(data stored in ACNUC9543 zone)

SWISSPROT: E9AT60_LEIMU

ID   E9AT60_LEIMU            Unreviewed;      1088 AA.
AC   E9AT60;
DT   05-APR-2011, integrated into UniProtKB/TrEMBL.
DT   05-APR-2011, sequence version 1.
DT   08-MAY-2019, entry version 41.
DE   SubName: Full=Putative pre-mRNA splicing factor ATP-dependent RNA helicase {ECO:0000313|EMBL:CBZ26134.1};
GN   ORFNames=LMXM_36_2830 {ECO:0000313|EMBL:CBZ26134.1};
OS   Leishmania mexicana (strain MHOM/GT/2001/U1103).
OC   Eukaryota; Euglenozoa; Kinetoplastida; Trypanosomatidae;
OC   Leishmaniinae; Leishmania.
OX   NCBI_TaxID=929439 {ECO:0000313|EMBL:CBZ26134.1, ECO:0000313|Proteomes:UP000007259};
RN   [1] {ECO:0000313|EMBL:CBZ26134.1, ECO:0000313|Proteomes:UP000007259}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MHOM/GT/2001/U1103 {ECO:0000313|EMBL:CBZ26134.1,
RC   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; FR799573; CBZ26134.1; -; Genomic_DNA.
DR   RefSeq; XP_003874634.1; XM_003874585.1.
DR   EnsemblProtists; CBZ26134; CBZ26134; LMXM_36_2830.
DR   GeneDB; LmxM.36.2830.1:pep; -.
DR   GeneID; 13448088; -.
DR   KEGG; lmi:LMXM_36_2830; -.
DR   EuPathDB; TriTrypDB:LmxM.36.2830; -.
DR   eggNOG; KOG0922; Eukaryota.
DR   eggNOG; COG1643; LUCA.
DR   HOGENOM; HOG000175261; -.
DR   KO; K12818; -.
DR   OMA; PERWEMK; -.
DR   Proteomes; UP000007259; Chromosome 20.
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; 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; 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; E9AT60.
DR   SWISS-2DPAGE; E9AT60.
KW   ATP-binding {ECO:0000256|SAAS:SAAS01176619};
KW   Complete proteome {ECO:0000313|Proteomes:UP000007259};
KW   Helicase {ECO:0000313|EMBL:CBZ26134.1};
KW   Hydrolase {ECO:0000256|SAAS:SAAS01176622};
KW   Nucleotide-binding {ECO:0000256|SAAS:SAAS01176608}.
FT   DOMAIN      434    597       Helicase ATP-binding.
FT                                {ECO:0000259|PROSITE:PS51192}.
FT   DOMAIN      619    799       Helicase C-terminal.
FT                                {ECO:0000259|PROSITE:PS51194}.
SQ   SEQUENCE   1088 AA;  123354 MW;  3A4565ECAB490A11 CRC64;
     MNVVGDAVAA VGGDDDAIAE QQDMSFLMKL QELYCKSVLY EQLEQMMGHP ATQEESDDYL
     DDVEGLVKLY CSEREAAKKM TPQGEEADAA AQREAVTEQH ILHSLSVAIN GEAEADEEPD
     IPMSSIQQLY HVLHDCLTTD TVETGLAVGS LLLADDAKRS AEEAARLAYQ QQQRHMHGGV
     DTTSMNTSTA ERKNAMKVSP EEMFRLAQHV RSGLADEAEL LKLRSEDNEE EGGGAQDVEL
     NDEEPRFLRN MGFSSMLHRR INYRAPLPSQ LLRDARTPQH RQAILDRLAQ RQQGDLSKLN
     SMEAVAQMQE KINMERRVIA RKAQRTQQQS REYDFGAIMS GRDDRSVLDE DRYGRRGGAL
     ESEEYSTQPT LLHSELNVLP EESGFRPQDM PTKLAPWMKH SFGHKPRFGL PETMQTIQEQ
     RISLPIYAKK EALLNFVDAH RVTVLVGETG SGKTTQIPQY LAEHGYADRG VIACTQPRRV
     AAETLAMRVA EEYGCRLGEE VGYTVRFRDV TSSLTKIKYM TDGMLLREAL LDDSFQRYSV
     IILDEAHERS ISTDLLFAIV RQALRKNEVL KVMVTSATLE TEKFCAYFGA SEPFRIEGRT
     FPVETYYLTD PTTDYVRAAL QTVMMIHLQE PPGDVLVFFT GQEEIELGGE QLFRWMEMLR
     RQVSTPLPDL MVLPLTATMP QEVQSKVFEP TPPGCRKVVL ATNVAETSIT ITNLYYVVDS
     GFCKQNIFDA KHGIDQLKVM PVSQAQAKQR SGRAGRIGPG KCYRMYTEKQ FTTDMVSETV
     PDIMRTSLFH VTLQLKAMGL DLLNLELMDC PPKGAIVSAL EKLRYLEALD DDGLLTPLGS
     RMAQLSIDPS QSKTLLTAVD LGCSEPVLTI VSMLAVQKRG VFYRPRDQQD ASDAARRQFM
     QPEGDQLTLM AVYDAWVENG MSEDWSKHNF LKHRMLVEAR DTRDQLKEML ARRNQHISHE
     NDTNLDQVRK SITAGYFFNA ARRVDSHTRS YVTLSDRREV YVHPSSVLID DPPKYVLYDD
     LRMTKREYMT ELLAIEPKWL VELAPAFYAR PKDGRLTKEQ AAERFTPILK SWETGSSWRI
     SRLKKQRR
//

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