MC6ZA_XENLA
ID MC6ZA_XENLA Reviewed; 823 AA.
AC Q498J7; O73711; Q6AZF4;
DT 16-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT 13-SEP-2005, sequence version 1.
DT 03-AUG-2022, entry version 82.
DE RecName: Full=Zygotic DNA replication licensing factor mcm6-A;
DE EC=3.6.4.12;
DE AltName: Full=Zygotic minichromosome maintenance protein 6-A;
DE Short=zMCM6-A;
DE Short=zMCM6a;
GN Name=zmcm6-a; Synonyms=zmcm6a {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:0000312|EMBL:AAH78072.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Embryo {ECO:0000312|EMBL:AAH78072.1};
RG NIH - Xenopus Gene Collection (XGC) project;
RL Submitted (JUL-2004) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000305, ECO:0000312|EMBL:AAC41268.1}
RP NUCLEOTIDE SEQUENCE [MRNA] OF 663-823, IDENTIFICATION IN A COMPLEX WITH
RP ZMCM3; MCM4 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).
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. May replace mmcm6 in
CC the complex that functions during licensing of DNA replication.
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; BC078072; AAH78072.1; -; mRNA.
DR EMBL; BC100191; AAI00192.1; -; mRNA.
DR EMBL; AF031140; AAC41268.1; -; mRNA.
DR RefSeq; NP_001131039.1; NM_001137567.1.
DR AlphaFoldDB; Q498J7; -.
DR SMR; Q498J7; -.
DR IntAct; Q498J7; 1.
DR MINT; Q498J7; -.
DR DNASU; 394426; -.
DR GeneID; 394426; -.
DR KEGG; xla:394426; -.
DR CTD; 394426; -.
DR Xenbase; XB-GENE-962683; mcm6.L.
DR OrthoDB; 266497at2759; -.
DR Proteomes; UP000186698; Chromosome 9_10L.
DR Bgee; 394426; Expressed in neurula embryo and 19 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; IC: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 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..823
FT /note="Zygotic DNA replication licensing factor mcm6-A"
FT /id="PRO_0000235884"
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 663..710
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 529..532
FT /note="Arginine finger"
FT COMPBIAS 667..683
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"
FT CONFLICT 103
FT /note="G -> S (in Ref. 1; AAH78072)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 823 AA; 93067 MW; EEF611337302DAB4 CRC64;
MDLVDPSQSA AAAAGTQLVK DEVAEKCQKL FQDFLEEFQG SDGELKYQSD AEELIRPERN
TLLVSFVDLE QFNQQLATTI QEEFYRVYPY LCRAVRAFAR DHGNIPQNKE FYVAFQDLPT
RHKIRELTTP RIGSLLRISA QVVRTHPVHP ELVSGTFLCL DCQTLVRDVE QQFKYTQPSI
CRNPVCANRR RFMLDTNKSR FVDFQKVRIQ ETQAELPRGS IPRSVEVILR AEAVESCQAG
DRCDFTGSLI VVPDISQLST PGVRAETSSR VGGREGYEAE GVQGLRALGV RDLSYKLVFL
ACYVCPTNPR FGGKELHEED MTAESIKNQM SVKEWEKVFE MSQDKNLYHN LCTSLFPTVH
GNDEVKRGIL LMLFGGVPKS TMEGTSLRGD INVCVVGDPS TAKSQFLKHV EEFSPRAVYT
SGKASTAAGL TAAVVKDEES HEFVIEAGAL MLADNGVCCI DEFDKMDTKD QVAIHEAMEQ
QTISITKAGV KATLNARTSI LAAANPVGGR YDRAKSLKQN VNLSAPIMSR FDLFFILVDE
CNEVTDYAIA RRIVDLHSRI EESIDRVYTV DEVRRYLLFA RQFKPKISKE SADFIVEQYK
RLRQRDGSGV TKSAWRITVR QLESMIRLSE GMARMHCSDE VQPKHVKEAF RLLNKSIIRV
ETPDVNLDQD DEHEPEDETQ EGTNGDAEVP NGVNGHVNGI NGHSQESNAA AAKPSLRLNF
AEYKRISNLL VQQLRKMEDE DETSQRRSEL MNWYLKEIES EIDSEEELIN RKQIIDKVIH
RLVHYDQILI ELTQTELKGT GDEVVAKEED PYLVVNPNYI LED
