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Database: UniProt
Entry: A4HEA7_LEIBR
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Original site: A4HEA7_LEIBR 
ID   A4HEA7_LEIBR            Unreviewed;       974 AA.
AC   A4HEA7;
DT   01-MAY-2007, integrated into UniProtKB/TrEMBL.
DT   01-MAY-2007, sequence version 1.
DT   27-MAR-2024, entry version 97.
DE   SubName: Full=Putative helicase-like protein {ECO:0000313|EMBL:CAM39160.1};
GN   ORFNames=LBRM_25_1610 {ECO:0000313|EMBL:CAM39160.1};
OS   Leishmania braziliensis.
OC   Eukaryota; Discoba; Euglenozoa; Kinetoplastea; Metakinetoplastina;
OC   Trypanosomatida; Trypanosomatidae; Leishmaniinae; Leishmania;
OC   Leishmania braziliensis species complex.
OX   NCBI_TaxID=5660 {ECO:0000313|EMBL:CAM39160.1, ECO:0000313|Proteomes:UP000007258};
RN   [1] {ECO:0000313|EMBL:CAM39160.1, ECO:0000313|Proteomes:UP000007258}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MHOM/BR/75/M2904 {ECO:0000313|EMBL:CAM39160.1,
RC   ECO:0000313|Proteomes:UP000007258};
RX   PubMed=17572675; DOI=10.1038/ng2053;
RA   Peacock C.S., Seeger K., Harris D., Murphy L., Ruiz J.C., Quail M.A.,
RA   Peters N., Adlem E., Tivey A., Aslett M., Kerhornou A., Ivens A.,
RA   Fraser A., Rajandream M.A., Carver T., Norbertczak H., Chillingworth T.,
RA   Hance Z., Jagels K., Moule S., Ormond D., Rutter S., Squares R.,
RA   Whitehead S., Rabbinowitsch E., Arrowsmith C., White B., Thurston S.,
RA   Bringaud F., Baldauf S.L., Faulconbridge A., Jeffares D., Depledge D.P.,
RA   Oyola S.O., Hilley J.D., Brito L.O., Tosi L.R., Barrell B., Cruz A.K.,
RA   Mottram J.C., Smith D.F., Berriman M.;
RT   "Comparative genomic analysis of three Leishmania species that cause
RT   diverse human disease.";
RL   Nat. Genet. 39:839-847(2007).
RN   [2] {ECO:0000313|EMBL:CAM39160.1, ECO:0000313|Proteomes:UP000007258}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MHOM/BR/75/M2904 {ECO:0000313|EMBL:CAM39160.1,
RC   ECO:0000313|Proteomes:UP000007258};
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; FR799000; CAM39160.1; -; Genomic_DNA.
DR   RefSeq; XP_001565665.1; XM_001565615.2.
DR   AlphaFoldDB; A4HEA7; -.
DR   STRING; 5660.A4HEA7; -.
DR   GeneID; 5416250; -.
DR   KEGG; lbz:LBRM_25_1610; -.
DR   VEuPathDB; TriTrypDB:LbrM.25.1610; -.
DR   VEuPathDB; TriTrypDB:LBRM2903_250029500; -.
DR   InParanoid; A4HEA7; -.
DR   OMA; RCLIFSN; -.
DR   Proteomes; UP000007258; Chromosome 25.
DR   GO; GO:0005524; F:ATP binding; IEA:InterPro.
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:0004386; F:helicase activity; IEA:UniProtKB-KW.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
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); 2.
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:CAM39160.1};
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:UP000007258};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833};
KW   Zinc-finger {ECO:0000256|ARBA:ARBA00022771}.
FT   DOMAIN          207..370
FT                   /note="Helicase ATP-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS51192"
FT   DOMAIN          505..708
FT                   /note="Helicase C-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS51194"
FT   REGION          1..43
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          65..106
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          655..676
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          689..726
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          899..974
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        697..726
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   974 AA;  106758 MW;  463B2F072BE42166 CRC64;
     MAATASSEST HRDVAPLKRP RETAVAAPSS SAPPEPALDA PAAKRLLTRR AASEDDDDEL
     TLLLGSQKAR QVRETDATMQ DVARAQQTPS PPLSPSWPGH RGGATVEASS GACAVSSLPW
     QTPSSATRET IARHFQRQFE WELHHSTELF DAFEPFFKDR ALNRIAADDE LRPVLHAALP
     VITSETVGAL PGCTLRSYQM EGVQFLLSHF HRGMSAILGD DMGLGKTAQV SAFLHSLKLL
     HNIDGPHLIV APLSTLTNWT RELARWAPQL RVVKYHGERR TRAATSAGRH NRHAVFVTTP
     ALLHLDKRVF RKRAWVTVVV DEAHVLKAHD TAITSASRKL TACYRVAVTG TPVHNNVQEV
     WSLMSFLYPW LMAAYDPGVR DPVRQAEECA KVLQYIMLRR TKADMELGIP PRVDEPLTKL
     VPTYVQLQLL SLLTAHALQE SSSGHQLHGH LSHQRAVCNH PLALRLLADK GRTNGSQEPI
     EKRMRAAGVP MDAAHLIDPS AKMRYLDTLL PQLKAQGHRC LIFSNFTTTL DLLEAVCQLR
     GHSYERLDGS CNRVERELAM LRYNHPASSC FLFLVTTTAG GVGVTLTGAD TVILFDAHFN
     PQLDRQAADR AHRIGQTRVV RVYRLCLQGT IEEHIRDIAA RKAYLGDFIV EGGQRHGARG
     RGRFTTNDDA DTPRITADDI REVLHRFEEK HRAKQQADGS PISSSTLLRS SDEADGSSSS
     GSGSLSAEDA MVKDLLHVEA NRLRGSAAAA VMRGGGGGGG ALASPPKQTH RCFCCGDVMH
     PMEPLLHCTA CPKAYHAACI GKRPPRSGEA VKRLWSCPRH ECFSCGKQQA ADGAIFMCDT
     CPRSFCFDCL DPRYLEMDAS GARLLHIRDT YAGMEEEEVK PKRSCYYVTC LRCCGLLSSS
     SSSAADDTDE TDDDNDDAGG YNTAAVVDSD GLEIADDDSD VSVEDDGNCR NNLGPLSLME
     GESRCGRQPE EEDE
//
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