ID C1GZP9_PARBA Unreviewed; 888 AA.
AC C1GZP9;
DT 26-MAY-2009, integrated into UniProtKB/TrEMBL.
DT 04-FEB-2015, sequence version 2.
DT 27-MAR-2024, entry version 93.
DE RecName: Full=DNA replication licensing factor MCM2 {ECO:0000256|ARBA:ARBA00018925};
DE EC=3.6.4.12 {ECO:0000256|ARBA:ARBA00012551};
GN ORFNames=PAAG_03993 {ECO:0000313|EMBL:EEH42072.2};
OS Paracoccidioides lutzii (strain ATCC MYA-826 / Pb01) (Paracoccidioides
OS brasiliensis).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Onygenales; Onygenales incertae sedis; Paracoccidioides.
OX NCBI_TaxID=502779 {ECO:0000313|EMBL:EEH42072.2, ECO:0000313|Proteomes:UP000002059};
RN [1] {ECO:0000313|EMBL:EEH42072.2, ECO:0000313|Proteomes:UP000002059}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC MYA-826 / Pb01 {ECO:0000313|Proteomes:UP000002059};
RX PubMed=22046142; DOI=10.1371/journal.pgen.1002345;
RA Desjardins C.A., Champion M.D., Holder J.W., Muszewska A., Goldberg J.,
RA Bailao A.M., Brigido M.M., Ferreira M.E., Garcia A.M., Grynberg M.,
RA Gujja S., Heiman D.I., Henn M.R., Kodira C.D., Leon-Narvaez H.,
RA Longo L.V.G., Ma L.-J., Malavazi I., Matsuo A.L., Morais F.V., Pereira M.,
RA Rodriguez-Brito S., Sakthikumar S., Salem-Izacc S.M., Sykes S.M.,
RA Teixeira M.M., Vallejo M.C., Walter M.E., Yandava C., Young S., Zeng Q.,
RA Zucker J., Felipe M.S., Goldman G.H., Haas B.J., McEwen J.G., Nino-Vega G.,
RA Puccia R., San-Blas G., Soares C.M., Birren B.W., Cuomo C.A.;
RT "Comparative genomic analysis of human fungal pathogens causing
RT paracoccidioidomycosis.";
RL PLoS Genet. 7:E1002345-E1002345(2011).
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
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DR EMBL; KN294000; EEH42072.2; -; Genomic_DNA.
DR RefSeq; XP_002794400.2; XM_002794354.2.
DR AlphaFoldDB; C1GZP9; -.
DR STRING; 502779.C1GZP9; -.
DR GeneID; 9097509; -.
DR KEGG; pbl:PAAG_03993; -.
DR VEuPathDB; FungiDB:PAAG_03993; -.
DR eggNOG; KOG0477; Eukaryota.
DR HOGENOM; CLU_000995_0_0_1; -.
DR OMA; TYERVTT; -.
DR OrthoDB; 5476523at2759; -.
DR Proteomes; UP000002059; Partially assembled 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:UP000002059};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771}.
FT DOMAIN 492..698
FT /note="MCM"
FT /evidence="ECO:0000259|PROSITE:PS50051"
FT REGION 1..67
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 93..117
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 702..745
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 860..888
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..19
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 39..53
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 93..108
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 866..880
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 888 AA; 99295 MW; CF662E7045F664EA CRC64;
MSVMYSSPLH PSSSAANRGL GKLTRRKRSR EPDDDNSSAL PPSSPPPSSP PMLPLEDDDA
ENDLDEEADF IGDIDDADEM AEEEDGIDLF ADTFERDYRP RGPEAYEGDD IDDTGEHEEL
DLATRRQLEA RLNRRDRELA RRRRMPAAFL QDDEDDGNVD LTKQPRRRRH HYDEDADEMD
MDIMDEEMTL EALAEIKAAN VTEWVAQPSV HRSIYREFKS FLTEFTDKDG TSVYGTLIRN
LGEINSESLE VSYAHLSDSK AIVAYFLANA PAEVLKIFDQ AAMEVTLLHY PDYHRIHNDI
HVRITNLPVM YTLRQLRQSH LNCLVRVSGV VTRRTGVYPQ LKYVMFNCTK CGITLGPFQQ
ESNAEIKISF CQNCQSRGPF TLNSEKTEYR NYQKMTLQES PGTVPAGRLP RHREVILLAD
LIDSAKPGDE VEITGIYRNH YDGQLNNKNG FPVFATILEA NHLVKSHDQL AGFHLTEEDE
RKIRALSRDP QIVDRIVRSI APSIYGHEDI KTAVALSLFG GVSKVAQGKM SIRGDINVLL
LGDPGTAKSQ VLKYVEKTAH RAVFATGQGA SAVGLTASVR RDPLTSEWTL EGGALVLADR
GTCLIDEFDK MNDQDRTSIH EAMEQQTISI SKAGIVTTLQ ARCAIVAAAN PIGGRYNGTI
PFSHNVELTE PILSRFDILC VVRDTVSPEE DELLAKFVVD SHSKANPPRP QTDEYGNPVP
RETSGDDEDE EMGESHPVNG ESGGAEQIPQ ELLRKYILYA RERCRPKLYQ IDQDKVARLF
ADMRRESLAT GAYPITVRHL EAIMRIAEAF CKMRLSDYCT AQDIDRAIAV TVDSFISSQK
VSCKKALSRA FAKYTLARPG TQKRRGPTVG ANSGLSSGQR NGMDRRGL
//
