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Database: UniProt
Entry: A0A0M8N4Y5_9HYPO
LinkDB: A0A0M8N4Y5_9HYPO
Original site: A0A0M8N4Y5_9HYPO 
ID   A0A0M8N4Y5_9HYPO        Unreviewed;       762 AA.
AC   A0A0M8N4Y5;
DT   09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT   09-DEC-2015, sequence version 1.
DT   27-MAR-2024, entry version 43.
DE   RecName: Full=DNA replication licensing factor MCM2 {ECO:0000256|ARBA:ARBA00018925};
DE            EC=3.6.4.12 {ECO:0000256|ARBA:ARBA00012551};
GN   ORFNames=ESCO_005749 {ECO:0000313|EMBL:KOS20050.1};
OS   Escovopsis weberi.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Hypocreomycetidae; Hypocreales; Hypocreaceae; Escovopsis.
OX   NCBI_TaxID=150374 {ECO:0000313|EMBL:KOS20050.1, ECO:0000313|Proteomes:UP000053831};
RN   [1] {ECO:0000313|EMBL:KOS20050.1, ECO:0000313|Proteomes:UP000053831}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   de Man T.J., Stajich J.E., Kubicek C.P., Chenthamara K., Atanasova L.,
RA   Druzhinina I.S., Birnbaum S., Barribeau S.M., Teiling C., Suen G.,
RA   Currie C., Gerardo N.M.;
RT   "The genome of the fungus Escovopsis weberi, a specialized disease agent of
RT   ant agriculture.";
RL   Submitted (JUL-2015) to the EMBL/GenBank/DDBJ databases.
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:KOS20050.1}.
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DR   EMBL; LGSR01000019; KOS20050.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0M8N4Y5; -.
DR   STRING; 150374.A0A0M8N4Y5; -.
DR   OrthoDB; 5476523at2759; -.
DR   Proteomes; UP000053831; 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; PF12619; MCM2_N; 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:UP000053831};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833};
KW   Zinc-finger {ECO:0000256|ARBA:ARBA00022771}.
FT   DOMAIN          447..653
FT                   /note="MCM"
FT                   /evidence="ECO:0000259|PROSITE:PS50051"
FT   REGION          1..21
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          52..71
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          660..696
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        660..692
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   762 AA;  85154 MW;  977084E14AE77FEB CRC64;
     MPSSPPDYNI AHGVEDDDDI EEEAQIQDDV DDLDEMAEDD VDLFREGFEA DYRDKDNDVY
     DGAGIDDDGD FDDMSLGDRR RLEAQLNRRD REVARQQRIP AAFLPGEDDE GDIDLTAQPR
     RRRHHYDEDP DDAMDADIME EELSLEALGD VKASNLTEWV SSPQVQRSIK REFKAFLTSY
     IDSNGNSVYG NRIRTLGEIN AESLEVSYEH LAESKAILAY FLANAPAELL KLFDEVAMDV
     VLLHYPDYER IHAEIHVRIF DLPVHYTLRQ LRQSHLNCLV RVSGVVTRRS GVFPQLKYVK
     FDCSKCGVTL GPFQQESNVE VKITYCQSCQ SRGPFTLNSE KTVYRNYQRL TLQESPGTVP
     AGRLPRQREV ILLWDLIDKA KPGEEIEVTG IYRNNYDAQL NNRNGFPVFA TILEANNVVK
     SHDQLAGFRL TEQDEDEIRK LSRDPGIVDK IINSIAPSIY GHTDIKTAVA LSLFGGVAKT
     GRGQHHVRGD INVLLLGDPG TAKSQVLKYA EKTAHRAVFA TGQGASAVGL TASVRRDPLT
     SEWTLEGGAL VLADRGTCLI DEFDKMNDQD RTSIHEAMEQ QTISISKAGI VTTLQARCGI
     IAAANPIGGR YNSTIPFSAN VELTEPILSR FDVLCVVRDL VEPAEDERLA RFIVGSHSRS
     HPLSQTQSRP DQSSNDADAM VTQPTTAGAS SASREAGDIP QELLRKYILY ARERCSPKLY
     HMDEDKVARL FADMRRESLA TGAYPITVSY RGDLTTEGRE GY
//
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