ID A0A093VGR5_TALMA Unreviewed; 950 AA.
AC A0A093VGR5;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 27-MAR-2024, entry version 46.
DE RecName: Full=DNA replication licensing factor MCM2 {ECO:0000256|ARBA:ARBA00018925};
DE EC=3.6.4.12 {ECO:0000256|ARBA:ARBA00012551};
GN ORFNames=GQ26_0101850 {ECO:0000313|EMBL:KFX49169.1};
OS Talaromyces marneffei PM1.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Trichocomaceae; Talaromyces;
OC Talaromyces sect. Talaromyces.
OX NCBI_TaxID=1077442 {ECO:0000313|EMBL:KFX49169.1, ECO:0000313|Proteomes:UP000029285};
RN [1] {ECO:0000313|EMBL:KFX49169.1, ECO:0000313|Proteomes:UP000029285}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PM1 {ECO:0000313|EMBL:KFX49169.1,
RC ECO:0000313|Proteomes:UP000029285};
RX PubMed=25330172; DOI=10.1371/journal.pgen.1004662;
RA Yang E., Wang G., Cai J., Woo P.C., Lau S.K., Yuen K.-Y., Chow W.-N.,
RA Lin X.;
RT "Signature Gene Expression Reveals Novel Clues to the Molecular Mechanisms
RT of Dimorphic Transition in Penicillium marneffei.";
RL PLoS Genet. 10:e1004662-e1004662(2014).
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:KFX49169.1}.
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DR EMBL; JPOX01000010; KFX49169.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A093VGR5; -.
DR Proteomes; UP000029285; 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 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..60
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"
SQ SEQUENCE 950 AA; 107074 MW; F87F037B7849C3C6 CRC64;
MLGDRNSAAN RGLGNLGRRK RDRELDDETS SVAPPSSPPA SSPPMLPFDD ELDRDEEDEL
EGDIDDIEEL AEDEDGIDLF ADGFERDYNG DQQQYRGAYI NDDEEQEELD MATRRQLDAR
LNKRDRELAR RRRMPAAFLQ DDDEEANMDL SRQVRRRRHH YDEDRDDMDM QDDILEEELS
LEELGDVKSA NLTDWILQPQ VMRTIGREFK AFMTEFIDAS GRSVYGERIK TLGEVNSASL
EVSYDHLVAA KAVLGFFVAN EPTEVLKIFD QAALETTLYH YPHFADIQNE IHVRITDLPL
CYSLRELRQS HLNCLVRVNG VVTRRTGVFP QLKFVMFRCN KCEVTLGPFQ QEAAQEVKIS
FCQNCQSRGP FTMNSEKTVY RNYQKLTLQE SPGSVPAGRL PRQREVILLA DLIDIAKPGD
EVEVTGIYRN SYDAQLNNKN GFPVFATILE ANHVVKSHDQ MAGFHLTEQD IEQIRLLSRE
PDIVDKIVRS IAPSIYGHED VKTAVALSLF GGVRKEAQGK MAIRGDINVL LLGDPGTAKS
QVLKYVEKSA HRAVFATGQG ASAVGLTASV RRDPLTSEWT LEGGALVLAD RGTCLIDEFD
KMNDQDRTSI HEAMEQQTIS ISKAGIVTTL QARCAVIAAA NPIGGRYNAT LPFSQNVMLT
EPILSRFDIL CVVRDTVQPA EDERLAKFVV ESHSRANPAK PLRDATGRTI NKDGDFIDEE
GYRVDKKGNR LPLTLEEQQS RAEARRKAEE EKEGEIPQEL LRKYILYARE RCHPKLYQID
QDKVARLFAD MRRESLVTGA YPITVRHLEA ILRIAEAFCK MRLSEYCSSQ DIDRAIAVTV
ESFIGSQKVS CKKALSRAFA NLIGSGGVFG IIPSASWISH GVLDWKIYVG GLPVNLYGKL
EPLADAETVE LRVVGLFFWH GISEHNCMVL IWEPYVLGYN YRGKRVVLSV
//
