ID   S3DUX3_GLAL2            Unreviewed;       886 AA.
AC   S3DUX3;
DT   18-SEP-2013, integrated into UniProtKB/TrEMBL.
DT   18-SEP-2013, sequence version 1.
DT   27-MAR-2024, entry version 40.
DE   SubName: Full=FtsH protease {ECO:0000313|EMBL:EPE30208.1};
GN   ORFNames=GLAREA_12931 {ECO:0000313|EMBL:EPE30208.1};
OS   Glarea lozoyensis (strain ATCC 20868 / MF5171).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC   Helotiales; Helotiaceae; Glarea.
OX   NCBI_TaxID=1116229 {ECO:0000313|EMBL:EPE30208.1, ECO:0000313|Proteomes:UP000016922};
RN   [1] {ECO:0000313|EMBL:EPE30208.1, ECO:0000313|Proteomes:UP000016922}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 20868 / MF5171 {ECO:0000313|Proteomes:UP000016922};
RX   PubMed=23688303; DOI=10.1186/1471-2164-14-339;
RA   Chen L., Yue Q., Zhang X., Xiang M., Wang C., Li S., Che Y.,
RA   Ortiz-Lopez F.J., Bills G.F., Liu X., An Z.;
RT   "Genomics-driven discovery of the pneumocandin biosynthetic gene cluster in
RT   the fungus Glarea lozoyensis.";
RL   BMC Genomics 14:339-339(2013).
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}.
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DR   EMBL; KE145365; EPE30208.1; -; Genomic_DNA.
DR   RefSeq; XP_008082885.1; XM_008084694.1.
DR   AlphaFoldDB; S3DUX3; -.
DR   STRING; 1116229.S3DUX3; -.
DR   MEROPS; M41.003; -.
DR   GeneID; 19471971; -.
DR   KEGG; glz:GLAREA_12931; -.
DR   eggNOG; KOG0731; Eukaryota.
DR   HOGENOM; CLU_000688_23_4_1; -.
DR   OMA; ARQKGNF; -.
DR   OrthoDB; 9585at2759; -.
DR   Proteomes; UP000016922; 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, ECO:0000313|EMBL:EPE30208.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000016922}.
FT   DOMAIN          440..581
FT                   /note="AAA+ ATPase"
FT                   /evidence="ECO:0000259|SMART:SM00382"
FT   REGION          44..105
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          193..229
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          860..886
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        52..70
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        86..100
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   886 AA;  97036 MW;  C8452737639E7ED1 CRC64;
     MSSILRLSSS SLAGIARGSV CRSTVRPGFA ACRLAASGRA NAPWQTRNFS STPRIREKKD
     ENEKKVEGKS APGTENLYEG KTPLSPTPEE KGEGKEEEQP LQDGYTYMNP QDLEAMESML
     KTWKQGMPPQ QVAHLEKSLE MMKKHGIPQE LRELVDKVRT SGKPMTLGDA ATLARLTTKA
     VYSTQKKVWE EEKSDKFPDF TSNERKSGGG AGSPPPGGNK GKGGSGPTPG FLQLDGGNFL
     VAAFASYLLF KLVMPGDQSR DITYQEFRST FFDKGLVEKL TVINRDRVRV DLHREATQAM
     YPESPAANPN FHYYFSIGSV EAFERRIDEA QSELQIPSSE RIPVSYATDT DAWALILSFG
     PTLLFIGAIF FFSRRASGGG GGASGVFGMG KSRAKQFNHE TDVKVKFKDV AGMDEAKMEI
     MEFVSFLKTP EQFERLGAKI PRGAILSGPP GTGKTLLAKA TAGESAVPFF SVSGSEFVEM
     FVGVGASRVR DLFAMARKNT PCIIFIDEID AIGKSRGKSG SLGGGNDERE ATLNQILTEM
     DGFNTQEQVV VLAGTNRPDV LDKALMRPGR FDRHIAIDRP TMDGRKQIFM VHLKKIVTNE
     DLEYLTGRLS ALTPGFSGAD IANCCNEAAL IAARTSAKSV AMIHFEQAIE RVIGGLEKRS
     LVLSPEEKKT VAYHEAGHAI CGWYFKHADP LLKVSIIPRG QGALGYAQYL PAGDTYLMNV
     NQLMDRMAMT LGGRVSEELH FETVTSGASD DFNKVTRMAT AMVTKWGMSK KLGPLHFEDD
     ENKLHKPFAE ATAQTIDSEV RRIVDDAYTK CRNLLESKKK EVGLVAEELL TKEVIGRDDM
     VRLLGPREFD ENKDFIKYFG GGPIPGGKSA PPPPPTEMPE GDTAVM
//