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Database: UniProt
Entry: F0YGS7_AURAN
LinkDB: F0YGS7_AURAN
Original site: F0YGS7_AURAN 
ID   F0YGS7_AURAN            Unreviewed;       577 AA.
AC   F0YGS7;
DT   03-MAY-2011, integrated into UniProtKB/TrEMBL.
DT   03-MAY-2011, sequence version 1.
DT   27-MAR-2024, entry version 68.
DE   RecName: Full=DNA replication licensing factor MCM7 {ECO:0000256|RuleBase:RU365012};
DE            EC=3.6.4.12 {ECO:0000256|RuleBase:RU365012};
GN   Name=MCM7 {ECO:0000256|RuleBase:RU365012};
GN   ORFNames=AURANDRAFT_72178 {ECO:0000313|EMBL:EGB05751.1};
OS   Aureococcus anophagefferens (Harmful bloom alga).
OC   Eukaryota; Sar; Stramenopiles; Ochrophyta; Pelagophyceae; Pelagomonadales;
OC   Aureococcus.
OX   NCBI_TaxID=44056 {ECO:0000313|Proteomes:UP000002729};
RN   [1] {ECO:0000313|EMBL:EGB05751.1, ECO:0000313|Proteomes:UP000002729}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CCMP 1984 {ECO:0000313|Proteomes:UP000002729};
RX   PubMed=21368207; DOI=10.1073/pnas.1016106108;
RA   Gobler C.J., Berry D.L., Dyhrman S.T., Wilhelm S.W., Salamov A.,
RA   Lobanov A.V., Zhang Y., Collier J.L., Wurch L.L., Kustka A.B., Dill B.D.,
RA   Shah M., VerBerkmoes N.C., Kuo A., Terry A., Pangilinan J., Lindquist E.A.,
RA   Lucas S., Paulsen I.T., Hattenrath-Lehmann T.K., Talmage S.C., Walker E.A.,
RA   Koch F., Burson A.M., Marcoval M.A., Tang Y.Z., Lecleir G.R., Coyne K.J.,
RA   Berg G.M., Bertrand E.M., Saito M.A., Gladyshev V.N., Grigoriev I.V.;
RT   "Niche of harmful alga Aureococcus anophagefferens revealed through
RT   ecogenomics.";
RL   Proc. Natl. Acad. Sci. U.S.A. 108:4352-4357(2011).
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:RU365012}.
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:RU365012};
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123,
CC       ECO:0000256|RuleBase:RU365012}. Plastid, chloroplast
CC       {ECO:0000256|ARBA:ARBA00004229}.
CC   -!- SIMILARITY: Belongs to the MCM family. {ECO:0000256|RuleBase:RU004070}.
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DR   EMBL; GL833139; EGB05751.1; -; Genomic_DNA.
DR   RefSeq; XP_009039590.1; XM_009041342.1.
DR   AlphaFoldDB; F0YGS7; -.
DR   EnsemblProtists; EGB05751; EGB05751; AURANDRAFT_72178.
DR   GeneID; 20228585; -.
DR   KEGG; aaf:AURANDRAFT_72178; -.
DR   eggNOG; KOG0482; Eukaryota.
DR   InParanoid; F0YGS7; -.
DR   OMA; IRAPSKW; -.
DR   OrthoDB; 147095at2759; -.
DR   Proteomes; UP000002729; Unassembled WGS sequence.
DR   GO; GO:0009507; C:chloroplast; IEA:UniProtKB-SubCell.
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:InterPro.
DR   GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR   GO; GO:0006270; P:DNA replication initiation; IEA:InterPro.
DR   Gene3D; 2.20.28.10; -; 1.
DR   Gene3D; 3.30.1640.10; mini-chromosome maintenance (MCM) complex, chain A, domain 1; 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; IPR008050; MCM7.
DR   InterPro; IPR018525; MCM_CS.
DR   InterPro; IPR001208; MCM_dom.
DR   InterPro; IPR027925; MCM_N.
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:SF26; DNA REPLICATION LICENSING FACTOR MCM7; 1.
DR   Pfam; PF00493; MCM; 1.
DR   Pfam; PF14551; MCM_N; 1.
DR   Pfam; PF17207; MCM_OB; 1.
DR   PRINTS; PR01657; MCMFAMILY.
DR   PRINTS; PR01663; MCMPROTEIN7.
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|ARBA:ARBA00023306, ECO:0000256|RuleBase:RU365012};
KW   DNA replication {ECO:0000256|ARBA:ARBA00022705,
KW   ECO:0000256|RuleBase:RU365012};
KW   DNA-binding {ECO:0000256|RuleBase:RU004070};
KW   Helicase {ECO:0000256|ARBA:ARBA00022806, ECO:0000256|RuleBase:RU365012};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU365012};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW   ECO:0000256|RuleBase:RU004070};
KW   Nucleus {ECO:0000256|ARBA:ARBA00023242, ECO:0000256|RuleBase:RU365012};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002729}.
FT   DOMAIN          347..553
FT                   /note="MCM"
FT                   /evidence="ECO:0000259|PROSITE:PS50051"
SQ   SEQUENCE   577 AA;  63798 MW;  19C25FC59FD31E03 CRC64;
     MDVETNTLRN FLSRFCDKSL PQSKQDKYIQ ALHAINLRQS RVLIIELDDL IQYLKDDVGD
     LVHGVVKNAK RYVNIFDGIA TEMLQQMDSA SPERVDVFDE LQRQRKHQMA VMQASGERNS
     IASERGEFLE SNRLSTVDEF PTALLRRHET RLLPTASSPA GALRGLRACD IGRLVKVCGI
     VTRTSDVKPL VEVVTYTCET CGCEVYDDVS RKKNFLPLSK CTSKRCNANK MGGRLFAQTR
     GSKFVKYQEL RVQELPLHVP VGHVPRSITV HCRGELTRQC APGDTVTLSG IFLPQRFSGF
     RGMKAGLISD TFLEAMSVDK EKKNYSEIEA DDKVDALIDD VADSPDAYSR LSRSIAPEIF
     GHEDVKRALL LQLVGGVTRT LGDGVRLRGD VNICLMGDPG VAKSQLLKSI ASTSPRGVYT
     TGKGSSGVGL TAAVVRDATT SEMSLEGGAL VLADCGICCI DEFDKMDEHD RTAIHEVMEQ
     QTVSIAKAGI TTTLNARSAV LAAANPLYGR YNKKKTMAEN INLPNSLLSR FDLLFLLLDK
     PEVEADIALA RHVTHVHRFL SNPDLDFEPY DSVFIRQ
//
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