LONM_ASPNC
ID LONM_ASPNC Reviewed; 1113 AA.
AC A2QCJ2;
DT 13-JUL-2010, integrated into UniProtKB/Swiss-Prot.
DT 06-MAR-2007, sequence version 1.
DT 03-AUG-2022, entry version 97.
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=An02g03760;
OS Aspergillus niger (strain CBS 513.88 / FGSC A1513).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Circumdati.
OX NCBI_TaxID=425011;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 513.88 / FGSC A1513 / ATCC MYA-4892;
RX PubMed=17259976; DOI=10.1038/nbt1282;
RA Pel H.J., de Winde J.H., Archer D.B., Dyer P.S., Hofmann G., Schaap P.J.,
RA Turner G., de Vries R.P., Albang R., Albermann K., Andersen M.R.,
RA Bendtsen J.D., Benen J.A.E., van den Berg M., Breestraat S., Caddick M.X.,
RA Contreras R., Cornell M., Coutinho P.M., Danchin E.G.J., Debets A.J.M.,
RA Dekker P., van Dijck P.W.M., van Dijk A., Dijkhuizen L., Driessen A.J.M.,
RA d'Enfert C., Geysens S., Goosen C., Groot G.S.P., de Groot P.W.J.,
RA Guillemette T., Henrissat B., Herweijer M., van den Hombergh J.P.T.W.,
RA van den Hondel C.A.M.J.J., van der Heijden R.T.J.M., van der Kaaij R.M.,
RA Klis F.M., Kools H.J., Kubicek C.P., van Kuyk P.A., Lauber J., Lu X.,
RA van der Maarel M.J.E.C., Meulenberg R., Menke H., Mortimer M.A.,
RA Nielsen J., Oliver S.G., Olsthoorn M., Pal K., van Peij N.N.M.E.,
RA Ram A.F.J., Rinas U., Roubos J.A., Sagt C.M.J., Schmoll M., Sun J.,
RA Ussery D., Varga J., Vervecken W., van de Vondervoort P.J.J., Wedler H.,
RA Woesten H.A.B., Zeng A.-P., van Ooyen A.J.J., Visser J., Stam H.;
RT "Genome sequencing and analysis of the versatile cell factory Aspergillus
RT niger CBS 513.88.";
RL Nat. Biotechnol. 25:221-231(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}.
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DR EMBL; AM270005; CAL00590.1; -; Genomic_DNA.
DR RefSeq; XP_001399512.1; XM_001399475.2.
DR AlphaFoldDB; A2QCJ2; -.
DR SMR; A2QCJ2; -.
DR MEROPS; S16.010; -.
DR PaxDb; A2QCJ2; -.
DR EnsemblFungi; CAL00590; CAL00590; An02g03760.
DR GeneID; 4978863; -.
DR KEGG; ang:ANI_1_516024; -.
DR VEuPathDB; FungiDB:An02g03760; -.
DR HOGENOM; CLU_004109_1_0_1; -.
DR Proteomes; UP000006706; Chromosome 4R.
DR GO; GO:0005759; C:mitochondrial 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:0043565; F:sequence-specific DNA binding; IEA:UniProtKB-UniRule.
DR GO; GO:0004252; F:serine-type endopeptidase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0034599; P:cellular response to oxidative stress; IEA:UniProtKB-UniRule.
DR GO; GO:0051131; P:chaperone-mediated protein complex assembly; IEA:UniProtKB-UniRule.
DR GO; GO:0035694; P:mitochondrial protein catabolic process; IEA:EnsemblFungi.
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; IEA:UniProtKB-UniRule.
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..61
FT /note="Mitochondrion"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03120"
FT CHAIN 62..1113
FT /note="Lon protease homolog, mitochondrial"
FT /id="PRO_0000395773"
FT DOMAIN 204..454
FT /note="Lon N-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01123"
FT DOMAIN 898..1084
FT /note="Lon proteolytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01122"
FT REGION 42..196
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 828..864
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 42..56
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 57..103
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 121..146
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 147..173
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 828..856
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 990
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03120"
FT ACT_SITE 1033
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03120"
FT BINDING 609..616
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03120"
SQ SEQUENCE 1113 AA; 122528 MW; 64DED076C576EDEC CRC64;
MLRGQTLPWR AALQQVSRPF IPRPLLAPSR YNVTARSILN ASRLHRSLPT SRAFSSSSIR
RREKPPPGDE KDDPAQKEQK DANEEKDVER APDARRKAAD PSGKQGSSHE PGAPTSGFAR
RKEKAGADKE QRGLEEDSKK DGNAVEGKGN SSDTPSPIPV NGGSDSRPSG ANNGGNEDGG
KKGKKGSGEK ALQKPSVPEV YPQVMAIPIA KRPLFPGFYK AITIRDPNVA AAIQDMMKRG
QPYVGAFLFK DENADGDVIE NLDDVYDVGV FAQITAAYPL RGEASGVTAV LYPHRRIKVS
SLLPPSDAAK AGTTDEKTSE RRGDVVASFE EGTAELAPKD HYEPTSFLRK YPVSLVNVEN
LAEEPYDKKS AIIRAVTSEI VNVCKEIASL NPLFRDQISA FYTDQFPGNL SDEPAKLADF
AAAVSAGELN EMQEVLELMN IEERLPKALV VLKKELMNAQ LQSKISKDVE AKIQKRQREY
WLMEQMKGIK RELGIESDGK DKLVEKFKEK AEKLAMPDAV KKVFDEELNK LAHLEPAASE
FNVTRNYLDW LTQIPWGQKS VENFGIQHAV KVLDEDHYGL KDVKDRILEF IAVGKLRGTV
EGKILCLVGP PGVGKTSIGK SIARALNRQY YRFSVGGLTD VAEIKGHRRT YVGALPGRII
QALKKCQTEN PLILIDEIDK IGRGHQGDPS SALLELLDPE QNSSFLDHYM DVPVDLSKVL
FVCTANVTDT IPRPLLDRME LIELSGYVAD EKMAIAQRYL APAARELTGL KEVDVNLTEE
AVEELIKSYC RESGVRNLKK QIEKVYRKAA YKIVRDLGED VLAEEKALTD EGKAVQEESQ
KETESPDSKS PVDPEKSTTE TPRVALKVPE SVQLSIGKDS LTDYVGPPIF TADRLYDTFP
PGVTMGLAWT SMGGAALYVE SILENALTPQ SRPGIDITGN LQNVMKESSQ IAYSFAKSVM
AKQFPENRFF EKAKLHMHCP EGAVPKDGPS AGITMATSLL SLALNHPLDP TIAMTGELTV
TGKVLRIGGL REKTVAARRA GAKKIVFPAD NMSDWLELPE NIKEGIEGHA VGWYSEVFDL
LFTDLDKGAA NHVWQKQLAE KPEKKSNEVE EDE
