ID   LONP2_ASPFU             Reviewed;         932 AA.
AC   Q4WVD9;
DT   13-JUL-2010, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2005, sequence version 1.
DT   03-AUG-2022, entry version 114.
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=AFUA_5G11750;
OS   Neosartorya fumigata (strain ATCC MYA-4609 / Af293 / CBS 101355 / FGSC
OS   A1100) (Aspergillus fumigatus).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC   Aspergillus subgen. Fumigati.
OX   NCBI_TaxID=330879;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC MYA-4609 / Af293 / CBS 101355 / FGSC A1100;
RX   PubMed=16372009; DOI=10.1038/nature04332;
RA   Nierman W.C., Pain A., Anderson M.J., Wortman J.R., Kim H.S., Arroyo J.,
RA   Berriman M., Abe K., Archer D.B., Bermejo C., Bennett J.W., Bowyer P.,
RA   Chen D., Collins M., Coulsen R., Davies R., Dyer P.S., Farman M.L.,
RA   Fedorova N., Fedorova N.D., Feldblyum T.V., Fischer R., Fosker N.,
RA   Fraser A., Garcia J.L., Garcia M.J., Goble A., Goldman G.H., Gomi K.,
RA   Griffith-Jones S., Gwilliam R., Haas B.J., Haas H., Harris D.E.,
RA   Horiuchi H., Huang J., Humphray S., Jimenez J., Keller N., Khouri H.,
RA   Kitamoto K., Kobayashi T., Konzack S., Kulkarni R., Kumagai T., Lafton A.,
RA   Latge J.-P., Li W., Lord A., Lu C., Majoros W.H., May G.S., Miller B.L.,
RA   Mohamoud Y., Molina M., Monod M., Mouyna I., Mulligan S., Murphy L.D.,
RA   O'Neil S., Paulsen I., Penalva M.A., Pertea M., Price C., Pritchard B.L.,
RA   Quail M.A., Rabbinowitsch E., Rawlins N., Rajandream M.A., Reichard U.,
RA   Renauld H., Robson G.D., Rodriguez de Cordoba S., Rodriguez-Pena J.M.,
RA   Ronning C.M., Rutter S., Salzberg S.L., Sanchez M., Sanchez-Ferrero J.C.,
RA   Saunders D., Seeger K., Squares R., Squares S., Takeuchi M., Tekaia F.,
RA   Turner G., Vazquez de Aldana C.R., Weidman J., White O., Woodward J.R.,
RA   Yu J.-H., Fraser C.M., Galagan J.E., Asai K., Machida M., Hall N.,
RA   Barrell B.G., Denning D.W.;
RT   "Genomic sequence of the pathogenic and allergenic filamentous fungus
RT   Aspergillus fumigatus.";
RL   Nature 438:1151-1156(2005).
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; AAHF01000003; EAL91437.1; -; Genomic_DNA.
DR   RefSeq; XP_753475.1; XM_748382.1.
DR   AlphaFoldDB; Q4WVD9; -.
DR   SMR; Q4WVD9; -.
DR   STRING; 746128.CADAFUBP00005805; -.
DR   EnsemblFungi; EAL91437; EAL91437; AFUA_5G11750.
DR   GeneID; 3511518; -.
DR   KEGG; afm:AFUA_5G11750; -.
DR   VEuPathDB; FungiDB:Afu5g11750; -.
DR   eggNOG; KOG2004; Eukaryota.
DR   HOGENOM; CLU_004109_4_0_1; -.
DR   InParanoid; Q4WVD9; -.
DR   OMA; MVNIEDK; -.
DR   OrthoDB; 528132at2759; -.
DR   Proteomes; UP000002530; Chromosome 5.
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_0000395789"
FT   DOMAIN          11..257
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          304..340
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   COMPBIAS        315..340
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
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;  102474 MW;  29420B125D6747F4 CRC64;
     MGSNNGRAMK LALVPLPKGS VLLPGVTLRI PVSNRPDLAN LLSALLDQTN LGKRDGNTIT
     FGCVPLRSPL LSNDGQQLID DGSVDGAKKE EFDAIDAGQA RKEDLFRYGT VGKVIGVQRR
     AYAEPFLVVQ GVQRFTIKHI LRERPFFEGE VVLHNERDAI SSDAETVELF QQLRQLSREL
     ITLLRLSSLL PSTGTRLSPL VARKFEVYIA KTDLSQAGNL ADFMADVADP TFEEKLRVLA
     SFALRTRLER VVELLARQVQ GIKNSVKVTT ISTSSFPSNS PFDISQIDPR DRELLARRVM
     AGLTGLTPPG AAGGRNNEDE KETNEVDELQ KRLQEAELSP EARKVADKEL RRLRKMNPAN
     AEYGVCRTYL ENIADIPWTK VTEDKLGPET LKRARNQLDE DHYGLETIKK RLLEYLAVLR
     LKQSTNQDVE RQIAALTKEL DAANEVLAEK DVPALSESDR VSLEAKLNLL QSRRLADKSP
     ILLLVGPPGT GKTSLARSVA TSLGRKFHRI SLGGVRDEAE IRGHRRTYVA AMPGLIVNGL
     KKVGVANPVF LLDEIDKVGG ANFQGDPSAA MLEVLDPEQN STFVDHYINI PIDLSKVLFI
     ATANSLDTIP APLLDRMETI TLSGYTTVEK RHIAKRHLIP KQIRANGLAE GQVVLSDEVV
     DKVITSYTRE SGVRNLEREL GSICRHKAVQ YADAVDNGRL DTYNPVVALG DLEDILGIER
     FDEEIAEKHG RPGVVTGLVA YSTGGQGSIL FIEVADMPGN GRVQLTGKLG DVLKESVEVA
     LTWVKAHSFE LGLTHDPNED IMKNRSLHVH CPAGAIPKDG PSAGLAHTIG LISLFTGKAV
     PPQIAMTGEV SLRGRVMPVG GIKEKLIGAH RAGVKTVLLP EQNRKDVKDV PQEVHDGLQI
     VYVRHIWEAI RQVWPGAHWP GQHHINFVES RL