ID S3CVE5_GLAL2 Unreviewed; 872 AA.
AC S3CVE5;
DT 18-SEP-2013, integrated into UniProtKB/TrEMBL.
DT 18-SEP-2013, sequence version 1.
DT 27-MAR-2024, entry version 60.
DE RecName: Full=DNA replication licensing factor MCM2 {ECO:0000256|ARBA:ARBA00018925};
DE EC=3.6.4.12 {ECO:0000256|ARBA:ARBA00012551};
GN ORFNames=GLAREA_03344 {ECO:0000313|EMBL:EPE30377.1};
OS Glarea lozoyensis (strain ATCC 20868 / MF5171).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC Helotiales; Helotiaceae; Glarea.
OX NCBI_TaxID=1116229 {ECO:0000313|EMBL:EPE30377.1, ECO:0000313|Proteomes:UP000016922};
RN [1] {ECO:0000313|EMBL:EPE30377.1, ECO:0000313|Proteomes:UP000016922}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 20868 / MF5171 {ECO:0000313|Proteomes:UP000016922};
RX PubMed=23688303; DOI=10.1186/1471-2164-14-339;
RA Chen L., Yue Q., Zhang X., Xiang M., Wang C., Li S., Che Y.,
RA Ortiz-Lopez F.J., Bills G.F., Liu X., An Z.;
RT "Genomics-driven discovery of the pneumocandin biosynthetic gene cluster in
RT the fungus Glarea lozoyensis.";
RL BMC Genomics 14:339-339(2013).
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
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DR EMBL; KE145363; EPE30377.1; -; Genomic_DNA.
DR RefSeq; XP_008081788.1; XM_008083597.1.
DR AlphaFoldDB; S3CVE5; -.
DR STRING; 1116229.S3CVE5; -.
DR GeneID; 19462399; -.
DR KEGG; glz:GLAREA_03344; -.
DR eggNOG; KOG0477; Eukaryota.
DR HOGENOM; CLU_000995_0_1_1; -.
DR OMA; TYERVTT; -.
DR OrthoDB; 5476523at2759; -.
DR Proteomes; UP000016922; 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 Reference proteome {ECO:0000313|Proteomes:UP000016922};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771}.
FT DOMAIN 485..691
FT /note="MCM"
FT /evidence="ECO:0000259|PROSITE:PS50051"
FT REGION 1..60
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 136..170
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 848..872
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..17
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 151..167
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 856..872
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 872 AA; 97731 MW; 2DA08D4A8076FB2D CRC64;
MSSPLRASMS SANRGPARNA RKRSREPEDA VMASSPAGDI RSSPPAYPIQ HGEDDDDDVE
EEIALDIDDV DELAEDEDGI DLFAGNYERD YRNVEDDAYD ARDIDDEGDY DELDAAARRQ
LEARLNRRDR ELARNRGQNA FLQDDEDDGN LDLTAQPRRR RHHYDEDEDE DMGDDIMEEE
LSLETLQDVK ASSLVEWVAQ HAVQRTIKRE FKAFLTEYTD EHGDSVYGNR IKTLGEVNAE
SLEVSYDHLS SSKAILAYFL ANAPGELLKL FDEVAMEVTL LHYPDYERIH SEIHVRISDL
PVHYTLRQLR QTHLNCLVRV SGVVTRRSGV FPQLKYVMFD CSKCHARLGP FQQESNVEVK
ITYCQNCQSR GPFNLNSEKT VYRNYQKLTL QESPGTVPAG RLPRHREVIL LWDLIDRAKP
GEEIEVTGVY RNNYDAQLNN KNGFPVFATI LEANNVVKSH DQLAGFRLTE EDEHQIRTLA
RDPQIIDKII HSMAPSIYGH TDIKTAVALS LFGGVAKERL GKLHIRGDIN VLLLGDPGTA
KSQVLKYVEK TAHRAVFATG QGASAVGLTA SVRKDPLTSE WTLEGGALVL ADRGTCLIDE
FDKMNDQDRT SIHEAMEQQT ISISKAGIVT TLQARCGIIA AANPIGGRYN STIPFSQNVE
LTEPILSRFD ILCVVRDTVD PAEDERLARF VVGSHGRSHP VTQATDENQN SMEMEHDSDL
RASAINGGEP KQEGEIPQEL LRKFILYARE RCSPKLYNID EEKVSKLFAD MRRESLATGA
YPITVRHLEA IMRISEAFCR MRLSDYVSSQ DVDRAIAVTI DSFVGSQKVS CKKALARAFA
KYTLARPGSG KKTGPGRNLE RTSQRAATAS MA
//
