ID   LONP2_EMENI             Reviewed;         932 AA.
AC   Q5BH58; C8VQK2;
DT   13-JUL-2010, integrated into UniProtKB/Swiss-Prot.
DT   26-APR-2005, sequence version 1.
DT   03-AUG-2022, entry version 113.
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=AN0122;
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 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; AACD01000004; EAA65300.1; -; Genomic_DNA.
DR   EMBL; BN001308; CBF90156.1; -; Genomic_DNA.
DR   RefSeq; XP_657726.1; XM_652634.1.
DR   AlphaFoldDB; Q5BH58; -.
DR   SMR; Q5BH58; -.
DR   STRING; 162425.CADANIAP00002625; -.
DR   PRIDE; Q5BH58; -.
DR   EnsemblFungi; CBF90156; CBF90156; ANIA_00122.
DR   EnsemblFungi; EAA65300; EAA65300; AN0122.2.
DR   GeneID; 2875898; -.
DR   KEGG; ani:AN0122.2; -.
DR   eggNOG; KOG2004; Eukaryota.
DR   HOGENOM; CLU_004109_4_0_1; -.
DR   InParanoid; Q5BH58; -.
DR   OMA; MVNIEDK; -.
DR   OrthoDB; 528132at2759; -.
DR   Proteomes; UP000000560; Chromosome VIII.
DR   Proteomes; UP000005890; Unassembled WGS sequence.
DR   GO; GO:0005782; C:peroxisomal 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; 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; IBA:GO_Central.
DR   GO; GO:0006515; P:protein quality control for misfolded or incompletely synthesized proteins; IEA:UniProtKB-UniRule.
DR   GO; GO:0006625; P:protein targeting to peroxisome; 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_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   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..932
FT                   /note="Lon protease homolog 2, peroxisomal"
FT                   /id="PRO_0000395794"
FT   DOMAIN          11..258
FT                   /note="Lon N-terminal"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01123"
FT   DOMAIN          729..916
FT                   /note="Lon proteolytic"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01122"
FT   REGION          298..328
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           930..932
FT                   /note="Microbody targeting signal"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03121"
FT   ACT_SITE        822
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03121"
FT   ACT_SITE        865
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03121"
FT   BINDING         486..493
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03121"
SQ   SEQUENCE   932 AA;  102748 MW;  1E963597BBE2A9C5 CRC64;
     MGTNGGRPTK LSLVPLPKGS VLLPGATLRI PVSNRPDLAN LLSSLLDRTN AIRRDANSIT
     FGCVPLCSPY LSKDGQHVID NGTVDEDKKE EFESLEAGQA RKEDLYRYGT LGKVIGVQRR
     AYSEPHLLVQ GVQRLTVRRV LRERPFFEAE CILHDEKETP LNDRETAELF QQLRQLSREL
     LTLLRYTSLI PNTGGPRLSP LIARKFELII TKSDLAQAGR LADVMADIAE SGLEDKLRVL
     AAFDVKTRLE RVVDILNKQN QIIRGSVKFT TISTDNIPPA SVLDISQIDP RIRDLLSRRG
     IPGASGTPPP GLGGRNNEAD EKESNELDEL QQRLKDAQLS PEAQKVADKE MRRLRKMMPV
     NQEYGVIRTY LENLADIPWT KVTEDKLGPE TLKAARKQLD DDHYGLEKIK KRLLEYLAVL
     RLKQSTNQGL EQQISILTKE LDNSGGDIEK DIPSLPESDR AAIESKLNAL TSKRTVDKSP
     ILLLVGPPGT GKTSLARSVA TALGRKFHRI SLGGVRDEAE IRGHRRTYVA AMPGVIVNGL
     KKVGVANPVF LLDEIDKIGG PNFQGDPSAA MLEVLDPEQN HTFVDHYINI PIDLSKVLFI
     ATANSLDTIP APLLDRMETI QLSGYTTVEK RHIAKRHLLP KQIRANGLSD GQVVLSDDVI
     DKTTTSYTRE SGVRNLEREL GSICRYKAVQ FADATDSAKL ESYNPVVTVD DLEEILGIER
     FDEEIAEKHG RPGVVTGLVA YSTGGQGSIL FIEVADMPGS GRVQLTGKLG DVLKESVEVA
     LTWVKAHSFE LGLTSDPNED IMKNRSLHVH CPSGAIPKDG PSAGLAHTIG LISLFSGKAV
     PPKLAMTGEV SLRGRVMPVG GIKEKLIGAL RAGVTTVLLP HQNRKDVKDV PEEVSNGLEI
     IYVKHIWEAI RHIWPDAHWP GQHHMDFVES RL