ID   MCM6M_XENTR             Reviewed;         821 AA.
AC   Q28CM3; Q05AR6;
DT   16-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT   04-APR-2006, sequence version 1.
DT   03-AUG-2022, entry version 96.
DE   RecName: Full=Maternal DNA replication licensing factor mcm6;
DE            EC=3.6.4.12;
DE   AltName: Full=Maternal minichromosome maintenance protein 6;
DE            Short=mMCM6;
GN   Name=mmcm6 {ECO:0000250|UniProtKB:Q5FWY4}; ORFNames=TEgg078c13.1;
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]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Egg;
RG   Sanger Xenopus tropicalis EST/cDNA project;
RL   Submitted (MAR-2006) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 2-821.
RC   STRAIN=N6; TISSUE=Ovary;
RG   NIH - Xenopus Gene Collection (XGC) project;
RL   Submitted (SEP-2006) 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. {ECO:0000250|UniProtKB:Q5FWY4}.
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. The heterodimer of mmcm3/mcm5 interacts with mcm4,
CC       mmcm6, mcm7 and weakly with mcm2. Component of the CMG helicase
CC       complex, composed of the mcm2-7 complex, the GINS complex and cdc45.
CC       {ECO:0000250|UniProtKB:Q5FWY4}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q5FWY4}.
CC       Chromosome {ECO:0000250|UniProtKB:Q5FWY4}. Note=Associated with
CC       chromatin before the formation of nuclei and detaches from it as DNA
CC       replication progresses. {ECO:0000250|UniProtKB:Q5FWY4}.
CC   -!- SIMILARITY: Belongs to the MCM family. {ECO:0000255}.
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DR   EMBL; CR926305; CAJ82233.1; -; mRNA.
DR   EMBL; BC123991; AAI23992.1; -; mRNA.
DR   RefSeq; NP_001016221.1; NM_001016221.2.
DR   AlphaFoldDB; Q28CM3; -.
DR   SMR; Q28CM3; -.
DR   STRING; 8364.ENSXETP00000034197; -.
DR   PaxDb; Q28CM3; -.
DR   Ensembl; ENSXETT00000034197; ENSXETP00000034197; ENSXETG00000015671.
DR   GeneID; 548975; -.
DR   KEGG; xtr:548975; -.
DR   CTD; 4175; -.
DR   Xenbase; XB-GENE-5870537; mcm6.2.
DR   eggNOG; KOG0480; Eukaryota.
DR   HOGENOM; CLU_000995_3_2_1; -.
DR   InParanoid; Q28CM3; -.
DR   OMA; VQDENMA; -.
DR   OrthoDB; 266497at2759; -.
DR   PhylomeDB; Q28CM3; -.
DR   TreeFam; TF105646; -.
DR   Proteomes; UP000008143; Chromosome 6.
DR   Proteomes; UP000790000; Unplaced.
DR   Bgee; ENSXETG00000015671; Expressed in ovary and 8 other tissues.
DR   ExpressionAtlas; Q28CM3; baseline.
DR   GO; GO:0000785; C:chromatin; ISS:UniProtKB.
DR   GO; GO:0071162; C:CMG complex; ISS:UniProtKB.
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; ISS:UniProtKB.
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; ISS:UniProtKB.
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; Chromosome; DNA replication; DNA-binding;
KW   Helicase; Hydrolase; Metal-binding; Nucleotide-binding; Nucleus;
KW   Reference proteome; Zinc; Zinc-finger.
FT   CHAIN           1..821
FT                   /note="Maternal DNA replication licensing factor mcm6"
FT                   /id="PRO_0000235888"
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   MOTIF           529..532
FT                   /note="Arginine finger"
FT   BINDING         397..404
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   821 AA;  92583 MW;  6EC14409164321B1 CRC64;
     MELGGPATAG ATDTAGQLFK DELSDKCQKL FLEFLEECKG KDGSNLYVSA AEELVRPERN
     TLVVNFTDIE YYNQQLATTI QEEYYRVYPH LCRAVRSFAR QMGNIPANKE FYVAFSDFPA
     RQKIRELSSA KIGTLLRISG QVVRTHPVHP ELVSGTFLCM DCQSVVKDVE QQFRYTQPTI
     CKNPVCANRR RFTLDTNKSR FVDFQKVRIQ ETQAELPRGA IPRSVEIILR AEAVETAMAG
     DRCDFTGTLI VVPDISALAA GDARMETGAK VTGGEGFNSE GVQGLKALGV RDLSYRLAFL
     ACHVGATNPR FGGKDLREED QTAESIKNQM TVQEWEKVFE MSQDKNLYHN LCTSLFPTIH
     GNDEIKRGVL LMLFGGVPKT TMEGTSLRGD INVCIVGDPS TSKSQFLKHV EEFSPRAVYT
     SGKASSAAGL TAAVVKDEES HEFVIEAGAL MLADNGVCCI DEFDKMDLKD QVAIHEAMEQ
     QTISITKAGV KATLNARTSI LAAANPVGGR YERSKSLKHN VNLSAPIMSR FDLFFILVDE
     CNEVTDYAIA RRIVDLHARN EESIERVYSI EDIQRYLLFA RQFQPKITKE AEEFIVEQYR
     RLRQRDGSGV AKSSWRITVR QLESLIRLSE SMARMHCSDE VQPKHVKEAF RLLSKSIIRV
     DTPDVSFDQG EDEKNVEEEV NNANLNNGEE AMETNQDEPI NDKPSTNAGL KMSFAEYKQI
     SNLLVLHMQK MEEVEEECHL TTTDLVNWYL KEMEAEIETE TELILKKRLI EKVIHRLINY
     DHILIELNKS ELKTMDDSKE TSEDAAEDRI LVVNPNYMLE D