ID A0A3B6EFD6_WHEAT Unreviewed; 849 AA.
AC A0A3B6EFD6;
DT 05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT 05-DEC-2018, sequence version 1.
DT 24-JAN-2024, entry version 25.
DE RecName: Full=DNA replication licensing factor MCM4 {ECO:0000256|RuleBase:RU368062};
DE EC=3.6.4.12 {ECO:0000256|RuleBase:RU368062};
GN ORFNames=CFC21_052044 {ECO:0000313|EMBL:KAF7042439.1};
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:TraesCS3A02G200400.1};
RN [1] {ECO:0000313|EMBL:KAF7042439.1}
RP NUCLEOTIDE SEQUENCE.
RC TISSUE=Leaf {ECO:0000313|EMBL:KAF7042439.1};
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:TraesCS3A02G200400.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Chinese Spring
RC {ECO:0000313|EnsemblPlants:TraesCS3A02G200400.1};
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:TraesCS3A02G200400.1}
RP IDENTIFICATION.
RG EnsemblPlants;
RL Submitted (OCT-2018) to UniProtKB.
RN [4] {ECO:0000313|EMBL:KAF7042439.1}
RP NUCLEOTIDE SEQUENCE.
RC TISSUE=Leaf {ECO:0000313|EMBL:KAF7042439.1};
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:RU368062}.
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:RU368062};
CC -!- SUBUNIT: Component of the MCM2-7 complex.
CC {ECO:0000256|RuleBase:RU368062}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
CC -!- SIMILARITY: Belongs to the MCM family. {ECO:0000256|ARBA:ARBA00008010,
CC ECO:0000256|RuleBase:RU004070}.
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DR EMBL; CM022220; KAF7042439.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A3B6EFD6; -.
DR SMR; A0A3B6EFD6; -.
DR STRING; 4565.A0A3B6EFD6; -.
DR EnsemblPlants; TraesCS3A02G200400.1; TraesCS3A02G200400.1; TraesCS3A02G200400.
DR Gramene; TraesCAD_scaffold_058298_01G000100.1; TraesCAD_scaffold_058298_01G000100.1; TraesCAD_scaffold_058298_01G000100.
DR Gramene; TraesCLE_scaffold_082171_01G000100.1; TraesCLE_scaffold_082171_01G000100.1; TraesCLE_scaffold_082171_01G000100.
DR Gramene; TraesCS3A02G200400.1; TraesCS3A02G200400.1; TraesCS3A02G200400.
DR Gramene; TraesKAR3A01G0210920.1; cds.TraesKAR3A01G0210920.1; TraesKAR3A01G0210920.
DR Gramene; TraesPAR_scaffold_058426_01G000100.1; TraesPAR_scaffold_058426_01G000100.1; TraesPAR_scaffold_058426_01G000100.
DR Gramene; TraesROB_scaffold_172997_01G000100.1; TraesROB_scaffold_172997_01G000100.1; TraesROB_scaffold_172997_01G000100.
DR Gramene; TraesWEE_scaffold_070204_01G000100.1; TraesWEE_scaffold_070204_01G000100.1; TraesWEE_scaffold_070204_01G000100.
DR OrthoDB; 147095at2759; -.
DR Proteomes; UP000019116; Chromosome 3A.
DR Proteomes; UP000815260; Chromosome 4A.
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:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR GO; GO:0003678; F:DNA helicase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0003697; F:single-stranded DNA binding; 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:1902975; P:mitotic DNA replication initiation; IBA:GO_Central.
DR CDD; cd17755; MCM4; 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 Gene3D; 1.10.10.10; Winged helix-like DNA-binding domain superfamily/Winged helix DNA-binding domain; 1.
DR InterPro; IPR003593; AAA+_ATPase.
DR InterPro; IPR031327; MCM.
DR InterPro; IPR008047; MCM_4.
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 InterPro; IPR036388; WH-like_DNA-bd_sf.
DR PANTHER; PTHR11630; DNA REPLICATION LICENSING FACTOR MCM FAMILY MEMBER; 1.
DR PANTHER; PTHR11630:SF66; DNA REPLICATION LICENSING FACTOR MCM4; 1.
DR Pfam; PF00493; MCM; 1.
DR Pfam; PF21128; MCM4_WHD; 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; PR01660; MCMPROTEIN4.
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 DNA replication {ECO:0000256|ARBA:ARBA00022705,
KW ECO:0000256|RuleBase:RU368062};
KW DNA-binding {ECO:0000256|ARBA:ARBA00023125, ECO:0000256|RuleBase:RU004070};
KW Helicase {ECO:0000256|ARBA:ARBA00022806, ECO:0000256|RuleBase:RU368062};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU368062};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW ECO:0000256|RuleBase:RU004070};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242, ECO:0000256|RuleBase:RU368062};
KW Reference proteome {ECO:0000313|Proteomes:UP000019116}.
FT DOMAIN 440..646
FT /note="MCM"
FT /evidence="ECO:0000259|PROSITE:PS50051"
FT REGION 1..119
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 405..424
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..37
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 72..97
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 849 AA; 93686 MW; F2E4B745E5F7F7ED CRC64;
MASNGGGNSN SPYSASSPDV RPSSPLPATN SSPPQSARRA GGRLRRGPTS SPSLGGFETP
PPPGRRTPSG AGAARQRQNW TGRFPPTPST PMSTDDVPLS SEAGEEDTPE TDGGGVGADA
TPVFVWGTNI SVQDVNAAIL RFLRHFRDPR DAGRVDPVMD EGKYMRAIHR ILELEGGESL
DVDAHDVFDH DPDLYGKMVR YPLEVLAIFD IVLMDLVARM EPLFEKHIQT RIYNLKSSIC
LRNLNPSDIE KMVSIKGMII RCSSVIPELK EAVFRCLVCG FYSEPVMVDR GRVTEPHICQ
KEQCKASNSM TLVHNRCRFA DKQIIKLQET PDEIPEGGTP HTVSVLMHDK LVDAGKPGDR
VEITGIYRAM SIRIGPSQRT VKSIFKTYID CLHIKKTDKS RLHIEDSMDT DNTNASKSSE
DGHVTDKIDK LKELSKLPDI YDRLTRSLAP NIWELDDVKR GLLCQLFGGN ALRLPSGANF
RGDINILLVG DPGTSKSQLL QYMHKLSPRG IYTSGRGSSA VGLTAYVAKD PETGETVLES
GALVLSDKGV CCIDEFDKMS DNARSMLHEV MEQQTVSIAK AGIIASLNAR TSVLACANPS
ESRYNPRLSV IDNIHLPPTL LSRFDLIYLI LDKADEQTDR RLAKHIVSLH FENPEVVEHQ
VLDLPTLVAY ISYARKYIQP KLSDEAAEEL TRGYVAMRQR GNNPGSRKKV ITATARQIES
LIRLSEALAR MRFSEVVGVL DVTEAFRLLE VAMQQSATDH ATGTIDMDLI MTGVSASERQ
RHDNLVAAIR DLVMEKMQLG GPSMRMAELL EEVRKQSSME VHQHDLRDAL GTLQSEGSVF
VHGDSFKRT
//
