ID A0A1V6R5K0_9EURO Unreviewed; 896 AA.
AC A0A1V6R5K0;
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};
GN ORFNames=PENSOL_c015G04325 {ECO:0000313|EMBL:OQD96591.1};
OS Penicillium solitum.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Penicillium.
OX NCBI_TaxID=60172 {ECO:0000313|EMBL:OQD96591.1, ECO:0000313|Proteomes:UP000191612};
RN [1] {ECO:0000313|Proteomes:UP000191612}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=IBT 29525 {ECO:0000313|Proteomes:UP000191612};
RX PubMed=28368369; DOI=10.1038/nmicrobiol.2017.44;
RA Nielsen J.C., Grijseels S., Prigent S., Ji B., Dainat J., Nielsen K.F.,
RA Frisvad J.C., Workman M., Nielsen J.;
RT "Global analysis of biosynthetic gene clusters reveals vast potential of
RT secondary metabolite production in Penicillium species.";
RL Nat. Microbiol. 2:17044-17044(2017).
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:OQD96591.1}.
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DR EMBL; MDYO01000015; OQD96591.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1V6R5K0; -.
DR STRING; 60172.A0A1V6R5K0; -.
DR OrthoDB; 5476523at2759; -.
DR Proteomes; UP000191612; 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:UP000191612};
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 1..63
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 869..896
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 15..29
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 32..46
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 896 AA; 100773 MW; 88A0F2DAA27DFC83 CRC64;
MDPLRASDSA ANRGRGANTR KRDREDDMSS PAPLPPSSPT ALGSSPPPIP FDMGDEDEDE
DRGLVQDIDD IDELAEDEDG IDLFGDNFER DYRDAAQDRY ENEAYIDDDE DHDEIDAGTR
RQLDARLNQR DRELARRRRM PAAFLQDDDD MELDLSRQPR RRRHHYDEDR EDIDMADEGM
EELSLEELAD VKAANITDWV TQPQVLRSIY REFKAFLTEF IDPTGQSVYG NRIKTLGEVN
SASLEVSYAH LSETKAALSY FLANEPTEVL KVFDQVALDV TLFHYPQYHD IHNEIHVRIT
DVPIIYTLRQ LRQSHLNCLI RVGGVVTRRT GVFPQLKYVM FLCQKCGITL GPFQQEASAE
VKISFCQNCQ SRGPFTVNSE KTVYRNYQKL TLQESPGSVP AGRLPRQREV VLLADLIDTA
KPGDEIEITG VYRNSYDAQL NNKNGFPVFA TVIEANHVVK AHDQLAGFNL TEEDEREIRA
LSRDPDIVDK IVRSMAPSIY GHQDVKTAVA LSLFGGVSKQ AQGKMNIRGD INVLLLGDPG
TAKSQVLKFV EKTAHRAVFA TGQGASAVGL TASVRRDPLT SEWTLEGGAL VLADRGTCLI
DEFDKMNDQD RTSIHEAMEQ QTISISKAGI VTTLQARCAV VSAANPKGGR YNSSIPFSEN
VDLTDPILSR FDILCVVRDL VDPAEDERLA NFVIESHHRS NPARPLRNEK GDLVDTDGHL
IDNEGYRINR DGQRLPPSQE EIAKRAAEKQ RAEEEKEGEI PQELLRKYIM YARERCHPKL
YQIDQDKVAR LFADMRRESL ATGAYPITVR HLEAIMRIAE SFCKMRLSEY CSSLDIDRAI
AVTVDSFIGS QKVSCKKALS RAFAKYTLSR PKPQSKRRAG IPVSNPHLPR AQSTAH
//
