MCM5_SCHPO
ID MCM5_SCHPO Reviewed; 720 AA.
AC P41389; Q9UTF5;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 2.
DT 03-AUG-2022, entry version 167.
DE RecName: Full=DNA replication licensing factor mcm5;
DE EC=3.6.4.12;
DE AltName: Full=Cell division control protein nda4;
DE AltName: Full=Minichromosome maintenance protein 5;
GN Name=mcm5; Synonyms=nda4; ORFNames=SPAC1B2.05, SPAC3F10.01;
OS Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina;
OC Schizosaccharomycetes; Schizosaccharomycetales; Schizosaccharomycetaceae;
OC Schizosaccharomyces.
OX NCBI_TaxID=284812;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=8298187; DOI=10.1091/mbc.4.10.1003;
RA Miyake S., Okishio N., Samejima I., Hiraoka Y., Toda T., Saitoh I.,
RA Yanagida M.;
RT "Fission yeast genes nda1+ and nda4+, mutations of which lead to S-phase
RT block, chromatin alteration and Ca2+ suppression, are members of the
RT CDC46/MCM2 family.";
RL Mol. Biol. Cell 4:1003-1015(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=972 / ATCC 24843;
RX PubMed=11859360; DOI=10.1038/nature724;
RA Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A.,
RA Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S.,
RA Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M.,
RA Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S.,
RA Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S.,
RA Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D.,
RA Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P.,
RA Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K.,
RA O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M.,
RA Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N.,
RA Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A.,
RA Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R.,
RA Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M.,
RA Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A.,
RA Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A.,
RA Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H.,
RA Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S.,
RA Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C.,
RA Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A.,
RA Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M.,
RA del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S.,
RA Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R.,
RA Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G.,
RA Nurse P.;
RT "The genome sequence of Schizosaccharomyces pombe.";
RL Nature 415:871-880(2002).
RN [3]
RP SUBUNIT.
RC STRAIN=SP011;
RX PubMed=11606526; DOI=10.1093/genetics/159.2.471;
RA Liang D.T., Forsburg S.L.;
RT "Characterization of Schizosaccharomyces pombe mcm7(+) and cdc23(+) (MCM10)
RT and interactions with replication checkpoints.";
RL Genetics 159:471-486(2001).
RN [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-350 AND SER-352, AND
RP IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=18257517; DOI=10.1021/pr7006335;
RA Wilson-Grady J.T., Villen J., Gygi S.P.;
RT "Phosphoproteome analysis of fission yeast.";
RL J. Proteome Res. 7:1088-1097(2008).
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 (By similarity). Role
CC in DNA replication and essential for viability. {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 -!- 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 (Probable). {ECO:0000269|PubMed:11606526, ECO:0000305}.
CC -!- INTERACTION:
CC P41389; O94450: SPAC1687.04; NbExp=2; IntAct=EBI-913821, EBI-7492115;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the MCM family. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; S68467; AAC60568.1; -; Genomic_DNA.
DR EMBL; CU329670; CAB61472.1; -; Genomic_DNA.
DR PIR; A48723; A48723.
DR PIR; T50141; T50141.
DR AlphaFoldDB; P41389; -.
DR SMR; P41389; -.
DR ComplexPortal; CPX-2945; MCM complex.
DR IntAct; P41389; 3.
DR MINT; P41389; -.
DR STRING; 4896.SPAC1B2.05.1; -.
DR iPTMnet; P41389; -.
DR MaxQB; P41389; -.
DR PaxDb; P41389; -.
DR PRIDE; P41389; -.
DR PomBase; SPAC1B2.05; mcm5.
DR eggNOG; KOG0481; Eukaryota.
DR HOGENOM; CLU_000995_7_2_1; -.
DR InParanoid; P41389; -.
DR PhylomeDB; P41389; -.
DR Reactome; R-SPO-176187; Activation of ATR in response to replication stress.
DR Reactome; R-SPO-68867; Assembly of the pre-replicative complex.
DR Reactome; R-SPO-68949; Orc1 removal from chromatin.
DR Reactome; R-SPO-68962; Activation of the pre-replicative complex.
DR Reactome; R-SPO-69052; Switching of origins to a post-replicative state.
DR PRO; PR:P41389; -.
DR Proteomes; UP000002485; Chromosome I.
DR GO; GO:0005737; C:cytoplasm; HDA:PomBase.
DR GO; GO:0005829; C:cytosol; HDA:PomBase.
DR GO; GO:0031261; C:DNA replication preinitiation complex; IC:PomBase.
DR GO; GO:0042555; C:MCM complex; IDA:PomBase.
DR GO; GO:0005656; C:nuclear pre-replicative complex; IC:PomBase.
DR GO; GO:0043596; C:nuclear replication fork; IC:PomBase.
DR GO; GO:0005634; C:nucleus; IDA:PomBase.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; NAS:PomBase.
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:0003697; F:single-stranded DNA binding; IBA:GO_Central.
DR GO; GO:0006270; P:DNA replication initiation; 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; EXP:PomBase.
DR GO; GO:0030174; P:regulation of DNA-templated DNA replication initiation; IDA:ComplexPortal.
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 1: Evidence at protein level;
KW ATP-binding; Cell cycle; DNA replication; DNA-binding; Helicase; Hydrolase;
KW Nucleotide-binding; Nucleus; Phosphoprotein; Reference proteome.
FT CHAIN 1..720
FT /note="DNA replication licensing factor mcm5"
FT /id="PRO_0000194112"
FT DOMAIN 322..529
FT /note="MCM"
FT MOTIF 504..507
FT /note="Arginine finger"
FT BINDING 372..379
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255"
FT MOD_RES 350
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18257517"
FT MOD_RES 352
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18257517"
FT CONFLICT 461
FT /note="A -> R (in Ref. 1; AAC60568)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 720 AA; 80100 MW; 52F3EA9DD127E56E CRC64;
MAAATGWERS AVYYTPVLPG EQELDSNVSH EKNFIQFIEE FVIDNDFIYR TQLRDNLVVK
QYMLNIDLRH LISYNEDLAH LLLSQPTDIL PLFESAVTTV AKRLLYRSQE NASTNIPTCQ
VTLRYDANIL PIRNLTASHI SKLVRVPGII IGASTLSCRA TALHLVCRNC RATRILQISG
GFSGVQLPRV CEAPVLDGEK KDCPMDPFII DHSKSTFIDQ QVLKLQEAPD MVPVGELPRH
ILLNADRYLT NQITPGTRCV ITGIFSIFQN KSVKASGAVA IRNPYIRVVG IQMDSNDGSK
STPLFSEEEE EEFLEISRTP NLYDIISNSI SPAIYGNVDI KKAIACLLFS GSKKILPDGM
RLRGDINVLL LGDPGTAKSQ FLKFVERLAP IAVYTSGKGS SAAGLTASIQ RDSVTREFYL
EGGAMVLADG GIVCIDEFDK MRDEDRVAIH EAMEQQTISI AKAGITTILN SRTSVLAAAN
PIFGRYDDMK TPGENIDFQS TILSRFDMIF IVKDEHDETK DRNIARHVIN LHTNLQESSE
TLAIGEIPFD KFRRYINYCR HKCAPNLDAE AAEKLSSQFV AIRKLVHQSE QDSNSRSTIP
ITVRQLEAII RITESLAKMS LSPIASEAHA TEAIRLFLTS TLAAATQSSP EVTEEVKKIE
ASLRKRLPIG FQASYRMLIR EYVNGHGYSQ HALEMALQIR SSKETIQLRN GGQTVYRSGV
