ID S8AX13_PENO1 Unreviewed; 389 AA.
AC S8AX13;
DT 16-OCT-2013, integrated into UniProtKB/TrEMBL.
DT 16-OCT-2013, sequence version 1.
DT 24-JAN-2024, entry version 48.
DE RecName: Full=AAA+ ATPase domain-containing protein {ECO:0000259|SMART:SM00382};
GN ORFNames=PDE_05790 {ECO:0000313|EMBL:EPS30838.1};
OS Penicillium oxalicum (strain 114-2 / CGMCC 5302) (Penicillium decumbens).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Penicillium.
OX NCBI_TaxID=933388 {ECO:0000313|EMBL:EPS30838.1, ECO:0000313|Proteomes:UP000019376};
RN [1] {ECO:0000313|EMBL:EPS30838.1, ECO:0000313|Proteomes:UP000019376}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=114-2 / CGMCC 5302 {ECO:0000313|Proteomes:UP000019376};
RX PubMed=23383313; DOI=10.1371/journal.pone.0055185;
RA Liu G., Zhang L., Wei X., Zou G., Qin Y., Ma L., Li J., Zheng H., Wang S.,
RA Wang C., Xun L., Zhao G.-P., Zhou Z., Qu Y.;
RT "Genomic and secretomic analyses reveal unique features of the
RT lignocellulolytic enzyme system of Penicillium decumbens.";
RL PLoS ONE 8:E55185-E55185(2013).
CC -!- SIMILARITY: Belongs to the AAA ATPase family.
CC {ECO:0000256|ARBA:ARBA00006914, ECO:0000256|RuleBase:RU003651}.
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DR EMBL; KB644412; EPS30838.1; -; Genomic_DNA.
DR AlphaFoldDB; S8AX13; -.
DR STRING; 933388.S8AX13; -.
DR eggNOG; KOG0728; Eukaryota.
DR HOGENOM; CLU_000688_2_0_1; -.
DR OrthoDB; 1465143at2759; -.
DR PhylomeDB; S8AX13; -.
DR Proteomes; UP000019376; Unassembled WGS sequence.
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 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; 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:SF12; 26S PROTEASOME REGULATORY SUBUNIT 8; 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 Nucleotide-binding {ECO:0000256|RuleBase:RU003651};
KW Proteasome {ECO:0000256|ARBA:ARBA00022942};
KW Reference proteome {ECO:0000313|Proteomes:UP000019376}.
FT DOMAIN 165..304
FT /note="AAA+ ATPase"
FT /evidence="ECO:0000259|SMART:SM00382"
FT COILED 11..45
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 389 AA; 43429 MW; 2AF46732694B1237 CRC64;
MALDNYYRNK IESMKLEIIQ GQAVLRRLEA QRNDYNSRVR LLREELGLLQ QPGSYVGEVV
KVMSTKKVLV KVHPEGKYVV DIADGVDIAK LTVGKRVALL SDSYKLEKML PSSVDPLVSL
MMVEKVPDST YDMIGGLDQQ IKEIKEVIEL GLKHPELFES LGIAQPKGVL LYGPPGTGKT
LLARAVAHHT DCRFIRVSGS ELVQKYIGEG SRMVRELFVM AREHAPSIIF MDEIDSIGSS
RIDSAGGGDS EVQRTMLELL NQLDGFEPTK NIKIIMATNR LDILDPALLR PGRIDRKIEF
PPPSVEARAD ILRIHSRSMN LTRGINLTKI AEKMNGCSGA ELKGVCTEAG MYALRERRVH
VTQEDFDLAT AKILNKHDDK EVAVSKLWK
//
