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Database: UniProt
Entry: A0A059F483_9MICR
LinkDB: A0A059F483_9MICR
Original site: A0A059F483_9MICR 
ID   A0A059F483_9MICR        Unreviewed;       671 AA.
AC   A0A059F483;
DT   09-JUL-2014, integrated into UniProtKB/TrEMBL.
DT   09-JUL-2014, sequence version 1.
DT   27-MAR-2024, entry version 48.
DE   RecName: Full=DNA replication licensing factor MCM3 {ECO:0000256|RuleBase:RU368061};
DE            EC=3.6.4.12 {ECO:0000256|RuleBase:RU368061};
GN   ORFNames=H312_00821 {ECO:0000313|EMBL:KCZ81781.1};
OS   Anncaliia algerae PRA339.
OC   Eukaryota; Fungi; Fungi incertae sedis; Microsporidia; Tubulinosematoidea;
OC   Tubulinosematidae; Anncaliia.
OX   NCBI_TaxID=1288291 {ECO:0000313|EMBL:KCZ81781.1, ECO:0000313|Proteomes:UP000030655};
RN   [1] {ECO:0000313|Proteomes:UP000030655}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PRA339 {ECO:0000313|Proteomes:UP000030655};
RG   The Broad Institute Genome Sequencing Platform;
RA   Cuomo C., Becnel J., Sanscrainte N., Walker B., Young S.K., Zeng Q.,
RA   Gargeya S., Fitzgerald M., Haas B., Abouelleil A., Alvarado L.,
RA   Arachchi H.M., Berlin A.M., Chapman S.B., Dewar J., Goldberg J., Griggs A.,
RA   Gujja S., Hansen M., Howarth C., Imamovic A., Larimer J., McCowan C.,
RA   Murphy C., Neiman D., Pearson M., Priest M., Roberts A., Saif S., Shea T.,
RA   Sisk P., Sykes S., Wortman J., Nusbaum C., Birren B.;
RL   Submitted (FEB-2013) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:KCZ81781.1, ECO:0000313|Proteomes:UP000030655}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PRA339 {ECO:0000313|EMBL:KCZ81781.1,
RC   ECO:0000313|Proteomes:UP000030655};
RG   The Broad Institute Genome Sequencing Platform;
RG   The Broad Institute Genome Sequencing Center for Infectious Disease;
RA   Cuomo C., Becnel J., Sanscrainte N., Walker B., Young S.K., Zeng Q.,
RA   Gargeya S., Fitzgerald M., Haas B., Abouelleil A., Alvarado L.,
RA   Arachchi H.M., Berlin A.M., Chapman S.B., Dewar J., Goldberg J., Griggs A.,
RA   Gujja S., Hansen M., Howarth C., Imamovic A., Larimer J., McCowan C.,
RA   Murphy C., Neiman D., Pearson M., Priest M., Roberts A., Saif S., Shea T.,
RA   Sisk P., Sykes S., Wortman J., Nusbaum C., Birren B.;
RT   "The Genome Sequence of Anncaliia algerae insect isolate PRA339.";
RL   Submitted (MAR-2014) 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:RU368061}.
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:RU368061};
CC   -!- SUBUNIT: Component of the MCM2-7 complex.
CC       {ECO:0000256|RuleBase:RU368061}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|RuleBase:RU368061}.
CC   -!- SIMILARITY: Belongs to the MCM family. {ECO:0000256|RuleBase:RU004070}.
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DR   EMBL; KK365137; KCZ81781.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A059F483; -.
DR   STRING; 1288291.A0A059F483; -.
DR   VEuPathDB; MicrosporidiaDB:H312_00821; -.
DR   HOGENOM; CLU_000995_6_0_1; -.
DR   Proteomes; UP000030655; 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:InterPro.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
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:InterPro.
DR   GO; GO:0006279; P:premeiotic DNA replication; IEA:UniProt.
DR   Gene3D; 2.20.28.10; -; 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; IPR008046; Mcm3.
DR   InterPro; IPR018525; MCM_CS.
DR   InterPro; IPR001208; MCM_dom.
DR   InterPro; IPR041562; MCM_lid.
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:SF46; DNA REPLICATION LICENSING FACTOR MCM3; 1.
DR   Pfam; PF00493; MCM; 1.
DR   Pfam; PF17855; MCM_lid; 1.
DR   Pfam; PF17207; MCM_OB; 1.
DR   PRINTS; PR01657; MCMFAMILY.
DR   PRINTS; PR01659; MCMPROTEIN3.
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|RuleBase:RU368061};
KW   DNA-binding {ECO:0000256|ARBA:ARBA00023125, ECO:0000256|RuleBase:RU004070};
KW   Helicase {ECO:0000256|ARBA:ARBA00022806, ECO:0000256|RuleBase:RU368061};
KW   Hydrolase {ECO:0000256|RuleBase:RU368061};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW   ECO:0000256|RuleBase:RU004070}; Nucleus {ECO:0000256|RuleBase:RU368061};
KW   Reference proteome {ECO:0000313|Proteomes:UP000030655}.
FT   DOMAIN          295..498
FT                   /note="MCM"
FT                   /evidence="ECO:0000259|PROSITE:PS50051"
SQ   SEQUENCE   671 AA;  75383 MW;  4FA2AC75F9847456 CRC64;
     MEHSSKISFT DVKPILDLNE LRITQPKFVE SIINDPLNVL PQHPNKKIIG SLGENIHNPR
     TLTCKSLSKL IAVEGIVTSV STVKPKLVKS VHFSEKTKIF YEKEYRDATM ISKLPITNTV
     YPTKDANGPL NTEFGMSTFI DYQNVVIQEL VETSPLGQLP RSMEAILSDD LINRVKPGDR
     VRLIGVYKPL VGMSNEFPKK FKSVLIVNNI EFINLDSAHM KVNIEKINEL TFQQLGEKGL
     EGIVVECEEN LQSKKFGEFD IKENASQTEK NNSSTNQNLI QSEHVIREIS KRKDILNLVA
     NSIAPSIYGH TNIKRAIALM LVGGNEIIRN NLSKTRGDIN ILLVGDPGTA KSQLLRYVKS
     ISPLCINTTG RGSTGVGLTA AVVFDKDTGD KRLEAGAMVI ADRGIVCIDE FDKMNDDDRV
     ALHEVMEQQT ISISKAGIST TLNARCTVLA AANPILGYYK ETYSPSHNIG LPESLLSRFD
     LIFIVLDRGD DERIADHILN KREDTHQLFL REYLKTAKEM KPTLTDRAGI AISKSFVELR
     QEKKLSVNVT PRMLETLIRL STAIAKIKLS NFVEEEDALE AIKILRETLE FKVTKEIVQE
     KKEEEQNVDE LISSVLYSYK ENHPETNSIS FDDFCKEVND LNVSPAQIRS VLNYLHSIDV
     ILFYDNTIFF L
//
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