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Database: UniProt
Entry: A0A2G8RWL2_9APHY
LinkDB: A0A2G8RWL2_9APHY
Original site: A0A2G8RWL2_9APHY 
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
//
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