ID A0A401GCG9_9APHY Unreviewed; 972 AA.
AC A0A401GCG9;
DT 08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT 08-MAY-2019, sequence version 1.
DT 27-MAR-2024, entry version 20.
DE RecName: Full=DNA replication licensing factor MCM6 {ECO:0000256|RuleBase:RU368064};
DE EC=3.6.4.12 {ECO:0000256|RuleBase:RU368064};
GN ORFNames=SCP_0210880 {ECO:0000313|EMBL:GBE79886.1};
OS Sparassis crispa.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Polyporales; Sparassidaceae; Sparassis.
OX NCBI_TaxID=139825 {ECO:0000313|EMBL:GBE79886.1, ECO:0000313|Proteomes:UP000287166};
RN [1] {ECO:0000313|EMBL:GBE79886.1, ECO:0000313|Proteomes:UP000287166}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=30375506; DOI=10.1038/s41598-018-34415-6;
RA Kiyama R., Furutani Y., Kawaguchi K., Nakanishi T.;
RT "Genome sequence of the cauliflower mushroom Sparassis crispa
RT (Hanabiratake) and its association with beneficial usage.";
RL Sci. Rep. 8:16053-16053(2018).
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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:GBE79886.1}.
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DR EMBL; BFAD01000002; GBE79886.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A401GCG9; -.
DR STRING; 139825.A0A401GCG9; -.
DR InParanoid; A0A401GCG9; -.
DR OrthoDB; 5476523at2759; -.
DR Proteomes; UP000287166; 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: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:0006270; P:DNA replication initiation; IEA:UniProtKB-UniRule.
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:UP000287166}.
FT DOMAIN 447..653
FT /note="MCM"
FT /evidence="ECO:0000259|PROSITE:PS50051"
FT REGION 1..66
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 764..846
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..36
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 774..788
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 798..831
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 972 AA; 107278 MW; 56C65E46C01BA90E CRC64;
MDANGLSSPP LRHSSLPPSS APVATQSSNG RSTPRRTRTD ALALGDEDAE PAAEGDDSTS
RRRRRARGQL DIDIPIVKDA VGESVQESFE TFLRTFTEEV TRAATPASDG DVPAAADAEL
IYIEQIHTMR EYELTTLYVD YGHLLQKDDV LADAIQKQYY RFLPYIRRAL HSLVAQYEPE
YLKLNPTAAA TDSVNLQSRE FNVAFYHLPL VSGIRELRTD KIGTLMSISG TVTRTSEVRP
ELLYGSFICE VCGGLVNEIE QQFKYTEPSL CPNPTCGNRI AWQLQIDTSK FTDWQKVRIQ
ENPSEIPTGS MPRSLDVILR SELVERAKAG DKCVFTGTFI VVPDVSQLGL PGGNKAELMR
EASKAGANSA ASAVGGAGVT GLKSLGVRDL QYKTAFLACM VHDADGRAGT NIRGEEEDGD
DDGQAFARSL TEPEFEELKA MLESDHIYSR LVESIAPTVY GHEIVKKGLL LQLMGGVHKQ
TPEGMHLRGD INICIVGDPS TSKSQFLKYI CSFLPRAVYT SGKASSAAGL TAAVVKDEET
GDFTIEAGAL MLADNGICAI DEFDKMDLSD QVAIHEAMEQ QTISIAKAGI HATLNARTSI
LAAANPVGGR YDRKKSLRAN VAMTAPIMSR FDLFFVVLDE CDEKSDLNIA KHIVNVHRFQ
DEAIHPEFST EALQRYIRYA RTFNPKLTPE AADVLVEKYR ILRQDDASGT GRNSYRITVR
QLESMIRLSE AIARANCTSE ITPAFVREAY SLLRQSIIHV EQDDIEFDEE ELEGEREGDR
RPRATQDDED ESQDVEMAAM ETEQSYQESL GLDGQGSGGL NGVSGSDATS RAGSMPAEPP
APPAHPKRRM VITHDKYMSL QSLIVLHLSQ VERETGRGVD RDELIDWYLE FREAEIQDVE
ELEYEKELIT KMLRKLVKDN FLIEIKGDVQ DSLPLSADES SGQPSFDGQG GNVRVYYMVH
PSVDTEESSS VP
//
