(data stored in ACNUC9543 zone)

SWISSPROT: E9B5Z9_LEIMU

ID   E9B5Z9_LEIMU            Unreviewed;       704 AA.
AC   E9B5Z9;
DT   05-APR-2011, integrated into UniProtKB/TrEMBL.
DT   05-APR-2011, sequence version 1.
DT   08-MAY-2019, entry version 40.
DE   SubName: Full=Putative pre-mRNA splicing factor ATP-dependent RNA helicase {ECO:0000313|EMBL:CBZ30670.1};
GN   ORFNames=LMXM_34_1200 {ECO:0000313|EMBL:CBZ30670.1};
OS   Leishmania mexicana (strain MHOM/GT/2001/U1103).
OC   Eukaryota; Euglenozoa; Kinetoplastida; Trypanosomatidae;
OC   Leishmaniinae; Leishmania.
OX   NCBI_TaxID=929439 {ECO:0000313|EMBL:CBZ30670.1, ECO:0000313|Proteomes:UP000007259};
RN   [1] {ECO:0000313|Proteomes:UP000007259}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MHOM/GT/2001/U1103 {ECO:0000313|Proteomes:UP000007259};
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
RT   change between species and strains of Leishmania.";
RL   Genome Res. 21:2129-2142(2011).
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DR   EMBL; FR799587; CBZ30670.1; -; Genomic_DNA.
DR   RefSeq; XP_003879116.1; XM_003879067.1.
DR   EnsemblProtists; CBZ30670; CBZ30670; LMXM_34_1200.
DR   GeneDB; LmxM.34.1200.1:pep; -.
DR   GeneID; 13450833; -.
DR   KEGG; lmi:LMXM_34_1200; -.
DR   EuPathDB; TriTrypDB:LmxM.34.1200; -.
DR   eggNOG; KOG0925; Eukaryota.
DR   eggNOG; COG1643; LUCA.
DR   HOGENOM; HOG000175261; -.
DR   KO; K12820; -.
DR   OMA; QWCVDFA; -.
DR   Proteomes; UP000007259; Chromosome 34.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0004386; F:helicase activity; IEA:UniProtKB-KW.
DR   GO; GO:0003676; F:nucleic acid binding; IEA:InterPro.
DR   CDD; cd00079; HELICc; 1.
DR   InterPro; IPR003593; AAA+_ATPase.
DR   InterPro; IPR011545; DEAD/DEAH_box_helicase_dom.
DR   InterPro; IPR002464; DNA/RNA_helicase_DEAH_CS.
DR   InterPro; IPR011709; DUF1605.
DR   InterPro; IPR007502; Helicase-assoc_dom.
DR   InterPro; IPR014001; Helicase_ATP-bd.
DR   InterPro; IPR001650; Helicase_C.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   Pfam; PF00270; DEAD; 1.
DR   Pfam; PF04408; HA2; 1.
DR   Pfam; PF00271; Helicase_C; 1.
DR   Pfam; PF07717; OB_NTP_bind; 1.
DR   SMART; SM00382; AAA; 1.
DR   SMART; SM00487; DEXDc; 1.
DR   SMART; SM00847; HA2; 1.
DR   SMART; SM00490; HELICc; 1.
DR   SUPFAM; SSF52540; SSF52540; 1.
DR   PROSITE; PS00690; DEAH_ATP_HELICASE; 1.
DR   PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
DR   PROSITE; PS51194; HELICASE_CTER; 1.
PE   4: Predicted;
DR   PRODOM; E9B5Z9.
DR   SWISS-2DPAGE; E9B5Z9.
KW   ATP-binding {ECO:0000256|SAAS:SAAS01176619};
KW   Complete proteome {ECO:0000313|Proteomes:UP000007259};
KW   Helicase {ECO:0000313|EMBL:CBZ30670.1};
KW   Hydrolase {ECO:0000256|SAAS:SAAS01176622};
KW   Nucleotide-binding {ECO:0000256|SAAS:SAAS01176608}.
FT   DOMAIN       40    201       Helicase ATP-binding.
FT                                {ECO:0000259|PROSITE:PS51192}.
FT   DOMAIN      226    404       Helicase C-terminal.
FT                                {ECO:0000259|PROSITE:PS51194}.
SQ   SEQUENCE   704 AA;  80003 MW;  37EAADE23F3034DB CRC64;
     MEAKHSSRNP LTGREYSSRY FTLLKGRERL PIFAAKSRIQ KLVSQYQTLL LVGETGSGKT
     TQVPQYILEL NPEHGIACTQ PRRVAATSVS ERVAEEMDVE LGEEVGYSIR FDDKSSEKTR
     LKYLTDGMLL REAMTDPLLS RYSVIVLDEA HERTVSTDIL IGTLKELLPK RPDLRIVVMS
     ATLEEKRFQE YFSEAPLVHI SGRMYGVEVY NSKAPEANYV EASIRTATQI HLYEGEGDIL
     IFLTGEDEIE TTVERLQSGI RMAEHSSANC HHGPVAVLPL YSALPPSQQR KVFQTVPEGT
     RKIVVATNVA ETSLTIDGVV FVIDCGFSKQ KVFNPKLRVE SLLVTPISQA SARQRCGRAG
     RTRPGKCFRL YTAKSFHSSL QPNTYPEILR CNLGSIVLHM KKMGIEDLVN FDFVEPPAPE
     TLMRALELLN YLGALDDDGN LTEEGNFMSE FPVDPEMASM LFHSPKFGSS EDIARICAML
     SVQNPFITPS NDQRGRALRC REQFYHPTGD HISYLNTFNV FYEMKNQSSS WCTENYINPR
     VMKQAVNIYR QLVGILRRLN LPICSTYTAQ QRRVQGHDVP AELEFANEVR RAIVKGYFTK
     VALSLPTKHQ FMTLKDDVKC LLFPSTYLNR RPKFVVFNEL VLTSNTYIRT VTAVSEDWLI
     ESSPSYFAHD EFEGITKQVF DEVFRRQGKE KERRSKRTRT PSDD
//

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