ID MCM3Z_XENTR Reviewed; 809 AA.
AC Q28BS0;
DT 27-JUN-2006, integrated into UniProtKB/Swiss-Prot.
DT 04-APR-2006, sequence version 1.
DT 27-MAR-2024, entry version 105.
DE RecName: Full=Zygotic DNA replication licensing factor mcm3;
DE EC=3.6.4.12;
DE AltName: Full=Zygotic minichromosome maintenance protein 3;
DE Short=zMCM3;
GN Name=zmcm3; ORFNames=TNeu014d13.1;
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] {ECO:0000312|EMBL:CAJ82887.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Neurula;
RG Sanger Xenopus tropicalis EST/cDNA project;
RL Submitted (MAR-2006) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Acts as a 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 (By similarity). {ECO:0000250|UniProtKB:P49739}.
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. Component of the CMG helicase complex, composed of the
CC mcm2-7 complex, the GINS complex and cdc45.
CC {ECO:0000250|UniProtKB:P49739}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:P49739}.
CC Chromosome {ECO:0000250|UniProtKB:P49739}. Note=Associated with
CC chromatin before the formation of nuclei and detaches from it as DNA
CC replication progresses. {ECO:0000250|UniProtKB:P49739}.
CC -!- SIMILARITY: Belongs to the MCM family. {ECO:0000255}.
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DR EMBL; CR942676; CAJ82887.1; -; mRNA.
DR RefSeq; NP_001039231.1; NM_001045766.1.
DR AlphaFoldDB; Q28BS0; -.
DR SMR; Q28BS0; -.
DR STRING; 8364.ENSXETP00000020877; -.
DR PaxDb; 8364-ENSXETP00000046917; -.
DR Ensembl; ENSXETT00000092089; ENSXETP00000064879; ENSXETG00000021701.
DR GeneID; 734092; -.
DR KEGG; xtr:734092; -.
DR AGR; Xenbase:XB-GENE-971646; -.
DR CTD; 734092; -.
DR Xenbase; XB-GENE-971646; zmcm3.
DR eggNOG; KOG0479; Eukaryota.
DR HOGENOM; CLU_000995_6_0_1; -.
DR InParanoid; Q28BS0; -.
DR OMA; EANHIMV; -.
DR OrthoDB; 5476523at2759; -.
DR PhylomeDB; Q28BS0; -.
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-68949; Orc1 removal from chromatin.
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 5.
DR Bgee; ENSXETG00000021701; Expressed in neurula embryo and 18 other cell types or tissues.
DR GO; GO:0071162; C:CMG complex; ISS:UniProtKB.
DR GO; GO:0042555; C:MCM complex; ISS:UniProtKB.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0004386; F:helicase activity; IEA:UniProtKB-KW.
DR GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR GO; GO:0032508; P:DNA duplex unwinding; IEA:InterPro.
DR GO; GO:0006270; P:DNA replication initiation; IEA:InterPro.
DR GO; GO:0030174; P:regulation of DNA-templated DNA replication initiation; IEA:UniProt.
DR CDD; cd17754; MCM3; 1.
DR Gene3D; 2.20.28.10; -; 1.
DR Gene3D; 3.30.1640.10; mini-chromosome maintenance (MCM) complex, chain A, domain 1; 1.
DR Gene3D; 2.40.50.140; Nucleic acid-binding proteins; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR InterPro; IPR003593; AAA+_ATPase.
DR InterPro; IPR031327; MCM.
DR InterPro; IPR008046; Mcm3.
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; DNA REPLICATION LICENSING FACTOR MCM FAMILY MEMBER; 1.
DR PANTHER; PTHR11630:SF46; DNA REPLICATION LICENSING FACTOR MCM3; 1.
DR Pfam; PF00493; MCM; 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; PR01659; MCMPROTEIN3.
DR SMART; SM00382; AAA; 1.
DR SMART; SM00350; MCM; 1.
DR SUPFAM; SSF50249; Nucleic acid-binding proteins; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 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; Nucleotide-binding; Nucleus; Reference proteome.
FT CHAIN 1..809
FT /note="Zygotic DNA replication licensing factor mcm3"
FT /id="PRO_0000240593"
FT DOMAIN 297..504
FT /note="MCM"
FT /evidence="ECO:0000255"
FT REGION 664..741
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 479..482
FT /note="Arginine finger"
FT COMPBIAS 664..716
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 347..354
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255"
SQ SEQUENCE 809 AA; 90823 MW; 449F25460591C718 CRC64;
MAAPAVTELE DQEMREAQRE YLDFLDDEED QGIYQSKVRD MISENQYRLI VNVNDLRKKN
EKRANMLMNN AFEGLIAFQR ALKDFVASID GTYAKQYEEF YIGLEGSFGN KHVTPRTLTS
RCLSCIVCVE GIVTKCSLVR PKVVRSVHYC PATKKTIERK YTDLTSLEAF PSSAVYPTKD
EENNPLETEY GLSIYKDHQT ITIQEMPEKA PAGQLPRSVD IILDDDLVDK VKPGDRVQVI
GTYRCLPSKQ NGYTSASFRT ILIACNVIQM SKEVTPVFSA DDLAKIKKFS KSHSKDIFEQ
LSRSLAPSIH GHLYIKKAIL CMLLGGVEKV LDNGTRIRGD INVLLIGDPS VAKSQLLRYV
LCTAPRAIPT TGRGSSGVGL TAAVTTDQET GERRLEAGAM VLADRGVVCI DEFDKMSDMD
RTAIHEVMEQ GRVTIAKAGI HARLNARCSV LAAANPVYGR YDQYKTPMDN IGLQDSLLSR
FDLLFIMLDQ MDPEQDREIS DHVLRMHRYR AAGEQDGDAM PLGSAVDILA TNDPNVTSEE
QQELQVYEKH DSLLHGVKKR KEKILSVEFM RKYVHVAKIF KPVLTQEAAS FIAEEYSRLR
NQDQLSTDVA RTSPVTARTL ETLIRLSTAH AKVRMSKTVQ LQDAEAAIEL VQYAYFKKVL
EKEKKRRRRD EDSDTEGEQQ TQPDGEAKKR RKKRRAQEGE SHDPYEFSDT EDETPVVHTP
KTPVNGQEEM ETDSSAKPGL SGERLKAFKS ALLGAFKSAH AQSIAMEALM EAINKRNDSP
FSQAEVKAAL ELMEEANHIM VSDNIVFLI
//
