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
//