ID A0A395NTD9_TRIAR Unreviewed; 710 AA.
AC A0A395NTD9;
DT 05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT 05-DEC-2018, sequence version 1.
DT 27-MAR-2024, entry version 21.
DE RecName: Full=ELMO domain-containing protein {ECO:0000259|PROSITE:PS51335};
GN ORFNames=TARUN_3106 {ECO:0000313|EMBL:RFU79097.1};
OS Trichoderma arundinaceum.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Hypocreaceae; Trichoderma.
OX NCBI_TaxID=490622 {ECO:0000313|EMBL:RFU79097.1, ECO:0000313|Proteomes:UP000266272};
RN [1] {ECO:0000313|EMBL:RFU79097.1, ECO:0000313|Proteomes:UP000266272}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=IBT 40837 {ECO:0000313|EMBL:RFU79097.1,
RC ECO:0000313|Proteomes:UP000266272};
RX PubMed=29649280; DOI=10.1371/journal.ppat.1006946;
RA Proctor R.H., McCormick S.P., Kim H.S., Cardoza R.E., Stanley A.M.,
RA Lindo L., Kelly A., Brown D.W., Lee T., Vaughan M.M., Alexander N.J.,
RA Busman M., Gutierrez S.;
RT "Evolution of structural diversity of trichothecenes, a family of toxins
RT produced by plant pathogenic and entomopathogenic fungi.";
RL PLoS Pathog. 14:e1006946-e1006946(2018).
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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:RFU79097.1}.
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DR EMBL; PXOA01000176; RFU79097.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A395NTD9; -.
DR STRING; 490622.A0A395NTD9; -.
DR Proteomes; UP000266272; 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:UP000266272};
KW SH3-binding {ECO:0000256|ARBA:ARBA00023036}.
FT DOMAIN 257..443
FT /note="ELMO"
FT /evidence="ECO:0000259|PROSITE:PS51335"
FT REGION 262..302
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 267..284
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 285..302
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 710 AA; 79246 MW; 169229FCC2A3C3CA CRC64;
MDQADIPALL SRLSSDEDAA RKMAVFKLQS SINDPAFADV FISSGGLVIL RRLIMGSGGN
TLAYSLQSLT RLLDIDIGWD IFQGPTASEL VERIVELIVT NPLVNILRGA MSILVALVGH
SQSNGPDSPT QDQGAFGFRA LKPAVAVYPQ FFDLVVQQLN SADHALCANA LMLVNALIRD
ALSTKSVMAS GNGKAAGEEW PKLMKRLQDL GLIKAVYKLM QGTGLQDLAH PALEFQNLSK
VIIRKWRDVR VDLERPEHRR SLKSLHLSSA PDRSTINGHV REGSSDTTTT KKDGRKHSPE
KWRRLGFETE SPAQDFDVAG YLGMMDLTDY VRKNEDRFQK LLLEQATRPM HERCPVARAS
LAMTMILYEH FDVDKADLED MKGYQGVETK DYDRVFRPLL LQWSRLHAAG LHSFFRIWKA
TGAALEDFDK VAELVRILIE RVVGQAPRTS DLLEVEEDLQ EYDISRLREL QMELLEMSFE
ETWGKHLYQV RDVLKQEALQ FVKEQRVRCL LHGAWFRRPA SQKDDTGEKK PWRFAKLSHN
RRYLHYTDFE KQMAQDPGLN SLMEKIDLTT ISSVVSNVSA SNDDSKTVAS GATIQNITSG
GEKSTTKITI YSFVNPADTA GGDTAKEQPV LALYPANPSV ASEWLDGLLM ILNQAPITAE
TSKLVNLVGG YGLKIRLLNV RMDAAIEGPP VGAGIVPSRE GLDEDYFYEV
//
