.
DR STRING; 692275.M3D5G6; -.
DR GeneID; 27902104; -.
DR eggNOG; KOG0929; Eukaryota.
DR HOGENOM; CLU_004694_0_0_1; -.
DR OMA; FVRHNAL; -.
DR OrthoDB; 4248238at2759; -.
DR Proteomes; UP000016931; 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; 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; 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 Coiled coil {ECO:0000256|SAM:Coils};
KW Reference proteome {ECO:0000313|Proteomes:UP000016931}.
FT DOMAIN 502..677
FT /note="SEC7"
FT /evidence="ECO:0000259|PROSITE:PS50190"
FT DOMAIN 810..939
FT /note="PH"
FT /evidence="ECO:0000259|PROSITE:PS50003"
FT REGION 1..88
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 129..148
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 202..259
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 272..388
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 421..517
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 951..981
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1117..1212
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1218..1237
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1249..1315
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1438..1630
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 1002..1029
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 33..49
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 53..86
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 227..242
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 280..340
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 364..385
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 421..459
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 468..517
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1120..1136
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1143..1159
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1175..1212
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1249..1274
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1279..1300
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1474..1490
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1492..1514
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1515..1537
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1565..1587
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1610..1630
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1630 AA; 180324 MW; 0946CB7681D3410D CRC64;
MPLLRRKSIL LWDSKKLHRQ QHEQQQQQQQ EQPHQHHQHE HEHVHDPGVE DSPCGSSLTT
TPSLDHPARP PSSSTSASSS LHPSAAASAA LLQHHPTLSS LPRPVSVAGE WPVGTSRLSH
ELHPDDIAET SADDHHENPG QSRSRFSLMK LRNHSEPHLW SRAKLEAERE RERAGEALPP
IPAVTAEGVL PMIVKTAPTM GAAEPDVQQQ GRERQLRPSV FRKPTTRSRA SEQDRRPSTD
MARSAKKGSS LRWRRGKTSG LEDLHRLSTM HLHDQHSAPP SYGEHSSSAL AVPVSQASDP
RISESSRSDG SSGDGQIYGS TTTTTHTVQT HTTFFKLPRR NKNRNSLFPL PIKLPPPDAS
PHDTNEPTTP RASTHSLTPE AVATPSTEVT AVRGAHAETE AFSQGSPKKL SFADPDMSLF
RRSSSRSEAS NTSSPLQPPI RFGMRDRSST QSSSGARSGG DADTPPPLSA SGRNSTSTAG
RSSFGGLLNL SRFRQSSEPH SPRHGSPGTR SKSNSFAMSR EALVIPERED GDTPGKYLER
LQSAVPRSVI AGILSKSSDS FAQAVLRSYT RRFPFFTEPI DMSLRKFLLE AELPKETQQV
DRVIQAFADR YHECNPGIYS SADVAYIIAF SIMMLHTDAF NRNNKRKMQK QDYIKNTSGQ
GISDEVLACF YDNICYTPFI HYDEDVDING ERVLHFTQSS KSGGRLKSAI PGAADITRKP
SGPVDPYNLI VEQKLDTLRP SIKDSIMMDD PYDYRGSHGD LDPQYLQRAF THTGIIQIIS
ARSRPAAYES QVVNGQPNLT ETQQGIVDLK ITKVGLLWRK SAKKKKTRSP WQEWGAILTG
SQLYLFKNSH WAKGLMHQFV THQKPGQSRT PVVFKPPLQD FKPDALIKTD NAVALVDATY
TRHKNAFTFI SNSGQEEVLL ADNESELHDW LGLINYAAAF RAAGVRIRGM TGSNDESTSA
PSLTRIQSSS SSKSFHTQNG EVTVSRRGLG AQLQRQVMAA RRQIMIRKIA EIEGEIENAY
RQLDGMLRNA RHLLILAPIA PRTRDEVVLA AGRADATIKW LRRDMWRLKC HRDILAMDVR
IDGMTASELE RLMPHHQPAE LESARKDRPK LLTRFGSHKI AKSPPQSPSA LNFNRPPTRE
SIDEGSGETS TTQPKPARAQ KEESSWRLPP LSLNAPPEEQ QNRRSVSSTL LSASPPASRT
SLQHSHSANS IQAVRTHSFE PSENGNSGKL SQTASVDEQE LQRLARANTN IDSAIGQDRS
ASGDAAALST SPESNKHKGV RRSLHKTLRE HHHGSHTHRH RRNKDSESTV RSGVAEAMEP
EVTTPGLTRE KPRFILHGKQ ASVVQFGGDW ERMKLRREQY EAGRASSEYQ SQLDAAYQRR
RSEAQERLRA GMTSPVVQEL RNSCTTDDDD DSASILSAES RSFRSDAEAA AAFAAVGHSG
KSLDSDEEES EFPGFDLSDW DPDTGRRTTI LGPFPVQPLQ QQQTPTKRRR FSSLQKGRDG
NIEDVEEYES SHHNNPENKG ISTSASAHST SPTGSRVVTP PDIPRNRENR RTVIGPPTFP
PYQALATAHQ GSYSTRATTT EEEAESSSAR GSFVEGEHGF VRAIGDDELR SMSSSLNSSP
EKKQKKQSSI
//
