ID A0A0K6FQC0_9AGAM Unreviewed; 828 AA.
AC A0A0K6FQC0;
DT 11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT 11-NOV-2015, sequence version 1.
DT 27-MAR-2024, entry version 37.
DE RecName: Full=DNA replication licensing factor MCM3 {ECO:0000256|RuleBase:RU368061};
DE EC=3.6.4.12 {ECO:0000256|RuleBase:RU368061};
GN ORFNames=RSOLAG22IIIB_03433 {ECO:0000313|EMBL:CUA68194.1};
OS Rhizoctonia solani.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Cantharellales; Ceratobasidiaceae; Rhizoctonia.
OX NCBI_TaxID=456999 {ECO:0000313|EMBL:CUA68194.1, ECO:0000313|Proteomes:UP000044841};
RN [1] {ECO:0000313|EMBL:CUA68194.1, ECO:0000313|Proteomes:UP000044841}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BBA 69670 {ECO:0000313|EMBL:CUA68194.1};
RA Noorani M.;
RL Submitted (JUL-2015) 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}.
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DR EMBL; CYGV01000335; CUA68194.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0K6FQC0; -.
DR Proteomes; UP000044841; 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 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:UP000044841}.
FT DOMAIN 302..508
FT /note="MCM"
FT /evidence="ECO:0000259|PROSITE:PS50051"
FT REGION 540..573
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 681..755
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 712..751
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 828 AA; 90704 MW; 03C0863931FC5D9E CRC64;
MAELPEPNLA DDIMRDRARI LQEFLEDTSR PDSTDYIAEI DNMLRLDETR LIVNIDDLRD
YNAEHAVGLL RQPHEYIPAF DAALLERVKI QHDTEKHDLS NKEYHVGFRG SFGDHHVSPR
TLRASHIGKM ISLEGIITRC SLVRPKMTRS VHYCEKTTMF YKCDYRDGTS LSSQGPTSTI
TPLADPDGNL LQMEVGYSTF RDHQRISIQE MPERAPPGQL PRSVDVIMDD DLVDKCKPGD
RVTLVGVYRS IGGGGGSGGF KTLILANNIV LLSTKSGGGV AQTRLTDSDI RNINKLAQKR
NIVSLLSSSL APSIYGHDYI KRAILLLLLG GAEKNLANGT HIRGDINILM VGDPSTAKSQ
LLRFVLSTAS LAIATTGRGS SGVGLTAAVT TDKETGERRL EAGAMVLADR GVVCIDEFDK
MSDVDRVAIH EVMEQQTVTI AKAGIHTSLN ARCSVIAAAN PVYGQYDVHK DPHKNIALPD
SLLSRFDLLF VVTDDVEENR DRKIADHVLR MHRYIPPGHE EGTPVNENLA QSLSVEAAAT
ANASGTTTEP FEKYDPLIRG GVAPGPTRST RSAAKKPEIL SIPFVKKYIQ YAKAKPAPVL
TKGAADWIVQ VYASLRNDEL EGNNKKTSPL TARTLETLIR LATAHAKARL SSKVEERDAM
AAEEILKFAL FKEVLKPERR KRRKLNTGAA GAGGQSDEED GSDDEMESAP QRMEMPQQQP
IAASKDKDNN VNGTNESMGD VPSSSAAQES QARGVAPERV AAFRSRLARL FQERFAEEEA
IPIESAVEAV NEGLPVDQLF GRIEASEIAE VMTAANEIML SDGIIYRL
//
