ID A0A100INE7_ASPNG Unreviewed; 464 AA.
AC A0A100INE7;
DT 13-APR-2016, integrated into UniProtKB/TrEMBL.
DT 13-APR-2016, sequence version 1.
DT 27-MAR-2024, entry version 36.
DE SubName: Full=26S protease regulatory subunit 6A-B {ECO:0000313|EMBL:GAQ44419.1};
GN ORFNames=ABL_07080 {ECO:0000313|EMBL:GAQ44419.1};
OS Aspergillus niger.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Circumdati.
OX NCBI_TaxID=5061 {ECO:0000313|EMBL:GAQ44419.1, ECO:0000313|Proteomes:UP000068243};
RN [1] {ECO:0000313|Proteomes:UP000068243}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=An76 {ECO:0000313|Proteomes:UP000068243};
RX PubMed=26893421; DOI=10.1128/genomeA.01700-15;
RA Gong W., Cheng Z., Zhang H., Liu L., Gao P., Wang L.;
RT "Draft genome sequence of Aspergillus niger strain An76.";
RL Genome Announc. 4:E0170015-E0170015(2016).
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:GAQ44419.1}.
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DR EMBL; BCMY01000012; GAQ44419.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A100INE7; -.
DR PaxDb; 5061-CADANGAP00013895; -.
DR VEuPathDB; FungiDB:An18g05230; -.
DR VEuPathDB; FungiDB:ASPNIDRAFT2_1154971; -.
DR VEuPathDB; FungiDB:ATCC64974_107640; -.
DR VEuPathDB; FungiDB:M747DRAFT_292306; -.
DR OMA; NKISHEH; -.
DR Proteomes; UP000068243; Unassembled WGS sequence.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0008540; C:proteasome regulatory particle, base subcomplex; IEA:UniProt.
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 Coiled coil {ECO:0000256|SAM:Coils};
KW Hydrolase {ECO:0000313|EMBL:GAQ44419.1};
KW Nucleotide-binding {ECO:0000256|RuleBase:RU003651};
KW Protease {ECO:0000313|EMBL:GAQ44419.1};
KW Proteasome {ECO:0000256|ARBA:ARBA00022942}.
FT DOMAIN 243..382
FT /note="AAA+ ATPase"
FT /evidence="ECO:0000259|SMART:SM00382"
FT REGION 1..55
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 68..102
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 1..46
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 464 AA; 51762 MW; 06CEFB638A62BF04 CRC64;
MSTLEDLDDL EREQRDKKKD QGDDGEGRKP EGEGDAEMKD ADAKKDEDDG LLDEEILSSS
TADIVKRRRM LENELRIMKS EYQRLTHEQN TMREKVKDNQ EKIENNRQLP YLVGNVVELL
DLDVEAEAAE EGANIDLDAT RVGKSAVIKT STRQTIYLPL IGLVDHEKLK PGDLIGVNKD
SYLVLDTLPA EYDNRVKAME VDEKPTEKYT DIGGLDKQIE EIVEAIVWPM KEADRFKKLG
IKAPKGALMY GPPGTGKTLL ARACAAETNA TFLKLAGPQL VQMFIGDGAK LVRDCFALAK
EKAPSIIFID ELDAVGTKRF DSEKSGDREV QRTMLELLNQ LDGFASDDRI KVLAATNRVD
VLDPALLRSG RLDRKIEFPL PNEEARANIL QIHSRKMAVD DRVNWAELAR STDEFGGAQL
KAVCVEAGMI ALRKGMSKVG HENYVDAISE VQAKKKDTNM GIYV
//
