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Database: UniProt
Entry: MCM3_CHICK
LinkDB: MCM3_CHICK
Original site: 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   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
//
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