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Database: UniProt
Entry: A0A420HP57_9PEZI
LinkDB: A0A420HP57_9PEZI
Original site: A0A420HP57_9PEZI 
ID   A0A420HP57_9PEZI        Unreviewed;       856 AA.
AC   A0A420HP57;
DT   08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT   08-MAY-2019, sequence version 1.
DT   27-MAR-2024, entry version 24.
DE   RecName: Full=DNA replication licensing factor MCM2 {ECO:0000256|ARBA:ARBA00018925};
DE            EC=3.6.4.12 {ECO:0000256|ARBA:ARBA00012551};
GN   ORFNames=OnM2_062008 {ECO:0000313|EMBL:RKF59201.1};
OS   Erysiphe neolycopersici.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC   Erysiphales; Erysiphaceae; Erysiphe.
OX   NCBI_TaxID=212602 {ECO:0000313|EMBL:RKF59201.1, ECO:0000313|Proteomes:UP000286134};
RN   [1] {ECO:0000313|EMBL:RKF59201.1, ECO:0000313|Proteomes:UP000286134}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=UMSG2 {ECO:0000313|EMBL:RKF59201.1};
RX   PubMed=30253736; DOI=10.1186/s12864-018-5069-z;
RA   Wu Y., Ma X., Pan Z., Kale S.D., Song Y., King H., Zhang Q., Presley C.,
RA   Deng X., Wei C.I., Xiao S.;
RT   "Comparative genome analyses reveal sequence features reflecting distinct
RT   modes of host-adaptation between dicot and monocot powdery mildew.";
RL   BMC Genomics 19:705-705(2018).
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:RKF59201.1}.
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DR   EMBL; MCFK01006218; RKF59201.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A420HP57; -.
DR   STRING; 212602.A0A420HP57; -.
DR   Proteomes; UP000286134; 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   CDD; cd17753; MCM2; 1.
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:UP000286134};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833};
KW   Zinc-finger {ECO:0000256|ARBA:ARBA00022771}.
FT   DOMAIN          475..681
FT                   /note="MCM"
FT                   /evidence="ECO:0000259|PROSITE:PS50051"
FT   REGION          1..49
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          686..716
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        699..716
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   856 AA;  96600 MW;  4B1CE08545005A37 CRC64;
     MSFTNRGAGH KRAREIEEEN DLGTSPLPID FRSSPPAYPI SHGVDDDNDD IEEEIALDID
     DIDEMIDEED GIDLFADNFE RDYADRKDEK YEGIDIDDAD YDDLDLAERR KLEARLNRRD
     RDLARAQQMP AGFLLDDGDD GDIDLSVQPR RRRHHYDEDD DMEDDIMDEE LSLETLQDVK
     ASSLVDWVSQ QAVQRSIKRE FKAFLTEYTD DNGVSVYGER IRTLGEINSE SLEVSYDHLT
     SSKAILAYFL ISAPGELLKL FDEVAMDVTL LHYPDYERIH SEIHVRISHL PVQFTLRQLR
     QSHLNCLVRV SGVVTRRSGV FPQLKYVMFD CGRCGARLGP FQQESSVEIK ISYCQNCQSR
     GPFNLNSEKT VYRNYQKLTL QESPGTVPTG RLPRHREVIL LWDLIDKAKP GEEIEVTGVY
     RNNYDSQLNN KNGFPVFATI LEANNVIKSH DQLAGFRLTE EDERKIRLLS RDPKIIDKII
     NSIAPSIYGH KDIKTAIALS LFGGVAKDRQ GKHHIRGDIN VLLLGDPGTA KSQVLKYVEK
     TAHRAVFTTG QGASAVGLTA SVRKDPLTGE WTLEGGALVL ADKGTCLIDE FDKMNDQDRT
     SIHEAMEQQT ISISKAGIVT TLQARCGIIA AANPIGGRYN STIPFSQNVQ LTEPILSRFD
     ILCVVRDTVD PEEDEFLARF VVGSHSRSHP SQTTETQNLN DADRDRPSVP RNESMNKDGI
     DQELFRKYIL YARERCNPKL YNIDEEKVSK LFADMRRESL ATGAYPITVR HLEAIMRISE
     AFCRMRLSEY VSSHDVDRAI AVTIDSFVGS QKISCKKALA RAFAKYTLSR TGKGKKSGVE
     KNLVRQGRSF GTISAA
//
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