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Q42932

- Q42932_NICPL

UniProt

Q42932 - Q42932_NICPL

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Protein
Submitted name: N.plumbaginifolia H+-translocating ATPase mRNA
Gene
N/A
Organism
Nicotiana plumbaginifolia (Leadwort-leaved tobacco) (Tex-Mex tobacco)
Status
Unreviewed - Annotation score: 1 out of 5 - Experimental evidence at protein leveli

Functioni

GO - Molecular functioni

  1. ATP binding Source: UniProtKB-KW
  2. cation-transporting ATPase activity Source: InterPro
  3. metal ion binding Source: InterPro

GO - Biological processi

  1. ATP biosynthetic process Source: InterPro
Complete GO annotation...

Keywords - Molecular functioni

HydrolaseUniRule annotation

Keywords - Ligandi

ATP-bindingUniRule annotationSAAS annotations, Nucleotide-binding

Names & Taxonomyi

Protein namesi
Submitted name:
N.plumbaginifolia H+-translocating ATPase mRNAImported
OrganismiNicotiana plumbaginifolia (Leadwort-leaved tobacco) (Tex-Mex tobacco)Imported
Taxonomic identifieri4092 [NCBI]
Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaeasteridslamiidsSolanalesSolanaceaeNicotianoideaeNicotianeaeNicotiana

Subcellular locationi

GO - Cellular componenti

  1. integral component of membrane Source: UniProtKB-KW
Complete GO annotation...

Keywords - Cellular componenti

Membrane

PTM / Processingi

Proteomic databases

ProMEXiQ42932.

Structurei

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3M50X-ray2.60P927-954[»]
3M51X-ray3.25P927-954[»]
4DX0X-ray3.40P927-954[»]
ProteinModelPortaliQ42932.
SMRiQ42932. Positions 905-956.

Miscellaneous databases

EvolutionaryTraceiQ42932.

Family & Domainsi

Sequence similaritiesi

Keywords - Domaini

Transmembrane, Transmembrane helixSAAS annotations

Family and domain databases

Gene3Di1.20.1110.10. 3 hits.
2.70.150.10. 2 hits.
3.40.1110.10. 1 hit.
InterProiIPR004014. ATPase_P-typ_cation-transptr_N.
IPR023299. ATPase_P-typ_cyto_domN.
IPR018303. ATPase_P-typ_P_site.
IPR023298. ATPase_P-typ_TM_dom.
IPR008250. ATPase_P-typ_transduc_dom_A.
IPR001757. Cation_transp_P_typ_ATPase.
IPR006534. H+_ATPase_P-typ_IIIA.
IPR023214. HAD-like_dom.
[Graphical view]
PfamiPF00690. Cation_ATPase_N. 1 hit.
PF00122. E1-E2_ATPase. 1 hit.
PF00702. Hydrolase. 1 hit.
[Graphical view]
PRINTSiPR00119. CATATPASE.
PR00120. HATPASE.
SMARTiSM00831. Cation_ATPase_N. 1 hit.
[Graphical view]
SUPFAMiSSF56784. SSF56784. 1 hit.
TIGRFAMsiTIGR01647. ATPase-IIIA_H. 1 hit.
TIGR01494. ATPase_P-type. 2 hits.
PROSITEiPS00154. ATPASE_E1_E2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q42932-1 [UniParc]FASTAAdd to Basket

« Hide

MGEKPEVLDA VLKETVDLEN IPIEEVFENL RCTKEGLSGP AAQERLAIFG    50
YNKLEEKKES KFLKFLGFMW NPLSWVMEAA AIMAIALANG GGKPPDWQDF 100
VGIITLLVIN STISFIEENN AGNAAAALMA RLAPKAKVLR DGKWDEQDAA 150
ILVPGDIISI KLGDIIPADA RLLEGDPLKI DQSALTGESL PVTKGPGDGV 200
YSGSTCKQGE IEAVVIATGV HTFFGKAAHL VDSTNQVGHF QKVLTAIGNF 250
CICSIAVGMI IEIIVMYPIQ HRKYRPGIDN LLVLLIGGIP IAMPTVLSVT 300
MAIGSHRLAQ QGAITKRMTA IEEMAGMDVL CSDKTGTLTL NKLTVDKNLV 350
EVFAKGVDAD TVVLMAARAS RTENQDAIDT AIVGMLSDPK EARAGIREIH 400
FLPFNPTDKR TALTYLDGEG KMHRVSKGAP EQILNLAHNK SDIERRVHSV 450
IDKFAERGLR SLGVAYQEVP EGRKESTGGP WQFIGLLPLF DPPRHDSAET 500
IRRALNLGVN VKMITGDQLA IGKETGRRLG MGTNMYPSSA LLGQTKDESI 550
ASLPIDELIE KADGFAGVFP EHKYEIVKRL QARKHICGMT GDGVNDAPAL 600
KKADIGIAVD DATDAARSAS DIVLTEPGLS VIISAVLTSR AIFQRMKNYT 650
IYAVSITIRI VLGFMLLALI WKFDFPPFMV LIIAILNDGT IMTISKDRVK 700
PSPLPDSWKL AEIFTTGVVL GGYLAMMTVI FFWAAYETDF FPRVFGVSTL 750
QKTATDDFRK LASAIYLQVS TISQALIFVT RSRSWSFVER PGLLLVVAFL 800
IAQLVATLIA VYANWAFAAI EGIGWGWAGV IWLYNLVFYF PLDIIKFLIR 850
YALSGRAWDL VLEQRIAFTR KKDFGKEQRE LQWAHAQRTL HGLQVPDTKL 900
FSEATNFNEL NQLAEEAKRR AEIARQRELH TLKGHVESVV KLKGLDIETI 950
QQSYTV 956
Length:956
Mass (Da):105,048
Last modified:November 1, 1996 - v1
Checksum:iEC09622F256CDFD6
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
M27888 Genomic DNA. Translation: AAA34052.1.
PIRiA43637.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
M27888 Genomic DNA. Translation: AAA34052.1 .
PIRi A43637.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
3M50 X-ray 2.60 P 927-954 [» ]
3M51 X-ray 3.25 P 927-954 [» ]
4DX0 X-ray 3.40 P 927-954 [» ]
ProteinModelPortali Q42932.
SMRi Q42932. Positions 905-956.
ModBasei Search...
MobiDBi Search...

Proteomic databases

ProMEXi Q42932.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Miscellaneous databases

EvolutionaryTracei Q42932.

Family and domain databases

Gene3Di 1.20.1110.10. 3 hits.
2.70.150.10. 2 hits.
3.40.1110.10. 1 hit.
InterProi IPR004014. ATPase_P-typ_cation-transptr_N.
IPR023299. ATPase_P-typ_cyto_domN.
IPR018303. ATPase_P-typ_P_site.
IPR023298. ATPase_P-typ_TM_dom.
IPR008250. ATPase_P-typ_transduc_dom_A.
IPR001757. Cation_transp_P_typ_ATPase.
IPR006534. H+_ATPase_P-typ_IIIA.
IPR023214. HAD-like_dom.
[Graphical view ]
Pfami PF00690. Cation_ATPase_N. 1 hit.
PF00122. E1-E2_ATPase. 1 hit.
PF00702. Hydrolase. 1 hit.
[Graphical view ]
PRINTSi PR00119. CATATPASE.
PR00120. HATPASE.
SMARTi SM00831. Cation_ATPase_N. 1 hit.
[Graphical view ]
SUPFAMi SSF56784. SSF56784. 1 hit.
TIGRFAMsi TIGR01647. ATPase-IIIA_H. 1 hit.
TIGR01494. ATPase_P-type. 2 hits.
PROSITEi PS00154. ATPASE_E1_E2. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

  1. "Molecular cloning of a family of plant genes encoding a protein homologous to plasma membrane H+-translocating ATPases."
    Boutry M., Michelet B., Goffeau A.
    Biochem. Biophys. Res. Commun. 162:567-574(1989) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE.
  2. "Identification and structure of small-molecule stabilizers of 14-3-3 protein-protein interactions."
    Rose R., Erdmann S., Bovens S., Wolf A., Rose M., Hennig S., Waldmann H., Ottmann C.
    Angew. Chem. Int. Ed. 49:4129-4132(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.60 ANGSTROMS) OF 927-954.
  3. "An optimised small-molecule stabiliser of the 14-3-3-PMA2 protein-protein interaction."
    Richter A., Rose R., Hedberg C., Waldmann H., Ottmann C.
    Chemistry 18:6520-6527(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (3.40 ANGSTROMS) OF 927-954.

Entry informationi

Entry nameiQ42932_NICPL
AccessioniPrimary (citable) accession number: Q42932
Entry historyi
Integrated into UniProtKB/TrEMBL: November 1, 1996
Last sequence update: November 1, 1996
Last modified: September 3, 2014
This is version 93 of the entry and version 1 of the sequence. [Complete history]
Entry statusiUnreviewed (UniProtKB/TrEMBL)

Miscellaneousi

Keywords - Technical termi

3D-structureImported

External Data

Dasty 3

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