CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-023575
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 DNA replication licensing factor Mcm7 
Protein Synonyms/Alias
 Minichromosome maintenance 7 protein; DmMCM3 
Gene Name
 Mcm7 
Gene Synonyms/Alias
 CG4978 
Created Date
 July 27, 2013 
Organism
 Drosophila melanogaster (Fruit fly) 
NCBI Taxa ID
 7227 
Lysine Modification
Position
Peptide
Type
References
545TYVHSHSKQPPTRVKacetylation[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
 Acts as component of the Mcm2-7 complex (Mcm complex) which is the putative replicative helicase essential for 'once per cell cycle' DNA replication initiation and elongation in eukaryotic cells. The active ATPase sites in the Mcm2-7 ring are formed through the interaction surfaces of two neighboring subunits such that a critical structure of a conserved arginine finger motif is provided in trans relative to the ATP-binding site of the Walker A box of the adjacent subunit. The six ATPase active sites, however, are likely to contribute differentially to the complex helicase activity. 
Sequence Annotation
 DOMAIN 332 538 MCM.
 NP_BIND 381 388 ATP (Potential).
 MOTIF 513 516 Arginine finger.  
Keyword
 ATP-binding; Cell cycle; Complete proteome; DNA replication; DNA-binding; Helicase; Hydrolase; Nucleotide-binding; Nucleus; Reference proteome. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 720 AA 
Protein Sequence
MARRDYAQDR ESIKTFLSEF CKCDDDGKKE FVYGSQLVKL AHREQVLITI DLDDLAEFNE 60
SLAEAVVDNC RRYTSIFSDV IAELLPSYKQ QEVHAKDALD VYIEHRLMME SRTRNPMEQR 120
DERNSFPSEL MKRFEVGFKP LSTEKAHSIR EVKAQHIGKL VTVRGIVTRC TEVKPMMVVA 180
TYTCDRCGSE TYQPVNSLSF TPVHDCPSDD CRVNKAGGRL YLQTRGSKFV KFQEVKMQEH 240
SDQVPVGHIP RSMTIMCRGE VTRMAQPGDH IVVSGVFLPL MRTGFAQMIQ GLLSETFLQA 300
HRIICINKND EISDKDAELT PEELEELAQD DFYERLATSL APEIYGHLDV KKALLLLLVG 360
GVDKRPDGMK IRGNINICLM GDPGVAKSQL LGYISRLAVR SQYTTGRGSS GVGLTAAVMK 420
DPLTGEMTLE GGALVLADQG VCCIDEFDKM ADQDRTAIHE VMEQQTISIA KAGIMTTLNA 480
RVSILAAANP AFGRYNPRRT VEQNIQLPAA LLSRFDLLWL IQDKPDRDND LRLAKHITYV 540
HSHSKQPPTR VKALDMNLMR RYINLCKRKN PTIPDELTDY IVGAYVELRR EARNQKDMTF 600
TSARNLLGIL RLSTALARLR LSDSVEKDDV AEALRLLEMS KDSLNQIHEH QKGHVPNTSD 660
RIFAIVRELA GSGKAVKISD IMDRCTTKGF KPDQVDKCID DYEELNVWQV NMGRTKITFM 720 
Gene Ontology
 GO:0042555; C:MCM complex; IEA:InterPro.
 GO:0005875; C:microtubule associated complex; IDA:FlyBase.
 GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
 GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
 GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
 GO:0003678; F:DNA helicase activity; IEA:InterPro.
 GO:0032508; P:DNA duplex unwinding; IEA:GOC.
 GO:0006270; P:DNA replication initiation; IEA:InterPro.
 GO:0007095; P:mitotic G2 DNA damage checkpoint; IGI:FlyBase. 
Interpro
 IPR003593; AAA+_ATPase.
 IPR008050; MCM7.
 IPR018525; MCM_CS.
 IPR001208; MCM_DNA-dep_ATPase.
 IPR012340; NA-bd_OB-fold.
 IPR027417; P-loop_NTPase. 
Pfam
 PF00493; MCM 
SMART
 SM00382; AAA
 SM00350; MCM 
PROSITE
 PS00847; MCM_1
 PS50051; MCM_2 
PRINTS
 PR01657; MCMFAMILY.
 PR01663; MCMPROTEIN7.