ID W7JI03_PLAFA Unreviewed; 929 AA.
AC W7JI03;
DT 16-APR-2014, integrated into UniProtKB/TrEMBL.
DT 16-APR-2014, sequence version 1.
DT 27-MAR-2024, entry version 53.
DE RecName: Full=DNA replication licensing factor MCM6 {ECO:0000256|RuleBase:RU368064};
DE EC=3.6.4.12 {ECO:0000256|RuleBase:RU368064};
GN ORFNames=C923_04923 {ECO:0000313|EMBL:EWC74429.1};
OS Plasmodium falciparum UGT5.1.
OC Eukaryota; Sar; Alveolata; Apicomplexa; Aconoidasida; Haemosporida;
OC Plasmodiidae; Plasmodium; Plasmodium (Laverania).
OX NCBI_TaxID=1237627 {ECO:0000313|EMBL:EWC74429.1, ECO:0000313|Proteomes:UP000030697};
RN [1] {ECO:0000313|EMBL:EWC74429.1, ECO:0000313|Proteomes:UP000030697}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=UGT5.1 {ECO:0000313|EMBL:EWC74429.1,
RC ECO:0000313|Proteomes:UP000030697};
RG The Broad Institute Genome Sequencing Platform;
RG The Broad Institute Genome Sequencing Center for Infectious Disease;
RA Neafsey D., Cheeseman I., Volkman S., Adams J., Walker B., Young S.K.,
RA Zeng Q., Gargeya S., Fitzgerald M., Haas B., Abouelleil A., Alvarado L.,
RA Arachchi H.M., Berlin A.M., Chapman S.B., Dewar J., Goldberg J., Griggs A.,
RA Gujja S., Hansen M., Howarth C., Imamovic A., Larimer J., McCowan C.,
RA Murphy C., Neiman D., Pearson M., Priest M., Roberts A., Saif S., Shea T.,
RA Sisk P., Sykes S., Wortman J., Nusbaum C., Birren B.;
RT "The Genome Sequence of Plasmodium falciparum UGT5.1.";
RL Submitted (FEB-2013) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Acts as component of the MCM2-7 complex (MCM complex) which
CC is the replicative helicase essential for 'once per cell cycle' DNA
CC replication initiation and elongation in eukaryotic cells. The active
CC ATPase sites in the MCM2-7 ring are formed through the interaction
CC surfaces of two neighboring subunits such that a critical structure of
CC a conserved arginine finger motif is provided in trans relative to the
CC ATP-binding site of the Walker A box of the adjacent subunit. The six
CC ATPase active sites, however, are likely to contribute differentially
CC to the complex helicase activity. {ECO:0000256|RuleBase:RU368064}.
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 Evidence={ECO:0000256|RuleBase:RU368064};
CC -!- SUBUNIT: Component of the MCM2-7 complex.
CC {ECO:0000256|RuleBase:RU368064}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|RuleBase:RU368064}.
CC -!- SIMILARITY: Belongs to the MCM family. {ECO:0000256|ARBA:ARBA00008010,
CC ECO:0000256|RuleBase:RU004070}.
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DR EMBL; KE124707; EWC74429.1; -; Genomic_DNA.
DR AlphaFoldDB; W7JI03; -.
DR SMR; W7JI03; -.
DR EnsemblProtists; EWC74429; EWC74429; C923_04923.
DR Proteomes; UP000030697; Unassembled WGS sequence.
DR GO; GO:0042555; C:MCM complex; IEA:UniProtKB-UniRule.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
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:InterPro.
DR GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR GO; GO:0006270; P:DNA replication initiation; IEA:UniProtKB-UniRule.
DR CDD; cd17757; MCM6; 1.
DR Gene3D; 1.20.58.870; -; 1.
DR Gene3D; 2.20.28.10; -; 1.
DR Gene3D; 2.40.50.140; Nucleic acid-binding proteins; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR InterPro; IPR031327; MCM.
DR InterPro; IPR008049; MCM6.
DR InterPro; IPR041024; Mcm6_C.
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; DNA REPLICATION LICENSING FACTOR MCM FAMILY MEMBER; 1.
DR PANTHER; PTHR11630:SF43; DNA REPLICATION LICENSING FACTOR MCM6; 1.
DR Pfam; PF00493; MCM; 1.
DR Pfam; PF18263; MCM6_C; 1.
DR Pfam; PF17855; MCM_lid; 1.
DR Pfam; PF17207; MCM_OB; 1.
DR PRINTS; PR01657; MCMFAMILY.
DR PRINTS; PR01662; MCMPROTEIN6.
DR SMART; SM00350; MCM; 1.
DR SUPFAM; SSF50249; Nucleic acid-binding proteins; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR PROSITE; PS00847; MCM_1; 1.
DR PROSITE; PS50051; MCM_2; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|RuleBase:RU004070};
KW Cell cycle {ECO:0000256|RuleBase:RU368064};
KW DNA replication {ECO:0000256|RuleBase:RU368064};
KW DNA-binding {ECO:0000256|ARBA:ARBA00023125, ECO:0000256|RuleBase:RU004070};
KW Helicase {ECO:0000256|ARBA:ARBA00022806, ECO:0000256|RuleBase:RU368064};
KW Hydrolase {ECO:0000256|RuleBase:RU368064};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW ECO:0000256|RuleBase:RU004070};
KW Reference proteome {ECO:0000313|Proteomes:UP000030697}.
FT DOMAIN 436..641
FT /note="MCM"
FT /evidence="ECO:0000259|PROSITE:PS50051"
FT REGION 1..68
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 45..64
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 929 AA; 105674 MW; 57F7E456F09FBD3D CRC64;
MSAIFNESEL SGLDAHSAFG NNETSSFQKK KRRIDENSQM SVNDLVDDGE EEEDDDDDEE
EPSYVQDQNM AKVFEKFLKT FSEKKSEEDD DDGDSIWKDS LNFDFPSNLE IAKDSHYVLL
LFSILQNSYS RNKVLIVDMK HVLMWEPTDK NRFDIGSQLY MYIKRHFLRI LDIFEKKVQL
LAESINPIKT KEVGKICLRF YNKKNPIHSL RSLRCEMLGE MISVRGQVTR TSDVRPELTL
AAFKCNECGN IINGVKQQFR YTQPSKCPSA SCSNMSDWSL VLEQSYFVDW QKIRLQEIAQ
ESPPGSMPRN MDVILRNDIV DSVHAGDRII VTGCLIVVPD IPTLMKPGDV PRSVARQLLK
KNENSLVSQG LTGIKGVGVQ DLNHKLCIYA CQIEKLNSSK KDNNFDEQTQ VDINCEEILN
CDDLKWLRDI AMHPNTIDIL AECIAPKIWG NLEIKKGALL MMTGGVQKIT SNCKLRGDIN
MCIVGDPGTA KSEILKYVES FAPRAIFTSG KGSTAAGLTA AVHRDPDQGD TVLEAGALMY
ADQGICCIDE FDKMDEKDRV AIHEAMEQQT ISITKAGIQA TLNARASVLA ACNPKYGRYD
TLKTFAQNVN IPAPLLSRFD LFYTMLDCID IDKDTSIANH LVSMHCGEEA EKHLRANAGK
LDSVKLEIYL ELSKRVKPLL TDEAKYKLIQ YYVSFRNIEY SPGAQRSMRM TVRQLESLIR
LSEAVAKLKF SHFVDVKHVE IACSIFKASM KKISNEKEIN LDEEFDKVNN SLMGNKVNKL
DQETENTEQN KKITTIKASE YQYISAIIFE IIKEYEFNNN NESITQDQLI ETYLQVYAKA
ESSEQVDEWI YKLKKIINRL INQDIKLLSE TNEDDPEKVI IRIHPNYAGP IVEGVSNKNT
YGYNTFKNYQ TQEKAPEDDV DFQEEIDNF
//
