ID F2SZH1_TRIRC Unreviewed; 382 AA.
AC F2SZH1;
DT 31-MAY-2011, integrated into UniProtKB/TrEMBL.
DT 31-MAY-2011, sequence version 1.
DT 02-APR-2025, entry version 42.
DE RecName: Full=Pru domain-containing protein {ECO:0000259|PROSITE:PS51917};
GN ORFNames=TERG_07943 {ECO:0000313|EMBL:EGD91723.1};
OS Trichophyton rubrum (strain ATCC MYA-4607 / CBS 118892) (Athlete's foot
OS fungus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Onygenales; Arthrodermataceae; Trichophyton.
OX NCBI_TaxID=559305 {ECO:0000313|EMBL:EGD91723.1, ECO:0000313|Proteomes:UP000008864};
RN [1] {ECO:0000313|Proteomes:UP000008864}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC MYA-4607 / CBS 118892 {ECO:0000313|Proteomes:UP000008864};
RX PubMed=22951933; DOI=10.1128/mbio.00259-12;
RA Martinez D.A., Oliver B.G., Graeser Y., Goldberg J.M., Li W.,
RA Martinez-Rossi N.M., Monod M., Shelest E., Barton R.C., Birch E.,
RA Brakhage A.A., Chen Z., Gurr S.J., Heiman D., Heitman J., Kosti I.,
RA Rossi A., Saif S., Samalova M., Saunders C.W., Shea T., Summerbell R.C.,
RA Xu J., Young S., Zeng Q., Birren B.W., Cuomo C.A., White T.C.;
RT "Comparative genome analysis of Trichophyton rubrum and related
RT dermatophytes reveals candidate genes involved in infection.";
RL MBio 3:E259-E259(2012).
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
CC Nucleus {ECO:0000256|ARBA:ARBA00004123}.
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DR EMBL; GG700658; EGD91723.1; -; Genomic_DNA.
DR RefSeq; XP_003231642.1; XM_003231594.1.
DR AlphaFoldDB; F2SZH1; -.
DR STRING; 559305.F2SZH1; -.
DR GeneID; 10371407; -.
DR VEuPathDB; FungiDB:TERG_07943; -.
DR eggNOG; KOG3037; Eukaryota.
DR HOGENOM; CLU_041798_4_0_1; -.
DR InParanoid; F2SZH1; -.
DR OMA; RSPQFMQ; -.
DR OrthoDB; 340431at2759; -.
DR Proteomes; UP000008864; 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 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:UP000008864}.
FT DOMAIN 1..140
FT /note="Pru"
FT /evidence="ECO:0000259|PROSITE:PS51917"
FT REGION 146..221
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 157..171
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 184..194
FT /note="Gly residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 196..208
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 382 AA; 41222 MW; 154EADCFFDCC9C1C CRC64;
MSIAPIITFK GGICELDTSV TPNAVKARPT PGYIYLYSED DLVHFCWRPR SAPIDQPELD
LVMVPSDGTF TPYKPTSAQR PSNPERPTNG RIYVLKFASS SQRHLFWLQS RSQHEQGNPA
WFSARDLKLG QIVNTLLQGE DIDVQDAIDS LPRGDDGNDG GDDDETMEDV EGTDHSPERR
RHGGSGGAGP GATGGDIREE GQESREGGAD GGRAAAGSDP SSVVQNFLRS LQGNNSQQET
TESRYTTLAD LLSTPSTLPF LESADESTLN QLLSSLPESL QLLSKQNSNA PVERISVDKK
RNALRKVLRS PQFAQSLGSL TMAIRDGGLP SISDALKIPV QNGGFMRRGG VPLGGGEAVK
AFVEGVRQQV EDNQKGDSME TD
//