ID A0A0B4I538_METMF Unreviewed; 321 AA.
AC A0A0B4I538;
DT 04-MAR-2015, integrated into UniProtKB/TrEMBL.
DT 04-MAR-2015, sequence version 1.
DT 27-MAR-2024, entry version 38.
DE SubName: Full=Proteasome A-type subunit {ECO:0000313|EMBL:KIE03199.1};
DE Flags: Fragment;
GN ORFNames=MAJ_00713 {ECO:0000313|EMBL:KIE03199.1};
OS Metarhizium majus (strain ARSEF 297).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Clavicipitaceae; Metarhizium;
OC Metarhizium majus.
OX NCBI_TaxID=1276143 {ECO:0000313|EMBL:KIE03199.1, ECO:0000313|Proteomes:UP000031176};
RN [1] {ECO:0000313|EMBL:KIE03199.1, ECO:0000313|Proteomes:UP000031176}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ARSEF 297 {ECO:0000313|EMBL:KIE03199.1,
RC ECO:0000313|Proteomes:UP000031176};
RX PubMed=25368161; DOI=10.1073/pnas.1412662111;
RA Hu X., Xiao G., Zheng P., Shang Y., Su Y., Zhang X., Liu X., Zhan S.,
RA St Leger R.J., Wang C.;
RT "Trajectory and genomic determinants of fungal-pathogen speciation and host
RT adaptation.";
RL Proc. Natl. Acad. Sci. U.S.A. 111:16796-16801(2014).
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:KIE03199.1}.
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DR EMBL; AZNE01000002; KIE03199.1; -; Genomic_DNA.
DR RefSeq; XP_014582192.1; XM_014726706.1.
DR AlphaFoldDB; A0A0B4I538; -.
DR HOGENOM; CLU_035750_0_1_1; -.
DR OrthoDB; 77945at2759; -.
DR Proteomes; UP000031176; 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:0006511; P:ubiquitin-dependent protein catabolic process; IEA:InterPro.
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; 3.
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:UP000031176}.
FT DOMAIN 8..30
FT /note="Proteasome alpha-type subunits"
FT /evidence="ECO:0000259|PROSITE:PS00388"
FT REGION 274..321
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 282..299
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 300..321
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:KIE03199.1"
SQ SEQUENCE 321 AA; 34983 MW; 46917C3F6E83EE42 CRC64;
MTSIGTGYDL LNSIFSPDGR NFQVEYAVKA VENGGTSIGI RCKDGVVLAV EKVVTSKLLK
PGANKRIATV DSHVGVVRNL ATPLPKQTHF YTKRVFGAEA NLCTQVYSGM VPDGRHFVDR
ARDESQSWRQ NFKTPIPTAD LASRMGGYLQ AYTMYGSVRP FGITAIVGGV DTSEETPVDG
EVGSGPKCGA GGKVPGKHGG PFLYMIEPSG LYWGYYGAAT GKGRQAAKAE LEKLDLQSGN
MTMEEAVKEA ARIIYIAQKD NKDKDFELEM TWISGVDGPT KGRHVEVPKE LREEAERLAK
AEDDSDDDDE NDKKDDDKME E
//
