ID A0A0N4XZF3_NIPBR Unreviewed; 252 AA.
AC A0A0N4XZF3;
DT 09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT 09-DEC-2015, sequence version 1.
DT 27-MAR-2024, entry version 32.
DE RecName: Full=proteasome endopeptidase complex {ECO:0000256|ARBA:ARBA00012039};
DE EC=3.4.25.1 {ECO:0000256|ARBA:ARBA00012039};
GN ORFNames=NBR_LOCUS8552 {ECO:0000313|EMBL:VDL72141.1};
OS Nippostrongylus brasiliensis (Rat hookworm).
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Strongyloidea; Heligmosomidae; Nippostrongylus.
OX NCBI_TaxID=27835 {ECO:0000313|Proteomes:UP000038043, ECO:0000313|WBParaSite:NBR_0000855101-mRNA-1};
RN [1] {ECO:0000313|WBParaSite:NBR_0000855101-mRNA-1}
RP IDENTIFICATION.
RG WormBaseParasite;
RL Submitted (FEB-2017) to UniProtKB.
RN [2] {ECO:0000313|EMBL:VDL72141.1, ECO:0000313|Proteomes:UP000271162}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RG Pathogen Informatics;
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}.
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DR EMBL; UYSL01020020; VDL72141.1; -; Genomic_DNA.
DR STRING; 27835.A0A0N4XZF3; -.
DR WBParaSite; NBR_0000855101-mRNA-1; NBR_0000855101-mRNA-1; NBR_0000855101.
DR OMA; GELHYAY; -.
DR Proteomes; UP000038043; Unplaced.
DR Proteomes; UP000271162; 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 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; IPR001353; Proteasome_sua/b.
DR InterPro; IPR023333; Proteasome_suB-type.
DR PANTHER; PTHR32194:SF0; ATP-DEPENDENT PROTEASE SUBUNIT HSLV; 1.
DR PANTHER; PTHR32194; METALLOPROTEASE TLDD; 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 Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Protease {ECO:0000256|ARBA:ARBA00022670};
KW Reference proteome {ECO:0000313|Proteomes:UP000271162};
KW Zymogen {ECO:0000256|ARBA:ARBA00023145}.
FT ACT_SITE 64
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PIRSR:PIRSR600243-1"
SQ SEQUENCE 252 AA; 27633 MW; 845B20240C0ECEA2 CRC64;
MWGCGFDEHD EETADIAVIK QQFLHEPVPS SFAFPQPPLG IQAKDFVATH FGKDAKNMQF
RKGTTTLGFI YEPATSNDKG GIIIAVDSRA SSGEYISSKS VMKILDIGDH MVATMAGGAA
DCQFWTRTVA KYCNLFELRE KTQITVSAAS KYFANVLYGY RGMGLSVGSM IAGYDKRGPQ
IFKVDSDGDR SQMKICSVGS GSLNAYGILD THYKPKMTDE EAMKLGRRAI MHATYRDSGS
GGVCNCKLYY IQ
//
