MCM6_ANOGA
ID MCM6_ANOGA Reviewed; 814 AA.
AC Q7Q0Q1;
DT 02-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT 02-MAY-2006, sequence version 3.
DT 03-AUG-2022, entry version 123.
DE RecName: Full=DNA replication licensing factor Mcm6;
DE EC=3.6.4.12;
GN Name=Mcm6 {ECO:0000250|UniProtKB:Q9V461}; ORFNames=AGAP010219;
OS Anopheles gambiae (African malaria mosquito).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Nematocera; Culicoidea; Culicidae;
OC Anophelinae; Anopheles.
OX NCBI_TaxID=7165;
RN [1] {ECO:0000305}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PEST;
RX PubMed=12364791; DOI=10.1126/science.1076181;
RA Holt R.A., Subramanian G.M., Halpern A., Sutton G.G., Charlab R.,
RA Nusskern D.R., Wincker P., Clark A.G., Ribeiro J.M.C., Wides R.,
RA Salzberg S.L., Loftus B.J., Yandell M.D., Majoros W.H., Rusch D.B., Lai Z.,
RA Kraft C.L., Abril J.F., Anthouard V., Arensburger P., Atkinson P.W.,
RA Baden H., de Berardinis V., Baldwin D., Benes V., Biedler J., Blass C.,
RA Bolanos R., Boscus D., Barnstead M., Cai S., Center A., Chaturverdi K.,
RA Christophides G.K., Chrystal M.A.M., Clamp M., Cravchik A., Curwen V.,
RA Dana A., Delcher A., Dew I., Evans C.A., Flanigan M.,
RA Grundschober-Freimoser A., Friedli L., Gu Z., Guan P., Guigo R.,
RA Hillenmeyer M.E., Hladun S.L., Hogan J.R., Hong Y.S., Hoover J.,
RA Jaillon O., Ke Z., Kodira C.D., Kokoza E., Koutsos A., Letunic I.,
RA Levitsky A.A., Liang Y., Lin J.-J., Lobo N.F., Lopez J.R., Malek J.A.,
RA McIntosh T.C., Meister S., Miller J.R., Mobarry C., Mongin E., Murphy S.D.,
RA O'Brochta D.A., Pfannkoch C., Qi R., Regier M.A., Remington K., Shao H.,
RA Sharakhova M.V., Sitter C.D., Shetty J., Smith T.J., Strong R., Sun J.,
RA Thomasova D., Ton L.Q., Topalis P., Tu Z.J., Unger M.F., Walenz B.,
RA Wang A.H., Wang J., Wang M., Wang X., Woodford K.J., Wortman J.R., Wu M.,
RA Yao A., Zdobnov E.M., Zhang H., Zhao Q., Zhao S., Zhu S.C., Zhimulev I.,
RA Coluzzi M., della Torre A., Roth C.W., Louis C., Kalush F., Mural R.J.,
RA Myers E.W., Adams M.D., Smith H.O., Broder S., Gardner M.J., Fraser C.M.,
RA Birney E., Bork P., Brey P.T., Venter J.C., Weissenbach J., Kafatos F.C.,
RA Collins F.H., Hoffman S.L.;
RT "The genome sequence of the malaria mosquito Anopheles gambiae.";
RL Science 298:129-149(2002).
CC -!- FUNCTION: Acts as component of the Mcm2-7 complex (Mcm complex) which
CC is the putative replicative helicase essential for 'once per cell
CC cycle' DNA replication initiation and elongation in eukaryotic cells.
CC The active ATPase sites in the Mcm2-7 ring are formed through the
CC interaction surfaces of two neighboring subunits such that a critical
CC structure of a conserved arginine finger motif is provided in trans
CC relative to the ATP-binding site of the Walker A box of the adjacent
CC subunit. The six ATPase active sites, however, are likely to contribute
CC differentially to the complex helicase activity (By similarity).
CC {ECO:0000250}.
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 -!- SUBUNIT: Component of the Mcm2-7 complex. The complex forms a toroidal
CC hexameric ring with the proposed subunit order Mcm2-Mcm6-Mcm4-Mcm7-
CC Mcm3-Mcm5 (By simililarity). The heterodimers of Mcm4/Mcm6 and
CC Mcm3/Mcm5 interact with Mcm2 and Mcm7 (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. Note=Associated with
CC chromatin during cell cycles. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the MCM family. {ECO:0000255}.
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DR EMBL; AAAB01008980; EAA13795.3; -; Genomic_DNA.
DR RefSeq; XP_319406.3; XM_319406.3.
DR AlphaFoldDB; Q7Q0Q1; -.
DR SMR; Q7Q0Q1; -.
DR STRING; 7165.AGAP010219-PA; -.
DR PaxDb; Q7Q0Q1; -.
DR GeneID; 1279642; -.
DR KEGG; aga:AgaP_AGAP010219; -.
DR CTD; 1279642; -.
DR VEuPathDB; VectorBase:AGAP010219; -.
DR eggNOG; KOG0480; Eukaryota.
DR HOGENOM; CLU_000995_3_2_1; -.
DR InParanoid; Q7Q0Q1; -.
DR OMA; KYYIAQI; -.
DR OrthoDB; 266497at2759; -.
DR PhylomeDB; Q7Q0Q1; -.
DR Proteomes; UP000007062; Chromosome 3R.
DR GO; GO:0042555; C:MCM complex; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:RHEA.
DR GO; GO:0003678; F:DNA helicase activity; IEA:UniProtKB-EC.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0003697; F:single-stranded DNA binding; IBA:GO_Central.
DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR GO; GO:0006270; P:DNA replication initiation; IEA:InterPro.
DR GO; GO:0006268; P:DNA unwinding involved in DNA replication; IBA:GO_Central.
DR GO; GO:0000727; P:double-strand break repair via break-induced replication; IBA:GO_Central.
DR GO; GO:1902969; P:mitotic DNA replication; IBA:GO_Central.
DR Gene3D; 2.40.50.140; -; 1.
DR Gene3D; 3.40.50.300; -; 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; PTHR11630; 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; SSF50249; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR PROSITE; PS00847; MCM_1; 1.
DR PROSITE; PS50051; MCM_2; 1.
PE 3: Inferred from homology;
KW ATP-binding; Cell cycle; Cell division; DNA replication; DNA-binding;
KW Helicase; Hydrolase; Metal-binding; Mitosis; Nucleotide-binding; Nucleus;
KW Reference proteome; Zinc; Zinc-finger.
FT CHAIN 1..814
FT /note="DNA replication licensing factor Mcm6"
FT /id="PRO_0000233314"
FT DOMAIN 339..545
FT /note="MCM"
FT /evidence="ECO:0000255"
FT ZN_FING 152..179
FT /note="C4-type"
FT /evidence="ECO:0000255"
FT REGION 656..696
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 521..524
FT /note="Arginine finger"
FT COMPBIAS 659..675
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 676..696
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 389..396
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255"
SQ SEQUENCE 814 AA; 92481 MW; C80797CE2B318FFD CRC64;
MDVADAHVGQ LRVRDEVGVR CQKLFLDFLE EFKEDGEIKY LKTVENLVNP DRSTLEVSFE
DVENYNQTLA TAIIEEYYRI FPYLCQSVSN FVRDRTSLKK SKECYVSFVD VPTRHKVREL
STSKIGTLIR ISGQVVRTHP VHPELVLGTF VCLDCQTEIR DVEQQFKFTN PTICRNPVCA
NRRRFMLEVD KSLFIDFQKV RIQETQAELP RGCIPRSVEV ILRAEMVETV QAGDRYDFTG
TLIVIPDVGA LQLPGAKAEI GSRHKQGDNA AEGVRGLKAL GMRDLNYKMA FLACSVQVTS
SRFGGTDMPM SEVTSQIMKD QMTPAEWNKV YEMSRDPRLY QNLINSLFPS IYGNDEVKRG
ILLMLFGGVA KTTQEKTTLR GDINVCIVGD PSTAKSQFLK QVSDFSPRAV YTSGKASSAA
GLTAAVVRDE ESFDFVIEAG ALMLADNGIC CIDEFDKMDP HDQVAIHEAM EQQTISIAKA
GVRATLNART SILAAANPIG GRYDRSKSLQ QNIQLTAPIM SRFDLFFILV DECNEVVDYA
IARKIVDLHS HIEHSLDQVY SREDVLRYIM FARQFKPVIQ PEAMALLVEN YGHLRQRDTG
TTGKSTWRIT VRQLESMIRL SEAMAKMECS EEVTERHVKE AYRLLNKSII RVEQPDIHLD
EEEGEENENV MDIGEETPED TPRTNETEEN DQDTPAVAKK KLTLSFEEYK NLSNMLVIHM
RNEESRMESE ELDREGISKT ELINWYLSQV EDQLESVEEL MERKVLIEKV IDRLIYHDQV
IIPLKQAKLG ETDQDDAGDQ DVLLVVHPNY IVES
