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Database: UniProt
Entry: A0A0V0TIZ8_9BILA
LinkDB: A0A0V0TIZ8_9BILA
Original site: A0A0V0TIZ8_9BILA 
ID   A0A0V0TIZ8_9BILA        Unreviewed;       414 AA.
AC   A0A0V0TIZ8;
DT   16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT   16-MAR-2016, sequence version 1.
DT   27-MAR-2024, entry version 29.
DE   SubName: Full=26S protease regulatory subunit 6B {ECO:0000313|EMBL:KRX38950.1};
GN   Name=Psmc4 {ECO:0000313|EMBL:KRX38950.1};
GN   ORFNames=T05_10928 {ECO:0000313|EMBL:KRX38950.1};
OS   Trichinella murrelli.
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Enoplea; Dorylaimia;
OC   Trichinellida; Trichinellidae; Trichinella.
OX   NCBI_TaxID=144512 {ECO:0000313|EMBL:KRX38950.1, ECO:0000313|Proteomes:UP000055048};
RN   [1] {ECO:0000313|EMBL:KRX38950.1, ECO:0000313|Proteomes:UP000055048}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ISS417 {ECO:0000313|EMBL:KRX38950.1};
RA   Korhonen P.K., Edoardo P., Giuseppe L.R., Gasser R.B.;
RT   "Evolution of Trichinella species and genotypes.";
RL   Submitted (JAN-2015) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the AAA ATPase family.
CC       {ECO:0000256|ARBA:ARBA00006914, ECO:0000256|RuleBase:RU003651}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:KRX38950.1}.
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DR   EMBL; JYDJ01000248; KRX38950.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0V0TIZ8; -.
DR   STRING; 144512.A0A0V0TIZ8; -.
DR   Proteomes; UP000055048; Unassembled WGS sequence.
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   GO; GO:0008233; F:peptidase activity; IEA:UniProtKB-KW.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
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; IPR001270; ClpA/B.
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   PRINTS; PR00300; CLPPROTEASEA.
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:KRX38950.1};
KW   Nucleotide-binding {ECO:0000256|RuleBase:RU003651};
KW   Protease {ECO:0000313|EMBL:KRX38950.1};
KW   Proteasome {ECO:0000256|ARBA:ARBA00022942};
KW   Reference proteome {ECO:0000313|Proteomes:UP000055048}.
FT   DOMAIN          194..333
FT                   /note="AAA+ ATPase"
FT                   /evidence="ECO:0000259|SMART:SM00382"
SQ   SEQUENCE   414 AA;  47359 MW;  B06B6B5070E436CD CRC64;
     MKALKEIGIE FIKMSQAALE EHPLSRLNNI PTTDDLYDRV KKMENDLLLY EVQEAYIKQE
     QRNLRRERLH SQEEVKRIQS VPLVIGQFLE AVDQDFAIVG STTGSNYYVR ILSTIDRELL
     KPGSSVALHK YSNALVDILP PEADSSISML RFDERPTITY NDIGGLDMQK QEVREAVELP
     LTHFELYQQI GIDPPQGVLL YGPPGCGKTM LAKAVASQTT AAFIRVVGSE FVQKYLGEGP
     RMVRDVFRLA RENAPAIIFI DEIDAIATKR FDAQTGADRE VQRILLELLN QMDGFDRNRN
     VKVIMATNRA DTLDPALLRP GRLDRKIEFP LPDRRQKRLV FNTITSKMNL HEDVELEDLI
     SRPDKVSGAD INSICQEAGM LAVRENRYMV TARDFEKAHK RVMRRDEMVF DFYE
//
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