ID W6V6S7_ECHGR Unreviewed; 543 AA.
AC W6V6S7;
DT 16-APR-2014, integrated into UniProtKB/TrEMBL.
DT 16-APR-2014, sequence version 1.
DT 27-MAR-2024, entry version 39.
DE SubName: Full=26S protease regulatory subunit 6A {ECO:0000313|EMBL:EUB62119.1};
GN ORFNames=EGR_03140 {ECO:0000313|EMBL:EUB62119.1};
OS Echinococcus granulosus (Hydatid tapeworm).
OC Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Platyhelminthes; Cestoda;
OC Eucestoda; Cyclophyllidea; Taeniidae; Echinococcus;
OC Echinococcus granulosus group.
OX NCBI_TaxID=6210 {ECO:0000313|EMBL:EUB62119.1, ECO:0000313|Proteomes:UP000019149};
RN [1] {ECO:0000313|EMBL:EUB62119.1, ECO:0000313|Proteomes:UP000019149}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=24013640; DOI=10.1038/ng.2757;
RA Zheng H., Zhang W., Zhang L., Zhang Z., Li J., Lu G., Zhu Y., Wang Y.,
RA Huang Y., Liu J., Kang H., Chen J., Wang L., Chen A., Yu S., Gao Z.,
RA Jin L., Gu W., Wang Z., Zhao L., Shi B., Wen H., Lin R., Jones M.K.,
RA Brejova B., Vinar T., Zhao G., McManus D.P., Chen Z., Zhou Y., Wang S.;
RT "The genome of the hydatid tapeworm Echinococcus granulosus.";
RL Nat. Genet. 45:1168-1175(2013).
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
CC Nucleus {ECO:0000256|ARBA:ARBA00004123}.
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:EUB62119.1}.
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DR EMBL; APAU02000015; EUB62119.1; -; Genomic_DNA.
DR AlphaFoldDB; W6V6S7; -.
DR STRING; 6210.W6V6S7; -.
DR EnsemblMetazoa; XM_024492389.1; XP_024353315.1; GeneID_36338855.
DR OMA; HEANCSF; -.
DR OrthoDB; 1707207at2759; -.
DR Proteomes; UP000019149; Unassembled WGS sequence.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
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 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:SF7; 26S PROTEASOME REGULATORY SUBUNIT 6A; 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 Hydrolase {ECO:0000313|EMBL:EUB62119.1};
KW Nucleotide-binding {ECO:0000256|RuleBase:RU003651};
KW Protease {ECO:0000313|EMBL:EUB62119.1};
KW Proteasome {ECO:0000256|ARBA:ARBA00022942};
KW Reference proteome {ECO:0000313|Proteomes:UP000019149}.
FT DOMAIN 323..462
FT /note="AAA+ ATPase"
FT /evidence="ECO:0000259|SMART:SM00382"
SQ SEQUENCE 543 AA; 60931 MW; 38CE0E8691656D5C CRC64;
MKRILSPLAF IVVLPQYRWN PQITALRTED YHCDIARCVA TSTGRWAAMY VAVQVYTHVR
NPNVLRQAVS CLLLLAISVN HRLCTYPGVI VSGSGVECST RSGVISCKYP SNFLSGKMTS
IERPVWDDVD ESLIDEVMRM STEELVVHTR LLDGEIRIMK SELHRVDHEI KMKQSKVKDS
KSKIKMNKAL PYLVATVVEL LDVEPEDEEE DGANVDLDSQ RKGKCAVVKT STRQTYFLPV
IGLVPHEELK PGDLVGVNKD SYLILEKLPA EFDSRVKAME VDDRPTERYG DIGGLDKQIQ
ELIEAVVLPM THKDRFDAIG IQPPKGVLLY GPPGTGKTLL ARACAAQTKS TFLKLAAPQL
VQMFIGDGAK LVRDAFQLAK EKAPAIIFID ELDAIGTKRF DSEKAGDREV QRTMLELLNQ
LDGFQPNHEI KVIAATNRVD ILDPALLRSG RLDRKIEFPT PNEEARSRIM QIHSRKMNVH
EDVNFEELAR CTDDFNGAQC KAVCVEAGMI ALRRNATQVV HEDYMDAILE VQSKKKTNLN
YYA
//
