ID K2S3Z8_MACPH Unreviewed; 1039 AA.
AC K2S3Z8;
DT 28-NOV-2012, integrated into UniProtKB/TrEMBL.
DT 28-NOV-2012, sequence version 1.
DT 24-JAN-2024, entry version 65.
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=MPH_05539 {ECO:0000313|EMBL:EKG17249.1};
OS Macrophomina phaseolina (strain MS6) (Charcoal rot fungus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Dothideomycetes incertae sedis; Botryosphaeriales; Botryosphaeriaceae;
OC Macrophomina.
OX NCBI_TaxID=1126212 {ECO:0000313|EMBL:EKG17249.1, ECO:0000313|Proteomes:UP000007129};
RN [1] {ECO:0000313|EMBL:EKG17249.1, ECO:0000313|Proteomes:UP000007129}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MS6 {ECO:0000313|EMBL:EKG17249.1,
RC ECO:0000313|Proteomes:UP000007129};
RX PubMed=22992219; DOI=10.1186/1471-2164-13-493;
RA Islam M.S., Haque M.S., Islam M.M., Emdad E.M., Halim A., Hossen Q.M.M.,
RA Hossain M.Z., Ahmed B., Rahim S., Rahman M.S., Alam M.M., Hou S., Wan X.,
RA Saito J.A., Alam M.;
RT "Tools to kill: Genome of one of the most destructive plant pathogenic
RT fungi Macrophomina phaseolina.";
RL BMC Genomics 13:493-493(2012).
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,
CC ECO:0000256|RuleBase:RU000591}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:EKG17249.1}.
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DR EMBL; AHHD01000251; EKG17249.1; -; Genomic_DNA.
DR AlphaFoldDB; K2S3Z8; -.
DR STRING; 1126212.K2S3Z8; -.
DR VEuPathDB; FungiDB:MPH_05539; -.
DR eggNOG; KOG2004; Eukaryota.
DR HOGENOM; CLU_004109_1_0_1; -.
DR InParanoid; K2S3Z8; -.
DR OrthoDB; 1103874at2759; -.
DR Proteomes; UP000007129; 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 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|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};
KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_03120,
KW ECO:0000256|RuleBase:RU000591};
KW Protease {ECO:0000256|ARBA:ARBA00022670, ECO:0000256|HAMAP-Rule:MF_03120};
KW Reference proteome {ECO:0000313|Proteomes:UP000007129};
KW Serine protease {ECO:0000256|ARBA:ARBA00022825, ECO:0000256|HAMAP-
KW Rule:MF_03120}.
FT DOMAIN 165..433
FT /note="Lon N-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51787"
FT DOMAIN 876..1039
FT /note="Lon proteolytic"
FT /evidence="ECO:0000259|PROSITE:PS51786"
FT REGION 16..158
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 266..302
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 808..840
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 16..40
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 65..107
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 808..837
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 968
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03120,
FT ECO:0000256|PROSITE-ProRule:PRU01122"
FT ACT_SITE 1011
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03120,
FT ECO:0000256|PROSITE-ProRule:PRU01122"
FT BINDING 588..595
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03120"
SQ SEQUENCE 1039 AA; 114082 MW; 47F7B69A6225E231 CRC64;
MLYGQNLPWR AALRQASRQP SSLARISPST LPTASRSYHA AVTRCSPLAA RNRPIASLSS
RHFATTPARR KEKPPSSDSE DKSEQKQEED KKDNQGKLTE AETGADAKSK TPDPIPSSKD
GQGAAAGAGG QGGEAPPAGG EGGGRKRKSE RSLQKPSVPE VYPQVMAIPI GKRPLFPGFY
KAITIRNQAV AAAIHDMVQR GQPYIGAFLL KDDEADKDVI ESPDEVHEVG TFCQITSAFP
VQGEEPSMTA VLYPHRRIKM TSLIPPNRAA GETAAKAETT PVEGTEAEQP AKDQSTQDKK
GDVVASFEEG TLDQAKQVGQ YEPTSFLKKY EVSLVNVENL TEEPFDKKNQ NIRALVGEMV
NTFKEVAAIN SLFRDQISTF SMSQGAGNVG DDPAKLADFA AAVAQGESHE LQAALASMNI
EDRLHKALLV LKKEYMNAKL QDKILKDVEK KISKKQREYW LMEQMRGIRR ELGLETDGKD
KLVEKFKEKA SKLAMPEAVK KVFDEEVNKL AHLEPAASEF NVTRNYLDWL TQIPWGQRSA
ENFGIQNAMK VLDEDHHGLK DVKDRILEFI AVGKLRGTVE GKILCMVGPP GVGKTSIGKS
IARALNRQYY RFSVGGLTDV AEIKGHRRTY VGALPGRIIQ ALKKCQTENP LVLIDEVDKI
GRGHQGDPSS ALLELLDPEQ NSSFLDHYMD VPVDLSKVLF VCTANMTDTI PRPLLDRMEM
IELSGYVADE KMAIAERYLA PAAKELSGLK DVDVQLEKEA IAELINKYCR ESGVRNLKKQ
IEKVYRKSAL KIIQDLGEDV LSEDKALTEE GKQAQEEASK DNTDVKDTPE NIEAETTEKP
RVALQVPESV HVRITPENLK DYVGPPIFTA DRLYDTTPPG VAMGLAWTQM GGAALYVESI
LENALSAASR PGFERTGNLK NVMKESTVIA YSFAKSVMAR SFPENRFFEH AKIHMHCPEG
AVQKDGPSAG ITMATSLLSL ALDHPLDPTI AMTGELTVTG KVLRIGGLRE KTVAARRAGA
KTIIFPEDNL SDWLELPEV
//
