ID C0JW56_ORYLU Unreviewed; 275 AA.
AC C0JW56;
DT 05-MAY-2009, integrated into UniProtKB/TrEMBL.
DT 05-MAY-2009, sequence version 1.
DT 27-MAR-2024, entry version 47.
DE RecName: Full=Proteasome subunit beta {ECO:0000256|RuleBase:RU004203};
GN Name=PSMB10 {ECO:0000313|EMBL:ACN49172.1};
OS Oryzias luzonensis (Luzon ricefish).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Ovalentaria; Atherinomorphae; Beloniformes; Adrianichthyidae; Oryziinae;
OC Oryzias.
OX NCBI_TaxID=104659 {ECO:0000313|EMBL:ACN49172.1};
RN [1] {ECO:0000313|EMBL:ACN49172.1}
RP NUCLEOTIDE SEQUENCE.
RX PubMed=19350233; DOI=10.1007/s00251-009-0371-1;
RA Mehta R.B., Nonaka M.I., Nonaka M.;
RT "Comparative genomic analysis of the major histocompatibility complex class
RT I region in the teleost genus Oryzias.";
RL Immunogenetics 61:385-399(2009).
CC -!- FUNCTION: Component of the proteasome, a multicatalytic proteinase
CC complex which is characterized by its ability to cleave peptides with
CC Arg, Phe, Tyr, Leu, and Glu adjacent to the leaving group at neutral or
CC slightly basic pH. The proteasome has an ATP-dependent proteolytic
CC activity. {ECO:0000256|RuleBase:RU004203}.
CC -!- FUNCTION: The proteasome is a multicatalytic proteinase complex which
CC is characterized by its ability to cleave peptides with Arg, Phe, Tyr,
CC Leu, and Glu adjacent to the leaving group at neutral or slightly basic
CC pH. The proteasome has an ATP-dependent proteolytic activity. This
CC subunit is involved in antigen processing to generate class I binding
CC peptides. {ECO:0000256|ARBA:ARBA00025456}.
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: Component of the proteasome complex.
CC {ECO:0000256|RuleBase:RU004203}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|RuleBase:RU004203}.
CC Nucleus {ECO:0000256|RuleBase:RU004203}.
CC -!- SIMILARITY: Belongs to the peptidase T1B family.
CC {ECO:0000256|RuleBase:RU004203}.
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DR EMBL; FJ481085; ACN49172.1; -; Genomic_DNA.
DR AlphaFoldDB; C0JW56; -.
DR MEROPS; T01.A02; -.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
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; IPR016050; Proteasome_bsu_CS.
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; PS00854; PROTEASOME_BETA_1; 1.
DR PROSITE; PS51476; PROTEASOME_BETA_2; 1.
PE 3: Inferred from homology;
KW Cytoplasm {ECO:0000256|RuleBase:RU004203};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242, ECO:0000256|RuleBase:RU004203};
KW Proteasome {ECO:0000256|ARBA:ARBA00022942, ECO:0000256|RuleBase:RU004203}.
FT DOMAIN 236..268
FT /note="Proteasome beta subunit C-terminal"
FT /evidence="ECO:0000259|Pfam:PF12465"
FT ACT_SITE 42
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PIRSR:PIRSR600243-1"
SQ SEQUENCE 275 AA; 29683 MW; BA64D2E2620118E3 CRC64;
MALSNVLDSP AAGFNFDNAA RNAAFEGLFE GGQTPKPLKT GTTIAGVVFK DGVVLGADTR
ATSSEVVADK MCAKIHYISP NIYCCGAGTA ADTEKTTDLL SSNLTVFSLN SGRNPRVVMA
VNILQDMLYR YHGQIGANLI LGGVDCTGNH LYTVGPYGSV NKVPYLAMGS GDLAALGILE
DRFKHDLELE KAKELVRDAI HAGIMSDLGS GNNIDICVIT KQGVDYIRPF QESEYKETRK
PKYKYRPGTT PVLTKKVVPL KLEVVEETQQ RMDTA
//
