ID A0A1J7INN3_9PEZI Unreviewed; 870 AA.
AC A0A1J7INN3;
DT 15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT 15-FEB-2017, sequence version 1.
DT 27-MAR-2024, entry version 35.
DE RecName: Full=DNA replication licensing factor MCM2 {ECO:0000256|ARBA:ARBA00018925};
DE EC=3.6.4.12 {ECO:0000256|ARBA:ARBA00012551};
GN ORFNames=CONLIGDRAFT_618123 {ECO:0000313|EMBL:OIW28989.1};
OS Coniochaeta ligniaria NRRL 30616.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Sordariomycetidae; Coniochaetales; Coniochaetaceae; Coniochaeta.
OX NCBI_TaxID=1408157 {ECO:0000313|EMBL:OIW28989.1, ECO:0000313|Proteomes:UP000182658};
RN [1] {ECO:0000313|EMBL:OIW28989.1, ECO:0000313|Proteomes:UP000182658}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NRRL 30616 {ECO:0000313|EMBL:OIW28989.1,
RC ECO:0000313|Proteomes:UP000182658};
RG DOE Joint Genome Institute;
RA Jimenez D.J., Hector R.E., Riley R., Sun H., Grigoriev I.V.,
RA Van Elsas J.D., Nichols N.N.;
RT "Draft genome sequence of Coniochaeta ligniaria NRRL30616, a
RT lignocellulolytic fungus for bioabatement of inhibitors in plant biomass
RT hydrolysates.";
RL Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
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DR EMBL; KV875098; OIW28989.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1J7INN3; -.
DR STRING; 1408157.A0A1J7INN3; -.
DR InParanoid; A0A1J7INN3; -.
DR OrthoDB; 5476523at2759; -.
DR Proteomes; UP000182658; 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:UP000182658};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771}.
FT DOMAIN 489..695
FT /note="MCM"
FT /evidence="ECO:0000259|PROSITE:PS50051"
FT REGION 1..78
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 146..171
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 700..735
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..18
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 57..78
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 155..171
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 870 AA; 97531 MW; 9D3EF191AE4BB1AA CRC64;
MSSPLRSNMS SANRGATPRA NRKRSRTGGD DGASSVGIAS SPMPSSPPAF PISHGGDDED
DIEEEVEIQD DDIDDIDEMA EDDVDLFREG FERDYREKED DTYEGIDLDD EEYDQMNLGE
RRRLEAQLAR RDREVARRQR IPAAFLPGED EDGDLDLTAQ PRRRRHHYDE DPDEEMDANI
MDEELSLEAL QDVKASSLTE WVSQPPVQRT IKREFKAFLT EYTDESGSSV YGNRIRTLGE
INAESLEVSY DHLSTSKAIL AYFLANAPAE MLKLFDQVAM EVVLLHYPDY ERIHAEIHVR
IFDLPVHYTL RQLRQSHLNC LVRVSGVVTR RTGVFPQLKY VKFDCTKCGV TLGPFQQESN
VEVKITYCQS CQSRGPFTLN SEKTVYRNYQ KLTLQESPGT VPAGRLPRHR EVILLWDLID
KAKPGEEIEV TGIYRNNYDA QLNNRNGFPV FATILEANNV IKSHDQLAGF RLTEEDEHEI
RKLSKDPQIV DKIINSIAPS IYGHTDIKTA VALSLFGGVA KTTKGAHHIR GDINVLLLGD
PGTAKSQVLK YVEKTAHRAV FATGQGASAV GLTASVRRDP LTSEWTLEGG ALVLADKGTC
LIDEFDKMND QDRTSIHEAM EQQTISISKA GIVTTLQARC GIIAAANPIG GRYNSTIPFS
ANVELTEPIL SRFDILCVVR DTVEPEEDER LARFIVGSHS RSHPLSQGQG EESMDVEYES
QRASNTLVDE RSRKKEGEIP QELLRKYILY ARERCSPKLY HMDEDKVARL FADMRKESLA
TGAYPITVRH LEAIIRISES FCRMRLSEYC SAQDMDRAIA VTVDSFVGSQ KVSCKKALAR
AFAKYTLKRP GQDQRRGAAA RGGRAGTVAA
//
