MCM5_BOVIN
ID MCM5_BOVIN Reviewed; 734 AA.
AC Q0V8B7;
DT 17-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT 05-SEP-2006, sequence version 1.
DT 03-AUG-2022, entry version 94.
DE RecName: Full=DNA replication licensing factor MCM5 {ECO:0000250|UniProtKB:P33992};
DE EC=3.6.4.12;
GN Name=MCM5 {ECO:0000250|UniProtKB:P33992};
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX PubMed=16305752; DOI=10.1186/1471-2164-6-166;
RA Harhay G.P., Sonstegard T.S., Keele J.W., Heaton M.P., Clawson M.L.,
RA Snelling W.M., Wiedmann R.T., Van Tassell C.P., Smith T.P.L.;
RT "Characterization of 954 bovine full-CDS cDNA sequences.";
RL BMC Genomics 6:166-166(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.
CC {ECO:0000250|UniProtKB:P33992}.
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. The complex forms a toroidal
CC hexameric ring with the proposed subunit order MCM2-MCM6-MCM4-MCM7-
CC MCM3-MCM5. Interacts with ANKRD17. Interacts with MCMBP (By
CC similarity). Component of the CMG helicase complex, composed of the
CC MCM2-7 complex, the GINS complex and CDC45 (By similarity). Interacts
CC with TONSL; the interaction is direct (By similarity).
CC {ECO:0000250|UniProtKB:P33992, ECO:0000250|UniProtKB:P55862}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:P33992}.
CC Chromosome {ECO:0000250|UniProtKB:P55862}. Cytoplasm, cytosol
CC {ECO:0000250|UniProtKB:P33992}. Note=Associated with chromatin before
CC the formation of nuclei and detaches from it as DNA replication
CC progresses. {ECO:0000250|UniProtKB:P55862}.
CC -!- SIMILARITY: Belongs to the MCM family. {ECO:0000305}.
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DR EMBL; BT026302; ABG81458.1; -; mRNA.
DR RefSeq; NP_001068758.1; NM_001075290.1.
DR AlphaFoldDB; Q0V8B7; -.
DR SMR; Q0V8B7; -.
DR STRING; 9913.ENSBTAP00000020715; -.
DR PaxDb; Q0V8B7; -.
DR PRIDE; Q0V8B7; -.
DR GeneID; 506970; -.
DR KEGG; bta:506970; -.
DR CTD; 4174; -.
DR eggNOG; KOG0481; Eukaryota.
DR InParanoid; Q0V8B7; -.
DR OrthoDB; 266497at2759; -.
DR Proteomes; UP000009136; Unplaced.
DR GO; GO:0071162; C:CMG complex; ISS:UniProtKB.
DR GO; GO:0005829; C:cytosol; IEA:UniProtKB-SubCell.
DR GO; GO:0042555; C:MCM complex; IEA:InterPro.
DR GO; GO:0031090; C:organelle membrane; IEA:UniProt.
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:0003688; F:DNA replication origin binding; IEA:InterPro.
DR GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR GO; GO:0006270; P:DNA replication initiation; IEA:InterPro.
DR Gene3D; 2.40.50.140; -; 1.
DR Gene3D; 3.40.50.300; -; 1.
DR InterPro; IPR031327; MCM.
DR InterPro; IPR008048; MCM5.
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; PR01661; MCMPROTEIN5.
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 Acetylation; ATP-binding; Cell cycle; Chromosome; Cytoplasm;
KW DNA replication; DNA-binding; Helicase; Hydrolase; Nucleotide-binding;
KW Nucleus; Phosphoprotein; Reference proteome.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:P33992"
FT CHAIN 2..734
FT /note="DNA replication licensing factor MCM5"
FT /id="PRO_0000253035"
FT DOMAIN 331..537
FT /note="MCM"
FT MOTIF 512..515
FT /note="Arginine finger"
FT BINDING 381..388
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255"
FT MOD_RES 2
FT /note="N-acetylserine"
FT /evidence="ECO:0000250|UniProtKB:P33992"
FT MOD_RES 392
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P33992"
FT MOD_RES 396
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P33992"
FT MOD_RES 605
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P33992"
SQ SEQUENCE 734 AA; 82146 MW; 5821DD723601E865 CRC64;
MSGFDDPGIF YSDSFGGDNA ADEGQARKSQ LQRRFKEFLR QYRVGTDRTG FTFKYRDELK
RHYNLGEYWI EVEMEDLASF DEELADYLYK QPAEHLQLLE EAAKEVADEV TRPRPAGDEV
LQDIQVMLKS DASPSSIRSL KSDTMSHLVK IPGIVIAASG VRAKATRISI QCRSCHSTLT
NIAMRPGLDG YALPRKCNTD QAGRPKCPLD PYFIMPDKCK CVDFQTLKLQ ELPDAVPHGE
MPRHMQLYCD RYLCDKVVPG NRVTIMGIYS IKKFGLTSNR GRDRVGVGIR SAYIRVLGIQ
VDTDGSGRTF AGAMTPQEEE EFRRLAALPN IYELISKSIA PSIFGGTDMK KAIACLLFGG
SRKRLPDGLT RRGDINLLML GDPGTAKSQL LKFVEKCSPI GVYTSGKGSS AAGLTASVMR
DPSSRNFIME GGAMVLADGG VVCIDEFDKM REDDRVAIHE AMEQQTISIA KAGITTTLNS
RCSVLAAANS VFGRWDETKG EDNIDFMPTI LSRFDMIFIV KDEHNEERDV MLAKHVITLH
VSALTQAQAV EGEIDLAKLK KFIAYCRAKC GPRLSAEAAE KLKNRYIIMR SGARQHERDS
DRRSSIPITV RQLEAIVRIA EALSKMKLQP FATEADVEEA LRLFQVSTLD AALSGTLSGV
EGFTSQEDQE LLSRIEKQLK RRFAIGSQVS EHSIIQDFTK QKYPEHAIHK VLQLMLRRGE
IQHRMQRKVL YRLK
