| Tag | Content |
|---|
| CPLM ID | CPLM-006248 |
UniProt Accession | |
Genbank Protein ID | |
Genbank Nucleotide ID | |
Protein Name | Mitochondrial presequence protease |
Protein Synonyms/Alias | Cytosolic metalloprotease 1; Metalloprotease of 112 kDa |
Gene Name | CYM1 |
Gene Synonyms/Alias | MOP112; YDR430C; D9461.18 |
Created Date | July 27, 2013 |
Organism | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) |
NCBI Taxa ID | 559292 |
Lysine Modification | Position | Peptide | Type | References |
|---|
| 887 | LKSLETFKNSGRYIL | acetylation | [1] | | 938 | SGVTDDMKQARREQL | acetylation | [1] |
|
Reference | [1] Proteome-wide analysis of lysine acetylation suggests its broad regulatory scope in Saccharomyces cerevisiae. Henriksen P, Wagner SA, Weinert BT, Sharma S, Bacinskaja G, Rehman M, Juffer AH, Walther TC, Lisby M, Choudhary C. Mol Cell Proteomics. 2012 Nov;11(11):1510-22. [ PMID: 22865919] |
Functional Description | ATP-independent protease that degrades mitochondrial transit peptides after their cleavage both in intermembrane space and in matrix. Also degrades other unstructured peptides (By similarity). |
Sequence Annotation | ACT_SITE 87 87 Proton acceptor.
METAL 84 84 Zinc; catalytic.
METAL 88 88 Zinc; catalytic.
METAL 185 185 Zinc; catalytic (By similarity).
MOD_RES 920 920 Phosphoserine. |
Keyword | Complete proteome; Hydrolase; Metal-binding; Metalloprotease; Mitochondrion; Phosphoprotein; Protease; Reference proteome; Zinc. |
Sequence Source | UniProt (SWISSPROT/TrEMBL); GenBank; EMBL |
Protein Length | 989 AA |
Protein Sequence | MLRFQRFASS YAQAQAVRKY PVGGIFHGYE VRRILPVPEL RLTAVDLVHS QTGAEHLHID 60
RDDKNNVFSI AFKTNPPDST GVPHILEHTT LCGSVKYPVR DPFFKMLNKS LANFMNAMTG 120
PDYTFFPFST TNPQDFANLR GVYLDSTLNP LLKQEDFDQE GWRLEHKNIT DPESNIVFKG 180
VVYNEMKGQI SNANYYFWSK FQQSIYPSLN NSGGDPMKIT DLRYGDLLDF HHKNYHPSNA 240
KTFTYGNLPL VDTLKQLNEQ FSGYGKRARK DKLLMPIDLK KDIDVKLLGQ IDTMLPPEKQ 300
TKASMTWICG APQDTYDTFL LKVLGNLLMD GHSSVMYQKL IESGIGLEFS VNSGVEPTTA 360
VNLLTVGIQG VSDIEIFKDT VNNIFQNLLE TEHPFDRKRI DAIIEQLELS KKDQKADFGL 420
QLLYSILPGW TNKIDPFESL LFEDVLQRFR GDLETKGDTL FQDLIRKYIV HKPCFTFSIQ 480
GSEEFSKSLD DEEQTRLREK ITALDEQDKK NIFKRGILLQ EKQNEKEDLS CLPTLQIKDI 540
PRAGDKYSIE QKNNTMSRIT DTNGITYVRG KRLLNDIIPF ELFPYLPLFA ESLTNLGTTT 600
ESFSEIEDQI KLHTGGISTH VEVTSDPNTT EPRLIFGFDG WSLNSKTDHI FEFWSKILLE 660
TDFHKNSDKL KVLIRLLASS NTSSVADAGH AFARGYSAAH YRSSGAINET LNGIEQLQFI 720
NRLHSLLDNE ETFQREVVDK LTELQKYIVD TNNMNFFITS DSDVQAKTVE SQISKFMERL 780
PHGSCLPNGP KTSDYPLIGS KCKHTLIKFP FQVHYTSQAL LGVPYTHKDG SALQVMSNML 840
TFKHLHREVR EKGGAYGGGA SYSALAGIFS FYSYRDPQPL KSLETFKNSG RYILNDAKWG 900
VTDLDEAKLT IFQQVDAPKS PKGEGVTYFM SGVTDDMKQA RREQLLDVSL LDVHRVAEKY 960
LLNKEGVSTV IGPGIEGKTV SPNWEVKEL 989 |
Gene Ontology | GO:0005758; C:mitochondrial intermembrane space; IDA:SGD. GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. GO:0004222; F:metalloendopeptidase activity; IDA:SGD. GO:0051603; P:proteolysis involved in cellular protein catabolic process; IMP:SGD. |
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Pfam | |
SMART | |
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