ID   LONP2_NEUCR             Reviewed;         937 AA.
AC   Q7SA85;
DT   13-JUL-2010, integrated into UniProtKB/Swiss-Prot.
DT   15-DEC-2003, sequence version 1.
DT   03-AUG-2022, entry version 122.
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=NCU08303;
OS   Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 /
OS   FGSC 987).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Sordariomycetidae; Sordariales; Sordariaceae; Neurospora.
OX   NCBI_TaxID=367110;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987;
RX   PubMed=12712197; DOI=10.1038/nature01554;
RA   Galagan J.E., Calvo S.E., Borkovich K.A., Selker E.U., Read N.D.,
RA   Jaffe D.B., FitzHugh W., Ma L.-J., Smirnov S., Purcell S., Rehman B.,
RA   Elkins T., Engels R., Wang S., Nielsen C.B., Butler J., Endrizzi M.,
RA   Qui D., Ianakiev P., Bell-Pedersen D., Nelson M.A., Werner-Washburne M.,
RA   Selitrennikoff C.P., Kinsey J.A., Braun E.L., Zelter A., Schulte U.,
RA   Kothe G.O., Jedd G., Mewes H.-W., Staben C., Marcotte E., Greenberg D.,
RA   Roy A., Foley K., Naylor J., Stange-Thomann N., Barrett R., Gnerre S.,
RA   Kamal M., Kamvysselis M., Mauceli E.W., Bielke C., Rudd S., Frishman D.,
RA   Krystofova S., Rasmussen C., Metzenberg R.L., Perkins D.D., Kroken S.,
RA   Cogoni C., Macino G., Catcheside D.E.A., Li W., Pratt R.J., Osmani S.A.,
RA   DeSouza C.P.C., Glass N.L., Orbach M.J., Berglund J.A., Voelker R.,
RA   Yarden O., Plamann M., Seiler S., Dunlap J.C., Radford A., Aramayo R.,
RA   Natvig D.O., Alex L.A., Mannhaupt G., Ebbole D.J., Freitag M., Paulsen I.,
RA   Sachs M.S., Lander E.S., Nusbaum C., Birren B.W.;
RT   "The genome sequence of the filamentous fungus Neurospora crassa.";
RL   Nature 422:859-868(2003).
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; CM002239; EAA33280.1; -; Genomic_DNA.
DR   RefSeq; XP_962516.1; XM_957423.3.
DR   AlphaFoldDB; Q7SA85; -.
DR   SMR; Q7SA85; -.
DR   STRING; 5141.EFNCRP00000008426; -.
DR   PRIDE; Q7SA85; -.
DR   EnsemblFungi; EAA33280; EAA33280; NCU08303.
DR   GeneID; 3878657; -.
DR   KEGG; ncr:NCU08303; -.
DR   VEuPathDB; FungiDB:NCU08303; -.
DR   HOGENOM; CLU_004109_4_0_1; -.
DR   InParanoid; Q7SA85; -.
DR   OMA; MVNIEDK; -.
DR   BRENDA; 3.6.4.7; 3627.
DR   Proteomes; UP000001805; Chromosome 4, Linkage Group IV.
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; 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.
PE   3: Inferred from homology;
KW   ATP-binding; Hydrolase; Nucleotide-binding; Peroxisome; Protease;
KW   Reference proteome; Serine protease.
FT   CHAIN           1..937
FT                   /note="Lon protease homolog 2, peroxisomal"
FT                   /id="PRO_0000395796"
FT   DOMAIN          11..256
FT                   /note="Lon N-terminal"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01123"
FT   DOMAIN          734..921
FT                   /note="Lon proteolytic"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01122"
FT   MOTIF           935..937
FT                   /note="Microbody targeting signal"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03121"
FT   ACT_SITE        827
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03121"
FT   ACT_SITE        870
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03121"
FT   BINDING         491..498
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03121"
SQ   SEQUENCE   937 AA;  101726 MW;  3ADF9E9F593693F0 CRC64;
     MAHIRAPTVT IPLLPLPKQT VLLPGVVQRV AVSSTRPDIA SLLAAVYAKA ASQTPNGRID
     TIPIACVPLA SPLIGPEGHL LIENGDDKTE TADDVDPAKA TKADLFPYGV AAKITGVEGR
     GTGEFTLLVE GVTRIHVEKV ISDKAYLEGK VSSYADPALI TDAALEELFM SLKLLSRQFV
     TILRLSSLLP QSSGTPGLSP LLARRLDFYI AKQKYPGALA DFMANIVESS YEEKLEILTL
     IDVKERVAKV IELLDRQITN IKNSMRVTTI TATTLPFPMD PDAAKHGKIK PPVKAPGHGA
     GMPFSPQGGF MGRGGNADED QEPNEIEELQ KRLDAARLSP EAAKVADREI KRLKKIHPAQ
     AEYAVTRTYL ETLAEIPWTT TTDDRLGPDT LNRARKQLDE DHYGLDKVKK RLLEYLAVLR
     LKQAINDDVD SQIKQLEQEL GVASESSKED AAQSTPIDLG VDEKAKAGGD KLEALKSRRM
     VDKSPILLLV GPPGVGKTSL ARSVATALGR KFHRISLGGV RDEAEIRGHR RTYVAAMPGL
     IVQGLKKVGV ANPVFLLDEI DKVGGSSIHG DPSAAMLEVL DPEQNHNFTD HYVNVPIDLS
     KVLFIATANS LDTIPAPLLD RMETIYIPGY TTLEKRHIAM RHLVPKQLRV NGLDESQVSF
     TPEVVSRIIE SYTREAGVRN LEREISSVAR GKAVEFADAK DSGHPENYNP QLTVDDLEKF
     LGIEKFEEEI AEKTSRPGIV TGLVAYSSGG NGSILFIEVA DMPGNGSVQL TGKLGDVLKE
     SVEVALTWVK AHAYQLGLTQ SPSENIMKDR SIHVHCPSGA VPKDGPSSGI SQAIALISLF
     SGKAVPPTMA MTGEISLRGR ITAVGGIKEK LIGALRAGVK TVLLPAQNRK DAKDLPQEVK
     DGLEIIHVSH IWEAIRYVWP DGQWPSEHDY PSIESRL