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Database: UniProt
Entry: A0A1S3Z556_TOBAC
LinkDB: A0A1S3Z556_TOBAC
Original site: A0A1S3Z556_TOBAC 
ID   A0A1S3Z556_TOBAC        Unreviewed;       738 AA.
AC   A0A1S3Z556;
DT   12-APR-2017, integrated into UniProtKB/TrEMBL.
DT   12-APR-2017, sequence version 1.
DT   24-JAN-2024, entry version 33.
DE   RecName: Full=DNA replication licensing factor MCM5 {ECO:0000256|RuleBase:RU368063};
DE            EC=3.6.4.12 {ECO:0000256|RuleBase:RU368063};
GN   Name=LOC107783151 {ECO:0000313|RefSeq:XP_016459610.1};
OS   Nicotiana tabacum (Common tobacco).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   asterids; lamiids; Solanales; Solanaceae; Nicotianoideae; Nicotianeae;
OC   Nicotiana.
OX   NCBI_TaxID=4097 {ECO:0000313|Proteomes:UP000084051, ECO:0000313|RefSeq:XP_016459610.1};
RN   [1] {ECO:0000313|Proteomes:UP000084051}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. TN90 {ECO:0000313|Proteomes:UP000084051};
RX   PubMed=24807620; DOI=10.1038/ncomms4833;
RA   Sierro N., Battey J.N., Ouadi S., Bakaher N., Bovet L., Willig A.,
RA   Goepfert S., Peitsch M.C., Ivanov N.V.;
RT   "The tobacco genome sequence and its comparison with those of tomato and
RT   potato.";
RL   Nat. Commun. 5:3833-3833(2014).
RN   [2] {ECO:0000313|RefSeq:XP_016459610.1}
RP   IDENTIFICATION.
RG   RefSeq;
RL   Submitted (SEP-2023) to UniProtKB.
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|ARBA:ARBA00001665,
CC         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}.
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DR   RefSeq; XP_016459610.1; XM_016604124.1.
DR   AlphaFoldDB; A0A1S3Z556; -.
DR   SMR; A0A1S3Z556; -.
DR   STRING; 4097.A0A1S3Z556; -.
DR   PaxDb; 4097-A0A1S3Z556; -.
DR   GeneID; 107783151; -.
DR   KEGG; nta:107783151; -.
DR   OMA; ITYCKTR; -.
DR   OrthoDB; 147095at2759; -.
DR   Proteomes; UP000084051; Unplaced.
DR   GO; GO:0042555; C:MCM complex; IBA:GO_Central.
DR   GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR   GO; GO:0000347; C:THO complex; 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:0003697; F:single-stranded DNA binding; IBA:GO_Central.
DR   GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR   GO; GO:0032508; P:DNA duplex unwinding; IEA:UniProtKB-UniRule.
DR   GO; GO:0006270; P:DNA replication initiation; IBA:GO_Central.
DR   GO; GO:0000727; P:double-strand break repair via break-induced replication; IBA:GO_Central.
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:UP000084051}.
FT   DOMAIN          336..542
FT                   /note="MCM"
FT                   /evidence="ECO:0000259|PROSITE:PS50051"
SQ   SEQUENCE   738 AA;  81978 MW;  9AEC6B99FA92F313 CRC64;
     MSGWDEGAVY YSDQAQFPHG GGGATGDNEN GGASRHVILR KFKEFIRNFS DKTQPNVFPY
     REALLENQTH LIINLSDLLS YERDQTLPEL LRQNPADYLP LFETAAAEVL ASLRSRVAGE
     SGEMEEPEIG EVQILLRSEQ DPMSMRSLGA QCISKLVKVS GIVIAASRTK AKATYVTLLC
     KNCKNVKIVP CRPGLGGAIV PRSCDHVPQV GEDPCPIDPW VVVPDKSKYV DQQTLKLQEN
     PEDVPTGELP RNMLLSIDRH LVQTIVPGTR LTIMGIYSIF QASNSSTSHK GAVAVRQPYI
     RVVGMDETNE ANSRGSANFT VDEKEEFQKF ASDKDAYEKI CSKIAPSIFG HVDVKKAVAC
     LLFGGSRKFL PDGVRLRGDI NVLLLGDPST AKSQFLKFVE KTAPVAVYTS GKGSSAAGLT
     ASVIRDNSSR EFYLEGGAMV LADGGVVCID EFDKMRAEDR VAIHEAMEQQ TISIAKAGIT
     TVLNSRTSVL AAANPPSGRY DDLKTAQDNI DLQTTILSRF DLIFIVKDIR MFSQDKSIAS
     HIIKVHASAE ASRDDTRTSK EYNWLKRYIQ YCRTNCHPRL SPAAASMLQE SYVKIRQQMR
     RQSNDNGEAA AIPITVRQLE AIVRLSEALA RMRLAQIANE NHVTEAIRLF QNSTMDAARS
     GINQHINLTP EMAQEIKQAE AQIKRRMGIG SHISERRLID ELTRMGMNES IVRRALIIMH
     QRDEVEYKRE RRIIVRKA
//
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