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Database: UniProt
Entry: N1Q5E1_DOTSN
LinkDB: N1Q5E1_DOTSN
Original site: N1Q5E1_DOTSN 
ID   N1Q5E1_DOTSN            Unreviewed;       439 AA.
AC   N1Q5E1;
DT   26-JUN-2013, integrated into UniProtKB/TrEMBL.
DT   26-JUN-2013, sequence version 1.
DT   27-MAR-2024, entry version 43.
DE   RecName: Full=AAA+ ATPase domain-containing protein {ECO:0000259|SMART:SM00382};
GN   ORFNames=DOTSEDRAFT_141754 {ECO:0000313|EMBL:EME50405.1};
OS   Dothistroma septosporum (strain NZE10 / CBS 128990) (Red band needle blight
OS   fungus) (Mycosphaerella pini).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC   Dothideomycetidae; Mycosphaerellales; Mycosphaerellaceae; Dothistroma.
OX   NCBI_TaxID=675120 {ECO:0000313|EMBL:EME50405.1, ECO:0000313|Proteomes:UP000016933};
RN   [1] {ECO:0000313|Proteomes:UP000016933}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NZE10 / CBS 128990 {ECO:0000313|Proteomes:UP000016933};
RX   PubMed=23209441; DOI=10.1371/journal.pgen.1003088;
RA   de Wit P.J.G.M., van der Burgt A., Oekmen B., Stergiopoulos I.,
RA   Abd-Elsalam K.A., Aerts A.L., Bahkali A.H., Beenen H.G., Chettri P.,
RA   Cox M.P., Datema E., de Vries R.P., Dhillon B., Ganley A.R.,
RA   Griffiths S.A., Guo Y., Hamelin R.C., Henrissat B., Kabir M.S.,
RA   Jashni M.K., Kema G., Klaubauf S., Lapidus A., Levasseur A., Lindquist E.,
RA   Mehrabi R., Ohm R.A., Owen T.J., Salamov A., Schwelm A., Schijlen E.,
RA   Sun H., van den Burg H.A., van Ham R.C.H.J., Zhang S., Goodwin S.B.,
RA   Grigoriev I.V., Collemare J., Bradshaw R.E.;
RT   "The genomes of the fungal plant pathogens Cladosporium fulvum and
RT   Dothistroma septosporum reveal adaptation to different hosts and lifestyles
RT   but also signatures of common ancestry.";
RL   PLoS Genet. 8:E1003088-E1003088(2012).
RN   [2] {ECO:0000313|EMBL:EME50405.1, ECO:0000313|Proteomes:UP000016933}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NZE10 / CBS 128990 {ECO:0000313|Proteomes:UP000016933};
RX   PubMed=23236275; DOI=10.1371/journal.ppat.1003037;
RA   Ohm R.A., Feau N., Henrissat B., Schoch C.L., Horwitz B.A., Barry K.W.,
RA   Condon B.J., Copeland A.C., Dhillon B., Glaser F., Hesse C.N., Kosti I.,
RA   LaButti K., Lindquist E.A., Lucas S., Salamov A.A., Bradshaw R.E.,
RA   Ciuffetti L., Hamelin R.C., Kema G.H.J., Lawrence C., Scott J.A.,
RA   Spatafora J.W., Turgeon B.G., de Wit P.J.G.M., Zhong S., Goodwin S.B.,
RA   Grigoriev I.V.;
RT   "Diverse lifestyles and strategies of plant pathogenesis encoded in the
RT   genomes of eighteen Dothideomycetes fungi.";
RL   PLoS Pathog. 8:E1003037-E1003037(2012).
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}.
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DR   EMBL; KB446535; EME50405.1; -; Genomic_DNA.
DR   AlphaFoldDB; N1Q5E1; -.
DR   STRING; 675120.N1Q5E1; -.
DR   EnsemblFungi; EME50405; EME50405; DOTSEDRAFT_141754.
DR   eggNOG; KOG0729; Eukaryota.
DR   HOGENOM; CLU_000688_6_2_1; -.
DR   OMA; INGYKKF; -.
DR   OrthoDB; 5488626at2759; -.
DR   Proteomes; UP000016933; Unassembled WGS sequence.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR   GO; GO:0008540; C:proteasome regulatory particle, base subcomplex; IEA:EnsemblFungi.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR   GO; GO:0031625; F:ubiquitin protein ligase binding; IEA:EnsemblFungi.
DR   GO; GO:0045732; P:positive regulation of protein catabolic process; IEA:EnsemblFungi.
DR   GO; GO:0045899; P:positive regulation of RNA polymerase II transcription preinitiation complex assembly; IEA:EnsemblFungi.
DR   GO; GO:0070682; P:proteasome regulatory particle assembly; IEA:EnsemblFungi.
DR   GO; GO:0043161; P:proteasome-mediated ubiquitin-dependent protein catabolic process; IEA:EnsemblFungi.
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   Nucleotide-binding {ECO:0000256|RuleBase:RU003651};
KW   Proteasome {ECO:0000256|ARBA:ARBA00022942};
KW   Reference proteome {ECO:0000313|Proteomes:UP000016933}.
FT   DOMAIN          214..353
FT                   /note="AAA+ ATPase"
FT                   /evidence="ECO:0000259|SMART:SM00382"
SQ   SEQUENCE   439 AA;  48938 MW;  57B1D8C5E9EB7459 CRC64;
     MPSATGSNWE KYQKKFADDE VEEKKITPLT DEDIQVLKTY NSAPYAQALK ELEKAIKDKQ
     TSVNEKIGVK ESDTGLAPPH LWDIAADRQR MSEEQPLQVA RCTKIIPDEK DSEKSKYVIN
     VKQIAKFVVN LGERVSPTDI EEGMRVGVDR NKYQIMLPLP PKIDPSVTMM TVEDKPDVTY
     GDVGGCKEQI EKLREVVEMP LLSPERFVNL GIDPPKGALL YGPPGTGKTL CARAVANRTD
     ATFIRVIGSE LVQKYVGEGA RMVRELFEMA RTKKACIIFF DEIDAVGGAR FDDGAGGDNE
     VQRTMLELIT QLDGFDSRGN IKVMFATNRP STLDPALMRP GRIDRKIEFA LPDMEGRANI
     LRIHAKSMSV ERDIRWELIS RLCPNATGAE LRSVATEAGM FAIRARRKVA SEKDFLSAVE
     KVIRGGTKFS STAVYAQYN
//
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