ID A0A2K1QUW7_9PEZI Unreviewed; 944 AA.
AC A0A2K1QUW7;
DT 28-MAR-2018, integrated into UniProtKB/TrEMBL.
DT 28-MAR-2018, sequence version 1.
DT 27-MAR-2024, entry version 28.
DE RecName: Full=DNA replication licensing factor MCM6 {ECO:0000256|RuleBase:RU368064};
DE EC=3.6.4.12 {ECO:0000256|RuleBase:RU368064};
GN ORFNames=CAC42_5381 {ECO:0000313|EMBL:PNS18842.1};
OS Sphaceloma murrayae.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Dothideomycetidae; Myriangiales; Elsinoaceae; Sphaceloma.
OX NCBI_TaxID=2082308 {ECO:0000313|EMBL:PNS18842.1, ECO:0000313|Proteomes:UP000243797};
RN [1] {ECO:0000313|EMBL:PNS18842.1, ECO:0000313|Proteomes:UP000243797}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CQ-2017a {ECO:0000313|EMBL:PNS18842.1,
RC ECO:0000313|Proteomes:UP000243797};
RA Cheng Q.;
RT "Draft genome sequence of a variant of Elsinoe murrayae.";
RL Submitted (JUN-2017) 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}.
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:PNS18842.1}.
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DR EMBL; NKHZ01000039; PNS18842.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2K1QUW7; -.
DR STRING; 2082308.A0A2K1QUW7; -.
DR InParanoid; A0A2K1QUW7; -.
DR OrthoDB; 5476523at2759; -.
DR Proteomes; UP000243797; 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:UP000243797}.
FT DOMAIN 484..690
FT /note="MCM"
FT /evidence="ECO:0000259|PROSITE:PS50051"
FT REGION 1..59
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 188..214
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 804..832
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..43
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 804..821
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 944 AA; 104572 MW; 95260422374966BA CRC64;
MSSLFEAALQ SDNPQEQDTR SEASANTATQ RQQIRSSSRP RGPPSVSTPG PQSDVPGFED
DELVGARVLR RQMQNIDVAP VVDETAEQIA SLFQDFLDAF IEEPTSSGAP PSSTPASDRY
YVEQIKGLAR YSLSTLYVDF QHVMQFGQGI LAESIAEDYY RFQPYLVRGL HNLIAKYAPR
YFRQHRQPGT STAASNASTY GTDPSQDDSI ADRTPNQQTD KIFTLAFYNL PLVSRVRGLR
TDAIGRLASI SGTVTRTSEV RPELLLATFI CEACNTVVPN VEQVFRYSEP TQCPNSICGN
RQGWRLDIRQ STFVDWQKVR IQENSSEIPT GSMPRTMDVI LRGEMVDRAK AGEKCVFTGT
LIVVPDVSQF RVPGVRPQSM RDTSNTNRGG DAGGSGISGL KALGVRDLTY RMVFLANMVT
PDTSTAGQSS AQHLKGQSTN ILSSLNQTGP IEDTAAEQAQ QEYLNTLTQA EVNELREMVH
TPNIFMRLVD SLAPMVYGHS VIKKGLLLQL MGGVSKTTPE GMSLRGDINI CIVGDPSTSK
SQFLKYICSF LPRAVYTSGK ASSAAGLTAA VVKDEETGEF TIEAGALMLA DNGICAIDEF
DKMDIADQVA IHEAMEQQTI SIAKAGIQAT LNARTSILAA ANPVGGRYNR KTTLRSNINM
SAPIMSRFDL FFVVLDECNE AVDQHLARHI VGIHQLRDEA VTPEFSTEQL QRYIRFARTF
KPVFKDEAKA RLVQRYKELR ADDAQGGVGR NSYRITVRQL ESMIRLSEAI AKANCVDEIT
VEFVDEAFSL LRQSIVLVEK DDVEVEDEGQ ADEDADEMED VREESVQPQQ GQRTQIKYDK
YMAILNLMVR RVNDDQTVAE DGVSEDDLIV WYLEQVEESL ESQEDLEVER TLARKVLKKM
VKDNILMQLR GEGLVDDANA GEGSSAAQER VMYVMHPNCA VEEM
//
