ID A0A164TCE2_9CRUS Unreviewed; 738 AA.
AC A0A164TCE2;
DT 06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT 06-JUL-2016, sequence version 1.
DT 27-MAR-2024, entry version 31.
DE RecName: Full=DNA replication licensing factor MCM6 {ECO:0000256|RuleBase:RU368064};
DE EC=3.6.4.12 {ECO:0000256|RuleBase:RU368064};
GN ORFNames=APZ42_025209 {ECO:0000313|EMBL:KZS10347.1};
OS Daphnia magna.
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Crustacea; Branchiopoda;
OC Diplostraca; Cladocera; Anomopoda; Daphniidae; Daphnia.
OX NCBI_TaxID=35525 {ECO:0000313|EMBL:KZS10347.1, ECO:0000313|Proteomes:UP000076858};
RN [1] {ECO:0000313|EMBL:KZS10347.1, ECO:0000313|Proteomes:UP000076858}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Xinb3 {ECO:0000313|EMBL:KZS10347.1,
RC ECO:0000313|Proteomes:UP000076858};
RC TISSUE=Complete organism {ECO:0000313|EMBL:KZS10347.1};
RA Gilbert D.G., Choi J.-H., Mockaitis K., Colbourne J., Pfrender M.;
RT "EvidentialGene: Evidence-directed Construction of Genes on Genomes.";
RL Submitted (MAR-2016) to the EMBL/GenBank/DDBJ databases.
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|ARBA:ARBA00000600};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:13066;
CC Evidence={ECO:0000256|ARBA:ARBA00000600};
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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KZS10347.1}.
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DR EMBL; LRGB01001838; KZS10347.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A164TCE2; -.
DR STRING; 35525.A0A164TCE2; -.
DR Proteomes; UP000076858; Unassembled WGS sequence.
DR GO; GO:0042555; C:MCM complex; IEA:UniProtKB-UniRule.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
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:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR GO; GO:0006270; P:DNA replication initiation; IEA:UniProtKB-UniRule.
DR CDD; cd17757; MCM6; 1.
DR Gene3D; 1.20.58.870; -; 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:UP000076858}.
FT DOMAIN 296..502
FT /note="MCM"
FT /evidence="ECO:0000259|PROSITE:PS50051"
FT REGION 211..232
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 599..623
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 738 AA; 83801 MW; 5C7753D1ED9889B2 CRC64;
MDVAGAQQVQ NKVKDDVGQR CQKLFLDFLE GFEVDNEVKY LEKAKELVKP ERNTLQVSFQ
DVEKYNSNLA VTIVAEYYRV YPFLCQAVYS YVKDKAEFNV EKELYISFVD VSSKYKVRDL
KTASIGSLFQ ISGQVIRTHP VHPELVSATF VCLDCQTVIR DVEQQFKYTQ PSICRNPVCF
NRSRFMLNVN KSRFVDFQKV RIQETQAELP RGCIPRSSAR KPGEGPESEG VRGLKNLGVR
DLNYRLAFLA CSVTQSNPMF GGKDLHQEEM TAVDIKNQMS EQDWNRIYNM TQDVNLYDNL
IKSLFATIYG NDEIKRGILL MLFGGVPKKT VEHTTLRGDT NVCIVGDPST AKSQFLKQVA
EFTPRAVYTS GKASSAAGLT AAVVRDEESY EFVIEAGALM LADNGVCCID EFDKMDPRDQ
VAIHEAMEQQ TISITKAGVK ATLNARASIL AAANPIGGRY DRTKSLKQNV MMTAPIMSRF
DLFFILVDEC NEVVDYSIAR SIVDLHRRNV ESIQRVYQTE DIRRYITFAR KFQPKLTSRI
TVRQLESLIR LSEAMARMYC VSLVTKDHVK EAYRLLNKSI IRVEEPDIDL EDAEQANISV
EQDETNGVPS SEDTDKQTAS DATSDSAVQK KKISITYESY KAISNLLIMY LRRQEALDET
ESSRKSALIN WYLNEIADEI ETEQELTERK LLVERVVSRL IYQDQVIIPL SRTGLAGKEE
VTEDEDPLLV VHPNFVLE
//
