ID   LONP2_CANDC             Reviewed;        1247 AA.
AC   B9WEC4;
DT   13-JUL-2010, integrated into UniProtKB/Swiss-Prot.
DT   24-MAR-2009, sequence version 1.
DT   03-AUG-2022, entry version 71.
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   ORFNames=CD36_85340;
OS   Candida dubliniensis (strain CD36 / ATCC MYA-646 / CBS 7987 / NCPF 3949 /
OS   NRRL Y-17841) (Yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Debaryomycetaceae; Candida/Lodderomyces clade; Candida.
OX   NCBI_TaxID=573826;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CD36 / ATCC MYA-646 / CBS 7987 / NCPF 3949 / NRRL Y-17841;
RX   PubMed=19745113; DOI=10.1101/gr.097501.109;
RA   Jackson A.P., Gamble J.A., Yeomans T., Moran G.P., Saunders D., Harris D.,
RA   Aslett M., Barrell J.F., Butler G., Citiulo F., Coleman D.C.,
RA   de Groot P.W.J., Goodwin T.J., Quail M.A., McQuillan J., Munro C.A.,
RA   Pain A., Poulter R.T., Rajandream M.A., Renauld H., Spiering M.J.,
RA   Tivey A., Gow N.A.R., Barrell B., Sullivan D.J., Berriman M.;
RT   "Comparative genomics of the fungal pathogens Candida dubliniensis and
RT   Candida albicans.";
RL   Genome Res. 19:2231-2244(2009).
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; FM992690; CAX43035.1; -; Genomic_DNA.
DR   RefSeq; XP_002419441.1; XM_002419396.1.
DR   AlphaFoldDB; B9WEC4; -.
DR   SMR; B9WEC4; -.
DR   STRING; 42374.XP_002419441.1; -.
DR   EnsemblFungi; CAX43035; CAX43035; CD36_85340.
DR   GeneID; 8047097; -.
DR   KEGG; cdu:CD36_85340; -.
DR   CGD; CAL0000160445; Cd36_85340.
DR   VEuPathDB; FungiDB:CD36_85340; -.
DR   eggNOG; KOG2004; Eukaryota.
DR   HOGENOM; CLU_004109_4_0_1; -.
DR   OrthoDB; 528132at2759; -.
DR   Proteomes; UP000002605; Chromosome 3.
DR   GO; GO:0005782; C:peroxisomal matrix; IEA:UniProtKB-SubCell.
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; IEA:UniProtKB-UniRule.
DR   GO; GO:0006515; P:protein quality control for misfolded or incompletely synthesized proteins; IEA:UniProtKB-UniRule.
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; IPR003111; Lon_prtase_N.
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   Pfam; PF02190; LON_substr_bdg; 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   Serine protease.
FT   CHAIN           1..1247
FT                   /note="Lon protease homolog 2, peroxisomal"
FT                   /id="PRO_0000395792"
FT   DOMAIN          22..400
FT                   /note="Lon N-terminal"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01123"
FT   DOMAIN          989..1230
FT                   /note="Lon proteolytic"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01122"
FT   REGION          76..103
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          447..503
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          626..655
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        452..493
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        637..655
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        1099
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03121"
FT   ACT_SITE        1142
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03121"
FT   BINDING         721..728
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03121"
SQ   SEQUENCE   1247 AA;  139848 MW;  0FD55A67A54E534C CRC64;
     MAKYNNNNYA NKATNLKQQV VLPTYTLDSN LVLLPGIMYN VTFSRFKAAA LLYRYKNFIS
     QVSIINNLLS EYDFNSGNSN EEERSETEQK IEQSSLGQPE TYHEINPSVI STEAVEGIKE
     FFQYETNMKT GRGGKGEKEA KSTNDGIKEF DWLTLAIIPN LDKIKDPETN YSIGDAAKLT
     NVVTVARIIG IVDDSTNIKL TLQAITRGVQ ITDDSKMNQH KNGLKTNEQV IGIDWNHNVS
     DLKGKFNALQ KNYQQLFQSI DKFLIDYREA LDYNKNNSNN KNGNLSLIKG NATINNNKNS
     DDKSNQDIKS QNLLTLNPLA NALYMQLVGS KDFNKAFHRL EKLFSQVSKN DEYKIDNETY
     LRLVDLTCGI LPFPNFQKLA LLNKYKLDDR SVLINEMILQ LIQIFENLQT NNSFVNNWFH
     SEATNIQKAN VVANQLKSIR NLLEGMTKNR PIKSNKRNPG PASSSGPSFS NGKSSPGRAN
     ARPKSNHQDG FNGNDGDYND VDDDDDGDED LKAIFNFIKH KLPTISTLSA DSKRLILKDF
     KRVKASANSP GGGGNSDFHV LRNYLEIVMD IPWDNYVTKF KSNKDIDLKL AKKQLDDDHY
     GLEHVKKRLI QYLVVLKLLG INAEKDQSDK SQPIKDNSKD SPNSSSKALT KSPTSSLSRK
     TISSIVIANK DETYLAKQQA KTTNQKSITE AKTNPSTTMI TSNESIHVSK NNKSPIIMLA
     GPPGTGKTSL AKSIASALGR NFQRISLGGI KDESEIRGHR RTYVGAMPGL LIQALRKSRC
     MNPVILLDEI DKVIGGNNSG GVNKFNGDPS AALLEVLDPE QNNTFIDHYL GFPIDLSQVI
     FICTANDPWN MTRPLLDRLE TIEIGAYDYN EKLIIGKKYL LPRQIKRNGF PVVDTKKMTT
     VVAGSSNQDE FIRINDATMK KVILDYTRGE AGVRNFERRL GTLCRFKAVE YCEWLNKDIK
     NYNPIIDEND LPIYLGVPYS SGDVTTEGTV GVGVVHGLSY NSDGSGSVLV FESIGFDRRI
     SNKEHNGGNG ATLNMTGRLG EVLMESGKIG LVFIKSMIYK NILKFDNNNN NKHLLLDKYN
     NLDIHMHVPM GSVSKDGPSA GVTMALSFLS VLLDKPVPSD IAMTGEITLR GIILPIGGVK
     EKLMGAHLNS NIKRMIVPRE NRKDLIKEYS RSIEEAGEVL DHHLINDLIK DNEDKEFKLT
     QVEEYYQNKY GISLFYAKEF YDIIKIVWNE DEVLLKQDNS RLLEYHI