ID A0A075B1I0_ROZAC Unreviewed; 423 AA.
AC A0A075B1I0;
DT 01-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 01-OCT-2014, sequence version 1.
DT 27-MAR-2024, entry version 40.
DE SubName: Full=Proteasome, subunit alpha/beta domain-containing protein {ECO:0000313|EMBL:EPZ36213.1};
GN ORFNames=O9G_005832 {ECO:0000313|EMBL:EPZ36213.1};
OS Rozella allomycis (strain CSF55).
OC Eukaryota; Fungi; Fungi incertae sedis; Cryptomycota;
OC Cryptomycota incertae sedis; Rozella.
OX NCBI_TaxID=988480 {ECO:0000313|EMBL:EPZ36213.1, ECO:0000313|Proteomes:UP000030755};
RN [1] {ECO:0000313|EMBL:EPZ36213.1, ECO:0000313|Proteomes:UP000030755}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CSF55 {ECO:0000313|EMBL:EPZ36213.1,
RC ECO:0000313|Proteomes:UP000030755};
RX PubMed=23932404; DOI=10.1016/j.cub.2013.06.057;
RA James T.Y., Pelin A., Bonen L., Ahrendt S., Sain D., Corradi N.,
RA Stajich J.E.;
RT "Shared signatures of parasitism and phylogenomics unite Cryptomycota and
RT microsporidia.";
RL Curr. Biol. 23:1548-1553(2013).
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; KE560634; EPZ36213.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A075B1I0; -.
DR STRING; 988480.A0A075B1I0; -.
DR EnsemblFungi; EPZ36213; EPZ36213; O9G_005832.
DR HOGENOM; CLU_649161_0_0_1; -.
DR OrthoDB; 166567at2759; -.
DR Proteomes; UP000030755; 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:0016311; P:dephosphorylation; IEA:InterPro.
DR GO; GO:0006511; P:ubiquitin-dependent protein catabolic process; IEA:InterPro.
DR CDD; cd03754; proteasome_alpha_type_6; 1.
DR CDD; cd14500; PTP-IVa; 1.
DR Gene3D; 3.60.20.10; Glutamine Phosphoribosylpyrophosphate, subunit 1, domain 1; 1.
DR Gene3D; 3.90.190.10; Protein tyrosine phosphatase superfamily; 1.
DR InterPro; IPR029055; Ntn_hydrolases_N.
DR InterPro; IPR029021; Prot-tyrosine_phosphatase-like.
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 InterPro; IPR003595; Tyr_Pase_cat.
DR InterPro; IPR000387; Tyr_Pase_dom.
DR InterPro; IPR020422; TYR_PHOSPHATASE_DUAL_dom.
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 SMART; SM00404; PTPc_motif; 1.
DR SUPFAM; SSF52799; (Phosphotyrosine protein) phosphatases II; 1.
DR SUPFAM; SSF56235; N-terminal nucleophile aminohydrolases (Ntn hydrolases); 1.
DR PROSITE; PS51475; PROTEASOME_ALPHA_2; 1.
DR PROSITE; PS50056; TYR_PHOSPHATASE_2; 1.
DR PROSITE; PS50054; TYR_PHOSPHATASE_DUAL; 1.
PE 3: Inferred from homology;
KW Proteasome {ECO:0000256|ARBA:ARBA00022942, ECO:0000256|PROSITE-
KW ProRule:PRU00808}; Reference proteome {ECO:0000313|Proteomes:UP000030755}.
FT DOMAIN 9..173
FT /note="Tyrosine-protein phosphatase"
FT /evidence="ECO:0000259|PROSITE:PS50054"
FT DOMAIN 83..160
FT /note="Tyrosine specific protein phosphatases"
FT /evidence="ECO:0000259|PROSITE:PS50056"
SQ SEQUENCE 423 AA; 47051 MW; 15F2B922833B2A03 CRC64;
MAAARPHNQF SLVKYAHMSF LIMDAPSDSS LPLYVTELKK CNVKNVVRVC VPTYSTETLE
AADIRVHDWA FQDGAPPPPA IVSDWLNLVK LCFGKKVNGG SNEKHAEPTE TIAIHCVAGL
GRAPVLVAIA LIEAGMSPLD AVSFIRERRR GAINNIQLDY LEKYKKKQKS GCYDRHITVF
SPEGRLYQIG IYFSVFIIKE YAFKAINNSG LSSLGLRGKN GCVVITQLKI QDKLIDPSSV
SHIFQITPRI GCVMTGLTPD AKAQLIKARQ EAAEFRYKMG YEIPCDLLAK RIANINQVYT
QQAAMRPLGV SMILIGIDDE LGPQVFKCDP AGYYVGYKAT SAGNKHQEMV NHLEKQYKKS
EPESIEETVE LAITTLSNVL SINFKPSDIE IGVVTNDDPV FRKLNEQEIE HYLNLSLKSS
RIL
//
