ID A0A2S4PVF2_9PEZI Unreviewed; 724 AA.
AC A0A2S4PVF2;
DT 18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT 18-JUL-2018, sequence version 1.
DT 27-MAR-2024, entry version 20.
DE RecName: Full=ELMO domain-containing protein {ECO:0000259|PROSITE:PS51335};
GN ORFNames=EPUL_002761 {ECO:0000313|EMBL:POS86006.1};
OS Erysiphe pulchra.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC Erysiphales; Erysiphaceae; Erysiphe.
OX NCBI_TaxID=225359 {ECO:0000313|EMBL:POS86006.1, ECO:0000313|Proteomes:UP000237438};
RN [1] {ECO:0000313|EMBL:POS86006.1, ECO:0000313|Proteomes:UP000237438}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Cflorida {ECO:0000313|EMBL:POS86006.1};
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 -!- FUNCTION: Involved in cytoskeletal rearrangements required for
CC phagocytosis of apoptotic cells and cell motility. Acts in association
CC with DOCK1 and CRK. Was initially proposed to be required in complex
CC with DOCK1 to activate Rac Rho small GTPases. May enhance the guanine
CC nucleotide exchange factor (GEF) activity of DOCK1.
CC {ECO:0000256|ARBA:ARBA00024863}.
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:POS86006.1}.
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DR EMBL; PEDP01000434; POS86006.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2S4PVF2; -.
DR STRING; 225359.A0A2S4PVF2; -.
DR OrthoDB; 1473500at2759; -.
DR Proteomes; UP000237438; Unassembled WGS sequence.
DR GO; GO:0017124; F:SH3 domain binding; IEA:UniProtKB-KW.
DR GO; GO:0006915; P:apoptotic process; IEA:UniProtKB-KW.
DR Gene3D; 1.25.10.10; Leucine-rich Repeat Variant; 1.
DR Gene3D; 2.30.29.30; Pleckstrin-homology domain (PH domain)/Phosphotyrosine-binding domain (PTB); 1.
DR InterPro; IPR011989; ARM-like.
DR InterPro; IPR016024; ARM-type_fold.
DR InterPro; IPR024574; ELMO_ARM.
DR InterPro; IPR006816; ELMO_dom.
DR InterPro; IPR011993; PH-like_dom_sf.
DR InterPro; IPR001849; PH_domain.
DR PANTHER; PTHR12771:SF56; CED-12; 1.
DR PANTHER; PTHR12771; ENGULFMENT AND CELL MOTILITY; 1.
DR Pfam; PF11841; ELMO_ARM; 1.
DR Pfam; PF04727; ELMO_CED12; 1.
DR Pfam; PF16457; PH_12; 1.
DR SUPFAM; SSF48371; ARM repeat; 1.
DR PROSITE; PS51335; ELMO; 1.
PE 4: Predicted;
KW Apoptosis {ECO:0000256|ARBA:ARBA00022703};
KW Phagocytosis {ECO:0000256|ARBA:ARBA00022907};
KW Reference proteome {ECO:0000313|Proteomes:UP000237438};
KW SH3-binding {ECO:0000256|ARBA:ARBA00023036}.
FT DOMAIN 257..445
FT /note="ELMO"
FT /evidence="ECO:0000259|PROSITE:PS51335"
FT REGION 274..301
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 590..610
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 286..300
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 724 AA; 81970 MW; E534083C9839A00E CRC64;
MNQADIPELL TRLQSNEDST RKLAVFKLQA SINDPSIADV FISTGGLKIL RQLIMTASGN
TLAYALAALS RLLEVEMGWE IFESNGAEAL VERLVGLIVT HPLVNILRGA MSILVAVVSH
SQNSRESSKV PGVFGFRALK PAVAVYPQFF EMVVSQLKSA DHLLCSSALM LLNALLRDGL
SRVEPKEKNS GELSKAGEKW PQLINKLQDL GIVQAAYDLM QSSSLQDMTH SLLEFQAVSK
LILKKRRDTE VQLENSEHVG ILERIYISSQ KKSKNEAQSK IKQTENSSTD GKKKINKENP
DKWTNLGFQT ENLSWDFEQT GFLGLMDLAY FVAKDEDGFQ KLLQEQETRP FNERCPIARA
SLSVTRTLYD HFEIDRSDLE DIKNYRALDG MKNYADFFRP FILQWSRIHR KALSSFIILW
KQVGAEQEEF GKVVELLRIL VDKVLSGVAR TKDIKEIEEE IAGFDYRQLR KIQMEILNNA
FEDEWELHLT QIREELRNEA LQFMKEQRIR SLLNGAWFHR TETNSSIPES PNETTYSAAW
QYVKLSYDKR YLHYGDFDSQ AIKNPPLDIL SQKIDLENIS SVDSNTSLCG NEDSSAYTPT
TTVTARPSED PSTITGITIR CFDTIQNGDQ CNLDTSNGSI PEKIVLVLVP INKNLASSWL
DGLLMLLNQA PITSETSKLV NFICDYGLKI RLLNVRMDDF LDPLDGAGII PSREGLDDDY
FYEM
//