ID A0A0K0JNC9_BRUMA Unreviewed; 884 AA.
AC A0A0K0JNC9; A0A1I9G5V9;
DT 08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT 10-APR-2019, sequence version 2.
DT 24-JAN-2024, entry version 44.
DE RecName: Full=DNA replication licensing factor MCM4 {ECO:0000256|RuleBase:RU368062};
DE EC=3.6.4.12 {ECO:0000256|RuleBase:RU368062};
GN Name=Bm6489 {ECO:0000313|EMBL:CDQ02279.1};
GN Synonyms=Bm1_48490 {ECO:0000313|WBParaSite:Bm6489a.1};
GN ORFNames=BM_Bm6489 {ECO:0000313|EMBL:CDQ02279.1};
OS Brugia malayi (Filarial nematode worm).
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Spirurina; Spiruromorpha; Filarioidea; Onchocercidae; Brugia.
OX NCBI_TaxID=6279 {ECO:0000313|EMBL:CDQ02279.1};
RN [1] {ECO:0000313|EMBL:CDQ02279.1, ECO:0000313|Proteomes:UP000006672}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=FR3 {ECO:0000313|EMBL:CDQ02279.1,
RC ECO:0000313|Proteomes:UP000006672};
RX PubMed=17885136; DOI=10.1126/science.1145406;
RA Ghedin E., Wang S., Spiro D., Caler E., Zhao Q., Crabtree J., Allen J.E.,
RA Delcher A.L., Guiliano D.B., Miranda-Saavedra D., Angiuoli S.V., Creasy T.,
RA Amedeo P., Haas B., El-Sayed N.M., Wortman J.R., Feldblyum T., Tallon L.,
RA Schatz M., Shumway M., Koo H., Salzberg S.L., Schobel S., Pertea M.,
RA Pop M., White O., Barton G.J., Carlow C.K., Crawford M.J., Daub J.,
RA Dimmic M.W., Estes C.F., Foster J.M., Ganatra M., Gregory W.F.,
RA Johnson N.M., Jin J., Komuniecki R., Korf I., Kumar S., Laney S., Li B.W.,
RA Li W., Lindblom T.H., Lustigman S., Ma D., Maina C.V., Martin D.M.,
RA McCarter J.P., McReynolds L., Mitreva M., Nutman T.B., Parkinson J.,
RA Peregrin-Alvarez J.M., Poole C., Ren Q., Saunders L., Sluder A.E.,
RA Smith K., Stanke M., Unnasch T.R., Ware J., Wei A.D., Weil G.,
RA Williams D.J., Zhang Y., Williams S.A., Fraser-Liggett C., Slatko B.,
RA Blaxter M.L., Scott A.L.;
RT "Draft genome of the filarial nematode parasite Brugia malayi.";
RL Science 317:1756-1760(2007).
RN [2] {ECO:0000313|EMBL:CDQ02279.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=FR3 {ECO:0000313|EMBL:CDQ02279.1};
RG WormBase Consortium;
RA Ghedin E., Paulini M.;
RL Submitted (DEC-2012) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|WBParaSite:Bm6489a.1}
RP IDENTIFICATION.
RG WormBaseParasite;
RL Submitted (APR-2022) 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:RU368062}.
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:RU368062};
CC -!- SUBUNIT: Component of the MCM2-7 complex.
CC {ECO:0000256|RuleBase:RU368062}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
CC -!- SIMILARITY: Belongs to the MCM family. {ECO:0000256|ARBA:ARBA00008010,
CC ECO:0000256|RuleBase:RU004070}.
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DR EMBL; LN857024; CDQ02279.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0K0JNC9; -.
DR EnsemblMetazoa; Bm6489a.1; Bm6489a.1; WBGene00226750.
DR WBParaSite; Bm6489a.1; Bm6489a.1; WBGene00226750.
DR OMA; NRCSFAD; -.
DR OrthoDB; 5476523at2759; -.
DR Proteomes; UP000006672; 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:InterPro.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0003678; F:DNA helicase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0006270; P:DNA replication initiation; IEA:InterPro.
DR CDD; cd17755; MCM4; 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; IPR003593; AAA+_ATPase.
DR InterPro; IPR031327; MCM.
DR InterPro; IPR008047; MCM_4.
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:SF66; DNA REPLICATION LICENSING FACTOR MCM4; 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; PR01660; MCMPROTEIN4.
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:RU368062};
KW DNA-binding {ECO:0000256|ARBA:ARBA00023125, ECO:0000256|RuleBase:RU004070};
KW Helicase {ECO:0000256|ARBA:ARBA00022806, ECO:0000256|RuleBase:RU368062};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU368062};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW ECO:0000256|RuleBase:RU004070};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242, ECO:0000256|RuleBase:RU368062};
KW Reference proteome {ECO:0000313|Proteomes:UP000006672}.
FT DOMAIN 478..686
FT /note="MCM"
FT /evidence="ECO:0000259|PROSITE:PS50051"
FT REGION 1..67
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 82..118
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 17..67
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 884 AA; 99794 MW; 522FE61CD2823875 CRC64;
MSGNSLHSRS TRSRLHLRST TSRSPPSLHE TLSEASDNST RTTQQRTARN ASQSRSLHRT
VQQPLLSQEQ MIVEGGNTLN TEQEAVQRGQ SDRHSPTRSQ LTESSALQYG SDFDTSSQVG
STVSWQRAVR HMRSDINCAP SQHRTICIDS MEDDLSIDLE PGPKLYIWGT RICVFDVQRA
FRTFVNEFRP TSVSDDENVL TLPSNVRMEI DLERPYYLER LYEIDQSENI AFNLNLQHVK
LFSEALYRKI VCYPSDVIPY LDLTINEIFS EKYQKVLYAP IEVRPFNAQK TRNMRALNPQ
DIDQLITIGG MVIRASPLIP EMRQAYFQCT VCNFPVDVEV DRGRIEEPAV CRNCQSKYSF
QLVHNRSLFM DKQIVKLQES PDDMPAGQTP HTVTLFAHGD MVERVQPGDR VTVTGIYRAV
PARVNPRMRN VNSVYRTSID VLHFRKTDQN RLHQIDDGTH LTDERVCMIM NLAKRTDIVN
CLINAVAPSI YGHEDIKRGI LCLLFGGANK EDKTGNKVKL RSEINILLCG DPGTSKSQLL
QYVYRLVPRA QYTSGKGSSA VGLTASVARD PDTRHLVLQT GALVLADNGV CCIDEFDKMN
DSTRSILHEV MEQQTLSIAK AGIICQLNAR TSILAAANPV DSQWNQNKTI VDNIQLPHTL
LSRFDLIFLL VDSQNELYDR RLANHLVSLY YRETNNEGCE LLDLALLRDY IGYARSYVNP
LLNEASSRCL IDKYLQMRKA GSGFGQVSAY PRQLESLIRL AEAHAKIRLS SVVSVQDVED
AYSLYREALK QSAVDPSTGR VDINILAAGI SATTRQIIDQ LAEAIRGELS QRQGILISLK
KLMQQLRQND LSFTKELFDE AVNNLIKNEV LVRTGDKIRY VAAT
//
