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Database: UniProt
Entry: M3YSG6_MUSPF
LinkDB: M3YSG6_MUSPF
Original site: M3YSG6_MUSPF 
ID   M3YSG6_MUSPF            Unreviewed;      1145 AA.
AC   M3YSG6;
DT   01-MAY-2013, integrated into UniProtKB/TrEMBL.
DT   01-MAY-2013, sequence version 1.
DT   24-JAN-2024, entry version 66.
DE   RecName: Full=DNA helicase MCM9 {ECO:0000256|ARBA:ARBA00041085};
DE            EC=3.6.4.12 {ECO:0000256|ARBA:ARBA00012551};
DE   AltName: Full=Minichromosome maintenance 9 {ECO:0000256|ARBA:ARBA00042301};
GN   Name=MCM9 {ECO:0000313|Ensembl:ENSMPUP00000014276.1,
GN   ECO:0000313|RefSeq:XP_004740148.1, ECO:0000313|RefSeq:XP_004740149.1};
OS   Mustela putorius furo (European domestic ferret) (Mustela furo).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Carnivora; Caniformia; Musteloidea; Mustelidae;
OC   Mustelinae; Mustela.
OX   NCBI_TaxID=9669 {ECO:0000313|Ensembl:ENSMPUP00000014276.1};
RN   [1] {ECO:0000313|Ensembl:ENSMPUP00000014276.1}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (MAR-2023) to UniProtKB.
RN   [2] {ECO:0000313|RefSeq:XP_004740148.1, ECO:0000313|RefSeq:XP_004740149.1}
RP   IDENTIFICATION.
RC   TISSUE=Brain {ECO:0000313|RefSeq:XP_004740148.1,
RC   ECO:0000313|RefSeq:XP_004740149.1};
RG   RefSeq;
RL   Submitted (SEP-2023) to UniProtKB.
CC   -!- SUBCELLULAR LOCATION: Chromosome {ECO:0000256|ARBA:ARBA00004286}.
CC       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; AEYP01006503; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AEYP01006504; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AEYP01006505; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AEYP01006506; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   RefSeq; XP_004740148.1; XM_004740091.2.
DR   RefSeq; XP_004740149.1; XM_004740092.2.
DR   STRING; 9669.ENSMPUP00000014276; -.
DR   Ensembl; ENSMPUT00000014504.1; ENSMPUP00000014276.1; ENSMPUG00000014384.1.
DR   GeneID; 101684169; -.
DR   KEGG; mpuf:101684169; -.
DR   CTD; 254394; -.
DR   eggNOG; KOG0477; Eukaryota.
DR   GeneTree; ENSGT01090000260080; -.
DR   HOGENOM; CLU_000995_7_2_1; -.
DR   OMA; EYHKSDI; -.
DR   OrthoDB; 1342948at2759; -.
DR   Proteomes; UP000000715; Unplaced.
DR   GO; GO:0005694; C:chromosome; IEA:UniProtKB-SubCell.
DR   GO; GO:0097362; C:MCM8-MCM9 complex; IEA:Ensembl.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR   GO; GO:0003682; F:chromatin binding; IEA:Ensembl.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0003678; F:DNA helicase activity; IEA:Ensembl.
DR   GO; GO:0019899; F:enzyme binding; IEA:Ensembl.
DR   GO; GO:0032406; F:MutLbeta complex binding; IEA:Ensembl.
DR   GO; GO:0032407; F:MutSalpha complex binding; IEA:Ensembl.
DR   GO; GO:0032408; F:MutSbeta complex binding; IEA:Ensembl.
DR   GO; GO:0000724; P:double-strand break repair via homologous recombination; IEA:Ensembl.
DR   GO; GO:0007292; P:female gamete generation; IEA:Ensembl.
DR   GO; GO:0070716; P:mismatch repair involved in maintenance of fidelity involved in DNA-dependent DNA replication; IEA:Ensembl.
DR   GO; GO:0071168; P:protein localization to chromatin; IEA:Ensembl.
DR   GO; GO:0036298; P:recombinational interstrand cross-link repair; IEA:Ensembl.
DR   CDD; cd17760; MCM9; 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; 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   Chromosome {ECO:0000256|ARBA:ARBA00022454};
KW   DNA-binding {ECO:0000256|ARBA:ARBA00023125, ECO:0000256|RuleBase:RU004070};
KW   Helicase {ECO:0000256|ARBA:ARBA00022806,
KW   ECO:0000313|RefSeq:XP_004740148.1};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022806,
KW   ECO:0000313|RefSeq:XP_004740148.1};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW   ECO:0000256|RuleBase:RU004070};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000715}.
FT   DOMAIN          302..505
FT                   /note="MCM"
FT                   /evidence="ECO:0000259|PROSITE:PS50051"
FT   REGION          657..687
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          699..841
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          865..1049
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1063..1102
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        657..680
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        751..774
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        806..825
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        974..997
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        999..1017
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1033..1047
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1145 AA;  126372 MW;  54A4D5AFC6D07022 CRC64;
     MNSDQVTLVG QVFESYVSEY HKNDILLILK ESDEDAHYPV VVNAMTLFET NMEIGEYFNA
     FPNEVLTVFD SALRRSALTI LQSLSQPEGA SMKQNLHARI SGLPVCPELV REHIPKTKDV
     GHFLSVTGTV IRTSLVKILE FERDYMCNKC KHVFVVKADF EQYYTFCRPS SCPSLESCDS
     SKFTCLSGLS SSPTRCRDYQ EIKIQEQVQR LSVGSIPRSM KVILEDDLVD SCKSGDDLTI
     YGVVMQRWKP FQQDVRCEVE IVLKANYVQV NNEQSAGNII DEEVQKEFED FWESYKSDPF
     AGRNEILASL CPQVFGMYLV KLAVALVLAG GIQRTDATGT RVRGESHLLL VGDPGTGKSQ
     FLKYAAKITP RSVLTTGIGS TSAGLTVTAV KDSGEWNLEA GALVLADAGL CCIDEFNSLK
     EHDRTSIHEA MEQQTISVAK AGLVCKLNTR TTILAATNPK GQYDTHESVS VNIALGSPLL
     SRFDLILVLL DTKNEDWDRI ISSFILENKG YPSKSEKLWS MEKMKTYFCL IRNLQPTLSD
     EGNQVLLRYY QMQRQSDSRN AARTTIRLLE SLIRLAEAHA RLMFHDAVTL EDAVTAVSVM
     ESSMQGGALL GGVNALHTAF PENPLKQYQR QCELILEKLE LNNLLSEELR RLERLQNQNV
     HQSQPQAVEA ETNPGSSKND PGEAAKSRIW SAQQEVNWSM LTSSPGPSPE GSPLSDPLSH
     GGPSRPAKRK HSAEHKNSKD DSLDWFDSIA THQLEPQNTV PVSPKTNGGK MALQTFKNKA
     QGKEKGVPGQ RSKMETGQLP APGETEASRR PDHVDHVEGK EAKKAAVVPE AAGSAGEPDS
     VLTHHVSRKL HQLRKASAQE LCKNPATVPV QPVGPSLPRS SSLCGPKGAL ETSKRKRQKS
     LAQMEEPELG SAESPGPPLA KLAKFTFKRK SKLTHSPEDH SPMSPGTTKG AVPSPRVLRR
     VSREAVVPGK GPQKLASTSG SRNSDQQQDQ AMDVSQQALE EDSPREKSKR GPEGRVTEPE
     FELGNQTGRS PPTCQRDRKE DVSRNIKSSK VHACTLAKLA HFSFTSPSES KSEPPPPPES
     ENEGARGTSP RPGAAATVFG RKRKTFQLEG SSERLFFSKK SLFTLSELDD EALDFDWNEE
     IRRKP
//
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