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Database: UniProt
Entry: B7FSL4
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ID   LONM_PHATC              Reviewed;         882 AA.
AC   B7FSL4;
DT   13-JUL-2010, integrated into UniProtKB/Swiss-Prot.
DT   10-FEB-2009, sequence version 1.
DT   29-OCT-2014, entry version 42.
DE   RecName: Full=Lon protease homolog, mitochondrial {ECO:0000255|HAMAP-Rule:MF_03120};
DE            EC=3.4.21.- {ECO:0000255|HAMAP-Rule:MF_03120};
DE   Flags: Precursor;
GN   ORFNames=PHATRDRAFT_18202;
OS   Phaeodactylum tricornutum (strain CCAP 1055/1).
OC   Eukaryota; Stramenopiles; Bacillariophyta; Bacillariophyceae;
OC   Bacillariophycidae; Naviculales; Phaeodactylaceae; Phaeodactylum.
OX   NCBI_TaxID=556484;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CCAP 1055/1;
RX   PubMed=18923393; DOI=10.1038/nature07410;
RA   Bowler C., Allen A.E., Badger J.H., Grimwood J., Jabbari K., Kuo A.,
RA   Maheswari U., Martens C., Maumus F., Otillar R.P., Rayko E.,
RA   Salamov A., Vandepoele K., Beszteri B., Gruber A., Heijde M.,
RA   Katinka M., Mock T., Valentin K., Verret F., Berges J.A., Brownlee C.,
RA   Cadoret J.P., Chiovitti A., Choi C.J., Coesel S., De Martino A.,
RA   Detter J.C., Durkin C., Falciatore A., Fournet J., Haruta M.,
RA   Huysman M.J., Jenkins B.D., Jiroutova K., Jorgensen R.E., Joubert Y.,
RA   Kaplan A., Kroger N., Kroth P.G., La Roche J., Lindquist E.,
RA   Lommer M., Martin-Jezequel V., Lopez P.J., Lucas S., Mangogna M.,
RA   McGinnis K., Medlin L.K., Montsant A., Oudot-Le Secq M.P., Napoli C.,
RA   Obornik M., Parker M.S., Petit J.L., Porcel B.M., Poulsen N.,
RA   Robison M., Rychlewski L., Rynearson T.A., Schmutz J., Shapiro H.,
RA   Siaut M., Stanley M., Sussman M.R., Taylor A.R., Vardi A.,
RA   von Dassow P., Vyverman W., Willis A., Wyrwicz L.S., Rokhsar D.S.,
RA   Weissenbach J., Armbrust E.V., Green B.R., Van de Peer Y.,
RA   Grigoriev I.V.;
RT   "The Phaeodactylum genome reveals the evolutionary history of diatom
RT   genomes.";
RL   Nature 456:239-244(2008).
RN   [2]
RP   GENOME REANNOTATION.
RC   STRAIN=CCAP 1055/1;
RG   Diatom Consortium;
RA   Grigoriev I., Grimwood J., Kuo A., Otillar R.P., Salamov A.,
RA   Detter J.C., Lindquist E., Shapiro H., Lucas S., Glavina del Rio T.,
RA   Pitluck S., Rokhsar D., Bowler C.;
RL   Submitted (AUG-2008) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: ATP-dependent serine protease that mediates the
CC       selective degradation of misfolded, unassembled or oxidatively
CC       damaged polypeptides as well as certain short-lived regulatory
CC       proteins in the mitochondrial matrix. May also have a chaperone
CC       function in the assembly of inner membrane protein complexes.
CC       Participates in the regulation of mitochondrial gene expression
CC       and in the maintenance of the integrity of the mitochondrial
CC       genome. Binds to mitochondrial DNA in a site-specific manner.
CC       {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.
CC       {ECO:0000255|HAMAP-Rule:MF_03120}.
CC   -!- SIMILARITY: Contains 1 Lon domain. {ECO:0000255|HAMAP-
CC       Rule:MF_03120}.
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DR   EMBL; CM000606; EEC50499.1; -; Genomic_DNA.
DR   RefSeq; XP_002177685.1; XM_002177649.1.
DR   UniGene; Ptc.2084; -.
DR   ProteinModelPortal; B7FSL4; -.
DR   STRING; 2850.JGI18202; -.
DR   MEROPS; S16.002; -.
DR   EnsemblProtists; Phatr18202; Phatr18202; Phatr18202.
DR   GeneID; 7197221; -.
DR   KEGG; pti:PHATRDRAFT_18202; -.
DR   eggNOG; COG0466; -.
DR   HOGENOM; HOG000261409; -.
DR   InParanoid; B7FSL4; -.
DR   KO; K08675; -.
DR   GO; GO:0005759; C:mitochondrial matrix; IEA:UniProtKB-HAMAP.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-HAMAP.
DR   GO; GO:0004176; F:ATP-dependent peptidase activity; IEA:UniProtKB-HAMAP.
DR   GO; GO:0043565; F:sequence-specific DNA binding; IEA:UniProtKB-HAMAP.
DR   GO; GO:0004252; F:serine-type endopeptidase activity; IEA:UniProtKB-HAMAP.
DR   GO; GO:0034599; P:cellular response to oxidative stress; IEA:UniProtKB-HAMAP.
DR   GO; GO:0051131; P:chaperone-mediated protein complex assembly; IEA:UniProtKB-HAMAP.
DR   GO; GO:0006515; P:misfolded or incompletely synthesized protein catabolic process; IEA:UniProtKB-HAMAP.
DR   GO; GO:0070407; P:oxidation-dependent protein catabolic process; IEA:UniProtKB-HAMAP.
DR   GO; GO:0090296; P:regulation of mitochondrial DNA replication; IEA:UniProtKB-HAMAP.
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; IPR027065; Lon_Prtase.
DR   InterPro; IPR027503; Lonm_euk.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR008269; Pept_S16_C.
DR   InterPro; IPR003111; Pept_S16_N.
DR   InterPro; IPR008268; Peptidase_S16_AS.
DR   InterPro; IPR015947; PUA-like_domain.
DR   InterPro; IPR020568; Ribosomal_S5_D2-typ_fold.
DR   InterPro; IPR014721; Ribosomal_S5_D2-typ_fold_subgr.
DR   PANTHER; PTHR10046; PTHR10046; 1.
DR   Pfam; PF00004; AAA; 1.
DR   Pfam; PF02190; LON; 1.
DR   Pfam; PF05362; Lon_C; 1.
DR   PIRSF; PIRSF001174; Lon_proteas; 1.
DR   SMART; SM00382; AAA; 1.
DR   SUPFAM; SSF52540; SSF52540; 1.
DR   SUPFAM; SSF54211; SSF54211; 1.
DR   SUPFAM; SSF88697; SSF88697; 1.
DR   TIGRFAMs; TIGR00763; lon; 1.
DR   PROSITE; PS01046; LON_SER; 1.
PE   3: Inferred from homology;
KW   ATP-binding; Complete proteome; DNA-binding; Hydrolase; Mitochondrion;
KW   Nucleotide-binding; Protease; Reference proteome; Serine protease;
KW   Transit peptide.
FT   TRANSIT       1     34       Mitochondrion. {ECO:0000255|HAMAP-
FT                                Rule:MF_03120}.
FT   CHAIN        35    882       Lon protease homolog, mitochondrial.
FT                                /FTId=PRO_0000395770.
FT   DOMAIN       71    279       Lon. {ECO:0000255|HAMAP-Rule:MF_03120}.
FT   NP_BIND     435    442       ATP. {ECO:0000255|HAMAP-Rule:MF_03120}.
FT   ACT_SITE    784    784       {ECO:0000255|HAMAP-Rule:MF_03120}.
FT   ACT_SITE    827    827       {ECO:0000255|HAMAP-Rule:MF_03120}.
SQ   SEQUENCE   882 AA;  97656 MW;  021DFBDCF0C019F1 CRC64;
     MIHVLKSRST LLTASSIVRT SVGSSSRYSQ TRTYSRTHSW SKDASGGAIS VLPTKLPFGE
     QAPRFPHTLG LPLVSRPLFP GLVTSVTLTD EATIDAMEAL TKNQDQAYVS CFLRKKNPTG
     VSEGGVILAT PEVITDPSDI YHVGTFAQIQ RLTRGDETAA TLILLAHRRL DLEYVDKIGP
     PIDVTVKHWN RSDYTGADDT IRALSNEIIS TIREVAQVNM LFRENLQYFP MRVDANDPFR
     LADFAASISA SGTPEDLQAV LEEKDAEMRL HKALVLLNRE REVSKLQQEI SQKVEERMTE
     AQRKYFLTEQ LKSIKKELGM ERDDKDTLIE KYRKTLSEYP HVPEEAMETI DAELEKFSTL
     EKNSPEYNVT RSYLDWLTSV PWGVETEENF DIQKARKTLD RDHYGLDDVK DTILEFIAIG
     KLRGSVQGKI LCLSGPPGTG KTSIAKSVAD ALGRQFFRFS VGGLSDVSEI KGHRRTYIGA
     MPGKLIQCLK ATGTTNPVVL IDEIDKLGTG FRGDPASALL EVLDPGQNST FRDYFLDVPV
     DISKVLFICT ANELERIPGP LLDRMEVIRL SGYDLPEKVA IAEQYLVPKS MRDSGLLGVP
     ETLKLTIDAV RSLARWYARE AGVRNLAKYI DRITRKLALQ VVAESEGATL TDKSSRKSNT
     WEITEDNLHE YVGKPVFTSD RLYEDGPLPH GIVMGLAYTS MGGSALYIET QSIRRGLDSE
     GKTRGGGTLK VTGQLGDVMK ESTQIASTVA RARLSDIKPE SNFFDINDIH MHVPEGATPK
     DGPSAGVTMV TSMLSLALDR PIRNDLAMTG EVSLTGKVLA VGGIKEKIMG ARRAGIKCVI
     LPAANKRDYD EIPDYLKEDL EVHYADTFDK VYEVAFSSVD ST
//
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