ID A0A151GMC6_9HYPO Unreviewed; 1317 AA.
AC A0A151GMC6;
DT 08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT 08-JUN-2016, sequence version 1.
DT 27-MAR-2024, entry version 28.
DE RecName: Full=ELMO domain-containing protein {ECO:0000259|PROSITE:PS51335};
GN ORFNames=DCS_05272 {ECO:0000313|EMBL:KYK58259.1};
OS Drechmeria coniospora.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Ophiocordycipitaceae; Drechmeria.
OX NCBI_TaxID=98403 {ECO:0000313|EMBL:KYK58259.1, ECO:0000313|Proteomes:UP000076580};
RN [1] {ECO:0000313|EMBL:KYK58259.1, ECO:0000313|Proteomes:UP000076580}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ARSEF 6962 {ECO:0000313|EMBL:KYK58259.1,
RC ECO:0000313|Proteomes:UP000076580};
RX PubMed=26975455; DOI=10.1038/srep23122;
RA Zhang L., Zhou Z., Guo Q., Fokkens L., Miskei M., Pocsi I., Zhang W.,
RA Chen M., Wang L., Sun Y., Donzelli B.G., Gibson D.M., Nelson D.R.,
RA Luo J.G., Rep M., Liu H., Yang S., Wang J., Krasnoff S.B., Xu Y.,
RA Molnar I., Lin M.;
RT "Insights into Adaptations to a Near-Obligate Nematode Endoparasitic
RT Lifestyle from the Finished Genome of Drechmeria coniospora.";
RL Sci. Rep. 6:23122-23122(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}.
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:KYK58259.1}.
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DR EMBL; LAYC01000002; KYK58259.1; -; Genomic_DNA.
DR STRING; 98403.A0A151GMC6; -.
DR InParanoid; A0A151GMC6; -.
DR OrthoDB; 1473500at2759; -.
DR Proteomes; UP000076580; Chromosome 02.
DR GO; GO:0005615; C:extracellular space; IEA:InterPro.
DR GO; GO:0017124; F:SH3 domain binding; IEA:UniProtKB-KW.
DR GO; GO:0090729; F:toxin activity; IEA:UniProtKB-KW.
DR GO; GO:0006915; P:apoptotic process; IEA:UniProtKB-KW.
DR Gene3D; 3.90.210.10; Heat-Labile Enterotoxin, subunit A; 1.
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; IPR001144; Enterotoxin_A.
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; PF01375; Enterotoxin_a; 1.
DR Pfam; PF16457; PH_12; 1.
DR SUPFAM; SSF56399; ADP-ribosylation; 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:UP000076580};
KW SH3-binding {ECO:0000256|ARBA:ARBA00023036};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP};
KW Toxin {ECO:0000256|ARBA:ARBA00022656};
KW Virulence {ECO:0000256|ARBA:ARBA00023026}.
FT SIGNAL 1..26
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 27..1317
FT /note="ELMO domain-containing protein"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5007580723"
FT DOMAIN 873..1041
FT /note="ELMO"
FT /evidence="ECO:0000259|PROSITE:PS51335"
FT REGION 333..420
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 440..514
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1183..1206
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 333..349
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 369..383
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 398..415
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 440..458
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 464..489
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1317 AA; 144138 MW; 56192CB366105564 CRC64;
MMHLFSPRQG LVFHLLFSVQ CFTVSAVDTA LGNGPLDSSQ ALRVPLGALP NDHDDFHLPE
ENQGAIPWTI SSHVAGKPPP PPSLVFRYDL RDPDEVFSDG FKTRQLEREG RPSLVGWDIS
RHTYGSEENL ESTNYVSTTR LPKVAEEFGD DLDSGGEHSF FDSAELTEAA KRQNPDGSVN
YHHPIADVLE DAAARGPKMG YIYIIKPDPS FINVFQTLGP DGFQDKTNLR QQEFAAMVEI
KSDRIIGGYD LADPEKVIEF NPGYNQAYDR QRAGVGYRRL AHNSNEVISN MARIIRDSAE
LESRKLRQEA ALRHAPRHEW ESMSLSRFIQ EFTDRNAPPP TSTATYPSHQ GGPAEDERAG
TSSARTLKRP LDTAEDDGGS GIGGKHRCPR SEGCNPKHVT NPVMTASTGQ GESKADGTNA
DHVKELASDT TEQQKNALLQ TNHQGRMPIN PLGTKATKST DNEQDDEPDN EPDNEPDNEP
GDEPGDESGD ESGEGHGIET TNEAIEGRPS QTGATGKHLL ASLALTTHRG PVPVLVPDAP
STWPKAAGAG AVANGLQLET QQLGNRAEAI ASAPVPLQTK PRRQQGHDLA GSIFSAAHHL
ASQATPRRRP PPVVRLAMDQ ADIPALLSRL GSDEDGVRKM AVFKLQSSIN DPAFADVFIS
SGGLAVLRRM IMGSGGNTLA YSLQSLTRLL EVDMGWEIFE GPTATDLVER VVELIVTNPL
VNILRGAMSI LVSLVGHSQS SAVGSPGGAT PGPFGFRALK PAVAVYPHFF ELVIQQLRSA
DHALCANALM LINALIRDAI STSTLDAVGG SGGEEWVKLV KSLQDLGLTR AVYKLMQSSA
LQDLAHPMLE FQSLSKVLIR KWRDVGVDGE RPEHRRALES IHLASASDAS GRHDGAEKWR
RLGFETENPG QEFEPTGYLG IMDLTSYVRK HEDGFQKLLQ EQSTKPLTDR CPVARASLAM
TTMLYEHFEI ERSDAEDAKG YQGGETKDHD KLFRPLLLHW PRLHTAGLRA FFRIWKATGA
GEEDDFDKVA ALVRILVEQV VGGATRTKDV LEVEDELQDY DVGRLREVQM DLLELAFDAT
WGRHLHQVRE VLQQEALQFV KEQRVRCLLQ GSWFAKPTMK RATMDAQLAS STSTPWRFVK
LSHNRRYLHY ADFESQMAQD PGLDSLDDKV DLSTISSVVS NVSAPKDDAK STNSGSTAQH
QTAAGGSVRA TTKITIYGNA GAVDAEAGQG DRREVPILTL WPLSHSLASE WLDGLLMLLQ
QAPITAETSK LINLVSDYGL KIRLLNVRMD SPFEGPPPGA GIVPSRKGLD EDYFFEV
//
