ID A0A2P8AIP7_9PEZI Unreviewed; 888 AA.
AC A0A2P8AIP7;
DT 23-MAY-2018, integrated into UniProtKB/TrEMBL.
DT 23-MAY-2018, sequence version 1.
DT 27-MAR-2024, entry version 28.
DE RecName: Full=DNA replication licensing factor MCM3 {ECO:0000256|RuleBase:RU368061};
DE EC=3.6.4.12 {ECO:0000256|RuleBase:RU368061};
GN ORFNames=B9Z65_467 {ECO:0000313|EMBL:PSK60317.1};
OS Elsinoe australis.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Dothideomycetidae; Myriangiales; Elsinoaceae; Elsinoe.
OX NCBI_TaxID=40998 {ECO:0000313|EMBL:PSK60317.1, ECO:0000313|Proteomes:UP000243723};
RN [1] {ECO:0000313|EMBL:PSK60317.1, ECO:0000313|Proteomes:UP000243723}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NL1 {ECO:0000313|EMBL:PSK60317.1,
RC ECO:0000313|Proteomes:UP000243723};
RA Cheng Q.;
RT "Draft genome sequence of Elsinoe australis.";
RL Submitted (MAY-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: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|ARBA:ARBA00004123,
CC ECO:0000256|RuleBase:RU368061}.
CC -!- SIMILARITY: Belongs to the MCM family. {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:PSK60317.1}.
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DR EMBL; NHZQ01000003; PSK60317.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2P8AIP7; -.
DR STRING; 40998.A0A2P8AIP7; -.
DR Proteomes; UP000243723; 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: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:UniProt.
DR CDD; cd17754; MCM3; 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; IPR003593; AAA+_ATPase.
DR InterPro; IPR031327; MCM.
DR InterPro; IPR008046; Mcm3.
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: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; 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: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};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242, ECO:0000256|RuleBase:RU368061};
KW Reference proteome {ECO:0000313|Proteomes:UP000243723}.
FT DOMAIN 302..508
FT /note="MCM"
FT /evidence="ECO:0000259|PROSITE:PS50051"
FT REGION 673..813
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 673..690
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 712..745
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 758..788
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 790..806
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 888 AA; 97743 MW; 3085CA006C05AADA CRC64;
MDGLQLRDEA TRDRIRAAEE FLDPNDPRAR SYRAEIILML NRGLRRLTVS IDEIRSHSKE
MADGLLNQPF DFSQAFDRAL KNIVKTIPDR PSHETADDTM YYCAYVGAFG EFACNPRTLG
SNQLNHMISL EGIVTKCSLV RPKVIKSVHY NERKTTFHFR EYRDQTMSAS GAASTSVYPT
EDDEGNPLIT EYGHCLYRDH QTISIQEMPE RAPAGQLPRS VDVIMDDDMV DRVKPGDRIQ
LVGIYRTLGN RNASSGSATF RTLILANNII LLSSKSGGGI AQTTITDTDI RNINKLSKQK
RVFDLLSQSL APSIYGHDYI KKAILLMLLG GMEKNLENGT HLRGDINILM VGDPSTAKSQ
LLRFILNTAP LAIATTGRGS SGVGLTAAVT QDKETGERRL EAGAMVLADR GVVCIDEFDK
MSDVDRVAIH EVMEQQTVTI AKAGIHTSLN ARCSVVAAAN PIYGQYDVHK DPHKNIALPD
SLLSRFDLLF IVTDDIEDAR DRQVSEHVLR MHRYRQPGTE EGAPVREQAQ QTLGVGLDDE
ADGNRPSEVY EKFNQMLHAG VTVTVGRGSA RRTEVISIPF IKKYIQYAKS RIKPVLTKGA
ADHIVSTYSA LRNDELEGNQ RRTSPMTART LETLIRLATA HAKSRLSNRV EEKDAEVAEE
ILRFALFKEV VSDARKKRRR TERSPDAMSS DEDSDNDNEE GDVEANGDGA FRGTSSRRNG
TTPARSTRQN GRPANGASTP NGQANGDGAD EELYDVTPRT QRTSQVNGTA GQSSQISLAS
SLPASQLLES QDLDEEDEEE EDAAPEEAAG PQPIAPARVQ AFQSALGQLI DGPLFANDAA
DVEPLVAAVN ARLRGGDDAF GREEAEQALE ELNERNKIMF SGGIVYKI
//
