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 01-MAY-2013, entry version 33.
DE RecName: Full=Lon protease homolog, mitochondrial;
DE EC=3.4.21.-;
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 (By
CC similarity).
CC -!- SUBUNIT: Homohexamer or homoheptamer. Organized in a ring with a
CC central cavity (By similarity).
CC -!- SUBCELLULAR LOCATION: Mitochondrion matrix (By similarity).
CC -!- SIMILARITY: Belongs to the peptidase S16 family.
CC -!- SIMILARITY: Contains 1 Lon domain.
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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 KO; K08675; -.
DR ProtClustDB; CLSN2709172; -.
DR GO; GO:0005759; C:mitochondrial matrix; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004176; F:ATP-dependent peptidase activity; IEA:InterPro.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0004252; F:serine-type endopeptidase activity; IEA:InterPro.
DR GO; GO:0006515; P:misfolded or incompletely synthesized protein catabolic process; IEA:InterPro.
DR Gene3D; 3.30.230.10; -; 1.
DR HAMAP; MF_03120; lonm_euk; 1; -.
DR InterPro; IPR003593; AAA+_ATPase.
DR InterPro; IPR003959; ATPase_AAA_core.
DR InterPro; IPR027065; Lon_Prtase.
DR InterPro; IPR008269; Pept_S16_C.
DR InterPro; IPR004815; Pept_S16_lon.
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; SSF88697; PUA-like; 1.
DR SUPFAM; SSF54211; Ribosomal_S5_D2-typ_fold; 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 (Potential).
FT CHAIN 35 882 Lon protease homolog, mitochondrial.
FT /FTId=PRO_0000395770.
FT DOMAIN 71 279 Lon.
FT NP_BIND 435 442 ATP (By similarity).
FT ACT_SITE 784 784 By similarity.
FT ACT_SITE 827 827 By similarity.
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
//
