ID L5LD72_MYODS Unreviewed; 385 AA.
AC L5LD72;
DT 06-MAR-2013, integrated into UniProtKB/TrEMBL.
DT 06-MAR-2013, sequence version 1.
DT 27-MAR-2024, entry version 43.
DE SubName: Full=26S protease regulatory subunit 6A {ECO:0000313|EMBL:ELK23831.1};
GN ORFNames=MDA_GLEAN10019074 {ECO:0000313|EMBL:ELK23831.1};
OS Myotis davidii (David's myotis).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Chiroptera; Microchiroptera; Vespertilionidae;
OC Myotis.
OX NCBI_TaxID=225400 {ECO:0000313|EMBL:ELK23831.1, ECO:0000313|Proteomes:UP000010556};
RN [1] {ECO:0000313|Proteomes:UP000010556}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=23258410; DOI=10.1126/science.1230835;
RA Zhang G., Cowled C., Shi Z., Huang Z., Bishop-Lilly K.A., Fang X.,
RA Wynne J.W., Xiong Z., Baker M.L., Zhao W., Tachedjian M., Zhu Y., Zhou P.,
RA Jiang X., Ng J., Yang L., Wu L., Xiao J., Feng Y., Chen Y., Sun X.,
RA Zhang Y., Marsh G.A., Crameri G., Broder C.C., Frey K.G., Wang L.F.,
RA Wang J.;
RT "Comparative analysis of bat genomes provides insight into the evolution of
RT flight and immunity.";
RL Science 339:456-460(2013).
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
CC Nucleus {ECO:0000256|ARBA:ARBA00004123}.
CC -!- SIMILARITY: Belongs to the AAA ATPase family.
CC {ECO:0000256|ARBA:ARBA00006914, ECO:0000256|RuleBase:RU003651}.
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DR EMBL; KB113178; ELK23831.1; -; Genomic_DNA.
DR AlphaFoldDB; L5LD72; -.
DR eggNOG; KOG0652; Eukaryota.
DR Proteomes; UP000010556; Unassembled WGS sequence.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0000502; C:proteasome complex; IEA:UniProtKB-KW.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR GO; GO:0008233; F:peptidase activity; IEA:UniProtKB-KW.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR Gene3D; 1.10.8.60; -; 1.
DR Gene3D; 2.40.50.140; Nucleic acid-binding proteins; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR InterPro; IPR003593; AAA+_ATPase.
DR InterPro; IPR041569; AAA_lid_3.
DR InterPro; IPR003959; ATPase_AAA_core.
DR InterPro; IPR003960; ATPase_AAA_CS.
DR InterPro; IPR012340; NA-bd_OB-fold.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR032501; Prot_ATP_ID_OB_2nd.
DR PANTHER; PTHR23073; 26S PROTEASOME REGULATORY SUBUNIT; 1.
DR PANTHER; PTHR23073:SF7; 26S PROTEASOME REGULATORY SUBUNIT 6A; 1.
DR Pfam; PF00004; AAA; 1.
DR Pfam; PF17862; AAA_lid_3; 1.
DR Pfam; PF16450; Prot_ATP_ID_OB_C; 1.
DR SMART; SM00382; AAA; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR PROSITE; PS00674; AAA; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|RuleBase:RU003651};
KW Hydrolase {ECO:0000313|EMBL:ELK23831.1};
KW Nucleotide-binding {ECO:0000256|RuleBase:RU003651};
KW Protease {ECO:0000313|EMBL:ELK23831.1};
KW Proteasome {ECO:0000256|ARBA:ARBA00022942};
KW Reference proteome {ECO:0000313|Proteomes:UP000010556}.
FT DOMAIN 165..304
FT /note="AAA+ ATPase"
FT /evidence="ECO:0000259|SMART:SM00382"
SQ SEQUENCE 385 AA; 42992 MW; BC037A40B9D9BB49 CRC64;
MKSEVLRVTH ELQAMKDKIK ENSEKIKVNK TLPYLVSNVI ELLDVDPNDQ EEDGANIDLD
SQRKGKCAVI KTSTRQTYFL PVIGLVDAEK LKPGDLVGVN KDSYLILETL PTEYDSRVKA
MEVDERPTEQ YSDIGGLDKQ IQELVEAIVL PMNHKEKFEN LGIQPPKGVL MYGPPGTGKT
LLARACAAQT KATFLKLAGP QLVQMFIGDG AKLVRDAFAL AKEKAPSIIF IDELDAIGTK
RFDSEKAGDR EVQRTMLELL NQLDGFQPNT QVKVIAATNR VDILDPALLR SGRLDRKIEF
PMPNEEARAR IMQIHSRKMN VSPDVNYEEL ARCTDDFNGA QCKAVCVEAG MIALRRGATE
LTHEDYMEGI LEVQAKKKAN LQYYA
//
