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).
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
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
//