ID A0A395S577_9HYPO Unreviewed; 850 AA.
AC A0A395S577;
DT 05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT 05-DEC-2018, sequence version 1.
DT 27-MAR-2024, entry version 27.
DE RecName: Full=DNA replication licensing factor MCM2 {ECO:0000256|ARBA:ARBA00018925};
DE EC=3.6.4.12 {ECO:0000256|ARBA:ARBA00012551};
GN ORFNames=FLONG3_8454 {ECO:0000313|EMBL:RGP67528.1};
OS Fusarium longipes.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Nectriaceae; Fusarium.
OX NCBI_TaxID=694270 {ECO:0000313|EMBL:RGP67528.1, ECO:0000313|Proteomes:UP000266234};
RN [1] {ECO:0000313|EMBL:RGP67528.1, ECO:0000313|Proteomes:UP000266234}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NRRL 20695 {ECO:0000313|EMBL:RGP67528.1,
RC ECO:0000313|Proteomes:UP000266234};
RX PubMed=29649280; DOI=10.1371/journal.ppat.1006946;
RA Proctor R.H., McCormick S.P., Kim H.S., Cardoza R.E., Stanley A.M.,
RA Lindo L., Kelly A., Brown D.W., Lee T., Vaughan M.M., Alexander N.J.,
RA Busman M., Gutierrez S.;
RT "Evolution of structural diversity of trichothecenes, a family of toxins
RT produced by plant pathogenic and entomopathogenic fungi.";
RL PLoS Pathog. 14:e1006946-e1006946(2018).
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:RGP67528.1}.
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DR EMBL; PXOG01000202; RGP67528.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A395S577; -.
DR STRING; 694270.A0A395S577; -.
DR Proteomes; UP000266234; 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:UP000266234};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771}.
FT DOMAIN 481..687
FT /note="MCM"
FT /evidence="ECO:0000259|PROSITE:PS50051"
FT REGION 1..53
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 144..163
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 694..724
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 147..163
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 694..712
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 850 AA; 95232 MW; 207D2033C2951388 CRC64;
MSSPLHPSSA RPNRKRSRTG GSDGPSPGGM AESPMPSSPP EFNMAHGVED DDDIEEDVLI
EDDIDVIDEM AEDEVDLFRE GYENDYRDLE NDRYEVDGVD DEEYEKMGED ERRRVDRALD
QRDRAIARQQ GRRLPTALGL DEDMDDIDLS AQPRRRRHHY DEDPDDIMDT DIMAEELSLE
ALADVKASNL TEWVSLPAVQ RTIRREFKAF LTSYTDASGY SVYGNRIRTL GEVNAETLEV
SYDHLSESKA ILAYFLANAP AEMLKLFDEV AMDVVLLHYP DYERIHSEIH IRIFDLPVHY
TLRQLRQSHL NCLVRVSGVV TRRSGVFPQL KYVKFDCTKC GVTLGPFQQE SNVEVKITYC
QSCQSRGPFT LNSEKTVYRN YQKLTLQESP GTVPAGRLPR SREVILLWDL IDKAKPGEEI
EVTGIYRNNY DAQLNNRNGF PVFATILEAN NVIKSHDQLA GFRMTEEDEH NIRKLSRDPN
IVDKIINSIA PSIYGHTDIK TAVALSLFGG VAKTTKGAHH LRGDINVLLL GDPGTAKSQV
LKYAEKTAHR AVFATGQGAS AVGLTASVRR DPLTSEWTLE GGALVLADRG TCLIDEFDKM
NDQDRTSIHE AMEQQTISIS KAGIVTTLQA RCGVIAAANP IGGRYNSTAP FSANVELTEP
ILSRFDILCV VRDTVEPAED ERLARFIVGS HSRSHPLSQT AQDSMAVEHD TQAETQGSER
KPEGEIPQEL LRKYILYARE HCSPKLYHID EDKIARLFAD MRRESLATGA YPITVRHLEA
IIRISEAFCR MRLSEYCSAQ DIDRAIAVTV DSFVGSQKVS CKKALARAFA KYTLARPGSQ
KKNSQARGGR
//
