ID W4ITE4_PLAFP Unreviewed; 923 AA.
AC W4ITE4;
DT 19-MAR-2014, integrated into UniProtKB/TrEMBL.
DT 19-MAR-2014, sequence version 1.
DT 27-MAR-2024, entry version 54.
DE RecName: Full=DNA replication licensing factor MCM3 {ECO:0000256|RuleBase:RU368061};
DE EC=3.6.4.12 {ECO:0000256|RuleBase:RU368061};
DE Flags: Fragment;
GN ORFNames=PFUGPA_04385 {ECO:0000313|EMBL:ETW53370.1};
OS Plasmodium falciparum (isolate Palo Alto / Uganda).
OC Eukaryota; Sar; Alveolata; Apicomplexa; Aconoidasida; Haemosporida;
OC Plasmodiidae; Plasmodium; Plasmodium (Laverania).
OX NCBI_TaxID=57270 {ECO:0000313|EMBL:ETW53370.1, ECO:0000313|Proteomes:UP000019103};
RN [1] {ECO:0000313|EMBL:ETW53370.1, ECO:0000313|Proteomes:UP000019103}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Palo Alto/Uganda {ECO:0000313|EMBL:ETW53370.1,
RC ECO:0000313|Proteomes:UP000019103};
RG The Broad Institute Genome Sequencing Platform;
RG The Broad Institute Genome Sequencing Center for Infectious Disease;
RA Neafsey D., Hoffman S., Volkman S., Rosenthal P., Walker B., Young S.K.,
RA Zeng Q., Gargeya S., Fitzgerald M., Haas B., Abouelleil A., Allen A.W.,
RA Alvarado L., Arachchi H.M., Berlin A.M., Chapman S.B., Gainer-Dewar J.,
RA Goldberg J., Griggs A., Gujja S., Hansen M., Howarth C., Imamovic A.,
RA Ireland A., Larimer J., McCowan C., Murphy C., Pearson M., Poon T.W.,
RA Priest M., Roberts A., Saif S., Shea T., Sisk P., Sykes S., Wortman J.,
RA Nusbaum C., Birren B.;
RT "The Genome Annotation of Plasmodium falciparum Palo Alto/Uganda.";
RL Submitted (FEB-2013) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:ETW53370.1, ECO:0000313|Proteomes:UP000019103}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Palo Alto/Uganda {ECO:0000313|EMBL:ETW53370.1,
RC ECO:0000313|Proteomes:UP000019103};
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 Palo Alto/Uganda.";
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: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; KI927385; ETW53370.1; -; Genomic_DNA.
DR AlphaFoldDB; W4ITE4; -.
DR EnsemblProtists; ETW53370; ETW53370; PFUGPA_04385.
DR OMA; WNDTLDM; -.
DR Proteomes; UP000019103; 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: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};
KW Reference proteome {ECO:0000313|Proteomes:UP000019103}.
FT DOMAIN 392..597
FT /note="MCM"
FT /evidence="ECO:0000259|PROSITE:PS50051"
FT REGION 791..876
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 791..818
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 837..858
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 859..874
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT NON_TER 923
FT /evidence="ECO:0000313|EMBL:ETW53370.1"
SQ SEQUENCE 923 AA; 105379 MW; 8FAF51993CEAA585 CRC64;
MESLSIEKNS TPFGRSEYRT FNSELNYTLM DSSLNHSSIL DNSMKIEKDS RDKRLQKLNQ
NIVSEYESGR QSVVFTQQKY KQLLEGFLLF VQTNKYIHQK ITELRTEAID EYNRMQNKNI
PNIIIHQRLI CNINNFQTGN EQFELLAKCL IKEPYLALPA YQAAIKELWK SEDSKVDIDP
PKIGICGWLG RHHVTPRGLQ SSMINKLVAV EGVVNKCSTV QPKLVQSVYI GEAVHDMNAD
AKTSEKTVHL RPHYDITDFD KTAKDSGRPP ASDPEGRIMH KHEIGLCKYK NHQKFVIQET
PEDAPTGQMP RWVEVIVEDD LCDIVKCGDR VRVWGVYRAN CGQANSTNSG LGRSFLIANN
VLVKNKETYD SNLCISEADK KNFHAFAKKD NTIDILGYSF APSICGQDIV KKAIVLMLAG
GTERALPSHH IRGDIHIMLV GDPSCGKSQL LRYVMSIMPG TVSATGRGSS GVGLTAAIVT
DQDTGERVVE GGAMVMGDRR VVCIDEFDKM QPTDRVAIHE VMEQQTVTVA KAGIHTTLNA
RCTVLAAANP LYGCWNDALD MGQQLQFEPS LLSRFDLIFL VRDSATEQDD ERIAESVLRN
VTEKAKPIMN ESRNNQKNFV IQADSYDINP KAQHISIYNE RDINQNNDSN NMQENEEYET
PIFANRDEMI YYDKNGVEHE ILTVPFFKKY LHYVKNIFYH EKQRTDGWKP YPEVSDEACE
VITELYADLR ERASKYSHNK LIQGVTPRTL EAIIRIASSH AKLKLNRYVT SVDVNYAKKL
LMYTLFGEEI IDSNEEDEEE DEEEEDELEE DEEDDDDEEE KLKKKRRQRQ KRASRKRSGE
KKDLASNKKK KKKSEQPNEN GNENYMIDDL PSNKSNDTLD IKEIERLIVE NVTLNDPGDG
LKDVELLDLV QKKKKKKKNI YIY
//
