ID A0A0L0T4E5_ALLM3 Unreviewed; 914 AA.
AC A0A0L0T4E5;
DT 11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT 11-NOV-2015, sequence version 1.
DT 27-MAR-2024, entry version 49.
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=AMAG_20018 {ECO:0000313|EMBL:KNE69688.1};
OS Allomyces macrogynus (strain ATCC 38327) (Allomyces javanicus var.
OS macrogynus).
OC Eukaryota; Fungi; Fungi incertae sedis; Blastocladiomycota;
OC Blastocladiomycetes; Blastocladiales; Blastocladiaceae; Allomyces.
OX NCBI_TaxID=578462 {ECO:0000313|EMBL:KNE69688.1, ECO:0000313|Proteomes:UP000054350};
RN [1] {ECO:0000313|EMBL:KNE69688.1, ECO:0000313|Proteomes:UP000054350}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 38327 {ECO:0000313|EMBL:KNE69688.1,
RC ECO:0000313|Proteomes:UP000054350};
RG The Broad Institute Genome Sequencing Platform;
RA Russ C., Cuomo C., Burger G., Gray M.W., Holland P.W.H., King N.,
RA Lang F.B.F., Roger A.J., Ruiz-Trillo I., Young S.K., Zeng Q., Gargeya S.,
RA Fitzgerald M., Haas B., Abouelleil A., Alvarado L., Arachchi H.M.,
RA Berlin A., Chapman S.B., Gearin G., Goldberg J., Griggs A., Gujja S.,
RA Hansen M., Heiman D., Howarth C., Larimer J., Lui A., MacDonald P.J.P.,
RA McCowen C., Montmayeur A., Murphy C., Neiman D., Pearson M., Priest M.,
RA Roberts A., Saif S., Shea T., Sisk P., Stolte C., Sykes S., Wortman J.,
RA Nusbaum C., Birren B.;
RT "Annotation of Allomyces macrogynus ATCC 38327.";
RL Submitted (NOV-2009) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Proteomes:UP000054350}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 38327 {ECO:0000313|Proteomes:UP000054350};
RG The Broad Institute Genome Sequencing Platform;
RA Russ C., Cuomo C., Shea T., Young S.K., Zeng Q., Koehrsen M., Haas B.,
RA Borodovsky M., Guigo R., Alvarado L., Berlin A., Borenstein D., Chen Z.,
RA Engels R., Freedman E., Gellesch M., Goldberg J., Griggs A., Gujja S.,
RA Heiman D., Hepburn T., Howarth C., Jen D., Larson L., Lewis B., Mehta T.,
RA Park D., Pearson M., Roberts A., Saif S., Shenoy N., Sisk P., Stolte C.,
RA Sykes S., Walk T., White J., Yandava C., Burger G., Gray M.W.,
RA Holland P.W.H., King N., Lang F.B.F., Roger A.J., Ruiz-Trillo I.,
RA Lander E., Nusbaum C.;
RT "The Genome Sequence of Allomyces macrogynus strain ATCC 38327.";
RL Submitted (NOV-2009) 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|PIRNR:PIRNR001174, ECO:0000256|PROSITE-
CC ProRule:PRU01122, ECO:0000256|RuleBase:RU000591}.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|HAMAP-Rule:MF_03120}.
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DR EMBL; GG745361; KNE69688.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0L0T4E5; -.
DR STRING; 578462.A0A0L0T4E5; -.
DR EnsemblFungi; KNE69688; KNE69688; AMAG_20018.
DR VEuPathDB; FungiDB:AMAG_20018; -.
DR eggNOG; KOG2004; Eukaryota.
DR OMA; VLDCVPM; -.
DR OrthoDB; 1103874at2759; -.
DR Proteomes; UP000054350; 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; IPR008268; Peptidase_S16_AS.
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 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.
DR PROSITE; PS01046; LON_SER; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PIRNR:PIRNR001174};
KW DNA-binding {ECO:0000256|HAMAP-Rule:MF_03120};
KW Hydrolase {ECO:0000256|HAMAP-Rule:MF_03120, ECO:0000256|PIRNR:PIRNR001174};
KW Mitochondrion {ECO:0000256|ARBA:ARBA00023128, ECO:0000256|HAMAP-
KW Rule:MF_03120};
KW Nucleotide-binding {ECO:0000256|PIRNR:PIRNR001174,
KW ECO:0000256|PIRSR:PIRSR001174-2};
KW Protease {ECO:0000256|ARBA:ARBA00022670, ECO:0000256|HAMAP-Rule:MF_03120};
KW Reference proteome {ECO:0000313|Proteomes:UP000054350};
KW Serine protease {ECO:0000256|ARBA:ARBA00022825, ECO:0000256|HAMAP-
KW Rule:MF_03120}.
FT DOMAIN 22..292
FT /note="Lon N-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51787"
FT DOMAIN 685..872
FT /note="Lon proteolytic"
FT /evidence="ECO:0000259|PROSITE:PS51786"
FT REGION 124..185
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 738..780
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 126..153
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 763..777
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 778
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03120,
FT ECO:0000256|PIRSR:PIRSR001174-1"
FT ACT_SITE 821
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03120,
FT ECO:0000256|PIRSR:PIRSR001174-1"
FT BINDING 447..454
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PIRSR:PIRSR001174-2"
SQ SEQUENCE 914 AA; 99018 MW; 84BD12726D749E88 CRC64;
MATRATRAIC RRLPRQTRTR RCFALPITRR PLFPGFYKTV VIKDPEVIRA IKDLAESRQP
YVAAVLLKDE EADTDRIQSL DEIHQVGVFS QITNVYHTSP TGPGDDAPSL TAILYPHRRV
RISGLVNDSD SPSTTAAATT AAPVSTTESD AVTKPATAPD AAVAADADKP ETASEPTGSP
QSYLRSKYNV SVVHAETLHD EPYKKGNQLV RAITAEIVNV FKDIASLNPL FREQISAFSV
SQASTTIFDD PSKLADFAAA VSGGSDSEEL QGVLESLVIE ERLQKALYVL KKELVNAQLQ
SKISKEVESK IQKRQREYYL MEQLKGIKKE LGMESDGKDK LLEKFKERIQ YATLPATVAT
VIEEEMQKLG HLDPASSEFN VTRNYLDWLT CLPWGKYSQE VLDVEHAQQC LDEDHYGLKD
VKERILEFIA VGKLKGTVEG KIMCLSGPPV VGKTSIGKSI ARALGREFYR FSVGGLSDVA
EIKGHRRTYV GAMPGKLVQA LKKVQTENPL VLIDEIDKLG RGLQGDPASA LLELLDPEQN
SSFLDHYLDV PLDLSKVLFV CTANVLDTIP GPLLDRMEVI QLSGYVADEK VAIAEKYLAP
QARIASDTKC SMQQQLDRAI EDLIRYYCRE SGVRNLKKHI EKIYRKAAFK VVSAGANAEP
LQITPANLKD YVGNPPFSGE RLFEHPPAGV VMGLAWTAMG GSSLYIESVL EAPLTTESKP
ALTKTGQLGD VMKESSMLPV NGSRAEGAGQ CASDRPETVP KSTHTESPPP PAPPDGPSAG
ITMATSLISL AANTPIPPHI AMTGELTLSG KVLKIGGLKE KTIAAKRSGI TTILFPAANT
ADWAELPDFV KDGIEGRPVE WYSEVFDACF GEAVARGEFA KNAWPIVSAA TATAVLADMP
GTAAGSPPAS IGGA
//
