ID Q2UC60_ASPOR Unreviewed; 893 AA.
AC Q2UC60;
DT 24-JAN-2006, integrated into UniProtKB/TrEMBL.
DT 24-JAN-2006, sequence version 1.
DT 27-MAR-2024, entry version 128.
DE RecName: Full=DNA replication licensing factor MCM2 {ECO:0000256|ARBA:ARBA00018925};
DE EC=3.6.4.12 {ECO:0000256|ARBA:ARBA00012551};
GN ORFNames=AO090012000727 {ECO:0000313|EMBL:BAE60855.1};
OS Aspergillus oryzae (strain ATCC 42149 / RIB 40) (Yellow koji mold).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Circumdati.
OX NCBI_TaxID=510516 {ECO:0000313|EMBL:BAE60855.1, ECO:0000313|Proteomes:UP000006564};
RN [1] {ECO:0000313|EMBL:BAE60855.1, ECO:0000313|Proteomes:UP000006564}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 42149 / RIB 40 {ECO:0000313|Proteomes:UP000006564};
RX PubMed=16372010; DOI=10.1038/nature04300;
RA Machida M., Asai K., Sano M., Tanaka T., Kumagai T., Terai G., Kusumoto K.,
RA Arima T., Akita O., Kashiwagi Y., Abe K., Gomi K., Horiuchi H.,
RA Kitamoto K., Kobayashi T., Takeuchi M., Denning D.W., Galagan J.E.,
RA Nierman W.C., Yu J., Archer D.B., Bennett J.W., Bhatnagar D.,
RA Cleveland T.E., Fedorova N.D., Gotoh O., Horikawa H., Hosoyama A.,
RA Ichinomiya M., Igarashi R., Iwashita K., Juvvadi P.R., Kato M., Kato Y.,
RA Kin T., Kokubun A., Maeda H., Maeyama N., Maruyama J., Nagasaki H.,
RA Nakajima T., Oda K., Okada K., Paulsen I., Sakamoto K., Sawano T.,
RA Takahashi M., Takase K., Terabayashi Y., Wortman J., Yamada O.,
RA Yamagata Y., Anazawa H., Hata Y., Koide Y., Komori T., Koyama Y.,
RA Minetoki T., Suharnan S., Tanaka A., Isono K., Kuhara S., Ogasawara N.,
RA Kikuchi H.;
RT "Genome sequencing and analysis of Aspergillus oryzae.";
RL Nature 438:1157-1161(2005).
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
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DR EMBL; AP007161; BAE60855.1; -; Genomic_DNA.
DR RefSeq; XP_001727694.1; XM_001727642.1.
DR AlphaFoldDB; Q2UC60; -.
DR STRING; 510516.Q2UC60; -.
DR EnsemblFungi; BAE60855; BAE60855; AO090012000727.
DR GeneID; 5988168; -.
DR KEGG; aor:AO090012000727; -.
DR VEuPathDB; FungiDB:AO090012000727; -.
DR HOGENOM; CLU_000995_0_0_1; -.
DR OMA; TYERVTT; -.
DR OrthoDB; 5476523at2759; -.
DR Proteomes; UP000006564; Chromosome 4.
DR GO; GO:0000785; C:chromatin; IEA:EnsemblFungi.
DR GO; GO:0140445; C:chromosome, telomeric repeat region; IEA:EnsemblFungi.
DR GO; GO:0071162; C:CMG complex; IEA:EnsemblFungi.
DR GO; GO:0005737; C:cytoplasm; IEA:EnsemblFungi.
DR GO; GO:0042555; C:MCM complex; IEA:EnsemblFungi.
DR GO; GO:0005656; C:nuclear pre-replicative complex; IEA:EnsemblFungi.
DR GO; GO:0031298; C:replication fork protection complex; IEA:EnsemblFungi.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0003682; F:chromatin binding; IEA:EnsemblFungi.
DR GO; GO:0003688; F:DNA replication origin binding; IEA:EnsemblFungi.
DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0003697; F:single-stranded DNA binding; IEA:EnsemblFungi.
DR GO; GO:0017116; F:single-stranded DNA helicase activity; IEA:EnsemblFungi.
DR GO; GO:0006271; P:DNA strand elongation involved in DNA replication; IEA:EnsemblFungi.
DR GO; GO:0006268; P:DNA unwinding involved in DNA replication; IEA:EnsemblFungi.
DR GO; GO:0000727; P:double-strand break repair via break-induced replication; IEA:EnsemblFungi.
DR GO; GO:1902975; P:mitotic DNA replication initiation; IEA:EnsemblFungi.
DR GO; GO:0006267; P:pre-replicative complex assembly involved in nuclear cell cycle DNA replication; IEA:EnsemblFungi.
DR GO; GO:0006279; P:premeiotic DNA replication; IEA:EnsemblFungi.
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:UP000006564};
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..59
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 871..893
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..15
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 18..32
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 35..49
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 893 AA; 100700 MW; E2587F35CD9C3C80 CRC64;
MSSPLRPSYT AANRGLGNLN RRKRDREPDD ETSSIAPPSS PPPSSPPMLP YEDDERDEEA
ELLEDIDDLD EMAEEGEGID LFGDSFENDY TSRENDRYQG ADIDDEEQEE LDIGTRRQLE
ARLNRRDREL ARRSRMPRAF LQDDDDQNID LTRQPRRRRH HYDEDREDID MGEGDMEELS
LEEMMDIKAP NVTDWVLQPQ VLRSIYREFK AFLTEFTDDS GASVYGNKIK TLGEVNSASL
EVSYDHLSST RAVLAYFVAN EPTEVLKVFD QVALDVTLFH YPQYHDIHNE IHVRIIDLPT
VSTLRQLRQS HLNSLVRVTG VVTRRSGVFP QLKYIMFVCG KCNITLGPFQ QEASQEVKIS
YCQNCQSKGP FTVNSEKTVY RNYQKMTLQE SPGSVPAGRL PRQREVILLA DLIDSAKPGD
EVEVTGIYRN SYDAQLNNKN GFPVFATIIE ANHVIKSHDQ LAGFHLTEED EREIRALSRD
PEIVDKIIRS IAPSIYGHQD VKTAIALSLF GGVSKQAQGK MSIRGDINVL LLGDPGTAKS
QVLKYVEKTA HRAVFATGQG ASAVGLTASV RRDPLTSEWT LEGGALVLAD RGTCLIDEFD
KMNDQDRTSI HEAMEQQTIS ISKAGIVTTL QARCAVVAAA NPIGGRYNST APFNANVELT
EPILSRFDIL CVVRDLVDPA EDERLANFVV ESHHRANPAR PLRDEEGNLI DSDGNRIDEE
GYRLDREGNR LPFTPEEIAA REAANRKIEE EKEGEIPQEL LRKYILYARE RCHPKLYQID
QDKIARLFAD MRRESLATGA YPITVRHLEA IMRIAESFCK MRLSEYCSSQ DIDRAIAVTV
DSFIGSQKVS CKKALSRAFA KYILSRPKPQ SRRKAGIAAP NPYVPKATAP RAY
//
