dpa

Functionⁱ

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. Required for DNA replication and cell proliferation. Essential role in mitotic DNA replication but not in endoreplication.2 Publications

Catalytic activityⁱ

ATP + H₂O = ADP + phosphate.

Regions

Feature key	Position(s)	DescriptionActions	Graphical view	Length
Nucleotide bindingⁱ	512 – 519	ATPSequence analysis		8

GO - Molecular functionⁱ

ATP binding Source: UniProtKB-KW
DNA binding Source: UniProtKB-KW
DNA helicase activity Source: InterPro

View the complete GO annotation on QuickGO ...

GO - Biological processⁱ

DNA replication
Source: FlyBase
Inferred from mutant phenotypeⁱ
- 11290306
DNA replication initiation Source: InterPro
mitotic spindle organization
Source: FlyBase
Inferred from mutant phenotypeⁱ
- 11290306

View the complete GO annotation on QuickGO ...

Keywordsⁱ

Molecular function	DNA-binding, Helicase, Hydrolase
Biological process	DNA replication
Ligand	ATP-binding, Nucleotide-binding

Enzyme and pathway databases

Reactomeⁱ	R-DME-176187. Activation of ATR in response to replication stress. R-DME-68867. Assembly of the pre-replicative complex. R-DME-68949. Orc1 removal from chromatin. R-DME-68962. Activation of the pre-replicative complex. R-DME-69052. Switching of origins to a post-replicative state. R-DME-69300. Removal of licensing factors from origins.

Reactomeⁱ

R-DME-176187. Activation of ATR in response to replication stress.
R-DME-68867. Assembly of the pre-replicative complex.
R-DME-68949. Orc1 removal from chromatin.
R-DME-68962. Activation of the pre-replicative complex.
R-DME-69052. Switching of origins to a post-replicative state.
R-DME-69300. Removal of licensing factors from origins.

Names & Taxonomyⁱ

Protein namesⁱ	Recommended name: DNA replication licensing factor MCM4 (EC:3.6.4.12) Alternative name(s): Protein disc proliferation abnormal
Gene namesⁱ	Name:dpa ORF Names:CG1616
Organismⁱ	Drosophila melanogaster (Fruit fly)
Taxonomic identifierⁱ	7227 [NCBI]
Taxonomic lineageⁱ	cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Protostomia › Ecdysozoa › Panarthropoda › Arthropoda › Mandibulata › Pancrustacea › Hexapoda › Insecta › Dicondylia › Pterygota › Neoptera › Holometabola › Diptera › Brachycera › Muscomorpha › Eremoneura › Cyclorrhapha › Schizophora › Acalyptratae › Ephydroidea › Drosophilidae › Drosophilinae › Drosophilini › Drosophila › Sophophora › melanogaster group › melanogaster subgroup
Proteomesⁱ	UP000000803 Componentⁱ: Chromosome 2R

Organism-specific databases

Drosophila genome database More...FlyBaseⁱ	FBgn0015929. dpa.

FlyBaseⁱ

FBgn0015929. dpa.

Keywords - Cellular componentⁱ

Nucleus

Pathology & Biotechⁱ

Mutagenesis

Feature key	Position(s)	DescriptionActions	Graphical view	Length
Mutagenesisⁱ	518	K → A: Slihgtly reduces complex helicase activity. 1 Publication		1

PTM / Processingⁱ

Molecule processing

Feature key	Position(s)	DescriptionActions	Graphical view	Length
ChainⁱPRO_0000194104	1 – 866	DNA replication licensing factor MCM4Add BLAST		866

Amino acid modifications

Feature key	Position(s)	DescriptionActions	Length
Modified residueⁱ	55	Phosphoserine2 Publications	1
Modified residueⁱ	81	Phosphoserine1 Publication	1
Modified residueⁱ	87	Phosphothreonine1 Publication	1

Keywords - PTMⁱ

Phosphoprotein

Proteomic databases

PaxDbⁱ	Q26454.
PRIDEⁱ	Q26454.

PTM databases

iPTMnetⁱ	Q26454.

iPTMnetⁱ

Q26454.

Expressionⁱ

Gene expression databases

Bgeeⁱ	FBgn0015929.
ExpressionAtlasⁱ	Q26454. differential.
Genevisibleⁱ	Q26454. DM.

Interactionⁱ

Subunit structureⁱ

Component of the Mcm2-7 complex. The complex forms a toroidal hexameric ring with the proposed subunit order Mcm2-Mcm6-Mcm4-Mcm7-Mcm3-Mcm5 (Probable).Curated1 Publication

Binary interactionsⁱ

With	Entry	#Exp.	IntAct
CDC45L	O96989	4	EBI-175772,EBI-156880
Mcm2	P49735	9	EBI-175772,EBI-138228
Mcm6	Q9V461	4	EBI-175772,EBI-869161

Show more details

Protein-protein interaction databases

BioGridⁱ	61555. 14 interactors.
Database of interacting proteins More...DIPⁱ	DIP-35346N.
IntActⁱ	Q26454. 11 interactors.
STRINGⁱ	7227.FBpp0088055.

Structureⁱ

3D structure databases

ProteinModelPortalⁱ	Q26454.
ModBaseⁱ	Search...
MobiDBⁱ	Search...

Family & Domainsⁱ

Domains and Repeats

Feature key	Position(s)	DescriptionActions	Graphical view	Length
Domainⁱ	460 – 669	MCMAdd BLAST		210

Motif

Feature key	Position(s)	DescriptionActions	Graphical view	Length
Motifⁱ	644 – 647	Arginine finger		4

Sequence similaritiesⁱ

Belongs to the MCM family.Curated

Phylogenomic databases

eggNOGⁱ	KOG0478. Eukaryota. COG1241. LUCA.
Ensembl GeneTree More...GeneTreeⁱ	ENSGT00910000144163.
InParanoidⁱ	Q26454.
KEGG Orthology (KO) More...KOⁱ	K02212.
OMAⁱ	KNTIRIC.
Database of Orthologous Groups More...OrthoDBⁱ	EOG091G02V8.
PhylomeDBⁱ	Q26454.

Family and domain databases

InterProⁱ	View protein in InterPro IPR003593. AAA+_ATPase. IPR031327. MCM. IPR008047. MCM_4. IPR018525. MCM_CS. IPR001208. MCM_dom. IPR027925. MCM_N. IPR033762. MCM_OB. IPR012340. NA-bd_OB-fold. IPR027417. P-loop_NTPase.
PANTHERⁱ	PTHR11630. PTHR11630. 1 hit. PTHR11630:SF66. PTHR11630:SF66. 1 hit.
Pfam protein domain database More...Pfamⁱ	View protein in Pfam PF00493. MCM. 1 hit. PF14551. MCM_N. 1 hit. PF17207. MCM_OB. 1 hit.
PRINTSⁱ	PR01657. MCMFAMILY. PR01660. MCMPROTEIN4.
SMARTⁱ	View protein in SMART SM00382. AAA. 1 hit. SM00350. MCM. 1 hit.
SUPFAMⁱ	SSF50249. SSF50249. 1 hit. SSF52540. SSF52540. 1 hit.
PROSITEⁱ	View protein in PROSITE PS00847. MCM_1. 1 hit. PS50051. MCM_2. 1 hit.

Sequenceⁱ

Sequence statusⁱ: Complete.

Q26454-1 [UniParc]FASTA Add to basket

« Hide

        10         20         30         40         50
MSSPARSPSV GGATPKQGAR TPTRGIASQD VETPMRMGPG RAVRPSDNIS 
        60         70         80         90        100
LPPTSPGNIS LPATSPARGL GANMSEIDLS SPLNYGTPSS MGSIRTPRSG 
       110        120        130        140        150
IRGTPLRARP DIRTDKRIRQ VAIGGGSGLE PIPEKGSETT DPVSESSQAP 
       160        170        180        190        200
QLVVWGTNVV VSQCKSKFKS FIMRFIDPSA EQDEISENID VNQPLYLQKL 
       210        220        230        240        250
EEIHTLEEPY LNLNCAHLKT FDQDLYRQLI CYPQEVIPGF DMAINEMFFE 
       260        270        280        290        300
RYPAALLEHQ IQVRPFNADK TRNMRSLNPE DMDQLISISG MVIRSSNVIP 
       310        320        330        340        350
EMREAFFSCN ICSFSTTVEV DRGRINQPTL CTNCNTNHCF RLIHNRSEFT 
       360        370        380        390        400
DKQLVKLQES PDDMAAGQTP HNVLLYAHND LVDKVQPGDR VTVTGIYRAT 
       410        420        430        440        450
PLKTGGLSSS VKSVYKTHVD VVHFRKVDNK RLYEDEEGKD HIFPPERVEL 
       460        470        480        490        500
LQLLAKKPDI YDRLARAIAP SIYENDDIKK GILLQLFGGT KKKHATLGRQ 
       510        520        530        540        550
NFRSEIHLLL CGDPGTSKSQ MLQYVFNLVP RSQYTSGRGS SAVGLTAYVT 
       560        570        580        590        600
KDPETRQLVL QTGALVLADN GVCCIDEFDK MNDSTRSVLH EVMEQQTLSI 
       610        620        630        640        650
AKAGIICQLN ARTSILAAAN PAESQWNKRK NIIDNVQLPH TLLSRFDLIF 
       660        670        680        690        700
LVLDPQDEIF DKRLASHLVS LYYVTRHEEE DTMFDMSVLR DYIAYAREHL 
       710        720        730        740        750
SPTLSDEAQQ RLIQAYVDMR KVGAGRGQIS AYPRQLESLI RLSEAHAKVR 
       760        770        780        790        800
LSNQVELLDV EEAWRLHREA LKQSATDPLS GKIDVGILTT GLSTAARKKR 
       810        820        830        840        850
ADLVAAIKEN LKKKGKVLTV PYQKLFSDIK EGSQIMITRE QFEDALKEVQ 
       860 
DEGAIVVMGK NTIRIC

Length:866

Mass (Da):96,610

Last modified:November 2, 2001 - v2

Checksum:ⁱCF6ED69D2ADDA04E

GO

Experimental Info

Feature key	Position(s)	DescriptionActions	Graphical view	Length
Sequence conflictⁱ	435	D → E in AAB35644 (PubMed:7489728).Curated		1

Sequence databases

Select the link destinations: EMBLⁱ GenBankⁱ DDBJⁱ Links Updated	S80255 mRNA. Translation: AAB35644.1. AE013599 Genomic DNA. Translation: AAF59242.1.
PIRⁱ	S59872.
NCBI Reference Sequences More...RefSeqⁱ	NP_001286160.1. NM_001299231.1. NP_477185.1. NM_057837.5.
UniGeneⁱ	Dm.21562.

Genome annotation databases

EnsemblMetazoaⁱ	FBtr0088982; FBpp0088055; FBgn0015929. FBtr0345797; FBpp0311783; FBgn0015929.
GeneIDⁱ	35679.
KEGGⁱ	dme:Dmel_CG1616.

Similar proteinsⁱ

100% Identity
90% Identity
50% Identity

Protein	Similar proteins	Organisms	Length	Cluster ID	Cluster name	Size
Q26454	A0A0B4LEV2	Drosophila melanogaster (Fruit fly)	866	UniRef100_Q26454	Cluster: DNA replication licensing factor MCM4	2

Protein	Similar proteins	Organisms	Length	Cluster ID	Cluster name	Size
Q26454	A0A0B4LEV2 B4MIN6 A0A1W4VDK0 UPI0007E30042 UPI0007E5D01A UPI0007E71FAB UPI0007E7841A UPI0007E797A4 UPI0007E7A3D5 A0A0J9TVC7 +21	Drosophila melanogaster (Fruit fly) Drosophila willistoni (Fruit fly) Drosophila ficusphila (Fruit fly) Drosophila suzukii (Spotted-wing drosophila fruit fly) Drosophila takahashii (Fruit fly) Drosophila rhopaloa (Fruit fly) Drosophila elegans (Fruit fly) Drosophila eugracilis (Fruit fly) Drosophila biarmipes (Fruit fly) Drosophila simulans (Fruit fly) And more	866	UniRef90_Q26454	Cluster: DNA replication licensing factor MCM4	32

Protein	Similar proteins	Organisms	Length	Cluster ID	Cluster name	Size
Q26454	A0A0B4LEV2 B4MIN6 UPI0007E797A4 UPI0007E5D01A UPI0007E71FAB UPI0007E7841A UPI0007E7A3D5 A0A1W4VDK0 UPI0007E30042 B3N9Y3 +67	Drosophila melanogaster (Fruit fly) Drosophila willistoni (Fruit fly) Drosophila eugracilis (Fruit fly) Drosophila takahashii (Fruit fly) Drosophila rhopaloa (Fruit fly) Drosophila elegans (Fruit fly) Drosophila biarmipes (Fruit fly) Drosophila ficusphila (Fruit fly) Drosophila suzukii (Spotted-wing drosophila fruit fly) Drosophila erecta (Fruit fly) And more	866	UniRef50_Q26454	Cluster: DNA replication licensing factor MCM4	78

Cross-referencesⁱ

Sequence databases

Select the link destinations: EMBLⁱ GenBankⁱ DDBJⁱ Links Updated	S80255 mRNA. Translation: AAB35644.1. AE013599 Genomic DNA. Translation: AAF59242.1.
PIRⁱ	S59872.
NCBI Reference Sequences More...RefSeqⁱ	NP_001286160.1. NM_001299231.1. NP_477185.1. NM_057837.5.
UniGeneⁱ	Dm.21562.

3D structure databases

ProteinModelPortalⁱ	Q26454.
ModBaseⁱ	Search...
MobiDBⁱ	Search...

Protein-protein interaction databases

BioGridⁱ	61555. 14 interactors.
Database of interacting proteins More...DIPⁱ	DIP-35346N.
IntActⁱ	Q26454. 11 interactors.
STRINGⁱ	7227.FBpp0088055.

PTM databases

iPTMnetⁱ	Q26454.

iPTMnetⁱ

Q26454.

Proteomic databases

PaxDbⁱ	Q26454.
PRIDEⁱ	Q26454.

Protocols and materials databases

Structural Biology Knowledgebase	Search...

Structural Biology Knowledgebase

Search...

Genome annotation databases

EnsemblMetazoaⁱ	FBtr0088982; FBpp0088055; FBgn0015929. FBtr0345797; FBpp0311783; FBgn0015929.
GeneIDⁱ	35679.
KEGGⁱ	dme:Dmel_CG1616.

Organism-specific databases

CTDⁱ	103997.
Drosophila genome database More...FlyBaseⁱ	FBgn0015929. dpa.

Phylogenomic databases

eggNOGⁱ	KOG0478. Eukaryota. COG1241. LUCA.
Ensembl GeneTree More...GeneTreeⁱ	ENSGT00910000144163.
InParanoidⁱ	Q26454.
KEGG Orthology (KO) More...KOⁱ	K02212.
OMAⁱ	KNTIRIC.
Database of Orthologous Groups More...OrthoDBⁱ	EOG091G02V8.
PhylomeDBⁱ	Q26454.

Enzyme and pathway databases

Reactomeⁱ	R-DME-176187. Activation of ATR in response to replication stress. R-DME-68867. Assembly of the pre-replicative complex. R-DME-68949. Orc1 removal from chromatin. R-DME-68962. Activation of the pre-replicative complex. R-DME-69052. Switching of origins to a post-replicative state. R-DME-69300. Removal of licensing factors from origins.

Reactomeⁱ

R-DME-176187. Activation of ATR in response to replication stress.
R-DME-68867. Assembly of the pre-replicative complex.
R-DME-68949. Orc1 removal from chromatin.
R-DME-68962. Activation of the pre-replicative complex.
R-DME-69052. Switching of origins to a post-replicative state.
R-DME-69300. Removal of licensing factors from origins.

Miscellaneous databases

GenomeRNAiⁱ	35679.
Protein Ontology More...PROⁱ	PR:Q26454.

Gene expression databases

Bgeeⁱ	FBgn0015929.
ExpressionAtlasⁱ	Q26454. differential.
Genevisibleⁱ	Q26454. DM.

Family and domain databases

InterProⁱ	View protein in InterPro IPR003593. AAA+_ATPase. IPR031327. MCM. IPR008047. MCM_4. IPR018525. MCM_CS. IPR001208. MCM_dom. IPR027925. MCM_N. IPR033762. MCM_OB. IPR012340. NA-bd_OB-fold. IPR027417. P-loop_NTPase.
PANTHERⁱ	PTHR11630. PTHR11630. 1 hit. PTHR11630:SF66. PTHR11630:SF66. 1 hit.
Pfam protein domain database More...Pfamⁱ	View protein in Pfam PF00493. MCM. 1 hit. PF14551. MCM_N. 1 hit. PF17207. MCM_OB. 1 hit.
PRINTSⁱ	PR01657. MCMFAMILY. PR01660. MCMPROTEIN4.
SMARTⁱ	View protein in SMART SM00382. AAA. 1 hit. SM00350. MCM. 1 hit.
SUPFAMⁱ	SSF50249. SSF50249. 1 hit. SSF52540. SSF52540. 1 hit.
PROSITEⁱ	View protein in PROSITE PS00847. MCM_1. 1 hit. PS50051. MCM_2. 1 hit.
ProtoNetⁱ	Search...

Entry informationⁱ

Entry nameⁱ	MCM4_DROME
Accessionⁱ	Q26454Primary (citable) accession number: Q26454 Secondary accession number(s): Q9V4M5
Entry historyⁱ	Integrated into UniProtKB/Swiss-Prot:	November 1, 1997
	Last sequence update:	November 2, 2001
	Last modified:	March 28, 2018
	This is version 152 of the entry and version 2 of the sequence. See complete history.
Entry statusⁱ	Reviewed (UniProtKB/Swiss-Prot)
Annotation program	Drosophila annotation project

Miscellaneousⁱ

Keywords - Technical termⁱ

Complete proteome, Reference proteome

UniProtKB

UniParc

Help

UniRef

Proteomes

Annotation systems

Supporting data

UniProtKB - Q26454 (MCM4_DROME)

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DNA replication licensing factor MCM4

Select a section on the left to see content.

<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>Functioni

Regions

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Biological processi

Enzyme and pathway databases

<p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi

Organism-specific databases

<p>This section provides information on the location and the topology of the mature protein in the cell.<p><a href='/help/subcellular_location_section' target='_top'>More...</a></p>Subcellular locationi

Nucleus

Nucleus

Other locations

<p>This section provides information on the disease(s) and phenotype(s) associated with a protein.<p><a href='/help/pathology_and_biotech_section' target='_top'>More...</a></p>Pathology & Biotechi

Mutagenesis

<p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi

Molecule processing

Amino acid modifications

Proteomic databases

PTM databases

<p>This section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms.<p><a href='/help/expression_section' target='_top'>More...</a></p>Expressioni

Gene expression databases

<p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactioni

Protein-protein interaction databases

<p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structurei

3D structure databases

<p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi

Domains and Repeats

Motif

<p>This subsection of the ‘Family and domains’ section provides information about the sequence similarity with other proteins.<p><a href='/help/sequence_similarities' target='_top'>More...</a></p>Sequence similaritiesi

Phylogenomic databases

Family and domain databases

Experimental Info

Sequence databases

Genome annotation databases

<p>This section is used to point to information related to entries and found in data collections other than UniProtKB.<p><a href='/help/cross_references_section' target='_top'>More...</a></p>Cross-referencesi

Sequence databases

3D structure databases

Protein-protein interaction databases

PTM databases

Proteomic databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Miscellaneous databases

Gene expression databases

Family and domain databases

<p>This section provides general information on the entry.<p><a href='/help/entry_information_section' target='_top'>More...</a></p>Entry informationi

<p>This section contains any relevant information that doesn’t fit in any other defined sections<p><a href='/help/miscellaneous_section' target='_top'>More...</a></p>Miscellaneousi

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Functionⁱ

GO - Molecular functionⁱ

GO - Biological processⁱ

Names & Taxonomyⁱ

Subcellular locationⁱ

Pathology & Biotechⁱ

PTM / Processingⁱ

Expressionⁱ

Interactionⁱ

Structureⁱ

Family & Domainsⁱ

Sequence similaritiesⁱ

Cross-referencesⁱ

Entry informationⁱ

Miscellaneousⁱ