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Database: UniProt
Entry: A0A090N4N3_OSTTA
LinkDB: A0A090N4N3_OSTTA
Original site: A0A090N4N3_OSTTA 
ID   A0A090N4N3_OSTTA        Unreviewed;       710 AA.
AC   A0A090N4N3;
DT   26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT   26-NOV-2014, sequence version 1.
DT   27-MAR-2024, entry version 48.
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=OT_ostta02g02010 {ECO:0000313|EMBL:CEG01010.1};
OS   Ostreococcus tauri.
OC   Eukaryota; Viridiplantae; Chlorophyta; Mamiellophyceae; Mamiellales;
OC   Bathycoccaceae; Ostreococcus.
OX   NCBI_TaxID=70448 {ECO:0000313|EMBL:CEG01010.1, ECO:0000313|Proteomes:UP000009170};
RN   [1] {ECO:0000313|Proteomes:UP000009170}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=OTTH0595 {ECO:0000313|Proteomes:UP000009170};
RX   PubMed=16868079; DOI=10.1073/pnas.0604795103;
RA   Derelle E., Ferraz C., Rombauts S., Rouze P., Worden A.Z., Robbens S.,
RA   Partensky F., Degroeve S., Echeynie S., Cooke R., Saeys Y., Wuyts J.,
RA   Jabbari K., Bowler C., Panaud O., Piegu B., Ball S.G., Ral J.-P.,
RA   Bouget F.-Y., Piganeau G., De Baets B., Picard A., Delseny M., Demaille J.,
RA   Van de Peer Y., Moreau H.;
RT   "Genome analysis of the smallest free-living eukaryote Ostreococcus tauri
RT   unveils many unique features.";
RL   Proc. Natl. Acad. Sci. U.S.A. 103:11647-11652(2006).
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|ARBA:ARBA00001665,
CC         ECO:0000256|RuleBase:RU365012};
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123,
CC       ECO:0000256|RuleBase:RU365012}.
CC   -!- SIMILARITY: Belongs to the MCM family. {ECO:0000256|RuleBase:RU004070}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:CEG01010.1}.
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DR   EMBL; CAID01000002; CEG01010.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A090N4N3; -.
DR   STRING; 70448.A0A090N4N3; -.
DR   InParanoid; A0A090N4N3; -.
DR   OrthoDB; 147095at2759; -.
DR   Proteomes; UP000009170; Chromosome 2.
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:InterPro.
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   GO; GO:0006268; P:DNA unwinding involved in DNA replication; IEA:UniProt.
DR   CDD; cd17758; MCM7; 1.
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; IPR003593; AAA+_ATPase.
DR   InterPro; IPR031327; MCM.
DR   InterPro; IPR008050; MCM7.
DR   InterPro; IPR018525; MCM_CS.
DR   InterPro; IPR001208; MCM_dom.
DR   InterPro; IPR041562; MCM_lid.
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; PF17855; MCM_lid; 1.
DR   Pfam; PF14551; MCM_N; 1.
DR   Pfam; PF17207; MCM_OB; 1.
DR   PRINTS; PR01657; MCMFAMILY.
DR   PRINTS; PR01663; MCMPROTEIN7.
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; 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|ARBA:ARBA00023125, 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:UP000009170}.
FT   DOMAIN          319..525
FT                   /note="MCM"
FT                   /evidence="ECO:0000259|PROSITE:PS50051"
SQ   SEQUENCE   710 AA;  78720 MW;  CCE2848B223C2EE2 CRC64;
     MSEEVYAHDR ELIRGFLETF KSGAAKPLYI IAMQEIIDRQ SCSMQIELQH VKEFSEAERD
     QLVRRVVSNC KRYSTIFAEE IDKIMARMIE SSSMHPDDTA DIVLRHHFGD HRNGSAAPGS
     LRRHFDVFFK PATGTTPIKM REIRAKMIGK YVTFKGMCTR LTDVKPLMEV ACYTCEGCGQ
     EYFQEVTDTQ FIPIQFCQSQ TCNKNFALFI ETRASKFAKY QELRIQELSE DVPVGHVPRS
     MSVTLIGDMT RKLSPGDIAN ISGIFLPRQS AGYSGSSSLV STTYLYAMSV EPLKSQQAES
     EETPELIKRL KDISEIPDIY TYLAKSIAPE IYGHVDVKKA LLLLLCGGVT RKLPDGVKIR
     GDIHVCLMGD PGVAKSQLLK HIVSIAPRAV YTTGRGSSGV GLTASIQRDT VTTELILEGG
     ALVLADRGIC CIDEFDKMDE SDRTAIHEVM EQQTVSIAKA GITTTLNART TVLAAANPAF
     GRYNTSATPQ ENINLPAALL SRFDLMWLIL DTPDPDSDVE LARHVMCVHR EGRPPLNSFN
     PASASELRTY ISIARRFEPY IPEDVSDSIA GAYVGIRQAE DEAGNEATGY TTARTLLSII
     RLAEALARLR WSTVVYEKDV EQALKLMKMS KASLDMQKAA TAQLSDPIET LFLILRNWAG
     ENSSELITCT VAHQLAAKNS LLDVLSTCLT EYTALGVWVT DAENNITFIE
//
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