ID W7AUK3_PLAVN Unreviewed; 950 AA.
AC W7AUK3;
DT 16-APR-2014, integrated into UniProtKB/TrEMBL.
DT 16-APR-2014, sequence version 1.
DT 24-JAN-2024, entry version 49.
DE RecName: Full=DNA replication licensing factor MCM3 {ECO:0000256|RuleBase:RU368061};
DE EC=3.6.4.12 {ECO:0000256|RuleBase:RU368061};
GN ORFNames=PVPCR_1204270 {ECO:0000313|EMBL:CAD2110512.1}, YYG_02160
GN {ECO:0000313|EMBL:EUD72259.1};
OS Plasmodium vinckei petteri.
OC Eukaryota; Sar; Alveolata; Apicomplexa; Aconoidasida; Haemosporida;
OC Plasmodiidae; Plasmodium; Plasmodium (Vinckeia).
OX NCBI_TaxID=138298 {ECO:0000313|EMBL:EUD72259.1, ECO:0000313|Proteomes:UP000030659};
RN [1] {ECO:0000313|EMBL:EUD72259.1, ECO:0000313|Proteomes:UP000030659}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CR {ECO:0000313|EMBL:EUD72259.1,
RC ECO:0000313|Proteomes:UP000030659};
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 vinckei petteri CR.";
RL Submitted (FEB-2013) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:CAD2110512.1, ECO:0000313|Proteomes:UP000515268}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Ramaprasad A.;
RL Submitted (AUG-2020) 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:RU368061}.
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:RU368061};
CC -!- SUBUNIT: Component of the MCM2-7 complex.
CC {ECO:0000256|RuleBase:RU368061}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|RuleBase:RU368061}.
CC -!- SIMILARITY: Belongs to the MCM family. {ECO:0000256|RuleBase:RU004070}.
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DR EMBL; LR865417; CAD2110512.1; -; Genomic_DNA.
DR EMBL; KI965398; EUD72259.1; -; Genomic_DNA.
DR AlphaFoldDB; W7AUK3; -.
DR EnsemblProtists; EUD72259; EUD72259; YYG_02160.
DR VEuPathDB; PlasmoDB:PVPCR_1204270; -.
DR eggNOG; KOG0479; Eukaryota.
DR OrthoDB; 147095at2759; -.
DR Proteomes; UP000030659; Unassembled WGS sequence.
DR Proteomes; UP000515268; Chromosome PVPCR_12.
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:InterPro.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0004386; F:helicase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0032508; P:DNA duplex unwinding; IEA:UniProtKB-UniRule.
DR GO; GO:0006270; P:DNA replication initiation; IEA:InterPro.
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; IPR003593; AAA+_ATPase.
DR InterPro; IPR031327; MCM.
DR InterPro; IPR008046; Mcm3.
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:SF46; DNA REPLICATION LICENSING FACTOR MCM3; 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; SM00382; AAA; 1.
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; PS50051; MCM_2; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|RuleBase:RU004070};
KW DNA replication {ECO:0000256|RuleBase:RU368061};
KW DNA-binding {ECO:0000256|ARBA:ARBA00023125, ECO:0000256|RuleBase:RU004070};
KW Helicase {ECO:0000256|RuleBase:RU368061};
KW Hydrolase {ECO:0000256|RuleBase:RU368061};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW ECO:0000256|RuleBase:RU004070}; Nucleus {ECO:0000256|RuleBase:RU368061}.
FT DOMAIN 393..598
FT /note="MCM"
FT /evidence="ECO:0000259|PROSITE:PS50051"
FT REGION 795..871
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 795..815
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 824..839
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 840..859
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 950 AA; 108076 MW; F1D37C208940A465 CRC64;
MENLSIQKSV TPSRRSDFRA YNNSLINYTL MDSSINNSSI LDNSMRLDKE NKERKLQKIN
DNIISEYESG RQSVVFTQQK YKQLLEGFLL FVQTNKYIHQ KITELRADAT EEYNKMVDKN
IPNIIIHQRL ICNINNFQTG NEQFELLAKC LIKEPYLALP AYQAAIKELW KSQDSKIDIE
CPKIGISGWL GRHHVTPRGL QSSMINKLVA VEGVVNKCST VQPKLVQSVY IGEAVHDINA
DVRSEEKTVH LRPHYDITDF DKTAKDSGRP PASDPEGKIM HRHEIGLCKY KNHQKFVIQE
TPEDAPTGQM PRWVEVIVED DLCDIVKCGD RVRVWGVYRA SCGQANSTNS GLGRSFLIAN
NVLVKNKETY DTNLFISEAD KKNFHAFAKK QNTIDILGYS FAPSICGQDV VKKGIVLMLA
GGTERALPSH HIRGDIHIML VGDPSCGKSQ LLRYVMSIMP GTVSATGRGS SGVGLTAAIV
TDQDTGERVV EGGAMVMGDR RVVCIDEFDK MQQTDRVAIH EVMEQQTVTV AKAGIHTTLN
ARCTVLAAAN PLYGCWNDSL DMGQQLQFEP SLLSRFDLIF LVRDSTTEKD DERIAESVLR
NVTEKAKPIL NENRNSQKNF VIQADSYDIN QKAQHISIYN EREVNNNNNN DPNNSQDNEE
FETPIFANRD EMIYYDKDGV EHEILTVPFF KKYLHYVKNV FYNEKQRTDG WKPYPEVSDE
ACEVITELYA DLREKAAKYS HNKIIQGVTP RTLEAIIRIA SSHAKLKLNR YVTSVDVNYA
KKLLMYTLFG EEIVESEDEY EEDEEEEDYE DDDDEEYVHK PINKKNKTKA KKRTAEKQTT
SRKKNKTNKS KDNQDDNLMI DDHQSASTKA TPLDVREIER LIVENVTLND PGDGLRDEAL
LDLIILGNKD KMPHLAKLDI ATLRKIINSL NEMDGAPIYY VKKDRIVYKC
//
