ID   LONP2_ASHGO             Reviewed;        1004 AA.
AC   Q755E4;
DT   13-JUL-2010, integrated into UniProtKB/Swiss-Prot.
DT   09-JAN-2013, sequence version 2.
DT   03-AUG-2022, entry version 123.
DE   RecName: Full=Lon protease homolog 2, peroxisomal {ECO:0000255|HAMAP-Rule:MF_03121};
DE            EC=3.4.21.53 {ECO:0000255|HAMAP-Rule:MF_03121};
GN   OrderedLocusNames=AFL121W;
OS   Ashbya gossypii (strain ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056)
OS   (Yeast) (Eremothecium gossypii).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Eremothecium.
OX   NCBI_TaxID=284811;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056;
RX   PubMed=15001715; DOI=10.1126/science.1095781;
RA   Dietrich F.S., Voegeli S., Brachat S., Lerch A., Gates K., Steiner S.,
RA   Mohr C., Poehlmann R., Luedi P., Choi S., Wing R.A., Flavier A.,
RA   Gaffney T.D., Philippsen P.;
RT   "The Ashbya gossypii genome as a tool for mapping the ancient Saccharomyces
RT   cerevisiae genome.";
RL   Science 304:304-307(2004).
RN   [2]
RP   GENOME REANNOTATION.
RC   STRAIN=ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056;
RX   PubMed=23749448; DOI=10.1534/g3.112.002881;
RA   Dietrich F.S., Voegeli S., Kuo S., Philippsen P.;
RT   "Genomes of Ashbya fungi isolated from insects reveal four mating-type
RT   loci, numerous translocations, lack of transposons, and distinct gene
RT   duplications.";
RL   G3 (Bethesda) 3:1225-1239(2013).
CC   -!- FUNCTION: ATP-dependent serine protease that mediates the selective
CC       degradation of misfolded and unassembled polypeptides in the
CC       peroxisomal matrix. Necessary for type 2 peroxisome targeting signal
CC       (PTS2)-containing protein processing and facilitates peroxisome matrix
CC       protein import. {ECO:0000255|HAMAP-Rule:MF_03121}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Hydrolysis of proteins in presence of ATP.; EC=3.4.21.53;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_03121};
CC   -!- SUBCELLULAR LOCATION: Peroxisome matrix {ECO:0000255|HAMAP-
CC       Rule:MF_03121}.
CC   -!- SIMILARITY: Belongs to the peptidase S16 family. {ECO:0000255|HAMAP-
CC       Rule:MF_03121}.
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DR   EMBL; AE016819; AAS53253.2; -; Genomic_DNA.
DR   RefSeq; NP_985429.2; NM_210783.2.
DR   AlphaFoldDB; Q755E4; -.
DR   SMR; Q755E4; -.
DR   STRING; 33169.AAS53253; -.
DR   EnsemblFungi; AAS53253; AAS53253; AGOS_AFL121W.
DR   GeneID; 4621656; -.
DR   KEGG; ago:AGOS_AFL121W; -.
DR   eggNOG; KOG2004; Eukaryota.
DR   HOGENOM; CLU_004109_4_0_1; -.
DR   InParanoid; Q755E4; -.
DR   OMA; NKSPIIM; -.
DR   Proteomes; UP000000591; Chromosome VI.
DR   GO; GO:0005782; C:peroxisomal matrix; IBA:GO_Central.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0016887; F:ATP hydrolysis activity; IEA:UniProtKB-UniRule.
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:0016558; P:protein import into peroxisome matrix; IEA:UniProtKB-UniRule.
DR   GO; GO:0016485; P:protein processing; IBA:GO_Central.
DR   GO; GO:0006515; P:protein quality control for misfolded or incompletely synthesized proteins; IEA:UniProtKB-UniRule.
DR   GO; GO:0006625; P:protein targeting to peroxisome; IBA:GO_Central.
DR   Gene3D; 3.30.230.10; -; 1.
DR   Gene3D; 3.40.50.300; -; 1.
DR   HAMAP; MF_03121; lonp2_euk; 1.
DR   InterPro; IPR003593; AAA+_ATPase.
DR   InterPro; IPR003959; ATPase_AAA_core.
DR   InterPro; IPR008269; Lon_proteolytic.
DR   InterPro; IPR027065; Lon_Prtase.
DR   InterPro; IPR027501; Lonp2_euk.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR008268; Peptidase_S16_AS.
DR   InterPro; IPR020568; Ribosomal_S5_D2-typ_fold.
DR   InterPro; IPR014721; Ribosomal_S5_D2-typ_fold_subgr.
DR   PANTHER; PTHR10046; PTHR10046; 1.
DR   Pfam; PF00004; AAA; 1.
DR   Pfam; PF05362; Lon_C; 1.
DR   SMART; SM00382; AAA; 1.
DR   SUPFAM; SSF52540; SSF52540; 1.
DR   SUPFAM; SSF54211; SSF54211; 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; Hydrolase; Nucleotide-binding; Peroxisome; Protease;
KW   Reference proteome; Serine protease.
FT   CHAIN           1..1004
FT                   /note="Lon protease homolog 2, peroxisomal"
FT                   /id="PRO_0000395788"
FT   DOMAIN          28..293
FT                   /note="Lon N-terminal"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03121"
FT   DOMAIN          773..987
FT                   /note="Lon proteolytic"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01122"
FT   REGION          340..374
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           1002..1004
FT                   /note="Microbody targeting signal"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03121"
FT   ACT_SITE        872
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03121"
FT   ACT_SITE        915
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03121"
FT   BINDING         519..526
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03121"
SQ   SEQUENCE   1004 AA;  109780 MW;  3538D03B6FA60127 CRC64;
     MGLFGKDRGE RIAEFPCYLL ETGTHLVPLP GILYNLVIER TYGERILGQF RGIGEAVDGA
     LTGAGEAAEV PGRVAEVMKA FQERYDSGDK TQAVYICLVT EAAAGRHIGC IARLTGARAE
     GGELSVLLRG LVRAVVGQPV PSRRNEMWNG SVTVLDDAQR VATWGARQLD FARQGVFGAF
     EELDAGIGTF TARFKSSQKR GADGAAHLLT LSPLANTLFF HFSRSSFERS WKILRTMMHG
     FRDAKKDIRT AMDMLSVADL TVGLLPTTTA QRLEFLQAED PAARIKTFVR HMQQLLEVFG
     SLYRATEYVH DRFETHGPIA KSQLIANQLR SLRFYIDDIK RNKPESGPGG RSRRLLPRPA
     SGNSAAAGEE DDSEDSELVA IKRYVDEIEV KGVHADGVKM LKKDYRSLSK MHVQSTEYQM
     LRNYFDFIMG IPFGIYVSTP EIDLVASSRK LDNDHYGLVQ VKKRLLEYLC VLKLSANSPG
     VTADAGAIED GSATKRAVVY ENKAQEQRKT KVPFLLLVGP PGVGKTSVAK SVADVLGRRF
     QRISLGGIHN EAEIRGHRRT YVGAMAGMIV NALCKAGCMN PLILLDEIDK VLSVPAGAGA
     SRLNGDPGAA LLEVLDPEQN HTFTDHYVGF PVDLSQVLFF CTANDLSGMS EPLVDRMEVI
     HIEGYTYEEK IAIGRHFLLP KQIRLNSFDM TGINLSLTDD AWRTVVVDYT REAGVRNLDR
     QLGAIVRGKI VEYVENNMSG SGDDVVTQKN LPKFLGLPPH SLREEVTQTT SFAEKYGVVH
     GLSYNSDGTG GVLVFEVIRS GDSRDKRLTV QTTGNLGTVL SESVSIATSL VKSLLARHVV
     HSSADDTSVA EFFRSECHLH VPFGAVPKDG PSAGAAISLA LLSLALKRPV DPALCVTGEI
     TLRGKILPVG GVKEKLLAAQ LQGMGLALVP RGNRNDLVEL AEDNAETQQR LLADPALPEL
     ATLQHKLGMA VHYCSDFRDL VLHAWPTADN LWHACEDSSV RPQL