ID A0A318Z732_9EURO Unreviewed; 1026 AA.
AC A0A318Z732;
DT 10-OCT-2018, integrated into UniProtKB/TrEMBL.
DT 10-OCT-2018, sequence version 1.
DT 27-MAR-2024, entry version 25.
DE RecName: Full=DNA helicase {ECO:0000256|ARBA:ARBA00012551};
DE EC=3.6.4.12 {ECO:0000256|ARBA:ARBA00012551};
GN ORFNames=BP01DRAFT_324100 {ECO:0000313|EMBL:PYH43141.1};
OS Aspergillus saccharolyticus JOP 1030-1.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
OX NCBI_TaxID=1450539 {ECO:0000313|EMBL:PYH43141.1, ECO:0000313|Proteomes:UP000248349};
RN [1] {ECO:0000313|EMBL:PYH43141.1, ECO:0000313|Proteomes:UP000248349}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JOP 1030-1 {ECO:0000313|EMBL:PYH43141.1,
RC ECO:0000313|Proteomes:UP000248349};
RG DOE Joint Genome Institute;
RA Vesth T.C., Nybo J., Theobald S., Brandl J., Frisvad J.C., Nielsen K.F.,
RA Lyhne E.K., Kogle M.E., Kuo A., Riley R., Clum A., Nolan M., Lipzen A.,
RA Salamov A., Henrissat B., Wiebenga A., De Vries R.P., Grigoriev I.V.,
RA Mortensen U.H., Andersen M.R., Baker S.E.;
RT "The genomes of Aspergillus section Nigri reveals drivers in fungal
RT speciation.";
RL Submitted (DEC-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
CC -!- SIMILARITY: Belongs to the MCM family. {ECO:0000256|ARBA:ARBA00008010,
CC ECO:0000256|RuleBase:RU004070}.
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DR EMBL; KZ821246; PYH43141.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A318Z732; -.
DR STRING; 1450539.A0A318Z732; -.
DR OrthoDB; 5476523at2759; -.
DR Proteomes; UP000248349; 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:0003678; F:DNA helicase activity; IEA:InterPro.
DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR GO; GO:0006270; P:DNA replication initiation; IEA:InterPro.
DR GO; GO:0006279; P:premeiotic DNA replication; IEA:UniProt.
DR CDD; cd17755; MCM4; 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; IPR008047; MCM_4.
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:SF66; DNA REPLICATION LICENSING FACTOR MCM4; 1.
DR Pfam; PF00493; MCM; 1.
DR Pfam; PF21128; MCM4_WHD; 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; PR01660; MCMPROTEIN4.
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 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|RuleBase:RU004070};
KW DNA replication {ECO:0000256|ARBA:ARBA00022705};
KW DNA-binding {ECO:0000256|ARBA:ARBA00023125, ECO:0000256|RuleBase:RU004070};
KW Helicase {ECO:0000256|ARBA:ARBA00022806};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW ECO:0000256|RuleBase:RU004070}; Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW Reference proteome {ECO:0000313|Proteomes:UP000248349}.
FT DOMAIN 605..813
FT /note="MCM"
FT /evidence="ECO:0000259|PROSITE:PS50051"
FT REGION 1..216
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 337..369
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 16..48
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 66..81
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 121..163
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1026 AA; 113187 MW; AD5CD0EF72954C78 CRC64;
MSSPAANRRR GRLTRDSTIS SPARSSRSTR SQQHLQTSSP PPRDDQSQIT PRASRRLRGE
GPVPSSSPMF FQSSPMKANS SAESPDLRME EPSSPVRASS TMEDVETTPR GNAAVIRDSS
PIRYVSSSSP TRSLGRRAER SDIPSSSSGL FVSTRSVTDG NRGVSRRNDL HSGGFGSTPS
RRRRIFVDAN GVPTADAEPR SDATFSNIHP DTSEAEALGG SSTRVIWGTN ISIQDSMSAF
KNFLYNFAAK YRLWAEGASE EITRTMGKAA EEREYITMLN TMRQLGVTNL NLDAKNLKAY
PSTLKLWHQL HAYPQEIIPL MDQTVKDVMV ELAGKEMQRQ RSHNRHHQSQ SRDLSSAPAV
PSSDALMSDA GRTPQAEIQD LVQEVESNSY KVMPFGLDSA VNMRDLDPAD MDKLVSIKGL
VIRTTPIIPD MKEAFFRCQV CNHSVQVDID RGRIAEPAEC PRPICKAKNS MQLIHNRCAF
ADKQVIKLQE TPDSIPDGQT PHSVSLCVYD ELVDVCKAGD RVEVTGIFRC NPVRVNPRQR
TQKTLFKTYV DVLHVQKIDR KKLGIDASTV EQELSEQAAG DSEQVRKITA EEEEKIKRTA
TRPDIYELLS RSLAPSIYEM DDVKKGILLQ MFGGTNKTFE KGGNPRYRGD INVLLCGDPS
TSKSQLLRYV HKIAPRGVYT SGKGSSAVGL TAYVTRDPET RQMVLESGAL VLSDGGICCI
DEFDKMNEST RSVLHEVMEQ QTVSVAKAGI ITTLNARTSI LASANPIGSR YNPNLPVPQN
IDLPPTLLSR FDLVYLVLDR TDEQEDRRLA KHLVNMYLED KPENASTEEI LPIEFLTAYI
TYAKTRVHPV LTPAAGKALS DAYVNMRKLG DDIRSADRRI TATTRQLESM IRLSEAHARM
RLSTEVTADD VDEAVRLIRS AIKQAATDAR TGLIDMGLLT EGTSASERRN REAIKRGVLA
VVDELAGPTG GANWTNVFRV LNDQSSAAVD NAQFNDAVRA LETEGMVNVL GEGPRRTIRR
AAGALP
//
