ID I1NEZ7_SOYBN Unreviewed; 983 AA.
AC I1NEZ7;
DT 13-JUN-2012, integrated into UniProtKB/TrEMBL.
DT 09-JAN-2013, sequence version 2.
DT 27-MAR-2024, entry version 81.
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=100810927 {ECO:0000313|EnsemblPlants:KRG90539};
GN ORFNames=GLYMA_20G097700 {ECO:0000313|EMBL:KRG90539.1};
OS Glycine max (Soybean) (Glycine hispida).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; fabids; Fabales; Fabaceae; Papilionoideae; 50 kb inversion clade;
OC NPAAA clade; indigoferoid/millettioid clade; Phaseoleae; Glycine;
OC Glycine subgen. Soja.
OX NCBI_TaxID=3847 {ECO:0000313|EnsemblPlants:KRG90539};
RN [1] {ECO:0000313|EMBL:KRG90539.1, ECO:0000313|EnsemblPlants:KRG90539}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Williams 82 {ECO:0000313|EnsemblPlants:KRG90539};
RC TISSUE=Callus {ECO:0000313|EMBL:KRG90539.1};
RX PubMed=20075913; DOI=10.1038/nature08670;
RA Schmutz J., Cannon S.B., Schlueter J., Ma J., Mitros T., Nelson W.,
RA Hyten D.L., Song Q., Thelen J.J., Cheng J., Xu D., Hellsten U., May G.D.,
RA Yu Y., Sakurai T., Umezawa T., Bhattacharyya M.K., Sandhu D.,
RA Valliyodan B., Lindquist E., Peto M., Grant D., Shu S., Goodstein D.,
RA Barry K., Futrell-Griggs M., Abernathy B., Du J., Tian Z., Zhu L., Gill N.,
RA Joshi T., Libault M., Sethuraman A., Zhang X.-C., Shinozaki K.,
RA Nguyen H.T., Wing R.A., Cregan P., Specht J., Grimwood J., Rokhsar D.,
RA Stacey G., Shoemaker R.C., Jackson S.A.;
RT "Genome sequence of the palaeopolyploid soybean.";
RL Nature 463:178-183(2010).
RN [2] {ECO:0000313|EnsemblPlants:KRG90539}
RP IDENTIFICATION.
RC STRAIN=Williams 82 {ECO:0000313|EnsemblPlants:KRG90539};
RG EnsemblPlants;
RL Submitted (FEB-2018) to UniProtKB.
RN [3] {ECO:0000313|EMBL:KRG90539.1}
RP NUCLEOTIDE SEQUENCE.
RC TISSUE=Callus {ECO:0000313|EMBL:KRG90539.1};
RA Schmutz J., Cannon S., Schlueter J., Ma J., Mitros T., Nelson W., Hyten D.,
RA Song Q., Thelen J., Cheng J., Xu D., Hellsten U., May G., Yu Y.,
RA Sakurai T., Umezawa T., Bhattacharyya M., Sandhu D., Valliyodan B.,
RA Lindquist E., Peto M., Grant D., Shu S., Goodstein D., Barry K.,
RA Futrell-Griggs M., Abernathy B., Du J., Tian Z., Zhu L., Gill N., Joshi T.,
RA Libault M., Sethuraman A., Zhang X., Shinozaki K., Nguyen H., Wing R.,
RA Cregan P., Specht J., Grimwood J., Rokhsar D., Stacey G., Shoemaker R.,
RA Jackson S.;
RT "WGS assembly of Glycine max.";
RL Submitted (JUL-2018) 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,
CC ECO:0000256|RuleBase:RU000591}.
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DR EMBL; CM000853; KRG90539.1; -; Genomic_DNA.
DR RefSeq; XP_003555805.2; XM_003555757.3.
DR AlphaFoldDB; I1NEZ7; -.
DR SMR; I1NEZ7; -.
DR STRING; 3847.I1NEZ7; -.
DR PaxDb; 3847-GLYMA20G23010-1; -.
DR EnsemblPlants; KRG90539; KRG90539; GLYMA_20G097700.
DR GeneID; 100810927; -.
DR Gramene; KRG90539; KRG90539; GLYMA_20G097700.
DR KEGG; gmx:100810927; -.
DR eggNOG; KOG2004; Eukaryota.
DR HOGENOM; CLU_004109_1_0_1; -.
DR InParanoid; I1NEZ7; -.
DR OMA; GRYKITH; -.
DR OrthoDB; 1103874at2759; -.
DR Proteomes; UP000008827; Chromosome 20.
DR GO; GO:0005759; C:mitochondrial 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; IBA:GO_Central.
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:0003697; F:single-stranded DNA binding; IBA:GO_Central.
DR GO; GO:0034599; P:cellular response to oxidative stress; IEA:UniProtKB-UniRule.
DR GO; GO:0051131; P:chaperone-mediated protein complex assembly; IBA:GO_Central.
DR GO; GO:0007005; P:mitochondrion organization; IBA:GO_Central.
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; IBA:GO_Central.
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:UP000008827};
KW Serine protease {ECO:0000256|ARBA:ARBA00022825, ECO:0000256|HAMAP-
KW Rule:MF_03120}.
FT DOMAIN 106..315
FT /note="Lon N-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51787"
FT DOMAIN 786..970
FT /note="Lon proteolytic"
FT /evidence="ECO:0000259|PROSITE:PS51786"
FT REGION 694..738
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 696..711
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 712..733
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 876
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03120,
FT ECO:0000256|PROSITE-ProRule:PRU01122"
FT ACT_SITE 919
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03120,
FT ECO:0000256|PROSITE-ProRule:PRU01122"
FT BINDING 472..479
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03120"
SQ SEQUENCE 983 AA; 109175 MW; 336542BA6340018E CRC64;
MNQPSILKIP LPMLKLIASS SRIHRVHPTV LRPAHDSASP LLRVLSSLVG LSWRNTNVGG
RYFFCSGSSD SSDRVVDAGV QAADESESKA SAIVPTYPRP EDYLTVLALP LIHRPLFPGF
YMPVFVKDPK LLAALQESRE RQAPYAGAFL LKDEPEADPS AVSSSDTDKN VYDLKGKELF
NRLHEVGTLA QISSIHGDQV ILIGHRRLRI TEMVSEDPLT VKVDHLKDKT YNKDDDIIKA
TSFEVISTLR DVLKTSSLWR DHVQTYTKHI GDFTYPRLAD FGAAISGANK LQCQQVLEEL
DVYKRLKLTL ELVKKEMEIS KIQESIAKAI EEKISGEQRR YLLNEQLKAI KKELGLETDD
KTALTGKFRE RIEPKREKCP PHILQVIDEE LAKLQLLEAS SSEFSVTRNY LDWLTALPWG
EYSDENFDVT RAQKILDEDH YGLTDVKERI LEFIAVGKLR GTSQGKIICL SGPPGVGKTS
IGRSIARALN RKFFRFSVGG LADVAEIKGH RRTYIGAMPG KMVQCLKNVG TANPLVLIDE
IDKLGRGHAG DPASALLELL DPEQNANFLD HYLDVTIDLS KVLFVCTANV VEMIPNPLLD
RMEVVAIAGY ITDEKMHIAR DYLEKTTREA CGIKPKQVEV TDAAILALIE NYCREAGVRN
LQKHIEKIYR KIALQLVRQG EMIDATVEPI KENIDSDEFG QNTVQNKNSE LVEGSDPEKE
GETSDKVDKV QTDLSSDESQ CLEVAKESEE DKEIKTKTIE KVLVDESNLT DFVGKPVFHA
ERIYDQTPVG VVMGLAWTAM GGSTLYIETT LVEEGEGKGT LHPTGQLGDV MKESAQIAHT
VARAILLEKE PENPFFANSK LHLHVPAGAT PKDGPSAGCT MTTSLLSLAM KKPVKKDLAM
TGEVTLTGKI LPIGGVKEKT IAARRSEVKT IIFPSANRRD FDELAPNVKE GLDVHFVDDY
MQIFNLALGD DQSQNIERVI NVL
//
