ID I2H340_TETBL Unreviewed; 258 AA.
AC I2H340;
DT 11-JUL-2012, integrated into UniProtKB/TrEMBL.
DT 11-JUL-2012, sequence version 1.
DT 24-JAN-2024, entry version 47.
DE RecName: Full=Proteasome alpha-type subunits domain-containing protein {ECO:0000259|PROSITE:PS00388};
GN Name=TBLA0D02920 {ECO:0000313|EMBL:CCH60792.1};
GN ORFNames=TBLA_0D02920 {ECO:0000313|EMBL:CCH60792.1};
OS Tetrapisispora blattae (strain ATCC 34711 / CBS 6284 / DSM 70876 / NBRC
OS 10599 / NRRL Y-10934 / UCD 77-7) (Yeast) (Kluyveromyces blattae).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Tetrapisispora.
OX NCBI_TaxID=1071380 {ECO:0000313|EMBL:CCH60792.1, ECO:0000313|Proteomes:UP000002866};
RN [1] {ECO:0000313|EMBL:CCH60792.1, ECO:0000313|Proteomes:UP000002866}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 34711 / CBS 6284 / DSM 70876 / NBRC 10599 / NRRL Y-10934 /
RC UCD 77-7 {ECO:0000313|Proteomes:UP000002866};
RX PubMed=22123960; DOI=10.1073/pnas.1112808108;
RA Gordon J.L., Armisen D., Proux-Wera E., OhEigeartaigh S.S., Byrne K.P.,
RA Wolfe K.H.;
RT "Evolutionary erosion of yeast sex chromosomes by mating-type switching
RT accidents.";
RL Proc. Natl. Acad. Sci. U.S.A. 108:20024-20029(2011).
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 -!- SIMILARITY: Belongs to the peptidase T1A family. {ECO:0000256|PROSITE-
CC ProRule:PRU00808}.
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DR EMBL; HE806319; CCH60792.1; -; Genomic_DNA.
DR RefSeq; XP_004180311.1; XM_004180263.1.
DR AlphaFoldDB; I2H340; -.
DR STRING; 1071380.I2H340; -.
DR GeneID; 14495828; -.
DR KEGG; tbl:TBLA_0D02920; -.
DR eggNOG; KOG0178; Eukaryota.
DR HOGENOM; CLU_035750_4_3_1; -.
DR InParanoid; I2H340; -.
DR OMA; YVLNDNM; -.
DR OrthoDB; 166567at2759; -.
DR Proteomes; UP000002866; Chromosome 4.
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 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:SF13; PROTEASOME SUBUNIT ALPHA TYPE-4; 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:UP000002866}.
FT DOMAIN 6..28
FT /note="Proteasome alpha-type subunits"
FT /evidence="ECO:0000259|PROSITE:PS00388"
SQ SEQUENCE 258 AA; 28998 MW; F9F0AD43CBA1C9D4 CRC64;
MGSRRYDSRT TIFSPEGRLY QVEYALESIS HAGTSIGIMS KDGIVLLAER KITSKLLEQD
ILNEKLYKLS DKITLAVAGL TADAEILINI ARQFAQNYLM TYNEEIPVEI LVKKLSDIKQ
SYTQHGGLRP FGVSFIYAGY DDILGPQLYT SNPSGNYTGW KAISIGANTS AAQTLLQMDY
KDDMNLNDAM ELGLKTLSKT TDSSNLTYDR VELSIIKIDK ENDNKIIQKI YNPAEIKQLL
IKFGINKKND EDEDVEMK
//