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MCM6_ARATH
ID   MCM6_ARATH              Reviewed;         831 AA.
AC   F4KAB8;
DT   16-APR-2014, integrated into UniProtKB/Swiss-Prot.
DT   28-JUN-2011, sequence version 1.
DT   03-AUG-2022, entry version 72.
DE   RecName: Full=DNA replication licensing factor MCM6;
DE            EC=3.6.4.12;
DE   AltName: Full=Minichromosome maintenance protein 6;
DE            Short=AtMCM6;
GN   Name=MCM6; OrderedLocusNames=At5g44635; ORFNames=K15C23;
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;
RA   Kaneko T., Katoh T., Asamizu E., Sato S., Nakamura Y., Kotani H.,
RA   Tabata S.;
RT   "Structural analysis of Arabidopsis thaliana chromosome 5. XI.";
RL   Submitted (MAR-1999) to the EMBL/GenBank/DDBJ databases.
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   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   [4]
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   [5]
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}.
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DR   EMBL; AB024024; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; CP002688; AED95141.1; -; Genomic_DNA.
DR   RefSeq; NP_680393.1; NM_148088.2.
DR   AlphaFoldDB; F4KAB8; -.
DR   SMR; F4KAB8; -.
DR   BioGRID; 19742; 16.
DR   IntAct; F4KAB8; 14.
DR   MINT; F4KAB8; -.
DR   STRING; 3702.AT5G44635.1; -.
DR   PaxDb; F4KAB8; -.
DR   PRIDE; F4KAB8; -.
DR   ProteomicsDB; 250827; -.
DR   EnsemblPlants; AT5G44635.1; AT5G44635.1; AT5G44635.
DR   GeneID; 834492; -.
DR   Gramene; AT5G44635.1; AT5G44635.1; AT5G44635.
DR   KEGG; ath:AT5G44635; -.
DR   Araport; AT5G44635; -.
DR   TAIR; locus:504954997; AT5G44635.
DR   eggNOG; KOG0480; Eukaryota.
DR   HOGENOM; CLU_000995_3_2_1; -.
DR   InParanoid; F4KAB8; -.
DR   OMA; KYYIAQI; -.
DR   PhylomeDB; F4KAB8; -.
DR   PRO; PR:F4KAB8; -.
DR   Proteomes; UP000006548; Chromosome 5.
DR   ExpressionAtlas; F4KAB8; baseline and differential.
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:0006270; P:DNA replication initiation; IEA:InterPro.
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:1902969; P:mitotic DNA replication; IBA:GO_Central.
DR   Gene3D; 2.40.50.140; -; 1.
DR   Gene3D; 3.40.50.300; -; 1.
DR   InterPro; IPR031327; MCM.
DR   InterPro; IPR008049; MCM6.
DR   InterPro; IPR041024; Mcm6_C.
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; PTHR11630; 1.
DR   Pfam; PF00493; MCM; 1.
DR   Pfam; PF18263; MCM6_C; 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; PR01662; MCMPROTEIN6.
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..831
FT                   /note="DNA replication licensing factor MCM6"
FT                   /id="PRO_0000425996"
FT   DOMAIN          345..551
FT                   /note="MCM"
FT   ZN_FING         155..182
FT                   /note="C4-type"
FT                   /evidence="ECO:0000255"
FT   REGION          258..278
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          666..705
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           527..530
FT                   /note="Arginine finger"
FT   COMPBIAS        671..688
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         395..402
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   831 AA;  92851 MW;  310467E0D92DEB79 CRC64;
     MEAFGGFVMD EQAIQVENVF LEFLKSFRLD ANKPELYYEA EIEAIRGGES TMMYIDFSHV
     MGFNDALQKA IADEYLRFEP YLRNACKRFV IEMNPSFISD DTPNKDINVS FYNLPFTKRL
     RELTTAEIGK LVSVTGVVTR TSEVRPELLY GTFKCLDCGS VIKNVEQQFK YTQPTICVSP
     TCLNRARWAL LRQESKFADW QRVRMQETSK EIPAGSLPRS LDVILRHEIV EQARAGDTVI
     FTGTVVVIPD ISALAAPGER AECRRDSSQQ KSSTAGHEGV QGLKALGVRD LSYRLAFIAN
     SVQIADGSRN TDMRNRQNDS NEDDQQQFTA EELDEIQQMR NTPDYFNKLV GSMAPTVFGH
     QDIKRAVLLM LLGGVHKTTH EGINLRGDIN VCIVGDPSCA KSQFLKYTAG IVPRSVYTSG
     KSSSAAGLTA TVAKEPETGE FCIEAGALML ADNGICCIDE FDKMDIKDQV AIHEAMEQQT
     ISITKAGIQA TLNARTSILA AANPVGGRYD KSKPLKYNVN LPPAILSRFD LVYVMIDDPD
     EVTDYHIAHH IVRVHQKHEA ALSPEFTTVQ LKRYIAYAKT LKPKLSPEAR KLLVESYVAL
     RRGDTTPGTR VAYRMTVRQL EALIRLSEAI ARSHLEILVK PSHVLLAVRL LKTSVISVES
     GDIDLSEYQD ANGDNMDDTD DIENPVDGEE DQQNGAAEPA SATADNGAAA QKLVISEEEY
     DRITQALVIR LRQHEETVNK DSSELPGIRQ KELIRWFIDQ QNEKKKYSSQ EQVKLDIKKL
     RAIIESLVCK EGHLIVLANE QEEAAEAEET KKKSSQRDER ILAVAPNYVI E
 
 
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