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Database: UniProt
Entry: A0A319AXN7_ASPLB
LinkDB: A0A319AXN7_ASPLB
Original site: A0A319AXN7_ASPLB 
ID   A0A319AXN7_ASPLB        Unreviewed;       697 AA.
AC   A0A319AXN7;
DT   10-OCT-2018, integrated into UniProtKB/TrEMBL.
DT   10-OCT-2018, sequence version 1.
DT   27-MAR-2024, entry version 20.
DE   RecName: Full=ELMO domain-containing protein {ECO:0000259|PROSITE:PS51335};
GN   ORFNames=BO96DRAFT_428019 {ECO:0000313|EMBL:PYH50662.1};
OS   Aspergillus lacticoffeatus (strain CBS 101883).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC   Aspergillus subgen. Circumdati.
OX   NCBI_TaxID=1450533 {ECO:0000313|EMBL:PYH50662.1, ECO:0000313|Proteomes:UP000247441};
RN   [1] {ECO:0000313|EMBL:PYH50662.1, ECO:0000313|Proteomes:UP000247441}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CBS 101883 {ECO:0000313|EMBL:PYH50662.1,
RC   ECO:0000313|Proteomes:UP000247441};
RG   DOE Joint Genome Institute;
RA   Vesth T.C., Nybo J., Theobald S., Brandl J., Frisvad J.C., Nielsen K.F.,
RA   Lyhne E.K., Kogle M.E., Kuo A., Riley R., Clum A., Nolan M., Lipzen A.,
RA   Salamov A., Henrissat B., Wiebenga A., De Vries R.P., Grigoriev I.V.,
RA   Mortensen U.H., Andersen M.R., Baker S.E.;
RT   "The genomes of Aspergillus section Nigri reveals drivers in fungal
RT   speciation.";
RL   Submitted (DEC-2016) 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; KZ821391; PYH50662.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A319AXN7; -.
DR   OrthoDB; 1473500at2759; -.
DR   Proteomes; UP000247441; Unassembled WGS sequence.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
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   Glycosyltransferase {ECO:0000256|ARBA:ARBA00022676};
KW   Phagocytosis {ECO:0000256|ARBA:ARBA00022907};
KW   SH3-binding {ECO:0000256|ARBA:ARBA00023036};
KW   Transferase {ECO:0000256|ARBA:ARBA00022676}.
FT   DOMAIN          239..420
FT                   /note="ELMO"
FT                   /evidence="ECO:0000259|PROSITE:PS51335"
FT   REGION          255..280
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          589..608
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   697 AA;  79020 MW;  9CABF9F6D657C8C0 CRC64;
     METSISELVE RLGSDEDAVR KMAVFKLQGS IGDPSFADNF IAEGGLTRLR YLTLHASGNT
     LAYSLTSFAR ILEVDKGWDL VDQDMVERVV ELIVTHPLVN ILRGAMSILV SIVSHPYSGN
     HLSQDGNFGF RALKPAIAIY PQFLEMLVNR LSSADHALCA NALQLINSLM RDSITNDADT
     EWPKFIQKLQ DLGVIRAVYS LMQGSALQDH VHPLIEFQSL TKVLLRKWRE IYLDLERPEH
     RRALKGIYLA SSHERGQEKG VENGDEMRQS KKHSSEKWRR LGFETESPST QFEDTGFLGM
     MDLADYVRNH QDEFQKMLLE QSTKPPQQRC PIARASLSVT SILYQHFEVD KSEMDDSKGY
     LLLESRSNLD KVFEPLLLHW TRLHVAGLHA FFRLWKATGA EVEDYGKIVE LIRILIESVV
     GGAPRTKDVQ EVEEELANFE YGRLRELQME LLELAYEDAW GQHLQQMREE LYHEALQFVK
     EQRIRCLLHG AWFLNEGPIS SDAGTEQHSW KYAQLSHNRR FLHFGDFNAI LERRPELDTL
     PEKIDLSLVS SVVSNVSASS KDQSTAPAKD MPHAVSYTKI TVHGYSQPVH ETGDIHKSNG
     HRRTSSRSAQ GESALLSFCP QSTSVASEWL DGLLMLLNQQ PITAETNKLI SLVSDYGLKI
     RLLNVRFDDV AFAGETPQVP TRDGLDDNYY YDVFGGS
//
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