ID A0A0A2VR16_BEABA Unreviewed; 812 AA.
AC A0A0A2VR16;
DT 04-FEB-2015, integrated into UniProtKB/TrEMBL.
DT 04-FEB-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=BBAD15_g4259 {ECO:0000313|EMBL:KGQ10346.1};
OS Beauveria bassiana D1-5.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Cordycipitaceae; Beauveria.
OX NCBI_TaxID=1245745 {ECO:0000313|EMBL:KGQ10346.1, ECO:0000313|Proteomes:UP000030106};
RN [1] {ECO:0000313|EMBL:KGQ10346.1, ECO:0000313|Proteomes:UP000030106}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=D1-5 {ECO:0000313|EMBL:KGQ10346.1,
RC ECO:0000313|Proteomes:UP000030106};
RA Li Q., Wang L., Zhang Z., Wang Q., Ren J., Wang M., Xu W., Wang J., Lu Y.,
RA Du Q., Sun Z.;
RT "Genome sequencing and analysis of entomopathogenic fungi Beauveria
RT bassiana D1-5.";
RL Submitted (OCT-2012) 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}.
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:KGQ10346.1}.
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DR EMBL; ANFO01000326; KGQ10346.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0A2VR16; -.
DR STRING; 1245745.A0A0A2VR16; -.
DR EnsemblFungi; BB8028_0003g06630.1; BB8028_0003g06630.1; BB8028_0003g06630.
DR eggNOG; KOG0482; Eukaryota.
DR HOGENOM; CLU_000995_7_2_1; -.
DR Proteomes; UP000030106; Unassembled WGS sequence.
DR GO; GO:0000785; C:chromatin; IEA:EnsemblFungi.
DR GO; GO:0000781; C:chromosome, telomeric region; IEA:GOC.
DR GO; GO:0071162; C:CMG complex; IEA:EnsemblFungi.
DR GO; GO:0005737; C:cytoplasm; IEA:EnsemblFungi.
DR GO; GO:0042555; C:MCM complex; IEA:EnsemblFungi.
DR GO; GO:0097373; C:MCM core complex; IEA:EnsemblFungi.
DR GO; GO:0005656; C:nuclear pre-replicative complex; IEA:EnsemblFungi.
DR GO; GO:0031298; C:replication fork protection complex; IEA:EnsemblFungi.
DR GO; GO:0033679; F:3'-5' DNA/RNA helicase activity; IEA:EnsemblFungi.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:EnsemblFungi.
DR GO; GO:0003682; F:chromatin binding; IEA:EnsemblFungi.
DR GO; GO:0003688; F:DNA replication origin binding; IEA:EnsemblFungi.
DR GO; GO:0009378; F:four-way junction helicase activity; IEA:EnsemblFungi.
DR GO; GO:1904931; F:MCM complex binding; IEA:EnsemblFungi.
DR GO; GO:1990518; F:single-stranded 3'-5' DNA helicase activity; IEA:EnsemblFungi.
DR GO; GO:0003697; F:single-stranded DNA binding; IEA:EnsemblFungi.
DR GO; GO:0003727; F:single-stranded RNA binding; IEA:EnsemblFungi.
DR GO; GO:0006270; P:DNA replication initiation; IEA:EnsemblFungi.
DR GO; GO:0006271; P:DNA strand elongation involved in DNA replication; IEA:EnsemblFungi.
DR GO; GO:0006268; P:DNA unwinding involved in DNA replication; IEA:EnsemblFungi.
DR GO; GO:0000727; P:double-strand break repair via break-induced replication; IEA:EnsemblFungi.
DR GO; GO:0006267; P:pre-replicative complex assembly involved in nuclear cell cycle DNA replication; IEA:EnsemblFungi.
DR GO; GO:0006279; P:premeiotic DNA replication; IEA:EnsemblFungi.
DR GO; GO:0030466; P:silent mating-type cassette heterochromatin formation; IEA:EnsemblFungi.
DR GO; GO:0031509; P:subtelomeric heterochromatin formation; IEA:EnsemblFungi.
DR CDD; cd17758; MCM7; 1.
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; 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:UP000030106}.
FT DOMAIN 391..597
FT /note="MCM"
FT /evidence="ECO:0000259|PROSITE:PS50051"
FT REGION 50..76
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 59..76
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 812 AA; 91211 MW; 15498E1C9E38D3A0 CRC64;
MALREYKAIV NYETHQNAFE VFLKDFKTTP EHTITTAMGN ITIDEDDLSD EYDFMDDDDE
SSERRRRDRE HRRAPHHKYQ EIMQKLANRT QEEIVIDLDD LAAWENETGE GLKLVDSIEL
NTKHYVDIMS QAVDKVMPLP SSDVNFKDDV LDVLMARRQA RNRELEEAAE RDPTLEEDKF
PAELTRRYTL VFKPRVNGPD FASKALAVRH VRGDNLGHLI TVRAIVTRVS DVKPIVQVSA
YTCDRCGCEI FQPVTDRQYG PLMMCPSADC KNNQSKGQLN PSTRASKFLP FQEVKVQEMA
EQVPIGQIPR SLTVHCYGSL VRRVNPGDVV DISGIFLPTP YTGFKAMKAG LLTDTYLEAH
HIRQHKKAYS EMIVDPSLVR RIDKYRQTGQ VYELLAKSIA PEIYGHLDVK KALLLLLIGG
VGKEMGDGMK IRGDLNICMM GDPGVAKSQL LKYISKVAPR GVYTSGRGSS GVGLTAAVMR
DPVTDEMVLE GGALVLADNG ICCIDEFDKM DENDRTAIHE VMEQQTISIS KAGISTTLNA
RTSILAAANP IYGRYNPRIS PVENINLPAA LLSRFDIIFL LLDVPNRESD EQLAKHVAFV
HMNNRHPDIG TDNVVFSPHE VRSYVAQART YRPVVPESVT EYMIRTYVRM RDQQQRAEKK
GKQFTHTTPR TLLGVVRLAQ ALARLRFSEV VTQDDVDEAL RLIEASKDSL NIDYGNGRRG
LNASSRIYNL VKALADSGAC RADDAEDDEL GVELSMRKVK ERVIAKGFTE DQWMNALEEY
TTLDVWQTTG SGTRLVFVTA AGDDGNDDMD DL
//
