(data stored in ACNUC7421 zone)

HOGENOM: THAMM1_2_PE988

ID   THAMM1_2_PE988                       STANDARD;      PRT;   884 AA.
AC   THAMM1_2_PE988; E8T267;
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=Plasma-membrane proton-efflux P-type ATPase;
DE   (THAMM1_2.PE988).
GN   OrderedLocusNames=Theam_0995;
OS   THERMOVIBRIO AMMONIFICANS HB-1.
OC   Bacteria; Aquificae; Aquificales; Desulfurobacteriaceae; Thermovibrio.
OX   NCBI_TaxID=648996;
RN   [0]
RP   -.;
RG   -.;
RL   -.;
CC   -!- SEQ. DATA ORIGIN: Translated from the HOGENOM CDS THAMM1_2.PE988.
CC       Thermovibrio ammonificans HB-1 chromosome, complete genome.
CC       1..107808587 annotated by Ensembl
CC   -!- ANNOTATIONS ORIGIN:E8T267_THEA1
CC   -!- SIMILARITY: Belongs to the cation transport ATPase (P-type)
CC       family.
CC   -!- GENE_FAMILY: HOG000160005 [ FAMILY / ALN / TREE ]
DR   UniProtKB/Swiss-Prot; E8T267; -.
DR   EMBL; CP002444; ADU96962.1; -; Genomic_DNA.
DR   RefSeq; YP_004151603.1; NC_014926.1.
DR   GeneID; 10126036; -.
DR   GenomeReviews; CP002444_GR; Theam_0995.
DR   KEGG; tam:Theam_0995; -.
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; 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   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; 3.
DR   PROSITE; PS00154; ATPASE_E1_E2; 1.
DR   HOGENOMDNA; THAMM1_2.PE988; -.
KW   plasma-membrane proton-efflux P-type ATPase;
KW   ATP-binding; Complete proteome; Hydrolase; Nucleotide-binding;
KW   Phosphoprotein; Transmembrane.
SQ   SEQUENCE   884 AA;  UNKNOWN MW;  UNKNOWN CRC64;
     MAKIDEFKEK SIEETVKELG TSLERGLSEE EARRRLQKYG YNEIPEKEEP LWHRIFRRFW
     GPIPWMIEIA ALLSALVKHW EDFAIILTLL FVNAGVDFWQ EHKALSALKV LKEKLARKAL
     VLRDGKWKEV DARFLVPGDV IKIKIGDIIP ADVKLDHGGD YILVDQSALT GESLPVTKKP
     GDVAYANSVV KKGEIIAVVV ATGLDTYFGK TVQLVAKAEK EQRSHFQEMV IKVGNFLIAL
     TLVLIAITIF VELNRGKPFI ELLQFSLVLT VAAIPVALPA VLTVTMAIGA LYLAKRQVIV
     SRLAAIEELA GVDVLCSDKT GTLTMNKMTV SDPYTVGNYK PEDLMFYAAL ASKEENNDPI
     EIPIFEWLKK HNLYEKVKEC VQKKFVPFDP VRKRTEALVE CKGKKLVVTK GAPQVIIELC
     DKSEFDVEKA YKKVEELAEN GFRTLGVAYK APQEEKFHFV GLIPLYDPPR PDSKEAVQEA
     KRFGVEVKMV TGDNIAIARY IARILGIGDK IISARELRGE QEPKEYIVLA EIIAKALMKT
     LHNLSDKEIE EKTKQIVELV KKELQNAPLP KGIVRKHESE IIKIIEEANG FAEVFPEDKY
     FIVDKLQKAG HIVGMTGDGV NDAPALRKAD CGIAVANATD AARAAAALVL LKPGLKVIIK
     AFEIARQIFG RMEAYTIYRI AETIRVLFFM TLSILIFQFY PITTVMIILL ALLNDIPILS
     IAYDRVKIAE KPVRWDFYEL NVMSFWLGVA GVLSSFTIYF LLERYWHLPQ DLIQSIIFTK
     LIVAGHFTIF NTRVKDWFFK KPWPSAVLFI ATQGTSFLGT VIGVYGFHLM TPIGWKWGIF
     IWGYAFAWFL FNDAVKMAVL KMYRERKFMF APGHFKLIKK IFSA
//

If you have problems or comments...

PBIL Back to PBIL home page