MCM4_ARATH
ID MCM4_ARATH Reviewed; 847 AA.
AC Q0WVF5; Q9SIV8;
DT 16-APR-2014, integrated into UniProtKB/Swiss-Prot.
DT 05-SEP-2006, sequence version 1.
DT 03-AUG-2022, entry version 124.
DE RecName: Full=DNA replication licensing factor MCM4;
DE EC=3.6.4.12;
DE AltName: Full=Minichromosome maintenance protein 4;
DE Short=AtMCM4;
GN Name=MCM4; OrderedLocusNames=At2g16440; ORFNames=F16F14.6;
OS Arabidopsis thaliana (Mouse-ear cress).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX NCBI_TaxID=3702;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=10617197; DOI=10.1038/45471;
RA Lin X., Kaul S., Rounsley S.D., Shea T.P., Benito M.-I., Town C.D.,
RA Fujii C.Y., Mason T.M., Bowman C.L., Barnstead M.E., Feldblyum T.V.,
RA Buell C.R., Ketchum K.A., Lee J.J., Ronning C.M., Koo H.L., Moffat K.S.,
RA Cronin L.A., Shen M., Pai G., Van Aken S., Umayam L., Tallon L.J.,
RA Gill J.E., Adams M.D., Carrera A.J., Creasy T.H., Goodman H.M.,
RA Somerville C.R., Copenhaver G.P., Preuss D., Nierman W.C., White O.,
RA Eisen J.A., Salzberg S.L., Fraser C.M., Venter J.C.;
RT "Sequence and analysis of chromosome 2 of the plant Arabidopsis thaliana.";
RL Nature 402:761-768(1999).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=cv. Columbia;
RX PubMed=27862469; DOI=10.1111/tpj.13415;
RA Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA Town C.D.;
RT "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT genome.";
RL Plant J. 89:789-804(2017).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RA Totoki Y., Seki M., Ishida J., Nakajima M., Enju A., Kamiya A.,
RA Narusaka M., Shin-i T., Nakagawa M., Sakamoto N., Oishi K., Kohara Y.,
RA Kobayashi M., Toyoda A., Sakaki Y., Sakurai T., Iida K., Akiyama K.,
RA Satou M., Toyoda T., Konagaya A., Carninci P., Kawai J., Hayashizaki Y.,
RA Shinozaki K.;
RT "Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs.";
RL Submitted (JUL-2006) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP GENE FAMILY.
RX PubMed=17556508; DOI=10.1104/pp.107.101105;
RA Shultz R.W., Tatineni V.M., Hanley-Bowdoin L., Thompson W.F.;
RT "Genome-wide analysis of the core DNA replication machinery in the higher
RT plants Arabidopsis and rice.";
RL Plant Physiol. 144:1697-1714(2007).
RN [5]
RP SUBUNIT, AND INTERACTION WITH ETG1.
RX PubMed=18528439; DOI=10.1038/emboj.2008.107;
RA Takahashi N., Lammens T., Boudolf V., Maes S., Yoshizumi T., De Jaeger G.,
RA Witters E., Inze D., De Veylder L.;
RT "The DNA replication checkpoint aids survival of plants deficient in the
RT novel replisome factor ETG1.";
RL EMBO J. 27:1840-1851(2008).
RN [6]
RP TISSUE SPECIFICITY.
RX PubMed=19357199; DOI=10.1104/pp.109.136614;
RA Shultz R.W., Lee T.J., Allen G.C., Thompson W.F., Hanley-Bowdoin L.;
RT "Dynamic localization of the DNA replication proteins MCM5 and MCM7 in
RT plants.";
RL Plant Physiol. 150:658-669(2009).
CC -!- FUNCTION: Probable component of the MCM2-7 complex (MCM complex) that
CC may function as a DNA helicase and which is essential to undergo a
CC single round of replication initiation and elongation per cell cycle in
CC eukaryotic cells. {ECO:0000250}.
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 -!- SUBUNIT: Component of the minichromosome maintenance (MCM) complex, a
CC heterotetramer composed of MCM2, MCM3, MCM4, MCM5, MCM6 and MCM7.
CC Interacts with ETG1. {ECO:0000269|PubMed:18528439}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000305}.
CC -!- TISSUE SPECIFICITY: Expressed in shoot apex and flower buds.
CC {ECO:0000269|PubMed:19357199}.
CC -!- SIMILARITY: Belongs to the MCM family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAD22296.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AC007047; AAD22296.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002685; AEC06497.1; -; Genomic_DNA.
DR EMBL; AK226795; BAE98893.1; -; mRNA.
DR PIR; C84540; C84540.
DR RefSeq; NP_179236.3; NM_127197.5.
DR AlphaFoldDB; Q0WVF5; -.
DR SMR; Q0WVF5; -.
DR BioGRID; 1500; 6.
DR IntAct; Q0WVF5; 3.
DR MINT; Q0WVF5; -.
DR STRING; 3702.AT2G16440.1; -.
DR iPTMnet; Q0WVF5; -.
DR PaxDb; Q0WVF5; -.
DR PRIDE; Q0WVF5; -.
DR ProteomicsDB; 238241; -.
DR EnsemblPlants; AT2G16440.1; AT2G16440.1; AT2G16440.
DR GeneID; 816142; -.
DR Gramene; AT2G16440.1; AT2G16440.1; AT2G16440.
DR KEGG; ath:AT2G16440; -.
DR Araport; AT2G16440; -.
DR TAIR; locus:2042674; AT2G16440.
DR eggNOG; KOG0478; Eukaryota.
DR HOGENOM; CLU_000995_7_2_1; -.
DR InParanoid; Q0WVF5; -.
DR OMA; KNTIRIC; -.
DR OrthoDB; 266497at2759; -.
DR PhylomeDB; Q0WVF5; -.
DR PRO; PR:Q0WVF5; -.
DR Proteomes; UP000006548; Chromosome 2.
DR ExpressionAtlas; Q0WVF5; baseline and differential.
DR Genevisible; Q0WVF5; AT.
DR GO; GO:0009507; C:chloroplast; HDA:TAIR.
DR GO; GO:0042555; C:MCM complex; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0000347; C:THO complex; IDA:UniProtKB.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:RHEA.
DR GO; GO:0003678; F:DNA helicase activity; IEA:UniProtKB-EC.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0003697; F:single-stranded DNA binding; IBA:GO_Central.
DR GO; GO:0006260; P:DNA replication; IPI:TAIR.
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 GO; GO:0009555; P:pollen development; IMP:TAIR.
DR Gene3D; 1.10.10.10; -; 1.
DR Gene3D; 2.40.50.140; -; 1.
DR Gene3D; 3.40.50.300; -; 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; PTHR11630; 1.
DR PANTHER; PTHR11630:SF66; PTHR11630:SF66; 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; PR01660; MCMPROTEIN4.
DR SMART; SM00382; AAA; 1.
DR SMART; SM00350; MCM; 1.
DR SUPFAM; SSF50249; SSF50249; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR PROSITE; PS00847; MCM_1; 1.
DR PROSITE; PS50051; MCM_2; 1.
PE 1: Evidence at protein level;
KW ATP-binding; Cell cycle; DNA replication; DNA-binding; Helicase; Hydrolase;
KW Metal-binding; Nucleotide-binding; Nucleus; Reference proteome; Zinc;
KW Zinc-finger.
FT CHAIN 1..847
FT /note="DNA replication licensing factor MCM4"
FT /id="PRO_0000425991"
FT DOMAIN 435..641
FT /note="MCM"
FT ZN_FING 271..299
FT /note="C4-type"
FT /evidence="ECO:0000255"
FT REGION 1..123
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 617..620
FT /note="Arginine finger"
FT COMPBIAS 1..30
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 485..492
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
SQ SEQUENCE 847 AA; 93656 MW; 4585D9BC3EAA5640 CRC64;
MASDSSLGNT NDGPPSPGEN VSSPIENTYS SPAALHRRRR GRSSTPTQFA TPPPPPSRLA
SSNSTPPTSR PSAARSKGRN GHGGGGGGGG GGDPGTPMST DEPLPSSDDG EEDGGDDTTP
TFVWGTNISV QDVKSAIEMF VKHFREAREN SDDLFREGKY MVSIRKVIEI EGEWIDVDAF
DVFDYDPDLY NKMVRYPLEV LAIFDIVLMD IVSTINRLFE KHVQVRIFNL RTSTSMRNLN
PSDIEKMISL KGMIIRSSSI IPEIREAVFR CLVCGYFSDP IIVDRGKISE PPTCLKQECM
TKNSMTLVHN RCRFADKQIV RLQETPDEIP EGGTPHTVSL LLHDKLVDNG KPGDRIEVTG
IYRAMTVRVG PAHRTVKSVF KTYIDCLHIK KASKLRMSAE DPMDVDNSLR RVDEDVELDE
EKLRKFQELS KQPDIYERLS RSLAPNIWEL DDVKKGLLCQ LFGGNALNLA SGANFRGDIN
ILLVGDPGTS KSQLLQYIHK LSPRGIYTSG RGSSAVGLTA YVAKDPETGE TVLESGALVL
SDRGICCIDE FDKMSDSARS MLHEVMEQQT VSIAKAGIIA SLNARTSVLA CANPSGSRYN
PRLSVIENIH LPPTLLSRFD LIYLILDKPD EQTDRRLAKH IVALHFENAE SAQEEAIDIT
TLTTYVSYAR KNIHPKLSDE AAEELTRGYV ELRKAGKFAG SSKKVITATP RQIESLIRLS
EALARMRFSE WVEKHDVDEA FRLLRVAMQQ SATDHATGTI DMDLINTGVS ASERMRRDTF
ASSIRDIALE KMQIGGSSMR LSELLEELKK HGGNINTEIH LHDVRKAVAT LASEGFLVAE
GDRIKRV
