ID I7IFV4_BABMR Unreviewed; 897 AA.
AC I7IFV4;
DT 03-OCT-2012, integrated into UniProtKB/TrEMBL.
DT 03-OCT-2012, sequence version 1.
DT 24-JAN-2024, entry version 62.
DE RecName: Full=DNA replication licensing factor MCM4 {ECO:0000256|RuleBase:RU368062};
DE EC=3.6.4.12 {ECO:0000256|RuleBase:RU368062};
GN ORFNames=BMR1_01G03255 {ECO:0000313|EMBL:CCF73106.1};
OS Babesia microti (strain RI).
OC Eukaryota; Sar; Alveolata; Apicomplexa; Aconoidasida; Piroplasmida;
OC Babesiidae; Babesia.
OX NCBI_TaxID=1133968 {ECO:0000313|EMBL:CCF73106.1, ECO:0000313|Proteomes:UP000002899};
RN [1] {ECO:0000313|EMBL:CCF73106.1, ECO:0000313|Proteomes:UP000002899}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=RI {ECO:0000313|EMBL:CCF73106.1,
RC ECO:0000313|Proteomes:UP000002899};
RX PubMed=22833609; DOI=10.1093/nar/gks700;
RA Cornillot E., Hadj-Kaddour K., Dassouli A., Noel B., Ranwez V.,
RA Vacherie B., Augagneur Y., Bres V., Duclos A., Randazzo S., Carcy B.,
RA Debierre-Grockiego F., Delbecq S., Moubri-Menage K., Shams-Eldin H.,
RA Usmani-Brown S., Bringaud F., Wincker P., Vivares C.P., Schwarz R.T.,
RA Schetters T.P., Krause P.J., Gorenflot A., Berry V., Barbe V.,
RA Ben Mamoun C.;
RT "Sequencing of the smallest Apicomplexan genome from the human pathogen
RT Babesia microti.";
RL Nucleic Acids Res. 40:9102-9114(2012).
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; FO082871; CCF73106.1; -; Genomic_DNA.
DR RefSeq; XP_012647715.1; XM_012792261.1.
DR AlphaFoldDB; I7IFV4; -.
DR GeneID; 24423726; -.
DR KEGG; bmic:BMR1_01G03255; -.
DR VEuPathDB; PiroplasmaDB:BMR1_01G03255; -.
DR OMA; GRQNECK; -.
DR OrthoDB; 5476523at2759; -.
DR Proteomes; UP000002899; Chromosome I.
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:UniProtKB-UniRule.
DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR GO; GO:0006270; P:DNA replication initiation; IEA:InterPro.
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; 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; 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:0000313|EMBL:CCF73106.1};
KW Cell division {ECO:0000313|EMBL:CCF73106.1};
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:UP000002899}.
FT DOMAIN 493..694
FT /note="MCM"
FT /evidence="ECO:0000259|PROSITE:PS50051"
FT REGION 1..78
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..61
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 897 AA; 101357 MW; 9F826AE3431C49D0 CRC64;
MSNNRSSNTL HNNSQDNFSN DTQNTPNGTP LNSNNIPIPF QSSTNTGSQS NRNNTQDGRT
LAFDGHSMRR RSSINETPVR QFRNVDDQVD QGSISMRRRR VLNESIDTQH DTQYTQYGKT
PMVIRRIRAA RGDIGDMGRE FLMQDFEIER LPYIVDEEID QVYERFTNFF YDFNPLNYPD
ILTDLDNEII INSSTNEIQE LSYYAKKLLK IVEMTSEKTF PVDLAHIALF DRKLYHLIVN
YPADCICEID KIVRKCFEKL TTLVFNITES AIIPRIVLYN KPEFDTSRLL GPKDIETLVS
LKGIVVRFSN VIPEMTMAAF RCNGYKQSGL NRVTCNNEIY EHVIQGDVIE PMLCKNCGSR
NSFELVHNMC CFTSKQLIKL IELPEVLGKG QFPASISLYA YDECIDAAKP GDRVEITGIF
RASGVRMNPR MRNLSTIFKT FINVLHIRKI DKNSVKVPQM GIFDSTEEGK AEHLHLSPEL
ISQILNLSRD KNIYEKLIKS FAPSIYGRDD VKMGLLCQLF GGSKNDNTRS DIHILLCGDP
STAKSQFLQY VHKLSLRGIY TSGKGSSQVG LTAYVGKDPE TREYILESGA VVLSDRGICC
IDEFDKMNES ARTVLHEVME QQTVTIAKAG IVATLNARTA ILASANPINS RYDRRKAVVE
NINLPPSLFS RFDLIYLIID TANEIEDRAL ALSICSNFSD TQDVAPIDPH LFASYISYAR
ANCNPKLTPN AKEIIISEYL RLRSNDSVHT LFNGSTLSNK APSASTRQLE ALIRLSQAVA
KMRLSHTVEV GDVQEATRLM KVATFASLID PSSGKIDFDQ LHIGQTLVNM DRMREVKSVI
LKGIDVEPSN KDELYKVCQA NLPKWFDYKL FDDALFDLES SLSITVLQNG DVKRTIF
//