(data stored in ACNUC9543 zone)

SWISSPROT: E9B512_LEIMU

ID   E9B512_LEIMU            Unreviewed;       809 AA.
AC   E9B512;
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=ATP-dependent RNA helicase-like protein {ECO:0000313|EMBL:CBZ30331.1};
GN   ORFNames=LMXM_33_2260 {ECO:0000313|EMBL:CBZ30331.1};
OS   Leishmania mexicana (strain MHOM/GT/2001/U1103).
OC   Eukaryota; Euglenozoa; Kinetoplastida; Trypanosomatidae;
OC   Leishmaniinae; Leishmania.
OX   NCBI_TaxID=929439 {ECO:0000313|EMBL:CBZ30331.1, 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; FR799586; CBZ30331.1; -; Genomic_DNA.
DR   RefSeq; XP_003878779.1; XM_003878730.1.
DR   EnsemblProtists; CBZ30331; CBZ30331; LMXM_33_2260.
DR   GeneDB; LmxM.33.2260.1:pep; -.
DR   GeneID; 13452386; -.
DR   KEGG; lmi:LMXM_33_2260; -.
DR   EuPathDB; TriTrypDB:LmxM.33.2260; -.
DR   eggNOG; KOG0925; Eukaryota.
DR   eggNOG; COG1643; LUCA.
DR   HOGENOM; HOG000175261; -.
DR   OMA; ERTIDTD; -.
DR   Proteomes; UP000007259; Chromosome 33.
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; E9B512.
DR   SWISS-2DPAGE; E9B512.
KW   ATP-binding {ECO:0000256|SAAS:SAAS01176619};
KW   Complete proteome {ECO:0000313|Proteomes:UP000007259};
KW   Helicase {ECO:0000313|EMBL:CBZ30331.1};
KW   Hydrolase {ECO:0000256|SAAS:SAAS01176622};
KW   Nucleotide-binding {ECO:0000256|SAAS:SAAS01176608}.
FT   DOMAIN      112    275       Helicase ATP-binding.
FT                                {ECO:0000259|PROSITE:PS51192}.
FT   DOMAIN      322    503       Helicase C-terminal.
FT                                {ECO:0000259|PROSITE:PS51194}.
SQ   SEQUENCE   809 AA;  89796 MW;  AA9A1C3D64D8A157 CRC64;
     MLSRVKKTPM LLHPALRRLA LLFFLYCHAS GTLHTAHLMA LKRVREEAAE NGEVGLGDTL
     VSQLPKKRPD VAVCTSSSAL SPFTQQPFSA RYRQLLQSRQ RLPVYEKRHL IQETVRTNAV
     TLLVGETGSG KTTQVPHFLA ELQDTFTGVI ACTQPRRIAA ISVATRVAEE MDVPLGAQVG
     YHVRFDSRQC DATRVLYMTD GMLLREAFTD ADLKKYSVVV VDEAHERTID TDVVLGLLKR
     LLTRRPRFRL VVMSATLDVA KIQSYFPGSP LVHVSGRMHD VDVFYMPQPV RDYVEATVSC
     VLQLHKREPA GDILCFLTGE AEIERAVAAL HQALDSSSAA AFKEQEASVQ GPGTGLTLLK
     TSADDLARPA RPTEVVVLPL YGSLSLQEQQ KVFAAYPPNT RKVVVATNIA ETSVTIDGIV
     YVVDCGYQKQ SLYNSEARVD YLLPAVISKA SAEQRKGRAG RTRPGKCFRL YTSADFATFP
     DQTHPEILRT NIVNTVLLLL TLGVANPCEF PFIDPPSDQG MSDAFYQLLY FGAVDDGLQL
     TDFGRRMAVF PVDVCLARML LMASKHGCGA DAAVVAAMLE AGNAFSRPPS RLAEAREAHA
     RFDDADGDHV ALFRVFHAYF KNQQNGKRFC YENYLRHQTL QQAVQVYNQL RRLMGQLTIP
     VQSTYIPERE YVDTVALRKA VLEGFFTQVA FLTPVTPITH RAGADPTTRV YRTVRDALNV
     TLHRQSVLAA THKSRALPTW IVFDRLEVQG DSGTFIRTAS AVEVGWLLDV SDFYTDLSEI
     PDGEIAQVLR RAHEAESSAH PCKVKRESV
//

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