ID A0A091QK29_MERNU Unreviewed; 359 AA.
AC A0A091QK29;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 24-JAN-2024, entry version 24.
DE RecName: Full=26S proteasome non-ATPase regulatory subunit 11 {ECO:0000256|ARBA:ARBA00039723};
DE AltName: Full=26S proteasome regulatory subunit RPN6 {ECO:0000256|ARBA:ARBA00041252};
DE Flags: Fragment;
GN ORFNames=N331_11629 {ECO:0000313|EMBL:KFQ26971.1};
OS Merops nubicus (Northern carmine bee-eater).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Coraciiformes; Meropidae; Merops.
OX NCBI_TaxID=57421 {ECO:0000313|EMBL:KFQ26971.1, ECO:0000313|Proteomes:UP000052967};
RN [1] {ECO:0000313|EMBL:KFQ26971.1, ECO:0000313|Proteomes:UP000052967}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BGI_N331 {ECO:0000313|EMBL:KFQ26971.1};
RA Zhang G., Li C.;
RT "Genome evolution of avian class.";
RL Submitted (APR-2014) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Component of the 26S proteasome, a multiprotein complex
CC involved in the ATP-dependent degradation of ubiquitinated proteins.
CC This complex plays a key role in the maintenance of protein homeostasis
CC by removing misfolded or damaged proteins, which could impair cellular
CC functions, and by removing proteins whose functions are no longer
CC required. Therefore, the proteasome participates in numerous cellular
CC processes, including cell cycle progression, apoptosis, or DNA damage
CC repair. In the complex, PSMD11 is required for proteasome assembly.
CC Plays a key role in increased proteasome activity in embryonic stem
CC cells (ESCs): its high expression in ESCs promotes enhanced assembly of
CC the 26S proteasome, followed by higher proteasome activity.
CC {ECO:0000256|ARBA:ARBA00037179}.
CC -!- SUBUNIT: Component of the 19S proteasome regulatory particle complex.
CC The 26S proteasome consists of a 20S core particle (CP) and two 19S
CC regulatory subunits (RP). The regulatory particle is made of a lid
CC composed of 9 subunits including PSMD11, a base containing 6 ATPases
CC and few additional components. {ECO:0000256|ARBA:ARBA00038658}.
CC -!- SIMILARITY: Belongs to the proteasome subunit S9 family.
CC {ECO:0000256|ARBA:ARBA00007454}.
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DR EMBL; KK700503; KFQ26971.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A091QK29; -.
DR Proteomes; UP000052967; Unassembled WGS sequence.
DR GO; GO:0000502; C:proteasome complex; IEA:UniProtKB-KW.
DR Gene3D; 1.25.40.570; -; 1.
DR InterPro; IPR000717; PCI_dom.
DR InterPro; IPR040780; Rpn6_C_helix.
DR InterPro; IPR040773; Rpn6_N.
DR InterPro; IPR011990; TPR-like_helical_dom_sf.
DR InterPro; IPR036390; WH_DNA-bd_sf.
DR PANTHER; PTHR10678:SF2; 26S PROTEASOME NON-ATPASE REGULATORY SUBUNIT 11; 1.
DR PANTHER; PTHR10678; 26S PROTEASOME NON-ATPASE REGULATORY SUBUNIT 11/COP9 SIGNALOSOME COMPLEX SUBUNIT 2; 1.
DR Pfam; PF01399; PCI; 1.
DR Pfam; PF18503; RPN6_C_helix; 1.
DR Pfam; PF18055; RPN6_N; 1.
DR SMART; SM00753; PAM; 1.
DR SMART; SM00088; PINT; 1.
DR SUPFAM; SSF48452; TPR-like; 1.
DR SUPFAM; SSF46785; Winged helix' DNA-binding domain; 1.
DR PROSITE; PS50250; PCI; 1.
PE 3: Inferred from homology;
KW Proteasome {ECO:0000256|ARBA:ARBA00022942, ECO:0000313|EMBL:KFQ26971.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000052967}.
FT DOMAIN 161..329
FT /note="PCI"
FT /evidence="ECO:0000259|PROSITE:PS50250"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:KFQ26971.1"
FT NON_TER 359
FT /evidence="ECO:0000313|EMBL:KFQ26971.1"
SQ SEQUENCE 359 AA; 40627 MW; 0D4E4C255FE59E6F CRC64;
AELGGLLKYV RPFLNSISKA KAARLVRSLL DLFLDMEAAT GQEVDLCLEC IEWAKSEKRT
FLRQALEARL VSLYFDTKRY QEALQLGSQL LRELKKMDDK ALLVEVQLLE SKTYHALSNL
PKARAALTSA RTTANAIYCP PKLQAALDMQ SGIIHAAEEK DWKTAYSYFY EAFEGYDSID
NPKAITALKY MLLCKIMLNI PEDVQALVSG KLALRYAGRQ TEALKCVAQA SKNRSLADFE
KALTDYKVEL RDDPIINTHL AKLYDNLLEQ NLIRVIEPFS RVQIEHISSL IKLSKAEVER
KLSQMILDKK FHGILDQGEG VLIIFDEPPV DKTYEAALET IQNMSKVVDS LYNKAKKLT
//
