ID G0SH60_CHATD Unreviewed; 459 AA.
AC G0SH60;
DT 19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT 19-OCT-2011, sequence version 1.
DT 27-MAR-2024, entry version 56.
DE SubName: Full=26S protease regulatory subunit 4-like protein {ECO:0000313|EMBL:EGS17549.1};
GN ORFNames=CTHT_0068820 {ECO:0000313|EMBL:EGS17549.1};
OS Chaetomium thermophilum (strain DSM 1495 / CBS 144.50 / IMI 039719)
OS (Thermochaetoides thermophila).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Sordariomycetidae; Sordariales; Chaetomiaceae; Thermochaetoides.
OX NCBI_TaxID=759272 {ECO:0000313|Proteomes:UP000008066};
RN [1] {ECO:0000313|EMBL:EGS17549.1, ECO:0000313|Proteomes:UP000008066}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 1495 / CBS 144.50 / IMI 039719
RC {ECO:0000313|Proteomes:UP000008066};
RX PubMed=21784248; DOI=10.1016/j.cell.2011.06.039;
RA Amlacher S., Sarges P., Flemming D., van Noort V., Kunze R., Devos D.P.,
RA Arumugam M., Bork P., Hurt E.;
RT "Insight into structure and assembly of the nuclear pore complex by
RT utilizing the genome of a eukaryotic thermophile.";
RL Cell 146:277-289(2011).
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
CC -!- SIMILARITY: Belongs to the AAA ATPase family.
CC {ECO:0000256|ARBA:ARBA00006914, ECO:0000256|RuleBase:RU003651}.
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DR EMBL; GL988047; EGS17549.1; -; Genomic_DNA.
DR RefSeq; XP_006697167.1; XM_006697104.1.
DR AlphaFoldDB; G0SH60; -.
DR STRING; 759272.G0SH60; -.
DR GeneID; 18260920; -.
DR KEGG; cthr:CTHT_0068820; -.
DR eggNOG; KOG0726; Eukaryota.
DR HOGENOM; CLU_000688_2_3_1; -.
DR OMA; QDDTDPM; -.
DR OrthoDB; 1707207at2759; -.
DR Proteomes; UP000008066; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0008540; C:proteasome regulatory particle, base subcomplex; IEA:UniProt.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR GO; GO:0008233; F:peptidase activity; IEA:UniProtKB-KW.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR Gene3D; 1.10.8.60; -; 1.
DR Gene3D; 2.40.50.140; Nucleic acid-binding proteins; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR InterPro; IPR003593; AAA+_ATPase.
DR InterPro; IPR041569; AAA_lid_3.
DR InterPro; IPR003959; ATPase_AAA_core.
DR InterPro; IPR003960; ATPase_AAA_CS.
DR InterPro; IPR012340; NA-bd_OB-fold.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR032501; Prot_ATP_ID_OB_2nd.
DR PANTHER; PTHR23073; 26S PROTEASOME REGULATORY SUBUNIT; 1.
DR PANTHER; PTHR23073:SF24; 26S PROTEASOME REGULATORY SUBUNIT 4; 1.
DR Pfam; PF00004; AAA; 1.
DR Pfam; PF17862; AAA_lid_3; 1.
DR Pfam; PF16450; Prot_ATP_ID_OB_C; 1.
DR SMART; SM00382; AAA; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR PROSITE; PS00674; AAA; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|RuleBase:RU003651};
KW Hydrolase {ECO:0000313|EMBL:EGS17549.1};
KW Nucleotide-binding {ECO:0000256|RuleBase:RU003651};
KW Protease {ECO:0000313|EMBL:EGS17549.1};
KW Proteasome {ECO:0000256|ARBA:ARBA00022942};
KW Reference proteome {ECO:0000313|Proteomes:UP000008066}.
FT DOMAIN 237..376
FT /note="AAA+ ATPase"
FT /evidence="ECO:0000259|SMART:SM00382"
FT REGION 1..56
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 92..125
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 11..35
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 107..121
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 459 AA; 50966 MW; 45708560A69606DE CRC64;
MGQSQSGMGG GHDGRDEKDK KKEKPKYEPP PRPTTRVGRK KKKQGGASAA SKLPPVFPTS
RCKLRLLRMQ RIHDHLLLEE EYVENQERLR KAKAAKDSSG SSSELDTVDR LADERSRVDD
MRGSPMGVGT LEEMIDDDHA IVSSATGPEY YVSIMSFVDK DLLEPGASVL LHHKTVSIVG
VLTDDTDPLV SVMKLEKAPT ESYADIGGLE QQIQEVRESV ELPLLHPELY EEMGIKPPKG
VILYGAPGTG KTLLAKAVAN QTSATFLRIV GSELIQKYLG DGPRLVRQLF QVAAENAPSI
VFIDEIDAIG TKRYDSTSGG EREVQRTMLE LLNQLDGFDD RGDVKVIMAT NKIESLDPAL
IRPGRIDRKI LFENPDQNTK RKIFALHTSK MSLAEDVDLE EFIAQKDDLS GADIKAICTE
AGLMALRERR MRVQMSDFRA ARERVLRTKQ EGEPEGLYL
//
