ID W2RST0_9EURO Unreviewed; 1423 AA.
AC W2RST0;
DT 19-MAR-2014, integrated into UniProtKB/TrEMBL.
DT 19-MAR-2014, sequence version 1.
DT 27-MAR-2024, entry version 42.
DE RecName: Full=SEC7 domain-containing protein {ECO:0008006|Google:ProtNLM};
GN ORFNames=HMPREF1541_05797 {ECO:0000313|EMBL:ETN39571.1};
OS Cyphellophora europaea CBS 101466.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Chaetothyriomycetidae; Chaetothyriales; Cyphellophoraceae; Cyphellophora.
OX NCBI_TaxID=1220924 {ECO:0000313|EMBL:ETN39571.1, ECO:0000313|Proteomes:UP000030752};
RN [1] {ECO:0000313|EMBL:ETN39571.1, ECO:0000313|Proteomes:UP000030752}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 101466 {ECO:0000313|EMBL:ETN39571.1,
RC ECO:0000313|Proteomes:UP000030752};
RG The Broad Institute Genomics Platform;
RA Cuomo C., de Hoog S., Gorbushina A., Walker B., Young S.K., Zeng Q.,
RA Gargeya S., Fitzgerald M., Haas B., Abouelleil A., Allen A.W., Alvarado L.,
RA Arachchi H.M., Berlin A.M., Chapman S.B., Gainer-Dewar J., Goldberg J.,
RA Griggs A., Gujja S., Hansen M., Howarth C., Imamovic A., Ireland A.,
RA Larimer J., McCowan C., Murphy C., Pearson M., Poon T.W., Priest M.,
RA Roberts A., Saif S., Shea T., Sisk P., Sykes S., Wortman J., Nusbaum C.,
RA Birren B.;
RT "The Genome Sequence of Phialophora europaea CBS 101466.";
RL Submitted (MAR-2013) to the EMBL/GenBank/DDBJ databases.
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DR EMBL; KB822721; ETN39571.1; -; Genomic_DNA.
DR RefSeq; XP_008718356.1; XM_008720134.1.
DR STRING; 1220924.W2RST0; -.
DR GeneID; 19973136; -.
DR VEuPathDB; FungiDB:HMPREF1541_05797; -.
DR eggNOG; KOG0929; Eukaryota.
DR HOGENOM; CLU_004694_0_0_1; -.
DR InParanoid; W2RST0; -.
DR OrthoDB; 4248238at2759; -.
DR Proteomes; UP000030752; 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; 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; PF00169; PH; 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 Glycosyltransferase {ECO:0000256|ARBA:ARBA00022676};
KW Reference proteome {ECO:0000313|Proteomes:UP000030752};
KW Transferase {ECO:0000256|ARBA:ARBA00022676}.
FT DOMAIN 465..638
FT /note="SEC7"
FT /evidence="ECO:0000259|PROSITE:PS50190"
FT DOMAIN 760..889
FT /note="PH"
FT /evidence="ECO:0000259|PROSITE:PS50003"
FT REGION 1..213
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 231..272
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 291..491
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1031..1080
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1092..1126
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1153..1250
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1277..1327
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1339..1423
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 948..975
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 12..42
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 64..97
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 159..183
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 251..272
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 309..366
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 401..436
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 452..474
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1042..1080
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1092..1107
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1160..1179
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1199..1214
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1235..1250
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1277..1291
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1310..1327
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1353..1371
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1386..1402
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1403..1423
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1423 AA; 156684 MW; E3FC63E4122E978B CRC64;
MPFPSLRSRP GTGESSKHHR HTIFEAHSPK KSEKDAAKDR MSVHIPKFGS GDFGPPLIQR
EEPTPSPRRS DEGSGQEDED DVSKRVSSQE DHATADHLEP PTNSPAAIPE SDETAPPRPQ
RFSLLRFKNA SDPQLSFRFK KASTPPEERE PLPPAPAIIT TSPTVNDATA EPSKKSAQKL
FSGRSPSPFR RKGTVRHSNL GRSTTPDGHI TVAASTPDLH NEKASKLEQM HSLDGVPGPP
AYGDESSSQL AIPIERLSDS SRSDASSGEK VYARTTTTHV ITSTTTFFKL GRRKKNKGPL
FPLPEKLQPS TSERASFSTT GFEGGRRSMS PSRKSTSAVR FEPGTSGGDS GAASPTNSTV
ALTNAPFGSP GPSVLRKEST HSGQSTPPAA ALIPPRLGAR GRSSTMSSLG RSAERVGQDQ
PGSTRTSTST TGRRSFGDLL SLPHRLRQNS VPPPRHGSSN SPGTPGSKSN SLQIPREEVP
ELVYPKRDES DTPASYLEKL EAAVQRGSMA TILCKSADEF SRTCLRKYMR GFSYFGESID
MAIRKMLMEV ELPKETQQID RLLAGFADRY YECNPGIFSS TDETTFVAFS ILLLHSDTHN
KNNKRKMTKH DYFKNTQQGS VTVSSDILDC FYDNICYTPF IHFDDEVAIN SHRLHAPRPK
KSLIRVKSSE KLRGPVDPYL LILDNKLEVL RPSLKDVMDT EDTYRSTGTA ASFDIFELHR
AFLKSSVLQI VSARSRPDAF MSQATIFNPS EAQAGLVSIK VAKVGLLWRK SPKKKKTSSP
WQEWGAILTD SKLYFFKDIG WVKKLISQHE NHSKANTKSA PLIFKPALTE FQPDALISMD
DAVALYDSNY KRHKNALVLL KHGNIEEVFL ANSETDRNDF IQKINYAATF RSAGVRMRGP
LGTTYEGRQL FRKDSEISTA SADTAKHNGP LSPSMDPQAA WEIMFYRRQL ISEKISDYDE
KIAAVQKELE TLLRNARGLS VCLPIQQKTR ESLIMAAGRM SAKLKWTRVE LWRNKTHRDV
LALDLDQEAQ ADFPAPHGTP QKLTPVKSTA QSLARTDTET SKQTLSPTTS SKPGQSRRAS
QALLETGIDT VVENAPSVTS SPKTLQEPFA PTKRDSRPDM VQQSSTISQR LLHEHESAHI
EAGEEQVLRE AGLLGVDGNV TKEKRPDTSE SERDRVGAIS PSSDHFLRDR GSSVRRSLHR
SLRDHHHVHA SPSSSRHKKN RESGSSAVTE GDIKSTHSGE SEELRRGTGS FILHGKKASV
ITMGEEWRNM SAEERMKMRQ QNKKDDNDAV DDGTASIASR PSSRAESESV EANSVREVDP
RKLSVITQDH EDFVDAKTSL EGSVSRASHV DRGSLFVDAK DFRSSMDSRS VQEESDEDES
NSEDEDDTTS KGKAKAEDDT VRLTNSLGES SSAPGPAVTN GSS
//
