ID A0A2V3IYM1_9FLOR Unreviewed; 996 AA.
AC A0A2V3IYM1;
DT 12-SEP-2018, integrated into UniProtKB/TrEMBL.
DT 12-SEP-2018, sequence version 1.
DT 24-JAN-2024, entry version 25.
DE RecName: Full=DNA replication licensing factor MCM4 {ECO:0000256|RuleBase:RU368062};
DE EC=3.6.4.12 {ECO:0000256|RuleBase:RU368062};
GN ORFNames=BWQ96_03027 {ECO:0000313|EMBL:PXF47252.1};
OS Gracilariopsis chorda.
OC Eukaryota; Rhodophyta; Florideophyceae; Rhodymeniophycidae; Gracilariales;
OC Gracilariaceae; Gracilariopsis.
OX NCBI_TaxID=448386 {ECO:0000313|EMBL:PXF47252.1, ECO:0000313|Proteomes:UP000247409};
RN [1] {ECO:0000313|EMBL:PXF47252.1, ECO:0000313|Proteomes:UP000247409}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SKKU-2015 {ECO:0000313|EMBL:PXF47252.1,
RC ECO:0000313|Proteomes:UP000247409};
RC TISSUE=Whole body {ECO:0000313|EMBL:PXF47252.1};
RX PubMed=29688518; DOI=10.1093/molbev/msy081;
RA Lee J., Yang E.C., Graf L., Yang J.H., Qiu H., Zel Zion U., Chan C.X.,
RA Stephens T.G., Weber A.P.M., Boo G.H., Boo S.M., Kim K.M., Shin Y.,
RA Jung M., Lee S.J., Yim H.S., Lee J.H., Bhattacharya D., Yoon H.S.;
RT "Analysis of the draft genome of the red seaweed Gracilariopsis chorda
RT provides insights into genome size evolution in Rhodophyta.";
RL Mol. Biol. Evol. 0:0-0(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:RU368062}.
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:RU368062};
CC -!- SUBUNIT: Component of the MCM2-7 complex.
CC {ECO:0000256|RuleBase:RU368062}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
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:PXF47252.1}.
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DR EMBL; NBIV01000027; PXF47252.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2V3IYM1; -.
DR STRING; 448386.A0A2V3IYM1; -.
DR Proteomes; UP000247409; 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:UniProtKB-UniRule.
DR GO; GO:0006270; P:DNA replication initiation; IEA:InterPro.
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; IPR008047; MCM_4.
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:SF66; DNA REPLICATION LICENSING FACTOR MCM4; 1.
DR Pfam; PF00493; MCM; 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; PR01660; MCMPROTEIN4.
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 DNA replication {ECO:0000256|ARBA:ARBA00022705,
KW ECO:0000256|RuleBase:RU368062};
KW DNA-binding {ECO:0000256|ARBA:ARBA00023125, ECO:0000256|RuleBase:RU004070};
KW Helicase {ECO:0000256|ARBA:ARBA00022806, ECO:0000256|RuleBase:RU368062};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU368062};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW ECO:0000256|RuleBase:RU004070};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242, ECO:0000256|RuleBase:RU368062};
KW Reference proteome {ECO:0000313|Proteomes:UP000247409}.
FT DOMAIN 547..763
FT /note="MCM"
FT /evidence="ECO:0000259|PROSITE:PS50051"
FT REGION 1..139
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 174..243
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 778..800
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 7..78
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 125..139
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 226..242
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 996 AA; 109964 MW; 92F09FCD2DAD57C7 CRC64;
MADDPPAQNN RSPSPATRSS PRSTRSSPRN GSASPRPSSS RRSPRNGPSQ SSRPNAAARR
SVPPSRSRTP SVRHTPISTP SAARPPRAPP RSPADSSVVQ PTPQPVRALV PGPHRREFGL
SPIRFQTPTP HNGSESVDAR ANQTQTYLWD TNIAVEDCEQ RVVAFVRGFR LSQQSQSGEA
SAADLVLSQP SPPPRTPVTP QPLVNDDEEI RPGPAPAPAT LQPAEHPSPA AQSQSGRVDS
TDQVPVQEPF YMDVLRHLAE TGDSILNLDL THLHSFDSLL YRRVIEHPED LITIFDATIN
RIFCETFHEE AEAIEQNRRK SIQTRMYNLL SEQVQSMREL NPGDISKMVS IRGMVIRAST
VIPDIQAAMY RCTKCHAMKE VSIAHGRIEE PRKCMSCNSR DSFSLIHSRS QFADKQMVRL
QEAPENIPKG ETPATFTLVM YDSLVDSVKP GDRVEITGML RAVPVRVNPK NRTVRSVFRT
YIDCVHVRVL HHNRSRQDLE SSVAQKDVLG QPTEPNADVA FNHETVTTEQ KRQQQQFFEE
LSCHPELYER LTNSIAPSIF GMEDEKKGVL LQLFGGASKD GQGQANAESV GDGSSRFRSA
INVLLVGDPG TSKSQLLHSV HRLAPRGVYT SGRGSSAVGL TAYVTRDPDS DDYVLESGAL
VLSDRGICCI DEFDKMSEYA RSVLHEAMEQ QTVSIAKAGI IATLNARTSV LAAANPVNSR
YDTSKPVVEN IDLPPTLLTR FDLVFLVLDA PNEDSDRRLA NHIVSLFFKN YDEGQNLKKE
GENTTKREDD LPDELDFDEG IPEAPSYTSG KLLDAKTLTE YIAYAREKVD PILTESAAEA
LVNGYVEMRS AGRGGGTITA TPRQLESLIR LAEAHARMQL NKEVEEEDVK EAFRLVKSAL
RMSALDPNTG KIDMNLFAAG KSRGMDTMSQ HLERAIIDKL KEKSESGGLQ TNKLLEALRQ
TSDAVITPGD LREALRRLEQ QEEVVLTHRG TLVQLV
//
