ID C4Y6I1_CLAL4 Unreviewed; 934 AA.
AC C4Y6I1;
DT 28-JUL-2009, integrated into UniProtKB/TrEMBL.
DT 28-JUL-2009, sequence version 1.
DT 27-MAR-2024, entry version 83.
DE RecName: Full=DNA replication licensing factor MCM6 {ECO:0000256|RuleBase:RU368064};
DE EC=3.6.4.12 {ECO:0000256|RuleBase:RU368064};
GN ORFNames=CLUG_03764 {ECO:0000313|EMBL:EEQ39636.1};
OS Clavispora lusitaniae (strain ATCC 42720) (Yeast) (Candida lusitaniae).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Metschnikowiaceae; Clavispora.
OX NCBI_TaxID=306902 {ECO:0000313|EMBL:EEQ39636.1, ECO:0000313|Proteomes:UP000007703};
RN [1] {ECO:0000313|EMBL:EEQ39636.1, ECO:0000313|Proteomes:UP000007703}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 42720 {ECO:0000313|EMBL:EEQ39636.1,
RC ECO:0000313|Proteomes:UP000007703};
RX PubMed=19465905; DOI=10.1038/nature08064;
RA Butler G., Rasmussen M.D., Lin M.F., Santos M.A., Sakthikumar S.,
RA Munro C.A., Rheinbay E., Grabherr M., Forche A., Reedy J.L., Agrafioti I.,
RA Arnaud M.B., Bates S., Brown A.J., Brunke S., Costanzo M.C.,
RA Fitzpatrick D.A., de Groot P.W., Harris D., Hoyer L.L., Hube B., Klis F.M.,
RA Kodira C., Lennard N., Logue M.E., Martin R., Neiman A.M., Nikolaou E.,
RA Quail M.A., Quinn J., Santos M.C., Schmitzberger F.F., Sherlock G.,
RA Shah P., Silverstein K.A., Skrzypek M.S., Soll D., Staggs R.,
RA Stansfield I., Stumpf M.P., Sudbery P.E., Srikantha T., Zeng Q., Berman J.,
RA Berriman M., Heitman J., Gow N.A., Lorenz M.C., Birren B.W., Kellis M.,
RA Cuomo C.A.;
RT "Evolution of pathogenicity and sexual reproduction in eight Candida
RT genomes.";
RL Nature 459:657-662(2009).
CC -!- FUNCTION: Acts as 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. The active
CC ATPase sites in the MCM2-7 ring are formed through the interaction
CC surfaces of two neighboring subunits such that a critical structure of
CC a conserved arginine finger motif is provided in trans relative to the
CC ATP-binding site of the Walker A box of the adjacent subunit. The six
CC ATPase active sites, however, are likely to contribute differentially
CC to the complex helicase activity. {ECO:0000256|RuleBase:RU368064}.
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:0000256|RuleBase:RU368064};
CC -!- SUBUNIT: Component of the MCM2-7 complex.
CC {ECO:0000256|RuleBase:RU368064}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123,
CC ECO:0000256|RuleBase:RU368064}.
CC -!- SIMILARITY: Belongs to the MCM family. {ECO:0000256|ARBA:ARBA00008010,
CC ECO:0000256|RuleBase:RU004070}.
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DR EMBL; CH408079; EEQ39636.1; -; Genomic_DNA.
DR RefSeq; XP_002616523.1; XM_002616477.1.
DR AlphaFoldDB; C4Y6I1; -.
DR STRING; 306902.C4Y6I1; -.
DR GeneID; 8496753; -.
DR KEGG; clu:CLUG_03764; -.
DR VEuPathDB; FungiDB:CLUG_03764; -.
DR HOGENOM; CLU_000995_3_0_1; -.
DR InParanoid; C4Y6I1; -.
DR OMA; CQTEIRN; -.
DR OrthoDB; 5476523at2759; -.
DR Proteomes; UP000007703; Unassembled WGS sequence.
DR GO; GO:0071162; C:CMG complex; IEA:UniProt.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProt.
DR GO; GO:0042555; C:MCM complex; IEA:UniProtKB-UniRule.
DR GO; GO:0005656; C:nuclear pre-replicative complex; IEA:UniProt.
DR GO; GO:0031298; C:replication fork protection complex; IEA:UniProt.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:RHEA.
DR GO; GO:0003678; F:DNA helicase activity; IEA:InterPro.
DR GO; GO:0003688; F:DNA replication origin binding; IEA:UniProt.
DR GO; GO:0006270; P:DNA replication initiation; IEA:UniProtKB-UniRule.
DR GO; GO:0006268; P:DNA unwinding involved in DNA replication; IEA:UniProt.
DR GO; GO:0000727; P:double-strand break repair via break-induced replication; IEA:UniProt.
DR GO; GO:0006267; P:pre-replicative complex assembly involved in nuclear cell cycle DNA replication; IEA:UniProt.
DR GO; GO:0006279; P:premeiotic DNA replication; IEA:UniProt.
DR CDD; cd17757; MCM6; 1.
DR Gene3D; 1.20.58.870; -; 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; IPR031327; MCM.
DR InterPro; IPR008049; MCM6.
DR InterPro; IPR041024; Mcm6_C.
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:SF43; DNA REPLICATION LICENSING FACTOR MCM6; 1.
DR Pfam; PF00493; MCM; 1.
DR Pfam; PF18263; MCM6_C; 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; PR01662; MCMPROTEIN6.
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 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|RuleBase:RU004070};
KW Cell cycle {ECO:0000256|RuleBase:RU368064};
KW DNA replication {ECO:0000256|ARBA:ARBA00022705,
KW ECO:0000256|RuleBase:RU368064};
KW DNA-binding {ECO:0000256|ARBA:ARBA00023125, ECO:0000256|RuleBase:RU004070};
KW Helicase {ECO:0000256|ARBA:ARBA00022806, ECO:0000256|RuleBase:RU368064};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU368064};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW ECO:0000256|RuleBase:RU004070}; Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW Reference proteome {ECO:0000313|Proteomes:UP000007703}.
FT DOMAIN 441..647
FT /note="MCM"
FT /evidence="ECO:0000259|PROSITE:PS50051"
FT REGION 22..58
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 769..804
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 22..51
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 934 AA; 103644 MW; 59839F32B444A4FD CRC64;
MSNFVSSPRS IPSDAAQLLD SSRISSSLGR SANSPSSSQP NINFSDASQS QGARERDVRM
PASIRSAVEV PKVVDVTGEK VRESFEQFIE EFVDESSADD EWSGKIYLAQ IESMRVFEYS
TLYVDYQHLV GRENGVLATA ILEQYYRFNP FLLKGLHRLL KKYAPSLLYM NLLGNTGEDG
KQAHDNSSST SSGSTVNERV IQISFFNLPV THRIRDIRTD KIGSLMAISG TVTRTSEVRP
ELYKASFTCD MCSAVVDGIE QVFKYTEPTA CPSCPNQSYW TLNVAKSQFI DWQKVRIQEN
SNEIPTGSMP RTLDVILRGE AVERANPGDK CKFTGTEIVI PDVSQLGLPG IKAQSIKESA
GNASGLNSGV SGLKSLGVRD LTYKLAFFAC HVSSLISKAS GGESGEREVE FQGPNDQEAL
LNSLSDSEVS QLKEMVKDEH VYDKLVRSVS PAVFGHETIK KGILLQLLGG VHKQTVDGIN
LRGDINICVV GDPSTSKSQF LKYVCNFSPR AVYTSGKASS AAGLTAAVVK DEETGEYTIE
AGALMLADNG ICAIDEFDKM DITDQVAIHE AMEQQTISIA KAGIHATLNA RTSILAAANP
IGGRYNRKMG LRANLNMTAP IMSRFDLFFV VLDDCNEKID TQLASHIVDL HMLRDEAIDP
PYTAEQLSRY IKYAKTFKPK MTKDARDFLV AKYQELRSDD AQGLGRSSYR ITVRQLESMI
RLSEAIARAN CTEEITPTFV SEAYDLLRSS IIRVEMDDIQ IDDEIDDVAM HDDDDEGGED
NEDAGRPESN YNAPDYSGRT QARRAPKATI NYDKYVAMMN LIVKKISDDD SLGGEGLTKD
EIVDWYLHQK EDDLETEQDY HNERALAYKV LKRLEKDRIL MSVTQNINDD VLPGDEYDRA
QQASRTVYII HPNCAILDFF DNQTTERDND VGEE
//
