ID MCM3_CHICK Reviewed; 812 AA.
AC Q5ZMN2;
DT 26-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 23-NOV-2004, sequence version 1.
DT 24-JAN-2024, entry version 111.
DE RecName: Full=DNA replication licensing factor MCM3;
DE EC=3.6.4.12;
GN Name=MCM3; ORFNames=RCJMB04_1j4;
OS Gallus gallus (Chicken).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC Phasianinae; Gallus.
OX NCBI_TaxID=9031;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=CB; TISSUE=Bursa of Fabricius;
RX PubMed=15642098; DOI=10.1186/gb-2004-6-1-r6;
RA Caldwell R.B., Kierzek A.M., Arakawa H., Bezzubov Y., Zaim J., Fiedler P.,
RA Kutter S., Blagodatski A., Kostovska D., Koter M., Plachy J., Carninci P.,
RA Hayashizaki Y., Buerstedde J.-M.;
RT "Full-length cDNAs from chicken bursal lymphocytes to facilitate gene
RT function analysis.";
RL Genome Biol. 6:R6.1-R6.9(2005).
CC -!- FUNCTION: Acts as a component of the MCM2-7 complex (MCM complex) which
CC is the replicative helicase essential for 'once per cell cycle' DNA
CC replication initiation and elongation in eukaryotic cells. Core
CC component of CDC45-MCM-GINS (CMG) helicase, the molecular machine that
CC unwinds template DNA during replication, and around which the replisome
CC is built. The active ATPase sites in the MCM2-7 ring are formed through
CC the interaction surfaces of two neighboring subunits such that a
CC critical structure of a conserved arginine finger motif is provided in
CC trans relative to the ATP-binding site of the Walker A box of the
CC adjacent subunit. The six ATPase active sites, however, are likely to
CC contribute differentially to the complex helicase activity. Required
CC for the entry in S phase and for cell division.
CC {ECO:0000250|UniProtKB:P25205}.
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 Evidence={ECO:0000250|UniProtKB:P25205};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:13066;
CC Evidence={ECO:0000250|UniProtKB:P25205};
CC -!- SUBUNIT: Component of the MCM2-7 complex. The complex forms a toroidal
CC hexameric ring with the proposed subunit order MCM2-MCM6-MCM4-MCM7-
CC MCM3-MCM5. Component of the CMG helicase complex, a hexameric ring of
CC related MCM2-7 subunits stabilized by CDC45 and the tetrameric GINS
CC complex. {ECO:0000250|UniProtKB:P25205}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:P25205}.
CC Chromosome {ECO:0000250|UniProtKB:P25205}. Note=Associated with
CC chromatin before the formation of nuclei and detaches from it as DNA
CC replication progresses. {ECO:0000250|UniProtKB:P25205}.
CC -!- SIMILARITY: Belongs to the MCM family. {ECO:0000305}.
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DR EMBL; AJ719352; CAG31011.1; -; mRNA.
DR RefSeq; NP_001006421.1; NM_001006421.1.
DR AlphaFoldDB; Q5ZMN2; -.
DR SMR; Q5ZMN2; -.
DR BioGRID; 682782; 1.
DR STRING; 9031.ENSGALP00000026858; -.
DR PaxDb; 9031-ENSGALP00000042687; -.
DR GeneID; 422043; -.
DR KEGG; gga:422043; -.
DR CTD; 4172; -.
DR VEuPathDB; HostDB:geneid_422043; -.
DR eggNOG; KOG0479; Eukaryota.
DR InParanoid; Q5ZMN2; -.
DR PhylomeDB; Q5ZMN2; -.
DR PRO; PR:Q5ZMN2; -.
DR Proteomes; UP000000539; Unassembled WGS sequence.
DR GO; GO:0071162; C:CMG complex; ISS:UniProtKB.
DR GO; GO:0042555; C:MCM complex; ISS:UniProtKB.
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:InterPro.
DR GO; GO:0003682; F:chromatin binding; IDA:AgBase.
DR GO; GO:0004386; F:helicase activity; IEA:UniProtKB-KW.
DR GO; GO:0003697; F:single-stranded DNA binding; IBA:GO_Central.
DR GO; GO:0032508; P:DNA duplex unwinding; IEA:InterPro.
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 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..812
FT /note="DNA replication licensing factor MCM3"
FT /id="PRO_0000318904"
FT DOMAIN 296..503
FT /note="MCM"
FT REGION 663..741
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 478..481
FT /note="Arginine finger"
FT COMPBIAS 684..706
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 354
FT /ligand="ADP"
FT /ligand_id="ChEBI:CHEBI:456216"
FT /ligand_note="ligand shared with MCM5"
FT /evidence="ECO:0000250|UniProtKB:P25205"
FT BINDING 394
FT /ligand="ADP"
FT /ligand_id="ChEBI:CHEBI:456216"
FT /ligand_note="ligand shared with MCM5"
FT /evidence="ECO:0000250|UniProtKB:P25205"
FT BINDING 395
FT /ligand="ADP"
FT /ligand_id="ChEBI:CHEBI:456216"
FT /ligand_note="ligand shared with MCM5"
FT /evidence="ECO:0000250|UniProtKB:P25205"
FT BINDING 396
FT /ligand="ADP"
FT /ligand_id="ChEBI:CHEBI:456216"
FT /ligand_note="ligand shared with MCM5"
FT /evidence="ECO:0000250|UniProtKB:P25205"
FT BINDING 398
FT /ligand="ADP"
FT /ligand_id="ChEBI:CHEBI:456216"
FT /ligand_note="ligand shared with MCM5"
FT /evidence="ECO:0000250|UniProtKB:P25205"
FT BINDING 524
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /ligand_note="ligand shared with MCM7"
FT /evidence="ECO:0000250|UniProtKB:P25205"
FT BINDING 665
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /ligand_note="ligand shared with MCM7"
FT /evidence="ECO:0000250|UniProtKB:P25205"
SQ SEQUENCE 812 AA; 91251 MW; 5D65A2F86936E234 CRC64;
MAAPAGGLGD AELREAQRDY LDFLDDEEDQ GVYHGKVRDM ISDNQYRLLV NINDLRRRNE
KRANRLLSNA FEELIAFQRA LKDFVASVDA TYAKQYEDFY IGLEGSFGSK HVSPRTLTAC
FLSCIVCVEG IVTKCSLIRP KVVRSVHYCP ATKKTIERRY TDLTSLDAFP SSTVYPTKDE
ENNPLETEYG LSVYKDHQTI SIQEMPEKAP AGQLPRSVDV ILDDDLVDKV KPGDRIQVVG
TYRCLPGKKG GYTSGTFRTI LIACHIKQMS KDARPLYSAN DVAKIKRFSK SRSKDIFNQL
ARSLAPSIHG HEFIKKALLC MLLGGVEKVL ENGSRIRGDI NILLIGDPSV AKSQLLRYVL
GTAPRAVGTT GRGSSGVGLT AAVTTDQETG ERRLEAGAMV LADRGVVCID EFDKMSDIDR
TAIHEVMEQG RVTIAKAGIH ARLNSRCSVL AAANPVYGRY DQYKTPMENI GLQDSLLSRF
DLLFIMLDQM DSEQDREISD HVLRMHRYRN PNEQDGDAMP LGSAVEILAT DDPDFAQEEE
QELQVYEKHD DLLHGPNRRK EKIVSMEFMR KYIHVAKMIK PVLTQESADY IAEEYSSLRS
QNQMNSDIAR TSPVTARTLE TLIRLSTAHA KARMSKTVDL QDAEAALELV QFAYFKKVLE
KEKKRKKQVE DDSETEKEEE EEETQPEKEG RKQRRKKART EGEEESYDPY DFSDAEQEMP
EVQAHTPKTP ESSATGEAKK PELADPRLKA FKAALLEVFK SSHAQSVGLK NVMESINRDN
PEPFSLAGVK VALAHMQDDN QIMVSDDIIF LI
//