ID A0A2G5DBN9_AQUCA Unreviewed; 937 AA.
AC A0A2G5DBN9;
DT 31-JAN-2018, integrated into UniProtKB/TrEMBL.
DT 31-JAN-2018, sequence version 1.
DT 27-MAR-2024, entry version 32.
DE RecName: Full=DNA replication licensing factor MCM2 {ECO:0000256|ARBA:ARBA00018925};
DE EC=3.6.4.12 {ECO:0000256|ARBA:ARBA00012551};
GN ORFNames=AQUCO_02400011v1 {ECO:0000313|EMBL:PIA40647.1};
OS Aquilegia coerulea (Rocky mountain columbine).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Ranunculales; Ranunculaceae; Thalictroideae;
OC Aquilegia.
OX NCBI_TaxID=218851 {ECO:0000313|EMBL:PIA40647.1, ECO:0000313|Proteomes:UP000230069};
RN [1] {ECO:0000313|EMBL:PIA40647.1, ECO:0000313|Proteomes:UP000230069}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Goldsmith {ECO:0000313|Proteomes:UP000230069};
RA Hodges S., Kramer E., Nordborg M., Tomkins J., Borevitz J., Derieg N.,
RA Yan J., Mihaltcheva S., Hayes R.D., Rokhsar D.;
RT "WGS assembly of Aquilegia coerulea Goldsmith.";
RL Submitted (SEP-2017) to the EMBL/GenBank/DDBJ databases.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + H2O = ADP + H(+) + phosphate; Xref=Rhea:RHEA:13065,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; EC=3.6.4.12;
CC Evidence={ECO:0000256|ARBA:ARBA00001665};
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
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DR EMBL; KZ305041; PIA40647.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2G5DBN9; -.
DR Proteomes; UP000230069; 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:0016887; F:ATP hydrolysis activity; IEA:RHEA.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0004386; F:helicase activity; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0006270; P:DNA replication initiation; IEA:InterPro.
DR GO; GO:0006268; P:DNA unwinding involved in 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:UP000230069};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771}.
FT DOMAIN 500..706
FT /note="MCM"
FT /evidence="ECO:0000259|PROSITE:PS50051"
FT REGION 1..196
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 716..737
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..35
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 36..65
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 66..87
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 96..153
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 181..196
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 716..734
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 937 AA; 106593 MW; EB5214CBA7971969 CRC64;
MDNSDNPSTP GSPTSAGFST DRLPPNTSGT NESYSDEDEA AVDPEIIRDE PEEVEEEEDG
EDLFNDNYMD DYRRMEEHDQ YESVGLDDSM EDERDLDQIM ADRRAAEVEL DTKEGRNSNR
KLPRLLHDQD EDINYRRPKR SRADFRPPAD ARSYDDADAM QSSPGRSQRG HSRDDVPMTD
QTDDEPYEDD DDDEGEFEMY RVQGTLREWV TRDEVRRFIA KKFKEFLLTY VNPKNEQGEF
EYIRLINEMM RVNKCSLEID YKQFIYIHPN IAIWLADAPQ SVLEVMEEVA KNVVFNLHPN
YKEIHQKIYV RITNLPVYDQ IRNIRQIHLN TMIRIGGVVT RRTGVFPQLQ QVKYDCNKCG
TILGPFFQNS YSEVKVGSCP ECQSKGPFTV NIEQTIYRNY QKLTLQESPG IVPAGRLPRY
KEVILLNDLI DCARPGEEIE VTGIYTNNFD LSLNTKNGFP VFATVVEANY VTKKKDLFSA
YKLTVEDTNE IENLGRDPRI GERIIKSIAP SIYGHEDIKT ALALAMFGGQ EKNVQGKHRL
RGDINVLLLG DPGTAKSQFL KYVEKTGQRA VYTTGKGASA VGLTAAVHKD PVTREWTLEG
GALVLADRGI CLIDEFDKMN DQDRVSIHEA MEQQSISISK AGIVTSLQAR CSVIAAANPI
GGRYDSSKNF SQNVELTDPI VSRFDVLCVV KDVVDPVVDE MLASFVVNSH FKSQPKGANL
DDTSMNNSQE EDPSSTRLVD PEILSQDMLK KYITYAKLNI QPRLNEADLN KLTHVYAELR
RESSHGQGVP IAVRHIESMI RMSEAHARMH LRKDVAQEDV DMAIRVLLDS FISTQKFGVQ
KALQKSFRKY MTFKKEFNDL LLYLLRGLVR DAMHFEELVN GSAAGLTHID VKVKDLENKA
QEYEIYDLKP FFTSTLFSGA NFDLDEERGI IKHRLAG
//
