MCM3_ENTHI
ID MCM3_ENTHI Reviewed; 597 AA.
AC Q24849;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1997, sequence version 1.
DT 03-AUG-2022, entry version 95.
DE RecName: Full=DNA replication licensing factor MCM3;
DE EC=3.6.4.12;
GN Name=MCM3;
OS Entamoeba histolytica.
OC Eukaryota; Amoebozoa; Evosea; Archamoebae; Mastigamoebida; Entamoebidae;
OC Entamoeba.
OX NCBI_TaxID=5759;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 30459 / HM-1:IMSS;
RA Gangopadhyay S.S., Lohia A.;
RL Submitted (MAY-1996) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Acts as a factor that allows the DNA to undergo a single
CC round of replication per cell cycle. Required for DNA replication and
CC cell proliferation (By similarity). May act as a component of the MCM
CC complex which is the putative replicative helicase of the replication
CC licensing system in eukaryotic cells. {ECO:0000250}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + H2O = ADP + H(+) + phosphate; Xref=Rhea:RHEA:13065,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; EC=3.6.4.12;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the MCM family. {ECO:0000305}.
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DR EMBL; X98048; CAA66661.1; -; Genomic_DNA.
DR AlphaFoldDB; Q24849; -.
DR SMR; Q24849; -.
DR STRING; 5759.rna_EHI_103600-1; -.
DR VEuPathDB; AmoebaDB:EHI5A_077240; -.
DR VEuPathDB; AmoebaDB:EHI7A_062040; -.
DR VEuPathDB; AmoebaDB:EHI8A_049600; -.
DR VEuPathDB; AmoebaDB:EHI_103600; -.
DR VEuPathDB; AmoebaDB:KM1_109070; -.
DR eggNOG; KOG0479; Eukaryota.
DR GO; GO:0042555; C:MCM complex; IEA:InterPro.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:RHEA.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0003678; F:DNA helicase activity; IEA:UniProtKB-EC.
DR GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR GO; GO:0006270; P:DNA replication initiation; IEA:InterPro.
DR Gene3D; 2.40.50.140; -; 1.
DR Gene3D; 3.40.50.300; -; 1.
DR InterPro; IPR031327; MCM.
DR InterPro; IPR008046; Mcm3.
DR InterPro; IPR018525; MCM_CS.
DR InterPro; IPR001208; MCM_dom.
DR InterPro; IPR041562; MCM_lid.
DR InterPro; IPR033762; MCM_OB.
DR InterPro; IPR012340; NA-bd_OB-fold.
DR InterPro; IPR027417; P-loop_NTPase.
DR PANTHER; PTHR11630; PTHR11630; 1.
DR Pfam; PF00493; MCM; 1.
DR Pfam; PF17855; MCM_lid; 1.
DR Pfam; PF17207; MCM_OB; 1.
DR PRINTS; PR01657; MCMFAMILY.
DR PRINTS; PR01659; MCMPROTEIN3.
DR SMART; SM00350; MCM; 1.
DR SUPFAM; SSF50249; SSF50249; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR PROSITE; PS00847; MCM_1; 1.
DR PROSITE; PS50051; MCM_2; 1.
PE 3: Inferred from homology;
KW ATP-binding; Cell cycle; DNA replication; DNA-binding; Helicase; Hydrolase;
KW Nucleotide-binding; Nucleus.
FT CHAIN 1..597
FT /note="DNA replication licensing factor MCM3"
FT /id="PRO_0000194096"
FT DOMAIN 180..386
FT /note="MCM"
FT MOTIF 361..364
FT /note="Arginine finger"
FT BINDING 229..236
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255"
SQ SEQUENCE 597 AA; 66413 MW; 129D9BB171ED6566 CRC64;
MEGHIHHITP RNITASILQQ KVAVQGIITK SSQIRPLLQT AVQFCPLDYS THARDLSHAD
VMVKLSSKTP DGKPLELEPG LSTYKDFQTL VVQEMPESAP TGQMPRSVIV ILLDQLVDKG
KPGDRVIING TLKALAGPNH SSTFKVVLEA ENINTLQSEG PELTEIDKEN IKKVMKEENP
INLFSKSIAP SIYGHSDVKK AILLMLVGAT PKIRLRSRVR GDIHVMLCGD PSTAKSQLLR
YVMSIAPLAV STNGRGATGV GLTAAVVNDP DTNQRTLEAG AMVLADRGIC CVDEFDKMSI
EDRAAMHEVM EQQTVTVQKA GIHTGIKCKM SILAAANPSN GNYDFKKSPM ENLYFPESLL
SRFDLIFIIL DSSTEELDRK LSQHVLKMHR HFDALTEQRG DDEVNVLALV DAEREKIGDA
PVYQDSLCMK EKNYLLINSL KNMLLMLEIS PTPSLSESAS ETIADAYVKL RENERLKRIK
HNFKIKTLPI TARALDSLIR LAEAHARIRG SDTIDEIDAQ VAVQLILMKI WEGNITTHIA
RKVREYLTNE LIAECKDVIQ FDDILSICGI DKPTLMKILP QLSFGYDEDE EFVYKQN