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Database: UniProt
Entry: A0A0P1B113_PLAHL
LinkDB: A0A0P1B113_PLAHL
Original site: A0A0P1B113_PLAHL 
ID   A0A0P1B113_PLAHL        Unreviewed;       887 AA.
AC   A0A0P1B113;
DT   20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT   20-JAN-2016, sequence version 1.
DT   27-MAR-2024, entry version 40.
DE   RecName: Full=DNA replication licensing factor MCM6 {ECO:0000256|RuleBase:RU368064};
DE            EC=3.6.4.12 {ECO:0000256|RuleBase:RU368064};
OS   Plasmopara halstedii (Downy mildew of sunflower).
OC   Eukaryota; Sar; Stramenopiles; Oomycota; Peronosporales; Peronosporaceae;
OC   Plasmopara.
OX   NCBI_TaxID=4781 {ECO:0000313|EMBL:CEG47470.1, ECO:0000313|Proteomes:UP000054928};
RN   [1] {ECO:0000313|Proteomes:UP000054928}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Sharma Rahul, Thines Marco;
RL   Submitted (SEP-2014) 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: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; CCYD01002589; CEG47470.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0P1B113; -.
DR   STRING; 4781.A0A0P1B113; -.
DR   EnsemblProtists; CEG47470; CEG47470; CEG47470.
DR   OMA; CQTEIRN; -.
DR   OrthoDB; 5476523at2759; -.
DR   Proteomes; UP000054928; Unassembled WGS sequence.
DR   GO; GO:0042555; C:MCM complex; IEA:UniProtKB-UniRule.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0016887; F:ATP hydrolysis activity; IEA:RHEA.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0003678; F:DNA helicase activity; IEA:InterPro.
DR   GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR   GO; GO:0006270; P:DNA replication initiation; IEA:UniProtKB-UniRule.
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:UP000054928}.
FT   DOMAIN          394..600
FT                   /note="MCM"
FT                   /evidence="ECO:0000259|PROSITE:PS50051"
FT   REGION          1..22
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          292..319
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          724..774
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        295..318
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        726..741
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        742..774
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   887 AA;  98845 MW;  3863F32FA84FD5FC CRC64;
     MQTAGDGAKG VGAKRSRSGG PVLNPSAASI ELLVDSTAES VKTRFLQFLC GYGQQDDADE
     AMDPSKINYS QQAEVMRNTE TSSLFVDFSH VLEFDPDLAQ ALQAQYYRWE PYLRRSVFEF
     IRLEDAAYTV NEDANKTQRE FFVNFYNFQH VSHIRDLRTK SIGELLSFSG TVTRTSEVRP
     ELLFGAFTCA DCGGDTTGVE QQFRYSEPVK CQNPYCVNTF AWELNTEKSV FVDWQRVKVQ
     ENSDEIPAGS MPRSIDVILR HENVEQAKAG DRVVFTGTFI VVPDVSKFAQ AGGETAVATR
     NNDQSRRNGE NSTQGMQGEG VRGLKALGVR ELTYKTCFLA CSVQTMEQRF NSISIRSEYN
     EDNTEEQENG EAALQEFSDE EVASIRRMQQ DPDRYSKMAK SICPSVYGHD EIRKGILLML
     FGGVHKKTIE GIKLRGDINV CIVGDPSTAK SQFLKYIVGF LPRAIYASGK VSSAAGLTAS
     VTRDADSGDY CVEAGALMLA DNGICCIDEF DKMDPMDQVA IHEAMEQQTI SITKAGIQAT
     LNARTSILAA ANPYNGRYDK TKTLKYNVNI SAPIMSRFDL FFVILDDGDE VTDQKIAEHI
     VNIHMPSELQ VQATETGAYS EEELKRYIKF ARTLNPVITL ASKRMMVACY RSLRENDVVS
     NGQTNIAYRI TVRQLESMIR LSEALARLDL SETVMVSHVQ EAYRLLSKSI IHVDTQNVEL
     DVPLVVPDGK DGDDDRSNTG GTSMDDNDNG TSSGGNLSTG NVSNDYPSNE MQVTSSSSLS
     FERFARIQKA IGRFIREKEE EVLNAKVARD DITSEAQLTR EKQLFCSVID KLVQDKVLSV
     VDLVDEDGED LKLGDKVEDS TRHLSLEEQD AKKQQRYLTV HPNYAFE
//
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