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
//