LONM_PICST
ID LONM_PICST Reviewed; 1086 AA.
AC A3M072;
DT 13-JUL-2010, integrated into UniProtKB/Swiss-Prot.
DT 13-JUL-2010, sequence version 3.
DT 03-AUG-2022, entry version 90.
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; Fragment;
GN Name=PIM1 {ECO:0000255|HAMAP-Rule:MF_03120}; ORFNames=PICST_64463;
OS Scheffersomyces stipitis (strain ATCC 58785 / CBS 6054 / NBRC 10063 / NRRL
OS Y-11545) (Yeast) (Pichia stipitis).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Debaryomycetaceae; Scheffersomyces.
OX NCBI_TaxID=322104;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 58785 / CBS 6054 / NBRC 10063 / NRRL Y-11545;
RX PubMed=17334359; DOI=10.1038/nbt1290;
RA Jeffries T.W., Grigoriev I.V., Grimwood J., Laplaza J.M., Aerts A.,
RA Salamov A., Schmutz J., Lindquist E., Dehal P., Shapiro H., Jin Y.-S.,
RA Passoth V., Richardson P.M.;
RT "Genome sequence of the lignocellulose-bioconverting and xylose-fermenting
RT yeast Pichia stipitis.";
RL Nat. Biotechnol. 25:319-326(2007).
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}.
CC -!- SEQUENCE CAUTION:
CC Sequence=ABN68665.2; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; CP000502; ABN68665.2; ALT_INIT; Genomic_DNA.
DR RefSeq; XP_001386694.2; XM_001386657.1.
DR AlphaFoldDB; A3M072; -.
DR SMR; A3M072; -.
DR STRING; 4924.XP_001386694.2; -.
DR EnsemblFungi; ABN68665; ABN68665; PICST_64463.
DR GeneID; 4840951; -.
DR KEGG; pic:PICST_64463; -.
DR eggNOG; KOG2004; Eukaryota.
DR HOGENOM; CLU_004109_1_0_1; -.
DR InParanoid; A3M072; -.
DR OrthoDB; 528132at2759; -.
DR Proteomes; UP000002258; Chromosome 8.
DR GO; GO:0005759; C:mitochondrial matrix; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR GO; GO:0004176; F:ATP-dependent peptidase activity; IEA:InterPro.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0004252; F:serine-type endopeptidase activity; IEA:UniProtKB-EC.
DR GO; GO:0006515; P:protein quality control for misfolded or incompletely synthesized proteins; IEA:InterPro.
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; 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.
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..55
FT /note="Mitochondrion"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03120"
FT CHAIN 56..1086
FT /note="Lon protease homolog, mitochondrial"
FT /id="PRO_0000395782"
FT DOMAIN 183..404
FT /note="Lon N-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01123"
FT DOMAIN 871..1059
FT /note="Lon proteolytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01122"
FT REGION 61..176
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 767..788
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 800..835
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 84..123
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 126..172
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 767..781
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 811..826
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 965
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03120"
FT ACT_SITE 1008
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03120"
FT BINDING 558..565
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03120"
FT NON_TER 1
SQ SEQUENCE 1086 AA; 120080 MW; 2F8A17374B4BA506 CRC64;
MLRTSCTSSL RRVVGKYVVS PLVASQIRFA TSSVRSQPYL LNSELTELPA QFKRYSSILL
TEKPEGDVPE SGPEPSGESG ISEKSNVEND KHDGNDEIKP EAEKNEKDEI EKPEIDKDAI
VETDGVSESS VENVSGSSSA AGGASAPPSG NSNNNNNNNN NNNDNDEPNE IVTNAGTGLY
PPLLAIPMKD RPPLPGRPFA INITDPEVIR SIYTIIDKRE PYFVLFHVKD PNEGDTDVIN
SKDSVYNIGV HCQIIRHTTP RPGVFNVLGY PLERCSLADL STPSEKKGET ETRKEGENFP
TSYLKGLKVS YATVKPVKDE PFDKTSTDIK SLVESLKALL SKMGAKNPLE KLQIKEGTEL
VNDPPRFADF VGSTIHGDPK KIQEILESLN IQTRLSKALE LLKVELKASL IKENTIHNLS
TKADEYQTRL FIKEFIKELQ KRAGIVESDD KKTSKFDERL KHLKMTEEAL EAYNAEKAKM
ESQNEHSSEL GVSERYLDWL TSIPWGIYSK DRFNIKQARE ILDRDHYGLK DVKDRILEFI
SMGRVSGKVD GKILCLTGPP GTGKTSIAKS IAESLNRKYV RIAMGGIQDV HEVKGHRRTY
VGSIPGRIIS ALKQAKTSNP LMLIDEIDKL DLSRSGGASS AFLEILDPEQ NNAFVDNYID
VKVDLSKVLF VCTANYLGNI SPPLRDRMEI IEVNGYTNNE KIEIAKRHLI PDAAKKAGLE
GGHVVIETKT ISRLIEKYCR ESGLRNIKKL ITRIFSKASL KIVEEVEARE GESKSKSEEA
KSEAITGSVT EISVEDATVK AQSIEEPSVE SASQKVDEAK PVESEELKSD EEEEEVVKLE
IPDDIKLEIT SANLKDYVGP EIYTRDRVYD IPPPGVATGL SYSTSGNGDA LYIESILTHS
IGSGSGHASI HVTGSLKDVM KESASIAYSF AKSYMVKNYP ENRFFEAAEI HVHCPDGAIP
KDGPSAGISF TSSLISLALQ KPLPPTIAMT GEITVTGRVL AVGGLREKIL GAKRYGCNTI
IFPKDIENEL EEIPEEVKEG VKFIPVEWYQ DVFDEIFPNL SSDEGNEVWK EEFNKLDKKK
ASNKKK
