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Database: UniProt
Entry: Q4QC77_LEIMA
LinkDB: Q4QC77_LEIMA
Original site: Q4QC77_LEIMA 
ID   Q4QC77_LEIMA            Unreviewed;       786 AA.
AC   Q4QC77;
DT   19-JUL-2005, integrated into UniProtKB/TrEMBL.
DT   19-JUL-2005, sequence version 1.
DT   27-MAR-2024, entry version 93.
DE   RecName: Full=ATP-dependent DNA helicase {ECO:0000256|RuleBase:RU363044};
DE            EC=3.6.4.12 {ECO:0000256|RuleBase:RU363044};
GN   ORFNames=LMJF_21_1190 {ECO:0000313|EMBL:CAJ04624.1};
OS   Leishmania major.
OC   Eukaryota; Discoba; Euglenozoa; Kinetoplastea; Metakinetoplastina;
OC   Trypanosomatida; Trypanosomatidae; Leishmaniinae; Leishmania.
OX   NCBI_TaxID=5664 {ECO:0000313|EMBL:CAJ04624.1, ECO:0000313|Proteomes:UP000000542};
RN   [1] {ECO:0000313|EMBL:CAJ04624.1, 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:CAJ04624.1, 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   -!- 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:RU363044};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000256|ARBA:ARBA00001946,
CC         ECO:0000256|RuleBase:RU363044};
CC   -!- SUBUNIT: Monomer. {ECO:0000256|ARBA:ARBA00011245}.
CC   -!- SIMILARITY: Belongs to the helicase family. PIF1 subfamily.
CC       {ECO:0000256|ARBA:ARBA00009781}.
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DR   EMBL; FR796417; CAJ04624.1; -; Genomic_DNA.
DR   RefSeq; XP_001683071.1; XM_001683019.1.
DR   AlphaFoldDB; Q4QC77; -.
DR   STRING; 5664.Q4QC77; -.
DR   EnsemblProtists; CAJ04624; CAJ04624; LMJF_21_1190.
DR   GeneID; 5651678; -.
DR   KEGG; lma:LMJF_21_1190; -.
DR   VEuPathDB; TriTrypDB:LmjF.21.1190; -.
DR   VEuPathDB; TriTrypDB:LMJFC_210021300; -.
DR   VEuPathDB; TriTrypDB:LMJLV39_210020000; -.
DR   VEuPathDB; TriTrypDB:LMJSD75_210020200; -.
DR   eggNOG; KOG0987; Eukaryota.
DR   HOGENOM; CLU_356976_0_0_1; -.
DR   InParanoid; Q4QC77; -.
DR   OMA; KTEWLLH; -.
DR   Proteomes; UP000000542; Chromosome 21.
DR   GO; GO:0005739; C:mitochondrion; IBA:GO_Central.
DR   GO; GO:0031981; C:nuclear lumen; IBA:GO_Central.
DR   GO; GO:0005634; C:nucleus; ISO:GeneDB.
DR   GO; GO:0005657; C:replication fork; IBA:GO_Central.
DR   GO; GO:0043139; F:5'-3' DNA helicase activity; IBA:GO_Central.
DR   GO; GO:0005524; F:ATP binding; ISO:GeneDB.
DR   GO; GO:0016887; F:ATP hydrolysis activity; IEA:RHEA.
DR   GO; GO:0000287; F:magnesium ion binding; ISO:GeneDB.
DR   GO; GO:0032508; P:DNA duplex unwinding; IBA:GO_Central.
DR   GO; GO:0006310; P:DNA recombination; IEA:UniProtKB-KW.
DR   GO; GO:0006281; P:DNA repair; IEA:UniProtKB-KW.
DR   GO; GO:0006260; P:DNA replication; IBA:GO_Central.
DR   GO; GO:0000723; P:telomere maintenance; IEA:InterPro.
DR   CDD; cd18037; DEXSc_Pif1_like; 1.
DR   CDD; cd18809; SF1_C_RecD; 1.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR   InterPro; IPR010285; DNA_helicase_pif1-like.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   PANTHER; PTHR47642; ATP-DEPENDENT DNA HELICASE; 1.
DR   PANTHER; PTHR47642:SF2; PHD-TYPE DOMAIN-CONTAINING PROTEIN; 1.
DR   Pfam; PF05970; PIF1; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 2.
PE   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|RuleBase:RU363044};
KW   DNA damage {ECO:0000256|ARBA:ARBA00022763, ECO:0000256|RuleBase:RU363044};
KW   DNA recombination {ECO:0000256|RuleBase:RU363044};
KW   DNA repair {ECO:0000256|ARBA:ARBA00023204, ECO:0000256|RuleBase:RU363044};
KW   Helicase {ECO:0000256|RuleBase:RU363044};
KW   Hydrolase {ECO:0000256|RuleBase:RU363044};
KW   Nucleotide-binding {ECO:0000256|RuleBase:RU363044};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000542}.
FT   REGION          126..187
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          208..244
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          718..786
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        126..141
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   786 AA;  84150 MW;  C774BA89A9AD8698 CRC64;
     MAAVAIRVPK PKMTMSAVQG KISVFAEDGE RIGQWGGTEC FLSRQGGLGP CLVVRSSRHK
     KHEGTFFQLV RLQRVVSTGV AQGRLTVMVP HEKRQCSVFI DTTEDLDELR MMAGVLQDKA
     RWKDMERNVA SRSRRGPQRG GKGDGGGRGS GELRDPGLAQ LSGSGVDSDD DYDASGEDTR
     KTHHDNDTVA VSAAQGDSFA AHSMVESLTH MTSSQSSVPQ RSTVVAGGGS SSSSGPTTSL
     TKAQQQRLKW TSEQQRAVQL VRAGHNVFVS GAAGTGKTEW LLHVLQHVLP RTRQHRGAKS
     KADLGAEGED QEQVVETGRV AVTAATGIAA RLIGGKTVHA FSGIGRGEGD PDAILQRVQS
     NPDVVRAWQR CEVLVIDEIS MLSSHTFALL DRVARVLRAP LAPPVSSSQR RQRTSNAALP
     FGGIQLLVVG DFLQLPPVSR GAGEEVQPAF MAAVWRACAF QQLVFTKDYR HAEDPRFAEC
     CAAVRRGECT PLVRQVLEAC LGRKLEERFG VEATTLLARR KDVDRYNAHR LQQLESMQFQ
     RYASEDYAAV PGADIDAEVS LPTVLTLKVG AQVVLLASLP NEPSLANGNL GLVGGFVAQA
     HGPALPLVRF STGVEAVVPA VTMEVHGRDG RLSLSRRQVP LQLAWALTVH RVQGMTLPMV
     RLALDKSFFE AGQAYVALSR VRKAEDLSLT ALDLDVVAAC VSVEARDFYG LGTVTSAPSS
     QPVITRAGSS PPLEPALSRE RDTACGKGSL RTDGVSGSGV PLSLADIEGG GSRVTATRKR
     AKTEDG
//
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