ID A0A421CYR4_9EURO Unreviewed; 464 AA.
AC A0A421CYR4;
DT 08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT 08-MAY-2019, sequence version 1.
DT 27-MAR-2024, entry version 22.
DE SubName: Full=26S proteasome regulatory subunit 6A {ECO:0000313|EMBL:RLL95001.1};
GN Name=RPT5 {ECO:0000313|EMBL:RLL95001.1};
GN ORFNames=CFD26_105132 {ECO:0000313|EMBL:RLL95001.1};
OS Aspergillus turcosus.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
OX NCBI_TaxID=1245748 {ECO:0000313|EMBL:RLL95001.1, ECO:0000313|Proteomes:UP000215289};
RN [1] {ECO:0000313|EMBL:RLL95001.1, ECO:0000313|Proteomes:UP000215289}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HMR AF 1038 {ECO:0000313|EMBL:RLL95001.1};
RA Parent-Michaud M., Dufresne P.J., Fournier E., Martineau C., Moreira S.,
RA Perkins V., De Repentigny L., Dufresne S.F.;
RT "Draft genome sequences of two Aspergillus turcosus clinical strains
RT isolated from bronchoalveolar lavage fluid: one azole-susceptible and the
RT other azole-resistant.";
RL Submitted (AUG-2018) 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:RLL95001.1}.
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DR EMBL; NIDN02000174; RLL95001.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A421CYR4; -.
DR STRING; 1245748.A0A421CYR4; -.
DR Proteomes; UP000215289; 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 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 Nucleotide-binding {ECO:0000256|RuleBase:RU003651};
KW Proteasome {ECO:0000256|ARBA:ARBA00022942, ECO:0000313|EMBL:RLL95001.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000215289}.
FT DOMAIN 243..382
FT /note="AAA+ ATPase"
FT /evidence="ECO:0000259|SMART:SM00382"
FT REGION 1..54
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..25
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 32..50
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 464 AA; 51694 MW; 720763794AB853B2 CRC64;
MSTLEDLEDL EREERDKKKD QGDGDGQQTG GDGDAEMKDA DAKKKDEEDD LLDEEILTSS
TADIVKRRRM LENELRIMKS EYQRLTHEQN TMREKVRDNQ EKIENNRQLP YLVGNVVELL
DLDVEAEAAE EGANIDLDAT RVGKSAVIKT STRQTIYLPL IGLVDHEKLK PGDLIGVNKD
SYLILDTLPA EYDNRVKAME VDEKPTEKYT DIGGLDKQIE EIVEAIVWPM KEAERFTKIG
IKAPKGALMY GPPGTGKTLL ARACAAETNA TFLKLAGPQL VQMFIGDGAK LVRDCFALAK
EKAPSIIFID ELDAVGTKRF DSEKSGDREV QRTMLELLNQ LDGFASDDRI KVLAATNRID
VLDPALLRSG RLDRKIEFPL PNEEARANIL QIHSRKMAVD DAVNWAELAR STDEFGGAQL
KAVCVEAGMI ALRKGMSKVG HENYVDAIAE VQAKKKDTNM GIYV
//
