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Database: UniProt
Entry: A0A0M9VUQ0_9HYPO
LinkDB: A0A0M9VUQ0_9HYPO
Original site: A0A0M9VUQ0_9HYPO 
ID   A0A0M9VUQ0_9HYPO        Unreviewed;       391 AA.
AC   A0A0M9VUQ0;
DT   09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT   09-DEC-2015, sequence version 1.
DT   27-MAR-2024, entry version 36.
DE   SubName: Full=Putative 26S protease subunit rpt4 {ECO:0000313|EMBL:KOS20133.1};
GN   ORFNames=ESCO_006098 {ECO:0000313|EMBL:KOS20133.1};
OS   Escovopsis weberi.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Hypocreomycetidae; Hypocreales; Hypocreaceae; Escovopsis.
OX   NCBI_TaxID=150374 {ECO:0000313|EMBL:KOS20133.1, ECO:0000313|Proteomes:UP000053831};
RN   [1] {ECO:0000313|EMBL:KOS20133.1, ECO:0000313|Proteomes:UP000053831}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   de Man T.J., Stajich J.E., Kubicek C.P., Chenthamara K., Atanasova L.,
RA   Druzhinina I.S., Birnbaum S., Barribeau S.M., Teiling C., Suen G.,
RA   Currie C., Gerardo N.M.;
RT   "The genome of the fungus Escovopsis weberi, a specialized disease agent of
RT   ant agriculture.";
RL   Submitted (JUL-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:KOS20133.1}.
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DR   EMBL; LGSR01000018; KOS20133.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0M9VUQ0; -.
DR   STRING; 150374.A0A0M9VUQ0; -.
DR   OrthoDB; 360215at2759; -.
DR   Proteomes; UP000053831; 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   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:SF155; 26S PROTEASOME REGULATORY SUBUNIT 10B; 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:KOS20133.1};
KW   Nucleotide-binding {ECO:0000256|RuleBase:RU003651};
KW   Protease {ECO:0000313|EMBL:KOS20133.1};
KW   Proteasome {ECO:0000256|ARBA:ARBA00022942};
KW   Reference proteome {ECO:0000313|Proteomes:UP000053831}.
FT   DOMAIN          168..307
FT                   /note="AAA+ ATPase"
FT                   /evidence="ECO:0000259|SMART:SM00382"
FT   COILED          21..55
FT                   /evidence="ECO:0000256|SAM:Coils"
SQ   SEQUENCE   391 AA;  43951 MW;  C6344437A049ECC9 CRC64;
     MTPEEERQAA LNSYRAKLIE SREWEAKLKN LRLEIKDLQK EYDRTEDNIK ALQSVGQIIG
     EVLKQLDDER FIVKASSGPR YVVGCRSKVD KTKLKQGTRV ALDMTTLTIM RMLPREVDPL
     VYNMSLEDPG QVSFAGIGGL NDQIRELREV IELPLKNPEL FLRVGIKPPK GVLLYGPPGT
     GKTLLARAVA SSLETNFLKV VSSAIVDKYI GESARLIREM FGYAKEHEPC IIFMDEIDAI
     GGRRFSEGTS ADREIQRTLM ELLNQLDGFD YLGKTKIIMA TNRPDTLDPA LLRAGRLDRK
     IEIPLPNEVG RLEILKIHAS SVVIDGDIDF ESVVKMSDGL NGADLRNVVT EAGLCAIKDY
     RDSVNQDDFN RAVRKVMEAK KLEGKLEYQK L
//
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