ID A0A109FI25_9BASI Unreviewed; 789 AA.
AC A0A109FI25;
DT 13-APR-2016, integrated into UniProtKB/TrEMBL.
DT 13-APR-2016, sequence version 1.
DT 27-MAR-2024, entry version 27.
DE RecName: Full=ELMO domain-containing protein {ECO:0000259|PROSITE:PS51335};
GN ORFNames=RHOSPDRAFT_33683 {ECO:0000313|EMBL:KWU44861.1};
OS Rhodotorula sp. JG-1b.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Pucciniomycotina;
OC Microbotryomycetes; Sporidiobolales; Sporidiobolaceae; Rhodotorula.
OX NCBI_TaxID=1305733 {ECO:0000313|EMBL:KWU44861.1, ECO:0000313|Proteomes:UP000062823};
RN [1] {ECO:0000313|EMBL:KWU44861.1, ECO:0000313|Proteomes:UP000062823}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JG-1b {ECO:0000313|EMBL:KWU44861.1,
RC ECO:0000313|Proteomes:UP000062823};
RG DOE Joint Genome Institute;
RA Goordial J., Raymond-Bouchard I., Riley R., Ronholm J., Shapiro N.,
RA Woyke T., Grigoriev I.V., Labutti K.M., Greer C., Whyte L., Bakermans C.;
RT "Draft genome of eurypsychrophile Rhodotorula sp. JG1b isolated from
RT permafrost in the hyper-arid Upper Elevation McMurdo Dry Valleys,
RT Antarctica.";
RL Submitted (DEC-2015) 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}.
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DR EMBL; KQ954476; KWU44861.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A109FI25; -.
DR STRING; 1305733.A0A109FI25; -.
DR OrthoDB; 1473500at2759; -.
DR Proteomes; UP000062823; 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:UP000062823};
KW SH3-binding {ECO:0000256|ARBA:ARBA00023036}.
FT DOMAIN 360..513
FT /note="ELMO"
FT /evidence="ECO:0000259|PROSITE:PS51335"
FT REGION 1..54
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 789 AA; 86721 MW; 2AC2C93FD2DFD860 CRC64;
MIRDQLQPTA STSRLPLHAP PRRTAVGPID STAAGSSPSP SPSSILKPPP SKNDKVQLSR
PYYFYWGEKR VKARIDPEVP LVEVVKQLVR SSQLALEAKY AANPEAYALR EHTTGELVSD
RNLGEMLETA TYFDLVKNPD HEARIVVRKL SSADPAALKQ TTFSLRSQLT DVAFRTAFIR
ADGIPTLQAI IRRGSGNTLA YALASLHVLL DTDGLTFDSL FIARLVDIVA LEALVNVTRP
ATAVLCTLAS NARQRAPAYS TFVDILLRQR LLLPALVERL ATGDLELSDL TVDLLDQLLI
GSVDTADARI PDKLEATDAW RAIAKILETN VGAPAKRFSS LHTSLMRYLQ AASLAPITED
DYHYFDEIWL ASHLKDVDES CRWRRLGFQT EAPQYEFDGV GLLGLKMLKR FAEDSQNEFA
ETLREHEGVP DPARRIPLST ISNIVLALLL SHLASPDPTA NDDALSPYLF RLSDCHALAA
QFFQRMWEAG EAAGAQDLDR IARMTRSQIA HVLDLKREKS WFRVRQEFLN ADFAAVRDRQ
LRELAADHAL LATPKAQALK SRLYSEAYDR VRRQRVAALE AGAWFRLAAA SPSLSGSHVH
QRGDKLAPPL WRFYRLSPDH RELSWADTVE PGRTKLEPDA LTSSVSVDSI VDIKSAEGPD
MATSTASHNG PELAASGLDS VRRRFHALQG STRSRPSSDR AGAADEPLSF ALSFTSGAPV
QLVAPDEATY TDWVDGLCAL KPGGAIVTRK TLQYIDSLAD IGTRIKLLDL QDRPPERGSS
STGEVAPAG
//
