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Database: UniProt
Entry: A0A0V1MFR8_9BILA
LinkDB: A0A0V1MFR8_9BILA
Original site: A0A0V1MFR8_9BILA 
ID   A0A0V1MFR8_9BILA        Unreviewed;       505 AA.
AC   A0A0V1MFR8;
DT   16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT   16-MAR-2016, sequence version 1.
DT   27-MAR-2024, entry version 28.
DE   SubName: Full=26S protease regulatory subunit 6A {ECO:0000313|EMBL:KRZ70435.1};
GN   Name=PSMC3 {ECO:0000313|EMBL:KRZ70435.1};
GN   ORFNames=T10_8286 {ECO:0000313|EMBL:KRZ70435.1};
OS   Trichinella papuae.
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Enoplea; Dorylaimia;
OC   Trichinellida; Trichinellidae; Trichinella.
OX   NCBI_TaxID=268474 {ECO:0000313|EMBL:KRZ70435.1, ECO:0000313|Proteomes:UP000054843};
RN   [1] {ECO:0000313|EMBL:KRZ70435.1, ECO:0000313|Proteomes:UP000054843}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ISS1980 {ECO:0000313|EMBL:KRZ70435.1};
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   -!- 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:KRZ70435.1}.
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DR   EMBL; JYDO01000114; KRZ70435.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0V1MFR8; -.
DR   STRING; 268474.A0A0V1MFR8; -.
DR   Proteomes; UP000054843; 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   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   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   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   Hydrolase {ECO:0000313|EMBL:KRZ70435.1};
KW   Nucleotide-binding {ECO:0000256|RuleBase:RU003651};
KW   Protease {ECO:0000313|EMBL:KRZ70435.1};
KW   Proteasome {ECO:0000256|ARBA:ARBA00022942};
KW   Reference proteome {ECO:0000313|Proteomes:UP000054843}.
FT   DOMAIN          207..346
FT                   /note="AAA+ ATPase"
FT                   /evidence="ECO:0000259|SMART:SM00382"
FT   COILED          22..70
FT                   /evidence="ECO:0000256|SAM:Coils"
SQ   SEQUENCE   505 AA;  57486 MW;  CE894860A0516FD4 CRC64;
     MDRIPLSDYL KSKKKRIMNM DRLELLKEIK RTERKKLLLK KEVHALEKEF HEHQQAIKMI
     QSELQRYKRL PFIVCTVSEI LKVNEVVGAK NITNTDKVDA AGKQNHDELI VVKAFSRLTY
     ILPNSGLIKP GVLKVGDLVA MSRDGLKLVE LLPSEYDPRI KGMELINQPN QQFCDIGGLD
     NQIQEMIEAV IYPITHKEYF EAFRVQPPKG VLMYGPPGTG KTMLARALAS NAKCTFLKLS
     GTALLQRYVG EGAKMVREAF RLAKEKAPTV LFIDEIDSIG SKRHNPDRGS DHEVHRTMLE
     LLTQMDGFKV NENIRVIAAT NRPDVLDPAL TRSGRFDRKV ELPLPNEKAR VQIMQIYAQK
     MNVSPKVNFE ELARCTDDFN GAQCKAVVTE AGMVALRENK VQITHEHFLA AILEDRIWLM
     YIVTLKFLLH INDYMSTNIC KITKTNDRFQ CRTLFCTLLF SMIFDDLTKS ESSSSDDFDE
     NASDYLNQEE HLIASSTSTS DESSV
//
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