MCM3_CHICK
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 03-AUG-2022, entry version 106.
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 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. Required for DNA
CC replication and cell proliferation (By similarity).
CC {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 (By similarity). The complex
CC forms a toroidal hexameric ring with the proposed subunit order MCM2-
CC MCM6-MCM4-MCM7-MCM3-MCM5 (By similarity). Component of the CMG helicase
CC complex, composed of the MCM2-7 complex, the GINS complex and CDC45 (By
CC similarity). {ECO:0000250|UniProtKB:P25205,
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: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.ENSGALP00000042687; -.
DR PaxDb; Q5ZMN2; -.
DR GeneID; 422043; -.
DR KEGG; gga:422043; -.
DR CTD; 4172; -.
DR VEuPathDB; HostDB:geneid_422043; -.
DR eggNOG; KOG0479; Eukaryota.
DR InParanoid; Q5ZMN2; -.
DR OrthoDB; 266497at2759; -.
DR PhylomeDB; Q5ZMN2; -.
DR PRO; PR:Q5ZMN2; -.
DR Proteomes; UP000000539; Unplaced.
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:RHEA.
DR GO; GO:0003682; F:chromatin binding; IDA:AgBase.
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; 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 346..353
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255"
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
