ID A0A2G8RWL2_9APHY Unreviewed; 972 AA.
AC A0A2G8RWL2;
DT 31-JAN-2018, integrated into UniProtKB/TrEMBL.
DT 31-JAN-2018, sequence version 1.
DT 24-JAN-2024, entry version 23.
DE RecName: Full=Lon protease homolog {ECO:0000256|RuleBase:RU000592};
DE EC=3.4.21.- {ECO:0000256|RuleBase:RU000592};
GN ORFNames=GSI_11659 {ECO:0000313|EMBL:PIL25906.1};
OS Ganoderma sinense ZZ0214-1.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Polyporales; Polyporaceae; Ganoderma.
OX NCBI_TaxID=1077348 {ECO:0000313|EMBL:PIL25906.1, ECO:0000313|Proteomes:UP000230002};
RN [1] {ECO:0000313|EMBL:PIL25906.1, ECO:0000313|Proteomes:UP000230002}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ZZ0214-1 {ECO:0000313|EMBL:PIL25906.1,
RC ECO:0000313|Proteomes:UP000230002};
RX PubMed=26046933; DOI=10.1038/srep11087;
RA Zhu Y., Xu J., Sun C., Zhou S., Xu H., Nelson D.R., Qian J., Song J.,
RA Luo H., Xiang L., Li Y., Xu Z., Ji A., Wang L., Lu S., Hayward A., Sun W.,
RA Li X., Schwartz D.C., Wang Y., Chen S.;
RT "Chromosome-level genome map provides insights into diverse defense
RT mechanisms in the medicinal fungus Ganoderma sinense.";
RL Sci. Rep. 5:11087-11087(2015).
CC -!- SIMILARITY: Belongs to the peptidase S16 family. {ECO:0000256|PROSITE-
CC ProRule:PRU01122, ECO:0000256|RuleBase:RU000591}.
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:PIL25906.1}.
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DR EMBL; AYKW01000045; PIL25906.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2G8RWL2; -.
DR STRING; 1077348.A0A2G8RWL2; -.
DR OrthoDB; 1103874at2759; -.
DR Proteomes; UP000230002; 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; IPR015947; PUA-like_sf.
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 SMART; SM00464; LON; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR SUPFAM; SSF88697; PUA domain-like; 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|ARBA:ARBA00022840, ECO:0000256|RuleBase:RU000591};
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:UP000230002};
KW Serine protease {ECO:0000256|ARBA:ARBA00022825, ECO:0000256|PROSITE-
KW ProRule:PRU01122}.
FT DOMAIN 7..212
FT /note="Lon N-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51787"
FT DOMAIN 766..956
FT /note="Lon proteolytic"
FT /evidence="ECO:0000259|PROSITE:PS51786"
FT REGION 254..287
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 412..431
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 453..487
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 861
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01122"
FT ACT_SITE 904
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01122"
SQ SEQUENCE 972 AA; 105883 MW; 7D797C29603D243E CRC64;
MPTLATLPVL TLPHPLVLLP TARVQLPLHD ATGSRLIELV QRSETQLVIA TVPCSSSSTL
HPWGTTARVV RIVRPLSKSP QRLYHVTLQG LSRIYFPDTK SDAPFAPSDL IQLKAEYPKA
DDAPSPETVA PFRAAATKLL ESLAQNATQQ SRKDAYAKIS QMMEEVSDDR TPWMADVIVA
GINKVEYDDK LDFLSAAGSD DRLRRATELF VKQASISEVT KKIAQSIDES LSKQQKEFFL
RQQLAAIQRE LSNLNRAPSG GSGPEVPNGF PKPGSELDDN EQSEAEDMAE IRSKIEAMAK
DSEERKMAVR EWKRLQRIPS GSVEHGVIRS YLEWVTSIPW PSSAAFANAT SSDKLRDRGF
LADARKQLDV DHYGLEKIKR RLIEYLAVVR LKQLQAEAPL VADLPPLLPA SPSVNGEGGS
GDAAASAGQR SEGDATARAL ALISKALKLG TSAEPKAKPD AAVPSSQSQL ALVPKRSGSG
KAKRGAGSKA VKGPILLFVG PPGTGKTSLG QSIARALDRP FQRISLGGVR DEAEIRGHRR
TYVASGPGSI VQALRKAGRP DPVILLDEVD KIGQSNFHGD PAAALLEVLD PEQNHSFNDH
YINVPIDLSQ VLFICTSNSL ETMSAPLLDR CEIVQLSGYT YDEKMHIARK FLLPKQLKAN
GLTAEHVTLT QPTLLHIATH YTREAGVRSL ERAIGAVVRY KAVEWAEYAD GAGIQNANQL
PAIEVQQSEA EKAKTKGRTY KKVVEEHELE KILGIARWDE EELHREERRG LVYGLVVTGM
GEGGLLPIET TVVPGSGQLK LTGSLGDVIK ESGELALSWV KSHAYDLYIT KLRAQDPLKH
PDPIDIHLHL PSGAVKKDGP SAGIAMTCAF VSLLTGACVP TNIAMTGEVT LRGRVGPVGG
IKEKVLGAHR AQITKVILPW ANRKDVEHDV PLEVRADLQF VFVRTMEEVL EAAFGKGVLN
WRRNVLVMES RL
//