3.4.21.105: rhomboid protease
This is an abbreviated version!
For detailed information about rhomboid protease, go to the full flat file.
Word Map on EC 3.4.21.105
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3.4.21.105
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flap
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drosophila
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medial
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dorsal
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posterior
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ventral
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glossitis
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midline
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trapezius
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shoulder
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thalamic
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scapula
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fossa
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pilonidal
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reuniens
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serratus
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paraventricular
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levator
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er-associated
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intercostal
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ventromedial
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ventrolateral
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mediodorsal
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intralaminar
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parafascicular
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sacrococcygeal
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abduct
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electromyographic
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paracentral
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retrotranslocation
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aesthetic
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latissimus
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cheilitis
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birefringent
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erector
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anteroventral
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nicastrin
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anteromedial
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supraspinatus
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incerta
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clavicle
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myofascial
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site-2
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argos
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extradural
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seromas
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petrous
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infraspinatus
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gurken
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glenohumeral
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analysis
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medicine
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molecular biology
Reaction
cleaves type-1 transmembrane domains using a catalytic dyad composed of serine and histidine that are contributed by different transmembrane domains
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Synonyms
AAR, AarA, AqRho, Derlin-1, EhROM1, GlpG, GlpP, intramembrane protease, microneme rhomboid protease, More, paGlpG, PARL, PBANKA_110650, PbROM1, Pcp1, Pcp1/Rbd1, pfROM4, presenilin associated rhomboid like protein, presenilin-associated rhomboid-like, presenilin-associated rhomboid-like protein, presenilins-associated rhomboid-like protein, PSARL, Rbd1, Rbd1p, RBL1, RBL10, RBL11, RBL12, RBL2, RBL3, RBL4, RBL5, RBL6, RBL7, RBL8, RBL9, Rhbdd1, RHBDL, RHBDL2, RHBDL4, RHDBL-2, Rho, RHO-1, rho-4, Rho-7, RhoII, Rhomboid, Rhomboid 4, rhomboid intramembrane protease, rhomboid Pcp1/Rbd1, rhomboid peptidase Pcp1, rhomboid protease, Rhomboid protease AarA, Rhomboid protease glpG, Rhomboid protease gluP, rhomboid protease Pcp1, rhomboid protease PSARL, Rhomboid protein, rhomboid protein 1, rhomboid protein 4, rhomboid pseudoprotease, rhomboid serine protease, rhomboid-1, rhomboid-1 protease, rhomboid-2, rhomboid-3, rhomboid-4, rhomboid-like protein, rhomboid-like protein 10, rhomboid-related protein 4, rhomboid-type protease Pcp1, ROM1, ROM4, ROM5, Spitz protease, TgROM1, TgROM2, TgROM3, TgROM4, TgROM5, Ygr101w, Yqgp
ECTree
Subunits
Subunits on EC 3.4.21.105 - rhomboid protease
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x * 69000, SDS-PAGE
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x * 69000, SDS-PAGE
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x * 3000, and x* 33000, SDS-PAGE
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x * 31000, SDS-PAGE. Upon incubation of enzyme at 37 °C, lower species start to occur
dimer
2 * 54700, native protein, 2 * 94543, protein with detergent bound, calculated
dimer
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2 * 54700, native protein, 2 * 94543, protein with detergent bound, calculated
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dimer
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2 * 31772, native protein, 2 * 71615, protein with detergent bound, calculated
dimer
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2 * 31772, native protein, 2 * 71615, protein with detergent bound, calculated
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dimer
2 * 22124, native protein, 2 * 61967, protein with detergent bound, calculated. Enzyme is dimeric and functional in dodecylmaltoside detergent solution. The dimer is present in the lipid bilayer suggesting a physiological dimer. Rhomboids form oligomers that are facilitated by the membrane domain
dimer
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2 * 22124, native protein, 2 * 61967, protein with detergent bound, calculated. Enzyme is dimeric and functional in dodecylmaltoside detergent solution. The dimer is present in the lipid bilayer suggesting a physiological dimer. Rhomboids form oligomers that are facilitated by the membrane domain
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additional information
protein is predecited to have 7 transmembrane domains
additional information
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protein is predecited to have 7 transmembrane domains
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additional information
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rhomboids do not function as a partof a multiprotein complex
additional information
determination and classification of intramembrane rhomboid topology, modeling, overview
additional information
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determination and classification of intramembrane rhomboid topology, modeling, overview
additional information
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rhomboids do not function as a part of a multiprotein complex
additional information
determination and classification of intramembrane rhomboid topology, modeling, overview
additional information
GlpG structure and active site structure, overview
additional information
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GlpG structure and active site structure, overview
additional information
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molecular structure, alternative conformations for the putative gating helix 5 of GlpG, GlpG forms a water-filled cavity on the extracellular side of GlpG, with the catalytic serine at its base, overview
additional information
structure modeling, structure-function relationship, overview
additional information
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structure modeling, structure-function relationship, overview
additional information
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protein is predecited to have 6 transmembrane domains
additional information
the cytoplasmic domain of the Escherichia coli GlpG rhomboid protease undergoes slow dimerization via domain swapping. Micromolar concentrations of micelles enhance monomer-dimer exchange rates by more than 1000fold. Detergents bearing a phosphocholine headgroup are true catalysts, with hexadecylphosphocholine reducing the 26 kcal/mol free energy barrier by more than 11 kcal/mol while preserving the 5 kcal/mol difference between monomer and dimer states. Catalysis involves the formation of a micelle-bound intermediate with a partially unfolded structure that is primed for domain swapping
additional information
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the cytoplasmic domain of the Escherichia coli GlpG rhomboid protease undergoes slow dimerization via domain swapping. Micromolar concentrations of micelles enhance monomer-dimer exchange rates by more than 1000fold. Detergents bearing a phosphocholine headgroup are true catalysts, with hexadecylphosphocholine reducing the 26 kcal/mol free energy barrier by more than 11 kcal/mol while preserving the 5 kcal/mol difference between monomer and dimer states. Catalysis involves the formation of a micelle-bound intermediate with a partially unfolded structure that is primed for domain swapping
additional information
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protein is predecited to have 6 transmembrane domains
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additional information
molecular structure, alternative conformations for the putative gating helix 5 of GlpG, overview
additional information
protein is predecited to have 6 transmembrane domains
additional information
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protein is predecited to have 6 transmembrane domains
additional information
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protein is predecited to have 6 transmembrane domains
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additional information
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determination and classification of intramembrane rhomboid topology, modeling, overview
additional information
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determination and classification of intramembrane rhomboid topology, modeling, overview
additional information
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determination and classification of intramembrane rhomboid topology, modeling, overview
additional information
determination and classification of intramembrane rhomboid topology, modeling, overview
additional information
determination and classification of intramembrane rhomboid topology, modeling, overview
additional information
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the intramembrane enzyme possesses an N-terminal cytosolic domain NRho consisting of an alpha/beta fold, solution NMR structure and dynamics, structural plasticity may facilitate the ability of NRho to recognize and associate with membranes, membrane protein topology, overview
additional information
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determination and classification of intramembrane rhomboid topology, modeling, overview
additional information
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determination and classification of intramembrane rhomboid topology, modeling, overview