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Database: UniProt
Entry: A0A165UBU1_9AGAM
LinkDB: A0A165UBU1_9AGAM
Original site: A0A165UBU1_9AGAM 
ID   A0A165UBU1_9AGAM        Unreviewed;       766 AA.
AC   A0A165UBU1;
DT   06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT   06-JUL-2016, sequence version 1.
DT   27-MAR-2024, entry version 21.
DE   RecName: Full=ELMO domain-containing protein {ECO:0000259|PROSITE:PS51335};
GN   ORFNames=NEOLEDRAFT_1154882 {ECO:0000313|EMBL:KZT27925.1};
OS   Neolentinus lepideus HHB14362 ss-1.
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC   Gloeophyllales; Gloeophyllaceae; Neolentinus.
OX   NCBI_TaxID=1314782 {ECO:0000313|EMBL:KZT27925.1, ECO:0000313|Proteomes:UP000076761};
RN   [1] {ECO:0000313|EMBL:KZT27925.1, ECO:0000313|Proteomes:UP000076761}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=HHB14362 ss-1 {ECO:0000313|EMBL:KZT27925.1,
RC   ECO:0000313|Proteomes:UP000076761};
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; KV425560; KZT27925.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A165UBU1; -.
DR   STRING; 1314782.A0A165UBU1; -.
DR   InParanoid; A0A165UBU1; -.
DR   OrthoDB; 1473500at2759; -.
DR   Proteomes; UP000076761; 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:UP000076761};
KW   SH3-binding {ECO:0000256|ARBA:ARBA00023036}.
FT   DOMAIN          352..508
FT                   /note="ELMO"
FT                   /evidence="ECO:0000259|PROSITE:PS51335"
FT   REGION          1..30
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          652..673
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        659..673
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   766 AA;  86098 MW;  3E14B4469E6D8F6E CRC64;
     MANNSNARSN ASTTGANGAS RPKSLLVPTN SVTTKDGVTV RARIEPTLTV DDVIRQLCLN
     LQLRDPPGMF ALRDETDELV TNDNLRKKIK GRVHLKLVNS PSLEAVDVVE KLSLRDERTL
     RKTLFSLQKF IREEQFANEF LQRDGLSELL DVISVSHGNT LAYALLAMQN LMDLDHGWSN
     LDNSFIFRVV QILSSPQSLI NVCRPATAIL KKLVEADPHS APGPLMASSS RSPPSVPPGS
     VYRYGFDAVF EQMRREKGML ETVVSRLGSA DTSMILYSMM LINSLLSHAT DARWEEFTNE
     LEKLNVRKAV IRVMSSHTIE DLTSCILDFQ ANMIRVTYRK KMTLVEPAAE YSHAAALKSI
     WSASKLQEEL DNEGQPQRWR LLGFGSEDIT HEFRDAGILG LYCLKHFAKS DPESFSKMVL
     EQLSRPAERR CPIARASNEI VELLSEHWAI FAPGYSTSTT FQPFFLNFLK VHALALNFFL
     RMWSESGAAA DDFPRVVALT RSQVKVALRQ ENVRAWHEVE HDFNESEYRA VRDRQMKELE
     MEDDLMSKAP MRNLSAKLYK ESYEFVRQQR IQCLLQGSWF VNAMPSSSPI SRDTLRKPSR
     PWRFMRLDNG LKYLHFVDST VKFPVRNGLE DLPDRIDIAQ ITEVATGTCA APPNMLRDQT
     DLPPTSPTSP SSLSFSLLTA DGSSLSDQIA PDQSRWADWT DGLNMLRRDG GHVASQETAG
     FVKALTDIGL KIKLLDLTGE RVDIPSGLVA GPPPTNTDFF FSDLYD
//
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