ID A0A158Q488_DRAME Unreviewed; 931 AA.
AC A0A158Q488;
DT 08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT 08-JUN-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=DME_LOCUS8143 {ECO:0000313|EMBL:VDN58170.1};
OS Dracunculus medinensis (Guinea worm).
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Spirurina; Dracunculoidea; Dracunculidae; Dracunculus.
OX NCBI_TaxID=318479 {ECO:0000313|Proteomes:UP000038040, ECO:0000313|WBParaSite:DME_0000426001-mRNA-1};
RN [1] {ECO:0000313|WBParaSite:DME_0000426001-mRNA-1}
RP IDENTIFICATION.
RG WormBaseParasite;
RL Submitted (APR-2016) to UniProtKB.
RN [2] {ECO:0000313|EMBL:VDN58170.1, ECO:0000313|Proteomes:UP000274756}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RG Pathogen Informatics;
RL Submitted (NOV-2018) to the EMBL/GenBank/DDBJ databases.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; UYYG01001166; VDN58170.1; -; Genomic_DNA.
DR STRING; 318479.A0A158Q488; -.
DR WBParaSite; DME_0000426001-mRNA-1; DME_0000426001-mRNA-1; DME_0000426001.
DR Proteomes; UP000038040; Unplaced.
DR Proteomes; UP000274756; Unassembled WGS sequence.
DR GO; GO:0042555; C:MCM complex; IEA:InterPro.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
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 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:UP000274756};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771}.
FT DOMAIN 488..694
FT /note="MCM"
FT /evidence="ECO:0000259|PROSITE:PS50051"
FT REGION 1..183
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..28
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 72..96
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 132..149
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 156..171
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 931 AA; 105773 MW; ED29261EA6A1EFF2 CRC64;
MSERSGSRRA SQNSSARQRS GSISSRSRHS SRRSARRQLT FEDSDSSNSP PSGAEAANDE
IDPIAELFGN ELNVEDDQEN DTNIGDGEES SEDLFGEDME RDYQAQPELD IYSESGMDDS
QYSVLSPSAR RAAERQMDRR DGIENEADLF YSREDEEEDE RQPRRRKEEE EKEDEDVEDE
ELPIDIVENL RGRTTRDHVS DVAVAKEIQR RFKNFLRNFR DPKTGKLKYI EAIKQMAAEN
RESVVLDYDD LASENGEQHI CYFLPDAPVQ IFGYLSRATT NIVLSMFPHY TRITPEVKIR
LRGMPVVDDI RMLRQIHLNM LVRVTGVVTV TTGMLPQLSL IKFDCLACGG LIGPFVQLQN
EECKPTTCPF CNTRGPFELN MEQTIYHNYQ RIIIQESPNK VAAGRLPRSK DVILTGDLCN
SCKPGDEIDV TGIYVNNYDG SMNSKHGFPV FSTVIHANYV IKKDKITSDS LTDEDIKIIK
ELSRDPNIAE RIFASIAPSI YGHEDVKRAI ALALFRGVEK NPGKKHNIRG DINVLLCGDP
GTAKSQFLRY AAHTAPRAVL TTGQGASAVG LTAYVQRHPV THEWTLEAGA MVLADKGVCL
IDEFDKMNDQ DRTSIHEAME QQSISISKAG IVTSLHARCT VIAAANPISG RYDITRTFAE
NVDLTEPILS RFDVLCVIRD VVDPNEDERL ANFVVASHHM HHPYNFIRDL ETENQIPDSE
ELQQLDDESK VKIIPQQLLR KYFMYARMNI CPKLQKIPQD KISKLFADMR RESLVTGSVA
VTVRNVESII RLSEAHARLH LRQNVNEDDV NVAIQIMLES FISTQKASIM RQMRKNFARY
LTFNRDNNEL LLFLLKEIAR GQIYFEKVRR GSASGFGTIS IPEYKFLDKA HQYHIENVKM
FYKSEVFKAN NFTYNARNKT IVLTFFADNS P
//
