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3.A.1.122.14
ABC transporter of unknown function, but aspects of its structure and mechanism of action are known (Yuan et al. 2001; Zoghbi and Altenberg 2013).  Nucleotide-binding domain dimerization occurs as a result of binding to the natural nucleotide triphosphates, ATP, GTP, CTP and UTP, as well as the analog ATP-gamma-S. All the natural nucleotide triphosphates are hydrolyzed at similar rates, whereas ATP-gamma-S is not hydrolyzed. The non-hydrolyzable ATP analog AMP-PNP, frequently assumed to produce the nucleotide-bound conformation, failed to elicit nucleotide-binding domain dimerization (Fendley et al. 2016).

Accession Number:Q58206
Protein Name:Uncharacterized ABC transporter ATP-binding protein MJ0796
Length:235
Molecular Weight:26566.00
Species:Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440) [243232]
Number of TMSs:1
Substrate Unknown

Cross database links:

Structure:
1F3O   1L2T   3TIF     

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)
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FASTA formatted sequence
1:	MIKLKNVTKT YKMGEEIIYA LKNVNLNIKE GEFVSIMGPS GSGKSTMLNI IGCLDKPTEG 
61:	EVYIDNIKTN DLDDDELTKI RRDKIGFVFQ QFNLIPLLTA LENVELPLIF KYRGAMSGEE 
121:	RRKRALECLK MAELEERFAN HKPNQLSGGQ QQRVAIARAL ANNPPIILAD EPTGALDSKT 
181:	GEKIMQLLKK LNEEDGKTVV VVTHDINVAR FGERIIYLKD GEVEREEKLR GFDDR