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Database: UniProt
Entry: A0A135UBZ0_9PEZI
LinkDB: A0A135UBZ0_9PEZI
Original site: A0A135UBZ0_9PEZI 
ID   A0A135UBZ0_9PEZI        Unreviewed;       439 AA.
AC   A0A135UBZ0;
DT   06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT   06-JUL-2016, sequence version 1.
DT   27-MAR-2024, entry version 28.
DE   SubName: Full=26S protease regulatory subunit 7 {ECO:0000313|EMBL:KXH57891.1};
GN   ORFNames=CSAL01_09097 {ECO:0000313|EMBL:KXH57891.1};
OS   Colletotrichum salicis.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Hypocreomycetidae; Glomerellales; Glomerellaceae; Colletotrichum;
OC   Colletotrichum acutatum species complex.
OX   NCBI_TaxID=1209931 {ECO:0000313|EMBL:KXH57891.1, ECO:0000313|Proteomes:UP000070121};
RN   [1] {ECO:0000313|EMBL:KXH57891.1, ECO:0000313|Proteomes:UP000070121}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CBS 607.94 {ECO:0000313|EMBL:KXH57891.1,
RC   ECO:0000313|Proteomes:UP000070121};
RA   Baroncelli R., Thon M.R.;
RT   "The genome sequence of Colletotrichum salicis CBS 607.94.";
RL   Submitted (FEB-2014) to the EMBL/GenBank/DDBJ databases.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
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:KXH57891.1}.
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DR   EMBL; JFFI01001592; KXH57891.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A135UBZ0; -.
DR   STRING; 1209931.A0A135UBZ0; -.
DR   OrthoDB; 5488626at2759; -.
DR   Proteomes; UP000070121; Unassembled WGS sequence.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
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; IPR048723; PRS7-like_OB.
DR   PANTHER; PTHR23073; 26S PROTEASOME REGULATORY SUBUNIT; 1.
DR   PANTHER; PTHR23073:SF13; 26S PROTEASOME REGULATORY SUBUNIT 7; 1.
DR   Pfam; PF00004; AAA; 1.
DR   Pfam; PF17862; AAA_lid_3; 1.
DR   Pfam; PF21236; PRS7_OB; 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   Hydrolase {ECO:0000313|EMBL:KXH57891.1};
KW   Nucleotide-binding {ECO:0000256|RuleBase:RU003651};
KW   Protease {ECO:0000313|EMBL:KXH57891.1};
KW   Proteasome {ECO:0000256|ARBA:ARBA00022942};
KW   Reference proteome {ECO:0000313|Proteomes:UP000070121}.
FT   DOMAIN          214..353
FT                   /note="AAA+ ATPase"
FT                   /evidence="ECO:0000259|SMART:SM00382"
SQ   SEQUENCE   439 AA;  48979 MW;  DA66981D81459E20 CRC64;
     MPSATGQNWE KYQKTYADDE VEEKKITPLT DEDIQVLKTY GAAPYGAAIK KLEQQIKEKQ
     TSVDEKIGVK ESDTGLAPPH LWDVAADRQR MSEEQPLQVA RCTKIIPDEK DDSKSKYVIN
     VKQIAKFVVQ LGERVSPTDI EEGMRVGVDR NKYQILLPLP PKIDASVTMM TVEEKPDVTY
     GDVGGSKEQV EKLREVVEMP LLSPERFVNL GIDPPKGALL YGPPGTGKTL CARAVANRTD
     ATFIRVIGSE LVQKYVGEGA RMVRELFEMA RTKKACIIFF DEIDAIGGAR FDDGAGGDNE
     VQRTMLELIT QLDGFDARGN IKVMFATNRP STLDPALMRP GRIDRKIEFS LPDLEGRANI
     LRIHAKSMSV ERDIRWELIS RLCPNATGAE LRSVCTEAGM FAIRARRKVA TEKDFLSAVD
     KVIKANLKFN STASYMQYN
//
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