ID U1HNQ6_ENDPU Unreviewed; 397 AA.
AC U1HNQ6;
DT 13-NOV-2013, integrated into UniProtKB/TrEMBL.
DT 13-NOV-2013, sequence version 1.
DT 02-APR-2025, entry version 32.
DE RecName: Full=Pru domain-containing protein {ECO:0000259|PROSITE:PS51917};
GN ORFNames=EPUS_02500 {ECO:0000313|EMBL:ERF70634.1};
OS Endocarpon pusillum (strain Z07020 / HMAS-L-300199) (Lichen-forming
OS fungus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Chaetothyriomycetidae; Verrucariales; Verrucariaceae; Endocarpon.
OX NCBI_TaxID=1263415 {ECO:0000313|EMBL:ERF70634.1, ECO:0000313|Proteomes:UP000019373};
RN [1] {ECO:0000313|Proteomes:UP000019373}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Z07020 / HMAS-L-300199 {ECO:0000313|Proteomes:UP000019373};
RX PubMed=24438332; DOI=10.1186/1471-2164-15-34;
RA Wang Y.-Y., Liu B., Zhang X.-Y., Zhou Q.-M., Zhang T., Li H., Yu Y.-F.,
RA Zhang X.-L., Hao X.-Y., Wang M., Wang L., Wei J.-C.;
RT "Genome characteristics reveal the impact of lichenization on lichen-
RT forming fungus Endocarpon pusillum Hedwig (Verrucariales, Ascomycota).";
RL BMC Genomics 15:34-34(2014).
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
CC Nucleus {ECO:0000256|ARBA:ARBA00004123}.
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DR EMBL; KE721301; ERF70634.1; -; Genomic_DNA.
DR RefSeq; XP_007803692.1; XM_007805501.1.
DR AlphaFoldDB; U1HNQ6; -.
DR GeneID; 19237553; -.
DR eggNOG; KOG3037; Eukaryota.
DR HOGENOM; CLU_041798_4_0_1; -.
DR OMA; RSPQFMQ; -.
DR OrthoDB; 340431at2759; -.
DR Proteomes; UP000019373; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0008541; C:proteasome regulatory particle, lid subcomplex; IEA:TreeGrafter.
DR GO; GO:0061133; F:endopeptidase activator activity; IEA:TreeGrafter.
DR GO; GO:0070628; F:proteasome binding; IEA:TreeGrafter.
DR FunFam; 1.10.2020.20:FF:000004; WGS project CABT00000000 data, contig 2.6; 1.
DR Gene3D; 1.10.2020.20; -; 1.
DR Gene3D; 2.30.29.70; Proteasomal ubiquitin receptor Rpn13/ADRM1; 1.
DR InterPro; IPR006773; Rpn13/ADRM1.
DR InterPro; IPR044868; Rpn13/ADRM1_Pru.
DR InterPro; IPR038633; Rpn13/ADRM1_Pru_sf.
DR InterPro; IPR032368; RPN13_DEUBAD.
DR InterPro; IPR038108; RPN13_DEUBAD_sf.
DR PANTHER; PTHR12225; ADHESION REGULATING MOLECULE 1 110 KDA CELL MEMBRANE GLYCOPROTEIN; 1.
DR PANTHER; PTHR12225:SF0; PROTEASOMAL UBIQUITIN RECEPTOR ADRM1; 1.
DR Pfam; PF04683; Rpn13_ADRM1_Pru; 1.
DR Pfam; PF16550; RPN13_C; 1.
DR PROSITE; PS51917; PRU; 1.
PE 4: Predicted;
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW Proteasome {ECO:0000256|ARBA:ARBA00022942};
KW Reference proteome {ECO:0000313|Proteomes:UP000019373}.
FT DOMAIN 1..140
FT /note="Pru"
FT /evidence="ECO:0000259|PROSITE:PS51917"
FT REGION 149..220
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 160..171
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 172..181
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 195..207
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 211..220
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 397 AA; 42418 MW; 8D343D2A50F5F593 CRC64;
MSISPIITFK AGLCDLNTAT DPPRVKALPE PGYIYLYSED DLVYFCWRQR SASLDNPGLK
LVMIPGDASF TPYKATSSQT PSNPNKPTNG RIYVLKFTSS SQRHLFWLQS RSQHESSDPA
WFSARDLKLG QIVNTLLQGE DIDVQQAIAN LPNDRNGPDR DDDDATMEDV EGQNHDADHH
RGGSGGAGPD ATGGDVREEG QEAREGGADG GRAATTGSTD ASSIIQNFLK SMEGTNAGQS
NPQGNLFTTL ADLLTPASTI PLIDSADERV IDKFLDFLPS TLLALAQEID DAAAVSTDAS
SADAAKQAIG LEQKKDILRR VLRSPQFSQS LSSLTVALRD GGLPSISEAL SIPVTNGGFM
RRGGVPLGGG DAVEAFLNGV KEHVKSNSQA KNKMDRD
//
