ID A0A2Z6Q728_9GLOM Unreviewed; 840 AA.
AC A0A2Z6Q728;
DT 10-OCT-2018, integrated into UniProtKB/TrEMBL.
DT 10-OCT-2018, sequence version 1.
DT 27-MAR-2024, entry version 25.
DE RecName: Full=DNA replication licensing factor MCM3 {ECO:0000256|RuleBase:RU368061};
DE EC=3.6.4.12 {ECO:0000256|RuleBase:RU368061};
GN ORFNames=RCL2_001140900 {ECO:0000313|EMBL:GES84285.1}, RclHR1_12360003
GN {ECO:0000313|EMBL:GBB85923.1};
OS Rhizophagus clarus.
OC Eukaryota; Fungi; Fungi incertae sedis; Mucoromycota; Glomeromycotina;
OC Glomeromycetes; Glomerales; Glomeraceae; Rhizophagus.
OX NCBI_TaxID=94130 {ECO:0000313|EMBL:GBB85923.1, ECO:0000313|Proteomes:UP000247702};
RN [1] {ECO:0000313|EMBL:GBB85923.1, ECO:0000313|Proteomes:UP000247702}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HR1 {ECO:0000313|EMBL:GBB85923.1,
RC ECO:0000313|Proteomes:UP000247702};
RA Kobayashi Y.;
RT "The genome of Rhizophagus clarus HR1 reveals common genetic basis of
RT auxotrophy among arbuscular mycorrhizal fungi.";
RL Submitted (NOV-2017) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:GES84285.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=HR1 {ECO:0000313|EMBL:GES84285.1};
RA Maeda T., Kobayashi Y., Nakagawa T., Ezawa T., Yamaguchi K., Bino T.,
RA Nishimoto Y., Shigenobu S., Kawaguchi M.;
RT "Conservation and host-specific expression of non-tandemly repeated
RT heterogenous ribosome RNA gene in arbuscular mycorrhizal fungi.";
RL Submitted (OCT-2019) 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:GBB85923.1}.
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DR EMBL; BEXD01000265; GBB85923.1; -; Genomic_DNA.
DR EMBL; BLAL01000079; GES84285.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2Z6Q728; -.
DR STRING; 94130.A0A2Z6Q728; -.
DR Proteomes; UP000247702; Unassembled WGS sequence.
DR Proteomes; UP000615446; 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:UP000247702}.
FT DOMAIN 308..514
FT /note="MCM"
FT /evidence="ECO:0000259|PROSITE:PS50051"
FT REGION 678..740
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 688..703
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 704..725
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 840 AA; 94604 MW; 5A7A1D677B7A7BEC CRC64;
MASNTELQKL QDEAFLDRVR FFEEFLEADK EKLGIEKFYK VEIAQMLRNG ERRFIVNLNE
LRYYHAENAK KLEESPNEWI PAFEKALKNI IKNISSSIDG TEKSTNIEDQ NFYIGFNGTF
HNHVNPRTLK SIHLGKLICI EGIVSRCSLV RLKLAKSVHY CEKTGNFCSK EYHDSTSIGN
QIPSSSAYPT EDENGNPLTT EFGYSVYRDH QTICLQEMPE KMPPGLLTRS IDIILDDDLV
DKVKPGDRIQ LAGCYRAIGK PTQGSTSATF KTVIIANNVT ILSGEIGLKV ITDVDIANIE
KIAKNENIFE LLSRSLAPSI YGHDMIKKAI LLMLLGGKEQ NLSSGTHIRG DINILMVGDP
STSKSQLLRR VLNIAPLAIA TTGRGSTGVG LTAAVTRDKE TGEKSLEAGA MVLGDRGVVC
IDEFDKMIDT DRVAIHEVME QQTVTIAKAG IHTSLNARCS VIAAANPIYG QYNIHKDPAH
NIALPDSLLS RFDLVFVVTD EINEVRDSLI SKHVLRLHEY RPPNLEEGVP IKEDSGQTIF
MEEAEKNTEP TSVYMQYDLL SSDNDNDQRD SDQINFLSSE FLKKYIQYAK SHEEPRLGKA
AAAYLCELWV NLRNEEETDG QAKTSPLTPR ALDSLFRLAT AHAKARLGKR VTIKDAKVAE
EIVRFALFKE VSIRDRRKRR KTNVNDNDEI DSDDDTNDDD DSDKDETSSQ RSINTRKDKG
KGKMIEPLTD GSSSKETDDI MDTDETHKQS FIELNLDTLI IEDNREMISS DRMRLFQENL
NRIITNPLYE TSISLEVLIR EVNNNLPENQ AYTSEEINAA LKKMQDQNKV MITNDVIYMI
//
