ID A0A100IM53_ASPNG Unreviewed; 898 AA.
AC A0A100IM53;
DT 13-APR-2016, integrated into UniProtKB/TrEMBL.
DT 13-APR-2016, sequence version 1.
DT 27-MAR-2024, entry version 40.
DE RecName: Full=DNA replication licensing factor MCM2 {ECO:0000256|ARBA:ARBA00018925};
DE EC=3.6.4.12 {ECO:0000256|ARBA:ARBA00012551};
GN ORFNames=ABL_06413 {ECO:0000313|EMBL:GAQ43752.1};
OS Aspergillus niger.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Circumdati.
OX NCBI_TaxID=5061 {ECO:0000313|EMBL:GAQ43752.1, ECO:0000313|Proteomes:UP000068243};
RN [1] {ECO:0000313|Proteomes:UP000068243}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=An76 {ECO:0000313|Proteomes:UP000068243};
RX PubMed=26893421; DOI=10.1128/genomeA.01700-15;
RA Gong W., Cheng Z., Zhang H., Liu L., Gao P., Wang L.;
RT "Draft genome sequence of Aspergillus niger strain An76.";
RL Genome Announc. 4:E0170015-E0170015(2016).
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:GAQ43752.1}.
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DR EMBL; BCMY01000010; GAQ43752.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A100IM53; -.
DR PaxDb; 5061-CADANGAP00007856; -.
DR VEuPathDB; FungiDB:An09g04640; -.
DR VEuPathDB; FungiDB:ASPNIDRAFT2_1099304; -.
DR VEuPathDB; FungiDB:ATCC64974_9370; -.
DR VEuPathDB; FungiDB:M747DRAFT_299059; -.
DR OMA; TYERVTT; -.
DR Proteomes; UP000068243; 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 486..692
FT /note="MCM"
FT /evidence="ECO:0000259|PROSITE:PS50051"
FT REGION 1..86
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 736..758
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 869..898
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 35..49
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 53..84
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 898 AA; 101212 MW; 2E95085165A1FF59 CRC64;
MSSPLRPSDS AANRGLGNLG RRKRSREPDD ETSSVVPPSS PPPSSPPMLP FDDDDNERDE
EAELLGDIDD IDEMAEDEDG IDLFGDNFEK DYRSTADDQY RGEYIDDDGD HEELDVATRR
QLEARMNKRD RELERRRRMP AAFLQDDEDG DIDLTRQPRR RRHHYDEDRD DVEMGDDAME
ELSLEELTDV KASNLTDWVL QPQVLRSIYR EFKSFLTEYT DPAGASVYGN KIKTLGEVNS
ASLEVSYAHL LETKAALAYF LANEPTEVLK VFDQVALDVT LFHYPQYHDI HNEIHVRITD
LPVSYTLRQL RQSHLNCLIR VSGVVTRRTG VFPQLKYVMF VCGKCNITLG PFQQEASAEV
KISYCQNCQS KGPFSVHSEK TVYRNYQKMT LQESPGSVPA GRLPRQREVV LLADLIDSAK
PGDEIEVTGI YRNSYDAQLN NKNGFPVFAT IIEANHVVKS HDQLAGFHLT EEDEREIRAL
SRDPEIVDKI VRSVAPSIYG HLDVKTAIAL SLFGGVSKEA QGKMSIRGDI NVLLLGDPGT
AKSQFLKYTE KTAHRAVFAT GQGASAVGLT ASVRRDPLTS EWTLEGGALV LADRGTCLID
EFDKMNDQDR TSIHEAMEQQ TISISKAGIV TTLQARCAVV AAANPIGGRY NSSAPFSENV
QLTEPILSRF DILCVVRDLV DPSEDERLAN FVIESHHRAN PARPLRDQDG NLINADGHPI
DEDGYRIDKK TKQRLPLTDE ELATRDAEKQ RREDEKDGEI PQELLRKYIL YARERCHPKL
YQIDQDKIAR LFADMRRESL ATGAYPITVR HLEAIMRIAE SFCKMRLSEY CSAQDIDRAI
AVTVDSFIGS QKISCKKALS RAFAKYTLSR PKPQSKRRAG IPAPDPFKPR MQSSTRAR
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