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Database: UniProt
Entry: N1JDA0_BLUG1
LinkDB: N1JDA0_BLUG1
Original site: N1JDA0_BLUG1 
ID   N1JDA0_BLUG1            Unreviewed;      1014 AA.
AC   N1JDA0;
DT   26-JUN-2013, integrated into UniProtKB/TrEMBL.
DT   26-JUN-2013, sequence version 1.
DT   27-MAR-2024, entry version 63.
DE   RecName: Full=DNA helicase {ECO:0000256|ARBA:ARBA00012551};
DE            EC=3.6.4.12 {ECO:0000256|ARBA:ARBA00012551};
GN   ORFNames=BGHDH14_bgh00746 {ECO:0000313|EMBL:CCU75897.1};
OS   Blumeria graminis f. sp. hordei (strain DH14) (Barley powdery mildew)
OS   (Oidium monilioides f. sp. hordei).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC   Erysiphales; Erysiphaceae; Blumeria; Blumeria hordei.
OX   NCBI_TaxID=546991 {ECO:0000313|EMBL:CCU75897.1, ECO:0000313|Proteomes:UP000015441};
RN   [1] {ECO:0000313|EMBL:CCU75897.1, ECO:0000313|Proteomes:UP000015441}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DH14 {ECO:0000313|EMBL:CCU75897.1};
RX   PubMed=21148392; DOI=10.1126/science.1194573;
RA   Spanu P.D., Abbott J.C., Amselem J., Burgis T.A., Soanes D.M., Stueber K.,
RA   Ver Loren van Themaat E., Brown J.K.M., Butcher S.A., Gurr S.J.,
RA   Lebrun M.-H., Ridout C.J., Schulze-Lefert P., Talbot N.J., Ahmadinejad N.,
RA   Ametz C., Barton G.R., Benjdia M., Bidzinski P., Bindschedler L.V.,
RA   Both M., Brewer M.T., Cadle-Davidson L., Cadle-Davidson M.M., Collemare J.,
RA   Cramer R., Frenkel O., Godfrey D., Harriman J., Hoede C., King B.C.,
RA   Klages S., Kleemann J., Knoll D., Koti P.S., Kreplak J., Lopez-Ruiz F.J.,
RA   Lu X., Maekawa T., Mahanil S., Micali C., Milgroom M.G., Montana G.,
RA   Noir S., O'Connell R.J., Oberhaensli S., Parlange F., Pedersen C.,
RA   Quesneville H., Reinhardt R., Rott M., Sacristan S., Schmidt S.M.,
RA   Schoen M., Skamnioti P., Sommer H., Stephens A., Takahara H.,
RA   Thordal-Christensen H., Vigouroux M., Wessling R., Wicker T., Panstruga R.;
RT   "Genome expansion and gene loss in powdery mildew fungi reveal tradeoffs in
RT   extreme parasitism.";
RL   Science 330:1543-1546(2010).
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
CC   -!- SIMILARITY: Belongs to the MCM family. {ECO:0000256|ARBA:ARBA00008010,
CC       ECO:0000256|RuleBase:RU004070}.
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:CCU75897.1}.
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DR   EMBL; CAUH01001849; CCU75897.1; -; Genomic_DNA.
DR   AlphaFoldDB; N1JDA0; -.
DR   STRING; 546991.N1JDA0; -.
DR   eggNOG; KOG0478; Eukaryota.
DR   HOGENOM; CLU_000995_7_0_1; -.
DR   InParanoid; N1JDA0; -.
DR   OrthoDB; 5476523at2759; -.
DR   Proteomes; UP000015441; 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:0051301; P:cell division; IEA:UniProtKB-KW.
DR   GO; GO:0006270; P:DNA replication initiation; IEA:InterPro.
DR   GO; GO:0006279; P:premeiotic DNA replication; IEA:UniProt.
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   Cell cycle {ECO:0000313|EMBL:CCU75897.1};
KW   Cell division {ECO:0000313|EMBL:CCU75897.1};
KW   Coiled coil {ECO:0000256|SAM:Coils};
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:UP000015441}.
FT   DOMAIN          615..809
FT                   /note="MCM"
FT                   /evidence="ECO:0000259|PROSITE:PS50051"
FT   REGION          1..41
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          65..182
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          855..882
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COMPBIAS        91..137
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        150..164
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1014 AA;  112776 MW;  802577DA5E978034 CRC64;
     MSSPPNGQPT PFQGTHGHLG NTAARRTLQR NSSRITPSSP VDAAAAQLQT EAASSQRYVD
     RDTNAFRSSS PVPYPSSPTP AHGRNIERDI SSPLRQMTTS QIQYDDNSTP RASSSRFARD
     SSPIRYAPSS SPGLNSYRRS VPPDIRSDSS GLFIRSSRGE NAGPMSSLNI RRRGDINSDS
     INTPRARRRI FMDESGNVTR DIPTEGSEAP TFSNLDPTTS DAAAMGGESQ LCIWGTNVSI
     NDTLSTFKSF LRGFTKKYRM WADGMSEEET SQESDAETKE YIETMKNMLT LGVTSLNLDF
     RNLKAYPKTQ KLWQQAQDYP QDVVTLMDQG IKDVMYELAE EETLRKRQLQ NRAIISQRNL
     KASSEPLMLS SERDEFDTQE RSQEVSEDLD LCQEVQKRSY RVRPFGLEKT INMRDLNPSD
     VDKIIAIKGL VIRTTPIIPD MKDAFFRCQV CNHTVKVDID RGRIAEPTKC PRPICDSPNS
     MQIVHNRSEF MDKQVIKFQE TPDSVPAGQT PHSITMCAYD ELVDFCKAGD RVEITGIFKA
     SPVRVNPRQR TLKNVYKTYI DVLHIQKVDK KRMGIDVSTV EQDLSEQTAT NIEEARRVSD
     EEKEKILQTA MRPDIYELLS RSLAPSIFEM DDVKKGILLQ LFGGTNKTFE KGGSPKYRGD
     INILLCGDPS TSKSQLLQYV HKIAPRGLYT SGKGSSAVGL TAYVTRDPET RQLVLESGAL
     VLSDGGVCCI DEFDKMSDAT RSVLHEVMEQ QTVSIAKAGI ITTLNARTSI LASANPIGSK
     YNPNLPIELM KQTTGRLARH LLSMYLDDKP QSASGGMEIL PVEFLTSYIS YARHTCQPRI
     SAEAAEELVT AYVEMRKLGE DIRAAERRIT ATTRQLESMI RLAEAHAKMR LSDTVGRDDV
     SEAVRLIKSA LKQAATDART GLIDMSLLTE GTSASERRRK ADLKRATLAL LDEMTGQGQS
     ARYIEVIKRL GEQSSMPIES SEFAEVVRLL EQEGLAMVVG EGVRKAIRRL TGAA
//
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