ID A0A067NYZ0_PLEOS Unreviewed; 658 AA.
AC A0A067NYZ0;
DT 03-SEP-2014, integrated into UniProtKB/TrEMBL.
DT 03-SEP-2014, sequence version 1.
DT 27-MAR-2024, entry version 33.
DE RecName: Full=AAA+ ATPase domain-containing protein {ECO:0000259|SMART:SM00382};
GN ORFNames=PLEOSDRAFT_48395 {ECO:0000313|EMBL:KDQ33288.1};
OS Pleurotus ostreatus PC15.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Agaricomycetidae; Agaricales; Pleurotineae; Pleurotaceae; Pleurotus.
OX NCBI_TaxID=1137138 {ECO:0000313|EMBL:KDQ33288.1, ECO:0000313|Proteomes:UP000027073};
RN [1] {ECO:0000313|Proteomes:UP000027073}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PC15 {ECO:0000313|Proteomes:UP000027073};
RX PubMed=24958869; DOI=10.1073/pnas.1400592111;
RA Riley R., Salamov A.A., Brown D.W., Nagy L.G., Floudas D., Held B.W.,
RA Levasseur A., Lombard V., Morin E., Otillar R., Lindquist E.A., Sun H.,
RA LaButti K.M., Schmutz J., Jabbour D., Luo H., Baker S.E., Pisabarro A.G.,
RA Walton J.D., Blanchette R.A., Henrissat B., Martin F., Cullen D.,
RA Hibbett D.S., Grigoriev I.V.;
RT "Extensive sampling of basidiomycete genomes demonstrates inadequacy of the
RT white-rot/brown-rot paradigm for wood decay fungi.";
RL Proc. Natl. Acad. Sci. U.S.A. 111:9923-9928(2014).
CC -!- SIMILARITY: Belongs to the AAA ATPase family.
CC {ECO:0000256|RuleBase:RU003651}.
CC -!- SIMILARITY: In the C-terminal section; belongs to the peptidase M41
CC family. {ECO:0000256|ARBA:ARBA00010044}.
CC -!- SIMILARITY: In the N-terminal section; belongs to the AAA ATPase
CC family. {ECO:0000256|ARBA:ARBA00010550}.
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DR EMBL; KL198004; KDQ33288.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A067NYZ0; -.
DR STRING; 1137138.A0A067NYZ0; -.
DR VEuPathDB; FungiDB:PLEOSDRAFT_48395; -.
DR HOGENOM; CLU_000688_9_2_1; -.
DR InParanoid; A0A067NYZ0; -.
DR OrthoDB; 9585at2759; -.
DR Proteomes; UP000027073; Unassembled WGS sequence.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR GO; GO:0004176; F:ATP-dependent peptidase activity; IEA:InterPro.
DR GO; GO:0004222; F:metalloendopeptidase activity; IEA:InterPro.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR Gene3D; 1.10.8.60; -; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR Gene3D; 1.20.58.760; Peptidase M41; 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; IPR027417; P-loop_NTPase.
DR InterPro; IPR000642; Peptidase_M41.
DR InterPro; IPR037219; Peptidase_M41-like.
DR PANTHER; PTHR23076:SF37; ATP-DEPENDENT ZINC METALLOPROTEASE YME1L1; 1.
DR PANTHER; PTHR23076; METALLOPROTEASE M41 FTSH; 1.
DR Pfam; PF00004; AAA; 1.
DR Pfam; PF17862; AAA_lid_3; 1.
DR Pfam; PF01434; Peptidase_M41; 1.
DR SMART; SM00382; AAA; 1.
DR SUPFAM; SSF140990; FtsH protease domain-like; 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:0000256|ARBA:ARBA00022801};
KW Nucleotide-binding {ECO:0000256|RuleBase:RU003651};
KW Protease {ECO:0000256|ARBA:ARBA00022670};
KW Reference proteome {ECO:0000313|Proteomes:UP000027073}.
FT DOMAIN 273..410
FT /note="AAA+ ATPase"
FT /evidence="ECO:0000259|SMART:SM00382"
FT REGION 1..30
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 156..175
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 590..628
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 658 AA; 71381 MW; ABE70136B040808F CRC64;
MIPRVGRSSG FSTGPSPSDK RVSASEHVAR SSVKAPFSPR YLSLGSIFSR NKPSPSPSPL
TVAHITSLES EANTNNHDVP KQLALFQALI QTDLKPGYEL VTTRWERMCE FDSSSPLLKS
DEAFQLYLTA LLRLGNPSSI PAAVRRRDSL LVGTGATTIP SQTEGSQGAS GRPVSKSQEI
ADSVLSAQAL GSTGTPVPPG SDMAKLAAAI QAAGGSAAAP VQVSIVELIL IIFAVLLENS
GLMKAGPRQA EFVPSEGKTV TFSDVHGVDE VKDVSLFELS SRSPGTGKTL LARAVAGEAG
VPFFFASGSD FEEMFVGVGA KRVRDLFAAA RKKQPAIIFI DELDAVGGKR SSRDQQYMKQ
TLNQLLVEMD GFMQTEGIIV IAATNFPESL DSALIRPGRF DRTIAVPLPD IRGRVQILNH
HMKGVTTSPD VDPTILARGT PGFSGADLQN MVNQAAIQAS KERATEVTLK HFEWAKDRIV
MGAERKSQYI DPKAKLATAF HETSQLPEDD QYSVSFKQYR AGIDVCLGGR VAEELTYGTE
NVSSGASSDL QKATGTATAM VKYWGFSDKI GRVYYGDRDN ISPQRRIEIE DEIRKLIQDS
EERVTKLLKE KQEELHRLAH ALVEHETLDA DEVRKVIKGE QIRNISEILQ EELSQTTP
//
