ID E5ACS9_LEPMJ Unreviewed; 1184 AA.
AC E5ACS9;
DT 08-FEB-2011, integrated into UniProtKB/TrEMBL.
DT 08-FEB-2011, sequence version 1.
DT 27-MAR-2024, entry version 74.
DE RecName: Full=AAA+ ATPase domain-containing protein {ECO:0000259|SMART:SM00382};
GN ORFNames=LEMA_P010680.1 {ECO:0000313|EMBL:CBY02281.1};
OS Leptosphaeria maculans (strain JN3 / isolate v23.1.3 / race Av1-4-5-6-7-8)
OS (Blackleg fungus) (Phoma lingam).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Pleosporomycetidae; Pleosporales; Pleosporineae; Leptosphaeriaceae;
OC Plenodomus; Plenodomus lingam/Leptosphaeria maculans species complex.
OX NCBI_TaxID=985895 {ECO:0000313|EMBL:CBY02281.1, ECO:0000313|Proteomes:UP000002668};
RN [1] {ECO:0000313|Proteomes:UP000002668}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JN3 / isolate v23.1.3 / race Av1-4-5-6-7-8
RC {ECO:0000313|Proteomes:UP000002668};
RX PubMed=21326234; DOI=10.1038/ncomms1189;
RA Rouxel T., Grandaubert J., Hane J.K., Hoede C., van de Wouw A.P.,
RA Couloux A., Dominguez V., Anthouard V., Bally P., Bourras S.,
RA Cozijnsen A.J., Ciuffetti L.M., Degrave A., Dilmaghani A., Duret L.,
RA Fudal I., Goodwin S.B., Gout L., Glaser N., Linglin J., Kema G.H.J.,
RA Lapalu N., Lawrence C.B., May K., Meyer M., Ollivier B., Poulain J.,
RA Schoch C.L., Simon A., Spatafora J.W., Stachowiak A., Turgeon B.G.,
RA Tyler B.M., Vincent D., Weissenbach J., Amselem J., Quesneville H.,
RA Oliver R.P., Wincker P., Balesdent M.-H., Howlett B.J.;
RT "Effector diversification within compartments of the Leptosphaeria maculans
RT genome affected by Repeat-Induced Point mutations.";
RL Nat. Commun. 2:202-202(2011).
CC -!- SIMILARITY: Belongs to the AAA ATPase family.
CC {ECO:0000256|ARBA:ARBA00006914}.
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DR EMBL; FP929139; CBY02281.1; -; Genomic_DNA.
DR RefSeq; XP_003845760.1; XM_003845712.1.
DR AlphaFoldDB; E5ACS9; -.
DR STRING; 985895.E5ACS9; -.
DR EnsemblFungi; CBY02281; CBY02281; LEMA_P010680.1.
DR GeneID; 13286521; -.
DR eggNOG; KOG0741; Eukaryota.
DR HOGENOM; CLU_008037_0_0_1; -.
DR InParanoid; E5ACS9; -.
DR OMA; HRESHFN; -.
DR OrthoDB; 553800at2759; -.
DR Proteomes; UP000002668; Genome.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR GO; GO:0035494; P:SNARE complex disassembly; IEA:InterPro.
DR CDD; cd00009; AAA; 1.
DR Gene3D; 1.10.8.60; -; 2.
DR Gene3D; 2.40.40.20; -; 1.
DR Gene3D; 3.10.330.10; -; 1.
DR Gene3D; 3.90.1140.10; Cyclic phosphodiesterase; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 2.
DR InterPro; IPR003593; AAA+_ATPase.
DR InterPro; IPR041569; AAA_lid_3.
DR InterPro; IPR009010; Asp_de-COase-like_dom_sf.
DR InterPro; IPR003959; ATPase_AAA_core.
DR InterPro; IPR003960; ATPase_AAA_CS.
DR InterPro; IPR004201; Cdc48_dom2.
DR InterPro; IPR029067; CDC48_domain_2-like_sf.
DR InterPro; IPR009097; Cyclic_Pdiesterase.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR039812; Vesicle-fus_ATPase.
DR PANTHER; PTHR23078:SF3; VESICLE-FUSING ATPASE; 1.
DR PANTHER; PTHR23078; VESICULAR-FUSION PROTEIN NSF; 1.
DR Pfam; PF00004; AAA; 2.
DR Pfam; PF17862; AAA_lid_3; 1.
DR Pfam; PF02933; CDC48_2; 1.
DR SMART; SM00382; AAA; 2.
DR SUPFAM; SSF50692; ADC-like; 1.
DR SUPFAM; SSF54585; Cdc48 domain 2-like; 1.
DR SUPFAM; SSF55144; LigT-like; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 2.
DR PROSITE; PS00674; AAA; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Protein transport {ECO:0000256|ARBA:ARBA00022927};
KW Reference proteome {ECO:0000313|Proteomes:UP000002668};
KW Transport {ECO:0000256|ARBA:ARBA00022448}.
FT DOMAIN 690..838
FT /note="AAA+ ATPase"
FT /evidence="ECO:0000259|SMART:SM00382"
FT DOMAIN 972..1108
FT /note="AAA+ ATPase"
FT /evidence="ECO:0000259|SMART:SM00382"
FT REGION 370..444
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1184 AA; 130325 MW; 4DF29D8496B2911D CRC64;
MTDGKAVPAH VSNAFVDLSG ISTSEFRNPY DALISACVDD PAQIQSKYTL HRTTRNAQQK
EKLLAADFPG VSIDPILQKL SNPSIEPGYK DPRHCLVFWG RPTQKVKEMI HRVQQELQTV
APNLWIMPQD CLHITVLEVT HSKTAEEIQQ LVEQIRTAAP AITDYPYNHR ARLIKPLIGY
DASALALSFV PAAGEGLPSG RTVTDDKFTY HHLRRDVFDL CRDAGVQVDS RYVVPSSHLT
IGRFIDTKDF SDQSGKPDPL KMKAFVAKIE EINTWLEREF WPEQNRGIIP AGGEFNVGEE
QGLNCRMGTL WYGGGETVHA VPKQQRSLER NARHTHFTLA GQLYLQLYLG TIDTWQTYFL
CYQTTNPSNM FNRDRLPGLP GSSPRPPPRN DGYGRPPAQQ QPPQRSPGPD TRMGGYDDRS
QRMPSRGPPG GGSPARQLRP IKSPGGNAYA FGNLVAVSPQ DFPPAPDGSD IYIILNGGYV
LSARPTQGCP PGEIGLTDAQ RTWAGITLGP QDVVSVQPYD AFSQSGGQSY LGAVEVEVGF
AARKTTDTPY DQDELATQFK KNFENQILAP GQQLLLDVKN IPLRMSVRTV QLVDLSMEKK
DSSAPPLTDP RARGILTSHT QIDFFKDART DIKLKASTRR PAANSIIQPG FKFEDMGIGG
LDTEFSAIFR RAFASRIFPP GLVEKLGIQH VRGILLYGPP GTGKTLIARQ IGSMLNAREP
KVINGPEVLN KYVGQSEENI RKLFADAEKE YKEKGDESGL HIIIFDELDA VCKQRGSGAG
GGTGVGDSVV NQLLSKLDGV DQLNNILLIG MTNRMDMIDE ALLRPGRLEV HMEISLPDES
GRAQILKIHT TKMRANDVLD SDVSLEELAR LTKNFSGAEL NGLVKAASSY AFSRHIKVGT
MAAINPDVEN MKVNRQDFMS ALDEVKPLFG VAEEELGKRL LRGIINFSPF IRDILDEGRL
YINQVRKPDS TPILSVALHG PPGSGKTALA AKMAIDSGYP FIKLISPEDM VGFSEMQKVQ
QLDKTFRDAY KSPLSVIVID NIEMLVDWVP IGPRFSNSVL VALKVLLEKQ PPKGRRLLIF
ATTTERSVLT QLDLFSRFDA EIAVPNVNTQ AELANVLQES GAFSESDQQR AIGEIQEITG
SAEVGVGIKK ILTGIETAKQ DQDVPGRFAR VMSRAIAANR GLQN
//
