ID A0A427XX82_9TREE Unreviewed; 809 AA.
AC A0A427XX82;
DT 08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT 08-MAY-2019, sequence version 1.
DT 27-MAR-2024, entry version 16.
DE RecName: Full=ELMO domain-containing protein {ECO:0000259|PROSITE:PS51335};
GN ORFNames=EHS24_007013 {ECO:0000313|EMBL:RSH83335.1};
OS Apiotrichum porosum.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Tremellomycetes;
OC Trichosporonales; Trichosporonaceae; Apiotrichum.
OX NCBI_TaxID=105984 {ECO:0000313|EMBL:RSH83335.1, ECO:0000313|Proteomes:UP000279236};
RN [1] {ECO:0000313|EMBL:RSH83335.1, ECO:0000313|Proteomes:UP000279236}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 27194 {ECO:0000313|EMBL:RSH83335.1,
RC ECO:0000313|Proteomes:UP000279236};
RA Aliyu H., Gorte O., Ochsenreither K.;
RT "Genome sequence of Apiotrichum porosum DSM 27194.";
RL Submitted (NOV-2018) 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:RSH83335.1}.
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DR EMBL; RSCE01000004; RSH83335.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A427XX82; -.
DR STRING; 105984.A0A427XX82; -.
DR OrthoDB; 1473500at2759; -.
DR Proteomes; UP000279236; 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; 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; SSF50729; PH domain-like; 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:UP000279236};
KW SH3-binding {ECO:0000256|ARBA:ARBA00023036}.
FT DOMAIN 385..565
FT /note="ELMO"
FT /evidence="ECO:0000259|PROSITE:PS51335"
FT REGION 1..26
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 400..422
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 809 AA; 90300 MW; 9209DAC0E4F9C569 CRC64;
MVHTPSPSKR SQNSVSPSFQ SGKNENAVPT NLITYKGRRI PARIDPDASI LRVVEIMAKS
FGAPEHHITL ALRDENDNLV TQTNIGAKVS SKETLKLVAA PVTEALAVVA SLHAANDKPG
EAGDPIVLPN NAEVLPPKLA LFNLQKYIKE DDFAVEFMLK GGVKLLVDML EKEGTGALTG
NSLAYALQGI RGVMDYDNGW GDLSDAFIDR VIVVLASSSA PNVVRPATVI VRKLMVASPK
AHSSGKGKSK AREGDSVNQY GFDRVFTRIV DVGHMVPDDH GGSPAEAVFR PIVKRLEGTR
DLELVAQSLA LINAALRSAQ QEGSKRYSDL ITVIEALGTR KYVARLIPSS QNNPVETRIF
DFQTRYANVL RYHSLRPVKP QNNPTHERYL DDVWQTGRLD SEDGGGHRAS PRPSMQDYQS
SGQRTWDGWR RMGLSIDYVE ASDPLNETEL FRSIGELGLE CLHYYAVHED NFHSVVLEQL
ARPADRRCPI GKASAECVKV LYDHYKISQS AQRGASHFQP FMLNFPRLHS LVLKFFLRMW
QDSESRLDDF ERLSYLVRSQ VRQTLADEHS KTWLDLEHDF LGADYRNIRE GQMEMIDKED
GLLERPAVAA LRAKVGHEAY EVMAEQRVIC MQQGGWFNTA HVLKSGIDVT TRANPTRPHR
FVRLSPNRRQ LGWSEYTVRP KEKPAFEQLR EKIDLANISE VRVQTGCAVG SRSPDTVSKN
SFSIMASPEL SLLDLDAIHA AQFAEWVDGL RVLKQEVPMS TQESANYMHI LTELALKVRL
LDITGDGIEI PQKVTFGTAP KSTDFWFAS
//
