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Database: UniProt
Entry: A0A369GWX4_9HYPO
LinkDB: A0A369GWX4_9HYPO
Original site: A0A369GWX4_9HYPO 
ID   A0A369GWX4_9HYPO        Unreviewed;      1398 AA.
AC   A0A369GWX4;
DT   07-NOV-2018, integrated into UniProtKB/TrEMBL.
DT   07-NOV-2018, sequence version 1.
DT   27-MAR-2024, entry version 16.
DE   RecName: Full=SEC7 domain-containing protein {ECO:0008006|Google:ProtNLM};
GN   ORFNames=CP533_6213 {ECO:0000313|EMBL:RDA89918.1};
OS   Ophiocordyceps camponoti-saundersi (nom. inval.).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Hypocreomycetidae; Hypocreales; Ophiocordycipitaceae; Ophiocordyceps.
OX   NCBI_TaxID=2039874 {ECO:0000313|EMBL:RDA89918.1, ECO:0000313|Proteomes:UP000253071};
RN   [1] {ECO:0000313|EMBL:RDA89918.1, ECO:0000313|Proteomes:UP000253071}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BCC 79314 {ECO:0000313|EMBL:RDA89918.1,
RC   ECO:0000313|Proteomes:UP000253071};
RA   Kobmoo N., Wichadakul D., Arnamnart N., Rodriguez De La Vega R.C.,
RA   Luangsa-Ard J.-J., Giraud T.;
RT   "A genome scan of diversifying selection in the zombie-ant fungus
RT   Ophiocordyceps unilateralis complex supports a role of enterotoxins in
RT   coevolution and host-specificity.";
RL   Submitted (OCT-2017) 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:RDA89918.1}.
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DR   EMBL; PDHQ01000238; RDA89918.1; -; Genomic_DNA.
DR   STRING; 2039874.A0A369GWX4; -.
DR   Proteomes; UP000253071; 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:UP000253071}.
FT   DOMAIN          434..595
FT                   /note="SEC7"
FT                   /evidence="ECO:0000259|PROSITE:PS50190"
FT   DOMAIN          722..851
FT                   /note="PH"
FT                   /evidence="ECO:0000259|PROSITE:PS50003"
FT   REGION          1..101
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          117..210
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          228..266
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          283..395
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          412..435
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          993..1196
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1219..1398
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          914..948
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COMPBIAS        10..24
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        32..46
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        47..77
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        165..191
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        228..265
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        285..319
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        343..375
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1016..1042
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1057..1103
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1106..1123
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1147..1169
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1319..1334
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1362..1383
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1398 AA;  153546 MW;  0AFEF062558E3FE2 CRC64;
     MPLLRRRGNI ASETDMRRHP PLAPRASHEN NTVPTADDRV RKSTRNGSRT DVPTPSVRPQ
     TQQRRRQTPT ALSEDTSPQP ADRGAESDPD NPAVPSLDPD TYKHRRFSIL RFRNASDPQL
     SLRARQQAEK PPPIPRPPAI VTTAPTNDIN GPRRVTSRMG LAAKFRRSSE VHRRDDGESG
     SRGRKQLREE SMPGGPRPSL MTLDGQSASS ATLPMVSASN GAALCLSDNR QSESSRSDAS
     SADRVSHASP TSTIKKSQPP KSQAPTAFSK LRRAMKPSDQ MFPMAHLPQK NSTTSTIGSA
     TSLGVGSTPR PSSARSASTP RGHADRCDDG SAAAPIAATV TARLNRGSDS RSNNSSPTRV
     NILRGRSSTM SSMGRDSTDE HMHPPTSRTS FSTGRKSFGD LFGLSRIRQN SELSRQGSLT
     PVTPGSITSK SNSLQLPRGS IVLPERRDDE SPAKYLARVE EVMGRGMIAS ALSKGTDPFL
     ATVLRSYMRK FSFFGDPMDM ALRKLLMEAV LPKETQQIDR CLQAFANRYH ECNPGIYSSP
     DQAYFIAFSL LILHTDVFNK NNKHKMQKAD YLKNTRGEGI FDDILECFYD NISYTPFIHV
     EDDIELGQER AFTNLSRKKP LSVANTGDPA KRAVKEPIDP YTLILDGNLD VLRPNLKDAM
     QLDDHYNYLG TAASLNLKDL QKTFFRTAVL QIVSARSRPD AFMTERTASN PKDAHPGIVD
     IKITKVGLLW RKETKKRKTR SPWQEWGAIL TGAQLYLFRN TSWVKNLMHQ YDNHIKAGHD
     GIPIIFKPPL EEFKPDALMS TQGAIALLDT TYKKHKNAFV YVRQGRLDEV LLADNEEERN
     DWLAKLNYAA AFRTSGVRMQ GVVGGHYDGI GRRGMRRLDS SDATQQVQTP TGTVSIARGR
     IDFKMAQDIQ TARREGIQQK VAEANGKVED AQRQLEDQLR NARHLQILAP IQPRTREQIL
     SAAARMAAQL EWTRIEIWKE KCHRDILVQD LAGDRPVSAS TESPTKSQPD VEPAPPRSKA
     EPKPGRVNAK EASSHHDEAP AEQKFQTPPP SAGRRPRGSQ DPSNPTSDGD SPRQGSIASF
     SSSPVLPVQS TTQTSQAVTR GEVGPNRSQD EVDAEERDFL RQTGLWDARP GTSYAEKTAE
     SSADGVDVGP DKGKIRRSLQ RTLRESAGHL SHHRGRKGKE VVGTGPCEDV PPDSMLTRGA
     GSFVVHGKKA SVINLGTELQ TLGQDEKTSA RKPAPVEEPA VVSPSTQSGG AEDDYHSAQE
     TASDSDGRRE STTSAGTATA RSFRELHRRY STAQAARSVS VGGRLTVRSD GESEAAVSFS
     DGPRQSGQRS SGTEAEESRN GRGVRPSQSQ TLRHEVREHD SDDDSDNDDD DDSDDDDDDD
     GPQESEHMSP RPVQAVNA
//
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