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DNA helicase (EC 3.6.4.12)

 A0A0L0NTZ1_CANAR        Unreviewed;       786 AA.
A0A0L0NTZ1;
11-NOV-2015, integrated into UniProtKB/TrEMBL.
11-NOV-2015, sequence version 1.
07-NOV-2018, entry version 27.
RecName: Full=DNA replication licensing factor MCM7 {ECO:0000256|RuleBase:RU365012};
EC=3.6.4.12 {ECO:0000256|RuleBase:RU365012};
Name=MCM7 {ECO:0000256|RuleBase:RU365012};
ORFNames=QG37_06030 {ECO:0000313|EMBL:KND97631.1};
Candida auris (Yeast).
Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina;
Saccharomycetes; Saccharomycetales; Metschnikowiaceae; Clavispora;
Clavispora/Candida clade.
NCBI_TaxID=498019 {ECO:0000313|EMBL:KND97631.1, ECO:0000313|Proteomes:UP000037122};
[1] {ECO:0000313|Proteomes:UP000037122}
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=6684 {ECO:0000313|Proteomes:UP000037122};
PubMed=26346253; DOI=10.1186/s12864-015-1863-z;
Chatterjee S., Alampalli S.V., Nageshan R.K., Chettiar S.T., Joshi S.,
Tatu U.S.;
"Draft genome of a commonly misdiagnosed multidrug resistant pathogen
Candida auris.";
BMC Genomics 16:686-686(2015).
-!- FUNCTION: Acts as component of the mcm2-7 complex (mcm complex)
which is the putative replicative helicase essential for 'once per
cell cycle' DNA replication initiation and elongation in
eukaryotic cells. The active ATPase sites in the mcm2-7 ring are
formed through the interaction surfaces of two neighboring
subunits such that a critical structure of a conserved arginine
finger motif is provided in trans relative to the ATP-binding site
of the Walker A box of the adjacent subunit. The six ATPase active
sites, however, are likely to contribute differentially to the
complex helicase activity. {ECO:0000256|RuleBase:RU365012}.
-!- CATALYTIC ACTIVITY: ATP + H(2)O = ADP + phosphate.
{ECO:0000256|RuleBase:RU365012, ECO:0000256|SAAS:SAAS00536515}.
-!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|RuleBase:RU365012,
ECO:0000256|SAAS:SAAS00536536}.
-!- SIMILARITY: Belongs to the MCM family.
{ECO:0000256|RuleBase:RU004070}.
-!- CAUTION: The sequence shown here is derived from an
EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is
preliminary data. {ECO:0000313|EMBL:KND97631.1}.
-----------------------------------------------------------------------
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EMBL; LGST01000041; KND97631.1; -; Genomic_DNA.
RefSeq; XP_018167355.1; XM_018314937.1.
EnsemblFungi; KND97631; KND97631; QG37_06030.
GeneID; 28879722; -.
KEGG; caur:QG37_06030; -.
KO; K02210; -.
Proteomes; UP000037122; Unassembled WGS sequence.
GO; GO:0042555; C:MCM complex; IEA:InterPro.
GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
GO; GO:0003678; F:DNA helicase activity; IEA:InterPro.
GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
GO; GO:0006270; P:DNA replication initiation; IEA:InterPro.
InterPro; IPR003593; AAA+_ATPase.
InterPro; IPR031327; MCM.
InterPro; IPR008050; MCM7.
InterPro; IPR018525; MCM_CS.
InterPro; IPR001208; MCM_dom.
InterPro; IPR027925; MCM_N.
InterPro; IPR033762; MCM_OB.
InterPro; IPR012340; NA-bd_OB-fold.
InterPro; IPR027417; P-loop_NTPase.
PANTHER; PTHR11630; PTHR11630; 1.
PANTHER; PTHR11630:SF26; PTHR11630:SF26; 1.
Pfam; PF00493; MCM; 1.
Pfam; PF14551; MCM_N; 1.
Pfam; PF17207; MCM_OB; 1.
PRINTS; PR01657; MCMFAMILY.
PRINTS; PR01663; MCMPROTEIN7.
SMART; SM00382; AAA; 1.
SMART; SM00350; MCM; 1.
SUPFAM; SSF50249; SSF50249; 1.
SUPFAM; SSF52540; SSF52540; 1.
PROSITE; PS00847; MCM_1; 1.
PROSITE; PS50051; MCM_2; 1.
3: Inferred from homology;
ATP-binding {ECO:0000256|RuleBase:RU365012,
ECO:0000256|SAAS:SAAS00536375};
Cell cycle {ECO:0000256|RuleBase:RU365012};
Coiled coil {ECO:0000256|SAM:Coils};
Complete proteome {ECO:0000313|Proteomes:UP000037122};
DNA replication {ECO:0000256|RuleBase:RU365012,
ECO:0000256|SAAS:SAAS00619122};
DNA-binding {ECO:0000256|RuleBase:RU004070,
ECO:0000256|SAAS:SAAS00628874};
Helicase {ECO:0000256|RuleBase:RU365012,
ECO:0000256|SAAS:SAAS00536375};
Hydrolase {ECO:0000256|RuleBase:RU365012,
ECO:0000256|SAAS:SAAS00536375};
Nucleotide-binding {ECO:0000256|RuleBase:RU365012,
ECO:0000256|SAAS:SAAS00536375};
Nucleus {ECO:0000256|RuleBase:RU365012,
ECO:0000256|SAAS:SAAS00536508}.
DOMAIN 393 599 MCM. {ECO:0000259|PROSITE:PS50051}.
COILED 144 164 {ECO:0000256|SAM:Coils}.
SEQUENCE 786 AA; 88698 MW; F52D2582B659BD66 CRC64;
MSTTTTLPAI QINVNYNELK AHIRDFFTHF KSLSDIDLDV DAELQELGIK YLDLLQKIAN
RDISTLYIAL DDIKLYQENQ FFSSSQPSQP SLVNLLNHIL KNTHHFVELF SLVVDELMPE
PTKEYSVKDD VLDVILHQRK LRNLRVSQEN RDELNALNAG LSQQTNNDWQ NSQQADDLLL
VNMFPPKLTR RYHLYFKPLS DRTKALAVRD VKGPHVGKYI TVRGIVTRVS DVKPSVLVNA
YTCDKCGHEI FQEVNSKVFQ PLTDCTSSVC KGDNQRGQLF MLTRASKFLS FQEVKIQEMA
SQVPVGHIPR TLTIHVNGDL VRLMNPGDIV DVSGIFLPSP YTGFRALKAG LLTETFLEAQ
YVQQHKKQYE SLDITPEIRD QMIALNREGN GTIYRRLAQS IAPEIYGHLD VKKILLLLLC
GGVTKEIGDG MRIRGDINVC LMGDPGVAKS QLLKAINKIA PRSVYTTGRG SSGVGLTAAV
MRDPVTDEMV LEGGALVLAD NGICCIDEFD KMEEGDRTAI HEVMEQQTIS ISKAGINTTL
NARTSILAAA NPLYGRYNPR LSPHENINLP AALLSRFDIM FLILDQASEE NDELLAEHVT
YVHREGRQPE MEFTPLDPQT IRQYISVART YRPVVPKEVG DHVVQLYIQM RKEAQRNEGS
VKKFSHITPR TLLGILRISQ ALARLRFDNV VRTTDVDEAL RLLLVSKSSM GGHDELERED
ITTRIMNVIR SIVRDEEQQT LNISDLHHRL GGMGYTQEQI DACIREYEQL EIFQVVENGE
SLLVVT


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