ID A0A1W5D6N2_9LECA Unreviewed; 870 AA.
AC A0A1W5D6N2;
DT 07-JUN-2017, integrated into UniProtKB/TrEMBL.
DT 07-JUN-2017, sequence version 1.
DT 27-MAR-2024, entry version 34.
DE RecName: Full=DNA replication licensing factor MCM2 {ECO:0000256|ARBA:ARBA00018925};
DE EC=3.6.4.12 {ECO:0000256|ARBA:ARBA00012551};
OS Lasallia pustulata.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Lecanoromycetes;
OC OSLEUM clade; Umbilicariomycetidae; Umbilicariales; Umbilicariaceae;
OC Lasallia.
OX NCBI_TaxID=136370 {ECO:0000313|EMBL:SLM38715.1, ECO:0000313|Proteomes:UP000192927};
RN [1] {ECO:0000313|Proteomes:UP000192927}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Sharma R., Thines M.;
RL Submitted (MAR-2017) to the EMBL/GenBank/DDBJ databases.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
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DR EMBL; FWEW01002698; SLM38715.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1W5D6N2; -.
DR OrthoDB; 5476523at2759; -.
DR Proteomes; UP000192927; 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 483..689
FT /note="MCM"
FT /evidence="ECO:0000259|PROSITE:PS50051"
FT REGION 1..56
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 132..171
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 851..870
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 29..43
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 148..165
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 870 AA; 97478 MW; 150B38E0ED761CF3 CRC64;
MSAANRGVSN PTRRKRSREP DDDIPSSSAA PPSSPPPSSP PVLPRDNEED ILDDPENELI
RDIDDADEMA EDEDGIDLFA DNFERDYKAR ENDAYAGADI DDEGDYDDLD LATRRQLEAR
LNKRDRELER RRRMPAAFLQ DEDEDGEMDL TRQPRRRRHH YDEEQEDEDM ADDVMEEELS
LETLQDVKAS SLTEWVAQPA VYRTISREFK SFLTEYTDEH GTSVYGTRVR TLGEINAESL
EVSYDHLSSS KAILAYFLAN APAEVLKIFD QVAMDVTLLH YPDYARIHSE IHVRISDLPV
HYTLRQLRQT HLNCLVRVSG VVTRRSGVFP QLKYVRFDCQ KCNITLGPFQ QESNVEVRIS
YCQNCQSRGP FTLNSEKTVY RNYQKLTLQE SPGTVPAGRL PRHREVILLW DVIDSAKPGE
EIEITGIYRN SYSAQLNNRN GFPVFATILE ANHVIKSHDQ LAGFRLTEED ERNIRALSRD
PQIVDKIVAS IAPSIYGHTD IKTAVALSLF GGVSKLAQGK HAIRGDINLL LLGDPGTAKS
QILKYIEKTA HRAVFATGQG ASAVGLTASV RRDPLTSEWG LEGGALVLAD RGVCLIDEFD
KMNDQDRTSI HEAMEQQTIS ISKAGIVTTL HARCAIVAAA NPIGGRYNGT IPFSQNVELT
EPILSRFDIL CVVRDTVDPA EDERLANFVV ASHGRAHPSA QSTDANQNAM EMRHGEDVRR
EQRNGGEQLG EGGIPQELLR KYILYARERC RPKLYQIDQD KVARLFADMR RESLATGAYP
ITVRHLEAIM RISEAFCKMR LSEYCTSVDI DRAIAVTVDS FVGSQKVSCK KALARAFAKY
TLARPGSQKR AVQNGRGVGR GARRSMAVGA
//
