ID Q4QI01_LEIMA Unreviewed; 895 AA.
AC Q4QI01;
DT 19-JUL-2005, integrated into UniProtKB/TrEMBL.
DT 19-JUL-2005, sequence version 1.
DT 27-MAR-2024, entry version 124.
DE RecName: Full=DNA replication licensing factor MCM4 {ECO:0000256|RuleBase:RU368062};
DE EC=3.6.4.12 {ECO:0000256|RuleBase:RU368062};
GN ORFNames=LMJF_09_0250 {ECO:0000313|EMBL:CAJ02400.1};
OS Leishmania major.
OC Eukaryota; Discoba; Euglenozoa; Kinetoplastea; Metakinetoplastina;
OC Trypanosomatida; Trypanosomatidae; Leishmaniinae; Leishmania.
OX NCBI_TaxID=5664 {ECO:0000313|EMBL:CAJ02400.1, ECO:0000313|Proteomes:UP000000542};
RN [1] {ECO:0000313|EMBL:CAJ02400.1, ECO:0000313|Proteomes:UP000000542}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MHOM/IL/81/Friedlin {ECO:0000313|Proteomes:UP000000542};
RX PubMed=16020728; DOI=10.1126/science.1112680;
RA Ivens A.C., Peacock C.S., Worthey E.A., Murphy L., Aggarwal G.,
RA Berriman M., Sisk E., Rajandream M.A., Adlem E., Aert R., Anupama A.,
RA Apostolou Z., Attipoe P., Bason N., Bauser C., Beck A., Beverley S.M.,
RA Bianchettin G., Borzym K., Bothe G., Bruschi C.V., Collins M., Cadag E.,
RA Ciarloni L., Clayton C., Coulson R.M., Cronin A., Cruz A.K., Davies R.M.,
RA De Gaudenzi J., Dobson D.E., Duesterhoeft A., Fazelina G., Fosker N.,
RA Frasch A.C., Fraser A., Fuchs M., Gabel C., Goble A., Goffeau A.,
RA Harris D., Hertz-Fowler C., Hilbert H., Horn D., Huang Y., Klages S.,
RA Knights A., Kube M., Larke N., Litvin L., Lord A., Louie T., Marra M.,
RA Masuy D., Matthews K., Michaeli S., Mottram J.C., Muller-Auer S.,
RA Munden H., Nelson S., Norbertczak H., Oliver K., O'neil S., Pentony M.,
RA Pohl T.M., Price C., Purnelle B., Quail M.A., Rabbinowitsch E.,
RA Reinhardt R., Rieger M., Rinta J., Robben J., Robertson L., Ruiz J.C.,
RA Rutter S., Saunders D., Schafer M., Schein J., Schwartz D.C., Seeger K.,
RA Seyler A., Sharp S., Shin H., Sivam D., Squares R., Squares S., Tosato V.,
RA Vogt C., Volckaert G., Wambutt R., Warren T., Wedler H., Woodward J.,
RA Zhou S., Zimmermann W., Smith D.F., Blackwell J.M., Stuart K.D.,
RA Barrell B., Myler P.J.;
RT "The genome of the kinetoplastid parasite, Leishmania major.";
RL Science 309:436-442(2005).
RN [2] {ECO:0000313|EMBL:CAJ02400.1, ECO:0000313|Proteomes:UP000000542}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MHOM/IL/81/Friedlin {ECO:0000313|Proteomes:UP000000542};
RX PubMed=22038252; DOI=10.1101/gr.122945.111;
RA Rogers M.B., Hilley J.D., Dickens N.J., Wilkes J., Bates P.A.,
RA Depledge D.P., Harris D., Her Y., Herzyk P., Imamura H., Otto T.D.,
RA Sanders M., Seeger K., Dujardin J.C., Berriman M., Smith D.F.,
RA Hertz-Fowler C., Mottram J.C.;
RT "Chromosome and gene copy number variation allow major structural change
RT between species and strains of Leishmania.";
RL Genome Res. 21:2129-2142(2011).
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 -!- SIMILARITY: Belongs to the MCM family. {ECO:0000256|ARBA:ARBA00008010,
CC ECO:0000256|RuleBase:RU004070}.
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DR EMBL; FR796405; CAJ02400.1; -; Genomic_DNA.
DR RefSeq; XP_001681197.1; XM_001681145.1.
DR AlphaFoldDB; Q4QI01; -.
DR STRING; 5664.Q4QI01; -.
DR EnsemblProtists; CAJ02400; CAJ02400; LMJF_09_0250.
DR GeneID; 5649452; -.
DR KEGG; lma:LMJF_09_0250; -.
DR VEuPathDB; TriTrypDB:LmjF.09.0250; -.
DR VEuPathDB; TriTrypDB:LMJFC_090008900; -.
DR VEuPathDB; TriTrypDB:LMJLV39_090007900; -.
DR VEuPathDB; TriTrypDB:LMJSD75_090007600; -.
DR eggNOG; KOG0478; Eukaryota.
DR HOGENOM; CLU_000995_7_2_1; -.
DR InParanoid; Q4QI01; -.
DR OMA; TEIGDGW; -.
DR Proteomes; UP000000542; Chromosome 9.
DR GO; GO:0042555; C:MCM complex; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR GO; GO:0003678; F:DNA helicase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0003697; F:single-stranded DNA binding; IBA:GO_Central.
DR GO; GO:0006271; P:DNA strand elongation involved in DNA replication; IBA:GO_Central.
DR GO; GO:0006268; P:DNA unwinding involved in DNA replication; IBA:GO_Central.
DR GO; GO:0000727; P:double-strand break repair via break-induced replication; IBA:GO_Central.
DR GO; GO:1902975; P:mitotic DNA replication initiation; IBA:GO_Central.
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; IPR003593; AAA+_ATPase.
DR InterPro; IPR031327; MCM.
DR InterPro; IPR008047; MCM_4.
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; SM00382; AAA; 1.
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; PS50051; MCM_2; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|RuleBase:RU004070};
KW DNA replication {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}; Nucleus {ECO:0000256|RuleBase:RU368062};
KW Reference proteome {ECO:0000313|Proteomes:UP000000542}.
FT DOMAIN 380..601
FT /note="MCM"
FT /evidence="ECO:0000259|PROSITE:PS50051"
FT REGION 612..671
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 895 AA; 97293 MW; A1C251BEA9EB4FEE CRC64;
MQQRSEEYSY IWGTGIAMEV FRDEFRRYLE TFALGQVVVD PSRRTLPSSG GGAAAARSSV
SDTAAAAAAE YALQEKYYLK ELLRMHMQGR STLEVDFTWL QRVAPRLYVQ TVHHPTECLQ
MMSAVADEVY RDVLLLRHGI EVAEDVLITV AAKKLPSMWT LKQLSPQHIE QLLSIKGMVI
RVSKIVPEIR VACFQCWNCQ YQERSVSGDK GRIFEPTRCA HCGKTYSFKL QHNLSLYEDK
QLIKVQESPE HVADGETPIS IGVVVYGSMV DAVVPGDRVI VTGVYRSTPI RLNANTRIIK
SIFATHIDAV HIELVRATRA SEAGAKKGCF ANGNATGTGL HVSTPTLATA KNAEGDLSSA
VLMDTARLDM FHSLAHRPDI YDVLLHSFAR TIWGHDDVKR GILAQLFGGT AKTFVFSERI
GSGAAATTSS NSAVFRSELN VLLCGDPGVA KSQLLTQVHE IAPRGVYTSG KGSSSVGLTA
FVVQDSDTGE LVLEPGALVL SDRGLCCIDE FDKMNEATRS VLHEVMEQQT LSIAKAGIIA
QLNARTSILA AANPKDSQWN AQLNVVENLQ IEPTLLSRFD LIFLLLDCHD SVEDRRLAAH
VLSLYMDTSR SARTPRAVNS GSGAAGRRVP PQGGCSDDDS GEEGEATQWR STARAGQPTA
APDDATGTAS THVDAATGLP VEVQMELHGE VFLQGPPDAP YMPASILSEY IALARETIFP
KLTEASHKML ARCYVELRQA RGSSCTVSAT LRQLESMIRL SEARAKMRYG SEVSVEDVVE
AKRIISAALK KAATDPTTGL INLDMFHAAD PGKNTVEGNM RRLEELLKRR YLAQGRHTVS
VAELRSVFNE QQSGAARPVA PAQFVEFLAL LSGGDVVQSF TATTVTLAMA GAAPM
//
