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Database: UniProt
Entry: A0A016S5X5_9BILA
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ID   A0A016S5X5_9BILA        Unreviewed;       933 AA.
AC   A0A016S5X5;
DT   11-JUN-2014, integrated into UniProtKB/TrEMBL.
DT   11-JUN-2014, sequence version 1.
DT   24-JAN-2024, entry version 56.
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=Acey_s0289.g1510 {ECO:0000313|EMBL:EYB85886.1};
GN   Synonyms=Acey-C34B2.6 {ECO:0000313|EMBL:EYB85886.1};
GN   ORFNames=Y032_0289g1510 {ECO:0000313|EMBL:EYB85886.1};
OS   Ancylostoma ceylanicum.
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Strongylida;
OC   Ancylostomatoidea; Ancylostomatidae; Ancylostomatinae; Ancylostoma.
OX   NCBI_TaxID=53326 {ECO:0000313|EMBL:EYB85886.1, ECO:0000313|Proteomes:UP000024635};
RN   [1] {ECO:0000313|Proteomes:UP000024635}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=HY135 {ECO:0000313|Proteomes:UP000024635};
RX   PubMed=25730766; DOI=10.1038/ng.3237;
RA   Schwarz E.M., Hu Y., Antoshechkin I., Miller M.M., Sternberg P.W.,
RA   Aroian R.V.;
RT   "The genome and transcriptome of the zoonotic hookworm Ancylostoma
RT   ceylanicum identify infection-specific gene families.";
RL   Nat. Genet. 47:416-422(2015).
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: 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:EYB85886.1}.
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DR   EMBL; JARK01001625; EYB85886.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A016S5X5; -.
DR   STRING; 53326.A0A016S5X5; -.
DR   Proteomes; UP000024635; 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|HAMAP-
KW   Rule:MF_03120}; 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|HAMAP-Rule:MF_03120,
KW   ECO:0000256|PIRNR:PIRNR001174};
KW   Protease {ECO:0000256|ARBA:ARBA00022670, ECO:0000256|HAMAP-Rule:MF_03120};
KW   Reference proteome {ECO:0000313|Proteomes:UP000024635};
KW   Serine protease {ECO:0000256|ARBA:ARBA00022825, ECO:0000256|HAMAP-
KW   Rule:MF_03120}.
FT   DOMAIN          114..349
FT                   /note="Lon N-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS51787"
FT   DOMAIN          746..933
FT                   /note="Lon proteolytic"
FT                   /evidence="ECO:0000259|PROSITE:PS51786"
FT   REGION          216..248
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        840
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_03120,
FT                   ECO:0000256|PIRSR:PIRSR001174-1"
FT   ACT_SITE        883
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_03120,
FT                   ECO:0000256|PIRSR:PIRSR001174-1"
FT   BINDING         504..511
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_03120,
FT                   ECO:0000256|PIRSR:PIRSR001174-2"
SQ   SEQUENCE   933 AA;  104139 MW;  4AEF31F551B26650 CRC64;
     MNIISCICCF QVIVNSDRIR GMLRWGAAGL RCAVRVPLFR ATSLAVRPAL RVSRFSPSAF
     RVTGARLFSS SSNGDGEKPA PTEDDAASME TAIVEGTDIS GMSTINVPDV FPIVPLLAIN
     RYPLFPGFIK KVDIVKDDAL KQVIRNRIAL KQPYVGVFVK QDDENKEEIV TSLSQVFNVG
     CFAQIIEMRD HGKVMELVLS AHRRIRILET VDEGAAEEPH KTLNGRRAGL RKKGAAAQKP
     PTPPPERSSI LLVRTENVIA EPAERNNETK AKMQAVVQTI RDVVQYSALF GQQINLLLHP
     SQNVIENPVY LCDLVATLVQ SADTKELQEM MEEINVSRRL DKALVLIQKE KTVAKLKYDI
     NKDVEKKVQD QHRKYLLNEQ LKVIKKELGL EKDDKSAIIE KMEERLKELK VPEYAMKVIK
     EEQQKLQFLD PHSSEFSVTR NYLDWLTNVP WGVTSEENYD LQKARIALDQ GHYGMKDVKD
     RILEFIAVNM LKKHVGGKIL CLHGPPGTGK TSIARSIAEA LNRQYFRFSV GGMTDVAEIK
     GHRRTYVGAM PGKMIQCLKK VRTENPLVLI DEVDKIGSAG YHGDPASALL ELLDPEQNAN
     FNDHFLDVPV DLSRVLFLCT ANVVDQIPGP LKDRMELIDV SGYLAEEKIE IAQRYLIPQA
     RKETSLTEEQ LMIDNEAVEN IIKHYCRESG VRNLQKHIDR VFRKAALQIA DRPSDGSAQA
     TIVVNNENLE KYVGRPKFTS DRMYDKTPPG VIMGLAWTAM GGSALYIEAV LKKPVDLGSD
     KDGSLETTGN LGDVMKESVR AAFTVAKGVL AKDEPDNKFF EKAHIHIHVP EGATPKDGPS
     AGVTLVSSLL SLALDKPVTQ DMAMTGEISL TGKVLPVGGI KEKVIAARRV GAKRVFLPAE
     NRRDYDDLPE FMKQDLDVRF VSEYAELYQD LFE
//
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