ID J4H0A8_9APHY Unreviewed; 776 AA.
AC J4H0A8;
DT 31-OCT-2012, integrated into UniProtKB/TrEMBL.
DT 31-OCT-2012, sequence version 1.
DT 27-MAR-2024, entry version 40.
DE RecName: Full=ELMO domain-containing protein {ECO:0000259|PROSITE:PS51335};
GN ORFNames=FIBRA_00596 {ECO:0000313|EMBL:CCL98594.1};
OS Fibroporia radiculosa.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Polyporales; Fibroporiaceae; Fibroporia.
OX NCBI_TaxID=599839 {ECO:0000313|EMBL:CCL98594.1, ECO:0000313|Proteomes:UP000006352};
RN [1] {ECO:0000313|EMBL:CCL98594.1, ECO:0000313|Proteomes:UP000006352}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=TFFH 294 {ECO:0000313|EMBL:CCL98594.1,
RC ECO:0000313|Proteomes:UP000006352};
RX PubMed=22247176; DOI=10.1128/AEM.06745-11;
RA Tang J.D., Perkins A.D., Sonstegard T.S., Schroeder S.G., Burgess S.C.,
RA Diehl S.V.;
RT "Short-read sequencing for genomic analysis of the brown rot fungus
RT Fibroporia radiculosa.";
RL Appl. Environ. Microbiol. 78:2272-2281(2012).
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}.
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DR EMBL; HE796892; CCL98594.1; -; Genomic_DNA.
DR RefSeq; XP_012177877.1; XM_012322487.1.
DR AlphaFoldDB; J4H0A8; -.
DR STRING; 599839.J4H0A8; -.
DR GeneID; 24093505; -.
DR HOGENOM; CLU_009191_1_0_1; -.
DR InParanoid; J4H0A8; -.
DR OrthoDB; 1473500at2759; -.
DR Proteomes; UP000006352; 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:UP000006352};
KW SH3-binding {ECO:0000256|ARBA:ARBA00023036}.
FT DOMAIN 359..514
FT /note="ELMO"
FT /evidence="ECO:0000259|PROSITE:PS51335"
FT REGION 1..48
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 776 AA; 87619 MW; FAEF226DE9781152 CRC64;
MSSNGEGSSK PTVSPTPTSA ANGSSPAPQA RGGLVPTNNV TTKDGSTVRT RIEPTLPVDD
VIRQLCINLK LKDPPSMYAL RDENDELVTN DNLRKKIKAK INLKLVSAPA LEATEIVEKL
ILRDAKLGLA LTSLRRYIRE EQFAEEFLRR DGLAELINII NTTHGNTLAY ALTAMQNLME
LDRGWNDLDD EFILKIVQIL SSKQSLINVC RPATAILKKL VEASPASTLT ANLASSSRGP
PAPPPDSVYR YGFEVVFEQM RKETRLLETV VERLGSADTT MALYSMMLIN SLLANMTDAR
WDEFTTSLER LNVRKAVIRL MSSHTIEDLT SCILDFQANM MRVTYKEKTT PVEPEIEESH
AAILKYIWSS SRISEDTSEV EVWRWRKLGF DSEDLTQEFR QVGLLGLHCL RYFVAKDPDY
WAKVVQEQRS RPDERRCPIA KASNEVVDLL SEHWAIYSPG YSTTTTFQPF FLNFLKVHTL
ATQFFLRMWN ESGASKNDFP RLVALTRSQV NVALRRENVR AWHEVEHDFS QCEYRAVRDR
QMQELEMEDD IMSKIPMRNL RAKLYKESFD FVRQQRIHCL LDGAWFTNAI PVTSTAHRET
VRRPNRPWRF MRLDNGLKYL HYVDATSKFP MKKGLEDLPE RIDLSAVNEI ATGTCAPYPG
TARDIDVPTP GSPVAVSPLS FSLLTTSGTS LADQIAPDQS RWADWTDGLN MLRKDGGHVA
SKETEMFVQA LTEIGLKIKL LDLTGERVDI PSGLATGAPP TSCDFFYSDL SYDPQA
//
