ID A0A093ZCZ6_9PEZI Unreviewed; 716 AA.
AC A0A093ZCZ6;
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=V492_05803 {ECO:0000313|EMBL:KFY08905.1};
OS Pseudogymnoascus sp. VKM F-4246.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC Leotiomycetes incertae sedis; Pseudeurotiaceae; Pseudogymnoascus.
OX NCBI_TaxID=1420902 {ECO:0000313|EMBL:KFY08905.1, ECO:0000313|Proteomes:UP000029299};
RN [1] {ECO:0000313|EMBL:KFY08905.1, ECO:0000313|Proteomes:UP000029299}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=VKM F-4246 {ECO:0000313|EMBL:KFY08905.1,
RC ECO:0000313|Proteomes:UP000029299};
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:KFY08905.1}.
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DR EMBL; JPJU01002068; KFY08905.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A093ZCZ6; -.
DR STRING; 1420902.A0A093ZCZ6; -.
DR HOGENOM; CLU_009191_0_0_1; -.
DR Proteomes; UP000029299; 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:UP000029299};
KW SH3-binding {ECO:0000256|ARBA:ARBA00023036}.
FT DOMAIN 274..443
FT /note="ELMO"
FT /evidence="ECO:0000259|PROSITE:PS51335"
FT REGION 272..297
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; 80618 MW; 2413FC0990937015 CRC64;
MDQAEIPSLL RSLSSEEDAL RKMAVFKLQS SINDPSFADV FISTGGLAIL RQLIMTTGGN
TLAYSLQSLS RLLEVDMGWE IFESAGAGEL VERVVELIVT HPLVNILRGA MSILVAIVSH
PQTTRGAIRT PGAFGFRTLK PAVAVYPQFF EMVVSQLNSA DHALCANALM LLNALMRDAI
TNDGGKDGTS KSSGTGEEWP KFIKRLQDLG VVRGAYRLMQ SSALQDLAHP LLEFQTLTKL
LTRKWRDMRV DLERPDHRRA LKGIHLASAP EKREHVTQMG RIEEVSDSAK KGSRKHNPEK
WRRLGFATES PAWEFDPMGY LGMMDLTDYV RKQEDNFQKI LLEQSSKPLH TRCPIARCSL
AVTAILYEHF GADKPETEDA KYYQMLESPQ NYDMIFKPLV LQWSRLHTAG LLAFFRLWKA
TGAVQDDFDK VAELVRILID KVVGSATRTK DIQEAEEEIA EFEYQRLREV QMEVLKFSFE
DQWGHHLQQV REELHNESLQ FVKEQRIRCL LQGSWFPRSA TRGDPDSAAS VRSLPWRFAR
LSHNRRYLHY ADFEVQAGYA PPLTELGEKL DVGTISSVVS NVTAGGEDDT SSISSSTSTL
KKEDLSAPPK RNTKNKITIN SYLPTESADE EQVERMLLTL DPQTHSLASE WLDGLLMLLN
QAPITAETNK LVGLVVDYGL KIRLLNVRLE DGMEAGEGKG LIPSREGLDE DYYYEV
//