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Database: UniProt
Entry: A0A0A1TRZ2_9HYPO
LinkDB: A0A0A1TRZ2_9HYPO
Original site: A0A0A1TRZ2_9HYPO 
ID   A0A0A1TRZ2_9HYPO        Unreviewed;       705 AA.
AC   A0A0A1TRZ2;
DT   04-FEB-2015, integrated into UniProtKB/TrEMBL.
DT   04-FEB-2015, sequence version 1.
DT   27-MAR-2024, entry version 30.
DE   RecName: Full=ELMO domain-containing protein {ECO:0000259|PROSITE:PS51335};
GN   ORFNames=VHEMI10508 {ECO:0000313|EMBL:CEJ95005.1};
OS   [Torrubiella] hemipterigena.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Hypocreomycetidae; Hypocreales; Clavicipitaceae;
OC   Clavicipitaceae incertae sedis; 'Torrubiella' clade.
OX   NCBI_TaxID=1531966 {ECO:0000313|EMBL:CEJ95005.1, ECO:0000313|Proteomes:UP000039046};
RN   [1] {ECO:0000313|EMBL:CEJ95005.1, ECO:0000313|Proteomes:UP000039046}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Horn F., Habel A., Scharf D.H., Dworschak J., Brakhage A.A., Guthke R.,
RA   Hertweck C., Linde J.;
RT   "Draft Genome Sequence and Gene Annotation of the Entomopathogenic Fungus
RT   Verticillium hemipterigenum.";
RL   Genome Announc. 3:e01439-e01414(2015).
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; CDHN01000008; CEJ95005.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0A1TRZ2; -.
DR   STRING; 1531966.A0A0A1TRZ2; -.
DR   HOGENOM; CLU_009191_0_0_1; -.
DR   OrthoDB; 1473500at2759; -.
DR   Proteomes; UP000039046; 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:UP000039046};
KW   SH3-binding {ECO:0000256|ARBA:ARBA00023036}.
FT   DOMAIN          247..435
FT                   /note="ELMO"
FT                   /evidence="ECO:0000259|PROSITE:PS51335"
FT   REGION          250..296
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   705 AA;  78835 MW;  749107245798AF55 CRC64;
     MDQADIPALL ARLSSDEDAA RKMAVFKLQT SINDPSFADV FISSGGLVIL RRLIMESSGN
     TLAYSLQSLT RLLEVDMGWD VFEGPTASDL VERIVQLIVT NPLVNILRGA MSILVALVGH
     SQSPQGDASP TTPGSFGFRA LKPAVAVYPQ FFELVVRELS SADHSLCANA LMLVNALIRD
     ALSNPSGDEW SKLIKRLQEL GIVKAVYKLM QSSALQDFAH PVLEFQTLSK LLLKRWRDIP
     VDVDHPEHRR SLKSLHLASA PERKESEPER DDPGSPDKKS PDKKSPKKHN PEKWRRLGFT
     SESPAHDFEI SGCLGMMDLS DYVKKNEDGY QKLLLEQASR PPLERCPIAR ASMTVTLVLC
     DHFEIDKADL EEAKGYHDLD PSRYDIIFQP FLLQWSRLHV AGLQAFFRLW KATGAQVGDF
     TKVAELLRIL VEEVVGQATR TKDVSEIEED MQEYDVARLR EVQMELLEMA FDDTWNEHLH
     QAREVQKQEA IQFVKEQRVR CLLQGSWFTR PTENGVGSKQ EASVWRFAKL SSNRRYLHYA
     DFGSKITPDP GLNTLKERID LSTISSVMSN VSANSDAAST RSDSTVQNVA NNNSSSKGST
     KITIYSYVDA TEVGRPGGDG AEYPILTLWP TTHSLASEWL DGLLMLLNQT PITAETKKLV
     QLVDYYGLKI RLLNVRMDTA LKGPPEGAGV VPSREGLDED YFFEI
//
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