ID Q4Q9N4_LEIMA Unreviewed; 1043 AA.
AC Q4Q9N4;
DT 19-JUL-2005, integrated into UniProtKB/TrEMBL.
DT 19-JUL-2005, sequence version 1.
DT 27-MAR-2024, entry version 111.
DE SubName: Full=Putative helicase-like protein {ECO:0000313|EMBL:CAJ05517.1};
GN ORFNames=LMJF_25_2050 {ECO:0000313|EMBL:CAJ05517.1};
OS Leishmania major.
OC Eukaryota; Discoba; Euglenozoa; Kinetoplastea; Metakinetoplastina;
OC Trypanosomatida; Trypanosomatidae; Leishmaniinae; Leishmania.
OX NCBI_TaxID=5664 {ECO:0000313|EMBL:CAJ05517.1, ECO:0000313|Proteomes:UP000000542};
RN [1] {ECO:0000313|EMBL:CAJ05517.1, 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:CAJ05517.1, 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).
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DR EMBL; FR796421; CAJ05517.1; -; Genomic_DNA.
DR RefSeq; XP_001683964.1; XM_001683912.1.
DR AlphaFoldDB; Q4Q9N4; -.
DR STRING; 5664.Q4Q9N4; -.
DR EnsemblProtists; CAJ05517; CAJ05517; LMJF_25_2050.
DR GeneID; 5652686; -.
DR KEGG; lma:LMJF_25_2050; -.
DR VEuPathDB; TriTrypDB:LmjF.25.2050; -.
DR VEuPathDB; TriTrypDB:LMJFC_250031400; -.
DR VEuPathDB; TriTrypDB:LMJLV39_250028100; -.
DR VEuPathDB; TriTrypDB:LMJSD75_250028100; -.
DR eggNOG; KOG0385; Eukaryota.
DR HOGENOM; CLU_292313_0_0_1; -.
DR InParanoid; Q4Q9N4; -.
DR OMA; RCLIFSN; -.
DR Proteomes; UP000000542; Chromosome 25.
DR GO; GO:0000785; C:chromatin; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR GO; GO:0016887; F:ATP hydrolysis activity; IBA:GO_Central.
DR GO; GO:0140658; F:ATP-dependent chromatin remodeler activity; IBA:GO_Central.
DR GO; GO:0003682; F:chromatin binding; IBA:GO_Central.
DR GO; GO:0051213; F:dioxygenase activity; IEA:UniProtKB-KW.
DR GO; GO:0003677; F:DNA binding; IBA:GO_Central.
DR GO; GO:0004386; F:helicase activity; IEA:UniProtKB-KW.
DR GO; GO:0042393; F:histone binding; IBA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0034728; P:nucleosome organization; IBA:GO_Central.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR CDD; cd17919; DEXHc_Snf; 1.
DR CDD; cd18793; SF2_C_SNF; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR Gene3D; 3.40.50.10810; Tandem AAA-ATPase domain; 1.
DR Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
DR InterPro; IPR014001; Helicase_ATP-bd.
DR InterPro; IPR001650; Helicase_C.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR038718; SNF2-like_sf.
DR InterPro; IPR049730; SNF2/RAD54-like_C.
DR InterPro; IPR000330; SNF2_N.
DR InterPro; IPR011011; Znf_FYVE_PHD.
DR InterPro; IPR001965; Znf_PHD.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR PANTHER; PTHR10799:SF1020; BTAF (TBP-ASSOCIATED FACTOR) HOMOLOG; 1.
DR PANTHER; PTHR10799; SNF2/RAD54 HELICASE FAMILY; 1.
DR Pfam; PF00271; Helicase_C; 1.
DR Pfam; PF00176; SNF2-rel_dom; 1.
DR SMART; SM00487; DEXDc; 1.
DR SMART; SM00490; HELICc; 1.
DR SMART; SM00249; PHD; 2.
DR SUPFAM; SSF57903; FYVE/PHD zinc finger; 2.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 2.
DR PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
DR PROSITE; PS51194; HELICASE_CTER; 1.
PE 4: Predicted;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Dioxygenase {ECO:0000256|ARBA:ARBA00022964};
KW Helicase {ECO:0000313|EMBL:CAJ05517.1};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Reference proteome {ECO:0000313|Proteomes:UP000000542};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771}.
FT DOMAIN 308..471
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 606..758
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
FT REGION 14..83
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 103..141
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 184..206
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 788..823
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 994..1043
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 40..54
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 123..137
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 190..206
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 796..823
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1002..1018
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1043 AA; 112651 MW; 23E22239C80E8746 CRC64;
MNLDNYFAKF LQKSSGRSAK GGESEKATLS SAAGAGVPVT PATATSSKQF SEGGGHKPSQ
GGGQSPGDAA EAQVQPSCGS PNAAFDQCYQ RQQQWDADAT EAMTVTALPE STHQRAPSLK
RSREAAMTTS SSPAPSHSAM DAPAATRLLT CRAASEDDDD ELALLLGSQK AKQVREADAM
LEGVARAQQA PSPPLSSSSP GHASNGVVGT SSACAVGILA WQTSSSATRE TIARYFQRQL
EWELHHSADL FAAFEPFFKD RALDRIAAND ALRPVLHAAP LSITSETVGA LPGCALRSYQ
VEGVQFLLSH FHRGMSAILG DDMGLGKTAQ VSAFLHTLKQ LHNIDGPHLI VAPLSTLTSW
TRELARWAPQ LRVVKYHGER RTRAAISSGR HNRHAVFVTT PALLHLDKRF FRKRAWVTVV
VDEAHVLKAH DTAITSASRK LTACYRVAVT GTPVHNNVQE VWSLMSFLYP WLMATYDPRA
RDPVRQAEEC AKVLQYIMLR RTKADVELGI PPRVDEPLTK LVPTDIQLQL LSLLTAHALQ
ESSTGHQLHG HLSHQRAVCN HPLALRLLAD KGRTHGSQGS VEKRMRAAGV PMDAAHLIDP
SAKMRYLDTL LPQLKEQGHR CLIFSNFTTT LDLLEAMCHL RGHSYERLDG SCNRVERELS
ILRYNHPASS CFLFLVTTTA GGVGVTLTGA DTVILFDAHF NPQLDRQAAD RAHRIGQART
VHVYRLCLQG TIEEHIRDIA ARKAYLGDFI VEGGQRHGAR GCGRSANDGA DAPCITADDI
REMLQQLDEK QHAKQQTDGS SVSSPTLLRP SDGAEGSTSS GSQAAADAMV KDLLRVVEKG
LQGAAATAGI HGAGRGLASP PKQTHSCFCC GGIMHPMEPL LHCMVCPKAY HAACIGERPP
RPGEAVKRFW SCPRHECFSC GKQQAADGAI FMCDACPRSF CFDCLDPRYL EMNASGAQLL
HIRDTYAGME EEEVEPRRSC YYVTCLRCCG LLSSSSSSAS EDTDEVDSDE DDVSDCDMAT
AVDSDGLASV DGHGGAGVEN GDN
//
