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Database: UniProt
Entry: A0A1J9QRR5_9PEZI
LinkDB: A0A1J9QRR5_9PEZI
Original site: A0A1J9QRR5_9PEZI 
ID   A0A1J9QRR5_9PEZI        Unreviewed;       394 AA.
AC   A0A1J9QRR5;
DT   15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT   15-FEB-2017, sequence version 1.
DT   27-MAR-2024, entry version 33.
DE   SubName: Full=26s protease regulatory subunit s10b {ECO:0000313|EMBL:OJD31144.1};
GN   ORFNames=BKCO1_5200076 {ECO:0000313|EMBL:OJD31144.1};
OS   Diplodia corticola.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC   Dothideomycetes incertae sedis; Botryosphaeriales; Botryosphaeriaceae;
OC   Diplodia.
OX   NCBI_TaxID=236234 {ECO:0000313|EMBL:OJD31144.1, ECO:0000313|Proteomes:UP000183809};
RN   [1] {ECO:0000313|EMBL:OJD31144.1, ECO:0000313|Proteomes:UP000183809}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CBS 112549 {ECO:0000313|EMBL:OJD31144.1,
RC   ECO:0000313|Proteomes:UP000183809};
RA   Fernandes I., De Jonge R., Van De Peer Y., Devreese B., Alves A.,
RA   Esteves A.C.;
RT   "Proteomics and genomics reveal pathogen-plant mechanisms compatible with a
RT   hemibiotrophic lifestyle of Diplodia corticola.";
RL   Submitted (OCT-2016) 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:OJD31144.1}.
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DR   EMBL; MNUE01000052; OJD31144.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1J9QRR5; -.
DR   STRING; 236234.A0A1J9QRR5; -.
DR   OrthoDB; 360215at2759; -.
DR   Proteomes; UP000183809; 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:OJD31144.1};
KW   Nucleotide-binding {ECO:0000256|RuleBase:RU003651};
KW   Protease {ECO:0000313|EMBL:OJD31144.1};
KW   Proteasome {ECO:0000256|ARBA:ARBA00022942};
KW   Reference proteome {ECO:0000313|Proteomes:UP000183809}.
FT   DOMAIN          171..310
FT                   /note="AAA+ ATPase"
FT                   /evidence="ECO:0000259|SMART:SM00382"
FT   COILED          24..58
FT                   /evidence="ECO:0000256|SAM:Coils"
SQ   SEQUENCE   394 AA;  44115 MW;  ED0668444306AB18 CRC64;
     MSGTGLDPER EHALDEYKAK LLESREWEAK LKALRLEIKG LQRDYDVSEE NIKALQSVGQ
     IIGEVLKQLD EERFIVKASS GPRYVVGCRS KVDKAKLKQG TRVALDMTTL TIMRMLPREV
     DPLVYNMSLE DPGQVSFGGI GGLNEQIREL REVIELPLKN PELFLRVGIK PPKGVLLYGP
     PGTGKTLLAR AVASSLETNF LKVVSSAIVD KYIGESARLI REMFGYAKEH EPCIIFMDEI
     DAIGGRRFSE GTSADREIQR TLMELLNQLD GFDYLGKTKI IMATNRPDTL DPALLRAGRL
     DRKIEIALPN EVGRLEIMKI HAASVQSEGE IDFESIVKMS DGFNGADLRN VVTEAGLFAI
     KDYRDAINQD DFNKAVRKMA ETKKLEGKLE YQKL
//
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