ID   MC6ZB_XENLA             Reviewed;         825 AA.
AC   Q7ZY18; O73710;
DT   16-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2003, sequence version 1.
DT   03-AUG-2022, entry version 99.
DE   RecName: Full=Zygotic DNA replication licensing factor mcm6-B;
DE            EC=3.6.4.12;
DE   AltName: Full=Zygotic minichromosome maintenance protein 6-B;
DE            Short=zMCM6-B;
DE            Short=zMCM6b;
GN   Name=zmcm6-b; Synonyms=zmcm6b {ECO:0000303|PubMed:9512418};
OS   Xenopus laevis (African clawed frog).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC   Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX   NCBI_TaxID=8355;
RN   [1] {ECO:0000305, ECO:0000312|EMBL:AAC41267.1}
RP   NUCLEOTIDE SEQUENCE [MRNA], IDENTIFICATION IN A COMPLEX WITH ZMCM3; MCM4
RP   AND MCM7, AND DEVELOPMENTAL STAGE.
RC   TISSUE=Embryo {ECO:0000269|PubMed:9512418};
RX   PubMed=9512418; DOI=10.1016/s0960-9822(98)70136-8;
RA   Sible J.C., Erikson E., Hendrickson M., Maller J.L., Gautier J.;
RT   "Developmental regulation of MCM replication factors in Xenopus laevis.";
RL   Curr. Biol. 8:347-350(1998).
RN   [2] {ECO:0000312|EMBL:AAH44019.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Embryo {ECO:0000312|EMBL:AAH44019.1};
RG   NIH - Xenopus Gene Collection (XGC) project;
RL   Submitted (JAN-2003) 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.
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 (By simililarity). Begins to associate with zmcm3, mcm4
CC       and mcm7 into mcm complexes at the neurula stage.
CC       {ECO:0000269|PubMed:9512418}.
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   -!- DEVELOPMENTAL STAGE: Expressed zygotically. Expression begins after the
CC       midblastula transition (MBT) at the neurula stage.
CC       {ECO:0000269|PubMed:9512418}.
CC   -!- SIMILARITY: Belongs to the MCM family. {ECO:0000255}.
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DR   EMBL; AF031139; AAC41267.1; -; mRNA.
DR   EMBL; BC044019; AAH44019.1; -; mRNA.
DR   RefSeq; NP_001080590.1; NM_001087121.1.
DR   AlphaFoldDB; Q7ZY18; -.
DR   SMR; Q7ZY18; -.
DR   ComplexPortal; CPX-2943; MCM complex.
DR   IntAct; Q7ZY18; 4.
DR   DNASU; 380282; -.
DR   GeneID; 380282; -.
DR   KEGG; xla:380282; -.
DR   CTD; 380282; -.
DR   Xenbase; XB-GENE-6256556; mcm6.S.
DR   OMA; KYYIAQI; -.
DR   OrthoDB; 266497at2759; -.
DR   Proteomes; UP000186698; Chromosome 9_10S.
DR   Bgee; 380282; Expressed in neurula embryo and 18 other tissues.
DR   GO; GO:0042555; C:MCM complex; IPI:UniProtKB.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0016887; F:ATP hydrolysis activity; IEA:RHEA.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
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:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR   GO; GO:0006270; P:DNA replication initiation; IEA:InterPro.
DR   GO; GO:0030174; P:regulation of DNA-templated DNA replication initiation; IDA:ComplexPortal.
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..825
FT                   /note="Zygotic DNA replication licensing factor mcm6-B"
FT                   /id="PRO_0000235885"
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          668..690
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
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"
FT   CONFLICT        550
FT                   /note="A -> T (in Ref. 1; AAC41267)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        581
FT                   /note="R -> K (in Ref. 1; AAC41267)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        793
FT                   /note="E -> A (in Ref. 1; AAC41267)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        810
FT                   /note="Missing (in Ref. 1; AAC41267)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   825 AA;  93378 MW;  A96CF39A8BE3FDF4 CRC64;
     MDLVDPSQSA AAAAGTQLVK DEVAEKCQKL FQDFLEEFRG SDGELKYQSD AEELIRPERN
     TLLVSFVDLE QFNQQLATTI QEEFYRVYPY LCRAVKAFAR DHGNIPQNKE FYVAFQELPT
     RHKIRELTTP RIGSLLRISG QVVRTHPVHP ELVSGTFLCL DCQTLVRDVE QQFKYTQPSI
     CRNPVCANRK RFMLDTNKSR FVDFQKVRIQ ETQAELPRGS IPRSVEVILR AEAVESCQAG
     DRCDFTGSLI VVPDISQLST PGVRAETSSR VGGREGYEAE GVQGLRALGV RDLSYKLVFL
     ACYVCPTNPR FGGKDLHEED MTAESIKNQM SVKEWEKVFE MSQDKNLYHN LCTSLFPTVH
     GNDEVKRGIL LMLFGGVPKS TMEGTSLRGD INVCVVGDPS TAKSQFLKHV EEFSPRAVYT
     SGKASTAAGL TAAVVRDEES HEFVIEAGAL MLADNGVCCI DEFDKMDTKD QVAIHEAMEQ
     QTISITKAGV KATLNARTSI LAAANPVGGR YDRAKSLKQN VNLSAPIMSR FDLFFILVDE
     CNEVTDYAIA RRIVDLHSRI EESIDRVYTL DEVRRYLLFA RQFKPKISKE SEDFIVEQYK
     RLRQRDGSGV TKSAWRITVR QLESMIRLSE GMARMHCSDE VQPKHVKEAF RLLNKSIIRV
     ETPDVNLDQE DEHEVEEPQE GINGDADVPN GVNGHINGIN GHAEETNAAP PKPSLRLNFA
     EYKRISNLLV LQLRKIEDED DENETSQRKS ELINWYLKEI ESEIDSEEEL VNRKQIIDKV
     IHRLVHYDQI LIELIQTGLK GTEDENVAKE EDPYLVVNPN YILED