ID G1PLW6_MYOLU Unreviewed; 1133 AA.
AC G1PLW6;
DT 19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT 19-OCT-2011, sequence version 1.
DT 27-MAR-2024, entry version 76.
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:ENSMLUP00000011869.2};
OS Myotis lucifugus (Little brown bat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Chiroptera; Microchiroptera; Vespertilionidae;
OC Myotis.
OX NCBI_TaxID=59463 {ECO:0000313|Ensembl:ENSMLUP00000011869.2, ECO:0000313|Proteomes:UP000001074};
RN [1] {ECO:0000313|Ensembl:ENSMLUP00000011869.2, ECO:0000313|Proteomes:UP000001074}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=21993624; DOI=10.1038/nature10530;
RA Lindblad-Toh K., Garber M., Zuk O., Lin M.F., Parker B.J., Washietl S.,
RA Kheradpour P., Ernst J., Jordan G., Mauceli E., Ward L.D., Lowe C.B.,
RA Holloway A.K., Clamp M., Gnerre S., Alfoldi J., Beal K., Chang J.,
RA Clawson H., Cuff J., Di Palma F., Fitzgerald S., Flicek P., Guttman M.,
RA Hubisz M.J., Jaffe D.B., Jungreis I., Kent W.J., Kostka D., Lara M.,
RA Martins A.L., Massingham T., Moltke I., Raney B.J., Rasmussen M.D.,
RA Robinson J., Stark A., Vilella A.J., Wen J., Xie X., Zody M.C., Baldwin J.,
RA Bloom T., Chin C.W., Heiman D., Nicol R., Nusbaum C., Young S.,
RA Wilkinson J., Worley K.C., Kovar C.L., Muzny D.M., Gibbs R.A., Cree A.,
RA Dihn H.H., Fowler G., Jhangiani S., Joshi V., Lee S., Lewis L.R.,
RA Nazareth L.V., Okwuonu G., Santibanez J., Warren W.C., Mardis E.R.,
RA Weinstock G.M., Wilson R.K., Delehaunty K., Dooling D., Fronik C.,
RA Fulton L., Fulton B., Graves T., Minx P., Sodergren E., Birney E.,
RA Margulies E.H., Herrero J., Green E.D., Haussler D., Siepel A., Goldman N.,
RA Pollard K.S., Pedersen J.S., Lander E.S., Kellis M.;
RT "A high-resolution map of human evolutionary constraint using 29 mammals.";
RL Nature 478:476-482(2011).
RN [2] {ECO:0000313|Ensembl:ENSMLUP00000011869.2}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-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; AAPE02018741; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AAPE02018742; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AAPE02018743; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AAPE02018744; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR RefSeq; XP_006089270.1; XM_006089208.2.
DR AlphaFoldDB; G1PLW6; -.
DR STRING; 59463.ENSMLUP00000011869; -.
DR Ensembl; ENSMLUT00000013048.2; ENSMLUP00000011869.2; ENSMLUG00000013047.2.
DR GeneID; 102425750; -.
DR KEGG; mlf:102425750; -.
DR CTD; 254394; -.
DR eggNOG; KOG0477; Eukaryota.
DR GeneTree; ENSGT01090000260080; -.
DR HOGENOM; CLU_000995_7_2_1; -.
DR InParanoid; G1PLW6; -.
DR OMA; CNKCKYV; -.
DR OrthoDB; 1342948at2759; -.
DR TreeFam; TF329421; -.
DR Proteomes; UP000001074; Unassembled WGS sequence.
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 Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW ECO:0000256|RuleBase:RU004070};
KW Reference proteome {ECO:0000313|Proteomes:UP000001074}.
FT DOMAIN 302..505
FT /note="MCM"
FT /evidence="ECO:0000259|PROSITE:PS50051"
FT REGION 656..737
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 752..908
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 921..1035
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1052..1108
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 656..678
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 687..708
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 778..792
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 864..878
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 879..895
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 989..1010
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1017..1033
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1052..1089
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1133 AA; 125360 MW; 27E76BBA78979FE5 CRC64;
MNSDQIALVG QVFESYVSEY HKNDILLILK ENDEDAHYPV VINAMTLFET NMEIGEYFNA
FPNEVLTIFD NSLRRSAMTI LESLSQPEGV SMKQNLHARI SGLPVCPELV REHIPKTKDV
GHFLSVTGTV IRTSLVKILE FERDYMCNKC KHVFVVKADF EQYYTFCRPS SCPSLESCDS
SKFTCLSDLS SSPTKCRDYQ EIKIQEQVQR LAIGNIPRSM KVILEDDLVD TCKSGDDLTI
YGVVMQRWKP FQRDVRCEVE IVLKANYVQV NNEQSAGIIM DEEVRKEFED FWEHYKSDPF
AGRNEILASL CPQVFGMYLV KLAVAMVLAG GIQRTDATGT RVRGESHLLL VGDPGTGKSQ
FLKYAAKITP RSVLTTGIGS TSAGLTVTAV KDSGEWNLEA GALVLADAGL CCIDEFNSLK
EHDRTSIHEA MEQQTISVAK AGLVCKLNTR TTILAATNPK GQYDPHESVS VNIALGSPLL
SRFDLILVLL DTKNEDWDRI ISSFILENKG YPSKSEKLWS MEKMKTYFSL IRNLQPTLSD
VGNQVLLRYY QMQRQSDSRN AARTTIRLLE SLIRLAEAHA RLMFRDTVTL EDAITVVSVM
ESSMQGGALL GGVNALHTSF PENPLEQYQR QCELILEKLE LHNLLSEELR RLERLQNQSV
YQSQPRTEAE TTPGSSGRDP RGESKFRTST QQEVNCGIPS SSTGGSPRGS PPLDPPPHLG
PNRSACRKDS AQHDSRDAGL DWFDSLTTHQ IEPKNTVSVS PGPKTTERKM VLKKSNNTSQ
GKEERESDQR SKLETGLLPA PGETGAPLRP ESVKGKKGKK AAAVSETAGI ADEPDSVLTH
HVPRKLHRLR KERAQELYGN PARPPSQPIS PPHPPSIPVR GPERKRQKSL PQVEEPEPES
VESSGAPVAK LAKFTFKQKS KLIHSPEDQS LVSPGRTDLA VRSPKISQHG TRGEAALSVK
GPGKLTSGKG GSDLLQGRAM GVSQQSSGKD RSRAERACGP GKRDIQPEFE PGNETGHLHL
TGERDKKEGL SCSNKSSKVH ACTLAKLANF SFTSSPESKS ASLPPSESMN SGERGPSPPP
TTTATMLGRK RKTFQLEEPP EKLSLSKKSL FTLPELEDEA LDFDWDEEMR KKP
//
