GenomeNet

Database: UniProt
Entry: A0A0D1XXT6_EXOME
LinkDB: A0A0D1XXT6_EXOME
Original site: A0A0D1XXT6_EXOME 
ID   A0A0D1XXT6_EXOME        Unreviewed;       724 AA.
AC   A0A0D1XXT6;
DT   29-APR-2015, integrated into UniProtKB/TrEMBL.
DT   29-APR-2015, sequence version 1.
DT   27-MAR-2024, entry version 47.
DE   RecName: Full=DNA replication licensing factor MCM5 {ECO:0000256|RuleBase:RU368063};
DE            EC=3.6.4.12 {ECO:0000256|RuleBase:RU368063};
GN   ORFNames=PV10_04251 {ECO:0000313|EMBL:KIV93006.1};
OS   Exophiala mesophila (Black yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Chaetothyriomycetidae; Chaetothyriales; Herpotrichiellaceae; Exophiala.
OX   NCBI_TaxID=212818 {ECO:0000313|EMBL:KIV93006.1, ECO:0000313|Proteomes:UP000054302};
RN   [1] {ECO:0000313|EMBL:KIV93006.1, ECO:0000313|Proteomes:UP000054302}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CBS 40295 {ECO:0000313|EMBL:KIV93006.1,
RC   ECO:0000313|Proteomes:UP000054302};
RG   The Broad Institute Genomics Platform;
RA   Cuomo C., de Hoog S., Gorbushina A., Stielow B., Teixiera M.,
RA   Abouelleil A., Chapman S.B., Priest M., Young S.K., Wortman J., Nusbaum C.,
RA   Birren B.;
RT   "The Genome Sequence of Exophiala mesophila CBS40295.";
RL   Submitted (JAN-2015) 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:RU368063}.
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:RU368063};
CC   -!- SUBUNIT: Component of the MCM2-7 complex.
CC       {ECO:0000256|RuleBase:RU368063}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123,
CC       ECO:0000256|RuleBase:RU368063}.
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; KN847522; KIV93006.1; -; Genomic_DNA.
DR   RefSeq; XP_016224580.1; XM_016368792.1.
DR   AlphaFoldDB; A0A0D1XXT6; -.
DR   STRING; 212818.A0A0D1XXT6; -.
DR   GeneID; 27322096; -.
DR   VEuPathDB; FungiDB:PV10_04251; -.
DR   HOGENOM; CLU_000995_7_2_1; -.
DR   OMA; ITYCKTR; -.
DR   OrthoDB; 5476523at2759; -.
DR   Proteomes; UP000054302; 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:0003688; F:DNA replication origin binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0004386; F:helicase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0032508; P:DNA duplex unwinding; IEA:UniProtKB-UniRule.
DR   GO; GO:0006270; P:DNA replication initiation; IEA:UniProtKB-UniRule.
DR   GO; GO:0006279; P:premeiotic DNA replication; IEA:UniProt.
DR   CDD; cd17756; MCM5; 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; IPR008048; MCM5.
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:SF42; DNA REPLICATION LICENSING FACTOR MCM5; 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; PR01661; MCMPROTEIN5.
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|RuleBase:RU368063};
KW   DNA replication {ECO:0000256|ARBA:ARBA00022705,
KW   ECO:0000256|RuleBase:RU368063};
KW   DNA-binding {ECO:0000256|ARBA:ARBA00023125, ECO:0000256|RuleBase:RU004070};
KW   Helicase {ECO:0000256|ARBA:ARBA00022806, ECO:0000256|RuleBase:RU368063};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU368063};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW   ECO:0000256|RuleBase:RU004070};
KW   Nucleus {ECO:0000256|ARBA:ARBA00023242, ECO:0000256|RuleBase:RU368063};
KW   Reference proteome {ECO:0000313|Proteomes:UP000054302}.
FT   DOMAIN          319..525
FT                   /note="MCM"
FT                   /evidence="ECO:0000259|PROSITE:PS50051"
SQ   SEQUENCE   724 AA;  80244 MW;  B8CEE369AA829CB6 CRC64;
     MDSRSTYSLS VLAPLYDAGS EPRTELQSKL KDFVLAFQID GSYIYRDQLR ENVLVKQYFC
     DIDLAHLISY DEELAHKLTT DPSDVIPLFE AALKQCTQRI VYPQSPSIDL PQHQLLLNSS
     VSHISIRDLN ATNVSHLVRI PGIVIGASTM SSKATLLNMR CRNCGHTKNL VVEGGFSGIS
     LPRQCGHTKE PGQEAGDSCP LDPYFVVHEK SQFIDQQILK LQEAPDQVPV GELPRHILIS
     ADRYLTNRVV PGSRCTVMGV FSIYQQNKGA KKDSAVAIRN PYLRAVGITT DVDHNNLAAT
     SFSEEEIQEF EEMSRLPDLY DRFARCIAPS IYGNLDIKKA IACLLMGGSK KVLPDGMKLR
     GDINVLLLGD PGTAKSQLLK FVEKVSPIAI YTSGKGSSAA GLTASVQRDT QSREFYLEGG
     AMVLADGGVV CIDEFDKMRD EDRVAIHEAM EQQTISIAKA GITTILNART SVLAAANPIF
     GRYDDLKSPG ENIDFQTTIL SRFDMIFIVR DDHDRNRDER IAKHVMSIQM GGQGVEEQAE
     SEFGVEKMKR YIRFCKSRCA PRLSYAATEK LSSHFVSIRN RVAQAERNSN VRSSIPITVR
     QLEAIIRITE SLAKLTLSAT AEEHHVDEAI RLFLASTMDA VTQGEGAGGM GGNRELMDEV
     SKVEEELRRR LPIGWSTSLG TLRREFVQGR GYSEAALARA LHVLQRRETV RLRNGGSQVY
     RSGV
//
DBGET integrated database retrieval system