ID A0A165GCV9_9APHY Unreviewed; 776 AA.
AC A0A165GCV9;
DT 06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT 06-JUL-2016, sequence version 1.
DT 27-MAR-2024, entry version 22.
DE RecName: Full=ELMO domain-containing protein {ECO:0000259|PROSITE:PS51335};
GN ORFNames=LAESUDRAFT_756360 {ECO:0000313|EMBL:KZT10174.1};
OS Laetiporus sulphureus 93-53.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Polyporales; Laetiporus.
OX NCBI_TaxID=1314785 {ECO:0000313|EMBL:KZT10174.1, ECO:0000313|Proteomes:UP000076871};
RN [1] {ECO:0000313|EMBL:KZT10174.1, ECO:0000313|Proteomes:UP000076871}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=93-53 {ECO:0000313|EMBL:KZT10174.1,
RC ECO:0000313|Proteomes:UP000076871};
RX PubMed=26659563; DOI=10.1093/molbev/msv337;
RA Nagy L.G., Riley R., Tritt A., Adam C., Daum C., Floudas D., Sun H.,
RA Yadav J.S., Pangilinan J., Larsson K.H., Matsuura K., Barry K., Labutti K.,
RA Kuo R., Ohm R.A., Bhattacharya S.S., Shirouzu T., Yoshinaga Y.,
RA Martin F.M., Grigoriev I.V., Hibbett D.S.;
RT "Comparative Genomics of Early-Diverging Mushroom-Forming Fungi Provides
RT Insights into the Origins of Lignocellulose Decay Capabilities.";
RL Mol. Biol. Evol. 33:959-970(2016).
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; KV427610; KZT10174.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A165GCV9; -.
DR STRING; 1314785.A0A165GCV9; -.
DR InParanoid; A0A165GCV9; -.
DR OrthoDB; 1473500at2759; -.
DR Proteomes; UP000076871; 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:UP000076871};
KW SH3-binding {ECO:0000256|ARBA:ARBA00023036}.
FT DOMAIN 358..513
FT /note="ELMO"
FT /evidence="ECO:0000259|PROSITE:PS51335"
FT REGION 1..39
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 776 AA; 87266 MW; 0EC87BFE3734B4FD CRC64;
MSANGDAPSR SVASPVPPST EGNGTSPQQK NRVVPTNTVT TKEAGTVRVR IVPNLPVDDV
VRQLCINLRL KDHPAMYALR DENDELVTND NLRKKVMAKA NFKLVNSPAI EAAEIVEKLV
LRDGKLGLAL TSLRRYIREE QFADEFLQRD GLNELIGVIK VSHGNMLAYA LTAMQNLMEL
DHGWDTLDDT FILKIVEILS SSQSLINVCR PATAILKKLV EASPAAAPTA HMASTSKGPP
APPPGSVYRY GFNAVFQQMR KDTRLLETVV DRLASADTTM ALYSMMLINS LLANVTDAYW
DEFTTAMERL NVRKAVIRLM SSHTIEDLTS CILDFQANMI RLTFRKKTTP VQPEIEESHN
ATLNYVWVSS KVSEEGEGEN IVKWRKLGFD SEDLTEEFRE VGTLGLYSLR HFVAKDPDYW
AKIIQEQLSR PEERRCPIAK ASNEVVDLLA EHWAIYAPGY STSTTFQPFF LNFSKVHALA
THFFLRMWNE SGASRGDFPR LVALTRSQVK EALKRENERQ WHEIEQDFLE CEYRAVRDRQ
MRELEMEDDS MSKGPMRALR GKLYKESFEF VRQQRIHCLQ EGAWFMNGIP IMSNISRDTI
RRPSRPWRFM RLDNSLRYLH YVDSAVKFVV RKGLEDLPER IDASLVSEVA TGTCMPFPSN
LRDVDVAAGP SSPLAASPLS FSLLTAGGAS LADQIAPDQS RWADWTDGLN MLRKDGGHVA
SQETEMFIQA LTDIGLKIKL LDLTGEKIDI PTGLAAGPPP TNCDFFFSDL SYDTQA
//
