ID A0A1B8GXC9_9PEZI Unreviewed; 932 AA.
AC A0A1B8GXC9;
DT 02-NOV-2016, integrated into UniProtKB/TrEMBL.
DT 02-NOV-2016, sequence version 1.
DT 24-JAN-2024, entry version 33.
DE RecName: Full=Lon protease homolog 2, peroxisomal {ECO:0000256|HAMAP-Rule:MF_03121};
DE EC=3.4.21.- {ECO:0000256|HAMAP-Rule:MF_03121};
GN ORFNames=VE01_01357 {ECO:0000313|EMBL:OBU00486.1};
OS Pseudogymnoascus verrucosus.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC Leotiomycetes incertae sedis; Pseudeurotiaceae; Pseudogymnoascus.
OX NCBI_TaxID=342668 {ECO:0000313|EMBL:OBU00486.1, ECO:0000313|Proteomes:UP000091956};
RN [1] {ECO:0000313|EMBL:OBU00486.1, ECO:0000313|Proteomes:UP000091956}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=UAMH 10579 {ECO:0000313|EMBL:OBU00486.1,
RC ECO:0000313|Proteomes:UP000091956};
RA Palmer J.M., Drees K.P., Foster J.T., Lindner D.L.;
RT "Comparative genomics of Pseudogymnoascus destructans, the fungus causing
RT white-nose syndrome of bats.";
RL Submitted (MAR-2016) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Proteomes:UP000091956}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=UAMH 10579 {ECO:0000313|Proteomes:UP000091956};
RX PubMed=29295979; DOI=10.1038/s41467-017-02441-z;
RA Palmer J.M., Drees K.P., Foster J.T., Lindner D.L.;
RT "Extreme sensitivity to ultraviolet light in the fungal pathogen causing
RT white-nose syndrome of bats.";
RL Nat. Commun. 9:35-35(2018).
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:0000256|HAMAP-Rule:MF_03121}.
CC -!- SUBCELLULAR LOCATION: Peroxisome matrix {ECO:0000256|ARBA:ARBA00004253,
CC ECO:0000256|HAMAP-Rule:MF_03121}.
CC -!- SIMILARITY: Belongs to the peptidase S16 family. {ECO:0000256|HAMAP-
CC Rule:MF_03121, ECO:0000256|PIRNR:PIRNR001174, ECO:0000256|PROSITE-
CC ProRule:PRU01122}.
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DR EMBL; KV460209; OBU00486.1; -; Genomic_DNA.
DR RefSeq; XP_018134218.1; XM_018270880.1.
DR AlphaFoldDB; A0A1B8GXC9; -.
DR STRING; 342668.A0A1B8GXC9; -.
DR GeneID; 28834743; -.
DR OrthoDB; 1103874at2759; -.
DR Proteomes; UP000091956; Unassembled WGS sequence.
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 CDD; cd19500; RecA-like_Lon; 1.
DR Gene3D; 1.10.8.60; -; 1.
DR Gene3D; 1.20.5.5270; -; 1.
DR Gene3D; 1.20.58.1480; -; 1.
DR Gene3D; 3.30.230.10; -; 1.
DR Gene3D; 2.30.130.40; LON domain-like; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 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_Su5_D2-typ_SF.
DR InterPro; IPR014721; Ribsml_uS5_D2-typ_fold_subgr.
DR PANTHER; PTHR10046; ATP DEPENDENT LON PROTEASE FAMILY MEMBER; 1.
DR PANTHER; PTHR10046:SF24; LON PROTEASE HOMOLOG 2, PEROXISOMAL; 1.
DR Pfam; PF00004; AAA; 1.
DR Pfam; PF05362; Lon_C; 1.
DR Pfam; PF02190; LON_substr_bdg; 1.
DR PIRSF; PIRSF001174; Lon_proteas; 2.
DR PRINTS; PR00830; ENDOLAPTASE.
DR SMART; SM00382; AAA; 1.
DR SMART; SM00464; LON; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR SUPFAM; SSF88697; PUA domain-like; 1.
DR SUPFAM; SSF54211; Ribosomal protein S5 domain 2-like; 1.
DR PROSITE; PS51787; LON_N; 1.
DR PROSITE; PS51786; LON_PROTEOLYTIC; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|HAMAP-
KW Rule:MF_03121};
KW Hydrolase {ECO:0000256|HAMAP-Rule:MF_03121, ECO:0000256|PIRNR:PIRNR001174};
KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_03121,
KW ECO:0000256|PIRNR:PIRNR001174};
KW Peroxisome {ECO:0000256|ARBA:ARBA00023140, ECO:0000256|HAMAP-
KW Rule:MF_03121};
KW Protease {ECO:0000256|ARBA:ARBA00022670, ECO:0000256|HAMAP-Rule:MF_03121};
KW Reference proteome {ECO:0000313|Proteomes:UP000091956};
KW Serine protease {ECO:0000256|ARBA:ARBA00022825, ECO:0000256|HAMAP-
KW Rule:MF_03121}.
FT DOMAIN 9..262
FT /note="Lon N-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51787"
FT DOMAIN 730..916
FT /note="Lon proteolytic"
FT /evidence="ECO:0000259|PROSITE:PS51786"
FT REGION 303..324
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 440..460
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 930..932
FT /note="Microbody targeting signal"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03121"
FT ACT_SITE 822
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03121,
FT ECO:0000256|PIRSR:PIRSR001174-1"
FT ACT_SITE 865
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03121,
FT ECO:0000256|PIRSR:PIRSR001174-1"
FT BINDING 487..494
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03121,
FT ECO:0000256|PIRSR:PIRSR001174-2"
SQ SEQUENCE 932 AA; 101133 MW; 7F8390A55C0789C1 CRC64;
MAPARAQKVP VIPLAADTVL LPGNGLRIPF AASRPDIPAL LSQVYTRASG KPASQRYHNA
HVICVPMNSP LLSSNGQKLL TENELKDKDG KASKYKIPDP ASAKKDDLFT WGTAAKISGV
EGRGTGEFSL IVEGVSRVRV LRVTQERPFF EAEVQYETDV APSPKDTEVQ AMFGTLKTLS
RELLALLRLT SLLPRLSGQS NLTPMLARRI EMFIAKKDIS EAGSLADFVS NLVEATLEEK
LQILAAIDVR TRLERAIELL NKQVAAIKGN IKITSMTSST VPMNGEIDLL NRQRSRTLNR
IAPMPGIPGS GQGPPQDDQE PNEVDELEQK IEAAGLTPEA AKVAGRELKR LKKMPQQQAE
YNVIRTYLEN LAEIPWSAVT EDKLGADTLK RARKQLDDDH YGLDKVKKRL LEYLAVLRLK
QSINDGVEAQ IKSAEAEATE LAKSAEKPED AAEAEPKKEV PAVDSSKIQI LKSKRMVDKS
PILLLAGPPG VGKTSLAKSI ATALGRKFHR ISLGGVRDEA EIRGHRRTYV ASMPGLIVSG
LKKVGVANPV ILLDEIDKVG TSNFHGDPSA AMLEVLDPEQ NHSFTDHYVN IPIDLSKVLF
IATANDLSTI PAPLLDRMET IQLPGYTTLE KRHIASQHLI PKQIRTNGLD LTNVIFPDEV
TSKIIESYTR EAGVRNLERE LGAVCRAKAV AYSDALDSSA LTSYNPVLTL AEIEEILGTE
KFDEELAETR ARPGIVTGLV AYASGGNGSI LFIEVADMPG SGSVQLTGTL GAVLKESVEV
ALSWVKAHAA DLGLAQPGEN IMKSRSIHVH CPGGAVPKDG PSAGMAHAIA LVSLFSDRAV
PPSVAMTGEL SLRGRVHPVG GIKEKLIGAL RAGVKKVILP EGNRKDARDL PDEVKQGLEI
VHVRHIWETI RLIWPETEWR GLAEFADVEA RI
//
