ID J3KCX0_COCIM Unreviewed; 314 AA.
AC J3KCX0;
DT 03-OCT-2012, integrated into UniProtKB/TrEMBL.
DT 27-MAY-2015, sequence version 2.
DT 27-MAR-2024, entry version 49.
DE RecName: Full=Tethering factor for nuclear proteasome STS1 {ECO:0000256|ARBA:ARBA00016204, ECO:0000256|RuleBase:RU368013};
GN ORFNames=CIMG_04159 {ECO:0000313|EMBL:EAS33135.3};
OS Coccidioides immitis (strain RS) (Valley fever fungus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Onygenales; Onygenaceae; Coccidioides.
OX NCBI_TaxID=246410 {ECO:0000313|EMBL:EAS33135.3, ECO:0000313|Proteomes:UP000001261};
RN [1] {ECO:0000313|Proteomes:UP000001261}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=RS {ECO:0000313|Proteomes:UP000001261};
RX PubMed=19717792; DOI=10.1101/gr.087551.108;
RA Sharpton T.J., Stajich J.E., Rounsley S.D., Gardner M.J., Wortman J.R.,
RA Jordar V.S., Maiti R., Kodira C.D., Neafsey D.E., Zeng Q., Hung C.-Y.,
RA McMahan C., Muszewska A., Grynberg M., Mandel M.A., Kellner E.M.,
RA Barker B.M., Galgiani J.N., Orbach M.J., Kirkland T.N., Cole G.T.,
RA Henn M.R., Birren B.W., Taylor J.W.;
RT "Comparative genomic analyses of the human fungal pathogens Coccidioides
RT and their relatives.";
RL Genome Res. 19:1722-1731(2009).
RN [2] {ECO:0000313|Proteomes:UP000001261}
RP GENOME REANNOTATION.
RC STRAIN=RS {ECO:0000313|Proteomes:UP000001261};
RX PubMed=20516208; DOI=10.1101/gr.103911.109;
RA Neafsey D.E., Barker B.M., Sharpton T.J., Stajich J.E., Park D.J.,
RA Whiston E., Hung C.-Y., McMahan C., White J., Sykes S., Heiman D.,
RA Young S., Zeng Q., Abouelleil A., Aftuck L., Bessette D., Brown A.,
RA FitzGerald M., Lui A., Macdonald J.P., Priest M., Orbach M.J.,
RA Galgiani J.N., Kirkland T.N., Cole G.T., Birren B.W., Henn M.R.,
RA Taylor J.W., Rounsley S.D.;
RT "Population genomic sequencing of Coccidioides fungi reveals recent
RT hybridization and transposon control.";
RL Genome Res. 20:938-946(2010).
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; GG704916; EAS33135.3; -; Genomic_DNA.
DR RefSeq; XP_001244718.1; XM_001244717.2.
DR AlphaFoldDB; J3KCX0; -.
DR STRING; 246410.J3KCX0; -.
DR GeneID; 4563037; -.
DR KEGG; cim:CIMG_04159; -.
DR VEuPathDB; FungiDB:CIMG_04159; -.
DR InParanoid; J3KCX0; -.
DR OMA; DYTPHFL; -.
DR OrthoDB; 2720936at2759; -.
DR Proteomes; UP000001261; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0000502; C:proteasome complex; IEA:UniProtKB-KW.
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 Proteasome {ECO:0000313|EMBL:EAS33135.3};
KW Protein transport {ECO:0000256|RuleBase:RU368013};
KW Reference proteome {ECO:0000313|Proteomes:UP000001261};
KW Transport {ECO:0000256|RuleBase:RU368013}.
FT REGION 24..85
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 35..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; 34462 MW; C5A815F66E084A23 CRC64;
MNSLVATPPI PPHFYEHNRF NTTSRFVSPM NPAGSRKRKA EDDNGSSDHD TRMSASPTSS
PALPTKPLAA RQIKRPRPNL SGRPLSLGRL FETLDSDALR SVLRSLCDRH PELGQEVVDT
APRPNITSAL QVLSNYQSTL QSSFPLGGNP SSDYAYNRVR PHVMNLLDAL NDFTPHFLPP
NETHPSTSLN YLDGVTEIIH QLPRWDTPHY NLEKEAAYEE IAKAWALVIR EASKRGGGIQ
LQYGEWDQKL AKHNQTSGGK LQDAVHALSA SLGWMAGNPS HPGPGCPQTD TASIRQQLLS
GTYGAGLPLK VGPW
//
