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Database: UniProt
Entry: A0A024GLJ0_9STRA
LinkDB: A0A024GLJ0_9STRA
Original site: A0A024GLJ0_9STRA 
ID   A0A024GLJ0_9STRA        Unreviewed;       809 AA.
AC   A0A024GLJ0;
DT   09-JUL-2014, integrated into UniProtKB/TrEMBL.
DT   09-JUL-2014, sequence version 1.
DT   24-JAN-2024, entry version 52.
DE   RecName: Full=DNA replication licensing factor MCM7 {ECO:0000256|RuleBase:RU365012};
DE            EC=3.6.4.12 {ECO:0000256|RuleBase:RU365012};
GN   Name=MCM7 {ECO:0000256|RuleBase:RU365012};
GN   ORFNames=BN9_087640 {ECO:0000313|EMBL:CCI47748.1};
OS   Albugo candida.
OC   Eukaryota; Sar; Stramenopiles; Oomycota; Albuginales; Albuginaceae; Albugo.
OX   NCBI_TaxID=65357 {ECO:0000313|EMBL:CCI47748.1, ECO:0000313|Proteomes:UP000053237};
RN   [1] {ECO:0000313|EMBL:CCI47748.1, ECO:0000313|Proteomes:UP000053237}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Ac Nc2 {ECO:0000313|EMBL:CCI47748.1,
RC   ECO:0000313|Proteomes:UP000053237};
RA   Gardiner A., Kemen E., Schultz-Larsen T., MacLean D., Van Oosterhout C.,
RA   Jones J.D.G.;
RT   "Recombination and specialization in a pathogen metapopulation.";
RL   Submitted (MAY-2012) 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:RU365012}.
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:RU365012};
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123,
CC       ECO:0000256|RuleBase:RU365012}.
CC   -!- SIMILARITY: Belongs to the MCM family. {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:CCI47748.1}.
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DR   EMBL; CAIX01000184; CCI47748.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A024GLJ0; -.
DR   STRING; 65357.A0A024GLJ0; -.
DR   InParanoid; A0A024GLJ0; -.
DR   OrthoDB; 147095at2759; -.
DR   Proteomes; UP000053237; Unassembled WGS sequence.
DR   GO; GO:0042555; C:MCM complex; IEA:InterPro.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
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: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; IPR008050; MCM7.
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:SF26; DNA REPLICATION LICENSING FACTOR MCM7; 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; PR01663; MCMPROTEIN7.
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:RU365012};
KW   DNA replication {ECO:0000256|ARBA:ARBA00022705,
KW   ECO:0000256|RuleBase:RU365012};
KW   DNA-binding {ECO:0000256|ARBA:ARBA00023125, ECO:0000256|RuleBase:RU004070};
KW   Helicase {ECO:0000256|ARBA:ARBA00022806, ECO:0000256|RuleBase:RU365012};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU365012};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW   ECO:0000256|RuleBase:RU004070};
KW   Nucleus {ECO:0000256|ARBA:ARBA00023242, ECO:0000256|RuleBase:RU365012};
KW   Reference proteome {ECO:0000313|Proteomes:UP000053237}.
FT   DOMAIN          383..589
FT                   /note="MCM"
FT                   /evidence="ECO:0000259|PROSITE:PS50051"
FT   REGION          1..50
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..49
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   809 AA;  90326 MW;  2CBE6EBEA7354CE1 CRC64;
     MNAAIPRASL NSSSNRQQQA SSSRHLGSDS QAGTHLLNSS NSTVPYNPSA GYQDDKAKCI
     RFLQTFTSHT DNSNTGPKYM TILQQVANRE RISIPISLDD VQIFDGEDDA LVYRIGRNTK
     RYISLFAEAV EECLPAPTRD LSGTEDILDV LRMHHPEETG QNHTEETDPE SARKSNIPRA
     LMRRFEIHLV PGIKLKSVAI RHVKARHVGS LVRITGMVTR VSNVKPLLTV ATYTCEICAF
     EVYQEVNARQ FTPLSQCPSD RCKTNRTNGR LVLQTKASKF EKFQELKFQE TPDQVPMGHV
     PRSLTVYLRG ELTRTCEPGS IVTICGIFLP LPISAQRQMQ MGLLTETYLE ATDVKNHKTR
     YSAMESNEAM ETQVLRLQQK SNIYEILSQS IAPEIYGHED VKKALLLLMI GGVTKRMDEG
     MRLRGDINIL LIGDPGVAKS QLLKHIVSIA PRGVYTTGKG SSGVGLTAAV IRDSITREMT
     LEGGALVLAD MGICAIDEFD KMEESDRTAI HEVMEQQTVS IAKAGITTTL NARTSVLAAA
     NPIYGRYNPK LSASQNINLS NALLSRFDLI FLILDHANYD RDETLARHVT YVHRYAKNPK
     MNFEPVRPEV LRYFVAIAKQ YTPHIPSELS GYIVEAYVTL RQQDANDQMR EMRQNGRQYA
     SDSNGNGNEG QTAMTARQLL SILRMSQALA RLRFATDVMH QDVDEAIRLV YASKASLLNQ
     TEDYTKNGRG HAINGTGFIG SSDVMSTIYR MVLEYAKDKD ICAVTIADIE PIVFRKGYTM
     QQLRSCIKYY SELDVMQMNA AGTTLHFVA
//
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