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Database: UniProt
Entry: A0A010RQY8_9PEZI
LinkDB: A0A010RQY8_9PEZI
Original site: A0A010RQY8_9PEZI 
ID   A0A010RQY8_9PEZI        Unreviewed;      1613 AA.
AC   A0A010RQY8;
DT   11-JUN-2014, integrated into UniProtKB/TrEMBL.
DT   11-JUN-2014, sequence version 1.
DT   22-FEB-2023, entry version 36.
DE   SubName: Full=Sec7 domain-containing protein {ECO:0000313|EMBL:EXF74683.1};
GN   ORFNames=CFIO01_08753 {ECO:0000313|EMBL:EXF74683.1};
OS   Colletotrichum fioriniae PJ7.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Hypocreomycetidae; Glomerellales; Glomerellaceae; Colletotrichum;
OC   Colletotrichum acutatum species complex.
OX   NCBI_TaxID=1445577 {ECO:0000313|EMBL:EXF74683.1, ECO:0000313|Proteomes:UP000020467};
RN   [1] {ECO:0000313|EMBL:EXF74683.1, ECO:0000313|Proteomes:UP000020467}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PJ7 {ECO:0000313|EMBL:EXF74683.1,
RC   ECO:0000313|Proteomes:UP000020467};
RA   Baroncelli R., Thon M.R.;
RT   "The genome sequence of Colletotrichum fioriniae PJ7.";
RL   Submitted (FEB-2014) 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:EXF74683.1}.
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DR   EMBL; JARH01000960; EXF74683.1; -; Genomic_DNA.
DR   RefSeq; XP_007601700.1; XM_007601638.1.
DR   STRING; 1445577.A0A010RQY8; -.
DR   KEGG; cfj:CFIO01_08753; -.
DR   eggNOG; KOG0929; Eukaryota.
DR   HOGENOM; CLU_001772_0_0_1; -.
DR   OrthoDB; 1369677at2759; -.
DR   Proteomes; UP000020467; 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; 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; SM00222; Sec7; 1.
DR   SUPFAM; SSF50729; PH domain-like; 1.
DR   SUPFAM; SSF48425; Sec7 domain; 1.
DR   PROSITE; PS50190; SEC7; 1.
PE   4: Predicted;
KW   Reference proteome {ECO:0000313|Proteomes:UP000020467}.
FT   DOMAIN          843..998
FT                   /note="SEC7"
FT                   /evidence="ECO:0000259|PROSITE:PS50190"
FT   REGION          1..133
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          147..262
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          321..826
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1027..1051
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1118..1169
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1303..1326
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1429..1479
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        45..60
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        61..80
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        111..128
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        164..179
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        212..227
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        234..262
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        333..354
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        391..411
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        420..435
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        482..523
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        572..586
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        631..646
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        675..698
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        742..769
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        791..826
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1140..1169
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1429..1474
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1613 AA;  175475 MW;  C41E706B875C16BB CRC64;
     MYADTPKRSS RRRPDLNINT SPPPAAYSNR PAAAVASRGE PTAAPAVPQT PPPSNRNRPP
     PPTSSSSVAK GKSNSSRALR GPALSRHADD SFLVDTPDSP DSFDMSSNKE NDNPDQSRPR
     DSHDLSLSPR NVTRDSLMAN MLMSLDQFSM GGPVGGPFGS SPPNMHDEPS QQYQYDTDGD
     GFSRSVRGGR PGHTYSYSSD FDADDASRIS SRGRRSNSSS NFQPGLHRIS SMREPLRSTA
     NSQRHMHSRG GKGSTKSSSS NSIDAGYAQV LSSTRWASGF GGRSSSFDYG HRPPALQATQ
     HQAQANGAPW HIEFSNTFFT DDYDAAPTPT VPGGPRRMIP PMTPPAPTIP QPPMAASTPA
     AAHAPSTVAV EPAEPPPIVL ERKRSSRSAK STSTSRRADN NNKTSTPREE VPPMPSSVPA
     SSAAPTSSPA TAPVTAFESE SAPAPHVGYG KTKEPVHAAP IPTQAPSQQT KEKPGFFRRV
     FGSSRSNASN NPPETQNSTG ITSSTSVDSV DQRSGNRSLH VANQMKPSAP APPSRDTSSS
     HSHHHVLQKK PSSFFRRRKK SVSADEVPPV PVAATLEPPM PPLVAPIQLP ITKDKLSAKP
     EPSPISSLRR VMNPYLKGSP VTPNTPLTPQ SAPVQPAYSE MTSDPAPASN GERAEEQPRS
     FSPEYDPSPN ARIREVRSGS RDDDDDYHPE HGRRTDTPTR PPPEPPISSE KRNNSFLDID
     GSDNEADTES RRGKIKKDRS HKSGKTSKEP SPSRKGTSDQ KDDTIRGRKN NRLAVAPADS
     DDEGNKSTLI LPMEGTRSAS RASGSTTTEY KSAMSGTPSV RVETTENSPK VLGTFEAMST
     KPLDEPDFIV GDPTEDDRQK AQKIYDGNED FIQKEKAAAW MGEEGPVRQR TLQAYMELYD
     FADKSILQSL RLICERLVFR AETQQVDRIL VAFSKRWCDC NTNHGFKASD VIHTICYSIM
     LLNTDLHLAD IEHKMTRSQF VKNTMTTITQ AVIEAAPDAF ERPTILPGKS NSALGGDDSR
     PSIEERFVSR RLSFRPPPRN EGDGSGDHCH DECGPLVKSP FDGSMRAWES QVEVVLKDIY
     ASIRDERLPL FGADPSKNLA PNTQSGLSVI GMLKRTPSVL SKAPSESQAS MRGRIAENGR
     ANSSRWNSKS RSRPRMGNPG FSSSRTSFED GNSIWSPTVS SATWSKLSLG RTQTSMSVDS
     LSSSFRGGDY QQSIGFANAL SQAVIRDDES CLGKEPSIMS DELKPAQLLD DESLELAGPP
     WVKEGMVIHK HHLDGIEKKA KDRHWNEVFA VIQRGQMSIF SFGTNKTGRK GRGRNATKGP
     AIVGGGNWQE NATNLGTFSL RQTLASTLPP PGYSRARPHV WALSLPTGAV HLFQVGTPEI
     SKEFVTTANY WSARLSTHPL VGGISNIEYG WSDAIINNAL VTAINEQTVG PATGRQRSNS
     RPGSSAAGNP RPSMSSFRSA ASLDHGSGGP YSSASRGNKL PGDRIHVAEW APPTQSMRPS
     NLPEEEQLES LLAYVKGIED ELQTHNQLRS PMLLAFTPRG NNAVRAMANW ERKSAYLLRE
     IVKFRTYVDC LQQAEARKTE IYGERDLARR AARGELDEGE IEFDVERDTP IRT
//
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