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Database: UniProt
Entry: A0A371DTZ9_9APHY
LinkDB: A0A371DTZ9_9APHY
Original site: A0A371DTZ9_9APHY 
ID   A0A371DTZ9_9APHY        Unreviewed;      1441 AA.
AC   A0A371DTZ9;
DT   07-NOV-2018, integrated into UniProtKB/TrEMBL.
DT   07-NOV-2018, sequence version 1.
DT   27-MAR-2024, entry version 15.
DE   RecName: Full=SEC7 domain-containing protein {ECO:0008006|Google:ProtNLM};
GN   ORFNames=OH76DRAFT_1477666 {ECO:0000313|EMBL:RDX55975.1};
OS   Polyporus brumalis.
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC   Polyporales; Polyporaceae; Polyporus.
OX   NCBI_TaxID=139420 {ECO:0000313|EMBL:RDX55975.1, ECO:0000313|Proteomes:UP000256964};
RN   [1] {ECO:0000313|EMBL:RDX55975.1, ECO:0000313|Proteomes:UP000256964}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BRFM 1820 {ECO:0000313|EMBL:RDX55975.1,
RC   ECO:0000313|Proteomes:UP000256964};
RX   PubMed=30061923; DOI=10.1186/s13068-018-1198-5;
RA   Miyauchi S., Rancon A., Drula E., Hage H., Chaduli D., Favel A., Grisel S.,
RA   Henrissat B., Herpoel-Gimbert I., Ruiz-Duenas F.J., Chevret D., Hainaut M.,
RA   Lin J., Wang M., Pangilinan J., Lipzen A., Lesage-Meessen L., Navarro D.,
RA   Riley R., Grigoriev I.V., Zhou S., Raouche S., Rosso M.N.;
RT   "Integrative visual omics of the white-rot fungus Polyporus brumalis
RT   exposes the biotechnological potential of its oxidative enzymes for
RT   delignifying raw plant biomass.";
RL   Biotechnol. Biofuels 11:201-201(2018).
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DR   EMBL; KZ857381; RDX55975.1; -; Genomic_DNA.
DR   STRING; 139420.A0A371DTZ9; -.
DR   Proteomes; UP000256964; 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; IPR041681; PH_9.
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; PF15410; PH_9; 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   Reference proteome {ECO:0000313|Proteomes:UP000256964}.
FT   DOMAIN          533..667
FT                   /note="SEC7"
FT                   /evidence="ECO:0000259|PROSITE:PS50190"
FT   DOMAIN          818..943
FT                   /note="PH"
FT                   /evidence="ECO:0000259|PROSITE:PS50003"
FT   REGION          1..34
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          92..182
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          242..523
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1002..1043
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1204..1353
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1394..1441
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        95..109
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        113..127
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        132..146
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        147..182
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        317..342
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        358..380
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        403..427
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        428..452
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        453..509
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1009..1043
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1204..1236
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1241..1349
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1407..1431
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1441 AA;  157414 MW;  7AB9E3835C1DE568 CRC64;
     MVALFGLSTK GSPARTTRNP DIATAPPPYS QDHSDPAVYA TATTTTTAHI VTTTTETTTH
     FFSLPLWRRR GTPAHAPRIT AAMSTDELGV MHTDSGQALS PSSLHSRDKD LPPTPNASPP
     SLTPPNRLSP DPHSLHESDD TTRQARIQAE SRSAVASVAS SRASSLQPCS RSSFALGESP
     NASQPTVVLA RAALGLGLPH GVPGVSASSS SLEVNTVSLF PPQSPITSRA QPRSLSIRHA
     KSFHREPGSA ADDPPPSAIR ERRRTRGLSL GPLSLMSSDI KGKQRETDND VIISDQKPLT
     RKSSFWSRKR VHSRPEPALA PPSPTPQPTL PAFPPVSPFN MNTPVPSPGL SANYPPDLQR
     RHSERSRKQS SPRKDDARQS PDQSPPVPTA SIHMRRRRGS QRPQTADSGT SPRLSFFAES
     RPFMTSPTSS PLPTPQEQPV LLPPPPHSEP RTRAQTNPPL LHRLSVNLFG GSSSNSQTPT
     STSSPNILDG QGLTSPPSSL GSSRPSLSKP SVDIPKPRAD EESPEVYLQR LVEAVSKTEV
     ATVLASSADA FHARALHIYI ERFNFVGDPL DVALRKLLME VGLPRETQQI DRVIEAFAAR
     YVQCNPNLFA SDDHPYILAF SLIMLHTDAF NKSNKRKMTK PDYIKNTRLP GVAPEVLDCF
     YDNIVFAPFI FIEDPLDVNG QRGLVPEAIS RRMSTINAPS PGALNGSGST LLGKSNKIDP
     YYLITRNLLD ELRVDVRALV PAESPYFYQG TAGPWNEDEL QRAFALACMV EVVGLENRYL
     ASPWFGMTVA GGPGPMFQSS LGSLPPLPPA SGGVFVVKVS KVGLLLRKED IIEGGRRALS
     RKWREWCVLL TGSQLLFFRD TTWASTIQAQ AQRTNGQVLP QTSLPQPDEM LSVRDTIAVF
     DKSYTKYANT LRLVMPDGRQ FLLQAQDERE MNEWIARINY ASAFKTAGVR MRSLGLSSRD
     IELTGMAAAA SHLKDVKHNL VQTPSPLVRT WNGRMSEDLD ILSRGAGDSE PTLPSNASAE
     GSRARHSTNV SISSDPTTPP YENSSRLFKA TFDEVKTELA TAKWRSLDEM SIRSSRKRAY
     SLESVLGSPG FSPTGRSSGD VKPRLSSRPE IIKSKVEDLK AKIALARTQL DTDMRFVRNL
     AVLTPFQRAT RDRVQAAVQN VAKRVMQVRL DMEKLVCHHD VLTADLAAEE RDWQRTKRLA
     MRAATEKLAS QREHDRAVER EAERVEEAER ERLPKLTLSA YVDQTEPQSI SSPVTIPRTG
     RSAHSGGPDS SMAASFQSAG SGTSSAWHSR QRSATVTVSS PHSSTTSPVE RGSYTASDNS
     LLDSPERQRA TPLAAQNSMD STTTTDEGGA HEKFYTAPEM AEEQAEEWNK TRAAKRVSLV
     KLPSDLRMSI LFGKHAREEV STPELPEDTA ATPTSTSSPP RRSSLSPYDK QPGATVTMLD
     L
//
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