ID A0A1Y3B1H0_EURMA Unreviewed; 1013 AA.
AC A0A1Y3B1H0;
DT 30-AUG-2017, integrated into UniProtKB/TrEMBL.
DT 30-AUG-2017, sequence version 1.
DT 27-MAR-2024, entry version 30.
DE RecName: Full=Mitochondrial chaperone BCS1 {ECO:0000256|ARBA:ARBA00016942};
DE AltName: Full=BCS1-like protein {ECO:0000256|ARBA:ARBA00032816};
GN ORFNames=BLA29_000802 {ECO:0000313|EMBL:OTF74641.1};
OS Euroglyphus maynei (Mayne's house dust mite).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Chelicerata; Arachnida; Acari;
OC Acariformes; Sarcoptiformes; Astigmata; Psoroptidia; Analgoidea;
OC Pyroglyphidae; Pyroglyphinae; Euroglyphus.
OX NCBI_TaxID=6958 {ECO:0000313|EMBL:OTF74641.1, ECO:0000313|Proteomes:UP000194236};
RN [1] {ECO:0000313|EMBL:OTF74641.1, ECO:0000313|Proteomes:UP000194236}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Arlian Lab {ECO:0000313|EMBL:OTF74641.1};
RC TISSUE=Whole body {ECO:0000313|EMBL:OTF74641.1};
RA Arlian L.G., Morgan M.S., Rider S.D.;
RT "Genome Survey of Euroglyphus maynei.";
RL Submitted (MAR-2017) to the EMBL/GenBank/DDBJ databases.
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 -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004167}; Single-
CC pass membrane protein {ECO:0000256|ARBA:ARBA00004167}. Mitochondrion
CC inner membrane {ECO:0000256|ARBA:ARBA00004434}; Single-pass membrane
CC protein {ECO:0000256|ARBA:ARBA00004434}.
CC -!- SIMILARITY: Belongs to the AAA ATPase family. BCS1 subfamily.
CC {ECO:0000256|ARBA:ARBA00007448}.
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:OTF74641.1}.
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DR EMBL; MUJZ01046074; OTF74641.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1Y3B1H0; -.
DR OrthoDB; 664379at2759; -.
DR Proteomes; UP000194236; Unassembled WGS sequence.
DR GO; GO:0005743; C:mitochondrial inner membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR CDD; cd19510; RecA-like_BCS1; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR Gene3D; 2.30.29.30; Pleckstrin-homology domain (PH domain)/Phosphotyrosine-binding domain (PTB); 1.
DR InterPro; IPR003593; AAA+_ATPase.
DR InterPro; IPR003959; ATPase_AAA_core.
DR InterPro; IPR014851; BCS1_N.
DR InterPro; IPR024574; ELMO_ARM.
DR InterPro; IPR006816; ELMO_dom.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR011993; PH-like_dom_sf.
DR InterPro; IPR001849; PH_domain.
DR PANTHER; PTHR23070; BCS1 AAA-TYPE ATPASE; 1.
DR PANTHER; PTHR23070:SF232; MITOCHONDRIAL CHAPERONE BCS1; 1.
DR Pfam; PF00004; AAA; 1.
DR Pfam; PF08740; BCS1_N; 1.
DR Pfam; PF11841; ELMO_ARM; 1.
DR Pfam; PF04727; ELMO_CED12; 1.
DR Pfam; PF16457; PH_12; 1.
DR SMART; SM00382; AAA; 1.
DR SMART; SM01024; BCS1_N; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR SUPFAM; SSF50729; PH domain-like; 1.
DR PROSITE; PS51335; ELMO; 1.
PE 3: Inferred from homology;
KW Membrane {ECO:0000256|ARBA:ARBA00022792};
KW Mitochondrion {ECO:0000256|ARBA:ARBA00022792};
KW Mitochondrion inner membrane {ECO:0000256|ARBA:ARBA00022792};
KW Reference proteome {ECO:0000313|Proteomes:UP000194236}.
FT DOMAIN 179..337
FT /note="ELMO"
FT /evidence="ECO:0000259|PROSITE:PS51335"
FT REGION 146..174
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1013 AA; 115572 MW; 9AD6FCF09273FF9B CRC64;
MIADGERRVL ILSLNILESA VLNAAKLFLP IIREQLPIKK LSLLLEHEKF PDIQQNVLAL
INAIIQNQDP SKRRDQFRIF KQTILRYVTD NGSEITHQLY VLQTLLLRSY DEQLNQGATP
EQANEKWREI RRNYDSEMDN LIKNQFNTNS TTTTNQSSNT SSTGGLNRSN STVSNKSNSF
NDALLMLNSN EMIDRFGLLP SKPNGAPATP AEIFADPPGL WILNLLCYYS GKHNESFVRF
IMANQSSSGE TRPYDCPLII ASFRILSLIV EILGIGKPPR DEGHEFYPML LKHEEPLEEF
FSIGLSLFNR TWHEIHATFN DLDIACDFLA EKFHKILANP NATVSFENFQ KELSKISYTE
ISHRWREERL KREQRKEEMP AIQELKRLLL PEMTTIVRDN RLNYLVRGTR FDKYTAKGQR
LKDKFWYCRL SPNHKTLLYG DVDEDCKNLD EKLISKFDIA DVGRLVVGKE CPHMRDSKGK
KTTMSLAFAL IPRDEDSING QQSPPLCFVA GKPEIFDYWI DGLNSLLQHD MISNETKKDV
EMLLDLDVKL RLLDIEGLNI PDQAPDHVYS VKIVVRSCFS SMAIGELIGS LQNNPYFGAG
FGLVGLTAAL AAGRKAAIVA WSGIRRYAFV TCEVNSKGLK MFFVIVFADS EKFEPDKSYQ
WILEWITRQS YRTQHVSMCT EFYEDEAGRI STRFAYIPSP GIHFFRYRGS IFRCERVREQ
MDALAGRPYE VVTLTTLGRD KSIFSFIFDE ARTIALAEAA NKTATYVPFG HEWRVFGQAR
SKRPIDSVIL DDGVAETLVS DVERFLSSAE WYHKRGIPYR RGYLLHGPPG SGKSSFIFAL
AGHLNYSICV LNLSDPSLTD DRLLHLVNTA PKDSLVLLED IDCSVRPRTD DGHPERWEGL
SRVTYSGLLN TLDGVVGSDA RILMMTTNHL ELLDDTITRP GRVDVKVLID DASDRQLKRA
FLRFFPTSSE SDGDEFVRHV RRTYPRPISM ARIQGHFLLH RDDPKAALKQ PIQ
//
