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Database: UniProt
Entry: A0A3P8WSM9_CYNSE
LinkDB: A0A3P8WSM9_CYNSE
Original site: A0A3P8WSM9_CYNSE 
ID   A0A3P8WSM9_CYNSE        Unreviewed;       688 AA.
AC   A0A3P8WSM9;
DT   13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT   13-FEB-2019, sequence version 1.
DT   27-MAR-2024, entry version 27.
DE   RecName: Full=DNA replication licensing factor MCM6 {ECO:0000256|RuleBase:RU368064};
DE            EC=3.6.4.12 {ECO:0000256|RuleBase:RU368064};
OS   Cynoglossus semilaevis (Tongue sole).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC   Carangaria; Pleuronectiformes; Pleuronectoidei; Cynoglossidae;
OC   Cynoglossinae; Cynoglossus.
OX   NCBI_TaxID=244447 {ECO:0000313|Ensembl:ENSCSEP00000029507.1, ECO:0000313|Proteomes:UP000265120};
RN   [1] {ECO:0000313|Ensembl:ENSCSEP00000029507.1, ECO:0000313|Proteomes:UP000265120}
RP   NUCLEOTIDE SEQUENCE.
RX   PubMed=24487278;
RA   Chen S., Zhang G., Shao C., Huang Q., Liu G., Zhang P., Song W., An N.,
RA   Chalopin D., Volff J.N., Hong Y., Li Q., Sha Z., Zhou H., Xie M., Yu Q.,
RA   Liu Y., Xiang H., Wang N., Wu K., Yang C., Zhou Q., Liao X., Yang L.,
RA   Hu Q., Zhang J., Meng L., Jin L., Tian Y., Lian J., Yang J., Miao G.,
RA   Liu S., Liang Z., Yan F., Li Y., Sun B., Zhang H., Zhang J., Zhu Y., Du M.,
RA   Zhao Y., Schartl M., Tang Q., Wang J.;
RT   "Whole-genome sequence of a flatfish provides insights into ZW sex
RT   chromosome evolution and adaptation to a benthic lifestyle.";
RL   Nat. Genet. 46:253-260(2014).
RN   [2] {ECO:0000313|Ensembl:ENSCSEP00000029507.1}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (SEP-2023) to UniProtKB.
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   AlphaFoldDB; A0A3P8WSM9; -.
DR   STRING; 244447.ENSCSEP00000029507; -.
DR   Ensembl; ENSCSET00000029908.1; ENSCSEP00000029507.1; ENSCSEG00000018899.1.
DR   GeneTree; ENSGT01050000244824; -.
DR   InParanoid; A0A3P8WSM9; -.
DR   OMA; CQTEIRN; -.
DR   Proteomes; UP000265120; Chromosome 20.
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; 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:SF73; 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|ARBA:ARBA00023306, 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:UP000265120}.
FT   DOMAIN          216..417
FT                   /note="MCM"
FT                   /evidence="ECO:0000259|PROSITE:PS50051"
FT   REGION          534..584
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   688 AA;  77739 MW;  D9EEEC1866707BEA CRC64;
     MDVAAATATA ENGREMVKDE LAEKCQKLFQ AFLEEFRAGD GEVKYVREAE ELIRPEKNTL
     LVSFTDLEGF NQELATTIQE EYYRVYPFLC RAVRNFARDH GNVPLNKEFY VAIEDLPTRH
     KIRELSSMRI GTLVRISGQV VRTHPVHPEL VSGTFLCTDC QAVIKDVPQQ FKYTPPAICK
     NPVCNNRARF HLDTHKSKFI DFQKACRRHL CLSISSKTVF KSLTGNDEVK RGVLLMLFGG
     VPKTTMERTS LRGDINVCIV GDPSTAKSQF LKHVEEFSPR AVYTSGKASS AAGLTAAVVR
     DEESHEFVIE AGALMLADNG VCCIDEFDKM DLKDQVAIHE AMEQQTISIT KAGVKATLNA
     RTSILAAANP VGGCYDRSKS LKQNVNLSAP IMSRFDLFFI LVDDCNEVTD YAIARRIVDL
     HSRVQESVDR LYSLDEIRRY LLFARQFKPK ISPESEEFIV EQYKHLRQRD GSGGVSKSAW
     RITVRQLESM IRLSEAMARM HCSDEVRPKH VKEAFRLLNK SIIRVETPDI NLEQDEEMEE
     EQQNEEDNIP NGVNGHVPAV NGHINGKNGD VNAHAEPGSQ SKPSLRLSFN EYKRISNLLV
     LHLRRVEEEE ELKKSAVVNW YLKEIESEID SEEELVNRKG MIEKVIQRLV DYDHILIELS
     QAGLKGSESE SSEGEGVLVV NPNYVLED
//
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