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Database: UniProt
Entry: A0A3B3D338_ORYME
LinkDB: A0A3B3D338_ORYME
Original site: A0A3B3D338_ORYME 
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
//
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