ID A0A2C9JXN3_BIOGL Unreviewed; 733 AA.
AC A0A2C9JXN3;
DT 20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT 20-DEC-2017, sequence version 1.
DT 08-NOV-2023, entry version 32.
DE RecName: Full=DNA replication licensing factor MCM5 {ECO:0000256|RuleBase:RU368063};
DE EC=3.6.4.12 {ECO:0000256|RuleBase:RU368063};
GN Name=106072150 {ECO:0000313|EnsemblMetazoa:BGLB009707-PB};
OS Biomphalaria glabrata (Bloodfluke planorb) (Freshwater snail).
OC Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Mollusca; Gastropoda;
OC Heterobranchia; Euthyneura; Panpulmonata; Hygrophila; Lymnaeoidea;
OC Planorbidae; Biomphalaria.
OX NCBI_TaxID=6526 {ECO:0000313|EnsemblMetazoa:BGLB009707-PB, ECO:0000313|Proteomes:UP000076420};
RN [1] {ECO:0000313|EnsemblMetazoa:BGLB009707-PB}
RP IDENTIFICATION.
RC STRAIN=BB02 {ECO:0000313|EnsemblMetazoa:BGLB009707-PB};
RG EnsemblMetazoa;
RL Submitted (MAY-2020) to UniProtKB.
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 RefSeq; XP_013087922.1; XM_013232468.1.
DR AlphaFoldDB; A0A2C9JXN3; -.
DR STRING; 6526.A0A2C9JXN3; -.
DR EnsemblMetazoa; BGLB009707-RB; BGLB009707-PB; BGLB009707.
DR GeneID; 106072150; -.
DR KEGG; bgt:106072150; -.
DR VEuPathDB; VectorBase:BGLB009707; -.
DR OrthoDB; 5476523at2759; -.
DR Proteomes; UP000076420; 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:0003688; F:DNA replication origin binding; IEA:UniProtKB-UniRule.
DR GO; GO:0004386; F:helicase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR GO; GO:0032508; P:DNA duplex unwinding; IEA:UniProtKB-UniRule.
DR GO; GO:0006270; P:DNA replication initiation; IEA:UniProtKB-UniRule.
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}.
FT DOMAIN 329..534
FT /note="MCM"
FT /evidence="ECO:0000259|PROSITE:PS50051"
FT REGION 1..26
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 733 AA; 82430 MW; C86543D4770B140F CRC64;
MEPGFDDVGI FYSDTFGPDE PNDESQIDRQ HIKKRLKQFI REFHERNFSY RYRDQLKRNY
NLKQFMLEVD LDDVGSYDET LAEKLLKQPS EHLPLFEEAA KEVADEITRP RPEGEEEVED
IQVMLTSASN ACGIRDLKSD QMSRLVKIPG IVIAASGIRS KAIRLAIQCR SCSNVINNIQ
VKPGLEGYAL PRKCNTEQAG RPKCPVDPFF IIPDKCKCVD FQTLKLQEAP EDVPNGELPR
HLQLYCDRYL CDRIVPGNRV TVMGIYSIKK TSKPTKRNNR DKVNVGIRLP YFRIVGVKID
TDGTGRTSGS SVTPSEEDEL RRLAATPNIY ETIAKSIAPS IYGSLDMKKA IACLLFGGSR
KRLPDGLTRR GDINMLMLGD PGTAKSQLLK FVERCSPIAV YTSGKGSSAA GLTASVMRDP
SSRGFVMEGG AMVLADGGVV CIDEFDKMRE DDRVAIHEAM EQQTISIAKA GITTTLNSRC
SVLAAANSVF GRWDDTKGGE NIDFMPTILS RFDMIFIVKD EHDEIRDMTL AKHVMNVHLN
ALQSTEEGKD GEIPLNTLKK YIAFCRNKCG PRLSEEAAEK LKNRYVLMRN KAGEYERETG
KKISIPITVR QLEAIIRIAE SQAKMRLAPF ATEADVDEAL RLFQVSTLDA ATTGDLAGAE
GFTTEEDQEL LSRIEKQIKR RFVIGSQVSE HAIVQDFTRQ KYPERAIHKV LTLMLRRGEI
QHRMQRKILF RVK
//
