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Database: UniProt
Entry: A0A2B7XMT0_9EURO
LinkDB: A0A2B7XMT0_9EURO
Original site: A0A2B7XMT0_9EURO 
ID   A0A2B7XMT0_9EURO        Unreviewed;      1434 AA.
AC   A0A2B7XMT0;
DT   20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT   20-DEC-2017, sequence version 1.
DT   27-MAR-2024, entry version 21.
DE   RecName: Full=SEC7 domain-containing protein {ECO:0008006|Google:ProtNLM};
GN   ORFNames=AJ80_06456 {ECO:0000313|EMBL:PGH13084.1};
OS   Polytolypa hystricis UAMH7299.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Onygenales; Onygenales incertae sedis; Polytolypa.
OX   NCBI_TaxID=1447883 {ECO:0000313|EMBL:PGH13084.1, ECO:0000313|Proteomes:UP000224634};
RN   [1] {ECO:0000313|EMBL:PGH13084.1, ECO:0000313|Proteomes:UP000224634}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=UAMH7299 {ECO:0000313|EMBL:PGH13084.1,
RC   ECO:0000313|Proteomes:UP000224634};
RA   Munoz J.F., Mcewen J.G., Clay O.K., Cuomo C.A.;
RT   "Comparative genomics in systemic dimorphic fungi from Ajellomycetaceae.";
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:PGH13084.1}.
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DR   EMBL; PDNA01000108; PGH13084.1; -; Genomic_DNA.
DR   STRING; 1447883.A0A2B7XMT0; -.
DR   OrthoDB; 4248238at2759; -.
DR   Proteomes; UP000224634; 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; 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:UP000224634};
KW   Transferase {ECO:0000256|ARBA:ARBA00022676}.
FT   DOMAIN          425..609
FT                   /note="SEC7"
FT                   /evidence="ECO:0000259|PROSITE:PS50190"
FT   DOMAIN          734..862
FT                   /note="PH"
FT                   /evidence="ECO:0000259|PROSITE:PS50003"
FT   REGION          1..261
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          274..402
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          881..904
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1069..1149
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1166..1249
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1266..1344
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1356..1434
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          923..950
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COMPBIAS        13..27
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        44..92
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        116..130
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        162..193
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        200..261
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        303..402
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        883..900
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1083..1149
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1180..1202
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1203..1223
FT                   /note="Basic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1276..1291
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1300..1344
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1360..1378
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1379..1409
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1410..1434
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1434 AA;  157524 MW;  7EE2C6604A1734BB CRC64;
     MPWKGWKHSE SGGNNAPGRN TPNAEAPTRH SEHVPRSLHP EDYSVSRLSE STTDLPLAGD
     SQAAAQTHAG DNPNETGRNS DHTSNQQTAR RKRFSMMRFR HASDPQLSAS FNQSKPPPVP
     AVPPPPTIIT TAPTLTNLDP PTKRKNPFKI SPKKSILSHG RANTREHTPS NTSPSHTPSA
     SIKSATAPQT MRASHISFEE PGRLSTTSLR SAGPRGSGDT SNQSGPVSGA RLSESSRSDA
     SSGENPLYRV GSRNGNSSSH SFFRIPRLRK NHSPLFPLPP ELHPSGSSSA HVSPVDKPSY
     PGSGKQALSN DPSREQLSPF HSPSQSSVGQ MTPATTSTTQ GLFRKDSVTS AHSARSSLSL
     TARTGRRGRS STMGSLADIQ DDPHQSSPDL VPSSRTSTTT TARKSFSDLF GFTHRMRQDS
     EPPVPGNGSS IFGAPITPAS ITSKPNSLSI ARELASFPAR EEGDTPATYL SQLENTVRRG
     AIATILSQSA EEFYAISLRR YMRTFAFFGD PIDMAIRKLL MEAELPKETQ QIDRVIQGFA
     DRYHECNPGI FSSPDQAYFI AFSLLILHTD VYNRNNKRKM QKQDYVRNTR GEGVDNEILE
     CLYENICYTP FIHVEDELNF SKQLHAPKPR RPLFRVPSTD HLPRVAKEPV DPYTLILDGK
     LNSLRPNLKD VMDTEDVYSL GELANSPDMN ALHTMFYKSC ILQIVSARSR PDAFLTQSSI
     ANPAEAQPGL VDIRVAKVGL LWRKEPQRKK TRSPWQEWGA ILTGSQLYLF RDIQWVKSLI
     SQCDKNQKNG RRHGVTFKPP LTDFKPDAVM STDEAVALLD SSYKKHKHAF LFVRHGGLEE
     VFLANSETEM HDWMTTLNYT SAFRTTGVRM RGMIGANYEG RRTTRADSVT SETSIPPDSA
     ALAASGSRRL DPVLVEEVSA ARRELMSRRI EEADEKVKSS QKELDDFLRN IRHLQILTPI
     HHRARDQVIL AAGRMSARVK WARLDMWRTK CYRQVLSLDL ANEERLMSSS SNKLRPTIST
     TRANEHDQAN SSAAAIPASP MSEYSFHTAP RPATPVSIGQ ASSVDQAIYQ TPPRPERGGV
     RNSLSPSEHS TPARKSSIAG SKPESTLQSP NRPTVGSLTR EASVTSSQGR VLDSSSGFLS
     SNHSTPTPSF IEAAEDHFNR ETGVLEEEYS SQAYDSVEPV TGAEKDKMQD APAEAGSSER
     RSKVRRSFHR SLREGPHHHR SKKGKDQAGA DDGSSKTGNE GLARAKGSFT VHGKKASVIT
     FGSEWQNISP EQRLKLRKSV QTEDSRVSDM LGPDDGTESL LSAASGTGKR THSLRSTSTT
     TAMSQRRFST PAVGMESGNG DQPTNNIVEL VVEEGPETTD IAPTQLSTTT TSTQQTLKPD
     EILEEETESI TNENDRSPTR QDETSVDEKS TTSLAHTMSR ENLNRASPEQ AVSA
//
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