GenomeNet

Database: UniProt
Entry: A0A0J9X361_GEOCN
LinkDB: A0A0J9X361_GEOCN
Original site: A0A0J9X361_GEOCN 
ID   A0A0J9X361_GEOCN        Unreviewed;       852 AA.
AC   A0A0J9X361;
DT   14-OCT-2015, integrated into UniProtKB/TrEMBL.
DT   14-OCT-2015, sequence version 1.
DT   08-NOV-2023, entry version 45.
DE   RecName: Full=DNA replication licensing factor MCM3 {ECO:0000256|RuleBase:RU368061};
DE            EC=3.6.4.12 {ECO:0000256|RuleBase:RU368061};
GN   ORFNames=BN980_GECA01s09338g {ECO:0000313|EMBL:CDO51617.1};
OS   Geotrichum candidum (Oospora lactis) (Dipodascus geotrichum).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Dipodascaceae; Geotrichum.
OX   NCBI_TaxID=1173061 {ECO:0000313|EMBL:CDO51617.1, ECO:0000313|Proteomes:UP000242525};
RN   [1] {ECO:0000313|EMBL:CDO51617.1, ECO:0000313|Proteomes:UP000242525}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CLIB 918 {ECO:0000313|EMBL:CDO51617.1,
RC   ECO:0000313|Proteomes:UP000242525};
RA   Casaregola S.;
RL   Submitted (MAR-2014) 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:RU368061}.
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:RU368061};
CC   -!- SUBUNIT: Component of the MCM2-7 complex.
CC       {ECO:0000256|RuleBase:RU368061}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123,
CC       ECO:0000256|RuleBase:RU368061}.
CC   -!- SIMILARITY: Belongs to the MCM family. {ECO:0000256|RuleBase:RU004070}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; CCBN010000001; CDO51617.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0J9X361; -.
DR   STRING; 1173061.A0A0J9X361; -.
DR   OrthoDB; 5476523at2759; -.
DR   Proteomes; UP000242525; Unassembled WGS sequence.
DR   GO; GO:0071162; C:CMG complex; IEA:UniProt.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProt.
DR   GO; GO:0042555; C:MCM complex; IEA:UniProtKB-UniRule.
DR   GO; GO:0005656; C:nuclear pre-replicative complex; IEA:UniProt.
DR   GO; GO:0031298; C:replication fork protection complex; IEA:UniProt.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR   GO; GO:0003688; F:DNA replication origin binding; IEA:UniProt.
DR   GO; GO:0004386; F:helicase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0006270; P:DNA replication initiation; IEA:InterPro.
DR   GO; GO:0006268; P:DNA unwinding involved in DNA replication; IEA:UniProt.
DR   GO; GO:0000727; P:double-strand break repair via break-induced replication; IEA:UniProt.
DR   GO; GO:0006267; P:pre-replicative complex assembly involved in nuclear cell cycle DNA replication; IEA:UniProt.
DR   GO; GO:0030174; P:regulation of DNA-templated DNA replication initiation; IEA:UniProt.
DR   CDD; cd17754; MCM3; 1.
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; IPR003593; AAA+_ATPase.
DR   InterPro; IPR031327; MCM.
DR   InterPro; IPR008046; Mcm3.
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:SF46; DNA REPLICATION LICENSING FACTOR MCM3; 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; PR01659; MCMPROTEIN3.
DR   SMART; SM00382; AAA; 1.
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:RU368061};
KW   DNA-binding {ECO:0000256|ARBA:ARBA00023125, ECO:0000256|RuleBase:RU004070};
KW   Helicase {ECO:0000256|ARBA:ARBA00022806, ECO:0000256|RuleBase:RU368061};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU368061};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW   ECO:0000256|RuleBase:RU004070};
KW   Nucleus {ECO:0000256|ARBA:ARBA00023242, ECO:0000256|RuleBase:RU368061}.
FT   DOMAIN          303..509
FT                   /note="MCM"
FT                   /evidence="ECO:0000259|PROSITE:PS50051"
FT   REGION          521..543
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          682..774
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        682..705
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        706..740
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        751..774
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   852 AA;  95305 MW;  6FE80C41500A1AAF CRC64;
     MSDNRFFDRE DALMSERMAV FTEFLDHPNG PTRYKDHIYL MLQKQERRLT ISLDELREFD
     KTFWRGVLNH PADYLPAMNS ALRETVFAVR DPRIHQIDEN ESFYVAFKGT FGDHFVNPRT
     IHATQLSKLV CIEGIVTRCS LVRPKIVRSV HYCENTGQFH SRDYRDPAVS FDPIPTTTVY
     PTEDGQNNPL ITEYGYSTYK DHQTISIQEM PEKAPAGQLP RGIDVILDDD LVDAAKPGDR
     IQLVGVYRSM GSNTQSQSST FKSLILATNI ILLSTKGNGD TAMQNITDTD VRNINKVSRK
     SNIFELLSQS LAPSIYGHDY IKKAILLMLL GGVEKNLDNG THLRGDINIL MVGDPSTAKS
     QMLRFVLNTA NLAIATTGRG SSGVGLTAAV TTDKETGERR LEAGAMVLAD RGVVCIDEFD
     KMSDVDRVAI HEVMEQQTVT IAKAGIHTSL NARCSVIAAA NPIYGQYDTH KDPHQNIALP
     DSLLSRFDLL FVVTDDVNDV RDRQISEHVL RMHRFLAPGA EEGVPVRENQ SQNLSVGDQD
     ERSADRDLPV YERFNSLLHA GLANSQQNPE DIEILSIPFI KKYIQYAKKR VQPILTQPAS
     DYIVATYAAL RNDTLGNNQR HTSPITARTL ETLIRLSTAH AKARLSNRIE EKDAEVAEEL
     LRFALFKEVI TNKNKRRRIN REPSEELAER TANIHIDDRE EVTANTSARV TRSQAVPSRT
     QEPPSSSMPP SSSVGLPSSL PFREDSQEPW PSQEDSQPSL THASQQSTNG SRLAPITGIT
     RTRLLQFQKA AGILLGSADF AEDTIPEERL TTAINASLPD NEKFSQQEIE SALQQMSDDN
     KIMWSGNVIY KM
//
DBGET integrated database retrieval system