ID Q54RU0_DICDI Unreviewed; 789 AA.
AC Q54RU0;
DT 24-MAY-2005, integrated into UniProtKB/TrEMBL.
DT 24-MAY-2005, sequence version 1.
DT 24-JAN-2024, entry version 142.
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 Synonyms=mcm7 {ECO:0000313|EMBL:EAL65910.1};
GN ORFNames=DDB_G0282933 {ECO:0000313|EMBL:EAL65910.1};
OS Dictyostelium discoideum (Social amoeba).
OC Eukaryota; Amoebozoa; Evosea; Eumycetozoa; Dictyostelia; Dictyosteliales;
OC Dictyosteliaceae; Dictyostelium.
OX NCBI_TaxID=44689 {ECO:0000313|EMBL:EAL65910.1, ECO:0000313|Proteomes:UP000002195};
RN [1] {ECO:0000313|EMBL:EAL65910.1, ECO:0000313|Proteomes:UP000002195}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AX4 {ECO:0000313|EMBL:EAL65910.1,
RC ECO:0000313|Proteomes:UP000002195};
RX PubMed=15875012; DOI=10.1038/nature03481;
RG The Dictyostelium discoideum Sequencing Consortium;
RA Eichinger L., Pachebat J.A., Glockner G., Rajandream M.A., Sucgang R.,
RA Berriman M., Song J., Olsen R., Szafranski K., Xu Q., Tunggal B.,
RA Kummerfeld S., Madera M., Konfortov B.A., Rivero F., Bankier A.T.,
RA Lehmann R., Hamlin N., Davies R., Gaudet P., Fey P., Pilcher K., Chen G.,
RA Saunders D., Sodergren E., Davis P., Kerhornou A., Nie X., Hall N.,
RA Anjard C., Hemphill L., Bason N., Farbrother P., Desany B., Just E.,
RA Morio T., Rost R., Churcher C., Cooper J., Haydock S., van Driessche N.,
RA Cronin A., Goodhead I., Muzny D., Mourier T., Pain A., Lu M., Harper D.,
RA Lindsay R., Hauser H., James K., Quiles M., Madan Babu M., Saito T.,
RA Buchrieser C., Wardroper A., Felder M., Thangavelu M., Johnson D.,
RA Knights A., Loulseged H., Mungall K., Oliver K., Price C., Quail M.A.,
RA Urushihara H., Hernandez J., Rabbinowitsch E., Steffen D., Sanders M.,
RA Ma J., Kohara Y., Sharp S., Simmonds M., Spiegler S., Tivey A., Sugano S.,
RA White B., Walker D., Woodward J., Winckler T., Tanaka Y., Shaulsky G.,
RA Schleicher M., Weinstock G., Rosenthal A., Cox E.C., Chisholm R.L.,
RA Gibbs R., Loomis W.F., Platzer M., Kay R.R., Williams J., Dear P.H.,
RA Noegel A.A., Barrell B., Kuspa A.;
RT "The genome of the social amoeba Dictyostelium discoideum.";
RL Nature 435:43-57(2005).
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}.
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:EAL65910.1}.
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DR EMBL; AAFI02000049; EAL65910.1; -; Genomic_DNA.
DR RefSeq; XP_639261.1; XM_634169.1.
DR AlphaFoldDB; Q54RU0; -.
DR SMR; Q54RU0; -.
DR STRING; 44689.Q54RU0; -.
DR PaxDb; 44689-DDB0232349; -.
DR GeneID; 8623831; -.
DR KEGG; ddi:DDB_G0282933; -.
DR dictyBase; DDB_G0282933; mcm7.
DR eggNOG; KOG0482; Eukaryota.
DR HOGENOM; CLU_000995_7_2_1; -.
DR InParanoid; Q54RU0; -.
DR OMA; AQHVTYV; -.
DR PhylomeDB; Q54RU0; -.
DR Reactome; R-DDI-68867; Assembly of the pre-replicative complex.
DR Reactome; R-DDI-68949; Orc1 removal from chromatin.
DR Reactome; R-DDI-68962; Activation of the pre-replicative complex.
DR Reactome; R-DDI-69052; Switching of origins to a post-replicative state.
DR Proteomes; UP000002195; Chromosome 4.
DR GO; GO:0042555; C:MCM complex; ISS:dictyBase.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:RHEA.
DR GO; GO:0003678; F:DNA helicase activity; IEA:InterPro.
DR GO; GO:0003697; F:single-stranded DNA binding; IBA:GO_Central.
DR GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR GO; GO:0006270; P:DNA replication initiation; IBA:GO_Central.
DR GO; GO:0006271; P:DNA strand elongation involved in DNA replication; IBA:GO_Central.
DR GO; GO:0006268; P:DNA unwinding involved in DNA replication; IBA:GO_Central.
DR GO; GO:0000727; P:double-strand break repair via break-induced replication; IBA:GO_Central.
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; 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; 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:UP000002195}.
FT DOMAIN 403..609
FT /note="MCM"
FT /evidence="ECO:0000259|PROSITE:PS50051"
FT REGION 1..33
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 789 AA; 89931 MW; 42ACE359B82FCD74 CRC64;
MENKPYTPFN NNNNFKKKNN NNNNNKKTFF KDNDGNSNNI TLSTGLDYLS EKEKCKDFLN
FFKCTDNGNI GGFEKYVEMM KEITQRKRKN FDIELDDVYN FNRDLVFVES IENQTSTYLR
LFTYALDELI PPPDLSSTRS AMGFNNDDGF DKNKEDQKFY QNSDMVLDLL ASQRIQRKKF
LQEQNRLDLD SNEFDFPQEI IRRFELHFIP RKGKSIIPIR LIRSELIGRL VTFSGVVTRV
TDVKPLVVIS LYTCDICGAE IFQEITSREF MPLFQCKSKQ CTEGGKQAGN LTLQTRGSKF
VKFQEIKVQE IANQVPIGHT PRSIKVYVRG ELTRMASPGD IVTMSGIFLP TPYTGHKAIK
AGLLADTYIE AMQILQHKKT YEQLDLTEEM LKKIQDESQN ENIYDRLAMS LAPEIYGHLD
VKKALLLMMV GGESKHMKDG MNIRGDINIC LMGDPGIAKS QLLKHIAKVA PRGIYTSGKG
SSGVGLTAAV IRDTMTGEFV LEGGSLVLAD MGICCIDEFD KMEDSDRTAI HEVMEQQTIS
IAKAGITTTL NARTSILAAA NPAYGRYNFD RSPDENFRLP HSLLSRFDLL FLMVDKADMD
NDRLLSEHVT YVHMHSKPPQ LSFEPFDSEF IRAYVSQARK IIPPVPKDLT NYIVDSYITL
RKQDSETKTP FTYTTARTLL GVLRLSQAFA RLKFSQQVSQ EDVEESMRLM FVSKQSIRFK
NEKKTPQNPS SIIYTLIKDH CALNRVKKVS IFDIQQKVFS SGFTQQHLDD CLNLYKSVLN
SNSNFISLI
//
