ID A0A167ZAW2_9HYPO Unreviewed; 421 AA.
AC A0A167ZAW2;
DT 06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT 06-JUL-2016, sequence version 1.
DT 27-MAR-2024, entry version 34.
DE SubName: Full=26S protease regulatory subunit 6B {ECO:0000313|EMBL:KZZ92415.1};
GN ORFNames=AAL_06041 {ECO:0000313|EMBL:KZZ92415.1};
OS Moelleriella libera RCEF 2490.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Clavicipitaceae; Moelleriella.
OX NCBI_TaxID=1081109 {ECO:0000313|EMBL:KZZ92415.1, ECO:0000313|Proteomes:UP000078544};
RN [1] {ECO:0000313|EMBL:KZZ92415.1, ECO:0000313|Proteomes:UP000078544}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=RCEF 2490 {ECO:0000313|EMBL:KZZ92415.1,
RC ECO:0000313|Proteomes:UP000078544};
RX PubMed=27071652; DOI=10.1093/gbe/evw082;
RA Shang Y., Xiao G., Zheng P., Cen K., Zhan S., Wang C.;
RT "Divergent and convergent evolution of fungal pathogenicity.";
RL Genome Biol. Evol. 8:1374-1387(2016).
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:KZZ92415.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AZGY01000015; KZZ92415.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A167ZAW2; -.
DR STRING; 1081109.A0A167ZAW2; -.
DR OrthoDB; 5477077at2759; -.
DR Proteomes; UP000078544; 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; 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:SF8; 26S PROTEASOME REGULATORY SUBUNIT 6B; 1.
DR Pfam; PF00004; AAA; 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:KZZ92415.1};
KW Nucleotide-binding {ECO:0000256|RuleBase:RU003651};
KW Protease {ECO:0000313|EMBL:KZZ92415.1};
KW Proteasome {ECO:0000256|ARBA:ARBA00022942};
KW Reference proteome {ECO:0000313|Proteomes:UP000078544}.
FT DOMAIN 198..337
FT /note="AAA+ ATPase"
FT /evidence="ECO:0000259|SMART:SM00382"
FT COILED 58..85
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 421 AA; 47066 MW; 9C6764299D69182F CRC64;
MGDVAVESQA NHVPFYKKTA ASTIPTIDSF EGLPSEGGDE YATLKKLQRQ LEYIQLQEEY
IKDEQRSLKR ELVRAQEEIK RIQSVPLVIG QFMEAIDQNS GIVQSSTGSN YFVRILSTLD
RELLKPSSSV ALHRHSNALV DILPPEADSS IAMLGADEKP DVTYADVGGL DMQKQEIREA
VELPLTHFDL YKQIGIDPPR GVLLYGPPGT GKTMLVKAVA NSTTASFIRV VGSEFVQKYL
GEGPRMVRDV FRMARENSPA IIFIDEIDAI ATKRFDAQTG ADREVQRILL ELLNQMDGFD
QTSNVKVIMA TNRADTLDPA LLRPGRLDRK IEFPSLRDRR ERRLIFTTIA SKMSLAPEVD
LDSLIVRNDP LSGAIIAAIM QEAGLRAVRK NRYNIIQSDL EDAYSAQVKG TNDDNKFDFY
K
//
