ID A0A1E7FF50_9STRA Unreviewed; 626 AA.
AC A0A1E7FF50;
DT 18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT 18-JAN-2017, sequence version 1.
DT 24-JAN-2024, entry version 28.
DE RecName: Full=DNA replication licensing factor MCM4 {ECO:0000256|RuleBase:RU368062};
DE EC=3.6.4.12 {ECO:0000256|RuleBase:RU368062};
DE Flags: Fragment;
GN ORFNames=FRACYDRAFT_146869 {ECO:0000313|EMBL:OEU16801.1};
OS Fragilariopsis cylindrus CCMP1102.
OC Eukaryota; Sar; Stramenopiles; Ochrophyta; Bacillariophyta;
OC Bacillariophyceae; Bacillariophycidae; Bacillariales; Bacillariaceae;
OC Fragilariopsis.
OX NCBI_TaxID=635003 {ECO:0000313|EMBL:OEU16801.1, ECO:0000313|Proteomes:UP000095751};
RN [1] {ECO:0000313|EMBL:OEU16801.1, ECO:0000313|Proteomes:UP000095751}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CCMP1102 {ECO:0000313|EMBL:OEU16801.1,
RC ECO:0000313|Proteomes:UP000095751};
RG DOE Joint Genome Institute;
RA Mock T., Otillar R.P., Strauss J., Dupont C., Frickenhaus S., Maumus F.,
RA Mcmullan M., Sanges R., Schmutz J., Toseland A., Valas R., Veluchamy A.,
RA Ward B.J., Allen A., Barry K., Falciatore A., Ferrante M., Fortunato A.E.,
RA Gloeckner G., Gruber A., Hipkin R., Janech M., Kroth P., Leese F.,
RA Lindquist E., Lyon B.R., Martin J., Mayer C., Parker M., Quesneville H.,
RA Raymond J., Uhlig C., Valentin K.U., Worden A.Z., Armbrust E.V., Bowler C.,
RA Green B., Moulton V., Van Oosterhout C., Grigoriev I.;
RT "Extensive genetic diversity and differential bi-allelic expression allows
RT diatom success in the polar Southern Ocean.";
RL Submitted (SEP-2016) 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:RU368062}.
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:RU368062};
CC -!- SUBUNIT: Component of the MCM2-7 complex.
CC {ECO:0000256|RuleBase:RU368062}.
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast
CC {ECO:0000256|ARBA:ARBA00004229}.
CC -!- SIMILARITY: Belongs to the MCM family. {ECO:0000256|ARBA:ARBA00008010,
CC ECO:0000256|RuleBase:RU004070}.
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DR EMBL; KV784358; OEU16801.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1E7FF50; -.
DR EnsemblProtists; OEU16801; OEU16801; FRACYDRAFT_146869.
DR KEGG; fcy:FRACYDRAFT_146869; -.
DR InParanoid; A0A1E7FF50; -.
DR OrthoDB; 5476523at2759; -.
DR Proteomes; UP000095751; Unassembled WGS sequence.
DR GO; GO:0009507; C:chloroplast; IEA:UniProtKB-SubCell.
DR GO; GO:0042555; C:MCM complex; IEA:UniProtKB-UniRule.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-KW.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0003678; F:DNA helicase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
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; IPR031327; MCM.
DR InterPro; IPR008047; MCM_4.
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:SF66; DNA REPLICATION LICENSING FACTOR MCM4; 1.
DR Pfam; PF00493; MCM; 1.
DR Pfam; PF21128; MCM4_WHD; 1.
DR Pfam; PF17855; MCM_lid; 1.
DR Pfam; PF17207; MCM_OB; 1.
DR PRINTS; PR01657; MCMFAMILY.
DR PRINTS; PR01660; MCMPROTEIN4.
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 DNA replication {ECO:0000256|RuleBase:RU368062};
KW DNA-binding {ECO:0000256|ARBA:ARBA00023125, ECO:0000256|RuleBase:RU004070};
KW Helicase {ECO:0000256|ARBA:ARBA00022806, ECO:0000256|RuleBase:RU368062};
KW Hydrolase {ECO:0000256|RuleBase:RU368062};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW ECO:0000256|RuleBase:RU004070}; Nucleus {ECO:0000256|RuleBase:RU368062};
KW Reference proteome {ECO:0000313|Proteomes:UP000095751}.
FT DOMAIN 212..420
FT /note="MCM"
FT /evidence="ECO:0000259|PROSITE:PS50051"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:OEU16801.1"
FT NON_TER 626
FT /evidence="ECO:0000313|EMBL:OEU16801.1"
SQ SEQUENCE 626 AA; 69435 MW; 906179399FC4F463 CRC64;
LPQIQVRPFN MKEVANLRCL DPIAMDTLVA LKGMIVRCSP IIPDLKVAHF SCCVCGHDHQ
VSIDRGRVEE PKQCPSCNTK DSYTLIHNRC IFADKQLVRL QETPDQVPAG QTPASCITFC
FDDLVDSCQP GDKVEVTGIL KAQPVRVNPK VTKLKSIYKT YVDVIHFRTI TGMEGKTGAG
GTGNTNKSKR GVMKLTKDRV QELVELSQRP DIYERLTQSL APSIWELDNV KKGVLCMMFG
GNHKRVKKHT KLCKRGDINI LLCGDPGTSK SQLLSYVHKL SSRGIYTSGK GSSAVGLTAS
VVRDPETRDL VLESGALVLS DRGICCIDEF DKMSDATRSI LHEAMEQQTV SIAKAGIISS
LNARTSILAS ANPVESRYNP NLSVVENIKL PPTLLSRFDL IYLILDAPNV DSDRKLAQHL
VGLYYEKPNV VTPPMDTELL RNYIDYAREH IHPRLSDEAS EELLTSYLEL RNPPGGNVGN
NGTRTISATP RQLESLIRTS EALAKMKYSS VVSRADAKEA VRLLKVATQA AATDPRTGRI
DMDMINTGRT EVERDMEESL YVGLKEFLIE RRGNRLAVRD VTRQLSEISN TQVPQDDVAT
ALRRLEADGM VQFNERNQSV FVRTGI
//
