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Database: UniProt
Entry: A0A1E3I9X5_9TREE
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ID   A0A1E3I9X5_9TREE        Unreviewed;       899 AA.
AC   A0A1E3I9X5;
DT   18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT   18-JAN-2017, sequence version 1.
DT   24-JAN-2024, entry version 31.
DE   RecName: Full=DNA replication licensing factor MCM4 {ECO:0000256|RuleBase:RU368062};
DE            EC=3.6.4.12 {ECO:0000256|RuleBase:RU368062};
GN   ORFNames=L203_05036 {ECO:0000313|EMBL:ODN85420.1};
OS   Cryptococcus depauperatus CBS 7841.
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Tremellomycetes;
OC   Tremellales; Cryptococcaceae; Cryptococcus.
OX   NCBI_TaxID=1295531 {ECO:0000313|EMBL:ODN85420.1, ECO:0000313|Proteomes:UP000094043};
RN   [1] {ECO:0000313|EMBL:ODN85420.1, ECO:0000313|Proteomes:UP000094043}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CBS 7841 {ECO:0000313|EMBL:ODN85420.1,
RC   ECO:0000313|Proteomes:UP000094043};
RA   Cuomo C., Litvintseva A., Heitman J., Chen Y., Sun S., Springer D.,
RA   Dromer F., Young S., Zeng Q., Chapman S., Gujja S., Saif S., Birren B.;
RT   "Evolution of pathogenesis and genome organization in the Tremellales.";
RL   Submitted (JUN-2016) 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: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:ODN85420.1}.
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DR   EMBL; AWGK01000022; ODN85420.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1E3I9X5; -.
DR   STRING; 1295531.A0A1E3I9X5; -.
DR   VEuPathDB; FungiDB:L203_05036; -.
DR   OrthoDB; 5476523at2759; -.
DR   Proteomes; UP000094043; Unassembled WGS sequence.
DR   GO; GO:0031261; C:DNA replication preinitiation complex; 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:0043596; C:nuclear replication fork; IEA:UniProt.
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:0051301; P:cell division; IEA:UniProtKB-KW.
DR   GO; GO:0006270; P:DNA replication initiation; IEA:InterPro.
DR   GO; GO:0033260; P:nuclear DNA replication; IEA:UniProt.
DR   GO; GO:0030174; P:regulation of DNA-templated DNA replication initiation; IEA:UniProt.
DR   CDD; cd17755; MCM4; 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; 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   Cell cycle {ECO:0000313|EMBL:ODN85420.1};
KW   Cell division {ECO:0000313|EMBL:ODN85420.1};
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:UP000094043}.
FT   DOMAIN          569..780
FT                   /note="MCM"
FT                   /evidence="ECO:0000259|PROSITE:PS50051"
FT   REGION          1..164
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          503..527
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..54
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        107..126
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        142..160
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   899 AA;  98399 MW;  245EE790AA8D89B1 CRC64;
     MSSPGRNRSS SPIHFPTSSV AGTPRASRVG QLSRAQLGTS SPLHFPSSSP HPSLPAGNGF
     HAPPSQLRSE AQSSQAVRRI RDETPLFFPS SGGSTPRHAR RGDIHSSFPF SSPSLARRNQ
     PAPSVARGSS PDGMDTDGPQ TPRALGSPTL TLSATGPSQA DGNHDEIDGM VKFIWGTTIS
     LQESMNLFRD FLRGFKPKYR AVYNAEQSRQ IVEEGGIAPS SMTLYDNLPV DKADNPLYET
     YLHRLRYTGE TNLNLDALNL LSFRPTKKLY HQLVNYPQEV IPIMDQVLRD VMIELGHEEL
     EKAQVRFSEG NLSQLELGVI TDEVREVETR VYKVRPFGGE KTVNMRDLNP GDTDRLVTVK
     GLVIRATPVI PDMTTAFFRC LVCQHTVQAD IDRGRINEPE KCPRDVCGLV GTMSLIHNRS
     EFTDKQVIRL QETPDAVPDG QTPHTVSLCV YDELVDLVKP GDRVIITGIF RSIPVRVNPR
     QRSIKSLYKT YLDVVHVKRT NTSRMGFDPT TRGGEKKPPG VGVGGEDDEE ELLAREDGDV
     MGQDGDAMGP SAGAEIEQKL LELSTRPDLY DILASSLAPS IYELDDVKKG ILLQLFGGTN
     KSIAKGGGGG GPRYRGDINV LMVGDPGTSK SQILQYVHKI APRGVYTSGK GSSAVGLTAY
     VTRDPDSKQL VLESGALVLS DGGVCCIDEF DKMSDATRSV LHEVMEQQTV SIAKAGIITT
     LNARTSILAA ANPINSRYDP KLPVPANIDL PPTLISRFDL LYLVLDQVDE INDRKLAKHL
     VGLYLSDGDD TPTDNIIPLE TLAAYITYAR SKVSPVITEA AGQALVQAYV DMRKAGMDSR
     TQEKRIIATT RQLESMIRLS EAHARMKLSD TVGIEDVQEA QRLIKSALRE NDVFEDPSR
//
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