ID A7ER00_SCLS1 Unreviewed; 731 AA.
AC A7ER00;
DT 11-SEP-2007, integrated into UniProtKB/TrEMBL.
DT 11-SEP-2007, sequence version 1.
DT 27-MAR-2024, entry version 71.
DE RecName: Full=ELMO domain-containing protein {ECO:0000259|PROSITE:PS51335};
GN ORFNames=SS1G_07753 {ECO:0000313|EMBL:EDN91892.1};
OS Sclerotinia sclerotiorum (strain ATCC 18683 / 1980 / Ss-1) (White mold)
OS (Whetzelinia sclerotiorum).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC Helotiales; Sclerotiniaceae; Sclerotinia.
OX NCBI_TaxID=665079 {ECO:0000313|EMBL:EDN91892.1, ECO:0000313|Proteomes:UP000001312};
RN [1] {ECO:0000313|Proteomes:UP000001312}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 18683 / 1980 / Ss-1 {ECO:0000313|Proteomes:UP000001312};
RX PubMed=21876677; DOI=.1371/journal.pgen.1002230;
RA Amselem J., Cuomo C.A., van Kan J.A., Viaud M., Benito E.P., Couloux A.,
RA Coutinho P.M., de Vries R.P., Dyer P.S., Fillinger S., Fournier E.,
RA Gout L., Hahn M., Kohn L., Lapalu N., Plummer K.M., Pradier J.M.,
RA Quevillon E., Sharon A., Simon A., ten Have A., Tudzynski B., Tudzynski P.,
RA Wincker P., Andrew M., Anthouard V., Beever R.E., Beffa R., Benoit I.,
RA Bouzid O., Brault B., Chen Z., Choquer M., Collemare J., Cotton P.,
RA Danchin E.G., Da Silva C., Gautier A., Giraud C., Giraud T., Gonzalez C.,
RA Grossetete S., Guldener U., Henrissat B., Howlett B.J., Kodira C.,
RA Kretschmer M., Lappartient A., Leroch M., Levis C., Mauceli E.,
RA Neuveglise C., Oeser B., Pearson M., Poulain J., Poussereau N.,
RA Quesneville H., Rascle C., Schumacher J., Segurens B., Sexton A., Silva E.,
RA Sirven C., Soanes D.M., Talbot N.J., Templeton M., Yandava C., Yarden O.,
RA Zeng Q., Rollins J.A., Lebrun M.H., Dickman M.;
RT "Genomic analysis of the necrotrophic fungal pathogens Sclerotinia
RT sclerotiorum and Botrytis cinerea.";
RL PLoS Genet. 7:E1002230-E1002230(2011).
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; CH476630; EDN91892.1; -; Genomic_DNA.
DR RefSeq; XP_001591128.1; XM_001591078.1.
DR AlphaFoldDB; A7ER00; -.
DR STRING; 665079.A7ER00; -.
DR GeneID; 5487453; -.
DR KEGG; ssl:SS1G_07753; -.
DR VEuPathDB; FungiDB:sscle_11g083640; -.
DR InParanoid; A7ER00; -.
DR OMA; WESHARP; -.
DR OrthoDB; 1473500at2759; -.
DR Proteomes; UP000001312; Unassembled WGS sequence.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0017124; F:SH3 domain binding; IEA:UniProtKB-KW.
DR GO; GO:0007015; P:actin filament organization; IBA:GO_Central.
DR GO; GO:0006915; P:apoptotic process; IEA:UniProtKB-KW.
DR GO; GO:0048870; P:cell motility; IBA:GO_Central.
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:UP000001312};
KW SH3-binding {ECO:0000256|ARBA:ARBA00023036}.
FT DOMAIN 258..446
FT /note="ELMO"
FT /evidence="ECO:0000259|PROSITE:PS51335"
FT REGION 266..302
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 594..646
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 287..302
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 594..635
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 731 AA; 81836 MW; 8D226C3EE071BF2A CRC64;
MDQADIPSLL SRLNSDEDAT RKMAVFKLQS SINDPSFADV FISSGGLSIL RQLIMTTNAN
TLAYSLQSLS RLLEVDMGWE IFESQGAGEL VERVVELIVT HPLVNILRGA MSILVAIVSH
PQSSGGRIKI PGAFGFRALK PAVAVYPQFF EMVVSQLNSA DHLLCANALM LLNALMRDAI
TNDNGQGKDN VSKSSGTGEE WPKFIKRLQD LGVIKSAYTL MQSSALQDLS HALLEFQSLT
KVLLGKWREV KVDLERPEHR RALKGIHLAS APEKKDGTNG TVAKGEVSEN GEKKGSRKHN
PEKWRRLGFE TESPAWEFES TGFLGMMDLT DYVRKNEDAF QKLLLEQSSK PLRERCPIAR
ASLMVTSILY DHFDVDKSDA EDAKTYLVLD GVKNYDKIFR PLLLQWSRLH SSSLQAFFRL
WKATGAEQDD FIKVAELVRI LVEQVVGQAS RTKDVLEVEE ELAEFEYSKL RNLQMELLEL
TFEDEWGQHL HQVRDELKHE ALLFVKEQRI RCLLQGAWFP RIIQPKIVSE EGSTSTKSLG
RRIPTTSWRF VKLSHNRRFL HYFDFDHQMS KEPTLDQLLE KIDLSTISSV VSNVSASHDD
GSSISSSSTL KDTNPSSKPN TTTKITINSY VGGENKPQPD GTDPAEKAIL TLMPPTHSLA
SEWLDGLLML LNQAPITSET NKLVGLVSEY GLKIRLLNVR LDDANGYGGP QPGAGKVPSR
DGLDEDYYYE V
//
