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LONM_DEBHA
ID   LONM_DEBHA              Reviewed;        1079 AA.
AC   Q6BKJ4;
DT   13-JUL-2010, integrated into UniProtKB/Swiss-Prot.
DT   04-NOV-2008, sequence version 2.
DT   03-AUG-2022, entry version 111.
DE   RecName: Full=Lon protease homolog, mitochondrial {ECO:0000255|HAMAP-Rule:MF_03120};
DE            EC=3.4.21.53 {ECO:0000255|HAMAP-Rule:MF_03120};
DE   Flags: Precursor;
GN   Name=PIM1 {ECO:0000255|HAMAP-Rule:MF_03120};
GN   OrderedLocusNames=DEHA2F21450g;
OS   Debaryomyces hansenii (strain ATCC 36239 / CBS 767 / BCRC 21394 / JCM 1990
OS   / NBRC 0083 / IGC 2968) (Yeast) (Torulaspora hansenii).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Debaryomycetaceae; Debaryomyces.
OX   NCBI_TaxID=284592;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 36239 / CBS 767 / BCRC 21394 / JCM 1990 / NBRC 0083 / IGC 2968;
RX   PubMed=15229592; DOI=10.1038/nature02579;
RA   Dujon B., Sherman D., Fischer G., Durrens P., Casaregola S., Lafontaine I.,
RA   de Montigny J., Marck C., Neuveglise C., Talla E., Goffard N., Frangeul L.,
RA   Aigle M., Anthouard V., Babour A., Barbe V., Barnay S., Blanchin S.,
RA   Beckerich J.-M., Beyne E., Bleykasten C., Boisrame A., Boyer J.,
RA   Cattolico L., Confanioleri F., de Daruvar A., Despons L., Fabre E.,
RA   Fairhead C., Ferry-Dumazet H., Groppi A., Hantraye F., Hennequin C.,
RA   Jauniaux N., Joyet P., Kachouri R., Kerrest A., Koszul R., Lemaire M.,
RA   Lesur I., Ma L., Muller H., Nicaud J.-M., Nikolski M., Oztas S.,
RA   Ozier-Kalogeropoulos O., Pellenz S., Potier S., Richard G.-F.,
RA   Straub M.-L., Suleau A., Swennen D., Tekaia F., Wesolowski-Louvel M.,
RA   Westhof E., Wirth B., Zeniou-Meyer M., Zivanovic Y., Bolotin-Fukuhara M.,
RA   Thierry A., Bouchier C., Caudron B., Scarpelli C., Gaillardin C.,
RA   Weissenbach J., Wincker P., Souciet J.-L.;
RT   "Genome evolution in yeasts.";
RL   Nature 430:35-44(2004).
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:0000255|HAMAP-Rule:MF_03120}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Hydrolysis of proteins in presence of ATP.; EC=3.4.21.53;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_03120};
CC   -!- SUBUNIT: Homohexamer or homoheptamer. Organized in a ring with a
CC       central cavity. {ECO:0000255|HAMAP-Rule:MF_03120}.
CC   -!- SUBCELLULAR LOCATION: Mitochondrion matrix {ECO:0000255|HAMAP-
CC       Rule:MF_03120}.
CC   -!- SIMILARITY: Belongs to the peptidase S16 family. {ECO:0000255|HAMAP-
CC       Rule:MF_03120}.
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DR   EMBL; CR382138; CAG89675.2; -; Genomic_DNA.
DR   RefSeq; XP_461277.2; XM_461277.1.
DR   AlphaFoldDB; Q6BKJ4; -.
DR   SMR; Q6BKJ4; -.
DR   STRING; 4959.XP_461277.2; -.
DR   MEROPS; S16.010; -.
DR   EnsemblFungi; CAG89675; CAG89675; DEHA2F21450g.
DR   GeneID; 2904269; -.
DR   KEGG; dha:DEHA2F21450g; -.
DR   VEuPathDB; FungiDB:DEHA2F21450g; -.
DR   eggNOG; KOG2004; Eukaryota.
DR   HOGENOM; CLU_004109_1_0_1; -.
DR   InParanoid; Q6BKJ4; -.
DR   OMA; AVGWYSE; -.
DR   OrthoDB; 528132at2759; -.
DR   Proteomes; UP000000599; Chromosome F.
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   Gene3D; 2.30.130.40; -; 1.
DR   Gene3D; 3.30.230.10; -; 1.
DR   Gene3D; 3.40.50.300; -; 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_S5_D2-typ_fold.
DR   InterPro; IPR014721; Ribosomal_S5_D2-typ_fold_subgr.
DR   PANTHER; PTHR43718; PTHR43718; 1.
DR   Pfam; PF00004; AAA; 1.
DR   Pfam; PF05362; Lon_C; 1.
DR   Pfam; PF02190; LON_substr_bdg; 1.
DR   SMART; SM00382; AAA; 1.
DR   SMART; SM00464; LON; 1.
DR   SUPFAM; SSF52540; SSF52540; 1.
DR   SUPFAM; SSF54211; SSF54211; 1.
DR   SUPFAM; SSF88697; SSF88697; 1.
DR   TIGRFAMs; TIGR00763; lon; 1.
DR   PROSITE; PS51787; LON_N; 1.
DR   PROSITE; PS51786; LON_PROTEOLYTIC; 1.
PE   3: Inferred from homology;
KW   ATP-binding; DNA-binding; Hydrolase; Mitochondrion; Nucleotide-binding;
KW   Protease; Reference proteome; Serine protease; Transit peptide.
FT   TRANSIT         1..60
FT                   /note="Mitochondrion"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03120"
FT   CHAIN           61..1079
FT                   /note="Lon protease homolog, mitochondrial"
FT                   /id="PRO_0000395778"
FT   DOMAIN          165..389
FT                   /note="Lon N-terminal"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01123"
FT   DOMAIN          865..1053
FT                   /note="Lon proteolytic"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01122"
FT   REGION          61..158
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          262..285
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          756..832
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        61..116
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        117..148
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        262..281
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        769..801
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        802..832
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        959
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03120"
FT   ACT_SITE        1002
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03120"
FT   BINDING         543..550
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03120"
SQ   SEQUENCE   1079 AA;  119970 MW;  FF484893619164F5 CRC64;
     MLRPRTYVRK LAWRCPRKSQ LGLRLATSVS SHKSLPLPMN FDISHSQSAF RAYQDIIHRN
     KSVGDDEPSQ RSENENNPSE SDKDSNQDPE TPKKDKESEN DKEPEKEKDI ENDNKVSSES
     NENVTLASSN TGGAAPPNGN NNGDDPDDSN PSLPVDPVTG LYPPLLAIPM KDRPPLPGRP
     FAINVTDPEV IRSIYTIIDK REPYFVLFHV KDSNEPDTDV INKKDSVYDI GVHCQIIRHT
     TPRPGVFNVL GYPLERCKLE ELTTPSSEKE AKSEEPSKED AESFPTSYLK GLNVSYATVK
     PVEDEPYDKS SAEIRSLVES LKTLLSKMGG KNPLEKLQIK EGTDLISDPS KFADFVGSTI
     HGDPKKIQEI LETLNIETRL SRALELLKVE LKASLIKEST IHNLSTKADE YQTRLFIKEF
     IKELQKRAGI SESEDKKTSK FDERLKHLKL TEEAMEAYNA EKAKMENQNE HSSELGVSER
     YLDWLTSIPW GVYSKDHFNI KQAREVLERD HYGLKDVKDR ILEFISLGKV SGKVDGKILC
     LAGPPGTGKT SIAKSIAESL NRKYVRIAMG GIQDVHEVKG HRRTYVGSIP GRIISALKQA
     KTSNPLMLID EIDKLDLSRG GGAASAFLEI LDPEQNNSFV DNYIDVKVDL SKVLFVCTAN
     YLGNIPAPLR DRMEIIDVSG YTNNEKIEIA KRHLIPEASK KAGLETNHVS ITNETISRLI
     EKYCRESGLR NVKKLITRIF SKASLKIVEE IEAKEALDSS KEKEGVTASS EEANVNSEST
     KSNTSQAEPV AESSTDISTK SKVASEKIET KEKKETNKEN GQSEEDQQPE PKFVIPEDIK
     LEITPANLKD YVGPEIYTRD RVYEFPPPGV ATGLSYSTSG NGDALYIESI LTHSIGSGSG
     VPGMHVTGSL KDVMKESASI AYSFTKSFMA KNYPDNRFFE AADIHVHCPD GAIPKDGPSA
     GISFTSSLVS LAINESLPPT VAMTGEITVT GRVLPVGGLR EKILGAKRYG CDTIIFPKDI
     ENELEEIPDE VKDGVTFIPV EWYQEVFDKI FPNATAQKCN EVWKEEFAKL DSKKKNKKK
 
 
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