ID A0A094HPA4_9PEZI Unreviewed; 716 AA.
AC A0A094HPA4;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 27-MAR-2024, entry version 28.
DE RecName: Full=ELMO domain-containing protein {ECO:0000259|PROSITE:PS51335};
GN ORFNames=V502_08324 {ECO:0000313|EMBL:KFZ10086.1};
OS Pseudogymnoascus sp. VKM F-4520 (FW-2644).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC Leotiomycetes incertae sedis; Pseudeurotiaceae; Pseudogymnoascus.
OX NCBI_TaxID=1420915 {ECO:0000313|EMBL:KFZ10086.1, ECO:0000313|Proteomes:UP000029308};
RN [1] {ECO:0000313|EMBL:KFZ10086.1, ECO:0000313|Proteomes:UP000029308}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=VKM F-4520 (FW-2644) {ECO:0000313|Proteomes:UP000029308};
RA Leushkin E.V., Logacheva M.D., Penin A.A., Sutormin R.A., Gerasimov E.S.,
RA Kochkina G.A., Ivanushkina N.E., Vasilenko O.V., Kondrashov A.S.,
RA Ozerskaya S.M.;
RT "Population genomics of a fungus Geomyces pannorum provides evidence of
RT horizontal gene transfer but not of sexual reproduction.";
RL Submitted (JUL-2014) 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:KFZ10086.1}.
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DR EMBL; JPKE01002886; KFZ10086.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A094HPA4; -.
DR STRING; 1420915.A0A094HPA4; -.
DR HOGENOM; CLU_009191_0_0_1; -.
DR OrthoDB; 1473500at2759; -.
DR Proteomes; UP000029308; 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:UP000029308};
KW SH3-binding {ECO:0000256|ARBA:ARBA00023036}.
FT DOMAIN 256..443
FT /note="ELMO"
FT /evidence="ECO:0000259|PROSITE:PS51335"
FT REGION 272..296
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 583..613
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 583..603
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 716 AA; 80660 MW; 45B582FDB4640EE7 CRC64;
MDQAEIPSLL RSLSSDEDAL RKMAVFKLQS SINDPSFADV FISTGGLSIL RRLIMTTGGN
TLAYSLQSLS RLLEVDMGWE IFESAGAGEL VERVVELIVT HPLVNILRGA MSILVAIVSH
PQTTRGAIRT PGAFGFRTLK PAVAVYPQFF EMVVSQLNSA DHALCANALM LLNALMRDAI
TNDGGKEGTS KSSGTGEEWP KFIKRLQDLG VVKGAYRLMQ SSALQDLAHP LLEFQALTKL
LLRKWREMRV DLERPDHRRA LKGIHLASAP EKREHVTQMG RVEEVSDSAK KGSRKHNPEK
WRRLGFVTES PAWEFDPMGY LGMMDLTDYV RKQEDNFQKI LLEQSSKPLH TRCPIARCSL
AVTAILYDHF GADKSETEDA KYYQMLESPQ NYDMIFRPLV LQWSRLHTAG LLAFFRLWKA
TGAVQDDFDK VAELVRILID KVVGSAPRTK DIQEAEEEIA EFEYHRLREV QMEVLKFSFE
DQWGHHLQQV REELHNESLQ FVKEQRIRCL LQGSWFPRSA TRGDPNSAAS VRSRPWRFAR
LSHNRRFLHY ADFDAQAGYA PPLTELAEKL DVGTISSVVS NVTAGGEDDT SSISSSTSTL
KKEDVNAPPK RNTRNKITVN SYVPTESAEE EQVERVILTL DPQTHSLASE WLDGLLMLLN
QAPITAETNK LVGLVVDYGL KIRLLNVRLE DGMEAGEGKG LIPTREGLDE DYYYEV
//