ID A0A165D575_EXIGL Unreviewed; 648 AA.
AC A0A165D575;
DT 06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT 06-JUL-2016, sequence version 1.
DT 27-MAR-2024, entry version 28.
DE SubName: Full=ATP-dependent metallopeptidase Hfl {ECO:0000313|EMBL:KZV83808.1};
GN ORFNames=EXIGLDRAFT_683451 {ECO:0000313|EMBL:KZV83808.1};
OS Exidia glandulosa HHB12029.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Auriculariales; Exidiaceae; Exidia.
OX NCBI_TaxID=1314781 {ECO:0000313|EMBL:KZV83808.1, ECO:0000313|Proteomes:UP000077266};
RN [1] {ECO:0000313|EMBL:KZV83808.1, ECO:0000313|Proteomes:UP000077266}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HHB12029 {ECO:0000313|EMBL:KZV83808.1,
RC ECO:0000313|Proteomes:UP000077266};
RX PubMed=26659563; DOI=10.1093/molbev/msv337;
RA Nagy L.G., Riley R., Tritt A., Adam C., Daum C., Floudas D., Sun H.,
RA Yadav J.S., Pangilinan J., Larsson K.H., Matsuura K., Barry K., Labutti K.,
RA Kuo R., Ohm R.A., Bhattacharya S.S., Shirouzu T., Yoshinaga Y.,
RA Martin F.M., Grigoriev I.V., Hibbett D.S.;
RT "Comparative Genomics of Early-Diverging Mushroom-Forming Fungi Provides
RT Insights into the Origins of Lignocellulose Decay Capabilities.";
RL Mol. Biol. Evol. 33:959-970(2016).
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000256|ARBA:ARBA00001947};
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; KV426254; KZV83808.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A165D575; -.
DR STRING; 1314781.A0A165D575; -.
DR InParanoid; A0A165D575; -.
DR OrthoDB; 9585at2759; -.
DR Proteomes; UP000077266; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
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: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 ATP-binding {ECO:0000256|RuleBase:RU003651};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Metalloprotease {ECO:0000256|ARBA:ARBA00023049};
KW Nucleotide-binding {ECO:0000256|RuleBase:RU003651};
KW Protease {ECO:0000256|ARBA:ARBA00022670};
KW Reference proteome {ECO:0000313|Proteomes:UP000077266};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 100..118
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 185..325
FT /note="AAA+ ATPase"
FT /evidence="ECO:0000259|SMART:SM00382"
FT REGION 605..648
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 624..648
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 648 AA; 71034 MW; 4F37D5958120C44E CRC64;
MSHNESKSRE ITWQEFRTAF LEKGLVDKLV VVNRKTVRVH LHSNATGIYG DSAPSGIFYF
SIGSVEAFER KLDEAQHEIG IPGHERIPVA YRDEVSITNI LLEFAPTVLI TGFVFYMIRR
SASGGSSGGG IFSIGKSKAK MFNKETQVQV KFDDVAGMDE AKEEIMEFVK FLKEPARYEK
LGAKIPRGAI LSGPPGTGKT LLAKATAGEA SVPFLSVSGS EFVEMFVGVG PSRVRDLFAS
AKKNAPCIIF VDEIDAIGKA RGKGGNYGGN DERESTLNQL LVEMDGFGTT EHVVVLAGTN
RPDVLDPALM RPGRFDRHIA IDRPDLSGRK QIFLVHLQPL RLAAEISGTE LDNFAHKLAV
LTPGFSGADI ANVCNEAALH AARHAGESVS DKNFETAIER VLTGLERKSR VLSPEEKKTV
AYHEAGHAVC GWFLEHADPL LKVSIIPRGV GALGYAQYLP PDRYLLSTPQ LFDRICMTLG
GRVSEEIFFG IEQITTGARD DLEKITRMAF EACATYGMND VIGPVSYGSR DGAQEQFQKP
FSEKTGEMLD GEVRKMINTA HRRTKELLTE HRADVEKVAQ LLLEKEVITR VDMIDLLGKR
PFAKKGDEMD EWLDKNTKRG ESSAPPPMDP PLGAPIAAAK DIPPPPPM
//
