ID A0A3B3D338_ORYME Unreviewed; 417 AA.
AC A0A3B3D338;
DT 05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT 05-DEC-2018, sequence version 1.
DT 27-MAR-2024, entry version 29.
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 Oryzias melastigma (Marine medaka).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Ovalentaria; Atherinomorphae; Beloniformes; Adrianichthyidae; Oryziinae;
OC Oryzias.
OX NCBI_TaxID=30732 {ECO:0000313|Ensembl:ENSOMEP00000024498.1, ECO:0000313|Proteomes:UP000261560};
RN [1] {ECO:0000313|Ensembl:ENSOMEP00000024498.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-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; A0A3B3D338; -.
DR STRING; 30732.ENSOMEP00000024498; -.
DR PaxDb; 30732-ENSOMEP00000024498; -.
DR Ensembl; ENSOMET00000009521.1; ENSOMEP00000024498.1; ENSOMEG00000005164.1.
DR GeneTree; ENSGT01020000230346; -.
DR OMA; QDIGGMD; -.
DR OrthoDB; 5477077at2759; -.
DR Proteomes; UP000261560; 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}.
FT DOMAIN 197..336
FT /note="AAA+ ATPase"
FT /evidence="ECO:0000259|SMART:SM00382"
FT REGION 1..28
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 36..70
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 417 AA; 47340 MW; E1B7CC31B6D638C1 CRC64;
MEDLVTVEKS PEEMPPVLSS RPQTGLSFLT PEPEDLEDLY SRYKKLQQEL EFLEVQEEYI
KDEQKNLKKE FLHAQEEVKR IQSIPLVIGQ FLEAVDQNTA IVGSTTGSNY YVRILSTIDR
ELLKPNASVA LHKHSNALVD VLPPEADSSI MMLTSDQKPD VMYADIGGMD IQKQEVREAV
ELPLTHFELY KQIGIDPPRG VLMYGPPGCG KTMLAKAVAH HTTAAFIRVV GSEFVQKYLG
EGPRMVRDVF RLAKENAPAI IFIDEIDAIA TKRFDAQTGA DREVQRILLE LLNQMDGFDQ
NVNVKVIMAT NRADTLDPAL LRPGRLDRKI EFPLPDRRQK RLIFSTITSK MNLSEEVDLE
DYVARPDKIS GADINSICQE AGMLAVRENR YIVLAKDFEK AYKTVIKKDE QEHEFYK
//