MCM3Z_XENLA
ID MCM3Z_XENLA Reviewed; 806 AA.
AC Q7ZXZ0;
DT 27-JUN-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 mcm3;
DE EC=3.6.4.12;
DE AltName: Full=Zygotic minichromosome maintenance protein 3;
DE Short=zMCM3;
GN Name=zmcm3 {ECO:0000250|UniProtKB:P49739, ECO:0000250|UniProtKB:Q498J7};
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:AAH44051.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Embryo {ECO:0000312|EMBL:AAH44051.1};
RG NIH - Xenopus Gene Collection (XGC) project;
RL Submitted (JAN-2003) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000305}
RP IDENTIFICATION IN A COMPLEX WITH ZMCM6, AND DEVELOPMENTAL STAGE.
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. {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) (By similarity). The
CC complex forms a toroidal hexameric ring with the proposed subunit order
CC mcm2-mcm6-mcm4-mcm7-mcm3-mcm5 (By similarity). Begins to associate with
CC zmcm6 into mcm complexes at the neurula stage (PubMed:9512418).
CC Component of the CMG helicase complex, composed of the mcm2-7 complex,
CC the GINS complex and cdc45 (By similarity).
CC {ECO:0000250|UniProtKB:P49739, ECO:0000269|PubMed:9512418}.
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 -!- DEVELOPMENTAL STAGE: Expressed zygotically.
CC {ECO:0000269|PubMed:9512418}.
CC -!- SIMILARITY: Belongs to the MCM family. {ECO:0000255}.
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DR EMBL; BC044051; AAH44051.1; -; mRNA.
DR RefSeq; NP_001080158.1; NM_001086689.1.
DR AlphaFoldDB; Q7ZXZ0; -.
DR SMR; Q7ZXZ0; -.
DR BioGRID; 98092; 1.
DR MaxQB; Q7ZXZ0; -.
DR DNASU; 379850; -.
DR GeneID; 379850; -.
DR KEGG; xla:379850; -.
DR CTD; 379850; -.
DR Xenbase; XB-GENE-971651; zmcm3.L.
DR OMA; EANHIMV; -.
DR OrthoDB; 266497at2759; -.
DR Proteomes; UP000186698; Chromosome 5L.
DR Bgee; 379850; Expressed in neurula embryo and 18 other tissues.
DR GO; GO:0071162; C:CMG complex; ISS:UniProtKB.
DR GO; GO:0042555; C:MCM complex; IDA:UniProtKB.
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: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; 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; PTHR11630; 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; 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; Chromosome; DNA replication; DNA-binding;
KW Helicase; Hydrolase; Nucleotide-binding; Nucleus; Reference proteome.
FT CHAIN 1..806
FT /note="Zygotic DNA replication licensing factor mcm3"
FT /id="PRO_0000240592"
FT DOMAIN 295..502
FT /note="MCM"
FT /evidence="ECO:0000255"
FT REGION 662..738
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 477..480
FT /note="Arginine finger"
FT COMPBIAS 662..713
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 345..352
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255"
SQ SEQUENCE 806 AA; 90547 MW; 046BDA2DFFF0AB9A CRC64;
MAAVTELDDQ EMREAQREYL DFLDDEEDQG IYQSKVRDMI SENQYRLIVN INDLRRKNEK
RASLLMNNAF EGLIAFQRAL KDFVASIDGT YAKQYEDFYI GLEGSFGSKH VTPRTLTSRF
LSSVVCVEGI VTKCSLVRPK VVRSVHYCPA TKKTIERKYT DLTSLEAFPS SAVYPTKDEE
NNPLETEYGL SIYKDHQTIT IQEMPEKAPA GQLPRSVDII LDDDLVDKVK PGDRVQVIGT
YRCLPSKQNG YTSASFRTIL IACNVIQMSK EVTPVFSADD LAKIKKFSKS HSKDVFEQLS
RSLAPSIHGH SYIKKAILCM LLGGVEKVLD NGTRIRGDIN VLLIGDPSVA KSQLLRYVLF
TAPRAIPTTG RGSSGVGLTA AVTTDQETGE RRLEAGAMVL ADRGVVCIDE FDKMSDMDRT
AIHEVMEQGR VTIAKAGIHA RLNARCSVLA AANPVYGRYD QYKTPMENIG LQDSLLSRFD
LLFIMLDQMD PEHDREISDH VLRMHRYRSA GEQDGDALPL GSAVDILATE DPNVTSEEQQ
ELQVYEKHDS LLHGVKKRRE KVLSMEFMRK YIHVAKIFKP VLTQEAASFI AEEYTRLRNQ
DQMSTDVART SPVTARSLET LIRLSTAHAK VRMSKTVQLQ DAEAALELVQ YAYFKKVLEK
EKKRRRREGE SDTEEEQTQP DGEGKKRRKK RRAQDGESHD PYEFSDTEDE TPVVHTPKTP
VNGQEEMETD SSAKPGLSGD RLKAFKSALL DAFKAAHAQS IAMAAMMEAI NKNNDSPFSQ
AEVKAALELM EEANHIMVSD NIVFLI
