ID L2GM36_VITCO Unreviewed; 715 AA.
AC L2GM36;
DT 06-MAR-2013, integrated into UniProtKB/TrEMBL.
DT 06-MAR-2013, sequence version 1.
DT 27-MAR-2024, entry version 56.
DE RecName: Full=DNA replication licensing factor MCM6 {ECO:0000256|RuleBase:RU368064};
DE EC=3.6.4.12 {ECO:0000256|RuleBase:RU368064};
GN ORFNames=VICG_01603 {ECO:0000313|EMBL:ELA41362.1};
OS Vittaforma corneae (strain ATCC 50505) (Microsporidian parasite) (Nosema
OS corneum).
OC Eukaryota; Fungi; Fungi incertae sedis; Microsporidia; Nosematidae;
OC Vittaforma.
OX NCBI_TaxID=993615 {ECO:0000313|EMBL:ELA41362.1, ECO:0000313|Proteomes:UP000011082};
RN [1] {ECO:0000313|Proteomes:UP000011082}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 50505 {ECO:0000313|Proteomes:UP000011082};
RG The Broad Institute Genome Sequencing Platform;
RA Cuomo C., Didier E., Bowers L., Young S.K., Zeng Q., Gargeya S.,
RA Fitzgerald M., Haas B., Abouelleil A., Alvarado L., Arachchi H.M.,
RA Berlin A., Chapman S.B., Gearin G., Goldberg J., Griggs A., Gujja S.,
RA Hansen M., Heiman D., Howarth C., Larimer J., Lui A., MacDonald P.J.P.,
RA McCowen C., Montmayeur A., Murphy C., Neiman D., Pearson M., Priest M.,
RA Roberts A., Saif S., Shea T., Sisk P., Stolte C., Sykes S., Wortman J.,
RA Nusbaum C., Birren B.;
RT "The genome sequence of Vittaforma corneae strain ATCC 50505.";
RL Submitted (MAY-2011) 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|RuleBase:RU368064}.
CC -!- SIMILARITY: Belongs to the MCM family. {ECO:0000256|ARBA:ARBA00008010,
CC ECO:0000256|RuleBase:RU004070}.
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DR EMBL; JH370145; ELA41362.1; -; Genomic_DNA.
DR RefSeq; XP_007605048.1; XM_007604986.1.
DR AlphaFoldDB; L2GM36; -.
DR STRING; 993615.L2GM36; -.
DR GeneID; 19882313; -.
DR VEuPathDB; MicrosporidiaDB:VICG_01603; -.
DR HOGENOM; CLU_000995_3_2_1; -.
DR InParanoid; L2GM36; -.
DR OMA; CQTEIRN; -.
DR OrthoDB; 1342623at2759; -.
DR Proteomes; UP000011082; 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:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0003678; F:DNA helicase activity; IEA:InterPro.
DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
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; 2.20.28.10; -; 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; 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; 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};
KW Reference proteome {ECO:0000313|Proteomes:UP000011082}.
FT DOMAIN 291..495
FT /note="MCM"
FT /evidence="ECO:0000259|PROSITE:PS50051"
SQ SEQUENCE 715 AA; 80689 MW; 4D717EE4C8D66465 CRC64;
MQYSLEDDFY NFLNESRGLP ERLQEVADAN KETFFIDLDD VRDASSQLFT EIHKDFIHKH
ELLNGIFKSY CLKNIERPLE VGFKNSGNRL KIRELRSDVL GDLVSFSGTV TRTTQVRPEL
HAGVFICRDC KSVIRDVRQE YKYTEPLFCP NHLCTNRRRF EVDLSESQFS NWQRIHVQEN
TEEVPNGCLP RSIDVVVRNE LCEQIKPGAS HIFTGYLVVV PDAVQVKLPS QKSVVAADGV
ADEKQKRSTG SKEMSYKLCF FCIYADIYIE NDGFTNDELA VVRRMLSTPD LYNKLSESLF
PTIHGHSNIK SAILLMLVGG VSKTKDIRLR GDINILLVGD PGTAKSQFLK QTSALNPRSI
YTSGKSSSAA GLTAAVVKDG ETGEFTIEAG ALMLSDLGVC CIDEFDKMTY KDQVSIHEAM
EQQTITISKA GINATLNSRT SILAAANPIR GRYDKRKTLR QNVNLSAPIM SRFDLYFVLI
DDPEPENDRN ISRHILQNHL VYNGSDRFGS GHSPDTSLSS SVLRPFSVEE VKLFIRYVKD
KMPVLTAESK KELIDKYVLL RQDSLVNTNN YRMTVRHLES LIRLSEALAK IHNESEVSPQ
YILEAFRLLK SSLVEIKSED VVLTAVDSLE SYSLPGKDLA KITNTLIYLL KSGTNIGKDE
LVSRYLLLVE ESLGTIAVYE NEKLKCEKVI DFLIGHEGVL FEMDGVVHIH PNYDY
//
