ID A0A078BEG2_STYLE Unreviewed; 943 AA.
AC A0A078BEG2;
DT 29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 29-OCT-2014, sequence version 1.
DT 24-JAN-2024, entry version 48.
DE RecName: Full=DNA replication licensing factor MCM2 {ECO:0000256|ARBA:ARBA00018925};
DE EC=3.6.4.12 {ECO:0000256|ARBA:ARBA00012551};
GN Name=Contig1044.g1137 {ECO:0000313|EMBL:CDW91542.1};
GN ORFNames=STYLEM_20698 {ECO:0000313|EMBL:CDW91542.1};
OS Stylonychia lemnae (Ciliate).
OC Eukaryota; Sar; Alveolata; Ciliophora; Intramacronucleata; Spirotrichea;
OC Stichotrichia; Sporadotrichida; Oxytrichidae; Stylonychinae; Stylonychia.
OX NCBI_TaxID=5949 {ECO:0000313|EMBL:CDW91542.1, ECO:0000313|Proteomes:UP000039865};
RN [1] {ECO:0000313|EMBL:CDW91542.1, ECO:0000313|Proteomes:UP000039865}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=130c {ECO:0000313|EMBL:CDW91542.1,
RC ECO:0000313|Proteomes:UP000039865};
RA Swart Estienne;
RL Submitted (JUN-2014) to the EMBL/GenBank/DDBJ databases.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
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DR EMBL; CCKQ01019523; CDW91542.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A078BEG2; -.
DR EnsemblProtists; CDW91542; CDW91542; STYLEM_20698.
DR InParanoid; A0A078BEG2; -.
DR OMA; NTDQGFP; -.
DR OrthoDB; 5476523at2759; -.
DR Proteomes; UP000039865; 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:0032508; P:DNA duplex unwinding; IEA:InterPro.
DR GO; GO:0006270; P:DNA replication initiation; IEA:InterPro.
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:UP000039865};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771}.
FT DOMAIN 487..693
FT /note="MCM"
FT /evidence="ECO:0000259|PROSITE:PS50051"
FT REGION 36..114
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 51..65
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 943 AA; 109066 MW; B43744954CD9B75C CRC64;
MSDSQRHSKK RKFNEVSNDL KKDEELLFGY LTLQQSNNEY RSGDKEEGDY EHVDEAMEDD
NDVYEEDDRE RHGIVESEDD GEDLLENMEQ DYERKDELDR YEADGIDDED QEELDYNDRR
EVDRKLAEEA RYKQRNKSRI PGAFMDDENE FSEEDELQRQ IRLERMKQLR QDREMDYNQD
VNMQDVLDYE DVKGKLSAWV QRPEVTRWIR KVFAHFLRTF NDENQQNVHE QKINEMCSNN
KQSLEINFTH LSQKYPTLAI WLAEEPALIL PIFNIVAYDI TLELFPEYNK IHKVIYVRIG
GLPVEDKLRD LRQIHLSALI KIRGVVTKRT NIMPELTQMF FKCNCGDIKG PIFHNTYVEA
KSYLGQCVMC QANGPYTLDE TKTIYRNYQK MTLQETPGTV PPGRVPRQKE VYVLQDLVDS
ARPGDEVEVT GIFVNRFEYM ANLKHGFPVF TTIIEANNIK RQGDEEIYDL TDEDKQQIIQ
LSKSSNIGKK IIDSIAPSIY GHKYVKKALA LCMFGGEAKD IGGKHRIRGD INCLLLGDPG
TAKSQFLKYV EQVFHRCVYT TGKGASAVGL TAGVHKDPIS GEWTLEGGAL VLADKGVCLI
DEFDKMNDSD RTSIHEAMEQ QSISISKAGI VTSLQARCTV IAAANPIKGT YNNALNFVDN
VDLTDPILSR FDILTVIKDE VNEEADDALA TFVINSHIKS HPEVQRDLKI GAENEAEAEP
EEIERREATK EWLQRNLLDD NRILSQVNEE TITQDLLKKY IMYARKYVHP KLNEIDKDKV
TQFYADIRRE STIVGGIPIA VRHIESVLRM SEAHAKMHLR DYVRSDDIDQ AIEMLLESFL
QSQKLSVARQ LGKKFEQYKS KKSDPNQLLV HLLKKMVNDR AIYEKFIKGI EEVEKIEVKI
PIEQFEHEAR DFSNHNLTDF YKSGLFSKDY KVDGRFIQST LKL
//