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Database: UniProt
Entry: A0A1S4B5R1_TOBAC
LinkDB: A0A1S4B5R1_TOBAC
Original site: A0A1S4B5R1_TOBAC 
ID   A0A1S4B5R1_TOBAC        Unreviewed;       743 AA.
AC   A0A1S4B5R1;
DT   12-APR-2017, integrated into UniProtKB/TrEMBL.
DT   12-APR-2017, sequence version 1.
DT   27-MAR-2024, entry version 34.
DE   RecName: Full=DNA replication licensing factor MCM5 {ECO:0000256|RuleBase:RU368063};
DE            EC=3.6.4.12 {ECO:0000256|RuleBase:RU368063};
GN   Name=LOC107804766 {ECO:0000313|RefSeq:XP_016484182.1};
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_016484182.1};
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_016484182.1}
RP   IDENTIFICATION.
RG   RefSeq;
RL   Submitted (NOV-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_016484182.1; XM_016628696.1.
DR   AlphaFoldDB; A0A1S4B5R1; -.
DR   SMR; A0A1S4B5R1; -.
DR   STRING; 4097.A0A1S4B5R1; -.
DR   PaxDb; 4097-A0A1S4B5R1; -.
DR   GeneID; 107804766; -.
DR   KEGG; nta:107804766; -.
DR   OMA; VIIVNEC; -.
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:0006270; P:DNA replication initiation; IBA:GO_Central.
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; 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          341..547
FT                   /note="MCM"
FT                   /evidence="ECO:0000259|PROSITE:PS50051"
SQ   SEQUENCE   743 AA;  82578 MW;  8431EAC1F0269255 CRC64;
     MIKIPNPEIC VSVETCSPLR HIGRICGVAC AREVPLSAEG HWRNGSRTCR KLSAPAALQR
     EKERRTEALL ENQTHLIINL SDLLSYERDQ TLPELLRQNP ADYLPLFETA AAEVLASLRS
     RVAGESGEME EPEIGEVQIL LRSEQDPMSM RSLGAQYISK LVKVSGIVIA ASRTKAKATY
     VTLLCKNCKN VKIVPCRPGL GGAIVPRSCD HVPQVGEDPC PIDPWVVVPD KSKYVDQQTL
     KLQENPEDVP TGELPRNMLL SIDRHLVQTI VPGTRLTIMG IYSVFQASNS STSHKGAVAV
     RQPYIRVVGM EETNEANSRG SANFTVDEKE EFQKFASDKD AYEKICSKIA PSIFGHVDVK
     KAVACLLFGG SRKFLPDGVR LRGDINVLLL GDPSTAKSQF LKFVEKTAPV AVYTSGKGSS
     AAGLTASVIR DNSSREFYLE GGAMVLADGG VVCIDEFDKM RAEDRVAIHE AMEQQTISIA
     KAGITTVLNS RTSVLAAANP PSGRYDDLKT AQDNIDLQTT ILSRFDLIFI VKDIRMFSQD
     KSIASHIIKV HASAEASRDD TRTSKEYNWL KRYIQYCRTN CHPRLSPAAA SMLQESYVKI
     RQQMRRQSND NGEAAAIPIT VRQLEAIVRL SEALARMRLA QIANENHVTE AIRLFQNSTM
     DAARSGINQH INLTPEMAHE IKQAEAQIKR RMGIGSHISE RRLIDELTRM GMNESIVRRA
     LIIMHQRDEV EYKRERRIIV RKA
//
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