ID A0A0C3DG29_9AGAM Unreviewed; 781 AA.
AC A0A0C3DG29;
DT 01-APR-2015, integrated into UniProtKB/TrEMBL.
DT 01-APR-2015, sequence version 1.
DT 27-MAR-2024, entry version 52.
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=SCLCIDRAFT_1221439 {ECO:0000313|EMBL:KIM55036.1};
OS Scleroderma citrinum Foug A.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Agaricomycetidae; Boletales; Sclerodermatineae; Sclerodermataceae;
OC Scleroderma.
OX NCBI_TaxID=1036808 {ECO:0000313|EMBL:KIM55036.1, ECO:0000313|Proteomes:UP000053989};
RN [1] {ECO:0000313|EMBL:KIM55036.1, ECO:0000313|Proteomes:UP000053989}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Foug A {ECO:0000313|EMBL:KIM55036.1,
RC ECO:0000313|Proteomes:UP000053989};
RG DOE Joint Genome Institute;
RA Kuo A., Kohler A., Nagy L.G., Floudas D., Copeland A., Barry K.W.,
RA Cichocki N., Veneault-Fourrey C., LaButti K., Lindquist E.A., Lipzen A.,
RA Lundell T., Morin E., Murat C., Sun H., Tunlid A., Henrissat B.,
RA Grigoriev I.V., Hibbett D.S., Martin F., Nordberg H.P., Cantor M.N.,
RA Hua S.X.;
RL Submitted (APR-2014) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Proteomes:UP000053989}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Foug A {ECO:0000313|Proteomes:UP000053989};
RG DOE Joint Genome Institute;
RG Mycorrhizal Genomics Consortium;
RA Kohler A., Kuo A., Nagy L.G., Floudas D., Copeland A., Barry K.W.,
RA Cichocki N., Veneault-Fourrey C., LaButti K., Lindquist E.A., Lipzen A.,
RA Lundell T., Morin E., Murat C., Riley R., Ohm R., Sun H., Tunlid A.,
RA Henrissat B., Grigoriev I.V., Hibbett D.S., Martin F.;
RT "Evolutionary Origins and Diversification of the Mycorrhizal Mutualists.";
RL Submitted (JAN-2015) 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: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}.
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DR EMBL; KN822142; KIM55036.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0C3DG29; -.
DR STRING; 1036808.A0A0C3DG29; -.
DR HOGENOM; CLU_000995_7_2_1; -.
DR InParanoid; A0A0C3DG29; -.
DR OrthoDB; 5476523at2759; -.
DR Proteomes; UP000053989; Unassembled WGS sequence.
DR GO; GO:0031261; C:DNA replication preinitiation complex; IEA:UniProt.
DR GO; GO:0042555; C:MCM complex; IEA:InterPro.
DR GO; GO:0005656; C:nuclear pre-replicative complex; IEA:UniProt.
DR GO; GO:0043596; C:nuclear replication fork; IEA:UniProt.
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:0006270; P:DNA replication initiation; IEA:InterPro.
DR GO; GO:0006279; P:premeiotic 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:UP000053989}.
FT DOMAIN 355..561
FT /note="MCM"
FT /evidence="ECO:0000259|PROSITE:PS50051"
FT REGION 698..735
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 781 AA; 88484 MW; EBE035C65F2B392C CRC64;
MSLPVVKISI SYEDELSIIR TFLSGFVRQE KDIDAGIADI VLDDDEHQPE GVLNRFKYMQ
QLQRIANRDQ QMLSIELEDI HQHEKTVTGL VAHIQNNTRR YVALFCEAVD ELMPTPTKDI
SDKDEVMDIL LHQRRERNEQ TEGQQEGFPA HLLRRYTLYF EPLKSDVAMA VREVRSMHLG
KLITLRGIVT RVSEVKPLLL VNAYTCDVCG SETFQQISNK TFAPIFDCQN ESECKKNGVR
GTLHMQTRAS RFSPFQEVKI QEMADQVPVG HIPRSTTVHV NGNLTRLMNP GDVVHLAGIF
LPIPYTGYQA IRAGLLTDTY LETHHIHQLK KQYSDMEMTP QIQQQIAEMQ TDPALYNKLA
QSIAPEIYGH IDVKKALLLL LVGGVTKTMG DGMKIRGDIN VCLMGDPGVA KSQLLKYISK
VAPRGVYTTG RGSSGVGLTA AVMRDPVTDE MVLEGGALVL ADNGICCIDE FDKMEESDRT
AIHEVMEQQT ISISKAGIST TLNARTSILA AANPLYGRYN PKVSPVENIN LPAALLSRFD
LLFLILDKPT REDDERLAQH VTHVHMHNIH PQLEFDVVDP TLMRHYIAQA RLRRPIVPRE
VSNYIVDSYV RLRKLSKDTA EQKKLHTYTS ARTLLGVLRL SQALARLRFA DIVQHDDVDE
ALRLMECSKE SLNEDEDRDY EPDRSVISQI YRLIKQMAAE GGRKRRKRQR RFGRGPGGER
DMDIDSDEDE DNEELPMIDV RSRVLSAGYT EAQLNDTIVE YESMDIWARV ANGARLRFID
I
//
