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1.A.2.2.2
The KirBac3.1 K+ channel (a dimer of dimers with gating visualized by atomic force microscopy, Jaroslawski et al., 2007) (regulated by binding lipids, G-proteins, nucleotides, and ions (H+, Ca2+, and Mg2+)). The 3-D structure is available (1XL6_A).  The inhibitory cholesterol binding site has been identified (Fürst et al. 2014). The constricted opening in this, and presumably other, Kir channels does not impede potassium conduction (Black et al. 2020).

Accession Number:D9N164
Protein Name:Potassium channel
Length:301
Molecular Weight:33738.00
Species:Magnetospirillum magnetotacticum [188]
Number of TMSs:3
Substrate K+

Cross database links:

Pfam: PF01007   

Gene Ontology

GO:0016020 C:membrane
GO:0005242 F:inward rectifier potassium channel activity
Structure:
1XL6   2WLH   2WLI   2WLJ   2WLK   2WLM   2WLN   2WLO   2X6A   2X6B   [...more]

External Searches:

  • Search: DB with
  • BLAST ExPASy (Swiss Institute of Bioinformatics (SIB) BLAST)
  • CDD Search (Conserved Domain Database)
  • Search COGs (Clusters of Orthologous Groups of proteins)
  • 2° Structure (Network Protein Sequence Analysis)

Analyze:

Predict TMSs (Predict number of transmembrane segments)
Window Size: Angle:  
FASTA formatted sequence
1:	MTGGMKPPAR KPRILNSDGS SNITRLGLEK RGWLDDHYHD LLTVSWPVFI TLITGLYLVT 
61:	NALFALAYLA CGDVIENARP GSFTDAFFFS VQTMATIGYG KLIPIGPLAN TLVTLEALCG 
121:	MLGLAVAASL IYARFTRPTA GVLFSSRMVI SDFEGKPTLM MRLANLRIEQ IIEADVHLVL 
181:	VRSEISQEGM VFRRFHDLTL TRSRSPIFSL SWTVMHPIDH HSPIYGETDE TLRNSHSEFL 
241:	VLFTGHHEAF AQNVHARHAY SCDEIIWGGH FVDVFTTLPD GRRALDLGKF HEIAQHHHHH 
301:	H