ID A0A2S4PZ41_9PEZI Unreviewed; 1462 AA.
AC A0A2S4PZ41;
DT 18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT 18-JUL-2018, sequence version 1.
DT 27-MAR-2024, entry version 24.
DE RecName: Full=SH3 domain-containing protein {ECO:0008006|Google:ProtNLM};
GN ORFNames=EPUL_001784 {ECO:0000313|EMBL:POS87303.1};
OS Erysiphe pulchra.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC Erysiphales; Erysiphaceae; Erysiphe.
OX NCBI_TaxID=225359 {ECO:0000313|EMBL:POS87303.1, ECO:0000313|Proteomes:UP000237438};
RN [1] {ECO:0000313|EMBL:POS87303.1, ECO:0000313|Proteomes:UP000237438}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Cflorida {ECO:0000313|EMBL:POS87303.1};
RA Wadl P.A., Mack B.M., Moore G., Beltz S.B.;
RT "Development of genomic resources for the powdery mildew, Erysiphe
RT pulchra.";
RL Submitted (OCT-2017) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the DOCK family. {ECO:0000256|PROSITE-
CC ProRule:PRU00983}.
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:POS87303.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; PEDP01000152; POS87303.1; -; Genomic_DNA.
DR STRING; 225359.A0A2S4PZ41; -.
DR OrthoDB; 8258at2759; -.
DR Proteomes; UP000237438; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR GO; GO:0005085; F:guanyl-nucleotide exchange factor activity; IEA:InterPro.
DR GO; GO:0007264; P:small GTPase mediated signal transduction; IEA:InterPro.
DR CDD; cd08679; C2_DOCK180_related; 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; IPR016024; ARM-type_fold.
DR InterPro; IPR027007; C2_DOCK-type_domain.
DR InterPro; IPR035892; C2_domain_sf.
DR InterPro; IPR026791; DOCK.
DR InterPro; IPR032376; DOCK_N.
DR InterPro; IPR042455; DOCK_N_sub1.
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; PF14429; DOCK-C2; 1.
DR Pfam; PF16172; DOCK_N; 1.
DR SMART; SM00326; SH3; 1.
DR SUPFAM; SSF48371; ARM repeat; 1.
DR SUPFAM; SSF50044; SH3-domain; 1.
DR PROSITE; PS51650; C2_DOCK; 1.
DR PROSITE; PS50002; SH3; 1.
PE 3: Inferred from homology;
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW Reference proteome {ECO:0000313|Proteomes:UP000237438};
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 597..783
FT /note="C2 DOCK-type"
FT /evidence="ECO:0000259|PROSITE:PS51650"
FT REGION 453..491
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 457..473
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 474..491
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1462 AA; 165745 MW; 1D5F7A67615D822D CRC64;
MPWLPLPQIA YAVATYPFSA QDPADLPLEL GDELYLIEQG GKDGEWYRGY LLAPPSLLVG
LTTSSGQTLE ARVFSGIFPR SCVEVREILG DDDSEELELK LLSLDMDGDI FTGDDLIQEI
KPLTLTKSKS NLRCKDSPKR KTWKQNSINN KHLSRLKIRD PILPKPPAPV PMLKIGDETP
TCVEQPLVDE IASCLREWHS THLHRLLLAE EYQSLNQMAR LVRSLDAARK QLLYGSLTKH
ELAKLQEKVV WDLVRGNKMF ADEVIVRDPS ERGRIMTADD SIIDVTQLQS IMSLLDEKPQ
LNIQERPKFH HLLVEVKNFV GTSTENTTLV IFLASKAMDK AYEVLSENYI VEVPPTIALA
SLAKTEVLRT LFVDLTGADI GELSTAENDL YLVVKVQSRQ RISENRSKER RFSRDGPPYE
RLVPQTASTI GKAGLKSLIW AGKVQRNTFS RHLHSTPKSL RTSDFRRSLT HSRDGSLKSF
QTTNTNTDGA SRSAFKTTRI GAFKINDIIN KQGECEIVMN MWAPVPEYRE TLVENLEEVV
QESNNFENSE RTERLQLNIK TFNFLDSEAL ITAKPTLLSN VVVTKKMGFS DAPTKPRSDI
YITIDEAFLP RKSLLGRAVG NPGGVVPLSQ NISGLNLQVT LEVRNLKGER LEGCIFPSSN
CEPQSSWEST VVGRGDSWKQ TLRLAIPESE VPNSHLFMVL TDVPYDPFAV CYLPLWDEQA
FLRNDQYSLL LYGYDENKKI TKRSENKVGY ISHPWDSKGK FRFGRNEVRA GSIATLRIQT
YLCSTTFLQN KILLDLLKWK ELPQTQVQEL LKQLVFVPEI EIVKMLNDVF NAIFGILVDQ
AGNNDCEDLV FSALITVLGI IYDRRFNIGP LVDQYAENNF YFPLAMPCLA RSLTRLLAKP
SDPDTSRQLR ATFKVVKYIL KFITRAKEQQ KEMEAAGTVG TTTTTSLTRN LRSIFKALDA
MMRSEAPVLI GSKTLAVQHF HTWLPALLGL LNREEIVHVA IDFMDSCSAV KGKLILYKLI
LIINYSKLDI FSEKEQRKAL CMNTVRWIEP LWEKTDEVEG QWRDQLRLCC SVVASQVQDL
VNEIPDYIPK IINSFSQILK TGSSLLSSEN NSKFSLLFPT TYPFPSKSIL RPSNFDEVLV
ELSAVLSAIS MQPAGIQLEL AADEMAKILQ DTLNVHLSIL NCEAFPASWL SVHVYHHRST
MKTLEYIGGI LLDSFIPDPD DAEQYNTELW KIFFTVLLKV IGSDILALET FPEQKRRAVW
KIAGDIRETG AELMQMTWDA NGWETTVEEK FRYGLSKVGG YQVQYVPYII GPIIELCLSV
HEGVRKVAVD VLRTIIVSEW NLSEDISIIQ TEIIDCLDRI FRSKRITESI VQKLFIVELE
QLFAPLSKHH GDPLYIATRE LITKTSEFLD LLVAVHSSET VSDATHLINY LRLIEFLRGM
QKEEILMSYI HKLAQLQSIR IY
//
