ID E6ZXD6_SPORE Unreviewed; 911 AA.
AC E6ZXD6;
DT 08-MAR-2011, integrated into UniProtKB/TrEMBL.
DT 08-MAR-2011, sequence version 1.
DT 27-MAR-2024, entry version 70.
DE RecName: Full=DNA replication licensing factor MCM3 {ECO:0000256|RuleBase:RU368061};
DE EC=3.6.4.12 {ECO:0000256|RuleBase:RU368061};
GN ORFNames=sr12749 {ECO:0000313|EMBL:CBQ71893.1};
OS Sporisorium reilianum (strain SRZ2) (Maize head smut fungus).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Ustilaginomycotina;
OC Ustilaginomycetes; Ustilaginales; Ustilaginaceae; Sporisorium.
OX NCBI_TaxID=999809 {ECO:0000313|EMBL:CBQ71893.1, ECO:0000313|Proteomes:UP000008867};
RN [1] {ECO:0000313|EMBL:CBQ71893.1, ECO:0000313|Proteomes:UP000008867}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SRZ2 {ECO:0000313|Proteomes:UP000008867};
RX PubMed=21148393; DOI=10.1126/science.1195330;
RA Schirawski J., Mannhaupt G., Muench K., Brefort T., Schipper K.,
RA Doehlemann G., Di Stasio M., Roessel N., Mendoza-Mendoza A., Pester D.,
RA Mueller O., Winterberg B., Meyer E., Ghareeb H., Wollenberg T.,
RA Muensterkoetter M., Wong P., Walter M., Stukenbrock E., Gueldener U.,
RA Kahmann R.;
RT "Pathogenicity determinants in smut fungi revealed by genome comparison.";
RL Science 330:1546-1548(2010).
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:RU368061}.
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:RU368061};
CC -!- SUBUNIT: Component of the MCM2-7 complex.
CC {ECO:0000256|RuleBase:RU368061}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|RuleBase:RU368061}.
CC -!- SIMILARITY: Belongs to the MCM family. {ECO:0000256|RuleBase:RU004070}.
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DR EMBL; FQ311452; CBQ71893.1; -; Genomic_DNA.
DR AlphaFoldDB; E6ZXD6; -.
DR EnsemblFungi; CBQ71893; CBQ71893; sr12749.
DR VEuPathDB; FungiDB:sr12749; -.
DR eggNOG; KOG0479; Eukaryota.
DR HOGENOM; CLU_000995_6_0_1; -.
DR OrthoDB; 5476523at2759; -.
DR Proteomes; UP000008867; Chromosome 3.
DR GO; GO:0000785; C:chromatin; IEA:EnsemblFungi.
DR GO; GO:0031261; C:DNA replication preinitiation complex; 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:0043596; C:nuclear replication fork; IEA:UniProt.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0004386; F:helicase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0032508; P:DNA duplex unwinding; IEA:UniProtKB-UniRule.
DR GO; GO:0006270; P:DNA replication initiation; IEA:InterPro.
DR GO; GO:0006279; P:premeiotic DNA replication; IEA:EnsemblFungi.
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; 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; PS50051; MCM_2; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|RuleBase:RU004070};
KW DNA replication {ECO:0000256|RuleBase:RU368061};
KW DNA-binding {ECO:0000256|ARBA:ARBA00023125, ECO:0000256|RuleBase:RU004070};
KW Helicase {ECO:0000256|ARBA:ARBA00022806, ECO:0000256|RuleBase:RU368061};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU368061};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW ECO:0000256|RuleBase:RU004070}; Nucleus {ECO:0000256|RuleBase:RU368061}.
FT DOMAIN 306..512
FT /note="MCM"
FT /evidence="ECO:0000259|PROSITE:PS50051"
FT REGION 684..800
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 697..714
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 761..776
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 911 AA; 100867 MW; 520ABF14528E0884 CRC64;
MSQAFDDNSN LDVPIFQDDV LRDRQRVFSE FLSKDEYQDA VRRMLRMDAR RLIINIDDLR
SYNRDFATGL LNEPNEYLPA FDAALHMSVE VAHNPLKEDI KGKQYYIGLR GSFGDHHVNP
RTLRSVHLGK MMSLEGIVTR CSLVRPKILK SVHYCEQTTK FHQREYRDAT MYGTLPPSST
VYPTEDESGN RLTTEYGHSL FRDHQMISIQ EMPERAPPGQ LPRSIDVVMD DDMVDRCKPG
DRIQLVGMYR SLGNRVGQSS SSTFRTLMIG NNLNLLSSKA GGGIAQAHIT DTDIRNINKI
AKRKNVFNLL SQSLAPSIYG HEYIKKAVLL LLLGGEEKNL PNGTHIRGDI NILMVGDPST
AKSQMLRFVL NTAPLAIATT GRGSSGVGLT AAVTTDKETG ERRLEAGAMV LADRGVICID
EFDKMSDVDR VAIHEVMEQQ TVTIAKAGIH TSLNARCSVV AAANPIYGQY DVHKDPHKNI
ALPDSLLSRF DLLFVVTDDV DEQRDRMISE HVLRMHRYLQ PGLEEGTPAV DNLDQALDVG
APEGTDADGA AMLGDTSPFE KYNPLLHSGV TSTSRGSDKK EVLSIAFIKK YIQYAKSRIH
PVLTKGAAEW IVNVYSNLRN DELSGNQKRT SPLTARTLET LIRLATAHAK SRLSSKVEER
DAEAAEEILR FALFKEVLGG RHGINKRRRT GNSPMSDDDD GQDDDEDNDD DSGDEAARPD
ANQAYRSGRS NRGGRGGRRG GQRYSEDGHS SDDDDDEGQS GLVSSQRSTR SNGAYATRAA
AGTRPKPKPA MVGPGGMDEE AFDDEDALEA MRSLDVEVVI PPLPVEASSS SSFGVSAQRT
EAFKEALSDL LFSSDGRLAE MDAIPLDELL PVMNEGRRTQ DLFDSNEARQ VLEQMHRENS
IMFSEDMVFK L
//
