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Database: UniProt
Entry: A0A2P7YL30_9PEZI
LinkDB: A0A2P7YL30_9PEZI
Original site: A0A2P7YL30_9PEZI 
ID   A0A2P7YL30_9PEZI        Unreviewed;       733 AA.
AC   A0A2P7YL30;
DT   23-MAY-2018, integrated into UniProtKB/TrEMBL.
DT   23-MAY-2018, sequence version 1.
DT   13-SEP-2023, entry version 25.
DE   RecName: Full=DNA replication licensing factor MCM5 {ECO:0000256|RuleBase:RU368063};
DE            EC=3.6.4.12 {ECO:0000256|RuleBase:RU368063};
GN   ORFNames=B9Z65_1852 {ECO:0000313|EMBL:PSK36669.1}, C1H76_0877
GN   {ECO:0000313|EMBL:TKX26723.1};
OS   Elsinoe australis.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC   Dothideomycetidae; Myriangiales; Elsinoaceae; Elsinoe.
OX   NCBI_TaxID=40998 {ECO:0000313|EMBL:PSK36669.1, ECO:0000313|Proteomes:UP000243723};
RN   [1] {ECO:0000313|EMBL:PSK36669.1, ECO:0000313|Proteomes:UP000243723}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NL1 {ECO:0000313|EMBL:PSK36669.1,
RC   ECO:0000313|Proteomes:UP000243723};
RA   Cheng Q.;
RT   "Draft genome sequence of Elsinoe australis.";
RL   Submitted (MAY-2017) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:TKX26723.1, ECO:0000313|Proteomes:UP000308133}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Hillstone_2 {ECO:0000313|EMBL:TKX26723.1,
RC   ECO:0000313|Proteomes:UP000308133};
RA   Stodart B., Jeffress S., Ash G., Arun Chinnappa K.;
RT   "Draft genome sequences of Elsinoe sp., causing black scab on jojoba.";
RL   Submitted (FEB-2018) 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   -!- 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:PSK36669.1}.
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DR   EMBL; NHZQ01000419; PSK36669.1; -; Genomic_DNA.
DR   EMBL; PTQR01000011; TKX26723.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2P7YL30; -.
DR   STRING; 40998.A0A2P7YL30; -.
DR   Proteomes; UP000243723; Unassembled WGS sequence.
DR   Proteomes; UP000308133; 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:0003688; F:DNA replication origin binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0004386; F:helicase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
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:0033260; P:nuclear DNA replication; IEA:UniProt.
DR   GO; GO:0030174; P:regulation of DNA-templated DNA replication initiation; 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:UP000243723}.
FT   DOMAIN          318..524
FT                   /note="MCM"
FT                   /evidence="ECO:0000259|PROSITE:PS50051"
SQ   SEQUENCE   733 AA;  81163 MW;  8EA436F028C9CBB2 CRC64;
     MDRQSIYTAS VFPEQTDENE DISRRKILQK LVSFILEFHV DNTFKYRDQI RENVLSKQYY
     CDVDIADLVA FDETVAHQLN NEPGEIIPLF ESAIKQCTQK IVYPSQRDVE LPEHQLLLHS
     SVNQTLIRGL TATHVSHLVR IPGIVIGAST LSSKSTVLHI QCRNCQHSQN IPVNGGFTGV
     SLPRTCARVQ LPGENSAKCP LDPYFVVHER CQFIDQQVIK LQEAPDDVPV GELPRHILIS
     ADRYLTNRVV PGSRCTVMGV FSIYQAAGKK NAAAVAIRNP YLRAVGIQTD VDHTAKGGAN
     FTAEEEQEFL EMSRRPDIYE RFAECIAPSI YGNKDIKKAI TCLLMGGSKK ILPDGMKLRG
     DINVLLLGDP GTAKSQLLKF VEKAAPIAIY TSGKGSSAAG LTASVQRDHS SREFYLEGGA
     MVLADGGVVC IDEFDKMRDE DRVAIHEAME QQTISIAKAG ITTILNARTS VLAAANPIFG
     RYDDMKSPGE NIDFQTTILS RFDLIFIVRD DHDRNRDERM AKHVMGIHMG GPGLQDDSSA
     HVGSIPVEKM KRYISYCKSR CAPRLSAEAA EKLSSHFVSI RRQVAQAEAS ANQRSSIPIT
     VRQLESLVRI TESLAKLTLS PIATEAHVDE AIRLFLGSTM DAVLSQGGEA GARNNGAGLN
     GNRELMDEIG KVEEELRRRL PIGWSTSLAS LQREFCERKG YSESSLHRAL WALQRRESVQ
     FRRGGAQVYR SGV
//
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