SPM_005900
  | Uniprot: A0A037UNX1
Description: Lon protease EC number: 3.4.21.53 Annotation score: 3 out of 5 Miscellaneous [CC]: Protein existence: Evidence at transcript level Catalytic activity: CATALYTIC ACTIVITY: Hydrolysis of proteins in presence of ATP. {ECO:0000256|HAMAP-Rule:MF_01973, ECO:0000256|PIRNR:PIRNR001174, ECO:0000256|SAAS:SAAS00004348}. Cofactor: Enzyme regulation: Function [CC]: FUNCTION: ATP-dependent serine protease that mediates the selective degradation of mutant and abnormal proteins as well as certain short-lived regulatory proteins. Required for cellular homeostasis and for survival from DNA damage and developmental changes induced by stress. Degrades polypeptides processively to yield small peptide fragments that are 5 to 10 amino acids long. Binds to DNA in a double-stranded, site-specific manner. {ECO:0000256|HAMAP-Rule:MF_01973, ECO:0000256|SAAS:SAAS00338846}. Pathway: Active site: ACT_SITE 677 677 {ECO:0000256|HAMAP-Rule:MF_01973, ECO:0000256|PIRSR:PIRSR001174-1}.; ACT_SITE 720 720 {ECO:0000256|HAMAP-Rule:MF_01973, ECO:0000256|PIRSR:PIRSR001174-1}. Binding site: Calcium binding: DNA binding: Metal binding: Nucleotide binding: NP_BIND 354 361 ATP. {ECO:0000256|HAMAP-Rule:MF_01973, ECO:0000256|PIRSR:PIRSR001174-2}. Site: Gene names (primary): lon Gene names (synonym): Mass: 87,217 Subunit structure [CC]: SUBUNIT: Homohexamer. Organized in a ring with a central cavity. {ECO:0000256|HAMAP-Rule:MF_01973, ECO:0000256|PIRNR:PIRNR001174, ECO:0000256|SAAS:SAAS00536021}. Gene ontology (GO): cytoplasm [GO:0005737]; ATP binding [GO:0005524]; ATP-dependent peptidase activity [GO:0004176]; sequence-specific DNA binding [GO:0043565]; serine-type endopeptidase activity [GO:0004252]; cellular response to stress [GO:0033554]; misfolded or incompletely synthesized protein catabolic process [GO:0006515] Gene ontology IDs: GO:0004176; GO:0004252; GO:0005524; GO:0005737; GO:0006515; GO:0033554; GO:0043565 Chain: Signal peptide: Domain [CC]: Sequence similarities: SIMILARITY: Belongs to the peptidase S16 family. {ECO:0000256|HAMAP-Rule:MF_01973, ECO:0000256|RuleBase:RU000591, ECO:0000256|SAAS:SAAS00536024}.; SIMILARITY: Contains 1 Lon N-terminal domain. {ECO:0000256|HAMAP-Rule:MF_01973}.; SIMILARITY: Contains 1 Lon proteolytic domain. {ECO:0000256|HAMAP-Rule:MF_01973}. Protein families: Peptidase S16 family Coiled coil: Domain [FT]: DOMAIN 10 200 LON. {ECO:0000259|SMART:SM00464}.; DOMAIN 346 491 AAA. {ECO:0000259|SMART:SM00382}. Motif: Region: EMBL: AGBZ02000004 ProteinModelPortal: MEROPS: S16.001 EnsemblBacteria KO: KAI92256 UniPathway: CDD: Gene3D: HAMAP: 3.30.230.10;3.40.50.300 InterPro: MF_01973 PANTHER: IPR003593;IPR003959;IPR027543;IPR004815;IPR027065;IPR003111;IPR027417;IPR008269;IPR008268;IPR015947;IPR020568;IPR014721 PIRSF: PTHR10046 PRINTS: PIRSF001174 PROSITE: Pfam: PS01046 ProDom: PF00004;PF05362;PF02190 SMART: SUPFAM: SM00382;SM00464 TIGRFAMs: SSF52540;SSF54211;SSF88697 |
240625-242944(+) >nucleotide sequence ATTTTTCCAGGCTTTGAACAAGTATTAGAGGTAGGACGAGATAAATCAATTTTAGCGGTA AATACAGCTAGCAAGGATTTTGATAATCATATTGTTTTAGTTAGTCAAAAAAAACCGTTA GAAGATAATCCAAAGTTATCTGAAATTTATCGAATTGGGATTTTAGCAGAGTTAAAAATT CGTAAAGTGTGGGAAGATGGTAGTTTAACAGTTAATTTTAAAGCAGTTGATCGGGTAAAA ATTTTAGATTTACGCGAAGGAGAATTTTATGCTGCTGATATTGATATTTTGAAGTCATTT GTTAAATCAGAAGATAAAATTGTTGAAAAATTAACAGCTAATATTAAAGAATTAATGGAA TTACAGGATATTTTGCCAGAAGATTTATTAGATCAAATTGGTGATTCAGTTGATGGGAAT GAAGTTGTTGATACAATTGCCCAATTTTTACCATTTATTCCAGTGGCGAAAAAACAAGAA ATTATTGAGGAATTAGATGTTGAAAAAAGGCTTCAAATTATTTTTGATCATTTAGTTAAT AAACAACAAGCAAATGATATTGATAATAAAATTAGCAAAAAAATTAAAGAACGAGTTGAT GAACAACAACGTGAATATTACTTACGGGAAAAATTAAAAGCAATTAAAGATGAATTAGAT GAATTTGATGGTGCAGCTGATGAAATGAAATTATATAAAGAACGATTAGCAAATGAACCA TTTCCAAAAAATATTAAAGAACGAATTGAACAAGAAATCACTCGTTATGAAGCATTGCCA CAAGCATCAAGTGAATCAAATATTATTCGAACTTATATTGATTGAATGATGCAAATTCCA TGACATGAAAAAACAGAAGAAAAAAATGATTTAAAATTTGCAAAAGAAGTGTTAGATAAA TATCATTTTGGTTTAGATAAAGTTAAAGAAAGAATTATTGAATACTTAGCTGTTAAAACA ATGACTAAATCTTTAAAAGGACAAATTATTTGTTTAGTAGGGCCACCAGGGGTTGGGAAA ACAAGTTTAGCAAAATCAATCGCTGAAGCAACAGGGCGAAAATTTGTTAAAATGGCCTTG GGAGGCGTAAAAGATGAGTCAGAAATTCGTGGACATCGTAAAACATATATTGGAGCAATG CCGGGGCGTATTATTCAGTCAATGAAACGTGCTGGTTCAATAAATCCATTATTCTTATTA GATGAAATTGACAAAATGGCCTCAGATTATCGTGGTGATCCTGCTAGTGCGATGTTAGAA GTATTAGATCCAGAACAAAATTCAACATTTTCTGACCACTACTTAGAAGAAACATATGAT TTAAGTGATGTTATGTTTATTGCAACAGCCAACTACTATGATAATATTCCAGAAGCTTTA ATTGATCGAATGGAAATTATTCAATTATCATCATATACTGAGTTGGAGAAATTCCATATT GCAAAAGATTATTTAGTGCCAAAAGTATTAAGTAATAATGGTTTAGCAGATGGACAATTA ACAATTACTGATGATGCAATTAATGAAATAATTAAATATTATACGCGTGAAGCAGGAGTT CGTCAGTTAGAACGAGATTTAAATGCCGTTGCACGGAAATTTATTTTTAAGTTCTTAAAT AAAGAAATGGTTAATTTAACAGTTAAACCAAACACTGTTAATGAACTATTAGGCAAACGT CGTTTTGAACATACTGAAAAAGAAAAAGAATCACAAGTTGGAGTTGTAACAGGGTTAGCA TATACTCAATTTGGTGGTGATATTTTACCAATTGAAGTTAATAGTTTCTTAGGAAAAGGT TCATTAGTGTTAACTGGAAAATTAGGTGACATAATGAAAGAATCAGCATCAATTGCATTA GACTATGTAAAAGCAAATTCTGGTAAATTTAACATTGATCCAAAATTCTTTGAAACACAT GATATTCATATTCATGTTCCAGAAGGAGCAGTTCCAAAAGACGGTCCATCAGCTGGAATT ACCTTAACAACAGCAATTATTAGTGCTTTAAGTAATCGTCCGGTATCAAAAGATATTGGA ATGACTGGTGAAATTACTTTGCGAGGACAAGTTTTACCAATTGGTGGGTTACGAGAAAAA TCAATTTCAGCCAACCGTAGTGGTTTAAAAACAATTTTAATTCCACATAAAAATATTAAA GATATTGAAGATATTCCAAAAGAAGTGCAAGAAACATTGAATATTATTCCAGTTGGAACA TATGATGAAGTTTTCAAAAATGTTTTTGGCACAAACTAG >protein sequence EDNPKLSEIYRIGILAELKIRKVWEDGSLTVNFKAVDRVKILDLREGEFYAADIDILKSF VKSEDKIVEKLTANIKELMELQDILPEDLLDQIGDSVDGNEVVDTIAQFLPFIPVAKKQE IIEELDVEKRLQIIFDHLVNKQQANDIDNKISKKIKERVDEQQREYYLREKLKAIKDELD EFDGAADEMKLYKERLANEPFPKNIKERIEQEITRYEALPQASSESNIIRTYIDWMMQIP WHEKTEEKNDLKFAKEVLDKYHFGLDKVKERIIEYLAVKTMTKSLKGQIICLVGPPGVGK TSLAKSIAEATGRKFVKMALGGVKDESEIRGHRKTYIGAMPGRIIQSMKRAGSINPLFLL DEIDKMASDYRGDPASAMLEVLDPEQNSTFSDHYLEETYDLSDVMFIATANYYDNIPEAL IDRMEIIQLSSYTELEKFHIAKDYLVPKVLSNNGLADGQLTITDDAINEIIKYYTREAGV RQLERDLNAVARKFIFKFLNKEMVNLTVKPNTVNELLGKRRFEHTEKEKESQVGVVTGLA YTQFGGDILPIEVNSFLGKGSLVLTGKLGDIMKESASIALDYVKANSGKFNIDPKFFETH DIHIHVPEGAVPKDGPSAGITLTTAIISALSNRPVSKDIGMTGEITLRGQVLPIGGLREK SISANRSGLKTILIPHKNIKDIEDIPKEVQETLNIIPVGTYDEVFKNVFGTN |
© Fisunov Lab of Proteomics, 2016.