ID A0A286ZJM4_PIG Unreviewed; 719 AA.
AC A0A286ZJM4;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 24-JAN-2024, entry version 40.
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|Ensembl:ENSSSCP00000050669.1,
GN ECO:0000313|VGNC:VGNC:90076};
OS Sus scrofa (Pig).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Suina; Suidae; Sus.
OX NCBI_TaxID=9823 {ECO:0000313|Ensembl:ENSSSCP00000050669.1, ECO:0000313|Proteomes:UP000008227};
RN [1] {ECO:0000313|Ensembl:ENSSSCP00000050669.1, ECO:0000313|Proteomes:UP000008227}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Duroc {ECO:0000313|Ensembl:ENSSSCP00000050669.1,
RC ECO:0000313|Proteomes:UP000008227};
RG Porcine genome sequencing project;
RL Submitted (NOV-2009) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSSSCP00000050669.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (JUL-2023) to UniProtKB.
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:ARBA00000600};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:13066;
CC Evidence={ECO:0000256|ARBA:ARBA00000600};
CC -!- SUBCELLULAR LOCATION: Chromosome {ECO:0000256|ARBA:ARBA00004286}.
CC Nucleus {ECO:0000256|ARBA:ARBA00004123, ECO:0000256|RuleBase:RU365012}.
CC -!- SIMILARITY: Belongs to the MCM family. {ECO:0000256|ARBA:ARBA00008010,
CC ECO:0000256|RuleBase:RU004070}.
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DR AlphaFoldDB; A0A286ZJM4; -.
DR SMR; A0A286ZJM4; -.
DR STRING; 9823.ENSSSCP00000050669; -.
DR Ensembl; ENSSSCT00000041433.2; ENSSSCP00000050669.1; ENSSSCG00000032180.2.
DR VGNC; VGNC:90076; MCM7.
DR GeneTree; ENSGT01050000244824; -.
DR InParanoid; A0A286ZJM4; -.
DR OMA; AQHVTYV; -.
DR OrthoDB; 5476523at2759; -.
DR Reactome; R-SSC-176187; Activation of ATR in response to replication stress.
DR Reactome; R-SSC-68867; Assembly of the pre-replicative complex.
DR Reactome; R-SSC-68949; Orc1 removal from chromatin.
DR Reactome; R-SSC-68962; Activation of the pre-replicative complex.
DR Reactome; R-SSC-69052; Switching of origins to a post-replicative state.
DR Proteomes; UP000008227; Chromosome 3.
DR Bgee; ENSSSCG00000032180; Expressed in hindlimb bud and 43 other cell types or tissues.
DR ExpressionAtlas; A0A286ZJM4; baseline and differential.
DR GO; GO:0071162; C:CMG complex; IEA:Ensembl.
DR GO; GO:0005829; C:cytosol; IEA:Ensembl.
DR GO; GO:0042555; C:MCM complex; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0031090; C:organelle membrane; 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:0003678; F:DNA helicase activity; IEA:Ensembl.
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:0008283; P:cell population proliferation; IEA:Ensembl.
DR GO; GO:0071466; P:cellular response to xenobiotic stimulus; IEA:Ensembl.
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 GO; GO:0042325; P:regulation of phosphorylation; IEA:Ensembl.
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 Chromosome {ECO:0000256|ARBA:ARBA00022454};
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:UP000008227}.
FT DOMAIN 332..537
FT /note="MCM"
FT /evidence="ECO:0000259|PROSITE:PS50051"
SQ SEQUENCE 719 AA; 81326 MW; 5851E236F9F1265F CRC64;
MALKDYALEK EKVKKFLQEF YQDDELGKKQ FKYGNQLVRL AHREQVAMYI DLDDVTEDDP
ELVDSICENT KRYARLFADA VQELLPQYKE REVVNKDVLD VYIEHRLMME QRSRDPGAAR
SPQNQYPPEL MRRFELYFQG PSSSKPRVIR EVRADSVGKL VTVRGIVTRV SEVKPRMVVA
TYTCDQCGAE TYQPIQSPTF MPLIMCPSQE CQTNRSGGRL YLQTRGSKFI KFQEMKMQEH
SDQVPVGNIP RSITVLVEGE NTRIAQPGDH VSVTGIFLPI LRTGFRQVVQ GLLSETYLEA
HRIVKMSKSE DDESGAGELS REELRQIAEE DFYEKLAASI APEIYGHEDV KKALLLLLVG
GVDQSPRGMK IRGNINICLM GDPGVAKSQL LSYIDRLAPR SQYTTGRGSS GVGLTAAVLR
DSVSGELTLE GGALVLADQG VCCIDEFDKM AEADRTAIHE VMEQQTISIA KAGILTTLNA
RCSILAAANP AYGRYNPRRS LEQNIQLPAA LLSRFDLLWL IQDRPDRDND LRLAQHITYV
HQHSRQPPAQ FEPLDMKLMR RYIAMCREKQ PTVPESLADY ITAAYVEMRR EAWASKDATY
TSARTLLAIL RLSTALARLR MVDTVEKEDV NEAIRLMEMS KDSLLGDKGQ TARTQRPADV
IFATVRELVS EGRSVRFSEA EQRCISRGFT PAQFQAALDE YEELNVWQVN TARTRITFV
//