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Database: UniProt
Entry: W6ZHK9_COCMI
LinkDB: W6ZHK9_COCMI
Original site: W6ZHK9_COCMI 
ID   W6ZHK9_COCMI            Unreviewed;       858 AA.
AC   W6ZHK9;
DT   16-APR-2014, integrated into UniProtKB/TrEMBL.
DT   16-APR-2014, sequence version 1.
DT   27-MAR-2024, entry version 59.
DE   RecName: Full=DNA replication licensing factor MCM2 {ECO:0000256|ARBA:ARBA00018925};
DE            EC=3.6.4.12 {ECO:0000256|ARBA:ARBA00012551};
GN   ORFNames=COCMIDRAFT_131 {ECO:0000313|EMBL:EUC51332.1};
OS   Bipolaris oryzae ATCC 44560.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC   Pleosporomycetidae; Pleosporales; Pleosporineae; Pleosporaceae; Bipolaris.
OX   NCBI_TaxID=930090 {ECO:0000313|EMBL:EUC51332.1};
RN   [1] {ECO:0000313|EMBL:EUC51332.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 44560 {ECO:0000313|EMBL:EUC51332.1};
RX   PubMed=23357949; DOI=10.1371/journal.pgen.1003233;
RA   Condon B.J., Leng Y., Wu D., Bushley K.E., Ohm R.A., Otillar R., Martin J.,
RA   Schackwitz W., Grimwood J., MohdZainudin N., Xue C., Wang R., Manning V.A.,
RA   Dhillon B., Tu Z.J., Steffenson B.J., Salamov A., Sun H., Lowry S.,
RA   LaButti K., Han J., Copeland A., Lindquist E., Barry K., Schmutz J.,
RA   Baker S.E., Ciuffetti L.M., Grigoriev I.V., Zhong S., Turgeon B.G.;
RT   "Comparative genome structure, secondary metabolite, and effector coding
RT   capacity across Cochliobolus pathogens.";
RL   PLoS Genet. 9:E1003233-E1003233(2013).
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
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DR   EMBL; KI963918; EUC51332.1; -; Genomic_DNA.
DR   RefSeq; XP_007682065.1; XM_007683875.1.
DR   AlphaFoldDB; W6ZHK9; -.
DR   STRING; 930090.W6ZHK9; -.
DR   GeneID; 19119837; -.
DR   KEGG; bor:COCMIDRAFT_131; -.
DR   eggNOG; KOG0477; Eukaryota.
DR   HOGENOM; CLU_000995_0_1_1; -.
DR   OrthoDB; 5476523at2759; -.
DR   Proteomes; UP000054032; 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   Zinc {ECO:0000256|ARBA:ARBA00022833};
KW   Zinc-finger {ECO:0000256|ARBA:ARBA00022771}.
FT   DOMAIN          479..685
FT                   /note="MCM"
FT                   /evidence="ECO:0000259|PROSITE:PS50051"
FT   REGION          1..73
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        47..73
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   858 AA;  95604 MW;  6719164B1BFB75BE CRC64;
     MSSANRGAGP ASRSNKRARD DEDLPSSAVH PPSSPMASSP PMLPNEDDAD MLDDDDIIRD
     VDDLEEDAEE AEGIDLFADD FENDYAAREN DAYEGQGIDD EGEYEELSLA ERRKLDASLN
     ARDREARRRM PAAFLPDDDE QDGLAGLMGR RRVRRHRYDE EDDMDMADDI MNEELTLEAL
     TDVKANTLTD WVAQPQVART IAREFKSFLT EYTDEHGHSV YGARIRTLGE VNAESLEVSF
     DHLAEQKATL AYWLANTPTE MLKIFDQVAM EVTLLHYPDY ERIHSEIHVR ITDVPVQYTL
     RQLRQSHLNS LVRVSGVVTR RSGVFPQLKY VKFDCTKCGV TLGPFHQDSN VEVKISFCQN
     CQSRGPFTVN SERTVYRNYQ KLTLQESPGT VPAGRLPRHR EVILLWDLID SAKPGEEIEV
     TGIYRNNYDA ALNNKNGFPV FATILEANYI VKSHDQLAGF RLTEDDEKEI RRLSKDPRIV
     DKIIGSIAPS IYGHTDIKTA VALSLFGGVS KEAPGRHSIR GDINVLLLGD PGTAKSQILK
     YVEKTAHRAV FATGQGASAV GLTASVRRDP MTSEWTLEGG ALVLADKGTC LIDEFDKMND
     QDRTSIHEAM EQQTISISKA GIVTTLQARC SIVAAANPIG GRYNSTIPFS QNVELTEPIL
     SRFDILCVVR DTVDPAEDER LAKFVVNSHG RAHPLVNSTY GYSDKAKASQ NGDDQMEVDG
     DAPVKEGEIP QELLRKYILY ARERCRPKLY QIEQDKIARL FADMRRESMA TGAYPITVRH
     LEAILRIAES FCKMRLSDYC SSVDIDRAIA VAVDSFVGSQ KVSAKKALAR AFAKYTLNRP
     GAVSAPTRGG RQTQRAAA
//
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