ID A0A197JHN7_9FUNG Unreviewed; 987 AA.
AC A0A197JHN7;
DT 05-OCT-2016, integrated into UniProtKB/TrEMBL.
DT 05-OCT-2016, sequence version 1.
DT 27-MAR-2024, entry version 34.
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=K457DRAFT_100338 {ECO:0000313|EMBL:OAQ24702.1};
OS Linnemannia elongata AG-77.
OC Eukaryota; Fungi; Fungi incertae sedis; Mucoromycota; Mortierellomycotina;
OC Mortierellomycetes; Mortierellales; Mortierellaceae; Linnemannia.
OX NCBI_TaxID=1314771 {ECO:0000313|EMBL:OAQ24702.1, ECO:0000313|Proteomes:UP000078512};
RN [1] {ECO:0000313|EMBL:OAQ24702.1, ECO:0000313|Proteomes:UP000078512}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AG-77 {ECO:0000313|EMBL:OAQ24702.1,
RC ECO:0000313|Proteomes:UP000078512};
RG DOE Joint Genome Institute;
RA Uehling J., Gryganskyi A., Hameed K., Tschaplinski T., Misztal P., Wu S.,
RA Desiro A., Vande Pol N., Du Z.-Y., Zienkiewicz A., Zienkiewicz K.,
RA Morin E., Tisserant E., Splivallo R., Hainaut M., Henrissat B., Ohm R.,
RA Kuo A., Yan J., Lipzen A., Nolan M., Labutti K., Barry K., Goldstein A.,
RA Labbe J., Schadt C., Tuskan G., Grigoriev I., Martin F., Vilgalys R.,
RA Bonito G.;
RT "Genome sequencing reveals origins of a unique bacterial endosymbiosis in
RT the earliest lineages of terrestrial Fungi.";
RL Submitted (MAY-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
CC -!- SIMILARITY: Belongs to the MCM family. {ECO:0000256|RuleBase:RU004070}.
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DR EMBL; KV442089; OAQ24702.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A197JHN7; -.
DR STRING; 1314771.A0A197JHN7; -.
DR OrthoDB; 1342948at2759; -.
DR Proteomes; UP000078512; Unassembled WGS sequence.
DR GO; GO:0031261; C:DNA replication preinitiation complex; IEA:UniProt.
DR GO; GO:0042555; C:MCM complex; IEA:UniProt.
DR GO; GO:0005656; C:nuclear pre-replicative complex; IEA:UniProt.
DR GO; GO:0043596; C:nuclear replication fork; IEA:UniProt.
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:0032508; P:DNA duplex unwinding; IEA:InterPro.
DR GO; GO:0006279; P:premeiotic DNA replication; IEA:UniProt.
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:UP000078512}.
FT DOMAIN 356..560
FT /note="MCM"
FT /evidence="ECO:0000259|PROSITE:PS50051"
FT REGION 108..135
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 602..647
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 786..848
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 895..921
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 947..987
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 108..126
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 630..646
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 810..835
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 895..914
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 964..987
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 987 AA; 109277 MW; 5D2394F2347331C4 CRC64;
MEIDSEDSFR DIATLRQGIQ EQHYHDICEI LYNPDITHHY SVVIDIMALV DSGTDPRLWS
DLAVSPHKVL PILDRILQDV QMEIIRLNDD DDLETQDLQR PNIYSYSNPS GSGFGRTTQS
MGSSRRMNGE GGKKRPMYLK PKCSARVMGL PAAESRRRTV PTCVDVGTFL SITATVIRTG
VVKMLENKKP VQCLMCKKTF DVLADVEQYN KVVMPSKCQA QGNIKPCNSY KFQMVEPPPG
QLPEGCRDYQ EIKIQEQTNK LTMGTIPGSM VVILHDDLVD HAKSGDDVTI TGTVIRRWKN
PIVGERCDIE LALLANHVFI HNEQRVGVGI TEEQRLDFEH FWEHARSKNV NKPFTARNQI
LSQICPKVYG LYIVKLAVML VLTGGVAKND DKSGLKVRGE PHLLLVGDPG TGKSQFLKYA
AELNPRSVLT TGIGSSSAGL TVTAVRDGNE WQLEAGALVL ADRGLCCIDE FGGMREHDKV
AIHEAMEQQS ISIAKAGIVC KLNTRCSVIA ATNPKGKYDP NESVSINIAL GSPLLSRFDI
VLVLMDTGNP NWDQKISSYI LDTRMRMDGQ FVPKRKRLTG KEIRRRRKKL RKIAKRKRME
ALGLQPGDDG YDSSISDDVS SVGGGSNAGQ AEDDEEDDEE VEQEATPDPW SLEKVKAYLI
WIKSTFKPKL TPPAEQVLVS YYQLQRKADL RNAARTTIRL LESLIRLSQA HARLMARNLV
TVQDAVVVIS LMEATAQGGA AVLGGINPLH ASFPKSAEEE YWRQESAMLD RLGLANLASQ
LQEGGYVDDE GQGAGYGEDD VVPGTDIEEM SRPGVKRRRE NSHGDDHDHH RNHYRTTSSP
SKRGSLGGNI RNVGLVAARS TSSSASTVST TALSTGSMVL DDQAEAEFLE RLRQSDPVSD
NNPNHNTMSR YSSGEGDGSL EEGFVGVKTE EEEAPLIDRR FALRQTQTQH SVGVVSPPVS
RKENKGKGVV RNRDFKDGFD HDERSYS
//
