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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 annotation, 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

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.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ42932.

Family & Domainsi

Sequence similaritiesi

Belongs to the cation transport ATPase (P-type) (TC 3.A.3) family. [View classification]UniRule annotation

Keywords - Domaini

Transmembrane, Transmembrane helixSAAS annotation

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

        10         20         30         40         50
MGEKPEVLDA VLKETVDLEN IPIEEVFENL RCTKEGLSGP AAQERLAIFG
60 70 80 90 100
YNKLEEKKES KFLKFLGFMW NPLSWVMEAA AIMAIALANG GGKPPDWQDF
110 120 130 140 150
VGIITLLVIN STISFIEENN AGNAAAALMA RLAPKAKVLR DGKWDEQDAA
160 170 180 190 200
ILVPGDIISI KLGDIIPADA RLLEGDPLKI DQSALTGESL PVTKGPGDGV
210 220 230 240 250
YSGSTCKQGE IEAVVIATGV HTFFGKAAHL VDSTNQVGHF QKVLTAIGNF
260 270 280 290 300
CICSIAVGMI IEIIVMYPIQ HRKYRPGIDN LLVLLIGGIP IAMPTVLSVT
310 320 330 340 350
MAIGSHRLAQ QGAITKRMTA IEEMAGMDVL CSDKTGTLTL NKLTVDKNLV
360 370 380 390 400
EVFAKGVDAD TVVLMAARAS RTENQDAIDT AIVGMLSDPK EARAGIREIH
410 420 430 440 450
FLPFNPTDKR TALTYLDGEG KMHRVSKGAP EQILNLAHNK SDIERRVHSV
460 470 480 490 500
IDKFAERGLR SLGVAYQEVP EGRKESTGGP WQFIGLLPLF DPPRHDSAET
510 520 530 540 550
IRRALNLGVN VKMITGDQLA IGKETGRRLG MGTNMYPSSA LLGQTKDESI
560 570 580 590 600
ASLPIDELIE KADGFAGVFP EHKYEIVKRL QARKHICGMT GDGVNDAPAL
610 620 630 640 650
KKADIGIAVD DATDAARSAS DIVLTEPGLS VIISAVLTSR AIFQRMKNYT
660 670 680 690 700
IYAVSITIRI VLGFMLLALI WKFDFPPFMV LIIAILNDGT IMTISKDRVK
710 720 730 740 750
PSPLPDSWKL AEIFTTGVVL GGYLAMMTVI FFWAAYETDF FPRVFGVSTL
760 770 780 790 800
QKTATDDFRK LASAIYLQVS TISQALIFVT RSRSWSFVER PGLLLVVAFL
810 820 830 840 850
IAQLVATLIA VYANWAFAAI EGIGWGWAGV IWLYNLVFYF PLDIIKFLIR
860 870 880 890 900
YALSGRAWDL VLEQRIAFTR KKDFGKEQRE LQWAHAQRTL HGLQVPDTKL
910 920 930 940 950
FSEATNFNEL NQLAEEAKRR AEIARQRELH TLKGHVESVV KLKGLDIETI

QQSYTV
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...

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: October 29, 2014
This is version 95 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