ID Q4Q417_LEIMA Unreviewed; 1103 AA.
AC Q4Q417;
DT 19-JUL-2005, integrated into UniProtKB/TrEMBL.
DT 19-JUL-2005, sequence version 1.
DT 24-JAN-2024, entry version 111.
DE SubName: Full=Putative DNA-dependent ATPase {ECO:0000313|EMBL:CAJ06440.1};
GN ORFNames=LMJF_33_1700 {ECO:0000313|EMBL:CAJ06440.1};
OS Leishmania major.
OC Eukaryota; Discoba; Euglenozoa; Kinetoplastea; Metakinetoplastina;
OC Trypanosomatida; Trypanosomatidae; Leishmaniinae; Leishmania.
OX NCBI_TaxID=5664 {ECO:0000313|EMBL:CAJ06440.1, ECO:0000313|Proteomes:UP000000542};
RN [1] {ECO:0000313|EMBL:CAJ06440.1, 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:CAJ06440.1, 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 -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
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DR EMBL; FR796429; CAJ06440.1; -; Genomic_DNA.
DR RefSeq; XP_001685931.1; XM_001685879.1.
DR AlphaFoldDB; Q4Q417; -.
DR STRING; 5664.Q4Q417; -.
DR EnsemblProtists; CAJ06440; CAJ06440; LMJF_33_1700.
DR GeneID; 5654593; -.
DR KEGG; lma:LMJF_33_1700; -.
DR VEuPathDB; TriTrypDB:LmjF.33.1700; -.
DR VEuPathDB; TriTrypDB:LMJFC_330028400; -.
DR VEuPathDB; TriTrypDB:LMJLV39_330026200; -.
DR VEuPathDB; TriTrypDB:LMJSD75_330025800; -.
DR eggNOG; KOG0385; Eukaryota.
DR HOGENOM; CLU_000315_0_2_1; -.
DR InParanoid; Q4Q417; -.
DR OMA; KEIYVSC; -.
DR Proteomes; UP000000542; Chromosome 33.
DR GO; GO:0031010; C:ISWI-type complex; ISO:GeneDB.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0008094; F:ATP-dependent activity, acting on DNA; IBA:GO_Central.
DR GO; GO:0140658; F:ATP-dependent chromatin remodeler activity; IEA:InterPro.
DR GO; GO:0051213; F:dioxygenase activity; IEA:UniProtKB-KW.
DR GO; GO:0003677; F:DNA binding; IBA:GO_Central.
DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR GO; GO:0031491; F:nucleosome binding; IEA:InterPro.
DR GO; GO:0044145; P:modulation of formation of structure involved in a symbiotic process; ISO:GeneDB.
DR CDD; cd00590; RRM_SF; 1.
DR CDD; cd18793; SF2_C_SNF; 1.
DR Gene3D; 1.10.1040.30; ISWI, HAND domain; 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 InterPro; IPR014001; Helicase_ATP-bd.
DR InterPro; IPR001650; Helicase_C.
DR InterPro; IPR009057; Homeobox-like_sf.
DR InterPro; IPR015194; ISWI_HAND-dom.
DR InterPro; IPR036306; ISWI_HAND-dom_sf.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR035979; RBD_domain_sf.
DR InterPro; IPR015195; SLIDE.
DR InterPro; IPR038718; SNF2-like_sf.
DR InterPro; IPR000330; SNF2_N.
DR PANTHER; PTHR45623; CHROMODOMAIN-HELICASE-DNA-BINDING PROTEIN 3-RELATED-RELATED; 1.
DR PANTHER; PTHR45623:SF49; ISW-1; 1.
DR Pfam; PF09110; HAND; 1.
DR Pfam; PF00271; Helicase_C; 1.
DR Pfam; PF09111; SLIDE; 1.
DR Pfam; PF00176; SNF2-rel_dom; 1.
DR SMART; SM00487; DEXDc; 1.
DR SMART; SM00490; HELICc; 1.
DR SUPFAM; SSF101224; HAND domain of the nucleosome remodeling ATPase ISWI; 1.
DR SUPFAM; SSF46689; Homeodomain-like; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 2.
DR SUPFAM; SSF54928; RNA-binding domain, RBD; 1.
DR PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
DR PROSITE; PS51194; HELICASE_CTER; 1.
PE 4: Predicted;
KW Dioxygenase {ECO:0000256|ARBA:ARBA00022964};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Reference proteome {ECO:0000313|Proteomes:UP000000542}.
FT DOMAIN 178..346
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 475..629
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
FT REGION 874..907
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1083..1103
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 874..890
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 891..906
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1103 AA; 125758 MW; C4638025743456DF CRC64;
MAAAIARRVR IRQDLHNTPA FERDMNDVAA QDLYEQILLS SIRSGSDPNA KAVVEVYEGY
MEPSYDPVKG ASVAASHRQV IQEIYREREV IIRTLRSSEE HRELSAFDRL LRETEFYTGV
REWKGASARG PRSRLYRHAS RDNEEDSTGF DMMHLTETPS YIRGKLRPYQ IEGVNWLLGL
FARGVNGILA DEMGLGKTFQ TIATIAYLKF TVGMPGPHLV VCPKSVMGNW YREFKHWCPG
LLVYKFHASS DIRPSIVKAH LHPTDRIKYD VIVTTFEMVL DELNLFKRIA WQYLIVDEAH
KLKNEEGRAH TALDSLQTSH RLIITGTPLQ NNLKELWALL HFLAPRLFND SESFDTWFDT
TSGQQDANVM SNLHKILAPL MIRRLKADVS TGIPPKKEIY VSCQLSKKQR EWYMNVLAKD
AEVLNKAGGS VASLTNVMMS LRKVINHPYL MDGGEEGPPF VTDEKLVRTS GKMVILDKLL
HRLRADVQGR HKVLIFSQFT SMLNILEDYC NMRGFMYCRI DGNTSGYDRD SQMASFNSPS
SDYFIFLLST RAGGLGINLQ AANHVILYDS DWNPQMDLQA QDRAHRIGQK RSVRVYRFVT
DGTLEEKMYR RALKKLYLDA VVVQQGRLQS KATNQATKEE LLSMITFGAE EIFKTRHEDV
TEADIDRLLD EGETISNQLT NDAKQQVQMS LASFQLGAEE ANIYDFEGVS YKTGAESRIL
HLRLSLPVSQ AELQAQCSQY GEVIKAVLHP NLKEALVYFR STSGAMEAKA KLPYESAFAS
RDSQTVVSSD MIAECIGVGE KLGRGHRMRE PVQLFTEADV ESMQKKATKA PPLKLPKLPK
FHPYQLYNAK RLTELHNTEV ALMVRNWKRK YEEKSDAQKS KESNEEGACD EADGKAEDED
ELLTEVEQEE RERLLSEGFP TWTFYEYRSV VSALTSGKMD LTDYAAIAAA VGGTKTVGEV
RDYVVALLER GEQCIKKFAL VEERIKKAKL RREAKENVFK AAKWKVETCE HPEKELTFKA
RGNVALDREI FLMAYETGFK ANNTSELVRT RPQHIFNVWY QSRPDGFFSK RLHTLMKSVQ
REWEKPADDD GAMPSKGHRR LEI
//