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Database: UniProt
Entry: A0A0N0DGY8_FUSLA
LinkDB: A0A0N0DGY8_FUSLA
Original site: A0A0N0DGY8_FUSLA 
ID   A0A0N0DGY8_FUSLA        Unreviewed;       389 AA.
AC   A0A0N0DGY8;
DT   09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT   09-DEC-2015, sequence version 1.
DT   24-JAN-2024, entry version 40.
DE   SubName: Full=26s protease regulatory subunit 8 {ECO:0000313|EMBL:KPA44794.1};
GN   ORFNames=FLAG1_02241 {ECO:0000313|EMBL:KPA44794.1};
OS   Fusarium langsethiae.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Hypocreomycetidae; Hypocreales; Nectriaceae; Fusarium.
OX   NCBI_TaxID=179993 {ECO:0000313|EMBL:KPA44794.1, ECO:0000313|Proteomes:UP000037904};
RN   [1] {ECO:0000313|EMBL:KPA44794.1, ECO:0000313|Proteomes:UP000037904}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Fl201059 {ECO:0000313|EMBL:KPA44794.1,
RC   ECO:0000313|Proteomes:UP000037904};
RA   Lysoe E., Divon H.H., Terzi V., Orru L., Lamontanara A., Kolseth A.-K.,
RA   Frandsen R.J., Nielsen K., Thrane U.;
RT   "The draft genome sequence of Fusarium langsethiae, a T-2/HT-2 mycotoxin
RT   producer.";
RL   Submitted (APR-2015) to the EMBL/GenBank/DDBJ databases.
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:KPA44794.1}.
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DR   EMBL; JXCE01000021; KPA44794.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0N0DGY8; -.
DR   OrthoDB; 1465143at2759; -.
DR   Proteomes; UP000037904; 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   GO; GO:0008233; F:peptidase activity; IEA:UniProtKB-KW.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
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   Hydrolase {ECO:0000313|EMBL:KPA44794.1};
KW   Nucleotide-binding {ECO:0000256|RuleBase:RU003651};
KW   Protease {ECO:0000313|EMBL:KPA44794.1};
KW   Proteasome {ECO:0000256|ARBA:ARBA00022942};
KW   Reference proteome {ECO:0000313|Proteomes:UP000037904}.
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;  43427 MW;  6DFF17871917268E CRC64;
     MALDEYYHNK IEAMKLEILK GQAALRRLEA QRNDYNSRVR LLREELGLLQ QPGSYVGEVV
     KVMSTKKILV KVHPEGKYVV DVSDSVDVAK LTPGKRVTLL SDSYKLEKML PSSVDPLVSL
     MMVEKVPDST YDMIGGLDQQ IKEIKEVIEL GLKHPELFES LGIAQPKGVL LYGPPGTGKT
     LLARAVAHHT ACKFIRVSGS ELVQKYIGEG SRMVRELFVM AREHAPSIIF MDEIDSIGSS
     RVEGSSGGDS EVQRTMLELL NQLDGFEPTK NIKVIMATNR LDILDPALLR PGRIDRKIEF
     PPPSVEARAD ILRIHSRKMN LTRGINLTKI AEKMNGCSGA ELKGVCTEAG MYALRERRVH
     VTQEDFELAT AKILNKHDDK EVSLGKLWK
//
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