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Database: UniProt
Entry: Q4Q417_LEIMA
LinkDB: Q4Q417_LEIMA
Original site: Q4Q417_LEIMA 
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
//
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