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Database: UniProt
Entry: I7IFV4_BABMR
LinkDB: I7IFV4_BABMR
Original site: I7IFV4_BABMR 
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
//
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