ID A0A9N9A9B5_9GLOM Unreviewed; 351 AA.
AC A0A9N9A9B5;
DT 13-SEP-2023, integrated into UniProtKB/TrEMBL.
DT 13-SEP-2023, sequence version 1.
DT 28-JAN-2026, entry version 8.
DE SubName: Full=17116_t:CDS:1 {ECO:0000313|EMBL:CAG8521149.1};
GN ORFNames=FCALED_LOCUS4705 {ECO:0000313|EMBL:CAG8521149.1};
OS Funneliformis caledonium.
OC Eukaryota; Fungi; Fungi incertae sedis; Mucoromycota; Glomeromycotina;
OC Glomeromycetes; Glomerales; Glomeraceae; Funneliformis.
OX NCBI_TaxID=1117310 {ECO:0000313|EMBL:CAG8521149.1, ECO:0000313|Proteomes:UP000789570};
RN [1] {ECO:0000313|EMBL:CAG8521149.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=UK204 {ECO:0000313|EMBL:CAG8521149.1};
RA Kallberg Y., Tangrot J., Rosling A.;
RL Submitted (JUN-2021) to the EMBL/GenBank/DDBJ databases.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
CC Nucleus {ECO:0000256|ARBA:ARBA00004123}.
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:CAG8521149.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CAJVPQ010000937; CAG8521149.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A9N9A9B5; -.
DR OrthoDB; 340431at2759; -.
DR Proteomes; UP000789570; 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 CDD; cd13314; PH_Rpn13; 1.
DR FunFam; 2.30.29.70:FF:000001; Proteasomal ubiquitin receptor ADRM1; 1.
DR Gene3D; 1.10.2020.20; -; 1.
DR Gene3D; 2.30.29.70; Proteasomal ubiquitin receptor Rpn13/ADRM1; 1.
DR InterPro; IPR044867; DEUBAD_dom.
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; PS51916; DEUBAD; 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:UP000789570}.
FT DOMAIN 11..126
FT /note="Pru"
FT /evidence="ECO:0000259|PROSITE:PS51917"
FT DOMAIN 227..333
FT /note="DEUBAD"
FT /evidence="ECO:0000259|PROSITE:PS51916"
FT REGION 126..146
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 173..205
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 321..351
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 174..183
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 184..200
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 327..351
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 351 AA; 38623 MW; 350C5D414241AA33 CRC64;
MATSLFPTPV PRRKYPVEFK AGKLKREEGS NWLKADERKG LIYMDQGEDQ LMHFFWKDRK
ANTVEDDFIL FPDEAEFIRV DQCTTGRVYI LNFKSSSRKL FYWMQDAKDE KDEENVAKLN
RLINDPQGGL AESRQQNNAG QLGSPFRNMD DLGFGVDQEQ LLQLLQGGLG GLPITSTTPA
SEPQSATAAT SEAGSGAQTT EQSTGFTPEQ LEQLGSLRNV LPSIQNPEGG TRPDVNLQDV
LSPNAIGPLL NNPEISSALF PHLPSNIERS PEELSAVVNS PQFAQALQSL SLALQSGQLG
PLLTQLGLDP SAGNGVEAFL RAVQEQAGRR QRDHNDDENA DDHSGDRMEE D
//
