MCM6Z_XENTR
ID MCM6Z_XENTR Reviewed; 823 AA.
AC Q6P1V8;
DT 16-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 100.
DE RecName: Full=Zygotic DNA replication licensing factor mcm6;
DE EC=3.6.4.12;
DE AltName: Full=Zygotic minichromosome maintenance protein 6;
DE Short=zMCM6;
GN Name=zmcm6 {ECO:0000250|UniProtKB:Q498J7};
OS Xenopus tropicalis (Western clawed frog) (Silurana tropicalis).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Silurana.
OX NCBI_TaxID=8364;
RN [1] {ECO:0000312|EMBL:AAH64853.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Embryo {ECO:0000312|EMBL:AAH64853.1};
RG NIH - Xenopus Gene Collection (XGC) project;
RL Submitted (JAN-2004) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Acts as component of the mcm2-7 complex (mcm complex) which
CC is the putative replicative helicase essential for 'once per cell
CC cycle' DNA replication initiation and elongation in eukaryotic cells.
CC The active ATPase sites in the mcm2-7 ring are formed through the
CC interaction surfaces of two neighboring subunits such that a critical
CC structure of a conserved arginine finger motif is provided in trans
CC relative to the ATP-binding site of the Walker A box of the adjacent
CC subunit. The six ATPase active sites, however, are likely to contribute
CC differentially to the complex helicase activity. The existence of
CC maternal and zygotic forms of mcm3 and mcm6 suggests that specific
CC forms of mcm2-7 complexes may be used during different stages of
CC development. May replace mmcm6 in the mcm2-7 complex (By similarity).
CC {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 mcm2-7 complex (RLF-M). The complex forms a
CC toroidal hexameric ring with the proposed subunit order mcm2-mcm6-mcm4-
CC mcm7-mcm3-mcm5. Begins to associate with zmcm3, mcm4 and mcm7 into mcm
CC complexes at the neurula stage (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. Note=Associated with
CC chromatin before the formation of nuclei and detaches from it as DNA
CC replication progresses. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the MCM family. {ECO:0000255}.
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DR EMBL; BC064853; AAH64853.1; -; mRNA.
DR RefSeq; NP_989393.1; NM_204062.1.
DR AlphaFoldDB; Q6P1V8; -.
DR SMR; Q6P1V8; -.
DR GeneID; 395030; -.
DR KEGG; xtr:395030; -.
DR CTD; 395030; -.
DR Xenbase; XB-GENE-962678; mcm6.
DR InParanoid; Q6P1V8; -.
DR OrthoDB; 266497at2759; -.
DR Reactome; R-XTR-176187; Activation of ATR in response to replication stress.
DR Reactome; R-XTR-68867; Assembly of the pre-replicative complex.
DR Reactome; R-XTR-68962; Activation of the pre-replicative complex.
DR Reactome; R-XTR-69052; Switching of origins to a post-replicative state.
DR Proteomes; UP000008143; Chromosome 9.
DR Proteomes; UP000790000; Unplaced.
DR GO; GO:0042555; C:MCM complex; ISS:UniProtKB.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
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 GO; GO:0030174; P:regulation of DNA-templated DNA replication initiation; IEA:UniProt.
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 2: Evidence at transcript 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..823
FT /note="Zygotic DNA replication licensing factor mcm6"
FT /id="PRO_0000235886"
FT DOMAIN 347..554
FT /note="MCM"
FT /evidence="ECO:0000255"
FT ZN_FING 159..186
FT /note="C4-type"
FT /evidence="ECO:0000255"
FT REGION 666..713
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 529..532
FT /note="Arginine finger"
FT COMPBIAS 667..681
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 397..404
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255"
SQ SEQUENCE 823 AA; 93003 MW; 7D044655FC3EE8E5 CRC64;
MDLVDPSQSA AAAAGTQTVK DEVSEKCQKL FQDFLEEFRG SDGELKYQSD AEELIRPERN
TLLVSFIDLE QFNQQLATTI QEEFYRVYPY LCRAVKAFAR DHGNVPQNKE FYVAFQDLPT
RHKIRELTTP RIGSLLRISG QVVRTHPVHP ELVSGTFLCL DCQTLVRDVE QQFKYTQPSI
CRNPVCANRR RFMLDTNKSR FVDFQKVRIQ ETQAELPRGS IPRSVEVILR AEAVESCQAG
DRCDFTGSLI VVPDISQLAT PGVRAETSAR VGGTEGYQAE GVQGLRALGV RDLSYKLVFL
ACYVCPTNPR FGGKDLHEED MTAESIKNQM SVKEWEKVFE MSQDKNLYHN LCTSLFPTVH
GNDEVKRGIL LMLFGGVPKT TMEGTSLRGD INVCIVGDPS TAKSQFLKHV EEFSPRAVYT
SGKASSAAGL TAAVVKDEES HEFVIEAGAL MLADNGVCCI DEFDKMDTKD QVAIHEAMEQ
QTISITKAGV KATLNARTSI LAAANPVGGR YDRAKSLKQN INLSAPIMSR FDLFFILVDE
CNEVTDYAIA RRIVDLHSRI EESIDRVYTL DEVRRYLLFA RQFKPKISKE SEDFIVEQYK
RLRQRDGTGV TKSAWRITVR QLESMIRLSE GMARMHCSDE VQPKHVKEAF RLLNKSIIRV
ETPDVNLDQE DEHEAEEEPQ EVINGDASVP SGVNGHVNGM NGHAEEPNAA TPKPSLRLNF
AEYKRISNLL VLQLRKMEDE DETSQRKSEL INWYLKEIES EIDSEEELVT RKQIIDKVVH
RLVHYDQILI ELTQTGLKGT GDEEVPKEED PYLVVNPNYI LED
