| Tag | Content |
|---|
| CPLM ID | CPLM-023351 |
UniProt Accession | |
Genbank Protein ID | |
Genbank Nucleotide ID | |
Protein Name | Presequence protease, mitochondrial |
Protein Synonyms/Alias | |
Gene Name | CG3107 |
Gene Synonyms/Alias | |
Created Date | July 27, 2013 |
Organism | Drosophila melanogaster (Fruit fly) |
NCBI Taxa ID | 7227 |
Lysine Modification | Position | Peptide | Type | References |
|---|
| 558 | VKLLDEVKIEKIYER | acetylation | [1] | | 561 | LDEVKIEKIYERGLI | acetylation | [1] | | 922 | YRDPNSTKTLNAFDE | acetylation | [1] |
|
Reference | [1] Proteome-wide mapping of the Drosophila acetylome demonstrates a high degree of conservation of lysine acetylation. Weinert BT, Wagner SA, Horn H, Henriksen P, Liu WR, Olsen JV, Jensen LJ, Choudhary C. Sci Signal. 2011 Jul 26;4(183):ra48. [ PMID: 21791702] |
Functional Description | ATP-independent protease that degrades mitochondrial transit peptides after their cleavage. Also degrades other unstructured peptides (By similarity). |
Sequence Annotation | ACT_SITE 131 131 Proton acceptor (By similarity).
METAL 128 128 Zinc; catalytic (By similarity).
METAL 132 132 Zinc; catalytic (By similarity).
METAL 229 229 Zinc; catalytic (By similarity). |
Keyword | Complete proteome; Hydrolase; Metal-binding; Metalloprotease; Mitochondrion; Protease; Reference proteome; Transit peptide; Zinc. |
Sequence Source | UniProt (SWISSPROT/TrEMBL); GenBank; EMBL |
Protein Length | 1034 AA |
Protein Sequence | MLKGGMLSRW KMWSPQYKIL RNHLINFKSV STYKNISGVN TKQPKSPRQF GCMPHVTKKR 60
KYKYEEGKTY HGFQCERVEH ISEFELTSYT FRYERTGTEL WHIDRNDSNN VFSINFRTTP 120
FDSTGLPHIL EHLSLCGSQK YPVRDPFFKM LNRSVATFMN AMTGPDYTIY PFSTMNEIDF 180
RNLQHIYLDA VFRPNLAYFD FLQEGWRLEN KDIFDKQSKL VIKGVVYNEM KGAFSENAQV 240
FSQNLLNNIF PDHTYRHVSG GNPLEIPKLA YNDLVEFHKK YYHPSNARIY SYGLFDASKT 300
LALLDEEYLS DQSWVDNSYS LIRQQERWTQ PRLVHISSRL DNMGTTIDRQ NQIAIALLMC 360
DATNIQESFE LHVLSEVLIR GPNSPFYKNL IEPNFSGGYN QTTGYSSDTK DTTFVVGLQD 420
LRVEDFKKCI EIFDKTIINS MNDGFDSQHV ESVLHNLELS LKHQNPNFGN TLLFNSTALW 480
NHDGDVVSNL RVSDMISGLR ESISQNKKYF QEKIEKYFAN NNHRLTLTMS PDEAYEDKFK 540
QAELELVEQK VKLLDEVKIE KIYERGLILD SYQKAESNTD LLPCLTMNDV RDPPKWPKLF 600
IQNVQNVRTQ ICKVPTNEIT YFKCMFNITG LSHEETQLMP LFCNVISAMG TTNYNYREFD 660
KHILLKTGGF DFKLHLIEDV RDSKSYSLSV MINTHALNNN VPEMFALCQE LIKNVRFDDS 720
ERLKMLIENY ISYISVGVAS SGHLYAMLGA TSQVCDAGKL KSLLYGVDHI DFMKNFVHST 780
STVDICDKLS TIASKVFNKD NMRGAINTTQ SYEPSAISNY EKFLESLPTF GKTQTSRNIH 840
YLDPSCQQYV MNIPVNYCAK ALFTVPYLHQ DHPTLRVLAK LLSAKYLLPV IREKNGAYGA 900
GAKISSDGIF SFYSYRDPNS TKTLNAFDET YKWLRANQNV IDQQSLFESK LGVLQQLDTP 960
IAPGNIGIDY FLYEVSQEDF ESYRSRMLSV TIDDLQCAIE NYFGKESMHY GKCILGPVNA 1020
NLELETSHKW IINN 1034 |
Gene Ontology | GO:0005759; C:mitochondrial matrix; ISS:UniProtKB. GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. GO:0004222; F:metalloendopeptidase activity; ISS:UniProtKB. GO:0006508; P:proteolysis; ISS:UniProtKB. |
Interpro | |
Pfam | |
SMART | |
PROSITE | |
PRINTS | |