ID A0A2T3ATU6_AMORE Unreviewed; 961 AA.
AC A0A2T3ATU6;
DT 18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT 18-JUL-2018, sequence version 1.
DT 27-MAR-2024, entry version 25.
DE RecName: Full=DNA replication licensing factor MCM6 {ECO:0000256|RuleBase:RU368064};
DE EC=3.6.4.12 {ECO:0000256|RuleBase:RU368064};
GN ORFNames=M430DRAFT_22241 {ECO:0000313|EMBL:PSS10907.1};
OS Amorphotheca resinae ATCC 22711.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC Helotiales; Amorphothecaceae; Amorphotheca.
OX NCBI_TaxID=857342 {ECO:0000313|EMBL:PSS10907.1, ECO:0000313|Proteomes:UP000241818};
RN [1] {ECO:0000313|EMBL:PSS10907.1, ECO:0000313|Proteomes:UP000241818}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 22711 {ECO:0000313|EMBL:PSS10907.1,
RC ECO:0000313|Proteomes:UP000241818};
RX PubMed=29315638; DOI=10.1111/nph.14974;
RA Martino E., Morin E., Grelet G.A., Kuo A., Kohler A., Daghino S.,
RA Barry K.W., Cichocki N., Clum A., Dockter R.B., Hainaut M., Kuo R.C.,
RA LaButti K., Lindahl B.D., Lindquist E.A., Lipzen A., Khouja H.R.,
RA Magnuson J., Murat C., Ohm R.A., Singer S.W., Spatafora J.W., Wang M.,
RA Veneault-Fourrey C., Henrissat B., Grigoriev I.V., Martin F.M., Perotto S.;
RT "Comparative genomics and transcriptomics depict ericoid mycorrhizal fungi
RT as versatile saprotrophs and plant mutualists.";
RL New Phytol. 217:1213-1229(2018).
CC -!- FUNCTION: Acts as component of the MCM2-7 complex (MCM complex) which
CC is the replicative helicase essential for 'once per cell cycle' DNA
CC replication initiation and elongation in eukaryotic cells. The active
CC ATPase sites in the MCM2-7 ring are formed through the interaction
CC surfaces of two neighboring subunits such that a critical structure of
CC a conserved arginine finger motif is provided in trans relative to the
CC ATP-binding site of the Walker A box of the adjacent subunit. The six
CC ATPase active sites, however, are likely to contribute differentially
CC to the complex helicase activity. {ECO:0000256|RuleBase:RU368064}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + H2O = ADP + H(+) + phosphate; Xref=Rhea:RHEA:13065,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; EC=3.6.4.12;
CC Evidence={ECO:0000256|RuleBase:RU368064};
CC -!- SUBUNIT: Component of the MCM2-7 complex.
CC {ECO:0000256|RuleBase:RU368064}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123,
CC ECO:0000256|RuleBase:RU368064}.
CC -!- SIMILARITY: Belongs to the MCM family. {ECO:0000256|ARBA:ARBA00008010,
CC ECO:0000256|RuleBase:RU004070}.
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DR EMBL; KZ679016; PSS10907.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2T3ATU6; -.
DR STRING; 857342.A0A2T3ATU6; -.
DR InParanoid; A0A2T3ATU6; -.
DR OrthoDB; 5476523at2759; -.
DR Proteomes; UP000241818; Unassembled WGS sequence.
DR GO; GO:0031261; C:DNA replication preinitiation complex; IEA:UniProt.
DR GO; GO:0042555; C:MCM complex; IEA:UniProtKB-UniRule.
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-UniRule.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:RHEA.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0003678; F:DNA helicase activity; IEA:InterPro.
DR GO; GO:0006270; P:DNA replication initiation; IEA:UniProtKB-UniRule.
DR GO; GO:0006279; P:premeiotic DNA replication; IEA:UniProt.
DR CDD; cd17757; MCM6; 1.
DR Gene3D; 1.20.58.870; -; 1.
DR Gene3D; 2.20.28.10; -; 1.
DR Gene3D; 3.30.1640.10; mini-chromosome maintenance (MCM) complex, chain A, domain 1; 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; IPR031327; MCM.
DR InterPro; IPR008049; MCM6.
DR InterPro; IPR041024; Mcm6_C.
DR InterPro; IPR018525; MCM_CS.
DR InterPro; IPR001208; MCM_dom.
DR InterPro; IPR041562; MCM_lid.
DR InterPro; IPR027925; MCM_N.
DR InterPro; IPR033762; MCM_OB.
DR InterPro; IPR012340; NA-bd_OB-fold.
DR InterPro; IPR027417; P-loop_NTPase.
DR PANTHER; PTHR11630; DNA REPLICATION LICENSING FACTOR MCM FAMILY MEMBER; 1.
DR PANTHER; PTHR11630:SF43; DNA REPLICATION LICENSING FACTOR MCM6; 1.
DR Pfam; PF00493; MCM; 1.
DR Pfam; PF18263; MCM6_C; 1.
DR Pfam; PF17855; MCM_lid; 1.
DR Pfam; PF14551; MCM_N; 1.
DR Pfam; PF17207; MCM_OB; 1.
DR PRINTS; PR01657; MCMFAMILY.
DR PRINTS; PR01662; MCMPROTEIN6.
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; PS00847; MCM_1; 1.
DR PROSITE; PS50051; MCM_2; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|RuleBase:RU004070};
KW Cell cycle {ECO:0000256|RuleBase:RU368064};
KW DNA replication {ECO:0000256|ARBA:ARBA00022705,
KW ECO:0000256|RuleBase:RU368064};
KW DNA-binding {ECO:0000256|ARBA:ARBA00023125, ECO:0000256|RuleBase:RU004070};
KW Helicase {ECO:0000256|ARBA:ARBA00022806, ECO:0000256|RuleBase:RU368064};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU368064};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW ECO:0000256|RuleBase:RU004070}; Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW Reference proteome {ECO:0000313|Proteomes:UP000241818}.
FT DOMAIN 479..685
FT /note="MCM"
FT /evidence="ECO:0000259|PROSITE:PS50051"
FT REGION 1..78
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 184..212
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 797..850
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 13..40
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 805..820
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 961 AA; 105720 MW; 4A27E5D95BE53D9B CRC64;
MASVMMSDVI DSDIGPSSRT GTPGARSRRR GSQGSSARPR GPPTESVGPM SDDEGFADDQ
IPVGSSRPRR NDRNIPRVED AIGQYVQINF EDFLEQFVED PVSSGAPPSS AVTTDKYYIA
QIHGLRTYQL STLYVDYTHL AQWKGGALAV GIVEEYYRFL PFLTKGLHTM IAKYEPRYFR
DHRQPVASSN QTSSGASNAA SASQSDFQGD KTPNQQTDKL FALAFYNLPL VTRIRHLRTN
NIGQLLSISG TVTRTSEVRP ELSLATFICE SCRSTVPNVE QTFRYTEPTQ CPNLECGNRH
GWRLDIRQST FVDWQKVRVQ ENSSEIPTGS MPRTMDVILR GEIVDRAKAG EKCIFTGALI
VVPDVSQLGL PGVRPMAVRD NQNRSGDANG VTGLKALGVR DLTYRLAFLA CMVTPDTTTP
GQASSQQLNG QSSNILASLN QTAPIDPNEP GEHAQEAVLA SMTHAEIEDL RKMVHSDHIY
SRLVNSIAPM VYGHEIVKKG ILLQLMSGVS KTTKEGMALR GDINICIVGD PSTSKSQFLK
YVCSFLPRAV YTSGKASSAA GLTAAVVKDE ETGEFTIEAG ALMLADNGIC AIDEFDKMDI
SDQVAIHEAM EQQTISIAKA GIQATLNART SILAAANPVG GRYNRKTTLR ANINMSAPIM
SRFDLFFVIL DECNENVDRH LAEHIVGIHQ LRDEAVQPEF TTEQLQRYIR FAKTFKPEFT
PEAREVLVQK YKELRSDDAQ GGIGRNSYRI TVRQLESMIR LSEAIAKANC VEEITPEFVI
EAFNLLRQSI ISVEKDDVEV DEDEDEVLNR RPRDIDGDAP MADGGDDEDG DHGPDGGAGA
NGSTPAPTSK KTKVTYDKYI SVVNLLVQRV NEDELGSGEG VEGEKLVEWY LEQKEDELAG
EEDYHAEKAL VKKIIKRMVK ENILMEIRGQ GLVGEDGQGS STTTAEHSVY VLHPNCAVEE
Y
//
