ID A0A1J1IEI9_9DIPT Unreviewed; 488 AA.
AC A0A1J1IEI9;
DT 15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT 15-FEB-2017, sequence version 1.
DT 27-MAR-2024, entry version 23.
DE RecName: Full=proteasome endopeptidase complex {ECO:0000256|ARBA:ARBA00012039};
DE EC=3.4.25.1 {ECO:0000256|ARBA:ARBA00012039};
GN ORFNames=CLUMA_CG011989 {ECO:0000313|EMBL:CRK98632.1};
OS Clunio marinus.
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Nematocera; Chironomoidea; Chironomidae;
OC Clunio.
OX NCBI_TaxID=568069 {ECO:0000313|EMBL:CRK98632.1, ECO:0000313|Proteomes:UP000183832};
RN [1] {ECO:0000313|EMBL:CRK98632.1, ECO:0000313|Proteomes:UP000183832}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Syromyatnikov M.Y., Popov V.N.;
RL Submitted (APR-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Non-catalytic component of the proteasome, a multicatalytic
CC proteinase complex which is characterized by its ability to cleave
CC peptides with Arg, Phe, Tyr, Leu, and Glu adjacent to the leaving group
CC at neutral or slightly basic pH. The proteasome has an ATP-dependent
CC proteolytic activity. {ECO:0000256|ARBA:ARBA00024953}.
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 -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004370}.
CC Mitochondrion outer membrane {ECO:0000256|ARBA:ARBA00004294}. Nucleus
CC {ECO:0000256|ARBA:ARBA00004123}.
CC -!- SIMILARITY: Belongs to the metaxin family.
CC {ECO:0000256|ARBA:ARBA00009170}.
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DR EMBL; CVRI01000048; CRK98632.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1J1IEI9; -.
DR STRING; 568069.A0A1J1IEI9; -.
DR OrthoDB; 2897805at2759; -.
DR Proteomes; UP000183832; Unassembled WGS sequence.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0005839; C:proteasome core complex; IEA:InterPro.
DR GO; GO:0001401; C:SAM 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; cd03211; GST_C_Metaxin2; 1.
DR CDD; cd03761; proteasome_beta_type_5; 1.
DR Gene3D; 1.20.1050.10; -; 1.
DR Gene3D; 3.60.20.10; Glutamine Phosphoribosylpyrophosphate, subunit 1, domain 1; 1.
DR InterPro; IPR036282; Glutathione-S-Trfase_C_sf.
DR InterPro; IPR033468; Metaxin_GST.
DR InterPro; IPR029055; Ntn_hydrolases_N.
DR InterPro; IPR000243; Pept_T1A_subB.
DR InterPro; IPR016050; Proteasome_bsu_CS.
DR InterPro; IPR001353; Proteasome_sua/b.
DR InterPro; IPR023333; Proteasome_suB-type.
DR InterPro; IPR019564; Sam37/metaxin_N.
DR PANTHER; PTHR32194:SF0; ATP-DEPENDENT PROTEASE SUBUNIT HSLV; 1.
DR PANTHER; PTHR32194; METALLOPROTEASE TLDD; 1.
DR Pfam; PF17171; GST_C_6; 1.
DR Pfam; PF00227; Proteasome; 1.
DR Pfam; PF10568; Tom37; 1.
DR PRINTS; PR00141; PROTEASOME.
DR SUPFAM; SSF47616; GST C-terminal domain-like; 1.
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|ARBA:ARBA00022490};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Protease {ECO:0000256|ARBA:ARBA00022670};
KW Proteasome {ECO:0000256|ARBA:ARBA00022942};
KW Reference proteome {ECO:0000313|Proteomes:UP000183832};
KW Zymogen {ECO:0000256|ARBA:ARBA00023145}.
FT DOMAIN 265..389
FT /note="Mitochondrial outer membrane transport complex
FT Sam37/metaxin N-terminal"
FT /evidence="ECO:0000259|Pfam:PF10568"
FT DOMAIN 414..478
FT /note="Metaxin glutathione S-transferase"
FT /evidence="ECO:0000259|Pfam:PF17171"
FT ACT_SITE 67
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PIRSR:PIRSR600243-1"
SQ SEQUENCE 488 AA; 55384 MW; 14EAB8F943B62050 CRC64;
MALNDILKQM PSMGYDFKDF APSEELDFES FQNNRVLAVP PYNNPSANLA KLQEGKDDIK
IQFDHGTTTL GFIYQGGVVL AVDSRATGGQ YIGSQSVRKV VEINDLLLGT LAGGAADCTY
WYRVLTSECR LYELRNKKKI SLAAATKIMN NIIYSYKNSG LSMGMILAGG DMKQVSLYYL
DSDGTRTTGK VFSVGSGSLF AYGVLDSGYR WDLTDEEAHE LGRRSIYHAT YRDAYSGEKV
EMNEKIIIYQ PYEAEQILLA ENASCLAVKT YLKMLGRDFL VKSCANAEFM APSGKRTKLP
VVQIGEFLAA EFEPIINLME YKKLSLTENF SNEDKDDLVT HMSLVDSILP NAELYITWCS
EVVLNEITKK RYGFVYPFPL NHIQNFRKRR AVLKQLNFYD WKNLTFDEVV ERVDKLCQSL
VMKLKDQEFF FGDKPSELDA LVFGHLFCIF TMELPASVSS LKETINKYIT LTQFCARIEK
KYFGKIKN
//
