desiccation/radiation resistance protein [Deinococcus knuensis]
PQQ-binding-like beta-propeller repeat protein( domain architecture ID 11445572)
PQQ (pyrrolo-quinoline quinone)-like beta-propeller repeat protein contains several instances of a beta-propeller repeat; similar to Bacillus subtilis protein YxaL
List of domain hits
Name | Accession | Description | Interval | E-value | |||||
PQQ super family | cl34291 | Outer membrane protein assembly factor BamB, contains PQQ-like beta-propeller repeat [Cell ... |
72-347 | 1.53e-23 | |||||
Outer membrane protein assembly factor BamB, contains PQQ-like beta-propeller repeat [Cell wall/membrane/envelope biogenesis]; The actual alignment was detected with superfamily member COG1520: Pssm-ID: 441129 [Multi-domain] Cd Length: 370 Bit Score: 102.58 E-value: 1.53e-23
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Name | Accession | Description | Interval | E-value | |||||
PQQ | COG1520 | Outer membrane protein assembly factor BamB, contains PQQ-like beta-propeller repeat [Cell ... |
72-347 | 1.53e-23 | |||||
Outer membrane protein assembly factor BamB, contains PQQ-like beta-propeller repeat [Cell wall/membrane/envelope biogenesis]; Pssm-ID: 441129 [Multi-domain] Cd Length: 370 Bit Score: 102.58 E-value: 1.53e-23
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PQQ_2 | pfam13360 | PQQ-like domain; This domain contains several repeats of the PQQ repeat. |
63-280 | 7.05e-23 | |||||
PQQ-like domain; This domain contains several repeats of the PQQ repeat. Pssm-ID: 433144 [Multi-domain] Cd Length: 233 Bit Score: 97.47 E-value: 7.05e-23
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assembly_YfgL | TIGR03300 | outer membrane assembly lipoprotein YfgL; Members of this protein family are YfgL, a ... |
72-351 | 1.14e-20 | |||||
outer membrane assembly lipoprotein YfgL; Members of this protein family are YfgL, a lipoprotein component of a complex that acts protein insertion into the bacterial outer membrane. Other members of this complex are NlpB, YfiO, and YaeT. This protein contains multiple copies of a repeat that, in other contexts, are associated with binding of the coenzyme PQQ. [Protein fate, Protein and peptide secretion and trafficking] Pssm-ID: 274511 [Multi-domain] Cd Length: 377 Bit Score: 93.84 E-value: 1.14e-20
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BamB_YfgL | cd10276 | Beta-barrel assembly machinery (Bam) complex component B and related proteins; BamB (YflG) is ... |
115-347 | 1.37e-19 | |||||
Beta-barrel assembly machinery (Bam) complex component B and related proteins; BamB (YflG) is a non-essential component of the beta-barrel assembly machinery (Bam), a multi-subunit complex that inserts proteins with beta-barrel topology into the outer membrane. BamB has been found to interact with BamA, which in turn binds and stabilizes pre-folded beta-barrel proteins; it has been suggested that BamB participates in the stabilization. Pssm-ID: 199834 [Multi-domain] Cd Length: 358 Bit Score: 90.47 E-value: 1.37e-19
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PRK11138 | PRK11138 | outer membrane biogenesis protein BamB; Provisional |
72-276 | 4.19e-10 | |||||
outer membrane biogenesis protein BamB; Provisional Pssm-ID: 236857 [Multi-domain] Cd Length: 394 Bit Score: 61.87 E-value: 4.19e-10
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PQQ | smart00564 | beta-propeller repeat; Beta-propeller repeat occurring in enzymes with pyrrolo-quinoline ... |
250-281 | 2.06e-05 | |||||
beta-propeller repeat; Beta-propeller repeat occurring in enzymes with pyrrolo-quinoline quinone (PQQ) as cofactor, in Ire1p-like Ser/Thr kinases, and in prokaryotic dehydrogenases. Pssm-ID: 128836 [Multi-domain] Cd Length: 33 Bit Score: 41.37 E-value: 2.06e-05
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Name | Accession | Description | Interval | E-value | ||||||
PQQ | COG1520 | Outer membrane protein assembly factor BamB, contains PQQ-like beta-propeller repeat [Cell ... |
72-347 | 1.53e-23 | ||||||
Outer membrane protein assembly factor BamB, contains PQQ-like beta-propeller repeat [Cell wall/membrane/envelope biogenesis]; Pssm-ID: 441129 [Multi-domain] Cd Length: 370 Bit Score: 102.58 E-value: 1.53e-23
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PQQ_2 | pfam13360 | PQQ-like domain; This domain contains several repeats of the PQQ repeat. |
63-280 | 7.05e-23 | ||||||
PQQ-like domain; This domain contains several repeats of the PQQ repeat. Pssm-ID: 433144 [Multi-domain] Cd Length: 233 Bit Score: 97.47 E-value: 7.05e-23
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assembly_YfgL | TIGR03300 | outer membrane assembly lipoprotein YfgL; Members of this protein family are YfgL, a ... |
72-351 | 1.14e-20 | ||||||
outer membrane assembly lipoprotein YfgL; Members of this protein family are YfgL, a lipoprotein component of a complex that acts protein insertion into the bacterial outer membrane. Other members of this complex are NlpB, YfiO, and YaeT. This protein contains multiple copies of a repeat that, in other contexts, are associated with binding of the coenzyme PQQ. [Protein fate, Protein and peptide secretion and trafficking] Pssm-ID: 274511 [Multi-domain] Cd Length: 377 Bit Score: 93.84 E-value: 1.14e-20
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BamB_YfgL | cd10276 | Beta-barrel assembly machinery (Bam) complex component B and related proteins; BamB (YflG) is ... |
115-347 | 1.37e-19 | ||||||
Beta-barrel assembly machinery (Bam) complex component B and related proteins; BamB (YflG) is a non-essential component of the beta-barrel assembly machinery (Bam), a multi-subunit complex that inserts proteins with beta-barrel topology into the outer membrane. BamB has been found to interact with BamA, which in turn binds and stabilizes pre-folded beta-barrel proteins; it has been suggested that BamB participates in the stabilization. Pssm-ID: 199834 [Multi-domain] Cd Length: 358 Bit Score: 90.47 E-value: 1.37e-19
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BamB_YfgL | cd10276 | Beta-barrel assembly machinery (Bam) complex component B and related proteins; BamB (YflG) is ... |
48-348 | 4.16e-17 | ||||||
Beta-barrel assembly machinery (Bam) complex component B and related proteins; BamB (YflG) is a non-essential component of the beta-barrel assembly machinery (Bam), a multi-subunit complex that inserts proteins with beta-barrel topology into the outer membrane. BamB has been found to interact with BamA, which in turn binds and stabilizes pre-folded beta-barrel proteins; it has been suggested that BamB participates in the stabilization. Pssm-ID: 199834 [Multi-domain] Cd Length: 358 Bit Score: 83.15 E-value: 4.16e-17
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BamB_YfgL | cd10276 | Beta-barrel assembly machinery (Bam) complex component B and related proteins; BamB (YflG) is ... |
57-230 | 1.44e-13 | ||||||
Beta-barrel assembly machinery (Bam) complex component B and related proteins; BamB (YflG) is a non-essential component of the beta-barrel assembly machinery (Bam), a multi-subunit complex that inserts proteins with beta-barrel topology into the outer membrane. BamB has been found to interact with BamA, which in turn binds and stabilizes pre-folded beta-barrel proteins; it has been suggested that BamB participates in the stabilization. Pssm-ID: 199834 [Multi-domain] Cd Length: 358 Bit Score: 72.36 E-value: 1.44e-13
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PRK11138 | PRK11138 | outer membrane biogenesis protein BamB; Provisional |
72-276 | 4.19e-10 | ||||||
outer membrane biogenesis protein BamB; Provisional Pssm-ID: 236857 [Multi-domain] Cd Length: 394 Bit Score: 61.87 E-value: 4.19e-10
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PRK11138 | PRK11138 | outer membrane biogenesis protein BamB; Provisional |
124-270 | 3.63e-09 | ||||||
outer membrane biogenesis protein BamB; Provisional Pssm-ID: 236857 [Multi-domain] Cd Length: 394 Bit Score: 58.79 E-value: 3.63e-09
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Luminal_IRE1_like | cd09213 | The Luminal domain, a dimerization domain, of Inositol-requiring protein 1-like proteins; The ... |
138-278 | 9.17e-09 | ||||||
The Luminal domain, a dimerization domain, of Inositol-requiring protein 1-like proteins; The Luminal domain is a dimerization domain present in Inositol-requiring protein 1 (IRE1), eukaryotic translation Initiation Factor 2-Alpha Kinase 3 (EIF2AK3), and similar proteins. IRE1 and EIF2AK3 are serine/threonine protein kinases (STKs) and are type I transmembrane proteins that are localized in the endoplasmic reticulum (ER). They are kinase receptors that are activated through the release of BiP, a chaperone bound to their luminal domains under unstressed conditions. This results in dimerization through their luminal domains, allowing trans-autophosphorylation of their kinase domains and activation. They play roles in the signaling of the unfolded protein response (UPR), which is activated when protein misfolding is detected in the ER in order to decrease the synthesis of new proteins and increase the capacity of the ER to cope with the stress. IRE1, also called Endoplasmic reticulum (ER)-to-nucleus signaling protein (or ERN), contains an endoribonuclease domain in its cytoplasmic side and acts as an ER stress sensor. It is the oldest and most conserved component of the UPR in eukaryotes. Its activation results in the cleavage of its mRNA substrate, HAC1 in yeast and Xbp1 in metazoans, promoting a splicing event that enables translation into a transcription factor which activates the UPR. EIF2AK3, also called PKR-like Endoplasmic Reticulum Kinase (PERK), phosphorylates the alpha subunit of eIF-2, resulting in the downregulation of protein synthesis. It functions as the central regulator of translational control during the UPR pathway. In addition to the eIF-2 alpha subunit, EIF2AK3 also phosphorylates Nrf2, a leucine zipper transcription factor which regulates cellular redox status and promotes cell survival during the UPR. Pssm-ID: 188873 [Multi-domain] Cd Length: 312 Bit Score: 57.12 E-value: 9.17e-09
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PQQ_DH_like | cd00216 | PQQ-dependent dehydrogenases and related proteins; This family is composed of dehydrogenases ... |
49-281 | 7.64e-08 | ||||||
PQQ-dependent dehydrogenases and related proteins; This family is composed of dehydrogenases with pyrroloquinoline quinone (PQQ) as a cofactor, such as ethanol, methanol, and membrane-bound glucose dehydrogenases. The alignment model contains an 8-bladed beta-propeller, and the family also includes distantly related proteins which are not enzymatically active and do not bind PQQ. Pssm-ID: 199833 [Multi-domain] Cd Length: 434 Bit Score: 54.92 E-value: 7.64e-08
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NHL_like_5 | cd14963 | Uncharacterized NHL-repeat domain in bacterial proteins; The NHL (NCL-1, HT2A and LIN-41) ... |
89-246 | 2.43e-07 | ||||||
Uncharacterized NHL-repeat domain in bacterial proteins; The NHL (NCL-1, HT2A and LIN-41) repeat is found in multiple tandem copies, typically as 6 instances. It is about 40 residues long and resembles the WD repeat and other beta-propeller structures. Pssm-ID: 271333 [Multi-domain] Cd Length: 268 Bit Score: 52.29 E-value: 2.43e-07
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PQQ_DH_like | cd00216 | PQQ-dependent dehydrogenases and related proteins; This family is composed of dehydrogenases ... |
76-281 | 4.40e-07 | ||||||
PQQ-dependent dehydrogenases and related proteins; This family is composed of dehydrogenases with pyrroloquinoline quinone (PQQ) as a cofactor, such as ethanol, methanol, and membrane-bound glucose dehydrogenases. The alignment model contains an 8-bladed beta-propeller, and the family also includes distantly related proteins which are not enzymatically active and do not bind PQQ. Pssm-ID: 199833 [Multi-domain] Cd Length: 434 Bit Score: 52.61 E-value: 4.40e-07
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YvrE | COG3386 | Sugar lactone lactonase YvrE [Carbohydrate transport and metabolism]; Sugar lactone lactonase ... |
130-237 | 7.95e-07 | ||||||
Sugar lactone lactonase YvrE [Carbohydrate transport and metabolism]; Sugar lactone lactonase YvrE is part of the Pathway/BioSystem: Non-phosphorylated Entner-Doudoroff pathway Pssm-ID: 442613 [Multi-domain] Cd Length: 266 Bit Score: 50.66 E-value: 7.95e-07
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PQQ_DH_like | cd00216 | PQQ-dependent dehydrogenases and related proteins; This family is composed of dehydrogenases ... |
153-280 | 2.41e-06 | ||||||
PQQ-dependent dehydrogenases and related proteins; This family is composed of dehydrogenases with pyrroloquinoline quinone (PQQ) as a cofactor, such as ethanol, methanol, and membrane-bound glucose dehydrogenases. The alignment model contains an 8-bladed beta-propeller, and the family also includes distantly related proteins which are not enzymatically active and do not bind PQQ. Pssm-ID: 199833 [Multi-domain] Cd Length: 434 Bit Score: 49.91 E-value: 2.41e-06
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PQQ_MDH | cd10278 | Large subunit of methanol dehydrogenase (moxF); Methanol dehydrogenase is a key enzyme in the ... |
78-204 | 5.17e-06 | ||||||
Large subunit of methanol dehydrogenase (moxF); Methanol dehydrogenase is a key enzyme in the utilization of C1 compounds as a source of energy and carbon by bacteria. It catalyzes the oxidation of methanol to formaldehyde, transfering two electrons per methanol to cytochrome c(L) as the acceptor. Methanol dehydrogenase belongs to a family of dehydrogenases with pyrroloquinoline quinone (PQQ) as cofactor, which also includes dehydrogenases specific to other alcohols and membrane-bound glucose dehydrogenases. This alignment model for the large subunit contains an 8-bladed beta-propeller; the functional enzyme forms a heterotetramer composed of two large and two small subunits. Pssm-ID: 199836 [Multi-domain] Cd Length: 553 Bit Score: 49.25 E-value: 5.17e-06
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PQQ_3 | pfam13570 | PQQ-like domain; |
154-190 | 6.94e-06 | ||||||
PQQ-like domain; Pssm-ID: 463925 [Multi-domain] Cd Length: 36 Bit Score: 42.96 E-value: 6.94e-06
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PQQ | COG1520 | Outer membrane protein assembly factor BamB, contains PQQ-like beta-propeller repeat [Cell ... |
44-232 | 6.94e-06 | ||||||
Outer membrane protein assembly factor BamB, contains PQQ-like beta-propeller repeat [Cell wall/membrane/envelope biogenesis]; Pssm-ID: 441129 [Multi-domain] Cd Length: 370 Bit Score: 48.27 E-value: 6.94e-06
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PQQ | COG1520 | Outer membrane protein assembly factor BamB, contains PQQ-like beta-propeller repeat [Cell ... |
209-320 | 9.95e-06 | ||||||
Outer membrane protein assembly factor BamB, contains PQQ-like beta-propeller repeat [Cell wall/membrane/envelope biogenesis]; Pssm-ID: 441129 [Multi-domain] Cd Length: 370 Bit Score: 47.89 E-value: 9.95e-06
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Vgb | COG4257 | Streptogramin lyase [Defense mechanisms]; |
130-346 | 1.10e-05 | ||||||
Streptogramin lyase [Defense mechanisms]; Pssm-ID: 443399 [Multi-domain] Cd Length: 270 Bit Score: 47.32 E-value: 1.10e-05
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PQQ | smart00564 | beta-propeller repeat; Beta-propeller repeat occurring in enzymes with pyrrolo-quinoline ... |
250-281 | 2.06e-05 | ||||||
beta-propeller repeat; Beta-propeller repeat occurring in enzymes with pyrrolo-quinoline quinone (PQQ) as cofactor, in Ire1p-like Ser/Thr kinases, and in prokaryotic dehydrogenases. Pssm-ID: 128836 [Multi-domain] Cd Length: 33 Bit Score: 41.37 E-value: 2.06e-05
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PQQ_mGDH | cd10280 | Membrane-bound PQQ-dependent glucose dehydrogenase; This bacterial subfamily of enzymes ... |
158-279 | 2.16e-05 | ||||||
Membrane-bound PQQ-dependent glucose dehydrogenase; This bacterial subfamily of enzymes belongs to the dehydrogenase family with pyrroloquinoline quinone (PQQ) as cofactor, and is the only subfamily that is bound to the membrane. Glucose dehydrogenase converts D-glucose to D-glucono-1,5-lactone in a reaction that is coupled with the respiratory chain in the periplasmic oxidation of sugars and alcohols in gram-negative bacteria. Ubiquinone functions as the electron acceptor. The alignment model contains an 8-bladed beta-propeller. Pssm-ID: 199838 [Multi-domain] Cd Length: 616 Bit Score: 47.19 E-value: 2.16e-05
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PQQ_3 | pfam13570 | PQQ-like domain; |
194-230 | 2.44e-05 | ||||||
PQQ-like domain; Pssm-ID: 463925 [Multi-domain] Cd Length: 36 Bit Score: 41.42 E-value: 2.44e-05
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PQQ_mGDH | cd10280 | Membrane-bound PQQ-dependent glucose dehydrogenase; This bacterial subfamily of enzymes ... |
90-145 | 3.03e-05 | ||||||
Membrane-bound PQQ-dependent glucose dehydrogenase; This bacterial subfamily of enzymes belongs to the dehydrogenase family with pyrroloquinoline quinone (PQQ) as cofactor, and is the only subfamily that is bound to the membrane. Glucose dehydrogenase converts D-glucose to D-glucono-1,5-lactone in a reaction that is coupled with the respiratory chain in the periplasmic oxidation of sugars and alcohols in gram-negative bacteria. Ubiquinone functions as the electron acceptor. The alignment model contains an 8-bladed beta-propeller. Pssm-ID: 199838 [Multi-domain] Cd Length: 616 Bit Score: 46.80 E-value: 3.03e-05
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YvrE | COG3386 | Sugar lactone lactonase YvrE [Carbohydrate transport and metabolism]; Sugar lactone lactonase ... |
37-196 | 4.88e-05 | ||||||
Sugar lactone lactonase YvrE [Carbohydrate transport and metabolism]; Sugar lactone lactonase YvrE is part of the Pathway/BioSystem: Non-phosphorylated Entner-Doudoroff pathway Pssm-ID: 442613 [Multi-domain] Cd Length: 266 Bit Score: 45.27 E-value: 4.88e-05
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YvrE | COG3386 | Sugar lactone lactonase YvrE [Carbohydrate transport and metabolism]; Sugar lactone lactonase ... |
169-277 | 5.02e-05 | ||||||
Sugar lactone lactonase YvrE [Carbohydrate transport and metabolism]; Sugar lactone lactonase YvrE is part of the Pathway/BioSystem: Non-phosphorylated Entner-Doudoroff pathway Pssm-ID: 442613 [Multi-domain] Cd Length: 266 Bit Score: 45.27 E-value: 5.02e-05
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PQQ_ADH_I | cd10277 | Ethanol dehydrogenase, a bacterial quinoprotein (PQQ-dependent type I alcohol dehydrogenase); ... |
55-165 | 8.60e-05 | ||||||
Ethanol dehydrogenase, a bacterial quinoprotein (PQQ-dependent type I alcohol dehydrogenase); This bacterial family of homodimeric ethanol dehydrogenases utilize pyrroloquinoline quinone (PQQ) as a cofactor. It represents proteins whose expression may be induced by ethanol, and which are similar to quinoprotein methanol dehydrogenases, but have higher specificities for ethanol and other primary and secondary alcohols. Dehydrogenases with PQQ cofactors, such as ethanol, methanol, and membrane-bound glucose dehydrogenases, form an 8-bladed beta-propeller. Pssm-ID: 199835 [Multi-domain] Cd Length: 529 Bit Score: 45.37 E-value: 8.60e-05
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NHL_PAL_like | cd14958 | Peptidyl-alpha-hydroxyglycine alpha-amidating lyase (PAL, EC 4.3.2.5); PAL catalyzes the ... |
44-339 | 9.85e-05 | ||||||
Peptidyl-alpha-hydroxyglycine alpha-amidating lyase (PAL, EC 4.3.2.5); PAL catalyzes the N-dealkylation of peptidyl-alpha-hydroxyglycine, which results in an alpha-amidated peptide and glyoxylate. Amidation of the C-terminus is required for the activity of many peptide hormones and neuropeptides. The catalytic residues of PAL are located on several NHL-repeats. The NHL (NCL-1, HT2A and LIN-41) repeat is found in multiple tandem copies, typically as 6 instances. It is about 40 residues long and resembles the WD repeat and other beta-propeller structures. Pssm-ID: 271328 [Multi-domain] Cd Length: 300 Bit Score: 44.56 E-value: 9.85e-05
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PQQ_3 | pfam13570 | PQQ-like domain; |
114-150 | 1.15e-04 | ||||||
PQQ-like domain; Pssm-ID: 463925 [Multi-domain] Cd Length: 36 Bit Score: 39.49 E-value: 1.15e-04
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PQQ_ADH_I | cd10277 | Ethanol dehydrogenase, a bacterial quinoprotein (PQQ-dependent type I alcohol dehydrogenase); ... |
158-279 | 1.20e-04 | ||||||
Ethanol dehydrogenase, a bacterial quinoprotein (PQQ-dependent type I alcohol dehydrogenase); This bacterial family of homodimeric ethanol dehydrogenases utilize pyrroloquinoline quinone (PQQ) as a cofactor. It represents proteins whose expression may be induced by ethanol, and which are similar to quinoprotein methanol dehydrogenases, but have higher specificities for ethanol and other primary and secondary alcohols. Dehydrogenases with PQQ cofactors, such as ethanol, methanol, and membrane-bound glucose dehydrogenases, form an 8-bladed beta-propeller. Pssm-ID: 199835 [Multi-domain] Cd Length: 529 Bit Score: 44.98 E-value: 1.20e-04
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NHL_like_3 | cd14956 | Uncharacterized NHL-repeat domain in bacterial proteins; The NHL (NCL-1, HT2A and LIN-41) ... |
41-271 | 5.32e-04 | ||||||
Uncharacterized NHL-repeat domain in bacterial proteins; The NHL (NCL-1, HT2A and LIN-41) repeat is found in multiple tandem copies, typically as 6 instances. It is about 40 residues long and resembles the WD repeat and other beta-propeller structures. Pssm-ID: 271326 [Multi-domain] Cd Length: 274 Bit Score: 42.27 E-value: 5.32e-04
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Luminal_IRE1 | cd09769 | The Luminal domain, a dimerization domain, of the Serine/Threonine protein kinase, ... |
138-232 | 1.43e-03 | ||||||
The Luminal domain, a dimerization domain, of the Serine/Threonine protein kinase, Inositol-requiring protein 1; The Luminal domain is a dimerization domain present in Inositol-requiring protein 1 (IRE1), a serine/threonine protein kinase (STK) and a type I transmembrane protein that is localized in the endoplasmic reticulum (ER). IRE1, also called Endoplasmic reticulum (ER)-to-nucleus signaling protein (or ERN), is a kinase receptor that also contains an endoribonuclease domain in the cytoplasmic side. It plays roles in the signaling of the unfolded protein response (UPR), which is activated when protein misfolding is detected in the ER in order to decrease the synthesis of new proteins and increase the capacity of the ER to cope with the stress. IRE1 acts as an ER stress sensor and is the oldest and most conserved component of the UPR in eukaryotes. During ER stress, IRE1 dimerizes through its luminal domain and forms oligomers, allowing the kinase domain to undergo trans-autophosphorylation. This leads to a conformational change that stimulates its endoribonuclease activity and results in the cleavage of its mRNA substrate, HAC1 in yeast and Xbp1 in metazoans, promoting a splicing event that enables translation into a transcription factor which activates the UPR. Mammals contain two IRE1 proteins, IRE1alpha (or ERN1) and IRE1beta (or ERN2). IRE1alpha is expressed in all cells and tissues while IRE1beta is found only in intestinal epithelial cells. Pssm-ID: 188875 [Multi-domain] Cd Length: 295 Bit Score: 40.76 E-value: 1.43e-03
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Vgb | COG4257 | Streptogramin lyase [Defense mechanisms]; |
49-196 | 1.78e-03 | ||||||
Streptogramin lyase [Defense mechanisms]; Pssm-ID: 443399 [Multi-domain] Cd Length: 270 Bit Score: 40.39 E-value: 1.78e-03
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PQQ | smart00564 | beta-propeller repeat; Beta-propeller repeat occurring in enzymes with pyrrolo-quinoline ... |
210-241 | 2.59e-03 | ||||||
beta-propeller repeat; Beta-propeller repeat occurring in enzymes with pyrrolo-quinoline quinone (PQQ) as cofactor, in Ire1p-like Ser/Thr kinases, and in prokaryotic dehydrogenases. Pssm-ID: 128836 [Multi-domain] Cd Length: 33 Bit Score: 35.59 E-value: 2.59e-03
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PQQ | smart00564 | beta-propeller repeat; Beta-propeller repeat occurring in enzymes with pyrrolo-quinoline ... |
170-201 | 3.45e-03 | ||||||
beta-propeller repeat; Beta-propeller repeat occurring in enzymes with pyrrolo-quinoline quinone (PQQ) as cofactor, in Ire1p-like Ser/Thr kinases, and in prokaryotic dehydrogenases. Pssm-ID: 128836 [Multi-domain] Cd Length: 33 Bit Score: 35.20 E-value: 3.45e-03
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PQQ | pfam01011 | PQQ enzyme repeat; The family represent a single repeat of a beta propeller. This propeller ... |
256-281 | 3.81e-03 | ||||||
PQQ enzyme repeat; The family represent a single repeat of a beta propeller. This propeller has been found in several enzymes which utilize pyrrolo-quinoline quinone as a prosthetic group. Pssm-ID: 395799 [Multi-domain] Cd Length: 36 Bit Score: 35.25 E-value: 3.81e-03
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PQQ_3 | pfam13570 | PQQ-like domain; |
234-270 | 6.83e-03 | ||||||
PQQ-like domain; Pssm-ID: 463925 [Multi-domain] Cd Length: 36 Bit Score: 34.49 E-value: 6.83e-03
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PQQ | smart00564 | beta-propeller repeat; Beta-propeller repeat occurring in enzymes with pyrrolo-quinoline ... |
90-121 | 7.66e-03 | ||||||
beta-propeller repeat; Beta-propeller repeat occurring in enzymes with pyrrolo-quinoline quinone (PQQ) as cofactor, in Ire1p-like Ser/Thr kinases, and in prokaryotic dehydrogenases. Pssm-ID: 128836 [Multi-domain] Cd Length: 33 Bit Score: 34.43 E-value: 7.66e-03
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Blast search parameters | ||||
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