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Database: UniProt
Entry: A0A1X0QCI9_9MICR
LinkDB: A0A1X0QCI9_9MICR
Original site: A0A1X0QCI9_9MICR 
ID   A0A1X0QCI9_9MICR        Unreviewed;       711 AA.
AC   A0A1X0QCI9;
DT   05-JUL-2017, integrated into UniProtKB/TrEMBL.
DT   05-JUL-2017, sequence version 1.
DT   27-MAR-2024, entry version 31.
DE   RecName: Full=DNA replication licensing factor MCM2 {ECO:0000256|ARBA:ARBA00018925};
DE            EC=3.6.4.12 {ECO:0000256|ARBA:ARBA00012551};
GN   Name=MCM2 {ECO:0000313|EMBL:ORD97529.1};
GN   ORFNames=HERIO_602 {ECO:0000313|EMBL:ORD97529.1};
OS   Hepatospora eriocheir.
OC   Eukaryota; Fungi; Fungi incertae sedis; Microsporidia; Hepatosporidae;
OC   Hepatospora.
OX   NCBI_TaxID=1081669 {ECO:0000313|EMBL:ORD97529.1, ECO:0000313|Proteomes:UP000192356};
RN   [1] {ECO:0000313|EMBL:ORD97529.1, ECO:0000313|Proteomes:UP000192356}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=GB1 {ECO:0000313|EMBL:ORD97529.1,
RC   ECO:0000313|Proteomes:UP000192356};
RX   PubMed=28345194; DOI=10.1111/1462-2920.13734;
RA   Wiredu Boakye D., Jaroenlak P., Prachumwat A., Williams T.A., Bateman K.S.,
RA   Itsathitphaisarn O., Sritunyalucksana K., Paszkiewicz K.H., Moore K.A.,
RA   Stentiford G.D., Williams B.A.;
RT   "Decay of the glycolytic pathway and adaptation to intranuclear parasitism
RT   within Enterocytozoonidae microsporidia.";
RL   Environ. Microbiol. 19:2077-2089(2017).
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:ORD97529.1}.
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DR   EMBL; LVKB01000019; ORD97529.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1X0QCI9; -.
DR   VEuPathDB; MicrosporidiaDB:A0H76_2943; -.
DR   VEuPathDB; MicrosporidiaDB:A0H76_567; -.
DR   VEuPathDB; MicrosporidiaDB:HERIO_602; -.
DR   Proteomes; UP000192356; Unassembled WGS sequence.
DR   GO; GO:0031261; C:DNA replication preinitiation complex; IEA:UniProt.
DR   GO; GO:0042555; C:MCM complex; IEA:InterPro.
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-KW.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0004386; F:helicase activity; IEA:UniProtKB-KW.
DR   GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0032508; P:DNA duplex unwinding; IEA:InterPro.
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; 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; IPR008045; MCM2.
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:SF44; DNA REPLICATION LICENSING FACTOR MCM2; 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; PR01658; MCMPROTEIN2.
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   4: Predicted;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW   DNA replication {ECO:0000256|ARBA:ARBA00022705};
KW   DNA-binding {ECO:0000256|ARBA:ARBA00023125};
KW   Helicase {ECO:0000256|ARBA:ARBA00022806};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW   Reference proteome {ECO:0000313|Proteomes:UP000192356};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833};
KW   Zinc-finger {ECO:0000256|ARBA:ARBA00022771}.
FT   DOMAIN          315..520
FT                   /note="MCM"
FT                   /evidence="ECO:0000259|PROSITE:PS50051"
SQ   SEQUENCE   711 AA;  80440 MW;  394A60F878BF225B CRC64;
     MQRRRTEENE FNFDGSDSDS IILGSELHTL ASIVNDDRSI EVNNQNENLE DIDLLNELLT
     FVNSNYSRVI RNMAAKNLES IEIDYRDLIR FDLFIEQPEK FLDILSESLT KVTNQYFPSY
     YQIKSKIYPR VVNVPVVDEL RGLRNVHLNK MVRVQGVVTR RSGVFNLFSL VKYICNKCKA
     SIGPFYHNSR TAPSIKCVEC QSSSSFTVDV TETVYRDFQK ITIQEIPGTV PPGSLPRSKE
     IYLFNDLIDF SKPGDEVDVC GIYKNDFSPY LNLKNNFPVF STMIIASSVS KKINKMEMTN
     EDVKEIIELS KDSNILERLI NSVCPSIHGH KNIKTSILLA MVGGNSKQNN SLRIRGDINV
     LLLGDPSMAK SQFLRYINVI SHRAVMATGQ GSSGVGLTAS VRRDPMLKEW TLEGGALVLA
     DQGICCIDEF DKMNEIDRTS IHEAMEQQSI SISKAGIVAS LHARCSVVAA ANPIKGKYNS
     ALSFSQNVNL SDPILSRFDL LCVVKDNIDE IEDSKIADFI IKNHKMGNNE EETDINQDLL
     KKYILYAKNN IVPIIASFDI KKITRLYSDL RKESLHSGIP ITARHIESIV RISEAFAKLR
     MSSTVSKTDI NSAIDITLNT FLSAQKYSIA KTLRKKFAKY FEENNEDLII YLLKKMITEK
     VTVTGEGSIN VNEFIQYCKF NEVIVTDNFY KSDTFIKSGY QIENNVIIKR N
//
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