DNA replication licensing factor mcm2 - Xenopus laevis (African clawed frog)

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P55861 (MCM2_XENLA) Reviewed, UniProtKB/Swiss-Prot

Last modified May 29, 2013. Version 89. History...

Clusters with 100%, 90%, 50% identity |

Documents (1) |

Third-party data

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Names·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

Names and origin

Protein names

Recommended name:
DNA replication licensing factor mcm2
EC=3.6.4.12

Alternative name(s):
BM28-homolog
Minichromosome maintenance protein 2
Short name=xMCM2
p112

Gene names

Name:

mcm2

Organism

Xenopus laevis (African clawed frog)

Taxonomic identifier

8355 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Amphibia › Batrachia › Anura › Pipoidea › Pipidae › Xenopodinae › Xenopus › Xenopus

Protein attributes

Sequence length	886 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	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 the entry in S phase and for cell division. Ref.2 Ref.4 Ref.7
Catalytic activity	ATP + H₂O = ADP + phosphate.
Subunit structure	Component of the mcm2-7 complex (RLF-M). The complex forms a toroidal hexameric ring with the proposed subunit order mcm2-mcm6-mcm4-mcm7-mcm3-mcm5 (By simililarity). Ref.1 Ref.2 Ref.4 Ref.5 Ref.7
Subcellular location	Nucleus. Note: Associated with chromatin before the formation of nuclei and detaches from it as DNA replication progresses. Ref.2 Ref.4
Post-translational modification	May be in a phosphorylated state in the mitotic mcm complex. Phosphorylated in the interphase mcm complex. Phosphorylated by the cdc7-dbf4 and cdc7-dbf4b complexes. Ref.6 Ref.8
Sequence similarities	Belongs to the MCM family. Contains 1 MCM domain.

Ontologies

Keywords
Biological process	Cell cycle DNA replication
Cellular component	Nucleus
Domain	Zinc-finger
Ligand	ATP-binding DNA-binding Metal-binding Nucleotide-binding Zinc
Molecular function	Helicase Hydrolase
Gene Ontology (GO)
Biological_process	ATP catabolic process Inferred from direct assay Ref.7. Source: GOC DNA replication initiation Inferred from electronic annotation. Source: InterPro DNA unwinding involved in replication Inferred from direct assay Ref.7. Source: UniProtKB cell cycle Inferred from electronic annotation. Source: UniProtKB-KW regulation of DNA-dependent DNA replication initiation Inferred from direct assay Ref.7 Ref.2. Source: UniProtKB
Cellular_component	MCM complex Inferred from direct assay Ref.7 Ref.2 Ref.5. Source: UniProtKB chromatin Inferred from direct assay Ref.7 Ref.2. Source: UniProtKB nucleus Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular_function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW DNA binding Inferred from electronic annotation. Source: UniProtKB-KW DNA helicase activity Inferred from electronic annotation. Source: InterPro metal ion binding Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
mmcm3	P49739	9	EBI-876864,EBI-491720

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 886

886

DNA replication licensing factor mcm2

PRO_0000194089

Regions

Domain

458 – 665

208

MCM

Zinc finger

314 – 340

C4-type Potential

Nucleotide binding

508 – 515

ATP Potential

Motif

640 – 643

Arginine finger

Experimental info

Sequence conflict

169

E → K in AAC60223. Ref.2

Sequence conflict

439

G → R in BAA09948. Ref.1

Sequence conflict

563

L → F in BAA09948. Ref.1

Sequence conflict

728

M → I in BAA09948. Ref.1

Sequences

Sequence

Length

Mass (Da)

Tools

P55861 [UniParc].

Last modified June 13, 2006. Version 2.
Checksum: 524C7B3673E2B2DD
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FASTA

886

100,262

        10         20         30         40         50         60 
MADSSESFNI ATSPRAGSRR DALTSSPGRD LPPFEDESEG MFGDGVVPEE EEDGEELIGD 

        70         80         90        100        110        120 
AMERDYRPIS ELDRYEVEGL DDEEDVEDLT ASQREAAEQS MRMRDREMGR ELGRMRRGLL 

       130        140        150        160        170        180 
YDSDEEEEDR PARKRRMAER AAEGAPEEDE EMIESIENLE DMKGHTVREW VSMAATRLEI 

       190        200        210        220        230        240 
YHRFKNFLRT HVDEHGHNVF KEKISDMCKE NKESLPVNYE DLAAREHVLA YFLPEAPAEM 

       250        260        270        280        290        300 
LKIFDEAAKE VVLVMYPKYD RIAREIHVRI SHLPLVEELR SLRQLHLNQL IRTSGVVTCC 

       310        320        330        340        350        360 
TGVLPQLSMV KYNCNKCNFI LGPFFQSQNQ EVRPGSCPEC QSFGPFEINM EETVYQNYQR 

       370        380        390        400        410        420 
ITIQESPGKV AAGRLPRSKD AILLADLVDS CKPGDEIELT GIYHNNYDGS LNTANGFPVF 

       430        440        450        460        470        480 
ATVILANHIT KKDDKVAVGE LTDEDVKAIV ALSKDERIGE RIFASIAPSI YGHEDIKRGL 

       490        500        510        520        530        540 
ALALFGGEAK NPGGKHKVRG DINVLLCGDP GTAKSQFLKY VEKVASRAVF TTGQGASAVG 

       550        560        570        580        590        600 
LTAYVQRHPV TKEWTLEAGA LVLADRGVCL IDEFDKMNDQ DRTSIHEAME QQSISISKAG 

       610        620        630        640        650        660 
IVTSLQARCT VIAASNPIGG RYDPSLTFSE NVDLTEPIVS RFDILCVVRD TVDPVQDEML 

       670        680        690        700        710        720 
ARFVVSSHIK HHPSSKDIAN GDAAEFALPN TFGVEALPQE VLKKYIMYAK EKIRPKLNQM 

       730        740        750        760        770        780 
DQDKVAKMYS DLRKESMATG SIPITVRHIE SMIRMAEAHA RMHLRDYVVE DDVNMAIRVM 

       790        800        810        820        830        840 
LESFIDTQKF SVMRSMRKTF ARYLAFRRDN NELLLFVLKQ LIAEQVTYQR NRYGAQQDTI 

       850        860        870        880 
EVPEKDLVDK ARQINIHNLS AFYDSDLFKM NKFTHDVKKK LIIQQF

« Hide

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Identification of two Xenopus laevis genes, xMCM2 and xCDC46, with sequence homology to MCM genes involved in DNA replication." Miyake S., Saito I., Kobayashi H., Yamashita S. Gene 175:71-75(1996) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], IDENTIFICATION IN A COMPLEX WITH MCM5. Tissue: Oocyte.
[2]	"Licensing of DNA replication by a multi-protein complex of MCM/P1 proteins in Xenopus eggs." Kubota Y., Mimura S., Nishimoto S., Masuda T., Nojima H., Takisawa H. EMBO J. 16:3320-3331(1997) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, IDENTIFICATION IN A COMPLEX WITH MMCM3; MCM4; MCM5; MMCM6 AND MCM7, SUBCELLULAR LOCATION. Tissue: Oocyte.
[3]	NIH - Xenopus Gene Collection (XGC) project Submitted (JAN-2003) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Embryo.
[4]	"The RLF-M component of the replication licensing system forms complexes containing all six MCM/P1 polypeptides." Thommes P., Kubota Y., Takisawa H., Blow J.J. EMBO J. 16:3312-3319(1997) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, IDENTIFICATION IN RLF-M COMPLEX, SUBCELLULAR LOCATION.
[5]	"Evidence for different MCM subcomplexes with differential binding to chromatin in Xenopus." Coue M., Amariglio F., Maiorano D., Bocquet S., Mechali M. Exp. Cell Res. 245:282-289(1998) [PubMed] [Europe PMC] [Abstract] Cited for: IDENTIFICATION IN MCM COMPLEXES.
[6]	"Distinct phosphoisoforms of the Xenopus Mcm4 protein regulate the function of the Mcm complex." Pereverzeva I., Whitmire E., Khan B., Coue M. Mol. Cell. Biol. 20:3667-3676(2000) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION.
[7]	"The ATPase activity of MCM2-7 is dispensable for pre-RC assembly but is required for DNA unwinding." Ying C.Y., Gautier J. EMBO J. 24:4334-4344(2005) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION OF THE MCM2-7 COMPLEX, IDENTIFICATION IN A COMPLEX WITH MMCM3; MCM4; MCM5; MMCM6 AND MCM7.
[8]	"Cdc7-Drf1 is a developmentally regulated protein kinase required for the initiation of vertebrate DNA replication." Takahashi T.S., Walter J.C. Genes Dev. 19:2295-2300(2005) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION.

Cross-references

Sequence databases
EMBL GenBank DDBJ	D63919 mRNA. Translation: BAA09948.1. U44047 mRNA. Translation: AAC60223.1. BC046274 mRNA. Translation: AAH46274.1.
PIR	JC5085.
RefSeq	NP_001080759.1. NM_001087290.1.
UniGene	Xl.382.
3D structure databases
ProteinModelPortal	P55861.
ModBase	Search...
Protein-protein interaction databases
IntAct	P55861. 6 interactions.
MINT	MINT-6540654.
Proteomic databases
PRIDE	P55861.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	380451.
KEGG	xla:380451.
Organism-specific databases
CTD	4171.
Xenbase	XB-GENE-999979. mcm2.
Phylogenomic databases
HOVERGEN	HBG106398.
KO	K02540.
Family and domain databases
Gene3D	2.40.50.140. 2 hits.
InterPro	IPR008045. MCM2. IPR018525. MCM_CS. IPR001208. MCM_DNA-dep_ATPase. IPR012340. NA-bd_OB-fold. IPR027417. P-loop_NTPase. [Graphical view]
Pfam	PF00493. MCM. 1 hit. PF12619. MCM2_N. 1 hit. [Graphical view]
PRINTS	PR01657. MCMFAMILY. PR01658. MCMPROTEIN2.
SMART	SM00350. MCM. 1 hit. [Graphical view]
SUPFAM	SSF50249. Nucleic_acid_OB. 1 hit. SSF52540. SSF52540. 1 hit.
PROSITE	PS00847. MCM_1. 1 hit. PS50051. MCM_2. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

MCM2_XENLA

Accession

Primary (citable) accession number: P55861
Secondary accession number(s): O42588, Q7ZX05

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 1, 1997
Last sequence update:	June 13, 2006
Last modified:	May 29, 2013
This is version 89 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

Names·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Binary interactions

With

Entry

#Exp.

IntAct

Notes

Sequence annotation (Features)

Molecule processing

Regions

Experimental info

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

Proteomic databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Family and domain databases

Entry information

Relevant documents