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Database: UniProt
Entry: A0A286ZJM4_PIG
LinkDB: A0A286ZJM4_PIG
Original site: A0A286ZJM4_PIG 
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
//
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