ID A7TT93_VANPO Unreviewed; 1011 AA.
AC A7TT93;
DT 02-OCT-2007, integrated into UniProtKB/TrEMBL.
DT 02-OCT-2007, sequence version 1.
DT 27-MAR-2024, entry version 105.
DE RecName: Full=DNA replication licensing factor MCM6 {ECO:0000256|RuleBase:RU368064};
DE EC=3.6.4.12 {ECO:0000256|RuleBase:RU368064};
GN ORFNames=Kpol_278p4 {ECO:0000313|EMBL:EDO14516.1};
OS Vanderwaltozyma polyspora (strain ATCC 22028 / DSM 70294 / BCRC 21397 / CBS
OS 2163 / NBRC 10782 / NRRL Y-8283 / UCD 57-17) (Kluyveromyces polysporus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Vanderwaltozyma.
OX NCBI_TaxID=436907 {ECO:0000313|Proteomes:UP000000267};
RN [1] {ECO:0000313|EMBL:EDO14516.1, ECO:0000313|Proteomes:UP000000267}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 22028 / DSM 70294 / BCRC 21397 / CBS 2163 / NBRC 10782 /
RC NRRL Y-8283 / UCD 57-17 {ECO:0000313|Proteomes:UP000000267};
RX PubMed=17494770; DOI=10.1073/pnas.0608218104;
RA Scannell D.R., Frank A.C., Conant G.C., Byrne K.P., Woolfit M., Wolfe K.H.;
RT "Independent sorting-out of thousands of duplicated gene pairs in two yeast
RT species descended from a whole-genome duplication.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:8397-8402(2007).
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; DS480551; EDO14516.1; -; Genomic_DNA.
DR RefSeq; XP_001642374.1; XM_001642324.1.
DR AlphaFoldDB; A7TT93; -.
DR STRING; 436907.A7TT93; -.
DR GeneID; 5542516; -.
DR KEGG; vpo:Kpol_278p4; -.
DR eggNOG; KOG0480; Eukaryota.
DR HOGENOM; CLU_000995_3_0_1; -.
DR InParanoid; A7TT93; -.
DR OMA; CQTEIRN; -.
DR OrthoDB; 5476523at2759; -.
DR PhylomeDB; A7TT93; -.
DR Proteomes; UP000000267; Unassembled WGS sequence.
DR GO; GO:0071162; C:CMG complex; IEA:UniProt.
DR GO; GO:0005737; C:cytoplasm; 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:0031298; C:replication fork protection complex; 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:0003678; F:DNA helicase activity; IEA:InterPro.
DR GO; GO:0003688; F:DNA replication origin binding; IEA:UniProt.
DR GO; GO:0006270; P:DNA replication initiation; IEA:UniProtKB-UniRule.
DR GO; GO:0006268; P:DNA unwinding involved in DNA replication; IEA:UniProt.
DR GO; GO:0000727; P:double-strand break repair via break-induced replication; IEA:UniProt.
DR GO; GO:0006267; P:pre-replicative complex assembly involved in nuclear cell cycle DNA replication; IEA:UniProt.
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:UP000000267}.
FT DOMAIN 505..711
FT /note="MCM"
FT /evidence="ECO:0000259|PROSITE:PS50051"
FT REGION 1..83
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 198..240
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 822..879
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..76
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 212..240
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 836..856
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1011 AA; 113155 MW; 541C70BB645E84D3 CRC64;
MSSPFRRNSY SNERPTGSSQ PPSSIGGGFG SSSALEQDSQ LDVRPQFPSS SLPVGNVGST
QDDSTQFSSQ RQYNAEALPQ DDLPMQGMRR RNINHIKKVD DVTGEKVREA FEQFLENYTN
PTETGELDRV YRTQIEFMKV YNLSTIYIDY QHLSQRENGA LAMAISEQYY RFLPFLQKGL
KRVIRKYAPE LLLTNDTFTN NENKERDSGN PDTQNSTDAN TIDNASSRMA TGSVTSGSPE
QTERVFQISF FNLPVVHRIR DIRSDKIGSL LSISGTVTRT SEVRPELYKA SFTCDICRAI
VDNVEQAFKY TEPTFCPNPS CENRSLWTLN LARSKFLDWQ KVRVQENSNE IPTGSMPRTL
DIILRGDCVE RAKPGDRCRF TGTEIVVPDV TQLGLPGVKA SSSLDSRGIT RSSEGLNNGV
TGIRSLGVRD LTYKISFLAC HVVSVSSNTN NQDSEGTKET EQQLISNLHS NNVYQDLEKD
QEVFLNSLNS HEINELKDMV KDEHIYSKLV KSISPAVFGH ESVKKGILLQ MLGGVHKTTV
EGIKLRGDIN ICIVGDPSTS KSQFLKYVTG FAPRAVYTSG KASSAAGLTA AVVRDEEAGD
YTIEAGALML ADNGVCCIDE FDKMDISDQV AIHEAMEQQT ISIAKAGIHA TLNARTSILA
AANPIGGRYN RKLSLRGNLN MTAPIMSRFD LFFVVLDDCN EHIDTELASH IVDLHMKRDM
AIDPPYSAEQ LRRYIKYART FKPILTKEAR EFLVKKYKEL RNDDAQGYSR SSYRITVRQL
ESMIRLSEAI ARANCVDEIT PDFVAEAYDL LRQSIIRVDV DDVEIDDEED NDGDDNNNNP
TNGENNENNE MSSGAPETAP TGPHGGIPEA SQTETAPKHK ATVTYDKYVS MMNLLVRKIA
EVERTEGNEL TATDIVDWYL IQKQDEFSSE SEYWQERKLA FKVLKRLVKD RILMAIHGTR
ENLDYVMEGD DGNEQLRTSP DDIVYVIHPN CEILDSLDQQ ESGGNADERI Q
//
