CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-007348
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Protein TMA108 
Protein Synonyms/Alias
 108 kDa translation machinery-associated protein 
Gene Name
 TMA108 
Gene Synonyms/Alias
 YIL137C 
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
667RASLTSSKLQSFLKKacetylation[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
 Putative zinc aminopeptidase which may be involved in ribosome biogenesis. 
Sequence Annotation
 REGION 293 297 Substrate binding (By similarity).
 ACT_SITE 331 331 Proton acceptor (By similarity).
 METAL 330 330 Zinc; catalytic (By similarity).
 METAL 334 334 Zinc; catalytic (By similarity).
 METAL 353 353 Zinc; catalytic (By similarity).  
Keyword
 Aminopeptidase; Complete proteome; Cytoplasm; Hydrolase; Metal-binding; Metalloprotease; Protease; Reference proteome; Ribosome biogenesis; Zinc. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 946 AA 
Protein Sequence
MSDNLLSLEN PVVPSHYELR LEIDPKQSSP NFKGSAIIHL KFNPNSTTLA SIEDSFTQFK 60
LHSKDLIVLS AHATIGSTKF DLKISQDTGK HLSIFNSESP IQLSNDCPLI LSVQYVGKIR 120
DIKTHHDKTF GIFKTNFMDR KTGTANNHVV ATHCQPFSAS NIFPCIDEPS NKSTFQLNIA 180
TDAQYKAVSN TPVEMVEALD SSQKHLVKFA KTPLMTTSVF GFSIGDLEFL KTEIKLEGDR 240
TIPVSIYAPW DIANAAFTLD TVQKYLPLLE SYFKCPYPLP KLDFVLLPYL SDMAMENFGM 300
ITIQLNHLLI PPNALANETV REQAQQLIVH ELVHQWMGNY ISFDSWESLW FNESFATWLA 360
CHILEQNGDL SHYWTSEPYL LQQVEPTMCR DAADVNGRSI FQIAQRNTGI DSQTSDIFDP 420
EAYTKGIIML RSLQLATGES HLQKGLESVF EDTKTFHARS VKPMDIWNHI GKFLKSQNIT 480
NFVSSWTRTP GLPVVKVEVE EKDGKTQTKL TQHRFINQLS TEEKDQLEDV PYQVPLFGVL 540
PDGKMDTKNV LLTDRTLKFD YPILVINHLA QGYYRVSYES EECYALINDK ITEETLSEID 600
LRKIFLDLSQ FIGDEGFQNS IHLHGLFKIL NHIASPSTKI ASKYWDPLSK GLEVLQTIDR 660
ASLTSSKLQS FLKKKIVIPL FNKIDWPHGE FDKSTNPHEL KVMSQVLFLN KNSAKCAELC 720
QIYFKHLLQG PRSSVPLELV NSILVVVSQH CANIKQWKKI FDLVKRSSCT GITNHVINMY 780
DQNSSETAML IQNGAIESLG FCLDSDIVKK TLNFITSNIE SEGMELALFG FNYNFKKRLN 840
KNEKPQDQVV RETIWEWYMG NFDQWARKAT RKGTTTGDHL HKALRSISLI IFQMFVADEP 900
QKIEKFINLE KEKLGQSLLS LDDIWASVQQ DEESRKTIRR DLASLV 946 
Gene Ontology
 GO:0005737; C:cytoplasm; IDA:SGD.
 GO:0004177; F:aminopeptidase activity; IEA:UniProtKB-KW.
 GO:0008237; F:metallopeptidase activity; IEA:UniProtKB-KW.
 GO:0008270; F:zinc ion binding; IEA:InterPro.
 GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
 GO:0042254; P:ribosome biogenesis; IMP:SGD. 
Interpro
 IPR024571; DUF3358.
 IPR001930; Peptidase_M1.
 IPR014782; Peptidase_M1_N. 
Pfam
 PF11838; DUF3358
 PF01433; Peptidase_M1 
SMART
  
PROSITE
 PS00142; ZINC_PROTEASE 
PRINTS
 PR00756; ALADIPTASE.