ID A0A319CF76_9EURO Unreviewed; 314 AA.
AC A0A319CF76;
DT 10-OCT-2018, integrated into UniProtKB/TrEMBL.
DT 10-OCT-2018, sequence version 1.
DT 24-JAN-2024, entry version 22.
DE RecName: Full=Tethering factor for nuclear proteasome STS1 {ECO:0000256|ARBA:ARBA00016204, ECO:0000256|RuleBase:RU368013};
GN ORFNames=BO82DRAFT_294331 {ECO:0000313|EMBL:PYH77193.1};
OS Aspergillus uvarum CBS 121591.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
OX NCBI_TaxID=1448315 {ECO:0000313|EMBL:PYH77193.1, ECO:0000313|Proteomes:UP000248340};
RN [1] {ECO:0000313|EMBL:PYH77193.1, ECO:0000313|Proteomes:UP000248340}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 121591 {ECO:0000313|EMBL:PYH77193.1,
RC ECO:0000313|Proteomes:UP000248340};
RG DOE Joint Genome Institute;
RA Vesth T.C., Nybo J., Theobald S., Brandl J., Frisvad J.C., Nielsen K.F.,
RA Lyhne E.K., Kogle M.E., Kuo A., Riley R., Clum A., Nolan M., Lipzen A.,
RA Salamov A., Henrissat B., Wiebenga A., De Vries R.P., Grigoriev I.V.,
RA Mortensen U.H., Andersen M.R., Baker S.E.;
RT "The genomes of Aspergillus section Nigri reveals drivers in fungal
RT speciation.";
RL Submitted (DEC-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Involved in ubiquitin-mediated protein degradation.
CC Regulatory factor in the ubiquitin/proteasome pathway that controls the
CC turnover of proteasome substrates. Targets proteasomes to the nucleus
CC and facilitates the degradation of nuclear proteins.
CC {ECO:0000256|ARBA:ARBA00025651, ECO:0000256|RuleBase:RU368013}.
CC -!- SUBUNIT: Binds the proteasome. {ECO:0000256|ARBA:ARBA00011464,
CC ECO:0000256|RuleBase:RU368013}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|RuleBase:RU368013}.
CC Nucleus {ECO:0000256|RuleBase:RU368013}.
CC -!- SIMILARITY: Belongs to the cut8/STS1 family.
CC {ECO:0000256|ARBA:ARBA00006199, ECO:0000256|RuleBase:RU368013}.
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DR EMBL; KZ821744; PYH77193.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A319CF76; -.
DR STRING; 1448315.A0A319CF76; -.
DR VEuPathDB; FungiDB:BO82DRAFT_294331; -.
DR OrthoDB; 2720936at2759; -.
DR Proteomes; UP000248340; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0071630; P:nuclear protein quality control by the ubiquitin-proteasome system; IEA:UniProtKB-UniRule.
DR GO; GO:0031144; P:proteasome localization; IEA:UniProtKB-UniRule.
DR GO; GO:0015031; P:protein transport; IEA:UniProtKB-UniRule.
DR Gene3D; 1.20.58.1590; Tethering factor for nuclear proteasome Cut8/Sts1; 1.
DR InterPro; IPR013868; Cut8/Sts1_fam.
DR InterPro; IPR038422; Cut8/Sts1_sf.
DR PANTHER; PTHR28032; FI02826P; 1.
DR PANTHER; PTHR28032:SF1; FI02826P; 1.
DR Pfam; PF08559; Cut8; 1.
PE 3: Inferred from homology;
KW Cytoplasm {ECO:0000256|RuleBase:RU368013};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242, ECO:0000256|RuleBase:RU368013};
KW Protein transport {ECO:0000256|RuleBase:RU368013};
KW Reference proteome {ECO:0000313|Proteomes:UP000248340};
KW Transport {ECO:0000256|RuleBase:RU368013};
KW Viral envelope protein {ECO:0000313|EMBL:PYH77193.1};
KW Virion {ECO:0000313|EMBL:PYH77193.1}.
FT REGION 1..81
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 34..49
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 50..65
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 314 AA; 34450 MW; 410A8C6F56BAABA6 CRC64;
MNSLVATPPV PPHHFYEPSR LSPSRPMSTP THTPNRKRKA DDDGNDHDGR MSASPTNSPA
FTPRTLPSNR HHIKRARPNV SGRPLSLPRL LETLDTDALR GVLRSMCERH PALMDEVIHT
APRPSVASAL QVLRNYQSNL QSSFPLGGSS ESDYAYNRVR QPLGSLLDAL SDFTPHFLPP
NETQASVSLS YLDGATDIIH ALPRWHTPQN NLERDSAYDE ICKAWVLVIR EAAKRGGGIQ
LQYGGWDQKL AKHNQNSDGK LQAAVNELGS SLGWMHRPDA QGYGSPGGND LGSIREQLLS
GTYGLGTPVK VGPW
//
