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Database: UniProt
Entry: A0A443SCU9_9ACAR
LinkDB: A0A443SCU9_9ACAR
Original site: A0A443SCU9_9ACAR 
ID   A0A443SCU9_9ACAR        Unreviewed;       448 AA.
AC   A0A443SCU9;
DT   08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT   08-MAY-2019, sequence version 1.
DT   27-MAR-2024, entry version 24.
DE   SubName: Full=26S protease regulatory subunit 4-like protein {ECO:0000313|EMBL:RWS25352.1};
GN   ORFNames=B4U80_11479 {ECO:0000313|EMBL:RWS25352.1};
OS   Leptotrombidium deliense.
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Chelicerata; Arachnida; Acari;
OC   Acariformes; Trombidiformes; Prostigmata; Anystina; Parasitengona;
OC   Trombiculoidea; Trombiculidae; Leptotrombidium.
OX   NCBI_TaxID=299467 {ECO:0000313|EMBL:RWS25352.1, ECO:0000313|Proteomes:UP000288716};
RN   [1] {ECO:0000313|EMBL:RWS25352.1, ECO:0000313|Proteomes:UP000288716}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=UoL-UT {ECO:0000313|EMBL:RWS25352.1};
RA   Dong X., Chaisiri K., Xia D., Armstrong S.D., Fang Y., Donnelly M.J.,
RA   Kadowaki T., McGarry J.W., Darby A.C., Makepeace B.L.;
RT   "Genomes of trombidid mites reveal novel predicted allergens and laterally-
RT   transferred genes associated with secondary metabolism.";
RL   Gigascience 0:0-0(2018).
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
CC   -!- SIMILARITY: Belongs to the AAA ATPase family.
CC       {ECO:0000256|ARBA:ARBA00006914, ECO:0000256|RuleBase:RU003651}.
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:RWS25352.1}.
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DR   EMBL; NCKV01003796; RWS25352.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A443SCU9; -.
DR   STRING; 299467.A0A443SCU9; -.
DR   EnsemblMetazoa; LDEU006689-RA; LDEU006689-PA; LDEU006689.
DR   VEuPathDB; VectorBase:LDEU006689; -.
DR   Proteomes; UP000288716; Unassembled WGS sequence.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
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   CDD; cd19502; RecA-like_PAN_like; 1.
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:SF24; 26S PROTEASOME REGULATORY SUBUNIT 4; 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:RWS25352.1};
KW   Nucleotide-binding {ECO:0000256|RuleBase:RU003651};
KW   Protease {ECO:0000313|EMBL:RWS25352.1};
KW   Proteasome {ECO:0000256|ARBA:ARBA00022942};
KW   Reference proteome {ECO:0000313|Proteomes:UP000288716}.
FT   DOMAIN          226..365
FT                   /note="AAA+ ATPase"
FT                   /evidence="ECO:0000259|SMART:SM00382"
FT   REGION          1..57
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          90..113
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..17
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        18..33
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        90..110
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   448 AA;  49862 MW;  0913618D42D2235E CRC64;
     MGNNQSGSGS GSGSGSDGQK DKSKKRDRPA APPPSRGGRR YGKRSKGPDA ASKLPGVTPH
     TRCRLKLLKL ERIHDWLLME EEFLKNSKIA QQEKAENEDE NDERNKVDDL RGTPMSVGNL
     EEIIDDVHAI VSTSVGSEHY VSILSFVDKD RLEPNCSVLL NHKVHAVVGV LSDDTDPMVN
     VMKLEKAPQE TYADIGGLDQ QIQEIKESVE LPLTHPEYYE EMGIKPPKGV ILYGPPGTGK
     TLLAKAVANQ TSATFLRVVG SELIQKYLGD GPKLVRDLFR VAEEHAPSIV FIDEIDAIGT
     KRYDSNSGGE REIQRTMLEL LNQLDGFDSR GDVKVVMATN RIETLDPALI RPGRIDRKIE
     FPLPDEKTKR RIFTIHTSRM TLSEDVNFDD IVLTKDDLSG ADIKAICTEA GLMALRERRM
     KVTNEDFKKS KDNVLYRKKE GTPEGLYL
//
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