ID R7S0P6_STEHR Unreviewed; 1055 AA.
AC R7S0P6;
DT 24-JUL-2013, integrated into UniProtKB/TrEMBL.
DT 24-JUL-2013, sequence version 1.
DT 27-MAR-2024, entry version 54.
DE RecName: Full=Lon protease homolog {ECO:0000256|RuleBase:RU000592};
DE EC=3.4.21.- {ECO:0000256|RuleBase:RU000592};
GN ORFNames=STEHIDRAFT_150722 {ECO:0000313|EMBL:EIM80122.1};
OS Stereum hirsutum (strain FP-91666) (White-rot fungus).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Russulales; Stereaceae; Stereum.
OX NCBI_TaxID=721885 {ECO:0000313|EMBL:EIM80122.1, ECO:0000313|Proteomes:UP000053927};
RN [1] {ECO:0000313|Proteomes:UP000053927}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=FP-91666 {ECO:0000313|Proteomes:UP000053927};
RX PubMed=22745431; DOI=10.1126/science.1221748;
RA Floudas D., Binder M., Riley R., Barry K., Blanchette R.A., Henrissat B.,
RA Martinez A.T., Otillar R., Spatafora J.W., Yadav J.S., Aerts A., Benoit I.,
RA Boyd A., Carlson A., Copeland A., Coutinho P.M., de Vries R.P.,
RA Ferreira P., Findley K., Foster B., Gaskell J., Glotzer D., Gorecki P.,
RA Heitman J., Hesse C., Hori C., Igarashi K., Jurgens J.A., Kallen N.,
RA Kersten P., Kohler A., Kuees U., Kumar T.K.A., Kuo A., LaButti K.,
RA Larrondo L.F., Lindquist E., Ling A., Lombard V., Lucas S., Lundell T.,
RA Martin R., McLaughlin D.J., Morgenstern I., Morin E., Murat C., Nagy L.G.,
RA Nolan M., Ohm R.A., Patyshakuliyeva A., Rokas A., Ruiz-Duenas F.J.,
RA Sabat G., Salamov A., Samejima M., Schmutz J., Slot J.C., St John F.,
RA Stenlid J., Sun H., Sun S., Syed K., Tsang A., Wiebenga A., Young D.,
RA Pisabarro A., Eastwood D.C., Martin F., Cullen D., Grigoriev I.V.,
RA Hibbett D.S.;
RT "The Paleozoic origin of enzymatic lignin decomposition reconstructed from
RT 31 fungal genomes.";
RL Science 336:1715-1719(2012).
CC -!- SIMILARITY: Belongs to the peptidase S16 family. {ECO:0000256|PROSITE-
CC ProRule:PRU01122, ECO:0000256|RuleBase:RU000591}.
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DR EMBL; JH687399; EIM80122.1; -; Genomic_DNA.
DR RefSeq; XP_007310736.1; XM_007310674.1.
DR AlphaFoldDB; R7S0P6; -.
DR GeneID; 18800092; -.
DR KEGG; shs:STEHIDRAFT_150722; -.
DR eggNOG; KOG2004; Eukaryota.
DR OMA; ICTANTM; -.
DR OrthoDB; 1103874at2759; -.
DR Proteomes; UP000053927; 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:UniProtKB-UniRule.
DR GO; GO:0004252; F:serine-type endopeptidase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0030163; P:protein catabolic process; IEA:InterPro.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR CDD; cd19500; RecA-like_Lon; 1.
DR Gene3D; 1.10.8.60; -; 1.
DR Gene3D; 1.20.5.5270; -; 1.
DR Gene3D; 1.20.58.1480; -; 1.
DR Gene3D; 3.30.230.10; -; 1.
DR Gene3D; 2.30.130.40; LON domain-like; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR InterPro; IPR003593; AAA+_ATPase.
DR InterPro; IPR003959; ATPase_AAA_core.
DR InterPro; IPR008269; Lon_proteolytic.
DR InterPro; IPR027065; Lon_Prtase.
DR InterPro; IPR003111; Lon_prtase_N.
DR InterPro; IPR046336; Lon_prtase_N_sf.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR008268; Peptidase_S16_AS.
DR InterPro; IPR020568; Ribosomal_Su5_D2-typ_SF.
DR InterPro; IPR014721; Ribsml_uS5_D2-typ_fold_subgr.
DR PANTHER; PTHR10046; ATP DEPENDENT LON PROTEASE FAMILY MEMBER; 1.
DR PANTHER; PTHR10046:SF24; LON PROTEASE HOMOLOG 2, PEROXISOMAL; 1.
DR Pfam; PF00004; AAA; 1.
DR Pfam; PF05362; Lon_C; 1.
DR Pfam; PF02190; LON_substr_bdg; 1.
DR PRINTS; PR00830; ENDOLAPTASE.
DR SMART; SM00382; AAA; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR SUPFAM; SSF54211; Ribosomal protein S5 domain 2-like; 1.
DR PROSITE; PS51787; LON_N; 1.
DR PROSITE; PS51786; LON_PROTEOLYTIC; 1.
DR PROSITE; PS01046; LON_SER; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|RuleBase:RU000591};
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Hydrolase {ECO:0000256|PROSITE-ProRule:PRU01122,
KW ECO:0000256|RuleBase:RU000591};
KW Nucleotide-binding {ECO:0000256|RuleBase:RU000591};
KW Protease {ECO:0000256|ARBA:ARBA00022670, ECO:0000256|PROSITE-
KW ProRule:PRU01122}; Reference proteome {ECO:0000313|Proteomes:UP000053927};
KW Serine protease {ECO:0000256|ARBA:ARBA00022825, ECO:0000256|PROSITE-
KW ProRule:PRU01122}.
FT DOMAIN 9..252
FT /note="Lon N-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51787"
FT DOMAIN 837..1038
FT /note="Lon proteolytic"
FT /evidence="ECO:0000259|PROSITE:PS51786"
FT REGION 294..351
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 409..432
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 509..531
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 769..801
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 471..504
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 294..319
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 943
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01122"
FT ACT_SITE 986
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01122"
SQ SEQUENCE 1055 AA; 114978 MW; AD38033D722FC277 CRC64;
MATTTSLELP TLALPHPLVL LPSARVIVPI TAPVAEALIR LADSAAENGQ TPVVAAVPLL
PPQQSKKNSE KLQTPKLNEW GVVARVVRLV RPPTRSSSQP HLLALQGLSR VRLLDVEAAS
PSFSKRDPIP LLAYERASLS PPNSGALIRT GGDGYGDGQD DGERPSKEEF ISFKNAALRM
LERLSQDTTQ SRKREAWVKI MGLVEDLEEE RAGWMADMLV STAGVEYADK IAHLSTPTTS
TRIKHATSLF IKLTSISEVS TKIASAVDES LSKQQKEFFL RQQLAAIQAE LSALNRPSPS
PNNSFQNPNN RTWNKSSRPG NADWPERVDG SASTNEGQGS ELDREGQEED DMLDVKRKIE
AMEVGSEERR VGVNEWRRLK RIPQQSAEYG VVRNYLEWLT SLPWPSSSLI EASDSSPSST
SSSTQSPPPQ SLRSRAFLTN AQRQLDADHY GLDRVKRRLI EYLAVVRLRE MMAAEEEARQ
IEAEAKAEAE RMAEAKEVDA AEQAVMASKE RDVSQTLAGE QTQVEGQHER MPKLAETVRR
RKPRRVKGPI LLFVGPPGTG KTSLGQSIAK ALGRPFQRIA LGGVRDEGEI RGHRRTYVAS
GPGTIVQALR KAGRSDLVLL LDEVDKVGQS NFHGDPSAAL LEVLDPEQNH AFNDHYINVP
IDLSQVLFIC TANTLDTIAA PLLDRCEIIH LSGYTYDEKL HIARRFLLPK QLSVNGLTPA
QLDLSDPALL HIVSHYTREA GVRSLERAIG SVVRFKAVEW AEYIDADASS STSSSSHASP
SMSPASTSTA SDGNNSITNT DPVQNALVKY RPTVEIDELE NILGIARWDE ETIGDREPRR
GVVYGLVVTG MGEGEIMPVE SIAVPGNGKL KLTGSLGNVI KESGELALSW VKTHAYELGV
TSSRTQDPLV TRRGVDVASG EDTSKIDIHL HLPAGAQKKD GPSAGIAMTC AFVSLLTGAC
VPPNVAMTGE ITLRGRVTPV GGIKEKVLGA HRAGITTVIL PWANRKDVKH DVPQEVRNGM
TFVFAKTVKE ALEAAFGKDT LAWRGEEAVL VESRL
//
