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Database: UniProt
Entry: A0A3B6PRQ6_WHEAT
LinkDB: A0A3B6PRQ6_WHEAT
Original site: A0A3B6PRQ6_WHEAT 
ID   A0A3B6PRQ6_WHEAT        Unreviewed;       758 AA.
AC   A0A3B6PRQ6;
DT   05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT   05-DEC-2018, sequence version 1.
DT   27-MAR-2024, entry version 25.
DE   RecName: Full=DNA replication licensing factor MCM5 {ECO:0000256|RuleBase:RU368063};
DE            EC=3.6.4.12 {ECO:0000256|RuleBase:RU368063};
GN   ORFNames=CFC21_089804 {ECO:0000313|EMBL:KAF7086520.1};
OS   Triticum aestivum (Wheat).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC   Pooideae; Triticodae; Triticeae; Triticinae; Triticum.
OX   NCBI_TaxID=4565 {ECO:0000313|EnsemblPlants:TraesCS6B02G393500.3};
RN   [1] {ECO:0000313|EMBL:KAF7086520.1}
RP   NUCLEOTIDE SEQUENCE.
RC   TISSUE=Leaf {ECO:0000313|EMBL:KAF7086520.1};
RX   PubMed=29069494;
RA   Zimin A.V., Puiu D., Hall R., Kingan S., Clavijo B.J., Salzberg S.L.;
RT   "The first near-complete assembly of the hexaploid bread wheat genome,
RT   Triticum aestivum.";
RL   Gigascience 6:1-7(2017).
RN   [2] {ECO:0000313|EnsemblPlants:TraesCS6B02G393500.3}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Chinese Spring
RC   {ECO:0000313|EnsemblPlants:TraesCS6B02G393500.3};
RX   PubMed=30115783; DOI=10.1126/science.aar7191;
RG   International wheat genome sequencing consortium (IWGSC);
RT   "Shifting the limits in wheat research and breeding using a fully annotated
RT   reference genome.";
RL   Science 361:EAAR7191-EAAR7191(2018).
RN   [3] {ECO:0000313|EnsemblPlants:TraesCS6B02G393500.3}
RP   IDENTIFICATION.
RG   EnsemblPlants;
RL   Submitted (OCT-2018) to UniProtKB.
RN   [4] {ECO:0000313|EMBL:KAF7086520.1}
RP   NUCLEOTIDE SEQUENCE.
RC   TISSUE=Leaf {ECO:0000313|EMBL:KAF7086520.1};
RA   Zimin A.V., Puiu D., Shumante A., Alonge M., Salzberg S.L.;
RT   "The second near-complete assembly of the hexaploid bread wheat (Triticum
RT   aestivum) genome.";
RL   Submitted (MAR-2020) 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:RU368063}.
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:RU368063};
CC   -!- SUBUNIT: Component of the MCM2-7 complex.
CC       {ECO:0000256|RuleBase:RU368063}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123,
CC       ECO:0000256|RuleBase:RU368063}.
CC   -!- SIMILARITY: Belongs to the MCM family. {ECO:0000256|RuleBase:RU004070}.
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DR   EMBL; CM022227; KAF7086520.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A3B6PRQ6; -.
DR   SMR; A0A3B6PRQ6; -.
DR   STRING; 4565.A0A3B6PRQ6; -.
DR   PaxDb; 4565-Traes_6BL_A012FAD0E-1; -.
DR   EnsemblPlants; TraesCS6B02G393500.3; TraesCS6B02G393500.3; TraesCS6B02G393500.
DR   Gramene; TraesCS6B02G393500.3; TraesCS6B02G393500.3; TraesCS6B02G393500.
DR   Gramene; TraesCS6B03G1110900.2; TraesCS6B03G1110900.2.CDS; TraesCS6B03G1110900.
DR   Proteomes; UP000019116; Chromosome 6B.
DR   Proteomes; UP000815260; Chromosome 6B.
DR   GO; GO:0042555; C:MCM complex; IBA:GO_Central.
DR   GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0003688; F:DNA replication origin binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0004386; F:helicase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
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:0006270; P:DNA replication initiation; IBA:GO_Central.
DR   GO; GO:0006268; P:DNA unwinding involved in DNA replication; IEA:UniProt.
DR   GO; GO:0000727; P:double-strand break repair via break-induced replication; IBA:GO_Central.
DR   CDD; cd17756; MCM5; 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; IPR008048; MCM5.
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:SF42; DNA REPLICATION LICENSING FACTOR MCM5; 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; PR01661; MCMPROTEIN5.
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|RuleBase:RU368063};
KW   DNA replication {ECO:0000256|ARBA:ARBA00022705,
KW   ECO:0000256|RuleBase:RU368063};
KW   DNA-binding {ECO:0000256|ARBA:ARBA00023125, ECO:0000256|RuleBase:RU004070};
KW   Helicase {ECO:0000256|ARBA:ARBA00022806, ECO:0000256|RuleBase:RU368063};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU368063};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW   ECO:0000256|RuleBase:RU004070};
KW   Nucleus {ECO:0000256|ARBA:ARBA00023242, ECO:0000256|RuleBase:RU368063};
KW   Reference proteome {ECO:0000313|Proteomes:UP000019116}.
FT   DOMAIN          354..560
FT                   /note="MCM"
FT                   /evidence="ECO:0000259|PROSITE:PS50051"
SQ   SEQUENCE   758 AA;  83968 MW;  B07DDB1D008B0598 CRC64;
     MSGWDEGAVF YSDQAQFPQG DPAAADITRH SALRKFKEFL RGFTGPTGDF PYRYPLPPSP
     RQIWSNRASR LTRGRVPLFL SSESLVHNRD HVTVAIEDLD AFDAELADRI RKAPADYLPL
     FETAGSEVLA SLRSKVAGET GEMEEPVTGD VQIFLSSKEN CVSMRSIGAD YMSKLVKIAG
     IAIAASRVKA KATHVTLLCK NCRSVRTVPC RPGLGGAIVP RSCDHVPQPG EEPCPLDPWI
     AVPDKSKYVD LQTLKLQENP EDVPTGELPR NVLLSVDRHL VQTIVPGTRL TVVGIYSVFQ
     ASGTNNQKGA VGVKQPYIRI VGLEQSRDDN TNGPSHFTLD EEMEFKEFAQ RPDAYAKICS
     MIGPSIYGHG DVKKAIACLL FGGSKKRLPD GVRLRGDIHA LLLGDPSTAK SQFLKFVEKT
     APIAVYTSGK GSSAAGLTAS VTRDSNSREF YLEGGAMVLA DGGVVCIDEF DKMRPEDRVA
     IHEAMEQQTI SIAKAGITTV LNSRTSVLAA ANPISGRYDD LKTAQDNIDL QTTILSRFDL
     IFIVKDVRMY EQDKRIANHI IKVHASGAAT QANKNTNANE GENWLKRYVE YCRNTCRPRL
     SEKAAEMLQN KYVEIRQKMR QQSHETGRAA AIPITVRQLE AIIRLSESLA KMRLTSVATP
     EHIEEAFRLF NVSTVDAARS GINEHLNLSP EIANEIKQAE AQIKRRMGIG SHISERRLLD
     ELNRMGMNES IVRRALVIMH QRDEVEYKRE RHVIVRKA
//
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