CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-027065
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 CG32549, isoform B 
Protein Synonyms/Alias
 CG32549, isoform F; RH50433p 
Gene Name
 CG32549-RF 
Gene Synonyms/Alias
 CG32549; Dmel_CG32549 
Created Date
 July 27, 2013 
Organism
 Drosophila melanogaster (Fruit fly) 
NCBI Taxa ID
 7227 
Lysine Modification
Position
Peptide
Type
References
168LYPNKFLKLDESRVYacetylation[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
  
Sequence Annotation
 ACT_SITE 77 77 Nucleophile (By similarity).
 ACT_SITE 79 79 Proton donor (By similarity).
 METAL 77 77 Magnesium (By similarity).
 METAL 79 79 Magnesium; via carbonyl oxygen (By
 METAL 376 376 Magnesium (By similarity).  
Keyword
 Complete proteome; Hydrolase; Magnesium; Metal-binding; Reference proteome. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 612 AA 
Protein Sequence
MQATPSEDAQ PQDPLKSFER DFCDLPPYQC EMSDSAPNTP GPCSTSALPK KYYRYAAHRV 60
FVNRSLHLEN IKYYGFDMDY TLAEYKSPQY EQLGFNLVKE RLVFMGYPKE ILQFEYDPTF 120
PVRGLWFDTL YGNLLKVDAY GNILVCVHGF EFIKHHQVYE LYPNKFLKLD ESRVYVLNTL 180
FNLPETYLLA CLVDFLTNSS DFVRVERGIK AGDLLFTYKS IFQDVRRAVD WVHSDGDLKR 240
RTTQNMAHYV KKDERLPTVL SRIRESGAKL FMLTNSDYTY TNEIMTYLFD FPHGATPDEP 300
HRDWKTYFDV IVVDARKPLF FDEGTVLRQV DTKTGSLKIG THVGPLQPGQ VYSGGSCELF 360
TKFINAKGKD VLYVGDHIFG DILKSKKIRG WRTFLIVPEL VRELHVWTDE CQLFAELQNL 420
DIKLGDLYRD LDSSAKVKPD ISQLRTCIRD VTHKMDMSYG MMGSLFRSGS RQTFFSSQVV 480
RYADVYAATL LNLIYYPFSY MFRAPAMLLP HESTVAHDQA HQPPPPLGPV PVPATGAASV 540
AASPDEPARI LAGTAEHVKD PKDLHRASSI VHTRPSTPTV VTHTHDEDYS EEEETPSGAE 600
SSTEAVRDAS ED 612 
Gene Ontology
 GO:0008253; F:5'-nucleotidase activity; IEA:EC.
 GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. 
Interpro
 IPR023214; HAD-like_dom.
 IPR008380; HAD-SF_hydro_IG_5-nucl.
 IPR016695; Pur_nucleotidase. 
Pfam
 PF05761; 5_nucleotid 
SMART
  
PROSITE
  
PRINTS