ID A9V184_MONBE Unreviewed; 985 AA.
AC A9V184;
DT 05-FEB-2008, integrated into UniProtKB/TrEMBL.
DT 05-FEB-2008, sequence version 1.
DT 24-JAN-2024, entry version 83.
DE RecName: Full=DNA helicase {ECO:0000256|ARBA:ARBA00012551};
DE EC=3.6.4.12 {ECO:0000256|ARBA:ARBA00012551};
DE AltName: Full=Minichromosome maintenance 9 {ECO:0000256|ARBA:ARBA00042301};
GN ORFNames=MONBRDRAFT_32709 {ECO:0000313|EMBL:EDQ88886.1};
OS Monosiga brevicollis (Choanoflagellate).
OC Eukaryota; Choanoflagellata; Craspedida; Salpingoecidae; Monosiga.
OX NCBI_TaxID=81824 {ECO:0000313|EMBL:EDQ88886.1, ECO:0000313|Proteomes:UP000001357};
RN [1] {ECO:0000313|EMBL:EDQ88886.1, ECO:0000313|Proteomes:UP000001357}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MX1 / ATCC 50154 {ECO:0000313|Proteomes:UP000001357};
RX PubMed=18273011; DOI=10.1038/nature06617;
RG JGI Sequencing;
RA King N., Westbrook M.J., Young S.L., Kuo A., Abedin M., Chapman J.,
RA Fairclough S., Hellsten U., Isogai Y., Letunic I., Marr M., Pincus D.,
RA Putnam N., Rokas A., Wright K.J., Zuzow R., Dirks W., Good M.,
RA Goodstein D., Lemons D., Li W., Lyons J.B., Morris A., Nichols S.,
RA Richter D.J., Salamov A., Bork P., Lim W.A., Manning G., Miller W.T.,
RA McGinnis W., Shapiro H., Tjian R., Grigoriev I.V., Rokhsar D.;
RT "The genome of the choanoflagellate Monosiga brevicollis and the origin of
RT metazoans.";
RL Nature 451:783-788(2008).
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
CC -!- SIMILARITY: Belongs to the MCM family. {ECO:0000256|RuleBase:RU004070}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CH991553; EDQ88886.1; -; Genomic_DNA.
DR RefSeq; XP_001746499.1; XM_001746447.1.
DR AlphaFoldDB; A9V184; -.
DR STRING; 81824.A9V184; -.
DR EnsemblProtists; EDQ88886; EDQ88886; MONBRDRAFT_32709.
DR GeneID; 5891579; -.
DR KEGG; mbr:MONBRDRAFT_32709; -.
DR eggNOG; KOG0477; Eukaryota.
DR InParanoid; A9V184; -.
DR Proteomes; UP000001357; Unassembled WGS sequence.
DR GO; GO:0042555; C:MCM complex; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR GO; GO:0003697; F:single-stranded DNA binding; IBA:GO_Central.
DR GO; GO:0032508; P:DNA duplex unwinding; IEA:InterPro.
DR GO; GO:0000724; P:double-strand break repair via homologous recombination; IBA:GO_Central.
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; IPR003593; AAA+_ATPase.
DR InterPro; IPR031327; MCM.
DR InterPro; IPR001208; MCM_dom.
DR InterPro; IPR041562; MCM_lid.
DR InterPro; IPR033762; MCM_OB.
DR InterPro; IPR012340; NA-bd_OB-fold.
DR InterPro; IPR027417; P-loop_NTPase.
DR PANTHER; PTHR11630:SF48; DNA HELICASE MCM9; 1.
DR PANTHER; PTHR11630; DNA REPLICATION LICENSING FACTOR MCM FAMILY MEMBER; 1.
DR Pfam; PF00493; MCM; 1.
DR Pfam; PF17855; MCM_lid; 1.
DR Pfam; PF17207; MCM_OB; 1.
DR PRINTS; PR01657; MCMFAMILY.
DR SMART; SM00382; AAA; 1.
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; PS50051; MCM_2; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|RuleBase:RU004070};
KW DNA-binding {ECO:0000256|ARBA:ARBA00023125, ECO:0000256|RuleBase:RU004070};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW ECO:0000256|RuleBase:RU004070};
KW Reference proteome {ECO:0000313|Proteomes:UP000001357}.
FT DOMAIN 267..482
FT /note="MCM"
FT /evidence="ECO:0000259|PROSITE:PS50051"
FT REGION 643..709
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 725..985
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 673..709
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 753..769
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 770..788
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 790..804
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 813..830
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 846..868
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 908..929
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 938..965
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 985 AA; 106486 MW; CB3B0FF0353E4D5F CRC64;
MLLLPPTDEM IPFYFDNEVL DISGYCEMLR EQPDRELARL QQVLIGAQRR IKNEHPLERD
MSLKKQVQPR IRFPTTCIND QLPSATDLNK LCWVRGTVVR VSSVRTLELK REYTCMQCGT
VFLQQAEIEQ NFAIRTPTSC PTGACDGRKF KSVGTIQPHL CCDYQDIKMQ QCMNSLEFGT
IPQSIHVILL HDLVDSCKAG DDVDVSAVVR QRWLAEKPDE RCVTELVLEA NSVVITNDKV
AAVNITDDLR QQFERHWSLR PERPLSQRNE IIASFCPQVY GLYVVKIAVM LVMTGGVPHV
DATGTRTRGE SHLLLVGDPG TGKSQFLKYA AKLIPRSVLT TGVGSTSAGL TVTAVKEDGK
LIRFEFRPAP GEWTLEAGAL VLADGGLCCI DEFNGIREHD RGAIHEAMEQ QTLSVAKAGL
VCKLKTRTSV LAATNPKGSY DVESSLSINV AMASPLLSRF DIIMVLLDVK NAEWDTVVSD
FILGECSERT SNPGTQQPSR DLNGGATDLW GMNKLKAYLA YIKSFDPGLS KPAERVLSRY
YQLQRMADTS LTARTTIRLL ESLVRLAQAH ARIMCHGEVT LMDAVVAVTI IESSMQGASL
LGACSPLHSC FPDDAEAEYL AQEALVLEKL GFPDLLGTTR LQTNQGWATS RGPIKPSDGS
GEGGPGPGNN APHGPHSPTN AGNTSSQSLD GVLGEDSAGQ NQGPHPTQAG YMFFSQAATL
SRVKAKRLER AQQRQSRNAS AVGLSAAAQR DQEQGRPDSE AREGGEDDHG NRDEEEDAEL
DAVLEEDSDS DFAPSMRHVA AKRAKITQEV LATPEEETVQ PSSSRPADVL SSDSSEDEEE
ARAIGSTTSE EASQPSLYSQ QQRQKRAGSA RVPTRASSMA SLEVFAFSRP DRPRREGGLR
GVVASGSASM ANLPSVGVTP STSSPTTAAP GDAAPHESTS GGGSSEPVPS SAAQPPPSSL
SDTGHTAAAH EAALGSPVRR KKSFR
//
