ID A0A3M9YLY9_9PEZI Unreviewed; 838 AA.
AC A0A3M9YLY9;
DT 13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT 13-FEB-2019, sequence version 1.
DT 27-MAR-2024, entry version 23.
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 ECO:0000313|EMBL:RNJ60776.1};
GN ORFNames=D7B24_005926 {ECO:0000313|EMBL:RNJ60776.1};
OS Verticillium nonalfalfae.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Glomerellales; Plectosphaerellaceae; Verticillium.
OX NCBI_TaxID=1051616 {ECO:0000313|EMBL:RNJ60776.1, ECO:0000313|Proteomes:UP000267145};
RN [1] {ECO:0000313|EMBL:RNJ60776.1, ECO:0000313|Proteomes:UP000267145}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=VnAa140 {ECO:0000313|EMBL:RNJ60776.1,
RC ECO:0000313|Proteomes:UP000267145};
RA Stajich J.E., Kasson M.T.;
RT "Genome sequence of Verticillium nonalfalfae VnAa140.";
RL Submitted (OCT-2018) 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:RNJ60776.1}.
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DR EMBL; RBVV01000004; RNJ60776.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A3M9YLY9; -.
DR STRING; 1051616.A0A3M9YLY9; -.
DR OrthoDB; 5476523at2759; -.
DR Proteomes; UP000267145; 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; 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}.
FT DOMAIN 415..621
FT /note="MCM"
FT /evidence="ECO:0000259|PROSITE:PS50051"
SQ SEQUENCE 838 AA; 93620 MW; 3AB29CFDF3B43DE3 CRC64;
MALRQFKAPV QYEAQLGTLP RDSALTWRQV LTTTTAAAFE SFLKDFKATP EQTITHALGN
VTINEDDFDE DDDVMEDDEV AEERRRRQKE ARTPQPKYQI ILQELADRKI NEVMLDLDDL
HGWEKSLEAD TGERLKLVES VELNTKHYVE IFSRAIDSQM PAPTNKESFK EDVLDVVMRR
REEHNQAMDV AVANGDLPAA AERFPAELTR RYTLAFKPRT QTVDHESKAM AVRDVRGEHL
GHLITVRAIA TRVSDVKPVV SVSAYYCEGC GSEIFQPVTD KQHTPLTMCP SETCKKNQSR
SQLQPSSRAS KFLPFQEVKV QEMAEQVPIG QIPRTLTVLC YGSSVRKVNP GDVVDISGIF
MPTPYTGFKA MKAGLLTDTY LEAHYILQHK KAYSEMIIDP ALVRRIEQYR QSGQVYELLA
KSIAPEIYGH VDVKKALLLL LIGGVTKEVK DGMKIRGDIN VCLMGDPGVA KSQLLKYISK
VAPRGVYTSG RGSSGVGLTA AVIRDPVTDE MVLEGGALVL ADNGICCIDE FDKMDDNDRT
AIHEVMEQQT ISISKAGIST TLNARTSILA AANPLYGRYN PRLSPVENIN LPAALLSRFD
IMFLILDTPN RESDAQLAKH VAYVHMHSRH PPVAGEDDVI FSPHEVRSYI AQARTYRPVV
TAGVMEYVSK TYVRMREAQR RAEKKGEQFT HVTPRTLLGI IRIAQALARL RFSNLVEQDD
VDEALRLLEA SKESLAADQG TGRQRLNPNS RIYNMVKALA DSGACRPDDA DEDDEYGVLS
LRKVKERVIA KGFTEDQWLA ALEEYNSLDV WQTAGNMTRL VFINASGNDA EREGSEDA
//
