ID A0A0E9NB86_SAICN Unreviewed; 704 AA.
AC A0A0E9NB86;
DT 24-JUN-2015, integrated into UniProtKB/TrEMBL.
DT 24-JUN-2015, sequence version 1.
DT 27-MAR-2024, entry version 39.
DE RecName: Full=proteasome endopeptidase complex {ECO:0000256|ARBA:ARBA00012039};
DE EC=3.4.25.1 {ECO:0000256|ARBA:ARBA00012039};
GN ORFNames=G7K_1316-t1 {ECO:0000313|EMBL:GAO47104.1};
OS Saitoella complicata (strain BCRC 22490 / CBS 7301 / JCM 7358 / NBRC 10748
OS / NRRL Y-17804).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina;
OC Taphrinomycotina incertae sedis; Saitoella.
OX NCBI_TaxID=698492 {ECO:0000313|EMBL:GAO47104.1, ECO:0000313|Proteomes:UP000033140};
RN [1] {ECO:0000313|EMBL:GAO47104.1, ECO:0000313|Proteomes:UP000033140}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NRRL Y-17804 {ECO:0000313|EMBL:GAO47104.1,
RC ECO:0000313|Proteomes:UP000033140};
RX PubMed=21914972; DOI=10.2323/jgam.57.243;
RA Nishida H., Hamamoto M., Sugiyama J.;
RT "Draft genome sequencing of the enigmatic yeast Saitoella complicata.";
RL J. Gen. Appl. Microbiol. 57:243-246(2011).
RN [2] {ECO:0000313|EMBL:GAO47104.1, ECO:0000313|Proteomes:UP000033140}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NRRL Y-17804 {ECO:0000313|EMBL:GAO47104.1,
RC ECO:0000313|Proteomes:UP000033140};
RX PubMed=24646756; DOI=10.2323/jgam.60.7;
RA Nishida H., Matsumoto T., Kondo S., Hamamoto M., Yoshikawa H.;
RT "The early diverging ascomycetous budding yeast Saitoella complicata has
RT three histone deacetylases belonging to the Clr6, Hos2, and Rpd3
RT lineages.";
RL J. Gen. Appl. Microbiol. 60:7-12(2014).
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: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
CC Nucleus {ECO:0000256|ARBA:ARBA00004123}.
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:GAO47104.1}.
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DR EMBL; BACD03000007; GAO47104.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0E9NB86; -.
DR STRING; 698492.A0A0E9NB86; -.
DR Proteomes; UP000033140; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0019774; C:proteasome core complex, beta-subunit complex; IEA:UniProt.
DR GO; GO:0019901; F:protein kinase binding; IEA:InterPro.
DR GO; GO:0004298; F:threonine-type endopeptidase activity; IEA:InterPro.
DR GO; GO:0043161; P:proteasome-mediated ubiquitin-dependent protein catabolic process; IEA:UniProt.
DR CDD; cd20558; CYCLIN_ScPCL7-like; 1.
DR CDD; cd03762; proteasome_beta_type_6; 1.
DR Gene3D; 1.10.472.10; Cyclin-like; 1.
DR Gene3D; 3.60.20.10; Glutamine Phosphoribosylpyrophosphate, subunit 1, domain 1; 1.
DR InterPro; IPR013922; Cyclin_PHO80-like.
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 PANTHER; PTHR32194; METALLOPROTEASE TLDD; 1.
DR PANTHER; PTHR32194:SF8; PROTEASOME SUBUNIT BETA; 1.
DR Pfam; PF08613; Cyclin; 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 4: Predicted;
KW Proteasome {ECO:0000256|ARBA:ARBA00022942};
KW Reference proteome {ECO:0000313|Proteomes:UP000033140}.
FT REGION 240..272
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 316..465
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 249..272
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 344..386
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 387..405
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 414..463
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 25
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PIRSR:PIRSR600243-1"
SQ SEQUENCE 704 AA; 77472 MW; 7313C6A4F0EECB7A CRC64;
MSATEVPGLH VDIAALKAGE VDLGTTIMAV KFKEGVIIAA DSRTTTGSYI ANRVTDKLTQ
LHDTIWCCRS GSAADTQAIA DIVHYYLQMY AVTAQRPTTK VAASMLQELC YTNKDGLSAG
LIVAGYDHRR GGEVYSIPLG GSIHKQDFAI GGSGSTYIYG FCDANYKEDM SKEEAMQFVK
SAVALAMSRD GSSGGVIRMA VITETGVDRS FYTQDDPVNT IPRFWEKSFA TPALVRCKPR
VNNASQPDRS CENERHREKQ KTSTGHHSDR QAVRRLFNQV LHESLHSGPA YIPLPRCSDG
PLHRMQVTHS PVLTATSTRP NLKRGSSAMS VACSPRHHPH PSPSLRSASY TSASMSPALV
PAATTPKTRT VQTPVCTGQV QSDKVTTNRP EVERYDSDSF KHPADPRRVV STAAAEMPQS
TNIPMGQESQ VSTTGEASQT TESNVERTDT ENTASSTKIP STPEQLPVAE PHLDLAHHPM
PDLLMMLATI LHKITSANDS MHYPHPRNIS NAHRSSPLLA FHARNVPSIS IHAYLTRILK
YCPTTNEVFL SLLVYFDRMS RRTNPQFYAG GEGIVQGEQQ PVFAIDSYNV HRLIIAGITV
ASKFFSDVFY TNSRYAKVGG LPLSELNHLE LQFLILNDFR LMIPLEELQR YGDQLLRFWA
SRDDGTVQSP APPTPQPGIP AGYMNAMPRQ VASYNGQENM HERD
//