ID B6QMJ9_TALMQ Unreviewed; 752 AA.
AC B6QMJ9;
DT 16-DEC-2008, integrated into UniProtKB/TrEMBL.
DT 16-DEC-2008, sequence version 1.
DT 27-MAR-2024, entry version 57.
DE SubName: Full=ELMO/CED-12 family protein {ECO:0000313|EMBL:EEA22287.1};
GN ORFNames=PMAA_060660 {ECO:0000313|EMBL:EEA22287.1};
OS Talaromyces marneffei (strain ATCC 18224 / CBS 334.59 / QM 7333)
OS (Penicillium marneffei).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Trichocomaceae; Talaromyces;
OC Talaromyces sect. Talaromyces.
OX NCBI_TaxID=441960 {ECO:0000313|EMBL:EEA22287.1, ECO:0000313|Proteomes:UP000001294};
RN [1] {ECO:0000313|Proteomes:UP000001294}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 18224 / CBS 334.59 / QM 7333
RC {ECO:0000313|Proteomes:UP000001294};
RX PubMed=25676766; DOI=10.1128/genomea.01559-14;
RA Nierman W.C., Fedorova-Abrams N.D., Andrianopoulos A.;
RT "Genome sequence of the AIDS-associated pathogen Penicillium marneffei
RT (ATCC18224) and its near taxonomic relative Talaromyces stipitatus
RT (ATCC10500).";
RL Genome Announc. 3:E0155914-E0155914(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; DS995903; EEA22287.1; -; Genomic_DNA.
DR RefSeq; XP_002150896.1; XM_002150860.1.
DR AlphaFoldDB; B6QMJ9; -.
DR STRING; 441960.B6QMJ9; -.
DR VEuPathDB; FungiDB:PMAA_060660; -.
DR HOGENOM; CLU_009191_0_0_1; -.
DR OrthoDB; 1473500at2759; -.
DR PhylomeDB; B6QMJ9; -.
DR Proteomes; UP000001294; 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 Glycosyltransferase {ECO:0000256|ARBA:ARBA00022676};
KW Phagocytosis {ECO:0000256|ARBA:ARBA00022907};
KW Reference proteome {ECO:0000313|Proteomes:UP000001294};
KW SH3-binding {ECO:0000256|ARBA:ARBA00023036};
KW Transferase {ECO:0000256|ARBA:ARBA00022676}.
FT DOMAIN 246..438
FT /note="ELMO"
FT /evidence="ECO:0000259|PROSITE:PS51335"
FT REGION 252..297
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 515..539
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 586..667
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 262..281
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 282..297
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 518..539
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 752 AA; 83930 MW; 44BC8AEACD2660F6 CRC64;
METLNPSDLV ARLASDEDAV RKMAAFKLQG SIGDPSFADI FIAEGGLSKL RYLILTTTGN
TLAYSLTSFA RLLEVDKGWE FVDEEVVERI VHLIVTHPLV NILRGAMAML VSIVSHPHIP
RSESEQSPPE EKEVYGFRAL KPAIDKHPQF LEMLVSRLSS ADHALCANAL QLINSLMRDS
ITNDEESEWP KFIKRLQDLG VIRAVYILMQ GSALQDHAHP LIEFQSLTKL LLRKWKNVPV
DLEKPDHRRA LKGIHLASNP AKKESGGSSA GGSSENSATA GENDIKKSRK HNPEKWRRLG
FQSESPAAEF HEMGFLGMMD LTDYVRKHQD DFQKMLLEQS AKPAEQRCPI ARASLAVTSV
LYEHFEVEKS ATDDAKSYLV LESRSNFDKV FKPLLLHWSR IHVASLQAFF RLWKATSAEV
ADFDKIVELV RILVESVVGG APRTKDVQDV EEELDDFEYQ RLRELQMELL ELTYEDAWGQ
HLRQVRDELQ HEALQFVKEQ RIRCLLQGAW FPNEPVSSPR PEDSSPIKTA DSKNKQSQGY
KYVQLSHNRR YLHFSDFDAI KETAPALDSL SNKIDLSIVS SVVSNVSASS DDSSGSTIKT
TPGNGNSSSL HPPPGTSSSS ATTTSSTKIT IHGYAPTIAS SSGPKSLATT NKESGHTRTG
SKTTQREIPL LTLRPQNHSI ASEWLDGLLM LLNQQPITSE TNKLVNLISN YGLKIRLLNV
RFDDAAFVGE TPKIPSREGL DEDYYYDVFG GV
//
