CBS domain-containing protein [Escherichia coli]
Protein Classification
nucleotidyltransferase family protein( domain architecture ID 10140128)
nucleotidyltransferase family protein containing a cystathionine beta-synthase (CBS) pair, called the Bateman domain, may transfer nucleotides onto phosphosugars
List of domain hits
| Name | Accession | Description | Interval | E-value | ||||
| NTP_transferase_like_2 | cd06426 | NTP_trnasferase_like_2 is a member of the nucleotidyl transferase family; This is a subfamily ... |
122-343 | 2.47e-121 | ||||
NTP_trnasferase_like_2 is a member of the nucleotidyl transferase family; This is a subfamily of nucleotidyl transferases. Nucleotidyl transferases transfer nucleotides onto phosphosugars. The activated sugars are precursors for synthesis of lipopolysaccharide, glycolipids and polysaccharides. Other subfamilies of nucleotidyl transferases include Alpha-D-Glucose-1-Phosphate Cytidylyltransferase, Mannose-1-phosphate guanyltransferase, and Glucose-1-phosphate thymidylyltransferase. : Pssm-ID: 133048 [Multi-domain] Cd Length: 220 Bit Score: 348.73 E-value: 2.47e-121
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| CBS_pair_NTP_transferase_assoc | cd04607 | Two tandem repeats of the cystathionine beta-synthase (CBS pair) domain associated with the ... |
4-112 | 1.64e-54 | ||||
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domain associated with the NTP (Nucleotidyl transferase) domain; This cd contains two tandem repeats of the cystathionine beta-synthase (CBS pair) domain associated with the NTP (Nucleotidyl transferase) domain downstream. The CBS domain, named after human CBS, is a small domain originally identified in cystathionine beta-synthase and is subsequently found in a wide range of different proteins. CBS domains usually occur in tandem repeats. They associate to form a so-called Bateman domain or a CBS pair based on crystallographic studies in bacteria. The CBS pair was used as a basis for this cd hierarchy since the human CBS proteins can adopt the typical core structure and form an intramolecular CBS pair. The interface between the two CBS domains forms a cleft that is a potential ligand binding site. The CBS pair coexists with a variety of other functional domains and this has been used to help in its classification here. It has been proposed that the CBS domain may play a regulatory role, although its exact function is unknown. Mutations of conserved residues within this domain are associated with a variety of human hereditary diseases, including congenital myotonia, idiopathic generalized epilepsy, hypercalciuric nephrolithiasis, and classic Bartter syndrome (CLC chloride channel family members), Wolff-Parkinson-White syndrome (gamma 2 subunit of AMP-activated protein kinase), retinitis pigmentosa (IMP dehydrogenase-1), and homocystinuria (cystathionine beta-synthase). : Pssm-ID: 341381 [Multi-domain] Cd Length: 112 Bit Score: 174.17 E-value: 1.64e-54
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| Name | Accession | Description | Interval | E-value | |||||
| NTP_transferase_like_2 | cd06426 | NTP_trnasferase_like_2 is a member of the nucleotidyl transferase family; This is a subfamily ... |
122-343 | 2.47e-121 | |||||
NTP_trnasferase_like_2 is a member of the nucleotidyl transferase family; This is a subfamily of nucleotidyl transferases. Nucleotidyl transferases transfer nucleotides onto phosphosugars. The activated sugars are precursors for synthesis of lipopolysaccharide, glycolipids and polysaccharides. Other subfamilies of nucleotidyl transferases include Alpha-D-Glucose-1-Phosphate Cytidylyltransferase, Mannose-1-phosphate guanyltransferase, and Glucose-1-phosphate thymidylyltransferase. Pssm-ID: 133048 [Multi-domain] Cd Length: 220 Bit Score: 348.73 E-value: 2.47e-121
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| GCD1 | COG1208 | NDP-sugar pyrophosphorylase, includes eIF-2Bgamma, eIF-2Bepsilon, and LPS biosynthesis protein ... |
121-346 | 2.83e-83 | |||||
NDP-sugar pyrophosphorylase, includes eIF-2Bgamma, eIF-2Bepsilon, and LPS biosynthesis protein s [Translation, ribosomal structure and biogenesis, Cell wall/membrane/envelope biogenesis]; Pssm-ID: 440821 [Multi-domain] Cd Length: 238 Bit Score: 252.38 E-value: 2.83e-83
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| CBS_pair_NTP_transferase_assoc | cd04607 | Two tandem repeats of the cystathionine beta-synthase (CBS pair) domain associated with the ... |
4-112 | 1.64e-54 | |||||
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domain associated with the NTP (Nucleotidyl transferase) domain; This cd contains two tandem repeats of the cystathionine beta-synthase (CBS pair) domain associated with the NTP (Nucleotidyl transferase) domain downstream. The CBS domain, named after human CBS, is a small domain originally identified in cystathionine beta-synthase and is subsequently found in a wide range of different proteins. CBS domains usually occur in tandem repeats. They associate to form a so-called Bateman domain or a CBS pair based on crystallographic studies in bacteria. The CBS pair was used as a basis for this cd hierarchy since the human CBS proteins can adopt the typical core structure and form an intramolecular CBS pair. The interface between the two CBS domains forms a cleft that is a potential ligand binding site. The CBS pair coexists with a variety of other functional domains and this has been used to help in its classification here. It has been proposed that the CBS domain may play a regulatory role, although its exact function is unknown. Mutations of conserved residues within this domain are associated with a variety of human hereditary diseases, including congenital myotonia, idiopathic generalized epilepsy, hypercalciuric nephrolithiasis, and classic Bartter syndrome (CLC chloride channel family members), Wolff-Parkinson-White syndrome (gamma 2 subunit of AMP-activated protein kinase), retinitis pigmentosa (IMP dehydrogenase-1), and homocystinuria (cystathionine beta-synthase). Pssm-ID: 341381 [Multi-domain] Cd Length: 112 Bit Score: 174.17 E-value: 1.64e-54
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| Arch_glmU | TIGR03992 | UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate N-acetyltransferase; The ... |
123-335 | 6.55e-40 | |||||
UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate N-acetyltransferase; The MJ_1101 protein from Methanococcus jannaschii has been characterized as the GlmU enzyme catalyzing the final two steps of UDP-GlcNAc biosynthesis. Many of the genes identified by this model are in proximity to the GlmS and GlmM genes and are also presumed to be GlmU. However, some archaeal genomes contain multiple closely-related homologs from this family and it is not clear what the substrate specificity is for each of them. Pssm-ID: 274908 [Multi-domain] Cd Length: 393 Bit Score: 145.04 E-value: 6.55e-40
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| NTP_transferase | pfam00483 | Nucleotidyl transferase; This family includes a wide range of enzymes which transfer ... |
124-346 | 2.78e-34 | |||||
Nucleotidyl transferase; This family includes a wide range of enzymes which transfer nucleotides onto phosphosugars. Pssm-ID: 425709 [Multi-domain] Cd Length: 243 Bit Score: 126.21 E-value: 2.78e-34
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| CBS | COG0517 | CBS domain [Signal transduction mechanisms]; |
8-120 | 2.17e-21 | |||||
CBS domain [Signal transduction mechanisms]; Pssm-ID: 440283 [Multi-domain] Cd Length: 128 Bit Score: 88.38 E-value: 2.17e-21
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| glgC | PRK05293 | glucose-1-phosphate adenylyltransferase; Provisional |
124-346 | 1.33e-11 | |||||
glucose-1-phosphate adenylyltransferase; Provisional Pssm-ID: 179997 [Multi-domain] Cd Length: 380 Bit Score: 64.89 E-value: 1.33e-11
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| IMPDH | pfam00478 | IMP dehydrogenase / GMP reductase domain; This family is involved in biosynthesis of guanosine ... |
8-120 | 1.05e-09 | |||||
IMP dehydrogenase / GMP reductase domain; This family is involved in biosynthesis of guanosine nucleotide. Members of this family contain a TIM barrel structure. In the inosine monophosphate dehydrogenases 2 CBS domains pfam00571 are inserted in the TIM barrel. This family is a member of the common phosphate binding site TIM barrel family. Pssm-ID: 459826 [Multi-domain] Cd Length: 463 Bit Score: 59.32 E-value: 1.05e-09
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| PRK10892 | PRK10892 | arabinose-5-phosphate isomerase KdsD; |
10-106 | 9.11e-08 | |||||
arabinose-5-phosphate isomerase KdsD; Pssm-ID: 182814 [Multi-domain] Cd Length: 326 Bit Score: 53.19 E-value: 9.11e-08
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| CBS | smart00116 | Domain in cystathionine beta-synthase and other proteins; Domain present in all 3 forms of ... |
8-49 | 1.39e-06 | |||||
Domain in cystathionine beta-synthase and other proteins; Domain present in all 3 forms of cellular life. Present in two copies in inosine monophosphate dehydrogenase, of which one is disordered in the crystal structure. A number of disease states are associated with CBS-containing proteins including homocystinuria, Becker's and Thomsen disease. Pssm-ID: 214522 [Multi-domain] Cd Length: 49 Bit Score: 44.81 E-value: 1.39e-06
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| Name | Accession | Description | Interval | E-value | |||||
| NTP_transferase_like_2 | cd06426 | NTP_trnasferase_like_2 is a member of the nucleotidyl transferase family; This is a subfamily ... |
122-343 | 2.47e-121 | |||||
NTP_trnasferase_like_2 is a member of the nucleotidyl transferase family; This is a subfamily of nucleotidyl transferases. Nucleotidyl transferases transfer nucleotides onto phosphosugars. The activated sugars are precursors for synthesis of lipopolysaccharide, glycolipids and polysaccharides. Other subfamilies of nucleotidyl transferases include Alpha-D-Glucose-1-Phosphate Cytidylyltransferase, Mannose-1-phosphate guanyltransferase, and Glucose-1-phosphate thymidylyltransferase. Pssm-ID: 133048 [Multi-domain] Cd Length: 220 Bit Score: 348.73 E-value: 2.47e-121
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| GCD1 | COG1208 | NDP-sugar pyrophosphorylase, includes eIF-2Bgamma, eIF-2Bepsilon, and LPS biosynthesis protein ... |
121-346 | 2.83e-83 | |||||
NDP-sugar pyrophosphorylase, includes eIF-2Bgamma, eIF-2Bepsilon, and LPS biosynthesis protein s [Translation, ribosomal structure and biogenesis, Cell wall/membrane/envelope biogenesis]; Pssm-ID: 440821 [Multi-domain] Cd Length: 238 Bit Score: 252.38 E-value: 2.83e-83
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| NTP_transferase | cd04181 | NTP_transferases catalyze the transfer of nucleotides onto phosphosugars; ... |
122-334 | 2.40e-69 | |||||
NTP_transferases catalyze the transfer of nucleotides onto phosphosugars; Nucleotidyltransferases transfer nucleotides onto phosphosugars. The enzyme family includes Alpha-D-Glucose-1-Phosphate Cytidylyltransferase, Mannose-1-phosphate guanyltransferase, and Glucose-1-phosphate thymidylyltransferase. The products are activated sugars that are precursors for synthesis of lipopolysaccharide, glycolipids and polysaccharides. Pssm-ID: 133024 [Multi-domain] Cd Length: 217 Bit Score: 216.29 E-value: 2.40e-69
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| CBS_pair_NTP_transferase_assoc | cd04607 | Two tandem repeats of the cystathionine beta-synthase (CBS pair) domain associated with the ... |
4-112 | 1.64e-54 | |||||
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domain associated with the NTP (Nucleotidyl transferase) domain; This cd contains two tandem repeats of the cystathionine beta-synthase (CBS pair) domain associated with the NTP (Nucleotidyl transferase) domain downstream. The CBS domain, named after human CBS, is a small domain originally identified in cystathionine beta-synthase and is subsequently found in a wide range of different proteins. CBS domains usually occur in tandem repeats. They associate to form a so-called Bateman domain or a CBS pair based on crystallographic studies in bacteria. The CBS pair was used as a basis for this cd hierarchy since the human CBS proteins can adopt the typical core structure and form an intramolecular CBS pair. The interface between the two CBS domains forms a cleft that is a potential ligand binding site. The CBS pair coexists with a variety of other functional domains and this has been used to help in its classification here. It has been proposed that the CBS domain may play a regulatory role, although its exact function is unknown. Mutations of conserved residues within this domain are associated with a variety of human hereditary diseases, including congenital myotonia, idiopathic generalized epilepsy, hypercalciuric nephrolithiasis, and classic Bartter syndrome (CLC chloride channel family members), Wolff-Parkinson-White syndrome (gamma 2 subunit of AMP-activated protein kinase), retinitis pigmentosa (IMP dehydrogenase-1), and homocystinuria (cystathionine beta-synthase). Pssm-ID: 341381 [Multi-domain] Cd Length: 112 Bit Score: 174.17 E-value: 1.64e-54
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| NTP_transferase_WcbM_like | cd06915 | WcbM_like is a subfamily of nucleotidyl transferases; WcbM protein of Burkholderia mallei is ... |
122-343 | 3.15e-45 | |||||
WcbM_like is a subfamily of nucleotidyl transferases; WcbM protein of Burkholderia mallei is involved in the biosynthesis, export or translocation of capsule. It is a subfamily of nucleotidyl transferases that transfer nucleotides onto phosphosugars. Pssm-ID: 133065 [Multi-domain] Cd Length: 223 Bit Score: 154.25 E-value: 3.15e-45
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| Arch_glmU | TIGR03992 | UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate N-acetyltransferase; The ... |
123-335 | 6.55e-40 | |||||
UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate N-acetyltransferase; The MJ_1101 protein from Methanococcus jannaschii has been characterized as the GlmU enzyme catalyzing the final two steps of UDP-GlcNAc biosynthesis. Many of the genes identified by this model are in proximity to the GlmS and GlmM genes and are also presumed to be GlmU. However, some archaeal genomes contain multiple closely-related homologs from this family and it is not clear what the substrate specificity is for each of them. Pssm-ID: 274908 [Multi-domain] Cd Length: 393 Bit Score: 145.04 E-value: 6.55e-40
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| G1P_TT_long | cd04189 | G1P_TT_long represents the long form of glucose-1-phosphate thymidylyltransferase; This family ... |
124-342 | 1.77e-38 | |||||
G1P_TT_long represents the long form of glucose-1-phosphate thymidylyltransferase; This family is the long form of Glucose-1-phosphate thymidylyltransferase. Glucose-1-phosphate thymidylyltransferase catalyses the formation of dTDP-glucose, from dTTP and glucose 1-phosphate. It is the first enzyme in the biosynthesis of dTDP-L-rhamnose, a cell wall constituent and a feedback inhibitor of the enzyme.There are two forms of Glucose-1-phosphate thymidylyltransferase in bacteria and archeae; short form and long form. The long form, which has an extra 50 amino acids c-terminal, is found in many species for which it serves as a sugar-activating enzyme for antibiotic biosynthesis and or other, unknown pathways, and in which dTDP-L-rhamnose is not necessarily produced.The long from enzymes also have a left-handed parallel helix domain at the c-terminus, whereas, th eshort form enzymes do not have this domain. The homotetrameric, feedback inhibited short form is found in numerous bacterial species that produce dTDP-L-rhamnose. Pssm-ID: 133032 [Multi-domain] Cd Length: 236 Bit Score: 136.93 E-value: 1.77e-38
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| NTP_transferase | pfam00483 | Nucleotidyl transferase; This family includes a wide range of enzymes which transfer ... |
124-346 | 2.78e-34 | |||||
Nucleotidyl transferase; This family includes a wide range of enzymes which transfer nucleotides onto phosphosugars. Pssm-ID: 425709 [Multi-domain] Cd Length: 243 Bit Score: 126.21 E-value: 2.78e-34
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| NTP_transferase_like_1 | cd06422 | NTP_transferase_like_1 is a member of the nucleotidyl transferase family; This is a subfamily ... |
121-342 | 1.13e-33 | |||||
NTP_transferase_like_1 is a member of the nucleotidyl transferase family; This is a subfamily of nucleotidyl transferases. Nucleotidyl transferases transfer nucleotides onto phosphosugars. The activated sugars are precursors for synthesis of lipopolysaccharide, glycolipids and polysaccharides. Other subfamilies of nucleotidyl transferases include Alpha-D-Glucose-1-Phosphate Cytidylyltransferase, Mannose-1-phosphate guanyltransferase, and Glucose-1-phosphate thymidylyltransferase. Pssm-ID: 133044 [Multi-domain] Cd Length: 221 Bit Score: 123.84 E-value: 1.13e-33
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| M1P_guanylylT_B_like_N | cd06425 | N-terminal domain of the M1P-guanylyltransferase B-isoform like proteins; GDP-mannose ... |
124-346 | 2.52e-32 | |||||
N-terminal domain of the M1P-guanylyltransferase B-isoform like proteins; GDP-mannose pyrophosphorylase (GTP: alpha-d-mannose-1-phosphate guanyltransferase) catalyzes the formation of GDP-d-mannose from GTP and alpha-d-mannose-1-Phosphate. It contains an N-terminal catalytic domain and a C-terminal Lefthanded-beta-Helix fold domain. GDP-d-mannose is the activated form of mannose for formation of cell wall lipoarabinomannan and various mannose-containing glycolipids and polysaccharides. The function of GDP-mannose pyrophosphorylase is essential for cell wall integrity, morphogenesis and viability. Repression of GDP-mannose pyrophosphorylase in yeast leads to phenotypes, such as cell lysis, defective cell wall, and failure of polarized growth and cell separation. Pssm-ID: 133047 [Multi-domain] Cd Length: 233 Bit Score: 120.78 E-value: 2.52e-32
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| rmlA_long | TIGR01208 | glucose-1-phosphate thymidylylransferase, long form; The family of known and putative ... |
124-338 | 1.18e-26 | |||||
glucose-1-phosphate thymidylylransferase, long form; The family of known and putative glucose-1-phosphate thymidyltransferase (also called dTDP-glucose synthase) shows a deep split into a short form (see TIGR01207) and a long form described by this model. The homotetrameric short form is found in numerous bacterial species that incorporate dTDP-L-rhamnose, which it helps synthesize, into the cell wall. It is subject to feedback inhibition. This form, in contrast, is found in many species for which it serves as a sugar-activating enzyme for antibiotic biosynthesis and or other, unknown pathways, and in which dTDP-L-rhamnose is not necessarily produced. Alternate name: dTDP-D-glucose synthase Pssm-ID: 273500 [Multi-domain] Cd Length: 353 Bit Score: 108.26 E-value: 1.18e-26
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| GlgC | COG0448 | Glucose-1-phosphate adenylyltransferase (ADP-glucose pyrophosphorylase) [Carbohydrate ... |
123-339 | 1.65e-22 | |||||
Glucose-1-phosphate adenylyltransferase (ADP-glucose pyrophosphorylase) [Carbohydrate transport and metabolism]; Pssm-ID: 440217 [Multi-domain] Cd Length: 377 Bit Score: 97.07 E-value: 1.65e-22
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| G1P_cytidylyltransferase | cd02524 | G1P_cytidylyltransferase catalyzes the production of CDP-D-Glucose; ... |
122-296 | 5.06e-22 | |||||
G1P_cytidylyltransferase catalyzes the production of CDP-D-Glucose; Alpha-D-Glucose-1-phosphate Cytidylyltransferase catalyzes the production of CDP-D-Glucose from alpha-D-Glucose-1-phosphate and MgCTP as substrate. CDP-D-Glucose is the precursor for synthesizing four of the five naturally occurring 3,6-dideoxy sugars-abequose (3,6-dideoxy-D-Xylo-hexose), ascarylose (3,6-dideoxy-L-arabino-hexose), paratose (3,6-dideoxy-D-ribohexose), and tyvelose (3,6-dideoxy-D-arabino-hexose. Deoxysugars are ubiquitous in nature where they function in a variety of biological processes, including cell adhesion, immune response, determination of ABO blood groups, fertilization, antibiotic function, and microbial pathogenicity. Pssm-ID: 133015 [Multi-domain] Cd Length: 253 Bit Score: 93.41 E-value: 5.06e-22
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| RmlA1 | COG1209 | dTDP-glucose pyrophosphorylase [Cell wall/membrane/envelope biogenesis]; |
124-338 | 6.45e-22 | |||||
dTDP-glucose pyrophosphorylase [Cell wall/membrane/envelope biogenesis]; Pssm-ID: 440822 [Multi-domain] Cd Length: 294 Bit Score: 94.00 E-value: 6.45e-22
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| PC_cytidylyltransferase | cd02523 | Phosphocholine cytidylyltransferases catalyze the synthesis of CDP-choline; This family ... |
124-343 | 2.01e-21 | |||||
Phosphocholine cytidylyltransferases catalyze the synthesis of CDP-choline; This family contains proteins similar to prokaryotic phosphocholine (P-cho) cytidylyltransferases. Phosphocholine (PC) cytidylyltransferases catalyze the transfer of a cytidine monophosphate from CTP to phosphocholine to form CDP-choline. PC is the most abundant phospholipid in eukaryotic membranes and it is also important in prokaryotic membranes. For pathogenic prokaryotes, the cell surface PC facilitates the interaction with host surface and induces attachment and invasion. In addition cell wall PC serves as scaffold for a group of choline-binding proteins that are secreted from the cells. Phosphocholine (PC) cytidylyltransferase is a key enzyme in the prokaryotic choline metabolism pathway. It has been hypothesized to consist of a choline transport system, a choline kinase, CTP:phosphocholine cytidylyltransferase, and a choline phosphotransferase that transfers P-Cho from CDP-Cho to either lipoteichoic acid or lipopolysaccharide. Pssm-ID: 133014 [Multi-domain] Cd Length: 229 Bit Score: 91.14 E-value: 2.01e-21
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| CBS | COG0517 | CBS domain [Signal transduction mechanisms]; |
8-120 | 2.17e-21 | |||||
CBS domain [Signal transduction mechanisms]; Pssm-ID: 440283 [Multi-domain] Cd Length: 128 Bit Score: 88.38 E-value: 2.17e-21
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| COG2905 | COG2905 | Signal-transduction protein containing cAMP-binding, CBS, and nucleotidyltransferase domains ... |
4-109 | 4.67e-21 | |||||
Signal-transduction protein containing cAMP-binding, CBS, and nucleotidyltransferase domains [Signal transduction mechanisms]; Pssm-ID: 442149 [Multi-domain] Cd Length: 124 Bit Score: 87.19 E-value: 4.67e-21
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| CBS_pair_SIS_assoc | cd04604 | Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with the ... |
1-106 | 4.81e-20 | |||||
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with the with the SIS (Sugar ISomerase) domain; This cd contains two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with the SIS (Sugar ISomerase) domain in the API [A5P (D-arabinose 5-phosphate) isomerase] protein KpsF/GutQ. These APIs catalyze the conversion of the pentose pathway intermediate D-ribulose 5-phosphate into A5P, a precursor of 3-deoxy-D-manno-octulosonate, which is an integral carbohydrate component of various glycolipids coating the surface of the outer membrane of Gram-negative bacteria, including lipopolysaccharide and many group 2 K-antigen capsules. The CBS domain, named after human CBS, is a small domain originally identified in cystathionine beta-synthase and is subsequently found in a wide range of different proteins. CBS domains usually occur in tandem repeats. They associate to form a so-called Bateman domain or a CBS pair based on crystallographic studies in bacteria. The CBS pair was used as a basis for this cd hierarchy since the human CBS proteins can adopt the typical core structure and form an intramolecular CBS pair. The interface between the two CBS domains forms a cleft that is a potential ligand binding site. The CBS pair coexists with a variety of other functional domains and this has been used to help in its classification here. It has been proposed that the CBS domain may play a regulatory role, although its exact function is unknown. Mutations of conserved residues within this domain are associated with a variety of human hereditary diseases, including congenital myotonia, idiopathic generalized epilepsy, hypercalciuric nephrolithiasis, and classic Bartter syndrome (CLC chloride channel family members), Wolff-Parkinson-White syndrome (gamma 2 subunit of AMP-activated protein kinase), retinitis pigmentosa (IMP dehydrogenase-1), and homocystinuria (cystathionine beta-synthase). Pssm-ID: 341378 [Multi-domain] Cd Length: 124 Bit Score: 84.36 E-value: 4.81e-20
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| COG1213 | COG1213 | Choline kinase [Lipid transport and metabolism]; |
124-343 | 2.35e-17 | |||||
Choline kinase [Lipid transport and metabolism]; Pssm-ID: 440826 [Multi-domain] Cd Length: 236 Bit Score: 79.90 E-value: 2.35e-17
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| CBS_pair_SF | cd02205 | Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains superfamily; The CBS ... |
8-112 | 2.80e-17 | |||||
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains superfamily; The CBS domain, named after human CBS, is a small domain originally identified in cystathionine beta-synthase and is subsequently found in a wide range of different proteins. CBS domains usually occur in tandem repeats. They associate to form a so-called Bateman domain or a CBS pair based on crystallographic studies in bacteria. The CBS pair was used as a basis for this cd hierarchy since the human CBS proteins can adopt the typical core structure and form an intramolecular CBS pair. The interface between the two CBS domains forms a cleft that is a potential ligand binding site. The CBS pair coexists with a variety of other functional domains and this has been used to help in its classification here. It has been proposed that the CBS domain may play a regulatory role, although its exact function is unknown. Mutations of conserved residues within this domain are associated with a variety of human hereditary diseases, including congenital myotonia, idiopathic generalized epilepsy, hypercalciuric nephrolithiasis, and classic Bartter syndrome (CLC chloride channel family members), Wolff-Parkinson-White syndrome (gamma 2 subunit of AMP-activated protein kinase), retinitis pigmentosa (IMP dehydrogenase-1), and homocystinuria (cystathionine beta-synthase). Pssm-ID: 341358 [Multi-domain] Cd Length: 113 Bit Score: 76.51 E-value: 2.80e-17
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| COG3448 | COG3448 | CBS-domain-containing membrane protein [Signal transduction mechanisms]; |
8-108 | 4.66e-15 | |||||
CBS-domain-containing membrane protein [Signal transduction mechanisms]; Pssm-ID: 442671 [Multi-domain] Cd Length: 136 Bit Score: 71.05 E-value: 4.66e-15
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| COG2524 | COG2524 | Predicted transcriptional regulator, contains C-terminal CBS domains [Transcription]; |
8-106 | 2.12e-14 | |||||
Predicted transcriptional regulator, contains C-terminal CBS domains [Transcription]; Pssm-ID: 442013 [Multi-domain] Cd Length: 206 Bit Score: 71.07 E-value: 2.12e-14
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| eIF-2B_gamma_N_like | cd02507 | The N-terminal of eIF-2B_gamma_like is predicted to have glycosyltransferase activity; ... |
122-256 | 4.18e-13 | |||||
The N-terminal of eIF-2B_gamma_like is predicted to have glycosyltransferase activity; N-terminal domain of eEIF-2B epsilon and gamma, subunits of eukaryotic translation initiators, is a subfamily of glycosyltranferase 2 and is predicted to have glycosyltranferase activity. eIF-2B is a guanine nucleotide-exchange factor which mediates the exchange of GDP (bound to initiation factor eIF2) for GTP, generating active eIF2.GTP complex. EIF2B is a complex multimeric protein consisting of five subunits named alpha, beta, gamma, delta and epsilon. Subunit epsilon shares sequence similarity with gamma subunit, and with a family of bifunctional nucleotide-binding enzymes such as ADP-glucose pyrophosphorylase, suggesting that epsilon subunit may play roles in nucleotide binding activity. In yeast, eIF2B gamma enhances the activity of eIF2B-epsilon leading to the idea that these subunits form the catalytic subcomplex. Pssm-ID: 133001 [Multi-domain] Cd Length: 216 Bit Score: 67.66 E-value: 4.18e-13
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| ADP_Glucose_PP | cd02508 | ADP-glucose pyrophosphorylase is involved in the biosynthesis of glycogen or starch; ... |
124-333 | 8.43e-13 | |||||
ADP-glucose pyrophosphorylase is involved in the biosynthesis of glycogen or starch; ADP-glucose pyrophosphorylase (glucose-1-phosphate adenylyltransferase) catalyzes a very important step in the biosynthesis of alpha 1,4-glucans (glycogen or starch) in bacteria and plants: synthesis of the activated glucosyl donor, ADP-glucose, from glucose-1-phosphate and ATP. ADP-glucose pyrophosphorylase is a tetrameric allosterically regulated enzyme. While a homotetramer in bacteria, in plant chloroplasts and amyloplasts, it is a heterotetramer of two different, yet evolutionary related, subunits. There are a number of conserved regions in the sequence of bacterial and plant ADP-glucose pyrophosphorylase subunits. It is a subfamily of a very diverse glycosy transferase family 2. Pssm-ID: 133002 [Multi-domain] Cd Length: 200 Bit Score: 66.41 E-value: 8.43e-13
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| eIF-2B_gamma_N | cd04198 | The N-terminal domain of gamma subunit of the eIF-2B is a subfamily of glycosyltransferase 2; ... |
122-279 | 1.81e-12 | |||||
The N-terminal domain of gamma subunit of the eIF-2B is a subfamily of glycosyltransferase 2; N-terminal domain of gamma subunit of the eukaryotic translation initiation factor 2B (eIF-2B): eIF-2B is a guanine nucleotide-exchange factor which mediates the exchange of GDP (bound to initiation factor eIF2) for GTP, generating active eIF2.GTP complex. EIF2B is a complex multimeric protein consisting of five subunits named alpha, beta, gamma, delta and epsilon. Subunit gamma shares sequence similarity with epsilon subunit, and with a family of bifunctional nucleotide-binding enzymes such as ADP-glucose pyrophosphorylase, suggesting that epsilon subunit may play roles in nucleotide binding activity. In yeast, eIF2B gamma enhances the activity of eIF2B-epsilon leading to the idea that these subunits form the catalytic subcomplex. Pssm-ID: 133041 [Multi-domain] Cd Length: 214 Bit Score: 65.76 E-value: 1.81e-12
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| CBS_pair_BON_assoc | cd04586 | Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with the ... |
6-105 | 3.46e-12 | |||||
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with the BON (bacterial OsmY and nodulation domain) domain; This cd contains two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with the BON (bacterial OsmY and nodulation domain) domain. BON is a putative phospholipid-binding domain found in a family of osmotic shock protection proteins. It is also found in some secretins and a group of potential haemolysins. Its likely function is attachment to phospholipid membranes. The CBS domain, named after human CBS, is a small domain originally identified in cystathionine beta-synthase and is subsequently found in a wide range of different proteins. CBS domains usually occur in tandem repeats. They associate to form a so-called Bateman domain or a CBS pair based on crystallographic studies in bacteria. The CBS pair was used as a basis for this cd hierarchy since the human CBS proteins can adopt the typical core structure and form an intramolecular CBS pair. The interface between the two CBS domains forms a cleft that is a potential ligand binding site. The CBS pair coexists with a variety of other functional domains and this has been used to help in its classification here. It has been proposed that the CBS domain may play a regulatory role, although its exact function is unknown. Mutations of conserved residues within this domain are associated with a variety of human hereditary diseases, including congenital myotonia, idiopathic generalized epilepsy, hypercalciuric nephrolithiasis, and classic Bartter syndrome (CLC chloride channel family members), Wolff-Parkinson-White syndrome (gamma 2 subunit of AMP-activated protein kinase), retinitis pigmentosa (IMP dehydrogenase-1), and homocystinuria (cystathionine beta-synthase). Pssm-ID: 341362 [Multi-domain] Cd Length: 137 Bit Score: 63.22 E-value: 3.46e-12
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| CBS_pair_NeuB | cd17773 | Two tandem repeats of the cystathionine beta-synthase (CBS pair) domain present in ... |
12-98 | 6.45e-12 | |||||
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domain present in N-acylneuraminate-9-phosphate synthase; This CD contains two tandem repeats of the cystathionine beta-synthase (CBS pair) domain present in N-acylneuraminate-9-phosphate synthase NeuB. NeuB catalyzes the condensation of phosphoenolpyruvate (PEP) and N-acetylmannosamine, directly forming N-acetylneuraminic acid (or sialic acid). The CBS domain, named after human CBS, is a small domain originally identified in cystathionine beta-synthase and is subsequently found in a wide range of different proteins. CBS domains usually occur in tandem repeats. They associate to form a so-called Bateman domain or a CBS pair based on crystallographic studies in bacteria. The CBS pair was used as a basis for this cd hierarchy since the human CBS proteins can adopt the typical core structure and form an intramolecular CBS pair. The interface between the two CBS domains forms a cleft that is a potential ligand binding site. The CBS pair coexists with a variety of other functional domains and this has been used to help in its classification here. It has been proposed that the CBS domain may play a regulatory role, although its exact function is unknown. Mutations of conserved residues within this domain are associated with a variety of human hereditary diseases, including congenital myotonia, idiopathic generalized epilepsy, hypercalciuric nephrolithiasis, and classic Bartter syndrome (CLC chloride channel family members), Wolff-Parkinson-White syndrome (gamma 2 subunit of AMP-activated protein kinase), retinitis pigmentosa (IMP dehydrogenase-1), and homocystinuria (cystathionine beta-synthase). Pssm-ID: 341409 [Multi-domain] Cd Length: 118 Bit Score: 61.88 E-value: 6.45e-12
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| glgC | PRK05293 | glucose-1-phosphate adenylyltransferase; Provisional |
124-346 | 1.33e-11 | |||||
glucose-1-phosphate adenylyltransferase; Provisional Pssm-ID: 179997 [Multi-domain] Cd Length: 380 Bit Score: 64.89 E-value: 1.33e-11
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| M1P_guanylylT_A_like_N | cd06428 | N-terminal domain of M1P_guanylyl_A_ like proteins are likely to be a isoform of GDP-mannose ... |
124-301 | 1.50e-11 | |||||
N-terminal domain of M1P_guanylyl_A_ like proteins are likely to be a isoform of GDP-mannose pyrophosphorylase; N-terminal domain of the M1P-guanylyltransferase A-isoform like proteins: The proteins of this family are likely to be a isoform of GDP-mannose pyrophosphorylase. Their sequences are highly conserved with mannose-1-phosphate guanyltransferase, but generally about 40-60 bases longer. GDP-mannose pyrophosphorylase (GTP: alpha-d-mannose-1-phosphate guanyltransferase) catalyzes the formation of GDP-d-mannose from GTP and alpha-d-mannose-1-Phosphate. It contains an N-terminal catalytic domain that resembles a dinucleotide-binding Rossmann fold and a C-terminal LbH fold domain. GDP-d-mannose is the activated form of mannose for formation of cell wall lipoarabinomannan and various mannose-containing glycolipids and polysaccharides. The function of GDP-mannose pyrophosphorylase is essential for cell wall integrity, morphogenesis and viability. Repression of GDP-mannose pyrophosphorylase in yeast leads to phenotypes including cell lysis, defective cell wall, and failure of polarized growth and cell separation. Pssm-ID: 133050 [Multi-domain] Cd Length: 257 Bit Score: 63.81 E-value: 1.50e-11
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| CBS_pair_bac_euk | cd04623 | Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains present in bacteria ... |
10-106 | 2.61e-11 | |||||
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains present in bacteria and eukaryotes; The CBS domain, named after human CBS, is a small domain originally identified in cystathionine beta-synthase and is subsequently found in a wide range of different proteins. CBS domains usually occur in tandem repeats. They associate to form a so-called Bateman domain or a CBS pair based on crystallographic studies in bacteria. The CBS pair was used as a basis for this cd hierarchy since the human CBS proteins can adopt the typical core structure and form an intramolecular CBS pair. The interface between the two CBS domains forms a cleft that is a potential ligand binding site. The CBS pair coexists with a variety of other functional domains and this has been used to help in its classification here. It has been proposed that the CBS domain may play a regulatory role, although its exact function is unknown. Mutations of conserved residues within this domain are associated with a variety of human hereditary diseases, including congenital myotonia, idiopathic generalized epilepsy, hypercalciuric nephrolithiasis, and classic Bartter syndrome (CLC chloride channel family members), Wolff-Parkinson-White syndrome (gamma 2 subunit of AMP-activated protein kinase), retinitis pigmentosa (IMP dehydrogenase-1), and homocystinuria (cystathionine beta-synthase). Pssm-ID: 341391 [Multi-domain] Cd Length: 113 Bit Score: 59.74 E-value: 2.61e-11
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| GT2_GlmU_N_bac | cd02540 | N-terminal domain of bacterial GlmU; The N-terminal domain of N-Acetylglucosamine-1-phosphate ... |
124-301 | 2.64e-11 | |||||
N-terminal domain of bacterial GlmU; The N-terminal domain of N-Acetylglucosamine-1-phosphate uridyltransferase (GlmU). GlmU is an essential bacterial enzyme with both an acetyltransferase and an uridyltransferase activity which have been mapped to the C-terminal and N-terminal domains, respectively. This family represents the N-terminal uridyltransferase. GlmU performs the last two steps in the synthesis of UDP-N-acetylglucosamine (UDP-GlcNAc), which is an essential precursor in both the peptidoglycan and the lipopolysaccharide metabolic pathways in Gram-positive and Gram-negative bacteria, respectively. Pssm-ID: 133020 [Multi-domain] Cd Length: 229 Bit Score: 62.53 E-value: 2.64e-11
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| CBS_pair_CAP-ED_NT_Pol-beta-like_DUF294_assoc | cd04587 | Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with the ... |
8-105 | 3.23e-11 | |||||
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with the bacterial CAP_ED (cAMP receptor protein effector domain) family of transcription factors, the NT (Nucleotidyltransferase) Pol-beta-like domain, and the DUF294 dom; This cd contains two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with the bacterial CAP_ED (cAMP receptor protein effector domain) family of transcription factors, the NT_Pol-beta-like domain, and the DUF294 domain. Members of CAP_ED, include CAP which binds cAMP, FNR (fumarate and nitrate reductase) which uses an iron-sulfur cluster to sense oxygen, and CooA a heme containing CO sensor. In all cases binding of the effector leads to conformational changes and the ability to activate transcription. The NT_Pol-beta-like domain includes the Nucleotidyltransferase (NT) domains of DNA polymerase beta and other family X DNA polymerases, as well as the NT domains of class I and class II CCA-adding enzymes, RelA- and SpoT-like ppGpp synthetases and hydrolases, 2'5'-oligoadenylate (2-5A)synthetases, Escherichia coli adenylyltransferase (GlnE), Escherichia coli uridylyl transferase (GlnD), poly (A) polymerases, terminal uridylyl transferases, Staphylococcus aureus kanamycin nucleotidyltransferase, and similar proteins. DUF294 is a putative nucleotidyltransferase with a conserved DxD motif. CBS is a small domain originally identified in cystathionine beta-synthase and subsequently found in a wide range of different proteins. The CBS domain, named after human CBS, is a small domain originally identified in cystathionine beta-synthase and is subsequently found in a wide range of different proteins. CBS domains usually occur in tandem repeats. They associate to form a so-called Bateman domain or a CBS pair based on crystallographic studies in bacteria. The CBS pair was used as a basis for this cd hierarchy since the human CBS proteins can adopt the typical core structure and form an intramolecular CBS pair. The interface between the two CBS domains forms a cleft that is a potential ligand binding site. The CBS pair coexists with a variety of other functional domains and this has been used to help in its classification here. It has been proposed that the CBS domain may play a regulatory role, although its exact function is unknown. Mutations of conserved residues within this domain are associated with a variety of human hereditary diseases, including congenital myotonia, idiopathic generalized epilepsy, hypercalciuric nephrolithiasis, and classic Bartter syndrome (CLC chloride channel family members), Wolff-Parkinson-White syndrome (gamma 2 subunit of AMP-activated protein kinase), retinitis pigmentosa (IMP dehydrogenase-1), and homocystinuria (cystathionine beta-synthase). Pssm-ID: 341363 [Multi-domain] Cd Length: 114 Bit Score: 59.75 E-value: 3.23e-11
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| CBS_pair_bac | cd04629 | Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains present in bacteria; ... |
2-106 | 5.33e-11 | |||||
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains present in bacteria; The CBS domain, named after human CBS, is a small domain originally identified in cystathionine beta-synthase and is subsequently found in a wide range of different proteins. CBS domains usually occur in tandem repeats. They associate to form a so-called Bateman domain or a CBS pair based on crystallographic studies in bacteria. The CBS pair was used as a basis for this cd hierarchy since the human CBS proteins can adopt the typical core structure and form an intramolecular CBS pair. The interface between the two CBS domains forms a cleft that is a potential ligand binding site. The CBS pair coexists with a variety of other functional domains and this has been used to help in its classification here. It has been proposed that the CBS domain may play a regulatory role, although its exact function is unknown. Mutations of conserved residues within this domain are associated with a variety of human hereditary diseases, including congenital myotonia, idiopathic generalized epilepsy, hypercalciuric nephrolithiasis, and classic Bartter syndrome (CLC chloride channel family members), Wolff-Parkinson-White syndrome (gamma 2 subunit of AMP-activated protein kinase), retinitis pigmentosa (IMP dehydrogenase-1), and homocystinuria (cystathionine beta-synthase). Pssm-ID: 341392 [Multi-domain] Cd Length: 116 Bit Score: 58.99 E-value: 5.33e-11
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| CBS_pair_AcuB_like | cd04584 | Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with the ... |
6-106 | 7.22e-11 | |||||
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with the ACT domain; The putative Acetoin Utilization Protein (Acub) from Vibrio Cholerae contains a CBS pair domain. The acetoin utilization protein plays a role in growth and sporulation on acetoin or butanediol for use as a carbon source. Acetoin is an important physiological metabolite excreted by many microorganisms. It is used as an external energy store by a number of fermentive bacteria. Acetoin is produced by the decarboxylation of alpha-acetolactate. Once superior carbon sources are exhausted, and the culture enters stationary phase, acetoin can be utilised in order to maintain the culture density. The conversion of acetoin into acetyl-CoA or 2,3-butanediol is catalysed by the acetoin dehydrogenase complex and acetoin reductase/2,3-butanediol dehydrogenase, respectively. Acetoin utilization proteins, acetylpolyamine amidohydrolases, and histone deacetylases are members of an ancient protein superfamily.This cd contains two tandem repeats of the cystathionine beta-synthase (CBS pair) domains in the acetoin utilization proteins in bacteria. Acetoin is a product of fermentative metabolism in many prokaryotic and eukaryotic microorganisms. They produce acetoin as an external carbon storage compound and then later reuse it as a carbon and energy source during their stationary phase and sporulation. In addition these CBS domains are associated with a downstream ACT (aspartate kinase/chorismate mutase/TyrA) domain, which is linked to a wide range of metabolic enzymes that are regulated by amino acid concentration. Pairs of ACT domains bind specifically to a particular amino acid leading to regulation of the linked enzyme. The CBS domain, named after human CBS, is a small domain originally identified in cystathionine beta-synthase and is subsequently found in a wide range of different proteins. CBS domains usually occur in tandem repeats. They associate to form a so-called Bateman domain or a CBS pair based on crystallographic studies in bacteria. The CBS pair was used as a basis for this cd hierarchy since the human CBS proteins can adopt the typical core structure and form an intramolecular CBS pair. The interface between the two CBS domains forms a cleft that is a potential ligand binding site. The CBS pair coexists with a variety of other functional domains and this has been used to help in its classification here. It has been proposed that the CBS domain may play a regulatory role, although its exact function is unknown. Mutations of conserved residues within this domain are associated with a variety of human hereditary diseases, including congenital myotonia, idiopathic generalized epilepsy, hypercalciuric nephrolithiasis, and classic Bartter syndrome (CLC chloride channel family members), Wolff-Parkinson-White syndrome (gamma 2 subunit of AMP-activated protein kinase), retinitis pigmentosa (IMP dehydrogenase-1), and homocystinuria (cystathionine beta-synthase). Pssm-ID: 341361 [Multi-domain] Cd Length: 130 Bit Score: 58.97 E-value: 7.22e-11
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| CBS_pair_arch | cd09836 | Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains; The CBS domain, ... |
6-109 | 9.21e-11 | |||||
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains; The CBS domain, named after human CBS, is a small domain originally identified in cystathionine beta-synthase and is subsequently found in a wide range of different proteins. CBS domains usually occur in tandem repeats. They associate to form a so-called Bateman domain or a CBS pair based on crystallographic studies in bacteria. The CBS pair was used as a basis for this cd hierarchy since the human CBS proteins can adopt the typical core structure and form an intramolecular CBS pair. The interface between the two CBS domains forms a cleft that is a potential ligand binding site. The CBS pair coexists with a variety of other functional domains and this has been used to help in its classification here. It has been proposed that the CBS domain may play a regulatory role, although its exact function is unknown. Mutations of conserved residues within this domain are associated with a variety of human hereditary diseases, including congenital myotonia, idiopathic generalized epilepsy, hypercalciuric nephrolithiasis, and classic Bartter syndrome (CLC chloride channel family members), Wolff-Parkinson-White syndrome (gamma 2 subunit of AMP-activated protein kinase), retinitis pigmentosa (IMP dehydrogenase-1), and homocystinuria (cystathionine beta-synthase). Pssm-ID: 341405 [Multi-domain] Cd Length: 116 Bit Score: 58.30 E-value: 9.21e-11
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| CBS_pair_voltage-gated_CLC_euk_bac | cd04592 | Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with the ... |
8-106 | 1.06e-10 | |||||
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with the voltage gated CLC (chloride channel) in eukaryotes and bacteria; This cd contains two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with the voltage gated CLC voltage-gated chloride channel. The CBS pairs here are found in the EriC CIC-type chloride channels in eukaryotes and bacteria. These ion channels are proteins with a seemingly simple task of allowing the passive flow of chloride ions across biological membranes. CIC-type chloride channels come from all kingdoms of life, have several gene families, and can be gated by voltage. The members of the CIC-type chloride channel are double-barreled: two proteins forming homodimers at a broad interface formed by four helices from each protein. The two pores are not found at this interface, but are completely contained within each subunit, as deduced from the mutational analyses, unlike many other channels, in which four or five identical or structurally related subunits jointly form one pore. The CBS domain, named after human CBS, is a small domain originally identified in cystathionine beta-synthase and is subsequently found in a wide range of different proteins. CBS domains usually occur in tandem repeats. They associate to form a so-called Bateman domain or a CBS pair based on crystallographic studies in bacteria. The CBS pair was used as a basis for this cd hierarchy since the human CBS proteins can adopt the typical core structure and form an intramolecular CBS pair. The interface between the two CBS domains forms a cleft that is a potential ligand binding site. The CBS pair coexists with a variety of other functional domains and this has been used to help in its classification here. It has been proposed that the CBS domain may play a regulatory role, although its exact function is unknown. Mutations of conserved residues within this domain are associated with a variety of human hereditary diseases, including congenital myotonia, idiopathic generalized epilepsy, hypercalciuric nephrolithiasis, and classic Bartter syndrome (CLC chloride channel family members), Wolff-Parkinson-White syndrome (gamma 2 subunit of AMP-activated protein kinase), retinitis pigmentosa (IMP dehydrogenase-1), and homocystinuria (cystathionine beta-synthase). Pssm-ID: 341368 [Multi-domain] Cd Length: 128 Bit Score: 58.53 E-value: 1.06e-10
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| LicC | COG4750 | CTP:phosphocholine cytidylyltransferase LicC [Cell wall/membrane/envelope biogenesis, Lipid ... |
124-183 | 1.24e-10 | |||||
CTP:phosphocholine cytidylyltransferase LicC [Cell wall/membrane/envelope biogenesis, Lipid transport and metabolism]; Pssm-ID: 443784 [Multi-domain] Cd Length: 228 Bit Score: 60.61 E-value: 1.24e-10
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| CBS_pair_CAP-ED_NT_Pol-beta-like_DUF294_assoc | cd17771 | CBS domain protein; This cd contains two tandem repeats of the cystathionine beta-synthase ... |
8-106 | 1.44e-10 | |||||
CBS domain protein; This cd contains two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with the bacterial CAP_ED (cAMP receptor protein effector domain) family of transcription factors, the NT_Pol-beta-like domain, and the DUF294 domain. Members of CAP_ED, include CAP which binds cAMP, FNR (fumarate and nitrate reductase) which uses an iron-sulfur cluster to sense oxygen, and CooA a heme containing CO sensor. In all cases binding of the effector leads to conformational changes and the ability to activate transcription. The NT_Pol-beta-like domain includes the Nucleotidyltransferase (NT) domains of DNA polymerase beta and other family X DNA polymerases, as well as the NT domains of class I and class II CCA-adding enzymes, RelA- and SpoT-like ppGpp synthetases and hydrolases, 2'5'-oligoadenylate (2-5A)synthetases, Escherichia coli adenylyltransferase (GlnE), Escherichia coli uridylyl transferase (GlnD), poly (A) polymerases, terminal uridylyl transferases, Staphylococcus aureus kanamycin nucleotidyltransferase, and similar proteins. DUF294 is a putative nucleotidyltransferase with a conserved DxD motif. CBS is a small domain originally identified in cystathionine beta-synthase and subsequently found in a wide range of different proteins. The CBS domain, named after human CBS, is a small domain originally identified in cystathionine beta-synthase and is subsequently found in a wide range of different proteins. CBS domains usually occur in tandem repeats. They associate to form a so-called Bateman domain or a CBS pair based on crystallographic studies in bacteria. The CBS pair was used as a basis for this cd hierarchy since the human CBS proteins can adopt the typical core structure and form an intramolecular CBS pair. The interface between the two CBS domains forms a cleft that is a potential ligand binding site. The CBS pair coexists with a variety of other functional domains and this has been used to help in its classification here. It has been proposed that the CBS domain may play a regulatory role, although its exact function is unknown. Mutations of conserved residues within this domain are associated with a variety of human hereditary diseases, including congenital myotonia, idiopathic generalized epilepsy, hypercalciuric nephrolithiasis, and classic Bartter syndrome (CLC chloride channel family members), Wolff-Parkinson-White syndrome (gamma 2 subunit of AMP-activated protein kinase), retinitis pigmentosa (IMP dehydrogenase-1), and homocystinuria (cystathionine beta-synthase). Pssm-ID: 341407 [Multi-domain] Cd Length: 115 Bit Score: 58.10 E-value: 1.44e-10
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| GlmU | COG1207 | Bifunctional protein GlmU, N-acetylglucosamine-1-phosphate-uridyltransferase ... |
124-301 | 4.38e-10 | |||||
Bifunctional protein GlmU, N-acetylglucosamine-1-phosphate-uridyltransferase/glucosamine-1-phosphate-acetyltransferase [Cell wall/membrane/envelope biogenesis]; Pssm-ID: 440820 [Multi-domain] Cd Length: 457 Bit Score: 60.81 E-value: 4.38e-10
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| IMPDH | pfam00478 | IMP dehydrogenase / GMP reductase domain; This family is involved in biosynthesis of guanosine ... |
8-120 | 1.05e-09 | |||||
IMP dehydrogenase / GMP reductase domain; This family is involved in biosynthesis of guanosine nucleotide. Members of this family contain a TIM barrel structure. In the inosine monophosphate dehydrogenases 2 CBS domains pfam00571 are inserted in the TIM barrel. This family is a member of the common phosphate binding site TIM barrel family. Pssm-ID: 459826 [Multi-domain] Cd Length: 463 Bit Score: 59.32 E-value: 1.05e-09
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| CBS_pair_DHH_polyA_Pol_assoc | cd04595 | Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with the ... |
10-108 | 2.31e-09 | |||||
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with the DHH and nucleotidyltransferase (NT) domains; This cd contains two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with an upstream DHH domain which performs a phosphoesterase function and a downstream nucleotidyltransferase (NT) domain of family X DNA polymerases. The CBS domain, named after human CBS, is a small domain originally identified in cystathionine beta-synthase and is subsequently found in a wide range of different proteins. CBS domains usually occur in tandem repeats. They associate to form a so-called Bateman domain or a CBS pair based on crystallographic studies in bacteria. The CBS pair was used as a basis for this cd hierarchy since the human CBS proteins can adopt the typical core structure and form an intramolecular CBS pair. The interface between the two CBS domains forms a cleft that is a potential ligand binding site. The CBS pair coexists with a variety of other functional domains and this has been used to help in its classification here. It has been proposed that the CBS domain may play a regulatory role, although its exact function is unknown. Mutations of conserved residues within this domain are associated with a variety of human hereditary diseases, including congenital myotonia, idiopathic generalized epilepsy, hypercalciuric nephrolithiasis, and classic Bartter syndrome (CLC chloride channel family members), Wolff-Parkinson-White syndrome (gamma 2 subunit of AMP-activated protein kinase), retinitis pigmentosa (IMP dehydrogenase-1), and homocystinuria (cystathionine beta-synthase). Pssm-ID: 341370 [Multi-domain] Cd Length: 110 Bit Score: 54.42 E-value: 2.31e-09
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| YtoI | COG4109 | Predicted transcriptional regulator containing CBS domains [Transcription]; |
10-112 | 3.54e-09 | |||||
Predicted transcriptional regulator containing CBS domains [Transcription]; Pssm-ID: 443285 [Multi-domain] Cd Length: 135 Bit Score: 54.53 E-value: 3.54e-09
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| CBS_pair_IMPDH | cd04601 | Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains in the inosine 5' ... |
10-110 | 6.30e-09 | |||||
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains in the inosine 5' monophosphate dehydrogenase (IMPDH) protein; This cd contains two tandem repeats of the cystathionine beta-synthase (CBS pair) domains in the inosine 5' monophosphate dehydrogenase (IMPDH) protein. IMPDH is an essential enzyme that catalyzes the first step unique to GTP synthesis, playing a key role in the regulation of cell proliferation and differentiation. The CBS domain, named after human CBS, is a small domain originally identified in cystathionine beta-synthase and is subsequently found in a wide range of different proteins. CBS domains usually occur in tandem repeats. They associate to form a so-called Bateman domain or a CBS pair based on crystallographic studies in bacteria. The CBS pair was used as a basis for this cd hierarchy since the human CBS proteins can adopt the typical core structure and form an intramolecular CBS pair. The interface between the two CBS domains forms a cleft that is a potential ligand binding site. The CBS pair coexists with a variety of other functional domains and this has been used to help in its classification here. It has been proposed that the CBS domain may play a regulatory role, although its exact function is unknown. Mutations of conserved residues within this domain are associated with a variety of human hereditary diseases, including congenital myotonia, idiopathic generalized epilepsy, hypercalciuric nephrolithiasis, and classic Bartter syndrome (CLC chloride channel family members), Wolff-Parkinson-White syndrome (gamma 2 subunit of AMP-activated protein kinase), retinitis pigmentosa (IMP dehydrogenase-1), and homocystinuria (cystathionine beta-synthase). Pssm-ID: 341376 [Multi-domain] Cd Length: 110 Bit Score: 53.19 E-value: 6.30e-09
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| glgC | PRK00844 | glucose-1-phosphate adenylyltransferase; Provisional |
123-345 | 1.00e-08 | |||||
glucose-1-phosphate adenylyltransferase; Provisional Pssm-ID: 234846 [Multi-domain] Cd Length: 407 Bit Score: 56.37 E-value: 1.00e-08
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| UGPase_prokaryotic | cd02541 | Prokaryotic UGPase catalyses the synthesis of UDP-glucose; Prokaryotic UDP-Glucose ... |
124-346 | 3.44e-08 | |||||
Prokaryotic UGPase catalyses the synthesis of UDP-glucose; Prokaryotic UDP-Glucose Pyrophosphorylase (UGPase) catalyzes a reversible production of UDP-Glucose and pyrophosphate (PPi) from glucose-1-phosphate and UTP. UDP-glucose plays pivotal roles in galactose utilization, in glycogen synthesis, and in the synthesis of the carbohydrate moieties of glycolipids , glycoproteins , and proteoglycans. UGPase is found in both prokaryotes and eukaryotes, although prokaryotic and eukaryotic forms of UGPase catalyze the same reaction, they share low sequence similarity. Pssm-ID: 133021 [Multi-domain] Cd Length: 267 Bit Score: 54.08 E-value: 3.44e-08
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| CBS_pair_HRP1_like | cd04622 | CBS pair domain found in Hypoxic Response Protein 1 (HRP1) -like proteinds; Mycobacterium ... |
8-105 | 3.61e-08 | |||||
CBS pair domain found in Hypoxic Response Protein 1 (HRP1) -like proteinds; Mycobacterium tuberculosis adapts to cellular stresses by upregulation of the dormancy survival regulon. Hypoxic response protein 1 (HRP1) is encoded by one of the most strongly upregulated genes in the dormancy survival regulon. HRP1 is a 'CBS-domain-only protein; however unlike other CBS containing proteins it does not appear to bind AMP. The biological function of the protein remains unclear, but is thought to contribute to the modulation of the host immune response. The CBS domain, named after human CBS, is a small domain originally identified in cystathionine beta-synthase and is subsequently found in a wide range of different proteins. CBS domains usually occur in tandem repeats. They associate to form a so-called Bateman domain or a CBS pair based on crystallographic studies in bacteria. The CBS pair was used as a basis for this cd hierarchy since the human CBS proteins can adopt the typical core structure and form an intramolecular CBS pair. The interface between the two CBS domains forms a cleft that is a potential ligand binding site. The CBS pair coexists with a variety of other functional domains and this has been used to help in its classification here. It has been proposed that the CBS domain may play a regulatory role, although its exact function is unknown. Mutations of conserved residues within this domain are associated with a variety of human hereditary diseases, including congenital myotonia, idiopathic generalized epilepsy, hypercalciuric nephrolithiasis, and classic Bartter syndrome (CLC chloride channel family members), Wolff-Parkinson-White syndrome (gamma 2 subunit of AMP-activated protein kinase), retinitis pigmentosa (IMP dehydrogenase-1), and homocystinuria (cystathionine beta-synthase). Pssm-ID: 341390 [Multi-domain] Cd Length: 115 Bit Score: 50.88 E-value: 3.61e-08
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| CBS_pair_GGDEF_assoc | cd04599 | Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with the ... |
8-109 | 4.69e-08 | |||||
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with the GGDEF (DiGuanylate-Cyclase (DGC)) domain; This cd contains two tandem repeats of the cystathionine beta-synthase (CBS pair) domains in association with the GGDEF (DiGuanylate-Cyclase (DGC)) domain. The GGDEF domain has been suggested to be homologous to the adenylyl cyclase catalytic domain and is thought to be involved in regulating cell surface adhesiveness in bacteria. The CBS domain, named after human CBS, is a small domain originally identified in cystathionine beta-synthase and is subsequently found in a wide range of different proteins. CBS domains usually occur in tandem repeats. They associate to form a so-called Bateman domain or a CBS pair based on crystallographic studies in bacteria. The CBS pair was used as a basis for this cd hierarchy since the human CBS proteins can adopt the typical core structure and form an intramolecular CBS pair. The interface between the two CBS domains forms a cleft that is a potential ligand binding site. The CBS pair coexists with a variety of other functional domains and this has been used to help in its classification here. It has been proposed that the CBS domain may play a regulatory role, although its exact function is unknown. Mutations of conserved residues within this domain are associated with a variety of human hereditary diseases, including congenital myotonia, idiopathic generalized epilepsy, hypercalciuric nephrolithiasis, and classic Bartter syndrome (CLC chloride channel family members), Wolff-Parkinson-White syndrome (gamma 2 subunit of AMP-activated protein kinase), retinitis pigmentosa (IMP dehydrogenase-1), and homocystinuria (cystathionine beta-synthase). Pssm-ID: 341374 [Multi-domain] Cd Length: 107 Bit Score: 50.42 E-value: 4.69e-08
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| G1P_TT_short | cd02538 | G1P_TT_short is the short form of glucose-1-phosphate thymidylyltransferase; This family is ... |
124-278 | 6.80e-08 | |||||
G1P_TT_short is the short form of glucose-1-phosphate thymidylyltransferase; This family is the short form of glucose-1-phosphate thymidylyltransferase. Glucose-1-phosphate thymidylyltransferase catalyses the formation of dTDP-glucose, from dTTP and glucose 1-phosphate. It is the first enzyme in the biosynthesis of dTDP-L-rhamnose, a cell wall constituent and a feedback inhibitor of the enzyme.There are two forms of Glucose-1-phosphate thymidylyltransferase in bacteria and archeae; short form and long form. The homotetrameric, feedback inhibited short form is found in numerous bacterial species that produce dTDP-L-rhamnose. The long form, which has an extra 50 amino acids c-terminal, is found in many species for which it serves as a sugar-activating enzyme for antibiotic biosynthesis and or other, unknown pathways, and in which dTDP-L-rhamnose is not necessarily produced. Pssm-ID: 133019 [Multi-domain] Cd Length: 240 Bit Score: 52.58 E-value: 6.80e-08
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| PRK15480 | PRK15480 | glucose-1-phosphate thymidylyltransferase RfbA; Provisional |
124-280 | 6.81e-08 | |||||
glucose-1-phosphate thymidylyltransferase RfbA; Provisional Pssm-ID: 185377 [Multi-domain] Cd Length: 292 Bit Score: 53.14 E-value: 6.81e-08
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| PRK10892 | PRK10892 | arabinose-5-phosphate isomerase KdsD; |
10-106 | 9.11e-08 | |||||
arabinose-5-phosphate isomerase KdsD; Pssm-ID: 182814 [Multi-domain] Cd Length: 326 Bit Score: 53.19 E-value: 9.11e-08
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| glgC | PRK00725 | glucose-1-phosphate adenylyltransferase; Provisional |
122-345 | 1.24e-07 | |||||
glucose-1-phosphate adenylyltransferase; Provisional Pssm-ID: 234824 [Multi-domain] Cd Length: 425 Bit Score: 52.92 E-value: 1.24e-07
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| CBS_pair_DHH_polyA_Pol_assoc | cd17772 | Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with the ... |
10-108 | 2.80e-07 | |||||
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with the DHH and nucleotidyltransferase (NT) domains; This cd contains two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with an upstream DHH domain which performs a phosphoesterase function and a downstream nucleotidyltransferase (NT) domain of family X DNA polymerases. The CBS domain, named after human CBS, is a small domain originally identified in cystathionine beta-synthase and is subsequently found in a wide range of different proteins. CBS domains usually occur in tandem repeats. They associate to form a so-called Bateman domain or a CBS pair based on crystallographic studies in bacteria. The CBS pair was used as a basis for this cd hierarchy since the human CBS proteins can adopt the typical core structure and form an intramolecular CBS pair. The interface between the two CBS domains forms a cleft that is a potential ligand binding site. The CBS pair coexists with a variety of other functional domains and this has been used to help in its classification here. It has been proposed that the CBS domain may play a regulatory role, although its exact function is unknown. Mutations of conserved residues within this domain are associated with a variety of human hereditary diseases, including congenital myotonia, idiopathic generalized epilepsy, hypercalciuric nephrolithiasis, and classic Bartter syndrome (CLC chloride channel family members), Wolff-Parkinson-White syndrome (gamma 2 subunit of AMP-activated protein kinase), retinitis pigmentosa (IMP dehydrogenase-1), and homocystinuria (cystathionine beta-synthase). Pssm-ID: 341408 [Multi-domain] Cd Length: 112 Bit Score: 48.33 E-value: 2.80e-07
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| CBS | pfam00571 | CBS domain; CBS domains are small intracellular modules that pair together to form a stable ... |
8-55 | 4.04e-07 | |||||
CBS domain; CBS domains are small intracellular modules that pair together to form a stable globular domain. This family represents a single CBS domain. Pairs of these domains have been termed a Bateman domain. CBS domains have been shown to bind ligands with an adenosyl group such as AMP, ATP and S-AdoMet. CBS domains are found attached to a wide range of other protein domains suggesting that CBS domains may play a regulatory role making proteins sensitive to adenosyl carrying ligands. The region containing the CBS domains in Cystathionine-beta synthase is involved in regulation by S-AdoMet. CBS domain pairs from AMPK bind AMP or ATP. The CBS domains from IMPDH and the chloride channel CLC2 bind ATP. Pssm-ID: 425756 [Multi-domain] Cd Length: 57 Bit Score: 46.44 E-value: 4.04e-07
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| CBS_arch_repeat1 | cd17777 | CBS pair domains found in archeal proteins, repeat 1; CBS pair domains found in archeal ... |
8-108 | 4.09e-07 | |||||
CBS pair domains found in archeal proteins, repeat 1; CBS pair domains found in archeal proteins that contain 2 repeats. The CBS domain, named after human CBS, is a small domain originally identified in cystathionine beta-synthase and is subsequently found in a wide range of different proteins. CBS domains usually occur in tandem repeats. They associate to form a so-called Bateman domain or a CBS pair based on crystallographic studies in bacteria. The CBS pair was used as a basis for this cd hierarchy since the human CBS proteins can adopt the typical core structure and form an intramolecular CBS pair. The interface between the two CBS domains forms a cleft that is a potential ligand binding site. The CBS pair coexists with a variety of other functional domains and this has been used to help in its classification here. Pssm-ID: 341413 [Multi-domain] Cd Length: 137 Bit Score: 48.49 E-value: 4.09e-07
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| COG2266 | COG2266 | GTP:adenosylcobinamide-phosphate guanylyltransferase [Coenzyme transport and metabolism]; GTP: ... |
125-172 | 7.71e-07 | |||||
GTP:adenosylcobinamide-phosphate guanylyltransferase [Coenzyme transport and metabolism]; GTP:adenosylcobinamide-phosphate guanylyltransferase is part of the Pathway/BioSystem: Cobalamine/B12 biosynthesis Pssm-ID: 441867 [Multi-domain] Cd Length: 185 Bit Score: 48.73 E-value: 7.71e-07
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| CBS_pair_ABC_OpuCA_assoc | cd04583 | Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains found associated with ... |
8-108 | 8.40e-07 | |||||
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains found associated with the ABC transporter OpuCA; This cd contains two tandem repeats of the cystathionine beta-synthase (CBS pair) domains found in association with the ABC transporter OpuCA. OpuCA is the ATP binding component of a bacterial solute transporter that serves a protective role to cells growing in a hyperosmolar environment but the function of the CBS domains in OpuCA remains unknown. In the related ABC transporter, OpuA, the tandem CBS domains have been shown to function as sensors for ionic strength, whereby they control the transport activity through an electronic switching mechanism. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. They are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins. The CBS domain, named after human CBS, is a small domain originally identified in cystathionine beta-synthase and is subsequently found in a wide range of different proteins. CBS domains usually occur in tandem repeats. They associate to form a so-called Bateman domain or a CBS pair based on crystallographic studies in bacteria. The CBS pair was used as a basis for this cd hierarchy since the human CBS proteins can adopt the typical core structure and form an intramolecular CBS pair. The interface between the two CBS domains forms a cleft that is a potential ligand binding site. The CBS pair coexists with a variety of other functional domains and this has been used to help in its classification here. It has been proposed that the CBS domain may play a regulatory role, although its exact function is unknown. Mutations of conserved residues within this domain are associated with a variety of human hereditary diseases, including congenital myotonia, idiopathic generalized epilepsy, hypercalciuric nephrolithiasis, and classic Bartter syndrome (CLC chloride channel family members), Wolff-Parkinson-White syndrome (gamma 2 subunit of AMP-activated protein kinase), retinitis pigmentosa (IMP dehydrogenase-1), and homocystinuria (cystathionine beta-synthase). Pssm-ID: 341360 [Multi-domain] Cd Length: 110 Bit Score: 47.13 E-value: 8.40e-07
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| PRK07807 | PRK07807 | GuaB1 family IMP dehydrogenase-related protein; |
8-108 | 1.05e-06 | |||||
GuaB1 family IMP dehydrogenase-related protein; Pssm-ID: 181127 [Multi-domain] Cd Length: 479 Bit Score: 50.29 E-value: 1.05e-06
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| CBS | COG0517 | CBS domain [Signal transduction mechanisms]; |
8-58 | 1.15e-06 | |||||
CBS domain [Signal transduction mechanisms]; Pssm-ID: 440283 [Multi-domain] Cd Length: 128 Bit Score: 47.17 E-value: 1.15e-06
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| glmU | PRK14355 | bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ... |
124-300 | 1.19e-06 | |||||
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate N-acetyltransferase GlmU; Pssm-ID: 237685 [Multi-domain] Cd Length: 459 Bit Score: 50.13 E-value: 1.19e-06
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| CBS | smart00116 | Domain in cystathionine beta-synthase and other proteins; Domain present in all 3 forms of ... |
8-49 | 1.39e-06 | |||||
Domain in cystathionine beta-synthase and other proteins; Domain present in all 3 forms of cellular life. Present in two copies in inosine monophosphate dehydrogenase, of which one is disordered in the crystal structure. A number of disease states are associated with CBS-containing proteins including homocystinuria, Becker's and Thomsen disease. Pssm-ID: 214522 [Multi-domain] Cd Length: 49 Bit Score: 44.81 E-value: 1.39e-06
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| COG2524 | COG2524 | Predicted transcriptional regulator, contains C-terminal CBS domains [Transcription]; |
8-53 | 1.43e-06 | |||||
Predicted transcriptional regulator, contains C-terminal CBS domains [Transcription]; Pssm-ID: 442013 [Multi-domain] Cd Length: 206 Bit Score: 48.34 E-value: 1.43e-06
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| CBS_archAMPK_gamma-repeat2 | cd04631 | CBS pair domains found in archeal 5'-AMP-activated protein kinase gamma subunit-like proteins; ... |
6-108 | 1.47e-06 | |||||
CBS pair domains found in archeal 5'-AMP-activated protein kinase gamma subunit-like proteins; Archeal gamma-subunit of 5'-AMP-activated protein kinase (AMPK) contains four CBS domains in tandem repeats, similar to eukaryotic homologs. AMPK is an important regulator of metabolism and of energy homeostasis. It is a heterotrimeric protein composed of a catalytic serine/threonine kinase subunit (alpha) and two regulatory subunits (beta and gamma). The gamma subunit senses the intracellular energy status by competitively binding AMP and ATP and is believed to be responsible for allosteric regulation of the whole complex. In humans mutations in gamma- subunit of AMPK are associated with hypertrophic cardiomiopathy, Wolff-Parkinson-White syndrome and glycogen storage in the skeletal muscle. The CBS domain, named after human CBS, is a small domain originally identified in cystathionine beta-synthase and is subsequently found in a wide range of different proteins. CBS domains usually occur in tandem repeats. They associate to form a so-called Bateman domain or a CBS pair based on crystallographic studies in bacteria. The CBS pair was used as a basis for this cd hierarchy since the human CBS proteins can adopt the typical core structure and form an intramolecular CBS pair. The interface between the two CBS domains forms a cleft that is a potential ligand binding site. The CBS pair coexists with a variety of other functional domains and this has been used to help in its classification here. Pssm-ID: 341394 [Multi-domain] Cd Length: 130 Bit Score: 46.84 E-value: 1.47e-06
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| PTZ00314 | PTZ00314 | inosine-5'-monophosphate dehydrogenase; Provisional |
10-120 | 1.85e-06 | |||||
inosine-5'-monophosphate dehydrogenase; Provisional Pssm-ID: 240355 [Multi-domain] Cd Length: 495 Bit Score: 49.58 E-value: 1.85e-06
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| CBS_pair_SF | cd02205 | Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains superfamily; The CBS ... |
10-51 | 2.49e-06 | |||||
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains superfamily; The CBS domain, named after human CBS, is a small domain originally identified in cystathionine beta-synthase and is subsequently found in a wide range of different proteins. CBS domains usually occur in tandem repeats. They associate to form a so-called Bateman domain or a CBS pair based on crystallographic studies in bacteria. The CBS pair was used as a basis for this cd hierarchy since the human CBS proteins can adopt the typical core structure and form an intramolecular CBS pair. The interface between the two CBS domains forms a cleft that is a potential ligand binding site. The CBS pair coexists with a variety of other functional domains and this has been used to help in its classification here. It has been proposed that the CBS domain may play a regulatory role, although its exact function is unknown. Mutations of conserved residues within this domain are associated with a variety of human hereditary diseases, including congenital myotonia, idiopathic generalized epilepsy, hypercalciuric nephrolithiasis, and classic Bartter syndrome (CLC chloride channel family members), Wolff-Parkinson-White syndrome (gamma 2 subunit of AMP-activated protein kinase), retinitis pigmentosa (IMP dehydrogenase-1), and homocystinuria (cystathionine beta-synthase). Pssm-ID: 341358 [Multi-domain] Cd Length: 113 Bit Score: 45.70 E-value: 2.49e-06
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| CBS_pair_MUG70_1 | cd17781 | Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains similar to MUG70 ... |
31-106 | 5.60e-06 | |||||
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains similar to MUG70 repeat1; Two tandem repeats of the cystathionine beta-synthase (CBS pair) domain, present in MUG70. The MUG70 protein, encoded by the Meiotically Up-regulated Gene 70, plays a role in meiosis and contains, beside the two CBS pairs, a PB1 domain. The CBS domain, named after human CBS, is a small domain originally identified in cystathionine beta-synthase and is subsequently found in a wide range of different proteins. CBS domains usually occur in tandem repeats. They associate to form a so-called Bateman domain or a CBS pair based on crystallographic studies in bacteria. The CBS pair was used as a basis for this cd hierarchy since the human CBS proteins can adopt the typical core structure and form an intramolecular CBS pair. The interface between the two CBS domains forms a cleft that is a potential ligand binding site. The CBS pair coexists with a variety of other functional domains and this has been used to help in its classification here. It has been proposed that the CBS domain may play a regulatory role, although its exact function is unknown. Mutations of conserved residues within this domain are associated with a variety of human hereditary diseases, including congenital myotonia, idiopathic generalized epilepsy, hypercalciuric nephrolithiasis, and classic Bartter syndrome (CLC chloride channel family members), Wolff-Parkinson-White syndrome (gamma 2 subunit of AMP-activated protein kinase), retinitis pigmentosa (IMP dehydrogenase-1), and homocystinuria (cystathionine beta-synthase). Pssm-ID: 341417 [Multi-domain] Cd Length: 118 Bit Score: 44.89 E-value: 5.60e-06
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| glmU | PRK14354 | bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ... |
124-290 | 7.12e-06 | |||||
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate N-acetyltransferase GlmU; Pssm-ID: 184643 [Multi-domain] Cd Length: 458 Bit Score: 47.52 E-value: 7.12e-06
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| PRK14869 | PRK14869 | putative manganese-dependent inorganic diphosphatase; |
10-58 | 9.35e-06 | |||||
putative manganese-dependent inorganic diphosphatase; Pssm-ID: 237843 [Multi-domain] Cd Length: 546 Bit Score: 47.13 E-value: 9.35e-06
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| CBS_pair_archHTH_assoc | cd04588 | Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains found in archaea and ... |
10-108 | 9.84e-06 | |||||
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains found in archaea and associated with helix turn helix domain; This cd contains two tandem repeats of the cystathionine beta-synthase (CBS pair) domains in the inosine 5' monophosphate dehydrogenase (IMPDH) protein. IMPDH is an essential enzyme that catalyzes the first step unique to GTP synthesis, playing a key role in the regulation of cell proliferation and differentiation. The CBS domain, named after human CBS, is a small domain originally identified in cystathionine beta-synthase and is subsequently found in a wide range of different proteins. CBS domains usually occur in tandem repeats. They associate to form a so-called Bateman domain or a CBS pair based on crystallographic studies in bacteria. The CBS pair was used as a basis for this cd hierarchy since the human CBS proteins can adopt the typical core structure and form an intramolecular CBS pair. The interface between the two CBS domains forms a cleft that is a potential ligand binding site. The CBS pair coexists with a variety of other functional domains and this has been used to help in its classification here. It has been proposed that the CBS domain may play a regulatory role, although its exact function is unknown. Mutations of conserved residues within this domain are associated with a variety of human hereditary diseases, including congenital myotonia, idiopathic generalized epilepsy, hypercalciuric nephrolithiasis, and classic Bartter syndrome (CLC chloride channel family members), Wolff-Parkinson-White syndrome (gamma 2 subunit of AMP-activated protein kinase), retinitis pigmentosa (IMP dehydrogenase-1), and homocystinuria (cystathionine beta-synthase). Pssm-ID: 341364 [Multi-domain] Cd Length: 111 Bit Score: 44.06 E-value: 9.84e-06
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| glgC | PRK02862 | glucose-1-phosphate adenylyltransferase; Provisional |
124-342 | 1.01e-05 | |||||
glucose-1-phosphate adenylyltransferase; Provisional Pssm-ID: 179486 [Multi-domain] Cd Length: 429 Bit Score: 47.19 E-value: 1.01e-05
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| PRK13389 | PRK13389 | UTP--glucose-1-phosphate uridylyltransferase GalU; |
111-183 | 1.05e-05 | |||||
UTP--glucose-1-phosphate uridylyltransferase GalU; Pssm-ID: 184021 [Multi-domain] Cd Length: 302 Bit Score: 46.44 E-value: 1.05e-05
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| CBS_pair_bact_arch | cd17775 | Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains present in bacteria ... |
8-109 | 1.57e-05 | |||||
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains present in bacteria and archaea; The CBS domain, named after human CBS, is a small domain originally identified in cystathionine beta-synthase and is subsequently found in a wide range of different proteins. CBS domains usually occur in tandem repeats. They associate to form a so-called Bateman domain or a CBS pair based on crystallographic studies in bacteria. The CBS pair was used as a basis for this cd hierarchy since the human CBS proteins can adopt the typical core structure and form an intramolecular CBS pair. The interface between the two CBS domains forms a cleft that is a potential ligand binding site. The CBS pair coexists with a variety of other functional domains and this has been used to help in its classification here. It has been proposed that the CBS domain may play a regulatory role, although its exact function is unknown. Mutations of conserved residues within this domain are associated with a variety of human hereditary diseases, including congenital myotonia, idiopathic generalized epilepsy, hypercalciuric nephrolithiasis, and classic Bartter syndrome (CLC chloride channel family members), Wolff-Parkinson-White syndrome (gamma 2 subunit of AMP-activated protein kinase), retinitis pigmentosa (IMP dehydrogenase-1), and homocystinuria (cystathionine beta-synthase). Pssm-ID: 341411 [Multi-domain] Cd Length: 117 Bit Score: 43.68 E-value: 1.57e-05
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| CBS_pair_CBS | cd04608 | Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with the ... |
8-84 | 2.01e-05 | |||||
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with the pyridoxal-phosphate (PALP) dependent enzyme domain; This cd contains two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with the pyridoxal-phosphate (PALP) dependent enzyme domain upstream. Cystathionine beta-synthase (CBS ) contains, besides the C-terminal regulatory CBS-pair, an N-terminal heme-binding module, followed by a pyridoxal phosphate (PLP) domain, which houses the active site. It is the first enzyme in the transsulfuration pathway, catalyzing the conversion of serine and homocysteine to cystathionine and water. In general, CBS domains usually occur in tandem repeats. They associate to form a so-called Bateman domain or a CBS pair based on crystallographic studies in bacteria. The CBS pair was used as a basis for this cd hierarchy since the human CBS proteins can adopt the typical core structure and form an intramolecular CBS pair. The interface between the two CBS domains forms a cleft that is a potential ligand binding site. The CBS pair coexists with a variety of other functional domains and this has been used to help in its classification here. It has been proposed that the CBS domain may play a regulatory role, although its exact function is unknown. Mutations of conserved residues within this domain are associated with a variety of human hereditary diseases, including congenital myotonia, idiopathic generalized epilepsy, hypercalciuric nephrolithiasis, and classic Bartter syndrome (CLC chloride channel family members), Wolff-Parkinson-White syndrome (gamma 2 subunit of AMP-activated protein kinase), retinitis pigmentosa (IMP dehydrogenase-1), and homocystinuria (cystathionine beta-synthase). Pssm-ID: 341382 [Multi-domain] Cd Length: 120 Bit Score: 43.29 E-value: 2.01e-05
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| CBS_pair_Mg_transporter | cd04606 | Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains in the magnesium ... |
8-109 | 2.52e-05 | |||||
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains in the magnesium transporter, MgtE; This cd contains two tandem repeats of the cystathionine beta-synthase (CBS pair) domain in the magnesium transporter, MgtE. MgtE and its homologs are found in eubacteria, archaebacteria, and eukaryota. Members of this family transport Mg2+ or other divalent cations into the cell via two highly conserved aspartates. The CBS domain, named after human CBS, is a small domain originally identified in cystathionine beta-synthase and is subsequently found in a wide range of different proteins. CBS domains usually occur in tandem repeats. They associate to form a so-called Bateman domain or a CBS pair based on crystallographic studies in bacteria. The CBS pair was used as a basis for this cd hierarchy since the human CBS proteins can adopt the typical core structure and form an intramolecular CBS pair. The interface between the two CBS domains forms a cleft that is a potential ligand binding site. The CBS pair coexists with a variety of other functional domains and this has been used to help in its classification here. It has been proposed that the CBS domain may play a regulatory role, although its exact function is unknown. Mutations of conserved residues within this domain are associated with a variety of human hereditary diseases, including congenital myotonia, idiopathic generalized epilepsy, hypercalciuric nephrolithiasis, and classic Bartter syndrome (CLC chloride channel family members), Wolff-Parkinson-White syndrome (gamma 2 subunit of AMP-activated protein kinase), retinitis pigmentosa (IMP dehydrogenase-1), and homocystinuria (cystathionine beta-synthase). Pssm-ID: 341380 [Multi-domain] Cd Length: 121 Bit Score: 43.09 E-value: 2.52e-05
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| gutQ | PRK11543 | arabinose-5-phosphate isomerase GutQ; |
13-105 | 2.53e-05 | |||||
arabinose-5-phosphate isomerase GutQ; Pssm-ID: 183186 [Multi-domain] Cd Length: 321 Bit Score: 45.53 E-value: 2.53e-05
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| glmU | PRK14357 | bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ... |
122-301 | 3.37e-05 | |||||
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate N-acetyltransferase GlmU; Pssm-ID: 237687 [Multi-domain] Cd Length: 448 Bit Score: 45.52 E-value: 3.37e-05
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| CBS_pair_HPP_assoc | cd04600 | Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with the ... |
8-111 | 4.78e-05 | |||||
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with the HPP motif domain; This cd contains two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with the HPP motif domain. These proteins are integral membrane proteins with four transmembrane spanning helices. The function of these proteins is uncertain, but they are thought to be transporters. The CBS domain, named after human CBS, is a small domain originally identified in cystathionine beta-synthase and is subsequently found in a wide range of different proteins. CBS domains usually occur in tandem repeats. They associate to form a so-called Bateman domain or a CBS pair based on crystallographic studies in bacteria. The CBS pair was used as a basis for this cd hierarchy since the human CBS proteins can adopt the typical core structure and form an intramolecular CBS pair. The interface between the two CBS domains forms a cleft that is a potential ligand binding site. The CBS pair coexists with a variety of other functional domains and this has been used to help in its classification here. It has been proposed that the CBS domain may play a regulatory role, although its exact function is unknown. Mutations of conserved residues within this domain are associated with a variety of human hereditary diseases, including congenital myotonia, idiopathic generalized epilepsy, hypercalciuric nephrolithiasis, and classic Bartter syndrome (CLC chloride channel family members), Wolff-Parkinson-White syndrome (gamma 2 subunit of AMP-activated protein kinase), retinitis pigmentosa (IMP dehydrogenase-1), and homocystinuria (cystathionine beta-synthase). Pssm-ID: 341375 [Multi-domain] Cd Length: 133 Bit Score: 42.55 E-value: 4.78e-05
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| glmU | PRK14360 | bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ... |
122-301 | 5.36e-05 | |||||
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate N-acetyltransferase GlmU; Pssm-ID: 184646 [Multi-domain] Cd Length: 450 Bit Score: 44.92 E-value: 5.36e-05
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| COG3448 | COG3448 | CBS-domain-containing membrane protein [Signal transduction mechanisms]; |
10-60 | 7.20e-05 | |||||
CBS-domain-containing membrane protein [Signal transduction mechanisms]; Pssm-ID: 442671 [Multi-domain] Cd Length: 136 Bit Score: 42.16 E-value: 7.20e-05
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| MgtE | COG2239 | Mg/Co/Ni transporter MgtE (contains CBS domain) [Inorganic ion transport and metabolism]; |
8-109 | 7.20e-05 | |||||
Mg/Co/Ni transporter MgtE (contains CBS domain) [Inorganic ion transport and metabolism]; Pssm-ID: 441840 [Multi-domain] Cd Length: 443 Bit Score: 44.29 E-value: 7.20e-05
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| PLN02274 | PLN02274 | inosine-5'-monophosphate dehydrogenase |
8-121 | 7.46e-05 | |||||
inosine-5'-monophosphate dehydrogenase Pssm-ID: 215154 [Multi-domain] Cd Length: 505 Bit Score: 44.27 E-value: 7.46e-05
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| MocA | COG2068 | CTP:molybdopterin cytidylyltransferase MocA [Coenzyme transport and metabolism]; |
124-165 | 7.52e-05 | |||||
CTP:molybdopterin cytidylyltransferase MocA [Coenzyme transport and metabolism]; Pssm-ID: 441671 [Multi-domain] Cd Length: 195 Bit Score: 43.23 E-value: 7.52e-05
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| CBS_pair_voltage-gated_CLC_archaea | cd04594 | Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with the ... |
6-115 | 7.83e-05 | |||||
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with the voltage gated CLC (chloride channel) in archaea; This cd contains two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with the voltage gated CLC voltage-gated chloride channel. The CBS pairs here are found in the EriC CIC-type chloride channels in archaea. These ion channels are proteins with a seemingly simple task of allowing the passive flow of chloride ions across biological membranes. CIC-type chloride channels come from all kingdoms of life, have several gene families, and can be gated by voltage. The members of the CIC-type chloride channel are double-barreled: two proteins forming homodimers at a broad interface formed by four helices from each protein. The two pores are not found at this interface, but are completely contained within each subunit, as deduced from the mutational analyses, unlike many other channels, in which four or five identical or structurally related subunits jointly form one pore. The CBS domain, named after human CBS, is a small domain originally identified in cystathionine beta-synthase and is subsequently found in a wide range of different proteins. CBS domains usually occur in tandem repeats. They associate to form a so-called Bateman domain or a CBS pair based on crystallographic studies in bacteria. The CBS pair was used as a basis for this cd hierarchy since the human CBS proteins can adopt the typical core structure and form an intramolecular CBS pair. The interface between the two CBS domains forms a cleft that is a potential ligand binding site. The CBS pair coexists with a variety of other functional domains and this has been used to help in its classification here. It has been proposed that the CBS domain may play a regulatory role, although its exact function is unknown. Mutations of conserved residues within this domain are associated with a variety of human hereditary diseases, including congenital myotonia, idiopathic generalized epilepsy, hypercalciuric nephrolithiasis, and classic Bartter syndrome (CLC chloride channel family members), Wolff-Parkinson-White syndrome (gamma 2 subunit of AMP-activated protein kinase), retinitis pigmentosa (IMP dehydrogenase-1), and homocystinuria (cystathionine beta-synthase). Pssm-ID: 341369 [Multi-domain] Cd Length: 107 Bit Score: 41.56 E-value: 7.83e-05
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| CBS_two-component_sensor_histidine_kinase_repeat1 | cd04620 | 2 tandem repeats of the CBS domain in the two-component sensor histidine kinase and ... |
12-111 | 7.88e-05 | |||||
2 tandem repeats of the CBS domain in the two-component sensor histidine kinase and related-proteins, repeat 1; This cd contains 2 tandem repeats of the CBS domain in the two-component sensor histidine kinase and related-proteins. Two-component regulation is the predominant form of signal recognition and response coupling mechanism used by bacteria to sense and respond to diverse environmental stresses and cues ranging from common environmental stimuli to host signals recognized by pathogens and bacterial cell-cell communication signals. The structures of both sensors and regulators are modular, and numerous variations in domain architecture and composition have evolved to tailor to specific needs in signal perception and signal transduction. The simplest histidine kinase sensors consists of only sensing and kinase domains. The more complex hybrid sensors contain an additional REC domain typical of two-component regulators and in some cases a C-terminal histidine phosphotransferase (HPT) domain. The CBS domain, named after human CBS, is a small domain originally identified in cystathionine beta-synthase and is subsequently found in a wide range of different proteins. CBS domains usually occur in tandem repeats. They associate to form a so-called Bateman domain or a CBS pair based on crystallographic studies in bacteria. The CBS pair was used as a basis for this cd hierarchy since the human CBS proteins can adopt the typical core structure and form an intramolecular CBS pair. The interface between the two CBS domains forms a cleft that is a potential ligand binding site. The CBS pair coexists with a variety of other functional domains and this has been used to help in its classification here. It has been proposed that the CBS domain may play a regulatory role, although its exact function is unknown. Mutations of conserved residues within this domain are associated with a variety of human hereditary diseases, including congenital myotonia, idiopathic generalized epilepsy, hypercalciuric nephrolithiasis, and classic Bartter syndrome (CLC chloride channel family members), Wolff-Parkinson-White syndrome (gamma 2 subunit of AMP-activated protein kinase), retinitis pigmentosa (IMP dehydrogenase-1), and homocystinuria (cystathionine beta-synthase). Pssm-ID: 341389 [Multi-domain] Cd Length: 136 Bit Score: 42.14 E-value: 7.88e-05
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| CBS_pair_peptidase_M50 | cd04639 | Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains found in the ... |
9-112 | 1.18e-04 | |||||
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains found in the metalloprotease peptidase M50; This cd contains two tandem repeats of the cystathionine beta-synthase (CBS pair) domains in peptidase M50. Members of the M50 metallopeptidase family include mammalian sterol-regulatory element binding protein (SREBP) site 2 proteases and various hypothetical bacterial homologues. The CBS domain, named after human CBS, is a small domain originally identified in cystathionine beta-synthase and is subsequently found in a wide range of different proteins. CBS domains usually occur in tandem repeats. They associate to form a so-called Bateman domain or a CBS pair based on crystallographic studies in bacteria. The CBS pair was used as a basis for this cd hierarchy since the human CBS proteins can adopt the typical core structure and form an intramolecular CBS pair. The interface between the two CBS domains forms a cleft that is a potential ligand binding site. The CBS pair coexists with a variety of other functional domains and this has been used to help in its classification here. It has been proposed that the CBS domain may play a regulatory role, although its exact function is unknown. Mutations of conserved residues within this domain are associated with a variety of human hereditary diseases, including congenital myotonia, idiopathic generalized epilepsy, hypercalciuric nephrolithiasis, and classic Bartter syndrome (CLC chloride channel family members), Wolff-Parkinson-White syndrome (gamma 2 subunit of AMP-activated protein kinase), retinitis pigmentosa (IMP dehydrogenase-1), and homocystinuria (cystathionine beta-synthase). Pssm-ID: 341397 [Multi-domain] Cd Length: 120 Bit Score: 41.02 E-value: 1.18e-04
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| CBS_pair_arch_MET2_assoc | cd04605 | Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with the ... |
10-108 | 1.59e-04 | |||||
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with the MET2 domain; This cd contains two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with the MET2 domain. Met2 is a key enzyme in the biosynthesis of methionine. It encodes a homoserine transacetylase involved in converting homoserine to O-acetyl homoserine. The CBS domain, named after human CBS, is a small domain originally identified in cystathionine beta-synthase and is subsequently found in a wide range of different proteins. CBS domains usually occur in tandem repeats. They associate to form a so-called Bateman domain or a CBS pair based on crystallographic studies in bacteria. The CBS pair was used as a basis for this cd hierarchy since the human CBS proteins can adopt the typical core structure and form an intramolecular CBS pair. The interface between the two CBS domains forms a cleft that is a potential ligand binding site. The CBS pair coexists with a variety of other functional domains and this has been used to help in its classification here. It has been proposed that the CBS domain may play a regulatory role, although its exact function is unknown. Mutations of conserved residues within this domain are associated with a variety of human hereditary diseases, including congenital myotonia, idiopathic generalized epilepsy, hypercalciuric nephrolithiasis, and classic Bartter syndrome (CLC chloride channel family members), Wolff-Parkinson-White syndrome (gamma 2 subunit of AMP-activated protein kinase), retinitis pigmentosa (IMP dehydrogenase-1), and homocystinuria (cystathionine beta-synthase). Pssm-ID: 341379 [Multi-domain] Cd Length: 116 Bit Score: 40.68 E-value: 1.59e-04
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| CBS_pair_bact_arch | cd17775 | Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains present in bacteria ... |
8-49 | 1.83e-04 | |||||
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains present in bacteria and archaea; The CBS domain, named after human CBS, is a small domain originally identified in cystathionine beta-synthase and is subsequently found in a wide range of different proteins. CBS domains usually occur in tandem repeats. They associate to form a so-called Bateman domain or a CBS pair based on crystallographic studies in bacteria. The CBS pair was used as a basis for this cd hierarchy since the human CBS proteins can adopt the typical core structure and form an intramolecular CBS pair. The interface between the two CBS domains forms a cleft that is a potential ligand binding site. The CBS pair coexists with a variety of other functional domains and this has been used to help in its classification here. It has been proposed that the CBS domain may play a regulatory role, although its exact function is unknown. Mutations of conserved residues within this domain are associated with a variety of human hereditary diseases, including congenital myotonia, idiopathic generalized epilepsy, hypercalciuric nephrolithiasis, and classic Bartter syndrome (CLC chloride channel family members), Wolff-Parkinson-White syndrome (gamma 2 subunit of AMP-activated protein kinase), retinitis pigmentosa (IMP dehydrogenase-1), and homocystinuria (cystathionine beta-synthase). Pssm-ID: 341411 [Multi-domain] Cd Length: 117 Bit Score: 40.60 E-value: 1.83e-04
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| eIF-2B_epsilon_N | cd04197 | The N-terminal domain of epsilon subunit of the eIF-2B is a subfamily of glycosyltransferase 2; ... |
124-254 | 2.15e-04 | |||||
The N-terminal domain of epsilon subunit of the eIF-2B is a subfamily of glycosyltransferase 2; N-terminal domain of epsilon subunit of the eukaryotic translation initiation factor 2B (eIF-2B): eIF-2B is a guanine nucleotide-exchange factor which mediates the exchange of GDP (bound to initiation factor eIF2) for GTP, generating active eIF2.GTP complex. EIF2B is a complex multimeric protein consisting of five subunits named alpha, beta, gamma, delta and epsilon. Subunit epsilon shares sequence similarity with gamma subunit, and with a family of bifunctional nucleotide-binding enzymes such as ADP-glucose pyrophosphorylase, suggesting that epsilon subunit may play roles in nucleotide binding activity. In yeast, eIF2B gamma enhances the activity of eIF2B-epsilon leading to the idea that these subunits form the catalytic subcomplex. Pssm-ID: 133040 [Multi-domain] Cd Length: 217 Bit Score: 41.82 E-value: 2.15e-04
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| CBS_pair_peptidase_M50 | cd04801 | Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains found in the ... |
8-106 | 2.65e-04 | |||||
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains found in the metalloprotease peptidase M50; This cd contains two tandem repeats of the cystathionine beta-synthase (CBS pair) domains in peptidase M50. Members of the M50 metallopeptidase family include mammalian sterol-regulatory element binding protein (SREBP) site 2 proteases and various hypothetical bacterial homologues. The CBS domain, named after human CBS, is a small domain originally identified in cystathionine beta-synthase and is subsequently found in a wide range of different proteins. CBS domains usually occur in tandem repeats. They associate to form a so-called Bateman domain or a CBS pair based on crystallographic studies in bacteria. The CBS pair was used as a basis for this cd hierarchy since the human CBS proteins can adopt the typical core structure and form an intramolecular CBS pair. The interface between the two CBS domains forms a cleft that is a potential ligand binding site. The CBS pair coexists with a variety of other functional domains and this has been used to help in its classification here. It has been proposed that the CBS domain may play a regulatory role, although its exact function is unknown. Mutations of conserved residues within this domain are associated with a variety of human hereditary diseases, including congenital myotonia, idiopathic generalized epilepsy, hypercalciuric nephrolithiasis, and classic Bartter syndrome (CLC chloride channel family members), Wolff-Parkinson-White syndrome (gamma 2 subunit of AMP-activated protein kinase), retinitis pigmentosa (IMP dehydrogenase-1), and homocystinuria (cystathionine beta-synthase). Pssm-ID: 341401 [Multi-domain] Cd Length: 113 Bit Score: 39.86 E-value: 2.65e-04
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| GalU | COG1210 | UTP-glucose-1-phosphate uridylyltransferase [Cell wall/membrane/envelope biogenesis]; |
126-183 | 3.33e-04 | |||||
UTP-glucose-1-phosphate uridylyltransferase [Cell wall/membrane/envelope biogenesis]; Pssm-ID: 440823 [Multi-domain] Cd Length: 288 Bit Score: 41.94 E-value: 3.33e-04
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| CpsB | COG0836 | Mannose-1-phosphate guanylyltransferase [Cell wall/membrane/envelope biogenesis]; |
121-182 | 3.39e-04 | |||||
Mannose-1-phosphate guanylyltransferase [Cell wall/membrane/envelope biogenesis]; Pssm-ID: 440598 [Multi-domain] Cd Length: 347 Bit Score: 41.98 E-value: 3.39e-04
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| PLN02241 | PLN02241 | glucose-1-phosphate adenylyltransferase |
124-342 | 3.61e-04 | |||||
glucose-1-phosphate adenylyltransferase Pssm-ID: 215133 [Multi-domain] Cd Length: 436 Bit Score: 42.15 E-value: 3.61e-04
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| glmU | PRK14359 | bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ... |
122-297 | 3.96e-04 | |||||
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate N-acetyltransferase GlmU; Pssm-ID: 237689 [Multi-domain] Cd Length: 430 Bit Score: 41.90 E-value: 3.96e-04
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| CBS_arch_repeat2 | cd17778 | CBS pair domains found in archeal proteins, repeat 2; CBS pair domains found in archeal ... |
8-108 | 4.42e-04 | |||||
CBS pair domains found in archeal proteins, repeat 2; CBS pair domains found in archeal proteins that contain 2 repeats. The CBS domain, named after human CBS, is a small domain originally identified in cystathionine beta-synthase and is subsequently found in a wide range of different proteins. CBS domains usually occur in tandem repeats. They associate to form a so-called Bateman domain or a CBS pair based on crystallographic studies in bacteria. The CBS pair was used as a basis for this cd hierarchy since the human CBS proteins can adopt the typical core structure and form an intramolecular CBS pair. The interface between the two CBS domains forms a cleft that is a potential ligand binding site. The CBS pair coexists with a variety of other functional domains and this has been used to help in its classification here. Pssm-ID: 341414 [Multi-domain] Cd Length: 131 Bit Score: 39.62 E-value: 4.42e-04
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| YtoI | COG4109 | Predicted transcriptional regulator containing CBS domains [Transcription]; |
8-57 | 4.76e-04 | |||||
Predicted transcriptional regulator containing CBS domains [Transcription]; Pssm-ID: 443285 [Multi-domain] Cd Length: 135 Bit Score: 39.90 E-value: 4.76e-04
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| CBS_pair_proteobact | cd04640 | Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains present in ... |
8-49 | 4.79e-04 | |||||
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains present in proteobacteria; The CBS domain, named after human CBS, is a small domain originally identified in cystathionine beta-synthase and is subsequently found in a wide range of different proteins. CBS domains usually occur in tandem repeats. They associate to form a so-called Bateman domain or a CBS pair based on crystallographic studies in bacteria. The CBS pair was used as a basis for this cd hierarchy since the human CBS proteins can adopt the typical core structure and form an intramolecular CBS pair. The interface between the two CBS domains forms a cleft that is a potential ligand binding site. The CBS pair coexists with a variety of other functional domains and this has been used to help in its classification here. It has been proposed that the CBS domain may play a regulatory role, although its exact function is unknown. Mutations of conserved residues within this domain are associated with a variety of human hereditary diseases, including congenital myotonia, idiopathic generalized epilepsy, hypercalciuric nephrolithiasis, and classic Bartter syndrome (CLC chloride channel family members), Wolff-Parkinson-White syndrome (gamma 2 subunit of AMP-activated protein kinase), retinitis pigmentosa (IMP dehydrogenase-1), and homocystinuria (cystathionine beta-synthase). Pssm-ID: 341398 [Multi-domain] Cd Length: 133 Bit Score: 39.85 E-value: 4.79e-04
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| PRK10122 | PRK10122 | UTP--glucose-1-phosphate uridylyltransferase GalF; |
124-183 | 7.92e-04 | |||||
UTP--glucose-1-phosphate uridylyltransferase GalF; Pssm-ID: 182252 [Multi-domain] Cd Length: 297 Bit Score: 40.64 E-value: 7.92e-04
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| CBS_pair_ABC_OpuCA_assoc | cd04583 | Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains found associated with ... |
6-45 | 8.14e-04 | |||||
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains found associated with the ABC transporter OpuCA; This cd contains two tandem repeats of the cystathionine beta-synthase (CBS pair) domains found in association with the ABC transporter OpuCA. OpuCA is the ATP binding component of a bacterial solute transporter that serves a protective role to cells growing in a hyperosmolar environment but the function of the CBS domains in OpuCA remains unknown. In the related ABC transporter, OpuA, the tandem CBS domains have been shown to function as sensors for ionic strength, whereby they control the transport activity through an electronic switching mechanism. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. They are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins. The CBS domain, named after human CBS, is a small domain originally identified in cystathionine beta-synthase and is subsequently found in a wide range of different proteins. CBS domains usually occur in tandem repeats. They associate to form a so-called Bateman domain or a CBS pair based on crystallographic studies in bacteria. The CBS pair was used as a basis for this cd hierarchy since the human CBS proteins can adopt the typical core structure and form an intramolecular CBS pair. The interface between the two CBS domains forms a cleft that is a potential ligand binding site. The CBS pair coexists with a variety of other functional domains and this has been used to help in its classification here. It has been proposed that the CBS domain may play a regulatory role, although its exact function is unknown. Mutations of conserved residues within this domain are associated with a variety of human hereditary diseases, including congenital myotonia, idiopathic generalized epilepsy, hypercalciuric nephrolithiasis, and classic Bartter syndrome (CLC chloride channel family members), Wolff-Parkinson-White syndrome (gamma 2 subunit of AMP-activated protein kinase), retinitis pigmentosa (IMP dehydrogenase-1), and homocystinuria (cystathionine beta-synthase). Pssm-ID: 341360 [Multi-domain] Cd Length: 110 Bit Score: 38.65 E-value: 8.14e-04
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| CBS_pair_Euryarchaeota | cd17784 | Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains present in ... |
6-106 | 1.05e-03 | |||||
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains present in Euryarchaeota; The CBS domain, named after human CBS, is a small domain originally identified in cystathionine beta-synthase and is subsequently found in a wide range of different proteins. CBS domains usually occur in tandem repeats. They associate to form a so-called Bateman domain or a CBS pair based on crystallographic studies in bacteria. The CBS pair was used as a basis for this cd hierarchy since the human CBS proteins can adopt the typical core structure and form an intramolecular CBS pair. The interface between the two CBS domains forms a cleft that is a potential ligand binding site. The CBS pair coexists with a variety of other functional domains and this has been used to help in its classification here. It has been proposed that the CBS domain may play a regulatory role, although its exact function is unknown. Mutations of conserved residues within this domain are associated with a variety of human hereditary diseases, including congenital myotonia, idiopathic generalized epilepsy, hypercalciuric nephrolithiasis, and classic Bartter syndrome (CLC chloride channel family members), Wolff-Parkinson-White syndrome (gamma 2 subunit of AMP-activated protein kinase), retinitis pigmentosa (IMP dehydrogenase-1), and homocystinuria (cystathionine beta-synthase). Pssm-ID: 341420 [Multi-domain] Cd Length: 120 Bit Score: 38.56 E-value: 1.05e-03
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| COG2905 | COG2905 | Signal-transduction protein containing cAMP-binding, CBS, and nucleotidyltransferase domains ... |
10-57 | 1.12e-03 | |||||
Signal-transduction protein containing cAMP-binding, CBS, and nucleotidyltransferase domains [Signal transduction mechanisms]; Pssm-ID: 442149 [Multi-domain] Cd Length: 124 Bit Score: 38.27 E-value: 1.12e-03
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| GDP-M1P_Guanylyltransferase | cd02509 | GDP-M1P_Guanylyltransferase catalyzes the formation of GDP-Mannose; GDP-mannose-1-phosphate ... |
122-186 | 1.18e-03 | |||||
GDP-M1P_Guanylyltransferase catalyzes the formation of GDP-Mannose; GDP-mannose-1-phosphate guanylyltransferase, also called GDP-mannose pyrophosphorylase (GDP-MP), catalyzes the formation of GDP-Mannose from mannose-1-phosphate and GTP. Mannose is a key monosaccharide for glycosylation of proteins and lipids. GDP-Mannose is the activated donor for mannosylation of various biomolecules. This enzyme is known to be bifunctional, as both mannose-6-phosphate isomerase and mannose-1-phosphate guanylyltransferase. This CD covers the N-terminal GDP-mannose-1-phosphate guanylyltransferase domain, whereas the isomerase function is located at the C-terminal half. GDP-MP is a member of the nucleotidyltransferase family of enzymes. Pssm-ID: 133003 [Multi-domain] Cd Length: 274 Bit Score: 40.25 E-value: 1.18e-03
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| IspD | COG1211 | 2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase [Lipid transport and metabolism]; ... |
124-191 | 1.24e-03 | |||||
2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase [Lipid transport and metabolism]; 2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase is part of the Pathway/BioSystem: Isoprenoid biosynthesis Pssm-ID: 440824 Cd Length: 224 Bit Score: 39.73 E-value: 1.24e-03
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| CDP-ME_synthetase | cd02516 | CDP-ME synthetase is involved in mevalonate-independent isoprenoid production; ... |
124-191 | 1.29e-03 | |||||
CDP-ME synthetase is involved in mevalonate-independent isoprenoid production; 4-diphosphocytidyl-2-methyl-D-erythritol synthase (CDP-ME), also called 2C-methyl-d-erythritol 4-phosphate cytidylyltransferase catalyzes the third step in the alternative (non-mevalonate) pathway of Isopentenyl diphosphate (IPP) biosynthesis: the formation of 4-diphosphocytidyl-2C-methyl-D-erythritol from CTP and 2C-methyl-D-erythritol 4-phosphate. This mevalonate independent pathway that utilizes pyruvate and glyceraldehydes 3-phosphate as starting materials for production of IPP occurs in a variety of bacteria, archaea and plant cells, but is absent in mammals. Thus, CDP-ME synthetase is an attractive targets for the structure-based design of selective antibacterial, herbicidal and antimalarial drugs. Pssm-ID: 133009 [Multi-domain] Cd Length: 218 Bit Score: 39.81 E-value: 1.29e-03
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| CBS_pair_inorgPPase | cd04597 | Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with ... |
10-106 | 1.67e-03 | |||||
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with family II inorganic pyrophosphatase; This cd contains two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with a subgroup of family II inorganic pyrophosphatases (PPases) that also contain a DRTGG domain. The homolog from Clostridium has been shown to be inhibited by AMP and activated by a novel effector, diadenosine 5',5-P1,P4-tetraphosphate (AP(4)A), which has been shown to bind to the CBS domain. The CBS domain, named after human CBS, is a small domain originally identified in cystathionine beta-synthase and is subsequently found in a wide range of different proteins. CBS domains usually occur in tandem repeats. They associate to form a so-called Bateman domain or a CBS pair based on crystallographic studies in bacteria. The CBS pair was used as a basis for this cd hierarchy since the human CBS proteins can adopt the typical core structure and form an intramolecular CBS pair. The interface between the two CBS domains forms a cleft that is a potential ligand binding site. The CBS pair coexists with a variety of other functional domains and this has been used to help in its classification here. Pssm-ID: 341372 [Multi-domain] Cd Length: 106 Bit Score: 37.71 E-value: 1.67e-03
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| NTP_transf_3 | pfam12804 | MobA-like NTP transferase domain; This family includes the MobA protein (Molybdopterin-guanine ... |
124-172 | 2.32e-03 | |||||
MobA-like NTP transferase domain; This family includes the MobA protein (Molybdopterin-guanine dinucleotide biosynthesis protein A). The family also includes a wide range of other NTP transferase domain. Pssm-ID: 463715 [Multi-domain] Cd Length: 159 Bit Score: 38.33 E-value: 2.32e-03
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| NeuA | COG1083 | CMP-N-acetylneuraminic acid synthetase, NeuA/PseF family [Cell wall/membrane/envelope ... |
233-343 | 3.27e-03 | |||||
CMP-N-acetylneuraminic acid synthetase, NeuA/PseF family [Cell wall/membrane/envelope biogenesis]; Pssm-ID: 440700 Cd Length: 228 Bit Score: 38.60 E-value: 3.27e-03
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| CBS_pair_ParBc_assoc | cd04610 | Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with a ... |
8-51 | 3.90e-03 | |||||
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with a ParBc (ParB-like nuclease) domain; This cd contains two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with a ParBc (ParB-like nuclease) domain downstream. The CBS domain, named after human CBS, is a small domain originally identified in cystathionine beta-synthase and is subsequently found in a wide range of different proteins. CBS domains usually occur in tandem repeats. They associate to form a so-called Bateman domain or a CBS pair based on crystallographic studies in bacteria. The CBS pair was used as a basis for this cd hierarchy since the human CBS proteins can adopt the typical core structure and form an intramolecular CBS pair. The interface between the two CBS domains forms a cleft that is a potential ligand binding site. The CBS pair coexists with a variety of other functional domains and this has been used to help in its classification here. It has been proposed that the CBS domain may play a regulatory role, although its exact function is unknown. Mutations of conserved residues within this domain are associated with a variety of human hereditary diseases, including congenital myotonia, idiopathic generalized epilepsy, hypercalciuric nephrolithiasis, and classic Bartter syndrome (CLC chloride channel family members), Wolff-Parkinson-White syndrome (gamma 2 subunit of AMP-activated protein kinase), retinitis pigmentosa (IMP dehydrogenase-1), and homocystinuria (cystathionine beta-synthase). Pssm-ID: 341383 [Multi-domain] Cd Length: 108 Bit Score: 36.53 E-value: 3.90e-03
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| GT2_BcE_like | cd04183 | GT2_BcbE_like is likely involved in the biosynthesis of the polysaccharide capsule; ... |
122-289 | 4.41e-03 | |||||
GT2_BcbE_like is likely involved in the biosynthesis of the polysaccharide capsule; GT2_BcbE_like: The bcbE gene is one of the genes in the capsule biosynthetic locus of Pasteurella multocida. Its deducted product is likely involved in the biosynthesis of the polysaccharide capsule, which is found on surface of a wide range of bacteria. It is a subfamily of Glycosyltransferase Family GT2, which includes diverse families of glycosyltransferases with a common GT-A type structural fold, which has two tightly associated beta/alpha/beta domains that tend to form a continuous central sheet of at least eight beta-strands. These are enzymes that catalyze the transfer of sugar moieties from activated donor molecules to specific acceptor molecules, forming glycosidic bonds. Pssm-ID: 133026 [Multi-domain] Cd Length: 231 Bit Score: 38.00 E-value: 4.41e-03
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| CBS_pair_arch2_repeat1 | cd04638 | Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains present in archaea, ... |
18-109 | 6.55e-03 | |||||
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains present in archaea, repeat 1; The CBS domain, named after human CBS, is a small domain originally identified in cystathionine beta-synthase and is subsequently found in a wide range of different proteins. CBS domains usually occur in tandem repeats. They associate to form a so-called Bateman domain or a CBS pair based on crystallographic studies in bacteria. The CBS pair was used as a basis for this cd hierarchy since the human CBS proteins can adopt the typical core structure and form an intramolecular CBS pair. The interface between the two CBS domains forms a cleft that is a potential ligand binding site. The CBS pair coexists with a variety of other functional domains and this has been used to help in its classification here. It has been proposed that the CBS domain may play a regulatory role, although its exact function is unknown. Mutations of conserved residues within this domain are associated with a variety of human hereditary diseases, including congenital myotonia, idiopathic generalized epilepsy, hypercalciuric nephrolithiasis, and classic Bartter syndrome (CLC chloride channel family members), Wolff-Parkinson-White syndrome (gamma 2 subunit of AMP-activated protein kinase), retinitis pigmentosa (IMP dehydrogenase-1), and homocystinuria (cystathionine beta-synthase). Pssm-ID: 341396 [Multi-domain] Cd Length: 109 Bit Score: 35.78 E-value: 6.55e-03
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| CBS_pair_HRP1_like | cd04622 | CBS pair domain found in Hypoxic Response Protein 1 (HRP1) -like proteinds; Mycobacterium ... |
10-49 | 6.56e-03 | |||||
CBS pair domain found in Hypoxic Response Protein 1 (HRP1) -like proteinds; Mycobacterium tuberculosis adapts to cellular stresses by upregulation of the dormancy survival regulon. Hypoxic response protein 1 (HRP1) is encoded by one of the most strongly upregulated genes in the dormancy survival regulon. HRP1 is a 'CBS-domain-only protein; however unlike other CBS containing proteins it does not appear to bind AMP. The biological function of the protein remains unclear, but is thought to contribute to the modulation of the host immune response. The CBS domain, named after human CBS, is a small domain originally identified in cystathionine beta-synthase and is subsequently found in a wide range of different proteins. CBS domains usually occur in tandem repeats. They associate to form a so-called Bateman domain or a CBS pair based on crystallographic studies in bacteria. The CBS pair was used as a basis for this cd hierarchy since the human CBS proteins can adopt the typical core structure and form an intramolecular CBS pair. The interface between the two CBS domains forms a cleft that is a potential ligand binding site. The CBS pair coexists with a variety of other functional domains and this has been used to help in its classification here. It has been proposed that the CBS domain may play a regulatory role, although its exact function is unknown. Mutations of conserved residues within this domain are associated with a variety of human hereditary diseases, including congenital myotonia, idiopathic generalized epilepsy, hypercalciuric nephrolithiasis, and classic Bartter syndrome (CLC chloride channel family members), Wolff-Parkinson-White syndrome (gamma 2 subunit of AMP-activated protein kinase), retinitis pigmentosa (IMP dehydrogenase-1), and homocystinuria (cystathionine beta-synthase). Pssm-ID: 341390 [Multi-domain] Cd Length: 115 Bit Score: 35.86 E-value: 6.56e-03
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| GT_2_like_f | cd04182 | GT_2_like_f is a subfamily of the glycosyltransferase family 2 (GT-2) with unknown function; ... |
124-165 | 7.31e-03 | |||||
GT_2_like_f is a subfamily of the glycosyltransferase family 2 (GT-2) with unknown function; GT-2 includes diverse families of glycosyltransferases with a common GT-A type structural fold, which has two tightly associated beta/alpha/beta domains that tend to form a continuous central sheet of at least eight beta-strands. These are enzymes that catalyze the transfer of sugar moieties from activated donor molecules to specific acceptor molecules, forming glycosidic bonds. Glycosyltransferases have been classified into more than 90 distinct sequence based families. Pssm-ID: 133025 [Multi-domain] Cd Length: 186 Bit Score: 37.15 E-value: 7.31e-03
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| CBS_two-component_sensor_histidine_kinase_repeat2 | cd17774 | 2 tandem repeats of the CBS domain in the two-component sensor histidine kinase and ... |
8-54 | 9.15e-03 | |||||
2 tandem repeats of the CBS domain in the two-component sensor histidine kinase and related-proteins, repeat 2; This cd contains 2 tandem repeats of the CBS domain in the two-component sensor histidine kinase and related-proteins. Two-component regulation is the predominant form of signal recognition and response coupling mechanism used by bacteria to sense and respond to diverse environmental stresses and cues ranging from common environmental stimuli to host signals recognized by pathogens and bacterial cell-cell communication signals. The structures of both sensors and regulators are modular, and numerous variations in domain architecture and composition have evolved to tailor to specific needs in signal perception and signal transduction. The simplest histidine kinase sensors consists of only sensing and kinase domains. The more complex hybrid sensors contain an additional REC domain typical of two-component regulators and in some cases a C-terminal histidine phosphotransferase (HPT) domain. The CBS domain, named after human CBS, is a small domain originally identified in cystathionine beta-synthase and is subsequently found in a wide range of different proteins. CBS domains usually occur in tandem repeats. They associate to form a so-called Bateman domain or a CBS pair based on crystallographic studies in bacteria. The CBS pair was used as a basis for this cd hierarchy since the human CBS proteins can adopt the typical core structure and form an intramolecular CBS pair. The interface between the two CBS domains forms a cleft that is a potential ligand binding site. The CBS pair coexists with a variety of other functional domains and this has been used to help in its classification here. It has been proposed that the CBS domain may play a regulatory role, although its exact function is unknown. Mutations of conserved residues within this domain are associated with a variety of human hereditary diseases, including congenital myotonia, idiopathic generalized epilepsy, hypercalciuric nephrolithiasis, and classic Bartter syndrome (CLC chloride channel family members), Wolff-Parkinson-White syndrome (gamma 2 subunit of AMP-activated protein kinase), retinitis pigmentosa (IMP dehydrogenase-1), and homocystinuria (cystathionine beta-synthase). Pssm-ID: 341410 [Multi-domain] Cd Length: 137 Bit Score: 35.98 E-value: 9.15e-03
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| CBS_archAMPK_gamma-repeat1 | cd17779 | signal transduction protein with CBS domains; Archeal gamma-subunit of 5'-AMP-activated ... |
6-108 | 9.95e-03 | |||||
signal transduction protein with CBS domains; Archeal gamma-subunit of 5'-AMP-activated protein kinase (AMPK) contains four CBS domains in tandem repeats, similar to eukaryotic homologs. AMPK is an important regulator of metabolism and of energy homeostasis. It is a heterotrimeric protein composed of a catalytic serine/threonine kinase subunit (alpha) and two regulatory subunits (beta and gamma). The gamma subunit senses the intracellular energy status by competitively binding AMP and ATP and is believed to be responsible for allosteric regulation of the whole complex. In humans mutations in gamma- subunit of AMPK are associated with hypertrophic cardiomiopathy, Wolff-Parkinson-White syndrome and glycogen storage in the skeletal muscle. The CBS domain, named after human CBS, is a small domain originally identified in cystathionine beta-synthase and is subsequently found in a wide range of different proteins. CBS domains usually occur in tandem repeats. They associate to form a so-called Bateman domain or a CBS pair based on crystallographic studies in bacteria. The CBS pair was used as a basis for this cd hierarchy since the human CBS proteins can adopt the typical core structure and form an intramolecular CBS pair. The interface between the two CBS domains forms a cleft that is a potential ligand binding site. The CBS pair coexists with a variety of other functional domains and this has been used to help in its classification here. Pssm-ID: 341415 [Multi-domain] Cd Length: 136 Bit Score: 36.05 E-value: 9.95e-03
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