ID A0A3S3P9I2_9ACAR Unreviewed; 274 AA.
AC A0A3S3P9I2;
DT 10-APR-2019, integrated into UniProtKB/TrEMBL.
DT 10-APR-2019, sequence version 1.
DT 27-MAR-2024, entry version 21.
DE RecName: Full=proteasome endopeptidase complex {ECO:0000256|ARBA:ARBA00012039};
DE EC=3.4.25.1 {ECO:0000256|ARBA:ARBA00012039};
GN ORFNames=B4U79_00664 {ECO:0000313|EMBL:RWS06165.1}, B4U79_09564
GN {ECO:0000313|EMBL:RWS10745.1}, B4U79_15321
GN {ECO:0000313|EMBL:RWS10747.1};
OS Dinothrombium tinctorium.
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Chelicerata; Arachnida; Acari;
OC Acariformes; Trombidiformes; Prostigmata; Anystina; Parasitengona;
OC Trombidioidea; Trombidiidae; Dinothrombium.
OX NCBI_TaxID=1965070 {ECO:0000313|EMBL:RWS10745.1, ECO:0000313|Proteomes:UP000285301};
RN [1] {ECO:0000313|EMBL:RWS10745.1, ECO:0000313|Proteomes:UP000285301}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=UoL-WK {ECO:0000313|EMBL:RWS10745.1};
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).
RN [2] {ECO:0000313|EMBL:RWS10745.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=UoL-WK {ECO:0000313|EMBL:RWS10745.1};
RA Dong X.;
RT "Trombidioid mite genomics.";
RL Submitted (NOV-2018) to the EMBL/GenBank/DDBJ databases.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Cleavage of peptide bonds with very broad specificity.;
CC EC=3.4.25.1; Evidence={ECO:0000256|ARBA:ARBA00001198};
CC -!- SUBUNIT: The 26S proteasome consists of a 20S proteasome core and two
CC 19S regulatory subunits. The 20S proteasome core is composed of 28
CC subunits that are arranged in four stacked rings, resulting in a
CC barrel-shaped structure. The two end rings are each formed by seven
CC alpha subunits, and the two central rings are each formed by seven beta
CC subunits. The catalytic chamber with the active sites is on the inside
CC of the barrel. {ECO:0000256|ARBA:ARBA00026071}.
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:RWS10745.1}.
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DR EMBL; NCKU01004300; RWS06165.1; -; Genomic_DNA.
DR EMBL; NCKU01001978; RWS10745.1; -; Genomic_DNA.
DR EMBL; NCKU01001977; RWS10747.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A3S3P9I2; -.
DR STRING; 1965070.A0A3S3P9I2; -.
DR Proteomes; UP000285301; Unassembled WGS sequence.
DR GO; GO:0005839; C:proteasome core complex; IEA:InterPro.
DR GO; GO:0004298; F:threonine-type endopeptidase activity; IEA:InterPro.
DR GO; GO:0051603; P:proteolysis involved in protein catabolic process; IEA:InterPro.
DR CDD; cd03763; proteasome_beta_type_7; 1.
DR Gene3D; 3.60.20.10; Glutamine Phosphoribosylpyrophosphate, subunit 1, domain 1; 1.
DR InterPro; IPR029055; Ntn_hydrolases_N.
DR InterPro; IPR000243; Pept_T1A_subB.
DR InterPro; IPR024689; Proteasome_bsu_C.
DR InterPro; IPR001353; Proteasome_sua/b.
DR InterPro; IPR023333; Proteasome_suB-type.
DR PANTHER; PTHR32194; METALLOPROTEASE TLDD; 1.
DR PANTHER; PTHR32194:SF4; PROTEASOME SUBUNIT BETA TYPE-7; 1.
DR Pfam; PF12465; Pr_beta_C; 1.
DR Pfam; PF00227; Proteasome; 1.
DR PRINTS; PR00141; PROTEASOME.
DR SUPFAM; SSF56235; N-terminal nucleophile aminohydrolases (Ntn hydrolases); 1.
DR PROSITE; PS51476; PROTEASOME_BETA_2; 1.
PE 4: Predicted;
KW Proteasome {ECO:0000313|EMBL:RWS10745.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000285301}.
FT DOMAIN 229..260
FT /note="Proteasome beta subunit C-terminal"
FT /evidence="ECO:0000259|Pfam:PF12465"
FT ACT_SITE 38
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PIRSR:PIRSR600243-1"
SQ SEQUENCE 274 AA; 29998 MW; F6971FA4DECA788F CRC64;
MALLPDLPKG GFVFENFQRN EFLKAKGFRA PKATKTGTTI VGCLVKDGVI LGADTRATSG
SVIADKYSDK IHYMAKNIYC CGAGTAADTL YVTRMVSSNL ELHRLNTNRV VPVICALRML
KQHLFRYQGY VSAALVLAGV DEDGAHLYSV TPHGSSDKLP FTTMGSGSLA AMAVFETRWK
PNMTIEEGKK LVRDSVAAGI FNDLGSGNNI DMCIITRDGV DYMRPYEEAN LKGQRLNSYV
FDKGATPILT VHTIPLEVEE VMVRHMDETM DTSA
//
