ID G3U4T6_LOXAF Unreviewed; 1134 AA.
AC G3U4T6;
DT 16-NOV-2011, integrated into UniProtKB/TrEMBL.
DT 16-NOV-2011, sequence version 1.
DT 27-MAR-2024, entry version 69.
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:ENSLAFP00000022844.1};
OS Loxodonta africana (African elephant).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Afrotheria; Proboscidea; Elephantidae; Loxodonta.
OX NCBI_TaxID=9785 {ECO:0000313|Ensembl:ENSLAFP00000022844.1, ECO:0000313|Proteomes:UP000007646};
RN [1] {ECO:0000313|Ensembl:ENSLAFP00000022844.1, ECO:0000313|Proteomes:UP000007646}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Isolate ISIS603380 {ECO:0000313|Ensembl:ENSLAFP00000022844.1,
RC ECO:0000313|Proteomes:UP000007646};
RA Di Palma F., Heiman D., Young S., Johnson J., Lander E.S., Lindblad-Toh K.;
RT "The Genome Sequence of Loxodonta africana (African elephant).";
RL Submitted (JUN-2009) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSLAFP00000022844.1}
RP IDENTIFICATION.
RC STRAIN=Isolate ISIS603380 {ECO:0000313|Ensembl:ENSLAFP00000022844.1};
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 AlphaFoldDB; G3U4T6; -.
DR Ensembl; ENSLAFT00000035040.1; ENSLAFP00000022844.1; ENSLAFG00000013902.4.
DR GeneTree; ENSGT01090000260080; -.
DR Proteomes; UP000007646; Unassembled WGS sequence.
DR GO; GO:0005694; C:chromosome; IEA:UniProtKB-SubCell.
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:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0004386; F:helicase activity; IEA:UniProtKB-KW.
DR GO; GO:0032508; P:DNA duplex unwinding; IEA:InterPro.
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:UP000007646}.
FT DOMAIN 304..507
FT /note="MCM"
FT /evidence="ECO:0000259|PROSITE:PS50051"
FT REGION 658..738
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 769..1040
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1053..1089
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 685..715
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 769..792
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 800..819
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 881..914
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 915..931
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 974..993
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 994..1009
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1134 AA; 126678 MW; 1A376660A241BA96 CRC64;
FKMNSDQVTL VGQVFESYVS EYHKNDILLI LKEMDEDAHY PVVVNAMTLF ETNMEIGEYF
NVFPNEVLTI FDSALRRSAL TILQSLSQPE DVSMKQNLHA RISGLPVCPE LVREHIPKTK
DVGHFLSVTG TVIRTSLVKV LEFERDYMCN KCKHVFVVKA DFEQYYTFCR PSSCPSLESC
DSSKFTCLSG LSSSPTKCRD YQEIKIQEQV QRLSVGSIPR SMKVILEDDL VDSCKSGDDL
TIYGVVMQRW KPFQQDVRCE VEIVLKANYV QVNNEQSTGI IMDEEVRKEF EDFWENYRSD
PFAGRNEILA SLCPQVFGLY LVKLAVAMVL AGGIQRTDAT GTRVRGESHL LLVGDPGTGK
SQFLKYAAKI TPRSVLTTGI GSTSAGLTVT AVKDSGEWNL EAGALVLADS GLCCIDEFNS
LKEHDRTSIH EAMEQQTISV AKAGLVCKLN TRTTILAATN PKGQYDPHES VSVNIALGSP
LLSRFDLILV LLDTKNEDWD RIISSFILEN KGYPSKSEKL WSMEKMKTYF CLIRNLQPTL
SDVGNQVLLR YYQMQRQSDS RNAARTTIRL LESLIRLAEA HARLMFRDTV TLEDAVAVVS
VMESSMQGGA LLGGVNALHT SFPENPLEQY QRQCELILEK LELQSLLSEE LRRLERLQNQ
SVHQSQPRPV EAETPPGFLR NDPGQESKFR TSTPQEINCS PGGSPLLNLP SHLEPNRSTS
REHSAEPQNS RDNSLDWFDS MATPQMEPKI TVHVSPSPKT TEKEVALKIS NSRSQGKEKS
RPGQSSKSEA GQLRAPGETD APLRPHKTFH VEGKKAKKAA MVSEVAVPAD EPDSVSTHHV
PSKLHKLRKE RAQELCRNPT REPSQPSSPS DPQSIPVHSP ERKLETPKRK RQKSLAQVEE
PELEGVERPP VAKLKKFTFK QKSKLIHSPH NHSHVSHGTG KMAVHSPKMS QLAAGTRKEA
ALPVKDPEEL RSTPGNRISG QLQIMTREAS QQPPQKDGSR EKKACAPEKR VIQPELGNQT
GHSHLTCEKE DSHNNKNSKV HACTLARLAD FSFASPSESK SEPPPPRPES KNWIARGPSP
PTTTATMLGS KRKTFQLEGS TEKLITSTKS LFTLPELDDE PLDFDWDEEI RKKP
//
