ID   LONP2_YARLI             Reviewed;         952 AA.
AC   Q6C0L7;
DT   13-JUL-2010, integrated into UniProtKB/Swiss-Prot.
DT   16-AUG-2004, sequence version 1.
DT   03-AUG-2022, entry version 119.
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=YALI0F23595g;
OS   Yarrowia lipolytica (strain CLIB 122 / E 150) (Yeast) (Candida lipolytica).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Dipodascaceae; Yarrowia.
OX   NCBI_TaxID=284591;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CLIB 122 / E 150;
RX   PubMed=15229592; DOI=10.1038/nature02579;
RA   Dujon B., Sherman D., Fischer G., Durrens P., Casaregola S., Lafontaine I.,
RA   de Montigny J., Marck C., Neuveglise C., Talla E., Goffard N., Frangeul L.,
RA   Aigle M., Anthouard V., Babour A., Barbe V., Barnay S., Blanchin S.,
RA   Beckerich J.-M., Beyne E., Bleykasten C., Boisrame A., Boyer J.,
RA   Cattolico L., Confanioleri F., de Daruvar A., Despons L., Fabre E.,
RA   Fairhead C., Ferry-Dumazet H., Groppi A., Hantraye F., Hennequin C.,
RA   Jauniaux N., Joyet P., Kachouri R., Kerrest A., Koszul R., Lemaire M.,
RA   Lesur I., Ma L., Muller H., Nicaud J.-M., Nikolski M., Oztas S.,
RA   Ozier-Kalogeropoulos O., Pellenz S., Potier S., Richard G.-F.,
RA   Straub M.-L., Suleau A., Swennen D., Tekaia F., Wesolowski-Louvel M.,
RA   Westhof E., Wirth B., Zeniou-Meyer M., Zivanovic Y., Bolotin-Fukuhara M.,
RA   Thierry A., Bouchier C., Caudron B., Scarpelli C., Gaillardin C.,
RA   Weissenbach J., Wincker P., Souciet J.-L.;
RT   "Genome evolution in yeasts.";
RL   Nature 430:35-44(2004).
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}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; CR382132; CAG78606.1; -; Genomic_DNA.
DR   RefSeq; XP_505795.1; XM_505795.1.
DR   AlphaFoldDB; Q6C0L7; -.
DR   SMR; Q6C0L7; -.
DR   STRING; 4952.CAG78606; -.
DR   EnsemblFungi; CAG78606; CAG78606; YALI0_F23595g.
DR   GeneID; 2908759; -.
DR   KEGG; yli:YALI0F23595g; -.
DR   VEuPathDB; FungiDB:YALI0_F23595g; -.
DR   HOGENOM; CLU_004109_4_0_1; -.
DR   InParanoid; Q6C0L7; -.
DR   OMA; GAWQVVD; -.
DR   BRENDA; 3.6.4.7; 1122.
DR   Proteomes; UP000001300; Chromosome F.
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; 2.30.130.40; -; 1.
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; IPR004815; Lon_bac/euk-typ.
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; IPR027501; Lonp2_euk.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR008268; Peptidase_S16_AS.
DR   InterPro; IPR015947; PUA-like_sf.
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   Pfam; PF02190; LON_substr_bdg; 1.
DR   PIRSF; PIRSF001174; Lon_proteas; 1.
DR   SMART; SM00382; AAA; 1.
DR   SMART; SM00464; LON; 1.
DR   SUPFAM; SSF52540; SSF52540; 1.
DR   SUPFAM; SSF54211; SSF54211; 1.
DR   SUPFAM; SSF88697; SSF88697; 1.
DR   TIGRFAMs; TIGR00763; lon; 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..952
FT                   /note="Lon protease homolog 2, peroxisomal"
FT                   /id="PRO_0000395799"
FT   DOMAIN          5..302
FT                   /note="Lon N-terminal"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01123"
FT   DOMAIN          756..942
FT                   /note="Lon proteolytic"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01122"
FT   REGION          179..198
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          457..477
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           950..952
FT                   /note="Microbody targeting signal"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03121"
FT   COMPBIAS        179..196
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        458..472
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        843
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03121"
FT   ACT_SITE        886
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03121"
FT   BINDING         493..500
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03121"
SQ   SEQUENCE   952 AA;  104250 MW;  D3AA8A23348D83AE CRC64;
     MDATLPLLTL PADTVVLPGV SMKVGLSKET AVAMLKLFEK PKDKDVAYSK ATQDLMSSVN
     KLQAFFKLKR TSADGYRNAS LITIACVPRI TQKQIKETGE NNEAGAHDSE SVTPVLGTNS
     TEVNTSVYSF GTVCRIVRFE RSGTEDFQIV VEGLSRLELG QLVDKSGLVP TARIKVRVDE
     DGESASSDES SDKEPTWSKT ELSQLEVLHA SAKEIIDLAA KSNATQFSKL MASQTTVAAS
     VMKQLTKLGP NPGSARDTRK TAGMLVDLLM AILPTDFEDK IAVLAAFSIP ERIAKGSEIL
     KTKLDMMKIT EKIDSTVDSK MNKQQREYLL RQKMRAIQEE LGETDDRGED DDLKELTQKL
     QSLKLSPEAD KVVSRELKRI KRMPPTQAEY QVCRTYLETI AELPWDKCTE DTVVTVDQAR
     TILDNDHYGL SHIKKRLLEY LAVLRLKSLR SESEVAQEET AAAASSEGPN GQLDDSAKPI
     DYSNRAPILL LVGPPGVGKT SLAKSVARAL GRKFQRLSLG GVRDESEIRG HRRTYVGAMP
     GLFIQGLRQV GVNNPVVLLD EIDKIGGANF HGDPAAAMLE VLDPEQNATF RDHYINFPVD
     LSKCIFIATA NNLDTIPAPL LDRMETVHLE GYTYMEKLHI AKKYLVPKQT KANGLEVDQV
     VIPDDVLLHI CTKYTREAGV RNLERKIGAV CRAKAVDYAK SLSADDGELI TVVDEAKKGA
     HSSYDPVVTI ENLTDILGME VYTDEDAQDA KEEPNSSHIG VVNGLAYMGT GNGGLLKFEA
     TQMPGKGQLK LTGKLGDVIQ ESAQIALSWV KSNAAALHID TDFDKVDIHL HAPAGAIPKD
     GPSAGVAMTL AFVSLFMGKP IPPSIAMTGE MTLRGRVLPV GGIREKLLGA HLAGVNRIML
     PLANKRDVDE EQRKGGDGGV LDKMEISYVK YMWDVLELVW DLRFDPMIES RL