(data stored in ACNUC7421 zone)

HOGENOM: LEDON1_18_PE151

ID   LEDON1_18_PE151                      STANDARD;      PRT;   974 AA.
AC   LEDON1_18_PE151; E9BDY2;
DT   00-JAN-0000 (Rel. 1, Created)
DT   00-JAN-0000 (Rel. 2, Last sequence update)
DT   00-JAN-0000 (Rel. 3, Last annotation update)
DE   SubName: Full=Complete genome, chromosome 18; (LEDON1_18.PE151).
GN   ORFNames=LDBPK_181510;
OS   LEISHMANIA DONOVANI BPK282A1.
OC   Eukaryota; Euglenozoa; Kinetoplastida; Trypanosomatidae; Leishmania.
OX   NCBI_TaxID=981087;
RN   [0]
RP   -.;
RG   -.;
RL   -.;
CC   -!- SEQ. DATA ORIGIN: Translated from the HOGENOM CDS LEDON1_18.PE151.
CC       Leishmania donovani BPK282A1 complete genome, chromosome 18
CC       annotated by Ensembl
CC   -!- ANNOTATIONS ORIGIN:E9BDY2_LEIDO
CC   -!- SIMILARITY: Belongs to the cation transport ATPase (P-type)
CC       family.
CC   -!- GENE_FAMILY: HOG000160005 [ FAMILY / ALN / TREE ]
DR   UniProtKB/Swiss-Prot; E9BDY2; -.
DR   EMBL; FR799605; CBZ33458.1; -; Genomic_DNA.
DR   GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0015662; F:ATPase activity, coupled to transmembrane movement of ions, phosphorylative mechanism; IEA:InterPDR   GO; GO:0046872; F:metal ion binding; IEA:InterPro.
DR   GO; GO:0046872; F:metal ion binding; IEA:InterPro.
DR   GO; GO:0006754; P:ATP biosynthetic process; IEA:InterPro.
DR   GO; GO:0006812; P:cation transport; IEA:InterPro.
DR   InterPro; IPR008250; ATPase_P-typ_ATPase-assoc-dom.
DR   InterPro; IPR004014; ATPase_P-typ_cation-transptr_N.
DR   InterPro; IPR023300; ATPase_P-typ_cyto_domA.
DR   InterPro; IPR023299; ATPase_P-typ_cyto_domN.
DR   InterPro; IPR000695; ATPase_P-typ_H-transp.
DR   InterPro; IPR001757; ATPase_P-typ_ion-transptr.
DR   InterPro; IPR018303; ATPase_P-typ_P_site.
DR   InterPro; IPR006534; ATPase_P-typ_PM_proton-efflux.
DR   InterPro; IPR023298; ATPase_P-typ_TM_dom.
DR   InterPro; IPR005834; Dehalogen-like_hydro.
DR   InterPro; IPR023214; HAD-like_dom.
DR   Gene3D; G3DSA:2.70.150.10; ATPase_P-typ_cyto_domA; 2.
DR   Gene3D; G3DSA:3.40.1110.10; ATPase_P-typ_cyto_domN; 2.
DR   Gene3D; G3DSA:1.20.1110.10; ATPase_P-typ_TM_dom; 2.
DR   Pfam; PF00690; Cation_ATPase_N; 1.
DR   Pfam; PF00122; E1-E2_ATPase; 1.
DR   Pfam; PF00702; Hydrolase; 1.
DR   PRINTS; PR00119; CATATPASE.
DR   PRINTS; PR00120; HATPASE.
DR   SMART; SM00831; Cation_ATPase_N; 1.
DR   SUPFAM; SSF56784; HAD-like_dom; 1.
DR   TIGRFAMs; TIGR01647; ATPase-IIIA_H; 1.
DR   TIGRFAMs; TIGR01494; ATPase_P-type; 2.
DR   PROSITE; PS00154; ATPASE_E1_E2; 1.
DR   HOGENOMDNA; LEDON1_18.PE151; -.
KW   CBZ33458.1000047545old_1320000031;
KW   ATP-binding; Hydrolase; Membrane; Nucleotide-binding; Phosphoprotein;
KW   Transmembrane; Transmembrane helix.
SQ   SEQUENCE   974 AA;  UNKNOWN MW;  UNKNOWN CRC64;
     MSSKKYELDA AAFEDKPESH SDAEMTPQKP QRRQSVLSKA VSEHDERATG PATDLLPPSK
     GLTTEEAEEL LKKYGRNELP EKKTPSWLIY VRGLWGPMPA ALWIAIIIEF ALENWPDGAI
     LFAIQIANAT IGWYETIKAG DAVAALKNSL KPTATVYRDS KWQQIDAAVL VPGDLVKLAS
     GSAVPADCSI NEGVIDVDEA ALTGESLPVT MGPEHMPKMG SNVVRGEVEG TVQYTGSLTF
     FGKTAALLQS VESDLGNIHV ILRRVMFSLC AISFMLCMCC FIYLLARFYE TFRHALQFAV
     VVLVVSIPIA LEIVVTTTLA VGSKHLSKHK IIVTKLSAIE MMSGVNMLCS DKTGTLTLNK
     MEIQEQCFTF EEGNDLKSTL VLAALAAKWR EPPRDALDTM VLGAADLDEC DNYQQLNFVP
     FDPTTKRTAA TLVDRRSGEK FDVTKGAPHV ILQMVYNQDE INDEVVDIID SLAARGVRCL
     SVAKTDQQGR WHMAGILTFL DPPRPDTKDT IRRSKEYGVD VKMITGDHLL IAKEMCRMLD
     LDPNILTADK LPQIKDANDL PEDLGEKYGD MMLSVGGFAQ VFPEHKFMIV ETLRQRGYTC
     AMTGDGVNDA PALKRADVGI AVHGATDAAR AAADMVLTEP GLSVVVEAML VSREVFQRML
     SFLTYRISAT LQLVCFFFIA CFSLTPKAYG SVDPHFQFFH LPVLMFMLIT LLNDGCLMTI
     GYDHVIPSER PQKWNLPVVF VSASILAAVA CGSSLMLLWI GLEGYSSQYY ENSWFHRLGL
     AQLPQGKLVT MMYLKISISD FLTLFSSRTG GHFFFYMPPS PILFCGAIIS LLVSTMAASF
     WHKSRPDNVL TEGLAWGQTN AEKLLPLWVW IYCIVWWLVQ DVVKVLAHIC MDAVDLFGCV
     SDASGSGPIK PYSDDMKGNG FEPVKKPAEK STEKALNLSV SSGPHKALEG VREDTHVLNE
     STSPVNAFSP KVKK
//

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