ID G2X9W0_VERDV Unreviewed; 389 AA.
AC G2X9W0;
DT 16-NOV-2011, integrated into UniProtKB/TrEMBL.
DT 16-NOV-2011, sequence version 1.
DT 24-JAN-2024, entry version 61.
DE SubName: Full=26S protease regulatory subunit 8 {ECO:0000313|EMBL:EGY15991.1};
GN ORFNames=VDAG_07155 {ECO:0000313|EMBL:EGY15991.1};
OS Verticillium dahliae (strain VdLs.17 / ATCC MYA-4575 / FGSC 10137)
OS (Verticillium wilt).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Glomerellales; Plectosphaerellaceae; Verticillium.
OX NCBI_TaxID=498257 {ECO:0000313|EMBL:EGY15991.1, ECO:0000313|Proteomes:UP000001611};
RN [1] {ECO:0000313|Proteomes:UP000001611}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=VdLs.17 / ATCC MYA-4575 / FGSC 10137
RC {ECO:0000313|Proteomes:UP000001611};
RX PubMed=21829347; DOI=10.1371/journal.ppat.1002137;
RA Klosterman S.J., Subbarao K.V., Kang S., Veronese P., Gold S.E.,
RA Thomma B.P.H.J., Chen Z., Henrissat B., Lee Y.-H., Park J.,
RA Garcia-Pedrajas M.D., Barbara D.J., Anchieta A., de Jonge R., Santhanam P.,
RA Maruthachalam K., Atallah Z., Amyotte S.G., Paz Z., Inderbitzin P.,
RA Hayes R.J., Heiman D.I., Young S., Zeng Q., Engels R., Galagan J.,
RA Cuomo C.A., Dobinson K.F., Ma L.-J.;
RT "Comparative genomics yields insights into niche adaptation of plant
RT vascular wilt pathogens.";
RL PLoS Pathog. 7:E1002137-E1002137(2011).
CC -!- SIMILARITY: Belongs to the AAA ATPase family.
CC {ECO:0000256|ARBA:ARBA00006914, ECO:0000256|RuleBase:RU003651}.
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DR EMBL; DS572709; EGY15991.1; -; Genomic_DNA.
DR RefSeq; XP_009654355.1; XM_009656060.1.
DR AlphaFoldDB; G2X9W0; -.
DR STRING; 498257.G2X9W0; -.
DR EnsemblFungi; EGY15991; EGY15991; VDAG_07155.
DR GeneID; 20708618; -.
DR KEGG; vda:VDAG_07155; -.
DR eggNOG; KOG0728; Eukaryota.
DR HOGENOM; CLU_000688_2_0_1; -.
DR InParanoid; G2X9W0; -.
DR OMA; TANCRVA; -.
DR OrthoDB; 1465143at2759; -.
DR Proteomes; UP000001611; Chromosome 5.
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:EGY15991.1};
KW Nucleotide-binding {ECO:0000256|RuleBase:RU003651};
KW Protease {ECO:0000313|EMBL:EGY15991.1};
KW Proteasome {ECO:0000256|ARBA:ARBA00022942};
KW Reference proteome {ECO:0000313|Proteomes:UP000001611}.
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; 43434 MW; AFB6FD465B496FF8 CRC64;
MALDSYYQNK IEAMKLEILK GQAVLRRLEA QRNDYNSRVR LLREELGLLQ QPGSYVGEVV
KVMGTKKVLV KVHPEGKYVV DIADSVDVTK LTVGKRVTLL SDSYKLEKML PSSVDPLVSL
MMVEKVPDST YDMIGGLDQQ IKEIKEVIEL GLKHPELFES LGIAQPKGVL LYGPPGTGKT
LLARAVAHHT DCKFIRVSGS ELVQKYIGEG SRMVRELFVM AREHAPSIIF MDEIDSIGSS
RVEGSSGGDS EVQRTMLELL NQLDGFEPTK NIKIIMATNR LDILDPALLR PGRIDRKIEF
PPPSVEARAD ILRIHSRKMN LTRGINLTKV AEKMNGCSGA ELKGVCTEAG MYALRERRVH
VTQEDFELAT AKILNKHDDK EVSLGKLWK
//