ID   LONM_NEUCR              Reviewed;        1107 AA.
AC   Q7S8C4;
DT   13-JUL-2010, integrated into UniProtKB/Swiss-Prot.
DT   15-DEC-2003, sequence version 1.
DT   03-AUG-2022, entry version 121.
DE   RecName: Full=Lon protease homolog, mitochondrial {ECO:0000255|HAMAP-Rule:MF_03120};
DE            EC=3.4.21.53 {ECO:0000255|HAMAP-Rule:MF_03120};
DE   Flags: Precursor;
GN   Name=pim1; ORFNames=NCU05261;
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, unassembled or oxidatively damaged
CC       polypeptides as well as certain short-lived regulatory proteins in the
CC       mitochondrial matrix. May also have a chaperone function in the
CC       assembly of inner membrane protein complexes. Participates in the
CC       regulation of mitochondrial gene expression and in the maintenance of
CC       the integrity of the mitochondrial genome. Binds to mitochondrial DNA
CC       in a site-specific manner. {ECO:0000255|HAMAP-Rule:MF_03120}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Hydrolysis of proteins in presence of ATP.; EC=3.4.21.53;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_03120};
CC   -!- SUBUNIT: Homohexamer or homoheptamer. Organized in a ring with a
CC       central cavity. {ECO:0000255|HAMAP-Rule:MF_03120}.
CC   -!- SUBCELLULAR LOCATION: Mitochondrion matrix {ECO:0000255|HAMAP-
CC       Rule:MF_03120}.
CC   -!- SIMILARITY: Belongs to the peptidase S16 family. {ECO:0000255|HAMAP-
CC       Rule:MF_03120}.
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DR   EMBL; CM002239; EAA32590.1; -; Genomic_DNA.
DR   RefSeq; XP_961826.1; XM_956733.2.
DR   AlphaFoldDB; Q7S8C4; -.
DR   SMR; Q7S8C4; -.
DR   STRING; 5141.EFNCRP00000005097; -.
DR   MEROPS; S16.010; -.
DR   EnsemblFungi; EAA32590; EAA32590; NCU05261.
DR   GeneID; 3877974; -.
DR   KEGG; ncr:NCU05261; -.
DR   VEuPathDB; FungiDB:NCU05261; -.
DR   HOGENOM; CLU_004109_1_0_1; -.
DR   InParanoid; Q7S8C4; -.
DR   OMA; YVGPPIY; -.
DR   Proteomes; UP000001805; Chromosome 4, Linkage Group IV.
DR   GO; GO:0005759; C:mitochondrial 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; IBA:GO_Central.
DR   GO; GO:0043565; F:sequence-specific DNA binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0004252; F:serine-type endopeptidase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0003697; F:single-stranded DNA binding; IBA:GO_Central.
DR   GO; GO:0034599; P:cellular response to oxidative stress; IEA:UniProtKB-UniRule.
DR   GO; GO:0051131; P:chaperone-mediated protein complex assembly; IBA:GO_Central.
DR   GO; GO:0035694; P:mitochondrial protein catabolic process; IEA:EnsemblFungi.
DR   GO; GO:0007005; P:mitochondrion organization; IBA:GO_Central.
DR   GO; GO:0070407; P:oxidation-dependent protein catabolic process; IEA:UniProtKB-UniRule.
DR   GO; GO:0006515; P:protein quality control for misfolded or incompletely synthesized proteins; 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_03120; lonm_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; IPR027503; Lonm_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; PTHR43718; PTHR43718; 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   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; DNA-binding; Hydrolase; Mitochondrion; Nucleotide-binding;
KW   Protease; Reference proteome; Serine protease; Transit peptide.
FT   TRANSIT         1..31
FT                   /note="Mitochondrion"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03120"
FT   CHAIN           32..1107
FT                   /note="Lon protease homolog, mitochondrial"
FT                   /id="PRO_0000395781"
FT   DOMAIN          166..439
FT                   /note="Lon N-terminal"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01123"
FT   DOMAIN          891..1077
FT                   /note="Lon proteolytic"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01122"
FT   REGION          32..152
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          273..329
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          808..858
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1085..1107
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        48..62
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        69..103
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        815..834
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        983
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03120"
FT   ACT_SITE        1026
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03120"
FT   BINDING         594..601
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03120"
SQ   SEQUENCE   1107 AA;  121200 MW;  C343DF42887E62D6 CRC64;
     MLSRQRIPRI LASRTSLAHS IRSFTSTTSS IRPVAAAGQH AVTRPRHERP TNLSSFSTYT
     ALGKKNDKGF FDNSIEPLSE EERKANVEHA EAEAKEAESK QAKSKSSTSD APPPAPEDGK
     AGAAGGSSAG SGSGADGGSG DGGKRGRKPG DKALAKPVVP EIYPQVMAIP IAKRPLFPGF
     YKAITIKDPN VAAAITEMIK RGQPYVGAFL FKDENADDDV IRNRDDVYDV GVFAQITSAF
     PMNNQNGEGA SLTAILYPHR RIKLSELIPP GSPEAASIDG AKEGAAPEPV PEPIPKVTDE
     SEQKGDVVAS FEESAVTPRP EPSQKPYEPT SFLKKYPVSL VNVENLTEEP YDPKSQVIRA
     VTNEIVNVFK EVASMNSLFR DQISTFSMSQ STGNVMAEPA KLADFAAAVS AGEPAELQEV
     LSSLNVEERM HKALLVLKKE HVNAQLQSKI TKDVEQKITK RQREYWLMEQ MKGIRRELGI
     ESDGKDKLVE KFKELADKLA MPEAVRKVFD DELNKLAHLE PAASEFNVTR NYLDWLTNIP
     WGQSSAENFD ILNAVKVLDE DHYGLKDVKD RILEFIAVGK LRGTVEGKIL CFVGPPGVGK
     TSIGKSIARA LGRQYYRFSV GGLTDVAEIK GHRRTYVGAL PGRVIQALKK CKTENPLILI
     DEIDKIGRGY QGDPSSALLE LLDPEQNGSF LDHYLDVPVD LSKVLFVCTA NLTDTIPRPL
     LDRMEVIRLS GYVADEKMAI AEKYLAPQAQ EMAGLKGVDV QLTKDAIEEL NKSYCRESGV
     RNLKKKIEQV YRKSALKIVQ DLGEQALPES EALTEEGKAA QEETEKKKSE EAASGETSSP
     KAATEASEKE TTEKPRVAMK IPEGVHVVIN KDNLKDYVGP PIFTSDRLYD VTPPGVTMGL
     AWTSMGGAAM YVESILQSAL TSKSAPSLEI TGNLKTVMKE SSAIAYSYAK AVMAKDFPKN
     RFFDKAKIHV HVPEGAVQKD GPSAGITMTT SLLSLALDTP IDPQIAMTGE LTLTGKVLRI
     GGLREKTVAA RRAGCKMVVF PEDNMSDWLE LPENVKEGIE GRPVRWYSEV FDLIFPKLDR
     EKANKSRIIE DDKSEKEESK KKNDDDE