ID A0A218XMU6_PUNGR Unreviewed; 718 AA.
AC A0A218XMU6;
DT 27-SEP-2017, integrated into UniProtKB/TrEMBL.
DT 27-SEP-2017, sequence version 1.
DT 27-MAR-2024, entry version 33.
DE RecName: Full=DNA replication licensing factor MCM7 {ECO:0000256|RuleBase:RU365012};
DE EC=3.6.4.12 {ECO:0000256|RuleBase:RU365012};
GN Name=LOC116209864 {ECO:0000313|RefSeq:XP_031399456.1};
GN Synonyms=MCM7 {ECO:0000256|RuleBase:RU365012};
GN ORFNames=CDL15_Pgr010922 {ECO:0000313|EMBL:OWM86098.1};
OS Punica granatum (Pomegranate).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Myrtales; Lythraceae; Punica.
OX NCBI_TaxID=22663 {ECO:0000313|EMBL:OWM86098.1, ECO:0000313|Proteomes:UP000197138};
RN [1] {ECO:0000313|Proteomes:UP000197138}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Dabenzi {ECO:0000313|Proteomes:UP000197138};
RX PubMed=28654223; DOI=10.1111/tpj.13625;
RA Qin G., Xu C., Ming R., Tang H., Guyot R., Kramer E.M., Hu Y., Yi X.,
RA Qi Y., Xu X., Gao Z., Pan H., Jian J., Tian Y., Yue Z., Xu Y.;
RT "The pomegranate (Punica granatum L.) genome and the genomics of
RT punicalagin biosynthesis.";
RL Plant J. 91:1108-1128(2017).
RN [2] {ECO:0000313|EMBL:OWM86098.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC TISSUE=Fresh leaf {ECO:0000313|EMBL:OWM86098.1};
RA Xu C.;
RT "The pomegranate genome and the genomics of punicalagin biosynthesis.";
RL Submitted (JUN-2017) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|RefSeq:XP_031399456.1}
RP IDENTIFICATION.
RC TISSUE=Leaf {ECO:0000313|RefSeq:XP_031399456.1};
RG RefSeq;
RL Submitted (NOV-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:ARBA00001665,
CC 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; MTKT01001090; OWM86098.1; -; Genomic_DNA.
DR RefSeq; XP_031399456.1; XM_031543596.1.
DR OrthoDB; 147095at2759; -.
DR Proteomes; UP000197138; Unassembled WGS sequence.
DR Proteomes; UP000515151; Chromosome 6.
DR GO; GO:0042555; C:MCM complex; IEA:InterPro.
DR GO; GO:0000347; C:THO complex; IEA:UniProt.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0003678; F:DNA helicase activity; IEA:InterPro.
DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR GO; GO:0006270; P:DNA replication initiation; IEA:InterPro.
DR GO; GO:0006268; P:DNA unwinding involved in 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; 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; 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 326..532
FT /note="MCM"
FT /evidence="ECO:0000259|PROSITE:PS50051"
SQ SEQUENCE 718 AA; 81409 MW; 580600FE53E7B265 CRC64;
MKDFNFKADK DLAKEFLSTF ADINGDLKYM NILQEVANRK TRAVQIDVED LFNYKDEFDE
FVRRVIENTR RYIAIFAEAI DELLPEPTEP FSDDDHDILL TQRSEDRRDT ADGVDPRQKM
PAEIKRFFEV YITATSKGRP YTIREVKASY IGQLVKISGI IIRCSDVKPL MQVAVYTCED
CGFEIYQDVS ARVFMPLVEC PSKRCEVNRK KGNLILQLRA SKFLKFQEAK IQELAEHVPK
GHIPRTMTVH FRGELTRKVA PGDVIELSGI FLPIPYTGFR AMRAGLVADT YLEAMSVNHF
KKKYDEYELR EEEEEQIAKL AEDGDIYNKL ARSLAPEIFG HDDIKKALLL LLVGAPHRKL
KDGMKIRGDL HICLMGDPGV AKSQLLKHII NVAPRGVYTT GKGSSGVGLT AAVQRDTVTN
EMVLEGGALV LADMGICAID EFDKMDESDR TAIHEVMEQQ TVSIAKAGIT TSLNARTAIL
AAANPAWGRY DLRRTPAENI NLPPALLSRF DLLWLILDKA DMDNDLEMAR HVVYVHQKRE
SPALGFTPLQ PSVLRAYISA ARRLSPYVPR DLEEYIASAY STIRQDEART NAPHSYTTVR
TLLSILRISG ALARLRFSEK VAQSDVDEAL RLMQMSKFSL YSEDRQKSGL DAISDIYSIL
RDEAARSNRM DISYAHALNW ISRKGYSEAQ LKECLEEYAE LNVWQIHPNT FDIRFIDA
//
