ID A0A2U9R3W8_PICKU Unreviewed; 264 AA.
AC A0A2U9R3W8;
DT 12-SEP-2018, integrated into UniProtKB/TrEMBL.
DT 12-SEP-2018, sequence version 1.
DT 27-MAR-2024, entry version 21.
DE RecName: Full=Proteasome alpha-type subunits domain-containing protein {ECO:0000259|PROSITE:PS00388};
GN ORFNames=C5L36_0B10165 {ECO:0000313|EMBL:AWU75779.1};
OS Pichia kudriavzevii (Yeast) (Issatchenkia orientalis).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Pichiaceae; Pichia.
OX NCBI_TaxID=4909 {ECO:0000313|EMBL:AWU75779.1, ECO:0000313|Proteomes:UP000249293};
RN [1] {ECO:0000313|EMBL:AWU75779.1, ECO:0000313|Proteomes:UP000249293}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS573 {ECO:0000313|EMBL:AWU75779.1,
RC ECO:0000313|Proteomes:UP000249293};
RA Douglass A.P., Offei B., Braun-Galleani S., Coughlan A.Y., Martos A.,
RA Ortiz-Merino R.A., Byrne K.P., Wolfe K.H.;
RT "Population genomics shows no distinction between pathogenic Candida krusei
RT and environmental Pichia kudriavzevii: One species, four names.";
RL Submitted (JUN-2018) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: The proteasome degrades poly-ubiquitinated proteins in the
CC cytoplasm and in the nucleus. It is essential for the regulated
CC turnover of proteins and for the removal of misfolded proteins. The
CC proteasome is a multicatalytic proteinase complex that is characterized
CC by its ability to cleave peptides with Arg, Phe, Tyr, Leu, and Glu
CC adjacent to the leaving group at neutral or slightly basic pH. It has
CC an ATP-dependent proteolytic activity. {ECO:0000256|ARBA:ARBA00003542}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
CC Nucleus {ECO:0000256|ARBA:ARBA00004123}.
CC -!- SIMILARITY: Belongs to the peptidase T1A family. {ECO:0000256|PROSITE-
CC ProRule:PRU00808}.
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DR EMBL; CP028774; AWU75779.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2U9R3W8; -.
DR STRING; 4909.A0A2U9R3W8; -.
DR VEuPathDB; FungiDB:C5L36_0B10165; -.
DR OrthoDB; 77945at2759; -.
DR Proteomes; UP000249293; Chromosome 2.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0019773; C:proteasome core complex, alpha-subunit complex; IEA:UniProtKB-UniRule.
DR GO; GO:0010499; P:proteasomal ubiquitin-independent protein catabolic process; IEA:UniProt.
DR GO; GO:0043161; P:proteasome-mediated ubiquitin-dependent protein catabolic process; IEA:UniProt.
DR CDD; cd03751; proteasome_alpha_type_3; 1.
DR Gene3D; 3.60.20.10; Glutamine Phosphoribosylpyrophosphate, subunit 1, domain 1; 1.
DR InterPro; IPR029055; Ntn_hydrolases_N.
DR InterPro; IPR023332; Proteasome_alpha-type.
DR InterPro; IPR000426; Proteasome_asu_N.
DR InterPro; IPR001353; Proteasome_sua/b.
DR PANTHER; PTHR11599:SF10; PROTEASOME SUBUNIT ALPHA TYPE-3; 1.
DR PANTHER; PTHR11599; PROTEASOME SUBUNIT ALPHA/BETA; 1.
DR Pfam; PF00227; Proteasome; 1.
DR Pfam; PF10584; Proteasome_A_N; 1.
DR SMART; SM00948; Proteasome_A_N; 1.
DR SUPFAM; SSF56235; N-terminal nucleophile aminohydrolases (Ntn hydrolases); 1.
DR PROSITE; PS00388; PROTEASOME_ALPHA_1; 1.
DR PROSITE; PS51475; PROTEASOME_ALPHA_2; 1.
PE 3: Inferred from homology;
KW Proteasome {ECO:0000256|ARBA:ARBA00022942, ECO:0000256|PROSITE-
KW ProRule:PRU00808}; Reference proteome {ECO:0000313|Proteomes:UP000249293}.
FT DOMAIN 8..30
FT /note="Proteasome alpha-type subunits"
FT /evidence="ECO:0000259|PROSITE:PS00388"
FT REGION 238..264
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 264 AA; 28870 MW; CDF46B303FC86945 CRC64;
MTSIGTGYDL SNSVFSPDGR NFQVEYASKA VENAGTSIGI KCKDGVILAT EKIITSKLLV
PGKNKRIQSI DRHVGVVYSG LIPDGRHLVN RGRDEAQSFK SLYKEPMGLE GLISRLGYYV
QAYTCYNSVR PFGINAIIGG VDDDGAHLYM LEPSGVYWGY LGAATGKGRQ AAKAELEKLD
LPNISARQAV KEAARIIHLV HEDNKDKDYE LEITWVSKSE TNGLHKFVPE ELLDEAKKFA
EQAAEGGSDS DSDSDSSSDE EMEK
//
