ID A0A3Q3A2J2_KRYMA Unreviewed; 416 AA.
AC A0A3Q3A2J2;
DT 10-APR-2019, integrated into UniProtKB/TrEMBL.
DT 10-APR-2019, sequence version 1.
DT 27-MAR-2024, entry version 26.
DE RecName: Full=26S proteasome regulatory subunit 6B {ECO:0000256|ARBA:ARBA00018274};
DE AltName: Full=26S proteasome AAA-ATPase subunit RPT3 {ECO:0000256|ARBA:ARBA00030361};
DE AltName: Full=Proteasome 26S subunit ATPase 4 {ECO:0000256|ARBA:ARBA00030935};
OS Kryptolebias marmoratus (Mangrove killifish) (Rivulus marmoratus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Ovalentaria; Atherinomorphae; Cyprinodontiformes; Rivulidae; Kryptolebias.
OX NCBI_TaxID=37003 {ECO:0000313|Ensembl:ENSKMAP00000010508.1, ECO:0000313|Proteomes:UP000264800};
RN [1] {ECO:0000313|Ensembl:ENSKMAP00000010508.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
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. PSMC4 belongs to the heterohexameric ring of AAA (ATPases
CC associated with diverse cellular activities) proteins that unfolds
CC ubiquitinated target proteins that are concurrently translocated into a
CC proteolytic chamber and degraded into peptides.
CC {ECO:0000256|ARBA:ARBA00002699}.
CC -!- SIMILARITY: Belongs to the AAA ATPase family.
CC {ECO:0000256|ARBA:ARBA00006914, ECO:0000256|RuleBase:RU003651}.
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DR AlphaFoldDB; A0A3Q3A2J2; -.
DR Ensembl; ENSKMAT00000010670.1; ENSKMAP00000010508.1; ENSKMAG00000007846.1.
DR GeneTree; ENSGT01020000230346; -.
DR OMA; QDIGGMD; -.
DR Proteomes; UP000264800; Unplaced.
DR GO; GO:0000502; C:proteasome complex; IEA:UniProtKB-KW.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR CDD; cd19502; RecA-like_PAN_like; 1.
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:SF8; 26S PROTEASOME REGULATORY SUBUNIT 6B; 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 Coiled coil {ECO:0000256|SAM:Coils};
KW Nucleotide-binding {ECO:0000256|RuleBase:RU003651};
KW Proteasome {ECO:0000256|ARBA:ARBA00022942};
KW Reference proteome {ECO:0000313|Proteomes:UP000264800}.
FT DOMAIN 196..335
FT /note="AAA+ ATPase"
FT /evidence="ECO:0000259|SMART:SM00382"
FT COILED 35..69
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 416 AA; 47237 MW; 5E2226A23CF46625 CRC64;
LEEVGSISLQ RNLHSFLTSR PQTGLSFLAP EPEDLEDLYT RYKKLQQELE FLEVQEEYIK
DEQKNLKKEF LHAQEEVKRI QSIPLVIGQF LEAVDQNTAI VGSTTGSNYY VRILSTIDRE
LLKPNASVAL HKHSNALVDV LPPEADSSIM MLTSDQKPDV MYADIGGMDI QKQEVREAVE
LPLTHFELYK QIGIDPPRGV LMYGPPGCGK TMLAKAVAHH TTAAFIRVVG SEFVQKYLGE
GPRMVRDVFR LAKENAPAII FIDEIDAIAT KRFDAQTGAD REVQRILLEL LNQMDGFDQN
VNVKVIMATN RADTLDPALL RPGRLDRKIE FPLPDRRQKR LIFSTITSKM NLSEEVDLED
YVARPDKISG ADINSICQEA GMLAVRENRY IVLAKDFEKA YKTVIKKDEQ EHEFYK
//
