ID L2GJI7_VITCO Unreviewed; 674 AA.
AC L2GJI7;
DT 06-MAR-2013, integrated into UniProtKB/TrEMBL.
DT 06-MAR-2013, sequence version 1.
DT 27-MAR-2024, entry version 58.
DE RecName: Full=DNA replication licensing factor MCM5 {ECO:0000256|RuleBase:RU368063};
DE EC=3.6.4.12 {ECO:0000256|RuleBase:RU368063};
GN ORFNames=VICG_01920 {ECO:0000313|EMBL:ELA41038.1};
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:ELA41038.1, 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:RU368063}.
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:RU368063};
CC -!- SUBUNIT: Component of the MCM2-7 complex.
CC {ECO:0000256|RuleBase:RU368063}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123,
CC ECO:0000256|RuleBase:RU368063}.
CC -!- SIMILARITY: Belongs to the MCM family. {ECO:0000256|RuleBase:RU004070}.
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DR EMBL; JH370151; ELA41038.1; -; Genomic_DNA.
DR RefSeq; XP_007605365.1; XM_007605303.1.
DR AlphaFoldDB; L2GJI7; -.
DR STRING; 993615.L2GJI7; -.
DR GeneID; 19882630; -.
DR VEuPathDB; MicrosporidiaDB:VICG_01920; -.
DR HOGENOM; CLU_000995_7_2_1; -.
DR InParanoid; L2GJI7; -.
DR OMA; ITYCKTR; -.
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:0016887; F:ATP hydrolysis activity; IEA:RHEA.
DR GO; GO:0003688; F:DNA replication origin binding; IEA:UniProtKB-UniRule.
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:UniProtKB-UniRule.
DR GO; GO:0006279; P:premeiotic DNA replication; IEA:UniProt.
DR CDD; cd17756; MCM5; 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; IPR008048; MCM5.
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:SF42; DNA REPLICATION LICENSING FACTOR MCM5; 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; PR01661; MCMPROTEIN5.
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:RU368063};
KW DNA replication {ECO:0000256|ARBA:ARBA00022705,
KW ECO:0000256|RuleBase:RU368063};
KW DNA-binding {ECO:0000256|ARBA:ARBA00023125, ECO:0000256|RuleBase:RU004070};
KW Helicase {ECO:0000256|ARBA:ARBA00022806, ECO:0000256|RuleBase:RU368063};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU368063};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW ECO:0000256|RuleBase:RU004070};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242, ECO:0000256|RuleBase:RU368063};
KW Reference proteome {ECO:0000313|Proteomes:UP000011082}.
FT DOMAIN 278..482
FT /note="MCM"
FT /evidence="ECO:0000259|PROSITE:PS50051"
SQ SEQUENCE 674 AA; 75232 MW; 194151CE677D7966 CRC64;
MEYHASEIKS IDLIANDRVI SEETLGKMFV EFVKEFKTTH KSYLNQLHTN LAQNIFSLNI
QLEHIGLFNQ ELFNRLLANP ESTIQVFERE ACSHFQLKNF QILFSSAGNC TKIRNLSALK
SNKIVKIQGI VVSASSIVTK PKELYVTCRS CLQSKMVRDI IPRSCDTSTK CPIDPYIIIP
EKSVVSDVQY AKIQENFEDI PTGETPRHFS IILEGSLVNK ISPGNQVKIT GIYSIRSSEE
KSFSFLKVLG VENSKSKIRT IFTEEEEALF KQMAKEDIYE KLARSIAPGI YGHEDVKKTL
ACMLFGGTRR VREDGITLRG DINVLLLGDP GVAKSQLLKF MESVTPIGVY TSGKGSSAAG
LTASIIKDRN NEFYLEGGAL VLADGGICCI DEFDKMNEQD RVAIHEAMEQ QTISIAKAGI
TTVLNSRTAV LAAANPVFGR YDDFKTPSEN IEFGTTILSR FDCIFIIKDK CGSEDRIMAE
HVLNLHKQDS NGNNASGAIP VDVVRNYVQY AKSKVFPTLS EAASSKLNRF YVDIRKQVSG
YEEKGAKKGT IPITVRQLEA IIRLSESLAK MELSSVVTTK HVDEAIRLFQ ASTMNAVAQG
HIIEGMARPE YMSEIESIIE KIERSMPVGT TVRFHELLHS VNCSEALVRR AIDFMVKQNK
LISKDFGKML IRRP
//
