LONM_CRYNJ
ID LONM_CRYNJ Reviewed; 1104 AA.
AC P0CQ16; Q55U62; Q5KI83;
DT 28-JUN-2011, integrated into UniProtKB/Swiss-Prot.
DT 28-JUN-2011, sequence version 1.
DT 03-AUG-2022, entry version 59.
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 {ECO:0000255|HAMAP-Rule:MF_03120}; OrderedLocusNames=CND03860;
OS Cryptococcus neoformans var. neoformans serotype D (strain JEC21 / ATCC
OS MYA-565) (Filobasidiella neoformans).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Tremellomycetes;
OC Tremellales; Cryptococcaceae; Cryptococcus;
OC Cryptococcus neoformans species complex.
OX NCBI_TaxID=214684;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JEC21 / ATCC MYA-565;
RX PubMed=15653466; DOI=10.1126/science.1103773;
RA Loftus B.J., Fung E., Roncaglia P., Rowley D., Amedeo P., Bruno D.,
RA Vamathevan J., Miranda M., Anderson I.J., Fraser J.A., Allen J.E.,
RA Bosdet I.E., Brent M.R., Chiu R., Doering T.L., Donlin M.J., D'Souza C.A.,
RA Fox D.S., Grinberg V., Fu J., Fukushima M., Haas B.J., Huang J.C.,
RA Janbon G., Jones S.J.M., Koo H.L., Krzywinski M.I., Kwon-Chung K.J.,
RA Lengeler K.B., Maiti R., Marra M.A., Marra R.E., Mathewson C.A.,
RA Mitchell T.G., Pertea M., Riggs F.R., Salzberg S.L., Schein J.E.,
RA Shvartsbeyn A., Shin H., Shumway M., Specht C.A., Suh B.B., Tenney A.,
RA Utterback T.R., Wickes B.L., Wortman J.R., Wye N.H., Kronstad J.W.,
RA Lodge J.K., Heitman J., Davis R.W., Fraser C.M., Hyman R.W.;
RT "The genome of the basidiomycetous yeast and human pathogen Cryptococcus
RT neoformans.";
RL Science 307:1321-1324(2005).
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=AAW43319.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AE017344; AAW43319.1; ALT_SEQ; Genomic_DNA.
DR RefSeq; XP_570626.1; XM_570626.1.
DR AlphaFoldDB; P0CQ16; -.
DR SMR; P0CQ16; -.
DR STRING; 5207.AAW43319; -.
DR PaxDb; P0CQ16; -.
DR EnsemblFungi; ALO60533; ALO60533; CND03865.
DR GeneID; 3256968; -.
DR KEGG; cne:CND03865; -.
DR VEuPathDB; FungiDB:CND03865; -.
DR eggNOG; KOG2004; Eukaryota.
DR eggNOG; KOG2910; Eukaryota.
DR InParanoid; P0CQ16; -.
DR Proteomes; UP000002149; Chromosome 4.
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: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; 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..58
FT /note="Mitochondrion"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03120"
FT CHAIN 59..1104
FT /note="Lon protease homolog, mitochondrial"
FT /id="PRO_0000395777"
FT DOMAIN 155..442
FT /note="Lon N-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01123"
FT DOMAIN 895..1082
FT /note="Lon proteolytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01122"
FT REGION 8..144
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 275..295
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 64..107
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 108..127
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 281..295
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 987
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03120"
FT ACT_SITE 1030
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03120"
FT BINDING 597..604
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03120"
SQ SEQUENCE 1104 AA; 120556 MW; 419D086E328397F9 CRC64;
MLPLRAFARL AQRPRLSRPT QLARSSLPRP SPSRPAAHYL ALAPAPSTRF LHSSPPVLKE
KRWLNNTPPE DDGEDGQNPK QDDQVEKPLP DAESSKSAEE RAKSQSSKPD IKASSSDSVS
SSAPAPGSAD GGSPPGAGGP KEVAKPVIPE IYPQVLAIPI THRPLFPGFY KAVTVRSPPV
IKAIRELQAH GQPYVGAFLL KDSTVDSDVV TDINQVQPVG VFCQITSCFT SQEGEGKPEA
LTAVLFPHRR IKINELVKSS GTKGDGTVGV GGLVEGSQDS AKGEGEVKSF ESEVPGVEEV
REELGTVSID SEQPDVHKEN RDLETKEVTQ IDFLHSLLPQ VSLTNVSNLS IEPYEKDSQV
IRAIMSELIS VFKEIAQLQP MFREQVTSFA ISNTSSQVFD EPDKLADLAA VVSTADVSDL
QAVLSSTSIE DRLQRALVLL KKELINAQLQ FKISRDVDTK IQKRQREYYL MEQLKGIKKE
LGMESDGKDK LVEGFKEKAS KLAMPEGVRK VFDEELNKLV HLEPAASEFN VTRNYIDWLT
QVPWGVHTPE NYNISHAIKI LDEDHYGLKD VKDRILEFMA IGKLRGSVEG KILCLVGPPG
VGKTSIGKSI AKALGRQFFR FSVGGLTDVA EIKGHRRTYI GAMPGKPIQA LKKVATENPL
ILIDEVDKIS KAYNGDPASA LLEMLDPEQN KSFLDHYLDV PIDLSKVLFV CTANVLETIP
GPLLDRMEVL EVSGYVSAEK MNIAERYLSP QAKVAAGLED VNIELEPGAI EALIRYYCRE
SGVRNLKKHI DKIYRKAAFK IVTDLGESGL PEPATPPAEN QVEAQYPDIK PASELTYNVI
PGTEVSGVDT KTDVTTVPRE PMKVPAGIHV KVTQENLKDY VGPPLYHKDR LYTHSPPAGV
STGLGYLGNG SGAVMPVEIN SMPGKGNLQL TGKLGEVIRE SAQIAMSWVK SNAYLLGITK
SEAEATLNDR DVHLHMPEGG IGKEGPSAGT AILTAFVSLF TKTRVDPDIA MTGEISLLGQ
VLPVGGLKEK ILAAHRAGIK KLIVPAGCKP DIDENVPESV KGGIEFVFVE DVRQVLHEAF
RGTEVEKRWQ ETLPMEEEPQ RERH
