MCM33_MAIZE
ID MCM33_MAIZE Reviewed; 768 AA.
AC Q9SX03;
DT 12-JUN-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 104.
DE RecName: Full=DNA replication licensing factor MCM3 homolog 3;
DE EC=3.6.4.12;
DE AltName: Full=Replication origin activator 3;
DE Short=ROA-3;
GN Name=ROA3;
OS Zea mays (Maize).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; PACMAD clade;
OC Panicoideae; Andropogonodae; Andropogoneae; Tripsacinae; Zea.
OX NCBI_TaxID=4577;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=cv. LG11; TISSUE=Root;
RA Sabelli P.A., Parker J.S., Barlow P.W.;
RT "cDNA and promoter sequences for MCM3 homologues from maize, and protein
RT localization in cycling cells.";
RL J. Exp. Bot. 50:1315-1322(1999).
CC -!- FUNCTION: Acts as a factor that allows the DNA to undergo a single
CC round of replication per cell cycle. Required for DNA replication and
CC cell proliferation (By similarity). May act as a component of the MCM
CC complex which is the putative replicative helicase of the replication
CC licensing system in eukaryotic cells. {ECO:0000250}.
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 -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the MCM family. {ECO:0000305}.
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DR EMBL; AF073331; AAD48087.1; -; mRNA.
DR AlphaFoldDB; Q9SX03; -.
DR SMR; Q9SX03; -.
DR PRIDE; Q9SX03; -.
DR MaizeGDB; 131629; -.
DR Proteomes; UP000007305; Unplaced.
DR ExpressionAtlas; Q9SX03; baseline and differential.
DR GO; GO:0042555; C:MCM complex; IBA:GO_Central.
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:0003697; F:single-stranded DNA binding; IBA:GO_Central.
DR GO; GO:0006271; P:DNA strand elongation involved in DNA replication; IBA:GO_Central.
DR GO; GO:0000727; P:double-strand break repair via break-induced replication; IBA:GO_Central.
DR GO; GO:1902975; P:mitotic DNA replication initiation; IBA:GO_Central.
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 2: Evidence at transcript level;
KW ATP-binding; Cell cycle; DNA replication; DNA-binding; Helicase; Hydrolase;
KW Nucleotide-binding; Nucleus; Reference proteome.
FT CHAIN 1..768
FT /note="DNA replication licensing factor MCM3 homolog 3"
FT /id="PRO_0000292981"
FT DOMAIN 290..497
FT /note="MCM"
FT REGION 661..690
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 472..475
FT /note="Arginine finger"
FT BINDING 340..347
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255"
SQ SEQUENCE 768 AA; 85209 MW; B5EB8658687B64F4 CRC64;
MEINEEAMAA HKRAFLDFLD QDVGKGVYMQ AVRDMVQNKR HRLIIGMDDL RNHNLDLARR
VIRTPGEYMQ PASDAVSEVA RNLDPKFLKE GERVMVGFSG PFGFHRVTPR DLMSSFIGTM
VCVEGIVTKC SLVRPKVVKS VHFCPVTGDF LSREYRDITS FVGLPTGSVY PTRDDNGNLL
VTEYGMCEYK DHQTLSMQEV PENSAPGQLP RTVDVIVEDD LVDCCKPGDR VSIVGVYKAL
PGKSKGSVSG VFRTVLIANN VSLLNKEANA PVYTREDLKR MKEISRRNDT FDLLGNSLAP
SIYGHLWIKK AVVLLMLGGV EKNLKNGTHL RGDINMMMVG DPSVAKSQLL RAVMNIAPLA
ISTTGRGSSG VGLTAAVTSD QETGERRLEA GAMVLADRGV VCIDEFDKMN DQDRVAIHEV
MEQQTVTIAK AGIHASLNAR CSVIAAANPI YGTYDRSLTP TKNIGLPDSL LSRFDLLFIV
LDQMDPEIDR QISEHVARMH RYCTDDGGAR SLDKEGYAEE DDGDANAAIF VKYDRMLHGQ
DRRRGKKSKQ DRLTVKFLKK YIHYAKNLIQ PRLTDEASDH IATSYAELRD GSANAKSGGG
TLPITARTLE TIIRLSTAHA KMKLRHEVLK SDVEAALQVL NFAIYHKELT EMEEREQREM
EMKQQADHDA GATGGTVDGH GSSGNDPMDV DVGSNDQNVS AERIQAFEAL LGQHVLANHI
DQMSIDEIEQ MVNRESTAPY TRSQVEFILE RMQDANRVMI RDGVVRII