ID A0A0B2WM98_METAS Unreviewed; 945 AA.
AC A0A0B2WM98;
DT 04-MAR-2015, integrated into UniProtKB/TrEMBL.
DT 04-MAR-2015, sequence version 1.
DT 27-MAR-2024, entry version 37.
DE SubName: Full=Proteasome, subunit alpha/beta {ECO:0000313|EMBL:KHN94145.1};
GN ORFNames=MAM_07985 {ECO:0000313|EMBL:KHN94145.1};
OS Metarhizium album (strain ARSEF 1941).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Clavicipitaceae; Metarhizium.
OX NCBI_TaxID=1081103 {ECO:0000313|EMBL:KHN94145.1, ECO:0000313|Proteomes:UP000030816};
RN [1] {ECO:0000313|EMBL:KHN94145.1, ECO:0000313|Proteomes:UP000030816}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ARSEF 1941 {ECO:0000313|EMBL:KHN94145.1,
RC ECO:0000313|Proteomes:UP000030816};
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: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
CC -!- SIMILARITY: Belongs to the fungal fucose-specific lectin family.
CC {ECO:0000256|ARBA:ARBA00009042}.
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:KHN94145.1}.
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DR EMBL; AZHE01000040; KHN94145.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0B2WM98; -.
DR STRING; 1081103.A0A0B2WM98; -.
DR HOGENOM; CLU_311018_0_0_1; -.
DR OrthoDB; 1104143at2759; -.
DR Proteomes; UP000030816; Unassembled WGS sequence.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0019774; C:proteasome core complex, beta-subunit complex; IEA:InterPro.
DR GO; GO:0043161; P:proteasome-mediated ubiquitin-dependent protein catabolic process; IEA:InterPro.
DR CDD; cd03759; proteasome_beta_type_3; 1.
DR Gene3D; 2.120.10.70; Fucose-specific lectin; 2.
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; IPR012475; Fungal_lectin.
DR InterPro; IPR029055; Ntn_hydrolases_N.
DR InterPro; IPR029021; Prot-tyrosine_phosphatase-like.
DR InterPro; IPR033811; Proteasome_beta_3.
DR InterPro; IPR016050; Proteasome_bsu_CS.
DR InterPro; IPR001353; Proteasome_sua/b.
DR InterPro; IPR023333; Proteasome_suB-type.
DR PANTHER; PTHR32194; METALLOPROTEASE TLDD; 1.
DR PANTHER; PTHR32194:SF11; PROTEASOME CORE PARTICLE SUBUNIT BETA 3; 1.
DR Pfam; PF07938; Fungal_lectin; 1.
DR Pfam; PF00227; Proteasome; 1.
DR SUPFAM; SSF52799; (Phosphotyrosine protein) phosphatases II; 1.
DR SUPFAM; SSF89372; Fucose-specific lectin; 1.
DR SUPFAM; SSF56235; N-terminal nucleophile aminohydrolases (Ntn hydrolases); 1.
DR PROSITE; PS00854; PROTEASOME_BETA_1; 1.
DR PROSITE; PS51476; PROTEASOME_BETA_2; 1.
PE 3: Inferred from homology;
KW Proteasome {ECO:0000256|ARBA:ARBA00022942, ECO:0000313|EMBL:KHN94145.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000030816};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..19
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 20..945
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5002096058"
FT REGION 528..641
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 656..693
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 538..591
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 592..606
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 620..634
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 945 AA; 104476 MW; 3A49F84D9D428C34 CRC64;
MFLCKALVFL VGAAAAVHGL VVRQTGGGQS YPDCDGLQRI ESVPDHMNSG DKLFRSSAPY
YLHEDSDQRI TEETIRCLRQ LGITHVISLN GEADNQAIRQ ALQDQGIAYT ALATPDFHAP
TVNQLQQGWD AFYGHRQGTL VWCGYGWGRT GTMITALQMY AQAERGETLR WTREQYHNEN
RVEADNQLDR LDQLQEHLRH RQPPFRDETV PMKVDEPLVQ RVRDGDFNGV DCPQVLDLAL
ALSLLSISDR TPRRRALPGE ECKQAQELFL REQCGVSDYS RPSAINLTSG SVHVFSRNGQ
GNLVETAWEN GQWWPYWIRR DGYIASQPAA MVINDNALRV YARSGSNELV EGALNDGAWQ
SWKGLGGEIA SAPTAIWLGE SLGVRVYARN KANHLVEITY SGGRWSDWEN LGGDIVGDPS
ALWMGDDVGI RVYARNRAGE LMEKAYQSGR WHEWKNLGGS ISSSPAAIAL APGDVRIYAR
NYQYELVEQG TRGGNWQNSW SGLGGGKFTG SPGAIWMGDR GILKCPRGVR HRSSQHPETT
TRMPFPPSMS CRRSATRTRQ LISAVKAAPV SSDQTQSRRR TSVSTTKSEV SRIPKSRLHA
DGSKSSAARP RESPPGGATA PANQRPPPPQ SSQLPPRQSG RCLASCRTQL VRPLSYHQPR
LTIRRHTQPG SFHKHRHEPP VKASPAKKLD RSISPPPERL LGSQSLTQQH NVVALLHQFV
IPPSLRAPGL PVPRTLPPVL TTLFPQKDGG ACVAMVGKDC VAIACDLRLG LQALTVSNNF
PKIFQYGDVF LGLTGLATDV STVADLFRYK VNMYRLREER AIAPRTFANL VSSSLYERRF
GPYFVSPVVA GLDPKTGKPF ICGFDSIGCI DFAKDFIVSG TASEQLFGMC EGLWEEDMGP
DALFETISQA LLNAVDRDAL SGWGAHVYII EKDKVTKRLL KGRQD
//
