LONM_EMENI
ID LONM_EMENI Reviewed; 1104 AA.
AC Q5AZT7; C8V214;
DT 13-JUL-2010, integrated into UniProtKB/Swiss-Prot.
DT 26-APR-2005, sequence version 1.
DT 03-AUG-2022, entry version 116.
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=AN6193;
OS Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 /
OS M139) (Aspergillus nidulans).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Nidulantes.
OX NCBI_TaxID=227321;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139;
RX PubMed=16372000; DOI=10.1038/nature04341;
RA Galagan J.E., Calvo S.E., Cuomo C., Ma L.-J., Wortman J.R., Batzoglou S.,
RA Lee S.-I., Bastuerkmen M., Spevak C.C., Clutterbuck J., Kapitonov V.,
RA Jurka J., Scazzocchio C., Farman M.L., Butler J., Purcell S., Harris S.,
RA Braus G.H., Draht O., Busch S., D'Enfert C., Bouchier C., Goldman G.H.,
RA Bell-Pedersen D., Griffiths-Jones S., Doonan J.H., Yu J., Vienken K.,
RA Pain A., Freitag M., Selker E.U., Archer D.B., Penalva M.A., Oakley B.R.,
RA Momany M., Tanaka T., Kumagai T., Asai K., Machida M., Nierman W.C.,
RA Denning D.W., Caddick M.X., Hynes M., Paoletti M., Fischer R., Miller B.L.,
RA Dyer P.S., Sachs M.S., Osmani S.A., Birren B.W.;
RT "Sequencing of Aspergillus nidulans and comparative analysis with A.
RT fumigatus and A. oryzae.";
RL Nature 438:1105-1115(2005).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139;
RX PubMed=19146970; DOI=10.1016/j.fgb.2008.12.003;
RA Wortman J.R., Gilsenan J.M., Joardar V., Deegan J., Clutterbuck J.,
RA Andersen M.R., Archer D., Bencina M., Braus G., Coutinho P., von Dohren H.,
RA Doonan J., Driessen A.J., Durek P., Espeso E., Fekete E., Flipphi M.,
RA Estrada C.G., Geysens S., Goldman G., de Groot P.W., Hansen K.,
RA Harris S.D., Heinekamp T., Helmstaedt K., Henrissat B., Hofmann G.,
RA Homan T., Horio T., Horiuchi H., James S., Jones M., Karaffa L.,
RA Karanyi Z., Kato M., Keller N., Kelly D.E., Kiel J.A., Kim J.M.,
RA van der Klei I.J., Klis F.M., Kovalchuk A., Krasevec N., Kubicek C.P.,
RA Liu B., Maccabe A., Meyer V., Mirabito P., Miskei M., Mos M., Mullins J.,
RA Nelson D.R., Nielsen J., Oakley B.R., Osmani S.A., Pakula T., Paszewski A.,
RA Paulsen I., Pilsyk S., Pocsi I., Punt P.J., Ram A.F., Ren Q., Robellet X.,
RA Robson G., Seiboth B., van Solingen P., Specht T., Sun J.,
RA Taheri-Talesh N., Takeshita N., Ussery D., vanKuyk P.A., Visser H.,
RA van de Vondervoort P.J., de Vries R.P., Walton J., Xiang X., Xiong Y.,
RA Zeng A.P., Brandt B.W., Cornell M.J., van den Hondel C.A., Visser J.,
RA Oliver S.G., Turner G.;
RT "The 2008 update of the Aspergillus nidulans genome annotation: a community
RT effort.";
RL Fungal Genet. Biol. 46:S2-13(2009).
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 ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AACD01000105; EAA57979.1; -; Genomic_DNA.
DR EMBL; BN001301; CBF69998.1; -; Genomic_DNA.
DR RefSeq; XP_663797.1; XM_658705.1.
DR AlphaFoldDB; Q5AZT7; -.
DR SMR; Q5AZT7; -.
DR STRING; 162425.CADANIAP00006816; -.
DR MEROPS; S16.010; -.
DR EnsemblFungi; CBF69998; CBF69998; ANIA_06193.
DR EnsemblFungi; EAA57979; EAA57979; AN6193.2.
DR GeneID; 2870781; -.
DR KEGG; ani:AN6193.2; -.
DR VEuPathDB; FungiDB:AN6193; -.
DR eggNOG; KOG2004; Eukaryota.
DR HOGENOM; CLU_004109_1_0_1; -.
DR InParanoid; Q5AZT7; -.
DR OMA; AVGWYSE; -.
DR OrthoDB; 528132at2759; -.
DR Proteomes; UP000000560; Chromosome I.
DR Proteomes; UP000005890; Unassembled WGS sequence.
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..54
FT /note="Mitochondrion"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03120"
FT CHAIN 55..1104
FT /note="Lon protease homolog, mitochondrial"
FT /id="PRO_0000395779"
FT DOMAIN 199..449
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 41..192
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 296..317
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 825..857
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 57..104
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..169
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 172..188
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 825..843
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 604..611
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03120"
SQ SEQUENCE 1104 AA; 121838 MW; 69DEA460FF11BEDE CRC64;
MLRGQTLRWR AALQTPRSLI LRPLFAPGGY NVGPRSVLET SRRFRSLPPS LRTFSSSTAR
RKEKPPPGDE KEDSNKKENK DNDDGTEDKE VERDPRRKQA DSSGKHGSSV DPGAPTSGFA
RRREKAADRD QRSVTEDAKR EAEAKGNSSD TPSAIPVSDS SSESKPSGSH NGGDDGGKKG
KKNDKALQKP SVPDVYPQVM AIPIAKRPLF PGFYKAITIR DPNVATAIQE MMKRGQPYVG
AFLFKDENAD GDVIESTDDV YDTGVFAQVT AAYPLRGEQS GVTAVLYPHR RIKISSLIPP
GDSTKSGNSE DKTTEKRGDV VASFEENAAE LVTKDHYEPT SFLRKYPVSL VNVENLTEEP
FDKKSAIIRA VTSEIVNVCK EIATLNPLFR DQISAFYTDQ FPGNLSDEPA KLADFAAAVS
GGELHELQEV LESMNIEERL PKGLVVLKKE LMNAQLQTKI SKDVEAKIQK RQREYWLMEQ
MKGIKRELGI ESDGKDKLVE KFKEKAEKLA MPEAVKKVFD EELNKLAHLE PAASEFNVTR
NYLDWLTQIP WGQKSVENFG ISHATDVLNE DHYGLKDVKD RILEFIAVGK LRGTVEGKIL
CLVGPPGVGK TSIGKSIARA LNRQYYRFSV GGLTDVAEIK GHRRTYVGAL PGRIIQALKK
CQTENPLILI DEVDKIGRGH QGDPSSALLE LLDPEQNSSF LDHYMDVPVD LSKVLFVCTA
NVTDTIPRPL LDRMELIELS GYVADEKMAI AQKYLAPAAR ELTGLKNVDV TLTEEAIEEL
IKSYCRESGV RNLKKQIEKV YRKAAFKIVS DLGEDVLAED KALTAEGKAA QEESEKETGP
IESTSEQEKA TTENPRVALN VPDSVHLSIG KDSLTDYVGP PIFTTDRLYD TFPPGVTMGL
AWTSMGGAAL YVESILENAL TPESQPGLDI TGNLQNVMKE STQIAYSFVK SVMAKQFPEN
RFFEKAKLHM HCPEGAVPKD GPSAGITMAT SLLSLALNHP LDPTIAMTGE LTVTGKVLRI
GGLREKTVAA RRAGAKTIIF PADNMSDWLE LPENIKSGIE GHAVSWYSEV FDILFADLDK
QAANRVWQKQ LSKEPKKSND KDDH
