ID A0A061HHC3_BLUGR Unreviewed; 801 AA.
AC A0A061HHC3;
DT 03-SEP-2014, integrated into UniProtKB/TrEMBL.
DT 03-SEP-2014, sequence version 1.
DT 27-MAR-2024, entry version 43.
DE RecName: Full=DNA replication licensing factor MCM4 {ECO:0000256|RuleBase:RU368062};
DE EC=3.6.4.12 {ECO:0000256|RuleBase:RU368062};
GN ORFNames=BGT96224_1805 {ECO:0000313|EMBL:EPQ64892.1},
GN BGT96224V2_LOCUS3371 {ECO:0000313|EMBL:SUZ10200.1};
OS Blumeria graminis f. sp. tritici 96224.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC Erysiphales; Erysiphaceae; Blumeria.
OX NCBI_TaxID=1268274 {ECO:0000313|EMBL:SUZ10200.1};
RN [1] {ECO:0000313|Proteomes:UP000053110}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=96224 {ECO:0000313|Proteomes:UP000053110};
RX PubMed=23852167; DOI=10.1038/ng.2704;
RA Wicker T., Oberhaensli S., Parlange F., Buchmann J.P., Shatalina M.,
RA Roffler S., Ben-David R., Dolezel J., Simkova H., Schulze-Lefert P.,
RA Spanu P.D., Bruggmann R., Amselem J., Quesneville H.,
RA Ver Loren van Themaat E., Paape T., Shimizu K.K., Keller B.;
RT "The wheat powdery mildew genome shows the unique evolution of an obligate
RT biotroph.";
RL Nat. Genet. 45:1092-1096(2013).
RN [2] {ECO:0000313|EMBL:EPQ64892.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=96224 {ECO:0000313|EMBL:EPQ64892.1};
RA Oberhaensli S., Wicker T., Keller B.;
RT "The wheat powdery mildew genome reveals unique evolution of an obligate
RT biotroph.";
RL Submitted (JAN-2013) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|EMBL:SUZ10200.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=96224 {ECO:0000313|EMBL:SUZ10200.1};
RA Quirk P.G., Krulwich T.A.;
RL Submitted (JUL-2018) to the EMBL/GenBank/DDBJ databases.
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:RU368062}.
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:RU368062};
CC -!- SUBUNIT: Component of the MCM2-7 complex.
CC {ECO:0000256|RuleBase:RU368062}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
CC -!- SIMILARITY: Belongs to the MCM family. {ECO:0000256|ARBA:ARBA00008010,
CC ECO:0000256|RuleBase:RU004070}.
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DR EMBL; KE375048; EPQ64892.1; -; Genomic_DNA.
DR EMBL; UIGY01000076; SUZ10200.1; -; Genomic_DNA.
DR HOGENOM; CLU_000995_7_0_1; -.
DR OrthoDB; 5476523at2759; -.
DR Proteomes; UP000053110; Unassembled WGS sequence.
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:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0003678; F:DNA helicase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR GO; GO:0006270; P:DNA replication initiation; IEA:InterPro.
DR GO; GO:0006279; P:premeiotic DNA replication; IEA:UniProt.
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; IPR008047; MCM_4.
DR InterPro; IPR018525; MCM_CS.
DR InterPro; IPR001208; MCM_dom.
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:SF66; DNA REPLICATION LICENSING FACTOR MCM4; 1.
DR Pfam; PF00493; MCM; 1.
DR Pfam; PF14551; MCM_N; 1.
DR Pfam; PF17207; MCM_OB; 1.
DR PRINTS; PR01657; MCMFAMILY.
DR PRINTS; PR01660; MCMPROTEIN4.
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 DNA replication {ECO:0000256|ARBA:ARBA00022705,
KW ECO:0000256|RuleBase:RU368062};
KW DNA-binding {ECO:0000256|RuleBase:RU004070};
KW Helicase {ECO:0000256|ARBA:ARBA00022806, ECO:0000256|RuleBase:RU368062};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU368062};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW ECO:0000256|RuleBase:RU004070};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242, ECO:0000256|RuleBase:RU368062};
KW Reference proteome {ECO:0000313|Proteomes:UP000053110}.
FT DOMAIN 615..801
FT /note="MCM"
FT /evidence="ECO:0000259|PROSITE:PS50051"
FT REGION 1..90
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 102..153
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 198..217
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..63
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 102..137
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 200..217
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 801 AA; 89172 MW; 693729FE892E1FA4 CRC64;
MSSSPNGQPT PSQGTHGQLG NTAARRTLQR NSSRMPPSSP GDAAAAQLQT EAASSQRYVD
RDANAIRSSS PVPYPSSPTP AHGRNMERDI SSPLRQMTTS QIQYDDNLTP RASSSRFARD
SSPIRYAPSS SPGLNSYRRS VPPDIRSDSS GLFIRSSRGE NAGLMSSLNI RRRGDINSDN
INTPRARRRI FMDESGNVTR DIPTEGSEAP TFSNLDPTTS DAAAMGGESQ LCIWGTNVSI
NDTLSTFKTF LRGFTKKYRM WADGMSEEET SQESDAETKE YIETMKNMLT LGVTSLNLDF
RNLKAYPKTQ KLWQQAQDYP QDVVTLMDQG IKDVMYELAE EETLRKRQLQ NKALISQRNL
KASSEPLMLS SERDELDTQE RSQGVSEELD LCQEVQKRSY RVRPFGLEKT INMRDLNPSD
VDKIIAIKGL VIRTTPIIPD MKDAFFRCQV CNHTVKVDID RGRIAEPTKC PRPICDSPNS
MQIVHNRSEF MDKQVIKFQE TPDSVPAGQT PHSITMCAYD ELVDFCKAGD RVEITGIFKA
SPVRVNPRQR TLKNVYKTYI DVLHIQKVDK KRMGIDVSTV EQDLSEQTAT NIEEARRVSD
EEKEKILQTA LRPDIYELLS RSLAPSIFEM DDVKKGILLQ LFGGTNKTFE KGGSPKYRGD
INILLCGDPS TSKSQLLQYV HKIAPRGLYT SGKGSSAVGL TAYVTRDPET RQLVLESGAL
VLSDGGVCCI DEFDKMSDAT RSVLHEVMEQ QTVSIAKAGI ITTLNARTSI LASANPIGSK
YNPNLPIELM KQMTDDLRAT Y
//
