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Database: UniProt
Entry: A0A1Y2E1R0_9PEZI
LinkDB: A0A1Y2E1R0_9PEZI
Original site: A0A1Y2E1R0_9PEZI 
ID   A0A1Y2E1R0_9PEZI        Unreviewed;       254 AA.
AC   A0A1Y2E1R0;
DT   30-AUG-2017, integrated into UniProtKB/TrEMBL.
DT   30-AUG-2017, sequence version 1.
DT   27-MAR-2024, entry version 17.
DE   SubName: Full=Nucleophile aminohydrolase {ECO:0000313|EMBL:ORY65256.1};
GN   ORFNames=BCR38DRAFT_484698 {ECO:0000313|EMBL:ORY65256.1};
OS   Pseudomassariella vexata.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Xylariomycetidae; Xylariales; Pseudomassariaceae; Pseudomassariella.
OX   NCBI_TaxID=1141098 {ECO:0000313|EMBL:ORY65256.1, ECO:0000313|Proteomes:UP000193689};
RN   [1] {ECO:0000313|EMBL:ORY65256.1, ECO:0000313|Proteomes:UP000193689}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CBS 129021 {ECO:0000313|EMBL:ORY65256.1,
RC   ECO:0000313|Proteomes:UP000193689};
RG   DOE Joint Genome Institute;
RA   Mondo S.J., Dannebaum R.O., Kuo R.C., Labutti K., Haridas S., Kuo A.,
RA   Salamov A., Ahrendt S.R., Lipzen A., Sullivan W., Andreopoulos W.B.,
RA   Clum A., Lindquist E., Daum C., Ramamoorthy G.K., Gryganskyi A., Culley D.,
RA   Magnuson J.K., James T.Y., O'Malley M.A., Stajich J.E., Spatafora J.W.,
RA   Visel A., Grigoriev I.V.;
RT   "Pervasive Adenine N6-methylation of Active Genes in Fungi.";
RL   Submitted (JUL-2016) to the EMBL/GenBank/DDBJ databases.
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}.
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:ORY65256.1}.
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DR   EMBL; MCFJ01000006; ORY65256.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1Y2E1R0; -.
DR   STRING; 1141098.A0A1Y2E1R0; -.
DR   InParanoid; A0A1Y2E1R0; -.
DR   OrthoDB; 166567at2759; -.
DR   Proteomes; UP000193689; Unassembled WGS sequence.
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:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR   GO; GO:0006511; P:ubiquitin-dependent protein catabolic process; IEA:InterPro.
DR   CDD; cd03754; proteasome_alpha_type_6; 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   InterPro; IPR034642; Proteasome_subunit_alpha6.
DR   PANTHER; PTHR11599:SF11; PROTEASOME SUBUNIT ALPHA TYPE-6; 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; PS51475; PROTEASOME_ALPHA_2; 1.
PE   3: Inferred from homology;
KW   Hydrolase {ECO:0000313|EMBL:ORY65256.1};
KW   Proteasome {ECO:0000256|ARBA:ARBA00022942, ECO:0000256|PROSITE-
KW   ProRule:PRU00808}; Reference proteome {ECO:0000313|Proteomes:UP000193689}.
FT   DOMAIN          7..29
FT                   /note="Proteasome alpha-type subunits"
FT                   /evidence="ECO:0000259|SMART:SM00948"
SQ   SEQUENCE   254 AA;  27855 MW;  B86F577A0CFBB439 CRC64;
     MSGSAGYDRH ITIFSEQGRL YQVEYAFKAI TAANIMAIGV RGKDCAVVLS QKKVPDKLID
     PSSVSHIFQI SPSVGCVMTG SIADARAFAQ RAQGEAAEFR YKFGYEMPCD VLAKRLANIS
     QVYTQRAYMR PYGVATTLIS LDSEFGPQLF KCDPAGYYVG YKGTAAGPKQ QEALNHLEKK
     LKNKDHAEGT WEDVVELAIT TLSTVLSMDF KKGEIEIGIV GGPQPDGKEG PNPNFRTLTE
     DEIDERLQAI AEKD
//
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