LONP2_ASPNC
ID LONP2_ASPNC Reviewed; 929 AA.
AC A2RAF6;
DT 13-JUL-2010, integrated into UniProtKB/Swiss-Prot.
DT 06-MAR-2007, sequence version 1.
DT 03-AUG-2022, entry version 100.
DE RecName: Full=Lon protease homolog 2, peroxisomal {ECO:0000255|HAMAP-Rule:MF_03121};
DE EC=3.4.21.53 {ECO:0000255|HAMAP-Rule:MF_03121};
GN ORFNames=An18g02980;
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 and unassembled polypeptides in the
CC peroxisomal matrix. Necessary for type 2 peroxisome targeting signal
CC (PTS2)-containing protein processing and facilitates peroxisome matrix
CC protein import. {ECO:0000255|HAMAP-Rule:MF_03121}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Hydrolysis of proteins in presence of ATP.; EC=3.4.21.53;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_03121};
CC -!- SUBCELLULAR LOCATION: Peroxisome matrix {ECO:0000255|HAMAP-
CC Rule:MF_03121}.
CC -!- SIMILARITY: Belongs to the peptidase S16 family. {ECO:0000255|HAMAP-
CC Rule:MF_03121}.
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DR EMBL; AM270401; CAK48682.1; -; Genomic_DNA.
DR AlphaFoldDB; A2RAF6; -.
DR SMR; A2RAF6; -.
DR PaxDb; A2RAF6; -.
DR PRIDE; A2RAF6; -.
DR EnsemblFungi; CAK48682; CAK48682; An18g02980.
DR VEuPathDB; FungiDB:An18g02980; -.
DR HOGENOM; CLU_004109_4_0_1; -.
DR Proteomes; UP000006706; Chromosome 8L.
DR GO; GO:0005782; C:peroxisomal 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:0004252; F:serine-type endopeptidase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0016558; P:protein import into peroxisome matrix; IEA:UniProtKB-UniRule.
DR GO; GO:0016485; P:protein processing; 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_03121; lonp2_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; IPR027501; Lonp2_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; PTHR10046; PTHR10046; 1.
DR Pfam; PF00004; AAA; 1.
DR Pfam; PF05362; Lon_C; 1.
DR Pfam; PF02190; LON_substr_bdg; 1.
DR PIRSF; PIRSF001174; Lon_proteas; 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; Hydrolase; Nucleotide-binding; Peroxisome; Protease;
KW Reference proteome; Serine protease.
FT CHAIN 1..929
FT /note="Lon protease homolog 2, peroxisomal"
FT /id="PRO_0000395790"
FT DOMAIN 11..255
FT /note="Lon N-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01123"
FT DOMAIN 727..914
FT /note="Lon proteolytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01122"
FT REGION 302..325
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 927..929
FT /note="Microbody targeting signal"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03121"
FT ACT_SITE 820
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03121"
FT ACT_SITE 863
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03121"
FT BINDING 484..491
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03121"
SQ SEQUENCE 929 AA; 102394 MW; 4D50DFB1459FD423 CRC64;
MGSNSGRTTK LPLVPLPKGS VLLPGITLRI PVSNRPDLAN LLSTIVDRSA VAKRDGTAIT
FGCVPLSSPY LSKDGQRLID DGSLDEDRRE EFDMIDAGQS RKEDLFRHGT IGKVIGIQRR
AYSEPALVVQ GVQRFTIRRV LKERPFFEAE AVVHDEKVSG DAETVELFQQ LRQLSRELLT
LLRLSSLLPS PGSRLSPLIA RKFELFITKS DVSHASRLAD FMADVADSGF EEKLRILASL
DVKIRLERVV EILTRQLQSI KSNVKVTTIT TNSFPSSGFD INQIDPRDRE ILARKAMAGL
SGLTPPGLSA GRNNDNDDKE SNEVDELQQR LQEAQLSPEA RKVADKELRR LRKMNPANAE
YGVCRTYLEN IADIPWTKMT EDQLGPETLK RARKQLDDDH YGLEKIKKRL LEYLAVLRLK
QSTNRDVERQ IESLSKELEA SDGGDLEKEV PVLSETDRVA VETKLHMLKT RRMGDKSPIL
LLVGPPGVGK TSLARSVASS LGRKFHRISL GGVRDEAEIR GHRRTYVAAM PGLIVSGLKK
VGVANPVFLL DEIDKVGGAN FQGDPSAAML EVLDPEQNHT FSDHYINIPI DLSKVLFIAT
ANSLDTIPAP LLDRMETISL SGYTTVEKRH IAKRHLIPKQ IRANGLSDGQ VVLSDEVIDK
IITSYTRESG VRNLERELGS VCRFKAVQFA DAGDAGRLDA YNPVVSMDEL EEILGIERFE
EEIAEKHGRP GVVTGLVAYS TGGQGSILFI EVADMPGNGR VQLTGKLGDV LKESVEVALT
WVKAHAFELG LTADPTEDIM KNRSLHVHCP SGAIPKDGPS AGLAHTMGLI SLFTGKAVPP
SVAMTGEVSL RGKVMPVGGI KEKLIGALRA GVKTVLLPHH NRKDVKDVPQ EVSEGLEIVY
VTHIWEAIRQ VWPDAHWPGQ HTHFIESRL
