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Database: UniProt
Entry: A0A409VLC5_9AGAR
LinkDB: A0A409VLC5_9AGAR
Original site: A0A409VLC5_9AGAR 
ID   A0A409VLC5_9AGAR        Unreviewed;       760 AA.
AC   A0A409VLC5;
DT   08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT   08-MAY-2019, sequence version 1.
DT   27-MAR-2024, entry version 19.
DE   RecName: Full=AAA+ ATPase domain-containing protein {ECO:0000259|SMART:SM00382};
GN   ORFNames=CVT26_009930 {ECO:0000313|EMBL:PPQ67033.1};
OS   Gymnopilus dilepis.
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC   Agaricomycetidae; Agaricales; Agaricineae; Hymenogastraceae; Gymnopilus.
OX   NCBI_TaxID=231916 {ECO:0000313|EMBL:PPQ67033.1, ECO:0000313|Proteomes:UP000284706};
RN   [1] {ECO:0000313|EMBL:PPQ67033.1, ECO:0000313|Proteomes:UP000284706}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SRW20 {ECO:0000313|EMBL:PPQ67033.1,
RC   ECO:0000313|Proteomes:UP000284706};
RX   PubMed=30283667; DOI=10.1002/evl3.42;
RA   Reynolds H.T., Vijayakumar V., Gluck-Thaler E., Korotkin H.B.,
RA   Matheny P.B., Slot J.C.;
RT   "Horizontal gene cluster transfer increased hallucinogenic mushroom
RT   diversity.";
RL   Evol. Lett. 2:88-101(2018).
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000256|ARBA:ARBA00001947};
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}.
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:PPQ67033.1}.
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DR   EMBL; NHYE01005615; PPQ67033.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A409VLC5; -.
DR   STRING; 231916.A0A409VLC5; -.
DR   InParanoid; A0A409VLC5; -.
DR   OrthoDB; 9585at2759; -.
DR   Proteomes; UP000284706; Unassembled WGS sequence.
DR   GO; GO:0016020; C:membrane; IEA:InterPro.
DR   GO; GO:0005524; F:ATP binding; IEA:InterPro.
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:0008270; F:zinc ion binding; IEA:InterPro.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR   CDD; cd19501; RecA-like_FtsH; 1.
DR   Gene3D; 1.10.8.60; -; 1.
DR   Gene3D; 3.40.1690.20; -; 1.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR   Gene3D; 1.20.58.760; Peptidase M41; 1.
DR   HAMAP; MF_01458; FtsH; 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; IPR005936; FtsH.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR011546; Pept_M41_FtsH_extracell.
DR   InterPro; IPR000642; Peptidase_M41.
DR   InterPro; IPR037219; Peptidase_M41-like.
DR   NCBIfam; TIGR01241; FtsH_fam; 1.
DR   PANTHER; PTHR43655; ATP-DEPENDENT PROTEASE; 1.
DR   PANTHER; PTHR43655:SF2; SD01613P; 1.
DR   Pfam; PF00004; AAA; 1.
DR   Pfam; PF17862; AAA_lid_3; 1.
DR   Pfam; PF06480; FtsH_ext; 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   Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Metalloprotease {ECO:0000256|ARBA:ARBA00023049};
KW   Protease {ECO:0000256|ARBA:ARBA00022670};
KW   Reference proteome {ECO:0000313|Proteomes:UP000284706}.
FT   DOMAIN          292..432
FT                   /note="AAA+ ATPase"
FT                   /evidence="ECO:0000259|SMART:SM00382"
FT   REGION          1..95
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          713..760
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        713..727
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        729..743
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   760 AA;  83594 MW;  36CA56C08D1C2C42 CRC64;
     MLSRSLRAAA RLRPRSVPIA AVRAFATPSP KKEGQSDNKP SKPELPKALE GFFKQYKESQ
     RRQPSSDQKS SSENQSGGRR DRKDQQQPPP PQQNGFNQQQ LAWIVASATA YLLWSSSSAH
     NSKEITWQEF RANFLDKGLV ESLTVVNKHH VRVKLHPNAS GTNPGEFYFT IGSVDAFERK
     IDDAQTELGI PSSERIPVSY VDEISSVGAL LNFAPTLLLI GVLYWISRRG SSGSAGGIFN
     IGKSRAKLFN HESEVKVKFS DVAGMDEAKE EIMEFVKFLK EPAKYEKLGA KIPRGAILSG
     PPGTGKTLLA KATAGEASVP FLSVSGSEFV EMFVGVGSSR VRDLFASAKK NAPCIIFIDE
     IDAIGKARGK GGSFGGNDER ESTLNQLLVE MDGFGTNEHI VVLAGTNRPD VLDPALMRPG
     RFDRHIAIDR PDVSGRKGIY LVHLKPIRLE DSLKSDLESF AQKLAVLTPG FSGADIANVC
     NEAALHAARR GSDYVEQVDF DTAIERVIVG LEKKSRVLSP EEKKTVAYHE AGHAICGWFL
     EHADPLLKVS IIPRGAGALG YAQYLPADRY LLSTPQMMDR ICMTLGGRVS EEIFFGAENI
     TTGAQDDLQK ITRMAFEACA NYGMNDVIGP VSYGGDRAAK ESWTKPFSEK TAEMLDFEVR
     KMITTAYSRT RDLLTLHKEN VEKVAKRLLE KEVITREDMI ELLGKRPFAG RADDMDKWLD
     ENRGEKSAPP PLESPPQSDV DDPLPQPAPM TKSLDDRSLL
//
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