ID A0A0C2XST5_HEBCY Unreviewed; 1113 AA.
AC A0A0C2XST5;
DT 01-APR-2015, integrated into UniProtKB/TrEMBL.
DT 01-APR-2015, sequence version 1.
DT 24-JAN-2024, entry version 41.
DE RecName: Full=Lon protease homolog, mitochondrial {ECO:0000256|HAMAP-Rule:MF_03120};
DE EC=3.4.21.53 {ECO:0000256|HAMAP-Rule:MF_03120};
GN Name=PIM1 {ECO:0000256|HAMAP-Rule:MF_03120};
GN ORFNames=M413DRAFT_72723 {ECO:0000313|EMBL:KIM40763.1};
OS Hebeloma cylindrosporum h7.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Agaricomycetidae; Agaricales; Agaricineae; Hymenogastraceae; Hebeloma.
OX NCBI_TaxID=686832 {ECO:0000313|EMBL:KIM40763.1, ECO:0000313|Proteomes:UP000053424};
RN [1] {ECO:0000313|EMBL:KIM40763.1, ECO:0000313|Proteomes:UP000053424}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=h7 {ECO:0000313|Proteomes:UP000053424};
RG DOE Joint Genome Institute;
RA Kuo A., Gay G., Dore J., Kohler A., Nagy L.G., Floudas D., Copeland A.,
RA Barry K.W., Cichocki N., Veneault-Fourrey C., LaButti K., Lindquist E.A.,
RA Lipzen A., Lundell T., Morin E., Murat C., Sun H., Tunlid A., Henrissat B.,
RA Grigoriev I.V., Hibbett D.S., Martin F., Nordberg H.P., Cantor M.N.,
RA Hua S.X.;
RL Submitted (APR-2014) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Proteomes:UP000053424}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=h7 {ECO:0000313|Proteomes:UP000053424};
RG DOE Joint Genome Institute;
RG Mycorrhizal Genomics Consortium;
RA Kohler A., Kuo A., Nagy L.G., Floudas D., Copeland A., Barry K.W.,
RA Cichocki N., Veneault-Fourrey C., LaButti K., Lindquist E.A., Lipzen A.,
RA Lundell T., Morin E., Murat C., Riley R., Ohm R., Sun H., Tunlid A.,
RA Henrissat B., Grigoriev I.V., Hibbett D.S., Martin F.;
RT "Evolutionary Origins and Diversification of the Mycorrhizal Mutualists.";
RL Submitted (JAN-2015) to the EMBL/GenBank/DDBJ databases.
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:0000256|HAMAP-Rule:MF_03120}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Hydrolysis of proteins in presence of ATP.; EC=3.4.21.53;
CC Evidence={ECO:0000256|HAMAP-Rule:MF_03120};
CC -!- SUBUNIT: Homohexamer or homoheptamer. Organized in a ring with a
CC central cavity. {ECO:0000256|HAMAP-Rule:MF_03120}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion matrix
CC {ECO:0000256|ARBA:ARBA00004305, ECO:0000256|HAMAP-Rule:MF_03120}.
CC -!- SIMILARITY: Belongs to the peptidase S16 family. {ECO:0000256|HAMAP-
CC Rule:MF_03120, ECO:0000256|PROSITE-ProRule:PRU01122}.
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DR EMBL; KN831782; KIM40763.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0C2XST5; -.
DR STRING; 686832.A0A0C2XST5; -.
DR HOGENOM; CLU_004109_1_0_1; -.
DR OrthoDB; 1103874at2759; -.
DR Proteomes; UP000053424; Unassembled WGS sequence.
DR GO; GO:0005759; C:mitochondrial 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:0043565; F:sequence-specific DNA binding; IEA:UniProtKB-UniRule.
DR GO; GO:0004252; F:serine-type endopeptidase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0034599; P:cellular response to oxidative stress; IEA:UniProtKB-UniRule.
DR GO; GO:0051131; P:chaperone-mediated protein complex assembly; IEA:UniProtKB-UniRule.
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; 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_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; IPR015947; PUA-like_sf.
DR InterPro; IPR020568; Ribosomal_Su5_D2-typ_SF.
DR InterPro; IPR014721; Ribsml_uS5_D2-typ_fold_subgr.
DR NCBIfam; TIGR00763; lon; 1.
DR PANTHER; PTHR43718; LON PROTEASE; 1.
DR PANTHER; PTHR43718:SF2; LON PROTEASE HOMOLOG, MITOCHONDRIAL; 1.
DR Pfam; PF00004; AAA; 1.
DR Pfam; PF05362; Lon_C; 1.
DR Pfam; PF02190; LON_substr_bdg; 1.
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_03120}; DNA-binding {ECO:0000256|HAMAP-Rule:MF_03120};
KW Hydrolase {ECO:0000256|HAMAP-Rule:MF_03120, ECO:0000256|PROSITE-
KW ProRule:PRU01122};
KW Mitochondrion {ECO:0000256|ARBA:ARBA00023128, ECO:0000256|HAMAP-
KW Rule:MF_03120}; Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_03120};
KW Protease {ECO:0000256|ARBA:ARBA00022670, ECO:0000256|HAMAP-Rule:MF_03120};
KW Reference proteome {ECO:0000313|Proteomes:UP000053424};
KW Serine protease {ECO:0000256|ARBA:ARBA00022825, ECO:0000256|HAMAP-
KW Rule:MF_03120}.
FT DOMAIN 161..425
FT /note="Lon N-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51787"
FT DOMAIN 894..1081
FT /note="Lon proteolytic"
FT /evidence="ECO:0000259|PROSITE:PS51786"
FT REGION 61..150
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 275..312
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 791..866
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1089..1113
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 77..99
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 101..129
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 288..302
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 819..849
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 986
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03120,
FT ECO:0000256|PROSITE-ProRule:PRU01122"
FT ACT_SITE 1029
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03120,
FT ECO:0000256|PROSITE-ProRule:PRU01122"
FT BINDING 580..587
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03120"
SQ SEQUENCE 1113 AA; 120884 MW; 320A6ECF9D96C68D CRC64;
MSRFASTFIR AAPALRHSLL SNNNTRPSLI LQQAAYNGAW KRGFTVSQIA AVRNGSSLKA
PRWVNSKSGE GQAPPATTPK EKEEGDVEKD GEEGVGNPEK TDSEPPSSSS SSSSSSDSSS
IHDADGPSSP PSSNVPPPPS QSGSGSGSIA KQSVPEIYPQ MLALPIARRP LFPGFYKAVV
VRNPAVVAAI KEMMKRGQPY LGAFLLKDEN TDSDVITDVN SVHPVGVFAQ ITSVFAAAGR
SADGGPNGEI EEGLTAVLYP HRRIKITELV KAGGAKMEEV EQQEEPQTVE PPTPPPTPPP
SAEKHLSEST SGPVQTAFLH KHDISIVNVE NLVTLPYNKD DQYIRAFMSE IVSVFKDIAQ
LNPLFRDQIT NISINQVAAN VFDEPDKLAD FAAAVSSGEV QELQDVLESL VVDDRLRKAL
LVLKKELINA QLQSKLSRDV DSKIAKRQRE YYLMEQLKGI KKELGMESDG KDKLIEKFRE
RAAGLKMPEG VRKVFDEELA KLQGLEPAAS EANVTRNYLD WLTQIPWGRH TPENYSIPHA
ETVLNEDHYG LTDVKSRILE FLAVGKLRGT VEGKIICLVG PPGVGKTSIG KSIARALGRR
FFRFSVGGLT DVAEIKGHRR TYVGALPGKI IQALKRVETE NPLVLIDEVD KIGRGINGDP
ASALLEMLDP EQNNGFLDHY MDVPVDLSRV LFVCTANNLD TIPAPLLDRM EVLEVSGYVS
EEKSVIAQRY LGPQAREASG LKGADVELEE GAVDVLIKYY CRESGVRNLK KHIEKIYRKA
ALKLVQDLGE EKLSEPPAPA SSAPPSTSEP HATPDTEKEP PSSAVSQEPT ESPIEPDTST
SSTPPEGAAS PRPVTTERKP MHIPESVHVR ITPENLKEYV GPPVYQKDRM YAYMPPPGVS
TGLGYLGNGS GAVMPIEAMS MPGKGGLQLT GKLGEVIRES AQIAQSWVRS NAFELGITKA
PEEQFLVDRD IHVHMPEGSI GKEGPSAGTA ILTAFVSLFT KTRVSQDIAM TGEVSLVGQV
LPVGGLKEKI LAAHRAGIKT IIAPAANRAD IEENVPESVK TGIRFVYVET VHEVLKEVFK
GSEIARRWEE TMREGDRAEG EKAAKEEEKE ESK
//
