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Database: UniProt
Entry: A0A395GYJ8_9EURO
LinkDB: A0A395GYJ8_9EURO
Original site: A0A395GYJ8_9EURO 
ID   A0A395GYJ8_9EURO        Unreviewed;      2119 AA.
AC   A0A395GYJ8;
DT   05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT   05-DEC-2018, sequence version 1.
DT   27-MAR-2024, entry version 23.
DE   SubName: Full=SH3 and Ded_cyto domain protein {ECO:0000313|EMBL:RAL00403.1};
GN   ORFNames=BO80DRAFT_96988 {ECO:0000313|EMBL:RAL00403.1};
OS   Aspergillus ibericus CBS 121593.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
OX   NCBI_TaxID=1448316 {ECO:0000313|EMBL:RAL00403.1, ECO:0000313|Proteomes:UP000249402};
RN   [1] {ECO:0000313|EMBL:RAL00403.1, ECO:0000313|Proteomes:UP000249402}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CBS 121593 {ECO:0000313|EMBL:RAL00403.1,
RC   ECO:0000313|Proteomes:UP000249402};
RG   DOE Joint Genome Institute;
RA   Vesth T.C., Nybo J., Theobald S., Brandl J., Frisvad J.C., Nielsen K.F.,
RA   Lyhne E.K., Kogle M.E., Kuo A., Riley R., Clum A., Nolan M., Lipzen A.,
RA   Salamov A., Henrissat B., Wiebenga A., De vries R.P., Grigoriev I.V.,
RA   Mortensen U.H., Andersen M.R., Baker S.E.;
RT   "The genomes of Aspergillus section Nigri reveals drivers in fungal
RT   speciation.";
RL   Submitted (FEB-2018) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the DOCK family. {ECO:0000256|PROSITE-
CC       ProRule:PRU00983}.
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DR   EMBL; KZ824440; RAL00403.1; -; Genomic_DNA.
DR   STRING; 1448316.A0A395GYJ8; -.
DR   VEuPathDB; FungiDB:BO80DRAFT_96988; -.
DR   OrthoDB; 8258at2759; -.
DR   Proteomes; UP000249402; Unassembled WGS sequence.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR   GO; GO:0005085; F:guanyl-nucleotide exchange factor activity; IEA:UniProtKB-KW.
DR   GO; GO:0007264; P:small GTPase mediated signal transduction; IEA:InterPro.
DR   CDD; cd08679; C2_DOCK180_related; 1.
DR   CDD; cd11684; DHR2_DOCK; 1.
DR   Gene3D; 1.25.40.410; -; 1.
DR   Gene3D; 2.60.40.150; C2 domain; 1.
DR   Gene3D; 1.20.1270.350; Dedicator of cytokinesis N-terminal subdomain; 1.
DR   Gene3D; 2.30.30.40; SH3 Domains; 1.
DR   InterPro; IPR027007; C2_DOCK-type_domain.
DR   InterPro; IPR035892; C2_domain_sf.
DR   InterPro; IPR026791; DOCK.
DR   InterPro; IPR043161; DOCK_C_lobe_A.
DR   InterPro; IPR032376; DOCK_N.
DR   InterPro; IPR042455; DOCK_N_sub1.
DR   InterPro; IPR027357; DOCKER_dom.
DR   InterPro; IPR046769; DOCKER_Lobe_A.
DR   InterPro; IPR036028; SH3-like_dom_sf.
DR   InterPro; IPR001452; SH3_domain.
DR   PANTHER; PTHR45653; DEDICATOR OF CYTOKINESIS; 1.
DR   PANTHER; PTHR45653:SF10; MYOBLAST CITY, ISOFORM B; 1.
DR   Pfam; PF06920; DHR-2_Lobe_A; 1.
DR   Pfam; PF14429; DOCK-C2; 1.
DR   Pfam; PF16172; DOCK_N; 1.
DR   SMART; SM00326; SH3; 1.
DR   SUPFAM; SSF50044; SH3-domain; 1.
DR   PROSITE; PS51650; C2_DOCK; 1.
DR   PROSITE; PS51651; DOCKER; 1.
DR   PROSITE; PS50002; SH3; 1.
PE   3: Inferred from homology;
KW   Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW   Guanine-nucleotide releasing factor {ECO:0000256|ARBA:ARBA00022658};
KW   Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW   Reference proteome {ECO:0000313|Proteomes:UP000249402};
KW   SH3 domain {ECO:0000256|ARBA:ARBA00022443, ECO:0000256|PROSITE-
KW   ProRule:PRU00192}.
FT   DOMAIN          7..88
FT                   /note="SH3"
FT                   /evidence="ECO:0000259|PROSITE:PS50002"
FT   DOMAIN          625..806
FT                   /note="C2 DOCK-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51650"
FT   DOMAIN          1449..1859
FT                   /note="DOCKER"
FT                   /evidence="ECO:0000259|PROSITE:PS51651"
FT   REGION          426..514
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1847..2088
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        427..514
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1905..1950
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1951..1969
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1970..1984
FT                   /note="Basic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        2005..2023
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        2024..2085
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   2119 AA;  236539 MW;  AF7F8342CDF7927A CRC64;
     MPWRPLPRIA FAVAIYPFQP TTPADLPLEL GDELYIIEQG GANGEWYRGY LVAPPSLLAG
     LTSTKGQTLE ARVFSGIFPR NCVEIREVLG DGEKTITNGD RSSMALLAGA EGEMRNSVAS
     FQDDENAFGE VSNVVIAKKG KPSQIFIQKL DEDGRGSPAS PRTPRRDLLR TNSMVLAPMN
     VAPRDPDAPK PAAPVPMLKI GDETPTSLSE PLVDEIASCL REWHSTNLHQ LLLSRQYVTV
     EEMSKIVQEL DFARRQLLYN VLTAQEKESL RQEVVWKLVR GNKALGGEII VRDPQQRGRL
     LTGDDSAVEL TRLQSEMGML DSSPTQQSDV AALHHLLLEV NAVSGHAPGP VTLAAYLCSQ
     SETGALVPLS ETYVLDIPSP EKFASMGQSA RLKTLFTDLS STDIGDSSTN GPKLYLIVAV
     RAPETASVTN AAAQPRSSIS RDSSSGSKQA TGVNQSVKGS LRTRRSMMWT SKPRGIQSPE
     QAKETSKNPP QSSGSSTSTI TKERSGSQST KDTTQIRTVG VGFLEVSQIL RQEKDAEQVI
     NIWSPSEESE DKEGRDDGFD GVVRTLLPSP TGKYVRSQRA ARLHFHLYPH VDPDADSLVR
     RNPTTLHNVI QTRRIGFSQA PTKPRSDIYV TISHATFPPE ALLSHPHSGQ VPVPAHTGLR
     NLQLTLEVRT SSGTRVERCV IPSSNHAAQT AWRTTIADRG APWNQTIRLN IPTDQIPTSH
     LIMSIADAPE FPFALAWMPL WDNQAFMRDG PHSLLLHAYD KCTSNIENGK GAYLSLPWSS
     LGKNESAKDE AITGPLATLR LDTHLCSTEY SQDQVILSLL NWRDRPVNEV LDTLKRVLFV
     PEIEIVKQLS SVLDSLFGIL VENAGNEEYE DLIFNNLVTV LGIVHDRRFN LGPLVDHYAD
     NQFNFPFATP CLVRSYLRLL PSSSDAQQSR NLRATFKVGR HVLKFIINAR QQQKAKEEGI
     GITRVQSTFN RDLHTIFKSL EALMKNPSPA MVGSKTLVVQ HFHTWLPELS KVLSRDEVIM
     IALSFIDSCK DVTGMLILYK LVLIQHYTRL EIFSSGSERK SLISSCISWL APYWGATGAV
     SDLYRDQVRL CCAIVAELLK QPDPYLYEFV PKIVSSYYSI IPDGVEETSY LSLLFSKSFP
     FQVKTSKYSQ RFDEALVELS AILAGAATIP NPKRPRLKGL ELSSFLSQAF EVHTSILNCE
     AYPESWLSVH VYNHRATVKS LEYLATILTN KFLPSPEEAE SFDTRLWETF FMTLLKVVSS
     DALALETYPE QKRRAIWKIA GDVREQGADL LHSSWESIGW ETTDEEREHY GLSKLGGYQV
     QYVPGLVAPI IELCLSVHEG LRHVAVDILR TMILSEWGLN QDLSIIETEV ISSLDNLFKR
     KNMSESVVQK LFIGELSEHF EGYAEFDEDL SNAVKALIAT VDELLDLFVA SQGGSMAESL
     HTLRLMKYMK DMGREDIFIR YVHELAQVQA AAGNFTEAGM ALQFHADLYD WDAQRTLPEL
     LNPAFPEQTS FERKESLYFA VIQYFEDAKA WAHALLCYKE LAQQYEDTVV DFAKLSRAHG
     SMAKIYDIIA KEDKQFPRYF RVLYKGLGFP TTLRDKEFII ECAATERMAT FIDRMQREHP
     AAQVVSSGEI QDYEGQFLHI NPVSVHRDVD HPVYQRSKIP QSVRDHLLVS EPCHFSSTLR
     RHVRDADVKA QWVEKTVYTT AEPFPNILRR SEVVEVKEVA LSPLQTALER TWRKTQELSM
     LQRRAASGED MSLNNLTEAL EQLLELNAAT PNCVAAYRQF LSDVPEEDEG GLVTPKPADP
     LKNALAVALI DHALAIKQAL AMYHRPAHQA TQAELMRRFE EAFGPEISSL RPAELETPQW
     PRRTTPKSLE ERQKQPASRA LSPEQELIRS SRKNHSRKHS AKQSVSHRIS VMNPFKRTNH
     VASNSVATVQ EAPKGSADSK VNGTTTEEHV NGEAADQDDA ATIHSRTTTR SRDTHHRRRS
     RLGDVLHKHA SSLSISPSAT EESQSQKKQR TRSASRDTAA KSHESMSRTT SHTNGTSTDD
     RPSVTSPKGG WSTIPSISDY PRPVTRSSMT SIRSPEITSP VSHTPGRRDS VLKRFSLLKG
     VSRKGSRLDF RTGTPVHEE
//
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