ID A0A0N1I2J6_LEPSE Unreviewed; 891 AA.
AC A0A0N1I2J6;
DT 09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT 09-DEC-2015, sequence version 1.
DT 27-MAR-2024, entry version 39.
DE RecName: Full=DNA replication licensing factor MCM6 {ECO:0000256|RuleBase:RU368064};
DE EC=3.6.4.12 {ECO:0000256|RuleBase:RU368064};
GN ORFNames=ABL78_7050 {ECO:0000313|EMBL:KPI83914.1};
OS Leptomonas seymouri.
OC Eukaryota; Discoba; Euglenozoa; Kinetoplastea; Metakinetoplastina;
OC Trypanosomatida; Trypanosomatidae; Leishmaniinae; Leptomonas.
OX NCBI_TaxID=5684 {ECO:0000313|EMBL:KPI83914.1, ECO:0000313|Proteomes:UP000038009};
RN [1] {ECO:0000313|EMBL:KPI83914.1, ECO:0000313|Proteomes:UP000038009}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 30220 {ECO:0000313|EMBL:KPI83914.1,
RC ECO:0000313|Proteomes:UP000038009};
RX PubMed=26317207;
RA Kraeva N., Butenko A., Hlavacova J., Kostygov A., Myskova J., Grybchuk D.,
RA Lestinova T., Votypka J., Volf P., Opperdoes F., Flegontov P., Lukes J.,
RA Yurchenko V.;
RT "Leptomonas seymouri: Adaptations to the Dixenous Life Cycle Analyzed by
RT Genome Sequencing, Transcriptome Profiling and Co-infection with Leishmania
RT donovani.";
RL PLoS Pathog. 11:E1005127-E1005127(2015).
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|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:KPI83914.1}.
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DR EMBL; LJSK01000310; KPI83914.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0N1I2J6; -.
DR EnsemblProtists; KPI83914; KPI83914; ABL78_7050.
DR VEuPathDB; TriTrypDB:Lsey_0310_0090; -.
DR OMA; HINAAAM; -.
DR OrthoDB; 5476523at2759; -.
DR Proteomes; UP000038009; Unassembled WGS sequence.
DR GO; GO:0042555; C:MCM complex; IEA:UniProtKB-UniRule.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
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:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR GO; GO:0006270; P:DNA replication initiation; IEA:UniProtKB-UniRule.
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; 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; 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|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|RuleBase:RU368064};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW ECO:0000256|RuleBase:RU004070}.
FT DOMAIN 388..594
FT /note="MCM"
FT /evidence="ECO:0000259|PROSITE:PS50051"
FT REGION 709..741
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 891 AA; 97953 MW; 780CA0DD2D714958 CRC64;
MNPPDIRDDP ALPQPTAEVA PVLEVDADGV RVREAVHLFL SRLVDPVLRA NLSLAAPSRG
DGDGSDSSLS YVVAQMERIS TSTSWSTCVV RWADLIRFDD DAAAVIESDY QRFSPFLNEA
LHQVLLQYYG EDYSNRGRCH PSLVFSNVPR CLTIRSLRAS LVGQLCSIKG VVTRTSQVRP
ELLVGVFRCS DCGAESLPIE QQFHYTEPPT CRNAQCENKN KFQLIPNHPH TRFGDWQKLR
MQEDTNNIPA GCMPRTMEVI VRSDAVEVAK PGDRVLAVGC AIVIPEVAKL FNLANRREVQ
RQMTGGQRAQ QDAQADMEGA TGLRALGVRD LSYRMCFLAT TITDGSGDDR KMTHAVKEAT
DGASEREEVV LTPAERQRVQ QMRRHDSLLK ALTSCVAPNV FKHDVVKLGL LLQMVGGVSK
TTVERITLRG DINACIVGDP STAKSQFLKW VSANMPRGVY TSGKASTASG LTATVTRDAD
TGERTIEAGA LMLSDRGICC IDEFDKMEMK DQVAIHEAME QQTISIAKAG IKATLNAKTS
LLAALNPIGG KYDRRRPLQK NIAMTAPIMS RFDLMFVIVD DSGDDADFAI ANQLLRLHRF
GGAAVRPPFT TEDFQLYLRY ARSLTPRLTF EASQLIVAAY RDMRLQDSLS NRSKVYRVTT
RLLESMIRLS EATAKIYMSE EVTPTHVEVA LELMRQSMST LDMTEVELVG GAGDEGSPNH
VEEQQQHQIG GSSTTVKREP EAAHGIGSNA VASIASEKRH GDGAGGSSYA EASNVGADAL
TSSTAVSAAT AEAPRRKVSI KADHYFAIVN RLVAHLKSLS EDMAPTRQEL VTWYLEQVKT
LNRPLLEAEL RYVNLVLSKL VKEGKLLEVD VNEGDAPRIF LDPNFNPDFT Q
//
