NCBI Conserved Domain Search

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: 190.11 E-value: 3.43e-58

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044790120  63 LSKALTIPDGTTVADACRRMATRRVDAALLTDASALLCGIITDKDVATRVIAEGFKPEETSVSKVMTRNPIFVMGDTLAV 142
Cdd:cd17781     1 PSPALTVPETTTVAEAAQLMAAKRTDAVLVVDDDGGLSGIFTDKDLARRVVASGLDPRSTLVSSVMTPNPLCVTMDTSAT 80

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 2044790120 143 DALQKMVQGKFRHLPVVE-NGEVVALLDITKCLYDAIA 179
Cdd:cd17781    81 DALDLMVEGKFRHLPVVDdDGDVVGVLDITKCLYDAIE 118

Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains similar to MUG70 repeat2; 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: 341418 [Multi-domain] Cd Length: 118 Bit Score: 180.14 E-value: 1.94e-54

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044790120 233 GAKVATVGLSDTVYTATKKMRDLRVNSVVIT-TNNKPQGILTSKDVLMRVVAVGLPPDTTPVEKVMTPNPECASLDTTIV 311
Cdd:cd17782     1 GTPPPLVSPKTTVREAARLMKENRTTAVLVMdNSGKVIGIFTSKDVVLRVLAAGLDPATTSVVRVMTPNPETAPPSTTIL 80

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 2044790120 312 DALHTMHDGKFLHLPVVDRDGQVVACVDVLQLTHGAVA 349
Cdd:cd17782    81 DALHKMHEGKFLNLPVVDDEGEIVGLVDVLQLTYATLQ 118

The MUG70 protein is a product of the meiotically up-regulated gene 70 which has a role in meiosis and harbors a PB1 domain. The PB1 domain is a modular domain mediating specific protein-protein interactions which play a role in many critical cell processes such as osteoclastogenesis, angiogenesis, early cardiovascular development, and cell polarity. A canonical PB1-PB1 interaction, which involves heterodimerization of two PB1 domains, is required for the formation of macromolecular signaling complexes ensuring specificity and fidelity during cellular signaling. The interaction between two PB1 domains depends on the type of PB1. There are three types of PB1 domains: type I which contains an OPCA motif, acidic amino acid cluster, type II which contains a basic cluster, and type I/II which contains both an OPCA motif and a basic cluster. Interactions of PB1 domains with other protein domains have been described as noncanonical PB1-interactions. The PB1 domain module is conserved in amoebas, fungi, animals, and plants.

Pssm-ID: 99730 Cd Length: 86 Bit Score: 137.45 E-value: 5.76e-39

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044790120 426 FSFKLEDRKGRVHRFNC-GTESLTELISAIVQRVGDDVDLNQLPHIMYEDDEGDRVLLGSDSDLVAAVNFARISGWKGLR 504
Cdd:cd06409     1 FAFKFKDPKGRVHRFRLrPSESLEELRTLISQRLGDDDFETHLYALSYVDDEGDIVLITSDSDLVAAVLVARSAGLKKLD 80


                  ....*.
gi 2044790120 505 LFLDYT 510
Cdd:cd06409    81 LHLHYP 86

Signal-transduction protein containing cAMP-binding, CBS, and nucleotidyltransferase domains [Signal transduction mechanisms];

Pssm-ID: 442149 [Multi-domain] Cd Length: 124 Bit Score: 123.40 E-value: 2.57e-33

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044790120  58 VKRLRLSKALTIPDGTTVADACRRMATRRVDAALLTDASALLCGIITDKDVATRVIAEGFKPEETSVSKVMTRNPIFVMG 137
Cdd:COG2905     1 VKDIMSRDVVTVSPDATVREAARLMTEKGVGSLVVVDDDGRLVGIITDRDLRRRVLAEGLDPLDTPVSEVMTRPPITVSP 80

                          90       100       110
                  ....*....|....*....|....*....|....
gi 2044790120 138 DTLAVDALQKMVQGKFRHLPVVENGEVVALLDIT 171
Cdd:COG2905    81 DDSLAEALELMEEHRIRHLPVVDDGKLVGIVSIT 114

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: 122.31 E-value: 4.53e-33

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044790120 234 AKVATVGLSDTVYTATKKMRDLRVNSVVITTNN-KPQGILTSKDVLMRVVAVGLPPDTTPVEKVMTPNPECASLDTTIVD 312
Cdd:cd17781     2 SPALTVPETTTVAEAAQLMAAKRTDAVLVVDDDgGLSGIFTDKDLARRVVASGLDPRSTLVSSVMTPNPLCVTMDTSATD 81

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 2044790120 313 ALHTMHDGKFLHLPVVDRDGQVVACVDVLQLTHGAVA 349
Cdd:cd17781    82 ALDLMVEGKFRHLPVVDDDGDVVGVLDITKCLYDAIE 118

Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains similar to MUG70 repeat2; 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: 341418 [Multi-domain] Cd Length: 118 Bit Score: 108.10 E-value: 7.10e-28

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044790120  64 SKALTIPDGTTVADACRRMATRRVDAALLTDASALLCGIITDKDVATRVIAEGFKPEETSVSKVMTRNPIFVMGDTLAVD 143
Cdd:cd17782     2 TPPPLVSPKTTVREAARLMKENRTTAVLVMDNSGKVIGIFTSKDVVLRVLAAGLDPATTSVVRVMTPNPETAPPSTTILD 81

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 2044790120 144 ALQKMVQGKFRHLPVVEN-GEVVALLDITKCLYDAIA 179
Cdd:cd17782    82 ALHKMHEGKFLNLPVVDDeGEIVGLVDVLQLTYATLQ 118

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: 103.66 E-value: 1.92e-26

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044790120  65 KALTIPDGTTVADACRRMATRRVDAALLTDASALlCGIITDKDVATRVIAEGFKPEeTSVSKVMTRNPIFVMGDTLAVDA 144
Cdd:cd04587     5 PPVTVPPDATIQEAAQLMSEERVSSLLVVDDGRL-VGIVTDRDLRNRVVAEGLDPD-TPVSEIMTPPPVTIDADALVFEA 82

                          90       100       110
                  ....*....|....*....|....*....|
gi 2044790120 145 LQKMVQGKFRHLPVVENGEVVALL---DIT 171
Cdd:cd04587    83 LLLMLERNIHHLPVVDDGRVVGVVtatDLM 112

Signal-transduction protein containing cAMP-binding, CBS, and nucleotidyltransferase domains [Signal transduction mechanisms];

Pssm-ID: 442149 [Multi-domain] Cd Length: 124 Bit Score: 101.83 E-value: 1.20e-25

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044790120 235 KVATVGLSDTVYTATKKMRDLRVNSVVIT-TNNKPQGILTSKDVLMRVVAVGLPPDTTPVEKVMTPNPECASLDTTIVDA 313
Cdd:COG2905     8 DVVTVSPDATVREAARLMTEKGVGSLVVVdDDGRLVGIITDRDLRRRVLAEGLDPLDTPVSEVMTRPPITVSPDDSLAEA 87

                          90       100
                  ....*....|....*....|..
gi 2044790120 314 LHTMHDGKFLHLPVVDrDGQVV 335
Cdd:COG2905    88 LELMEEHRIRHLPVVD-DGKLV 108

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: 98.65 E-value: 1.45e-24

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044790120 235 KVATVGLSDTVYTATKKMRDLRVNSVVITTNNKPQGILTSKDVLMRVVAVGLPPDtTPVEKVMTPNPECASLDTTIVDAL 314
Cdd:cd04587     5 PPVTVPPDATIQEAAQLMSEERVSSLLVVDDGRLVGIVTDRDLRNRVVAEGLDPD-TPVSEIMTPPPVTIDADALVFEAL 83

                          90       100
                  ....*....|....*....|....
gi 2044790120 315 HTMHDGKFLHLPVVDrDGQVVACV 338
Cdd:cd04587    84 LLMLERNIHHLPVVD-DGRVVGVV 106

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: 98.26 E-value: 1.77e-24

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044790120  67 LTIPDGTTVADACRRMATRRVDAALLTDASALLCGIITDKDVATRVIAEGFKPEETSVSKVMTRNPIFVMGDTLAVDALQ 146
Cdd:cd04623     5 VTVSPDATVAEALRLLAEKNIGALVVVDDGGRLVGILSERDYVRKLALRGASSLDTPVSEIMTRDVVTCTPDDTVEECMA 84

                          90       100
                  ....*....|....*....|....
gi 2044790120 147 KMVQGKFRHLPVVENGEVVALLDI 170
Cdd:cd04623    85 LMTERRIRHLPVVEDGKLVGIVSI 108

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: 97.88 E-value: 2.08e-24

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044790120 236 VATVGLSDTVYTATKKMRDLRVNSVVITTNNKPQGILTSKDVLMRVVAVGLPPDTTPVEKVMTPNPECASLDTTIVDALH 315
Cdd:cd04622     5 VVTVSPDTTLREAARLMRDLDIGALPVCEGDRLVGMVTDRDIVVRAVAEGKDPNTTTVREVMTGDVVTCSPDDDVEEAAR 84

                          90       100
                  ....*....|....*....|
gi 2044790120 316 TMHDGKFLHLPVVDRDGQVV 335
Cdd:cd04622    85 LMAEHQVRRLPVVDDDGRLV 104

CBS domain [Signal transduction mechanisms];

Pssm-ID: 440283 [Multi-domain] Cd Length: 128 Bit Score: 97.63 E-value: 4.41e-24

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044790120  57 TVKRLRLSKALTIPDGTTVADACRRMATRRVDAALLTDASALLCGIITDKDVATRVIAEGFKPEETSVSKVMTRNPIFVM 136
Cdd:COG0517     2 KVKDIMTTDVVTVSPDATVREALELMSEKRIGGLPVVDEDGKLVGIVTDRDLRRALAAEGKDLLDTPVSEVMTRPPVTVS 81

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 2044790120 137 GDTLAVDALQKMVQGKFRHLPVV-ENGEVVALL---DITKCLYDAIA 179
Cdd:COG0517    82 PDTSLEEAAELMEEHKIRRLPVVdDDGRLVGIItikDLLKALLEPLA 128

CBS domain [Signal transduction mechanisms];

Pssm-ID: 440283 [Multi-domain] Cd Length: 128 Bit Score: 95.70 E-value: 2.07e-23

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044790120 235 KVATVGLSDTVYTATKKMRDLRVNSVVITT-NNKPQGILTSKDVLMRVVAVGLPPDTTPVEKVMTPNPECASLDTTIVDA 313
Cdd:COG0517    10 DVVTVSPDATVREALELMSEKRIGGLPVVDeDGKLVGIVTDRDLRRALAAEGKDLLDTPVSEVMTRPPVTVSPDTSLEEA 89

                          90       100
                  ....*....|....*....|..
gi 2044790120 314 LHTMHDGKFLHLPVVDRDGQVV 335
Cdd:COG0517    90 AELMEEHKIRRLPVVDDDGRLV 111

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: 94.02 E-value: 5.52e-23

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044790120 233 GAKVATVGLSDTVYTATKKMRDLRVNSVVITTN-NKPQGILTSKDVLMRVVAVGLPPDTTPVEKVMTPNPECASLDTTIV 311
Cdd:cd04623     1 GRDVVTVSPDATVAEALRLLAEKNIGALVVVDDgGRLVGILSERDYVRKLALRGASSLDTPVSEIMTRDVVTCTPDDTVE 80

                          90       100
                  ....*....|....*....|....
gi 2044790120 312 DALHTMHDGKFLHLPVVDrDGQVV 335
Cdd:cd04623    81 ECMALMTERRIRHLPVVE-DGKLV 103

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: 93.38 E-value: 8.79e-23

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044790120 235 KVATVGLSDTVYTATKKMRDLRVNSVVIT-TNNKPQGILTSKDVLMRVVAVGLPPDTTPVEKVMTPNPECASLDTTIVDA 313
Cdd:cd17775     4 EVVTASPDTSVLEAARLMRDHHVGSVVVVeEDGKPVGIVTDRDIVVEVVAKGLDPKDVTVGDIMSADLITAREDDGLFEA 83

                          90       100       110
                  ....*....|....*....|....*....|...
gi 2044790120 314 LHTMHDGKFLHLPVVDRDGQVVACV---DVLQL 343
Cdd:cd17775    84 LERMREKGVRRLPVVDDDGELVGIVtldDILEL 116

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: 88.84 E-value: 3.38e-21

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044790120 235 KVATVGLSDTVYTATKKMRDLRVNSV-VITTNNKPQGILTSKDVLmRVVAVGLPPDTTPVEKVMTPNPECASLDTTIVDA 313
Cdd:cd02205     3 DVVTVDPDTTVREALELMAENGIGALpVVDDDGKLVGIVTERDIL-RALVEGGLALDTPVAEVMTPDVITVSPDTDLEEA 81

                          90       100
                  ....*....|....*....|..
gi 2044790120 314 LHTMHDGKFLHLPVVDRDGQVV 335
Cdd:cd02205    82 LELMLEHGIRRLPVVDDDGKLV 103

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: 89.12 E-value: 3.38e-21

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044790120 235 KVATVGLSDTVYTATKKMRDLRVNSVVITTN-NKPQGILTSKDVLmRVVAVGLPPDTtPVEKVMTPNPECASLDTTIVDA 313
Cdd:cd09836     4 PVVTVPPETTIREAAKLMAENNIGSVVVVDDdGKPVGIVTERDIV-RAVAEGIDLDT-PVEEIMTKNLVTVSPDESIYEA 81

                          90       100
                  ....*....|....*....|..
gi 2044790120 314 LHTMHDGKFLHLPVVDRDGQVV 335
Cdd:cd09836    82 AELMREHNIRHLPVVDGGGKLV 103

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: 88.35 E-value: 5.95e-21

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044790120  64 SKALTIPDGTTVADACRRMATRRVDAALLTDASALLCGIITDKDVaTRVIAEGfKPEETSVSKVMTRNPIFVMGDTLAVD 143
Cdd:cd09836     3 KPVVTVPPETTIREAAKLMAENNIGSVVVVDDDGKPVGIVTERDI-VRAVAEG-IDLDTPVEEIMTKNLVTVSPDESIYE 80

                          90       100       110
                  ....*....|....*....|....*....|...
gi 2044790120 144 ALQKMVQGKFRHLPVVENGE----VVALLDITK 172
Cdd:cd09836    81 AAELMREHNIRHLPVVDGGGklvgVISIRDLAR 113

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: 86.91 E-value: 1.91e-20

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044790120  64 SKALTIPDGTTVADACRRMATRRVDAALLTDASALLCGIITDKDVAtRVIAEGFKPEETSVSKVMTRNPIFVMGDTLAVD 143
Cdd:cd02205     2 RDVVTVDPDTTVREALELMAENGIGALPVVDDDGKLVGIVTERDIL-RALVEGGLALDTPVAEVMTPDVITVSPDTDLEE 80

                          90       100
                  ....*....|....*....|....*....
gi 2044790120 144 ALQKMVQGKFRHLPVV-ENGEVVALLDIT 171
Cdd:cd02205    81 ALELMLEHGIRRLPVVdDDGKLVGIVTRR 109

Predicted transcriptional regulator, contains C-terminal CBS domains [Transcription];

Pssm-ID: 442013 [Multi-domain] Cd Length: 206 Bit Score: 88.79 E-value: 3.60e-20

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044790120 156 LPVVENGEVVALLDITKCLYDAIARMERAAEKGNAIAAAVEGVERQWGNNANAAPSNFI-----ETLRERMFRPTLGSLL 230
Cdd:COG2524    13 LPLLAVVLAALLLLAALVLALTAAAAATVLLLAAAAAAAGAGGLGLLLLLLLIVLQAAAvrvvaEKELGLVLKMKVKDIM 92

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044790120 231 SEgaKVATVGLSDTVYTATKKMRDLRVNSVVITTNNKPQGILTSKDvLMRVVAVGLPPDTTPVEKVMTPNPECASLDTTI 310
Cdd:COG2524    93 TK--DVITVSPDTTLEEALELMLEKGISGLPVVDDGKLVGIITERD-LLKALAEGRDLLDAPVSDIMTRDVVTVSEDDSL 169

                         170       180
                  ....*....|....*....|....*
gi 2044790120 311 VDALHTMHDGKFLHLPVVDRDGQVV 335
Cdd:COG2524   170 EEALRLMLEHGIGRLPVVDDDGKLV 194

CBS-domain-containing membrane protein [Signal transduction mechanisms];

Pssm-ID: 442671 [Multi-domain] Cd Length: 136 Bit Score: 85.30 E-value: 1.09e-19

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044790120 235 KVATVGLSDTVYTATKKMRDLRVNSV-VITTNNKPQGILTSKDVLMRVVAVGLP-----PDTTPVEKVMTPNPECASLDT 308
Cdd:COG3448    11 DVVTVSPDTTLREALELMREHGIRGLpVVDEDGRLVGIVTERDLLRALLPDRLDeleerLLDLPVEDVMTRPVVTVTPDT 90

                          90       100
                  ....*....|....*....|....*..
gi 2044790120 309 TIVDALHTMHDGKFLHLPVVDRDGQVV 335
Cdd:COG3448    91 PLEEAAELMLEHGIHRLPVVDDDGRLV 117

Predicted transcriptional regulator, contains C-terminal CBS domains [Transcription];

Pssm-ID: 442013 [Multi-domain] Cd Length: 206 Bit Score: 86.09 E-value: 3.89e-19

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044790120  57 TVKRLRLSKALTIPDGTTVADACRRMATRRVDAALLTDASALLcGIITDKDVAtRVIAEGFKPEETSVSKVMTRNPIFVM 136
Cdd:COG2524    87 KVKDIMTKDVITVSPDTTLEEALELMLEKGISGLPVVDDGKLV-GIITERDLL-KALAEGRDLLDAPVSDIMTRDVVTVS 164

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 2044790120 137 GDTLAVDALQKMVQGKFRHLPVVE-NGEVVALL---DITKCL 174
Cdd:COG2524   165 EDDSLEEALRLMLEHGIGRLPVVDdDGKLVGIItrtDILRAL 206

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: 79.00 E-value: 1.21e-17

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044790120  68 TIPDGTTVADACRRMATRRVDAALLTDASALlCGIITDKDVATRVIAEGFKPEETSVSKVMTRNPIFVMGDTLAVDALQK 147
Cdd:cd04622     7 TVSPDTTLREAARLMRDLDIGALPVCEGDRL-VGMVTDRDIVVRAVAEGKDPNTTTVREVMTGDVVTCSPDDDVEEAARL 85

                          90       100
                  ....*....|....*....|....*..
gi 2044790120 148 MVQGKFRHLPVVENGE----VVALLDI 170
Cdd:cd04622    86 MAEHQVRRLPVVDDDGrlvgIVSLGDL 112

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: 77.58 E-value: 3.53e-17

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044790120  68 TIPDGTTVADACRRMATRRVDAALLTDASALLCGIITDKDVATRVIAEGFKPEETSVSKVMTRNPIFVMGDTLAVDALQK 147
Cdd:cd17775     7 TASPDTSVLEAARLMRDHHVGSVVVVEEDGKPVGIVTDRDIVVEVVAKGLDPKDVTVGDIMSADLITAREDDGLFEALER 86

                          90       100       110
                  ....*....|....*....|....*....|.
gi 2044790120 148 MVQGKFRHLPVV-ENGE---VVALLDITKCL 174
Cdd:cd17775    87 MREKGVRRLPVVdDDGElvgIVTLDDILELL 117

Predicted transcriptional regulator containing CBS domains [Transcription];

Pssm-ID: 443285 [Multi-domain] Cd Length: 135 Bit Score: 76.10 E-value: 1.94e-16

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044790120 235 KVATVGLSDTVYTATKKMRDLRVNSV-VITTNNKPQGILTSKDVLMRvvavglpPDTTPVEKVMTPNPECASLDTTIVDA 313
Cdd:COG4109    26 DVATLSEDDTVEDALELLEKTGHSRFpVVDENGRLVGIVTSKDILGK-------DDDTPIEDVMTKNPITVTPDTSLASA 98

                          90       100
                  ....*....|....*....|..
gi 2044790120 314 LHTMHDGKFLHLPVVDRDGQVV 335
Cdd:COG4109    99 AHKMIWEGIELLPVVDDDGRLL 120

CBS-domain-containing membrane protein [Signal transduction mechanisms];

Pssm-ID: 442671 [Multi-domain] Cd Length: 136 Bit Score: 75.67 E-value: 2.88e-16

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044790120  68 TIPDGTTVADACRRMATRRVDAALLTDASALLCGIITDKDVATRVIAEGF-----KPEETSVSKVMTRNPIFVMGDTLAV 142
Cdd:COG3448    14 TVSPDTTLREALELMREHGIRGLPVVDEDGRLVGIVTERDLLRALLPDRLdeleeRLLDLPVEDVMTRPVVTVTPDTPLE 93

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 2044790120 143 DALQKMVQGKFRHLPVV-ENGEVVALL---DITKCLYDAIAR 180
Cdd:COG3448    94 EAAELMLEHGIHRLPVVdDDGRLVGIVtrtDLLRALARLLEE 135

PB1 domain;

Pssm-ID: 395447 Cd Length: 84 Bit Score: 68.86 E-value: 1.49e-14

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044790120 425 TFSFKLEDRKGRVH-RFNCGTESLTELISAIVQRVGDDvdlNQLPHIMYEDDEGDRVLLGSDSDLVAAVNFARISGWKGL 503
Cdd:pfam00564   1 TVRLKLRYGGGIRRfLSVSRGISFEELRALVEQRFGLD---DVDFKLKYPDEDGDLVSLTSDEDLEEALEEARSLGSKSL 77


                  ....*..
gi 2044790120 504 RLFLDYT 510
Cdd:pfam00564  78 RLHVFPT 84

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: 67.73 E-value: 8.60e-14

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044790120 248 ATKKMRDLRVNSVVIT-TNNKPQGILTSKDVLMRVVAVGLPPDTtPVEKVMTPNPECASLDTTIVDALHTMHDGKFLHLP 326
Cdd:cd17771    18 ALETMHERRVGSMVVVdANRRPVGIFTLRDLLSRVALPQIDLDA-PISEVMTPDPVRLPPSASAFEAALLMAEHGFRHVC 96


                  ....*
gi 2044790120 327 VVDRD 331
Cdd:cd17771    97 VVDNG 101

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: 67.02 E-value: 2.36e-13

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044790120  69 IPDGTTVADACRRMATRRVDAALLTDASALLCGIITDKDVAtRVIAEGFKPEETSVSKVMTRNPIFVMGDTLAVDALQKM 148
Cdd:cd04604    18 VSPDTSLKEALLEMTRKGLGCTAVVDEDGRLVGIITDGDLR-RALEKGLDILNLPAKDVMTRNPKTISPDALAAEALELM 96

                          90       100
                  ....*....|....*....|...
gi 2044790120 149 VQGKFRHLPVV-ENGEVVALLDI 170
Cdd:cd04604    97 EEHKITVLPVVdEDGKPVGILHL 119

Predicted transcriptional regulator containing CBS domains [Transcription];

Pssm-ID: 443285 [Multi-domain] Cd Length: 135 Bit Score: 67.24 E-value: 2.36e-13

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044790120  61 LRLSKALTIPDGTTVADACRRMATRRVDAALLTDASALLCGIITDKDVATrviaegfKPEETSVSKVMTRNPIFVMGDTL 140
Cdd:COG4109    22 MTLEDVATLSEDDTVEDALELLEKTGHSRFPVVDENGRLVGIVTSKDILG-------KDDDTPIEDVMTKNPITVTPDTS 94

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 2044790120 141 AVDALQKMVQGKFRHLPVV-ENGEVVALL---DITKCL 174
Cdd:COG4109    95 LASAAHKMIWEGIELLPVVdDDGRLLGIIsrqDVLKAL 132

PB1 domain; Phox and Bem1p domain, present in many eukaryotic cytoplasmic signalling proteins. The domain adopts a beta-grasp fold, similar to that found in ubiquitin and Ras-binding domains. A motif, variously termed OPR, PC and AID, represents the most conserved region of the majority of PB1 domains, and is necessary for PB1 domain function. This function is the formation of PB1 domain heterodimers, although not all PB1 domain pairs associate.

Pssm-ID: 214770 Cd Length: 81 Bit Score: 65.30 E-value: 2.37e-13

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044790120  425 TFSFKLEDrKGRVHRFNC-GTESLTELISAIVQRVGDDvdlNQLPHIMYEDDEGDRVLLGSDSDLVAAVNFARISGWKGL 503
Cdd:smart00666   1 TVDVKLRY-GGETRRLSVpRDISFEDLRSKVAKRFGLD---NQSFTLKYQDEDGDLVSLTSDEDLEEAIEEYDSLGSKKL 76


                   ....*
gi 2044790120  504 RLFLD 508
Cdd:smart00666  77 RLHVF 81

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: 66.00 E-value: 3.25e-13

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044790120  65 KALTIPDGTTVADACRRMATRRVDAALLTDASALLCGIITDKDvatrvIAEGFKpEETSVSKVMTRNPIFVMGDTLAVDA 144
Cdd:cd04583     3 NPVTITPERTLAQAIEIMREKRVDSLLVVDKDNVLLGIVDIED-----INRNYR-KAKKVGEIMERDVFTVKEDSLLRDT 76

                          90       100
                  ....*....|....*....|....*....
gi 2044790120 145 LQKMVQGKFRHLPVV-ENGEVVALldITK 172
Cdd:cd04583    77 VDRILKRGLKYVPVVdEQGRLVGL--VTR 103

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: 66.68 E-value: 3.63e-13

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044790120 124 VSKVMTRNPIFV-MGDTLAvDALQKMVQGKFRHLPVVENGEVVALL---DITKclydaiarmeraaekgnaiaaavegve 199
Cdd:cd04584     2 VKDIMTKNVVTVtPDTSLA-EARELMKEHKIRHLPVVDDGKLVGIVtdrDLLR--------------------------- 53

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044790120 200 rqwgnnanAAPSNF----IETLRERMFRPTLGSLLSEgaKVATVGLSDTVYTATKKMRDLRVNSVVITTNNKPQGILTSK 275
Cdd:cd04584    54 --------ASPSKAtslsIYELNYLLSKIPVKDIMTK--DVITVSPDDTVEEAALLMLENKIGCLPVVDGGKLVGIITET 123


                  ...
gi 2044790120 276 DVL 278
Cdd:cd04584   124 DIL 126

The PB1 domain is a modular domain mediating specific protein-protein interactions which play a role in many critical cell processes, such as osteoclastogenesis, angiogenesis, early cardiovascular development, and cell polarity. A canonical PB1-PB1 interaction, which involves heterodimerization of two PB1 domain, is required for the formation of macromolecular signaling complexes ensuring specificity and fidelity during cellular signaling. The interaction between two PB1 domain depends on the type of PB1. There are three types of PB1 domains: type I which contains an OPCA motif, acidic aminoacid cluster, type II which contains a basic cluster, and type I/II which contains both an OPCA motif and a basic cluster. Interactions of PB1 domains with other protein domains have been described as a noncanonical PB1-interactions. The PB1 domain module is conserved in amoebas, fungi, animals, and plants.

Pssm-ID: 99716 [Multi-domain] Cd Length: 81 Bit Score: 63.84 E-value: 8.23e-13

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044790120 426 FSFKLEDrKGRVHRF--NCGTESLTELISAIVQRVGDDvdlNQLPHIMYEDDEGDRVLLGSDSDLVAAVNFARISGWKGL 503
Cdd:cd05992     1 VRVKVKY-GGEIRRFvvVSRSISFEDLRSKIAEKFGLD---AVSFKLKYPDEDGDLVTISSDEDLEEAIEEARRSGSKKL 76


                  ....*
gi 2044790120 504 RLFLD 508
Cdd:cd05992    77 RLFVF 81

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: 64.66 E-value: 1.53e-12

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044790120 124 VSKVMTRNPIFVMGDTLAVDALQKMVQGKFRHLPVVENGEVVALLDITkclyDAIARMERAAEKGNAIAAAVEGVerqwg 203
Cdd:cd17778     2 VKEFMTTPVVTIYPDDTLKEAMELMVTRGFRRLPVVSGGKLVGIVTAM----DIVKYFGSHEAKKRLTTGDIDEA----- 72

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2044790120 204 nnanaapsnFIETLRERMFRPtlgsllsegakVATVGLSDTVYTATKKMRDLRVNSVVIT-TNNKPQGILTSKDVLMR 280
Cdd:cd17778    73 ---------YSTPVEEIMSKE-----------VVTIEPDADIAEAARLMIKKNVGSLLVVdDEGELKGIITERDVLIA 130

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: 63.61 E-value: 2.69e-12

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044790120  65 KALTIPDGTTVADACRRMATRRVDAALLTDASALLCGIITDKDVATRVIAEGFKPEETS-VSKVMTRNPIFVMGDTLAVD 143
Cdd:cd04629     4 NPVTLTPDTSILEAVELLLEHKISGAPVVDEQGRLVGFLSEQDCLKALLEASYHCEPGGtVADYMSTEVLTVSPDTSIVD 83

                          90       100
                  ....*....|....*....|....*
gi 2044790120 144 ALQKMVQGKFRHLPVVENGEVVALL 168
Cdd:cd04629    84 LAQLFLKNKPRRYPVVEDGKLVGQI 108

Predicted transcriptional regulator, contains C-terminal CBS domains [Transcription];

Pssm-ID: 442013 [Multi-domain] Cd Length: 206 Bit Score: 65.68 E-value: 3.34e-12

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044790120  43 PGGAGRPLTSPGERTVKRLRLSKALTIPDGTTVADACRRMATRRVDAALLTDASALLCGIITDKDVATRVIAEGFKPEET 122
Cdd:COG2524     7 LALSLLLPLLAVVLAALLLLAALVLALTAAAAATVLLLAAAAAAAGAGGLGLLLLLLLIVLQAAAVRVVAEKELGLVLKM 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044790120 123 SVSKVMTRNPIFVMGDTLAVDALQKMVQGKFRHLPVVENGEVVALL---DITKCLYDAIARMERaaekgnaiaaavegve 199
Cdd:COG2524    87 KVKDIMTKDVITVSPDTTLEEALELMLEKGISGLPVVDDGKLVGIIterDLLKALAEGRDLLDA---------------- 150

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044790120 200 rqwgnnanaapsnfieTLRERMFRPtlgsllsegakVATVGLSDTVYTATKKMRDLRVNSVVIT-TNNKPQGILTSKDVL 278
Cdd:COG2524   151 ----------------PVSDIMTRD-----------VVTVSEDDSLEEALRLMLEHGIGRLPVVdDDGKLVGIITRTDIL 203

CBS-domain-containing membrane protein [Signal transduction mechanisms];

Pssm-ID: 442671 [Multi-domain] Cd Length: 136 Bit Score: 62.96 E-value: 7.61e-12

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044790120 124 VSKVMTRNPIFVMGDTLAVDALQKMVQGKFRHLPVV-ENGEVVALL---DItkclydaiarmeraaekgnaiaaavegve 199
Cdd:COG3448     4 VRDIMTRDVVTVSPDTTLREALELMREHGIRGLPVVdEDGRLVGIVterDL----------------------------- 54

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044790120 200 rqwgnnANAAPSNFIETLRERMFRPTLGSLLSEgaKVATVGLSDTVYTATKKMRDLRVNSV-VITTNNKPQGILTSKDVL 278
Cdd:COG3448    55 ------LRALLPDRLDELEERLLDLPVEDVMTR--PVVTVTPDTPLEEAAELMLEHGIHRLpVVDDDGRLVGIVTRTDLL 126

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: 61.57 E-value: 1.40e-11

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044790120  66 ALTIPDGTTVADACRRMATRRVDAALLTDASALLCGIITDKDVATRVIAEGFkPEETSVSKVMTRNPIFVMGDTLAVDAL 145
Cdd:cd17771     6 PVTCSPDTPLRAALETMHERRVGSMVVVDANRRPVGIFTLRDLLSRVALPQI-DLDAPISEVMTPDPVRLPPSASAFEAA 84

                          90       100
                  ....*....|....*....|...
gi 2044790120 146 QKMVQGKFRHLPVVENGEVVALL 168
Cdd:cd17771    85 LLMAEHGFRHVCVVDNGRLVGVV 107

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: 61.59 E-value: 2.53e-11

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044790120 236 VATVGLSDTVYTATKKMRDLRVNSVVITTNNKPQGILTSKDVLMrvVAVGLPPD----------------TTPVEKVMTP 299
Cdd:cd17777    12 VLSISPSAPILSAFEKMNRRGIRRLVVVDENKLEGILSARDLVS--YLGGGCLFkivesrhqgdlysalnREVVETIMTP 89

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 2044790120 300 NPECASLDTTIVDALHTMHDGKFLHLPVVDRDGQVVACV 338
Cdd:cd17777    90 NPVYVYEDSDLIEALTIMVTRGIGSLPVVDRDGRPVGIV 128

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: 60.90 E-value: 3.83e-11

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044790120 235 KVATVGLSDTVYTATKKMRDLRVNSVVITTNNKPQGILTSKDVL---------MRVVAVGLPPDTTPVEKVMTPNPECAS 305
Cdd:cd04584     9 NVVTVTPDTSLAEARELMKEHKIRHLPVVDDGKLVGIVTDRDLLraspskatsLSIYELNYLLSKIPVKDIMTKDVITVS 88

                          90       100       110
                  ....*....|....*....|....*....|
gi 2044790120 306 LDTTIVDALHTMHDGKFLHLPVVDrDGQVV 335
Cdd:cd04584    89 PDDTVEEAALLMLENKIGCLPVVD-GGKLV 117

Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains present in 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: 341412 [Multi-domain] Cd Length: 115 Bit Score: 59.73 E-value: 5.64e-11

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044790120 236 VATVGLSDTVYTATKKMRDLRVNSVVITTNNKPQGILTSKDVLMRVVAVGLPPDTTPVEKVMTPNPECASLDTTIVDALH 315
Cdd:cd17776     5 VVTVDADASLEDAAERMLRNRVGSVVVTDDGTPAGILTETDALHAGYATDDPFSEIPVRAVASRPLVTISPTATLREAAE 84

                          90
                  ....*....|....*.
gi 2044790120 316 TMHDGKFLHLPVVDRD 331
Cdd:cd17776    85 RMVDEGVKKLPVVDGL 100

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: 59.36 E-value: 1.18e-10

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044790120  68 TIPDGTTVADACRRMATRRVDAALLTDASALLcGIITDKDV--ATRVIAEGFKPEE-------TSVSKVMTRNPIFVMGD 138
Cdd:cd04584    12 TVTPDTSLAEARELMKEHKIRHLPVVDDGKLV-GIVTDRDLlrASPSKATSLSIYElnyllskIPVKDIMTKDVITVSPD 90

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 2044790120 139 TLAVDALQKMVQGKFRHLPVVENGEVVALL---DITKCL 174
Cdd:cd04584    91 DTVEEAALLMLENKIGCLPVVDGGKLVGIItetDILRAF 129

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: 58.61 E-value: 1.52e-10

                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2044790120 261 VITTNNKPQGILTSKDV---LMRvvavGLPPDTtPVEKVMTPNPECASLDTTIVDALHTMHDGKFLHLPVVDRDGQVV 335
Cdd:cd04607    30 VVDENRKLLGTVTDGDIrrgLLK----GLSLDA-PVEEVMNKNPITASPSTSREELLALMRAKKILQLPIVDEQGRVV 102

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: 58.32 E-value: 3.34e-10

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044790120 242 SDTVYTATKKMRDLRVNSVVITTNNKPQGILTSKDVLmRVVAVGLPPDTTPVEKVMTPNP----ECASLDttIVDALHTM 317
Cdd:cd04620    31 SCCLLSEDSIITEARSSCVLVVENQQLVGIFTERDVV-RLTASGIDLSGVTIAEVMTQPVitlkESEFQD--IFTVLSLL 107

                          90
                  ....*....|....*...
gi 2044790120 318 HDGKFLHLPVVDRDGQVV 335
Cdd:cd04620   108 RQHQIRHLPIVDDQGQLV 125

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: 57.82 E-value: 4.14e-10

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044790120 235 KVATVGLSDTVYTATKKMRDLRVNSV-VITTNNKPQGILTSKDVLMRVVAVGLPPD----------------------TT 291
Cdd:cd04586     4 DVVTVTPDTSVREAARLLLEHRISGLpVVDDDGKLVGIVSEGDLLRREEPGTEPRRvwwldallesperlaeeyvkahGR 83

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 2044790120 292 PVEKVMTPNPECASLDTTIVDALHTMHDGKFLHLPVVDrDGQVV 335
Cdd:cd04586    84 TVGDVMTRPVVTVSPDTPLEEAARLMERHRIKRLPVVD-DGKLV 126

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: 341393 [Multi-domain] Cd Length: 120 Bit Score: 57.22 E-value: 5.75e-10

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044790120  67 LTIPDGTTVADACRRMATRRVDAALLTDASALLC-GIITDKDVATRVIAEGFKPEETSVSKVMTRnPIFVMGDTLAVD-A 144
Cdd:cd04630    10 VTIDGLATVREALQLMKEHNVKSLIVEKRHEHDAyGIVTYTDILKKVIAEDRDPDLVNVYEIMTK-PAISVSPDLDIKyA 88

                          90       100
                  ....*....|....*....|....*..
gi 2044790120 145 LQKMVQGKFRHLPVVENGEVVALLDIT 171
Cdd:cd04630    89 ARLMARFNLKRAPVIENNELIGIVSMT 115

Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with the DRTGG domain; This cd contains two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with a DRTGG domain upstream. The function of the DRTGG domain, named after its conserved residues, is unknown. 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: 341371 [Multi-domain] Cd Length: 108 Bit Score: 56.32 E-value: 7.70e-10

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044790120 261 VITTNNKPQGILTSKDVlmrvvaVGLPPDTtPVEKVMTPNPECASLDTTIVDALHTM-HDGKFLhLPVVDRDGQVVACV- 338
Cdd:cd04596    30 VVDEENRVVGIVTAKDV------IGKEDDT-PIEKVMTKNPITVKPKTSVASAAHMMiWEGIEL-LPVVDENRKLLGVIs 101


                  ....*.
gi 2044790120 339 --DVLQ 342
Cdd:cd04596   102 rqDVLK 107

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: 56.78 E-value: 1.04e-09

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044790120  67 LTIPDGTTVADACRRMA-TRRVDAALLTDASAL--------------LCGIITDKDVaTRVIAEGFKPEETSVSKVMTRN 131
Cdd:cd04620    10 LTVSPDTPVIEAIALMSqTRSSCCLLSEDSIITearsscvlvvenqqLVGIFTERDV-VRLTASGIDLSGVTIAEVMTQP 88

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 2044790120 132 PIfvmgdTLAVDALQK-------MVQGKFRHLPVV-ENGEVVALL 168
Cdd:cd04620    89 VI-----TLKESEFQDiftvlslLRQHQIRHLPIVdDQGQLVGLI 128

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: 56.28 E-value: 1.40e-09

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044790120  64 SKALTIPDGTTVADACRRMATRRVDAALLTDASALLCGIITDKDV----------------------ATRVIAEGFKPEE 121
Cdd:cd04586     3 TDVVTVTPDTSVREAARLLLEHRISGLPVVDDDGKLVGIVSEGDLlrreepgteprrvwwldallesPERLAEEYVKAHG 82

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 2044790120 122 TSVSKVMTRNPIFVMGDTLAVDALQKMVQGKFRHLPVVENGEVV 165
Cdd:cd04586    83 RTVGDVMTRPVVTVSPDTPLEEAARLMERHRIKRLPVVDDGKLV 126

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: 341365 [Multi-domain] Cd Length: 113 Bit Score: 55.66 E-value: 1.48e-09

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044790120  63 LSKALTIPDGTTVADACRRMATRRVDAALLTDASaLLCGIITDKDVATRVIAEGfKPEETSVSKVMTRNPIFVMGDTLAV 142
Cdd:cd04589     2 LHPPLFVDAETSIREATRLMKENGADSLLVRDGD-GRVGIVTRTDLRDAVVLDG-QPVDTPVGEIATFPLISVEPDDFLF 79

                          90       100
                  ....*....|....*....|....*....
gi 2044790120 143 DALQKMVQGKFRHLPVVENGEVVALLDIT 171
Cdd:cd04589    80 NALLLMTRHRVKRVVVREGEEIVGVLEQT 108

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: 55.02 E-value: 2.36e-09

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044790120 235 KVATVGLSDTVYTATKKMRDLRVNSVVITTNNKPQGILTSKDVLmrvvavgLPPDTTPVEKVMTPNPECASLDTTIVDAL 314
Cdd:cd04610     4 DVITVSPDDTVKDVIKLIKETGHDGFPVVDDGKVVGYVTAKDLL-------GKDDDEKVSEIMSRDTVVADPDMDITDAA 76

                          90       100
                  ....*....|....*....|.
gi 2044790120 315 HTMHDGKFLHLPVVDRDGQVV 335
Cdd:cd04610    77 RVIFRSGISKLPVVDDEGNLV 97

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: 55.62 E-value: 2.75e-09

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044790120 241 LSDTVYTATKKMRDLRVNSVVITTNN--------KPQGILTSKDVLmRVVAVGLPPDTTPVEKVMTPNPECASLDTTIVD 312
Cdd:cd17774    12 PTASVLELAQLMAEHRVSCVVIVEEDeqqeknklIPVGIVTERDIV-QFQALGLDLSQTQAQTVMSSPLFSLRPDDSLWT 90

                          90       100
                  ....*....|....*....|.
gi 2044790120 313 ALHTMHDGKFLHLPVVDRDGQ 333
Cdd:cd17774    91 AHQLMQQRRIRRLVVVGEQGE 111

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: 54.85 E-value: 2.89e-09

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044790120  67 LTIPDGTTVADACRRMATRRVDAALLTDASALLcGIITDKDVAtRVIAEGFkpEETSVSKVMTRNPIFVMGDTLAVDALQ 146
Cdd:cd04588     5 ITLKPDATIKDAAKLLSENNIHGAPVVDDGKLV-GIVTLTDIA-KALAEGK--ENAKVKDIMTKDVITIDKDEKIYDAIR 80

                          90       100
                  ....*....|....*....|...
gi 2044790120 147 KMVQGKFRHLPVV-ENGEVVALL 168
Cdd:cd04588    81 LMNKHNIGRLIVVdDNGKPVGII 103

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: 53.73 E-value: 7.23e-09

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044790120  68 TIPDGTTVADACRRMATRRVDAALLTDASALLcGIITDKDVATrviAEGFKPEETSVSKVMTRNPIFVMGDTLAVDALQK 147
Cdd:cd04801     9 TVTPEMTVSELLDRMFEEKHLGYPVVENGRLV-GIVTLEDIRK---VPEVEREATRVRDVMTKDVITVSPDADAMEALKL 84

                          90       100
                  ....*....|....*....|....*...
gi 2044790120 148 MVQGKFRHLPVVENGEVVALL---DITK 172
Cdd:cd04801    85 MSQNNIGRLPVVEDGELVGIIsrtDLMR 112

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: 52.80 E-value: 1.22e-08

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044790120 238 TVGLSDTVYTATKKMRDLRVNSVVITTN-NKPQGILTSKDvlMRVVavglPPDTTPVEKVMTPNPE--CASLDTTIVDAL 314
Cdd:cd04601     6 TLSPDATVADVLELKAEYGISGVPVTEDgGKLVGIVTSRD--IRFE----TDLSTPVSEVMTPDERlvTAPEGITLEEAK 79

                          90       100
                  ....*....|....*....|..
gi 2044790120 315 HTMHDGKFLHLPVVDRDGQVVA 336
Cdd:cd04601    80 EILHKHKIEKLPIVDDNGELVG 101

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: 52.38 E-value: 2.55e-08

                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2044790120 260 VVITTNNKPQGILTSKDvLMRVVAVGLPPDTTPVEKVMTPNPECASLDTTIVDALHTMHDGKFLHLPVVDRDGQVV 335
Cdd:cd04604    40 AVVDEDGRLVGIITDGD-LRRALEKGLDILNLPAKDVMTRNPKTISPDALAAEALELMEEHKITVLPVVDEDGKPV 114

Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains found in diguanylate cyclase/phosphodiesterase proteins with PAS sensors, repeat 1; This cd contains two tandem repeats of the cystathionine beta-synthase (CBS pair) domains found in diguanylate cyclase/phosphodiesterase proteins with PAS sensors. PAS domains have been found to bind ligands, and to act as sensors for light and oxygen in signal transduction. 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: 341403 [Multi-domain] Cd Length: 116 Bit Score: 52.23 E-value: 2.80e-08

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044790120 244 TVYTATKKMRDLRVNSVVITTNNKPQGILTSKDVLmrvvAVGL-PPD--TTPVEKVMTPNPECASLDTTIVDALHTMHDG 320
Cdd:cd09833    15 PLADAAARMAERRCSSILIVENGEIVGIWTERDAL----KLDFsDPDafRRPISEVMSSPVLTIPQDTTLGEAAVRFRQE 90

                          90       100
                  ....*....|....*....|...
gi 2044790120 321 KFLHLPVVDRDGQ---VVACVDV 340
Cdd:cd09833    91 GVRHLLVVDDDGRpvgIVSQTDV 113

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: 52.73 E-value: 3.30e-08

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044790120  66 ALTIPDGTTVADACRRMATRRVDAALLTDASALLcGIITDKDVATRViaEGFKP----------------EETSVSKVMT 129
Cdd:cd17777    12 VLSISPSAPILSAFEKMNRRGIRRLVVVDENKLE-GILSARDLVSYL--GGGCLfkivesrhqgdlysalNREVVETIMT 88

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 2044790120 130 RNPIFVMGDTLAVDALQKMVQGKFRHLPVV-ENGEVV 165
Cdd:cd17777    89 PNPVYVYEDSDLIEALTIMVTRGIGSLPVVdRDGRPV 125

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: 51.68 E-value: 3.64e-08

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044790120  65 KALTIPDgTTVADACRRM---ATRrvdAALLTDASALLCGIITDKDVaTRVIAEGfKPEETSVSKVMTRNPIFVMGDTLA 141
Cdd:cd04607     4 KVLVSPD-TTIREAIEVIdkgALQ---IALVVDENRKLLGTVTDGDI-RRGLLKG-LSLDAPVEEVMNKNPITASPSTSR 77

                          90       100
                  ....*....|....*....|....*..
gi 2044790120 142 VDALQKMVQGKFRHLPVV-ENGEVVAL 167
Cdd:cd04607    78 EELLALMRAKKILQLPIVdEQGRVVGL 104

Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains of CcpN repressor; 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: 341387 [Multi-domain] Cd Length: 125 Bit Score: 52.11 E-value: 3.81e-08

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044790120  63 LSKALTIPDGTTVADACRRMATRRVDAALLTDASALLCGIITDKDVaTRVIAEGFKPEETSVSKVMTRNP--IFVMGDTL 140
Cdd:cd04617     3 MSVPVVVDETTSVYDAIVTLFLEDVGSLFVVDEEGYLVGVVSRKDL-LKATLGGQDLEKTPVSMIMTRMPniVTVTPDDS 81

                          90       100
                  ....*....|....*....|...
gi 2044790120 141 AVDALQKMVQGKFRHLPVVENGE 163
Cdd:cd04617    82 VLEAARKLIEHEIDSLPVVEKED 104

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: 51.65 E-value: 4.79e-08

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044790120  67 LTIPDGTTVADACRRMATRRVDAALLTDASALLCGIITDKDVATRVIAEGFKPEeTSVSKVMTRNPIFVMGDTLAVDALQ 146
Cdd:cd17784     5 ITAKPNEGVVEAFEKMLKHKISALPVVDDEGKLIGIVTATDLGHNLILDKYELG-TTVEEVMVKDVATVHPDETLLEAIK 83

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 2044790120 147 KM-----VQGKFRHLPVVENGEVVALL---DITKCL 174
Cdd:cd17784    84 KMdsnapDEEIINQLPVVDDGKLVGIIsdgDIIRAI 119

CBS-domain-containing membrane protein [Signal transduction mechanisms];

Pssm-ID: 442671 [Multi-domain] Cd Length: 136 Bit Score: 51.79 E-value: 5.49e-08

                          10        20        30        40
                  ....*....|....*....|....*....|....*....|...
gi 2044790120 293 VEKVMTPNPECASLDTTIVDALHTMHDGKFLHLPVVDRDGQVV 335
Cdd:COG3448     4 VRDIMTRDVVTVSPDTTLREALELMREHGIRGLPVVDEDGRLV 46

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: 54.70 E-value: 8.41e-08

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044790120 238 TVGLSDTVYTATKKMRDLRVNSVVITTNNKPQGILTSKDvlMRVVavglPPDTTPVEKVMTP-NPECASLDTTIVDALHT 316
Cdd:pfam00478  92 TLSPDATVADALALMERYGISGVPVVDDGKLVGIVTNRD--LRFE----TDLSQPVSEVMTKeNLVTAPEGTTLEEAKEI 165

                          90       100
                  ....*....|....*....|
gi 2044790120 317 MHDGKFLHLPVVDRDGQVVA 336
Cdd:pfam00478 166 LHKHKIEKLPVVDDNGRLVG 185

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: 50.49 E-value: 9.19e-08

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044790120  68 TIPDGTTVADACRRMATRRVDAALLTDASALLCGIITDKDVatRVIaegfKPEETSVSKVMTRNPIFV---MGDTLAvDA 144
Cdd:cd04601     6 TLSPDATVADVLELKAEYGISGVPVTEDGGKLVGIVTSRDI--RFE----TDLSTPVSEVMTPDERLVtapEGITLE-EA 78

                          90       100       110
                  ....*....|....*....|....*....|..
gi 2044790120 145 LQKMVQGKFRHLPVV-ENGEVVALL---DITK 172
Cdd:cd04601    79 KEILHKHKIEKLPIVdDNGELVGLItrkDIEK 110

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: 48.36 E-value: 1.33e-07

                          10        20        30        40
                  ....*....|....*....|....*....|....*....|...
gi 2044790120 293 VEKVMTPNPECASLDTTIVDALHTMHDGKFLHLPVVDRDGQVV 335
Cdd:pfam00571   1 VKDIMTKDVVTVSPDTTLEEALELMREHGISRLPVVDEDGKLV 43

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: 49.49 E-value: 2.33e-07

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044790120  64 SKALTIPDGTTVADACRRMATRRVDAALLTD-ASALLCGIITdKDVATRVIAEGFkpEETSVSKVMTRNPIFVMGDTLAV 142
Cdd:cd17772     2 SPVISVEPDTTIAEAAELMTRYNINALPVVDgGTGRLVGIIT-RQVAEKAIYHGL--GDLPVSEYMTTEFATVTPDAPLS 78

                          90       100
                  ....*....|....*....|...
gi 2044790120 143 DALQKMVQGKFRHLPVVENGEVV 165
Cdd:cd17772    79 EIQEIIVEQRQRLVPVVEDGRLV 101

Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with the DRTGG domain; This cd contains two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with a DRTGG domain upstream. The function of the DRTGG domain, named after its conserved residues, is unknown. 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: 341371 [Multi-domain] Cd Length: 108 Bit Score: 49.01 E-value: 3.01e-07

                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2044790120  99 LCGIITDKDVATrviaegfKPEETSVSKVMTRNPIFVMGDTLAVDALQKMVQGKFRHLPVVENG 162
Cdd:cd04596    37 VVGIVTAKDVIG-------KEDDTPIEKVMTKNPITVKPKTSVASAAHMMIWEGIELLPVVDEN 93

Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains present in archaea, repeat 2; This cd contains two tandem repeats of the cystathionine beta-synthase (CBS pair) domains found in Inosine monophosphate (IMP) dehydrogenases and related proteins including IMP dehydrogenase IX from Methanothermobacter. IMP dehydrogenase is an essential enzyme in the de novo biosynthesis of Guanosine monophosphate (GMP), catalyzing the NAD-dependent oxidation of IMP to xanthosine monophosphate (XMP). 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: 341386 [Multi-domain] Cd Length: 150 Bit Score: 49.97 E-value: 3.21e-07

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044790120  71 DGTTVADACRRMATRRVDAALLTDASALLCGIITDKDV--ATRV----------IA--------EGFK------------ 118
Cdd:cd04614    11 DETPLPVALRAMRLANVPAAPVLDSEGKLVGIVTERDLidVSRIveseeesgmsIAddedewswEGIRdvmslyyptsnv 90

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 2044790120 119 --PEETsVSKVMTRNPIFVMGDTLAVDALQKMVQGKFRHLPVVE-NGEVVALL 168
Cdd:cd04614    91 elPDKP-VKDVMTKDVVTAFPSSTVSEAAKKMIRNDIEQLPVVSgEGDLAGML 142

Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains present in 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: 341412 [Multi-domain] Cd Length: 115 Bit Score: 48.94 E-value: 3.58e-07

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044790120  68 TIPDGTTVADACRRMATRRVDAALLTDaSALLCGIITDKDvATRVIAEGFKP-EETSVSKVMTRNPIFVMGDTLAVDALQ 146
Cdd:cd17776     7 TVDADASLEDAAERMLRNRVGSVVVTD-DGTPAGILTETD-ALHAGYATDDPfSEIPVRAVASRPLVTISPTATLREAAE 84

                          90       100
                  ....*....|....*....|....*....
gi 2044790120 147 KMVQGKFRHLPVVENGEVVALLDITKCLY 175
Cdd:cd17776    85 RMVDEGVKKLPVVDGLDLVGILTATDIIR 113

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: 49.34 E-value: 4.15e-07

                          10        20        30        40
                  ....*....|....*....|....*....|....*....|...
gi 2044790120 293 VEKVMTPNPECASLDTTIVDALHTMHDGKFLHLPVVDrDGQVV 335
Cdd:cd04584     2 VKDIMTKNVVTVTPDTSLAEARELMKEHKIRHLPVVD-DGKLV 43

CBS domain [Signal transduction mechanisms];

Pssm-ID: 440283 [Multi-domain] Cd Length: 128 Bit Score: 48.71 E-value: 5.70e-07

                          10        20        30        40
                  ....*....|....*....|....*....|....*....|...
gi 2044790120 293 VEKVMTPNPECASLDTTIVDALHTMHDGKFLHLPVVDRDGQVV 335
Cdd:COG0517     3 VKDIMTTDVVTVSPDATVREALELMSEKRIGGLPVVDEDGKLV 45

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: 6.07e-07

                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 2044790120 124 VSKVMTRNPIFVMGDTLAVDALQKMVQGKFRHLPVV-ENGEVVALL---DITKCLYD 176
Cdd:pfam00571   1 VKDIMTKDVVTVSPDTTLEEALELMREHGISRLPVVdEDGKLVGIVtlkDLLRALLG 57

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: 47.49 E-value: 8.85e-07

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044790120  68 TIPDGTTVADACRRMatrrvdaaLLTDASAL-------LCGIITDKDVaTRVIAEGFKPEEtsVSKVMTRNPIFVMGDTL 140
Cdd:cd04595     6 TVSPDTTIEEARKIM--------LRYGHTGLpvvedgkLVGIISRRDV-DKAKHHGLGHAP--VKGYMSTNVITIDPDTS 74

                          90       100
                  ....*....|....*....|....*
gi 2044790120 141 AVDALQKMVQGKFRHLPVVENGEVV 165
Cdd:cd04595    75 LEEAQELMVEHDIGRLPVVEEGKLV 99

Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains present in archaea, repeat 2; 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: 341395 [Multi-domain] Cd Length: 127 Bit Score: 47.71 E-value: 1.25e-06

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044790120 234 AKVATVGLSDTVYTATKKMRDLRVNS-VVITTNNKPQGILTSKDVLMRVVAVGLPPDT------------TPVEKVMTPN 300
Cdd:cd04632     2 EEVITVNEDDTIGKAINLLREHGISRlPVVDDNGKLVGIVTTYDIVDFVVRPGTKTRGgdrggekermldLPVYDIMSSP 81

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 2044790120 301 PECASLDTTIVDALHTMHDGKFLHLPVVDRDGQVVACV---DVL 341
Cdd:cd04632    82 VVTVTRDATVADAVERMLENDISGLVVTPDDNMVIGILtktDVL 125

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: 47.34 E-value: 1.36e-06

                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2044790120  99 LCGIITDKDVATrviaegfKPEETSVSKVMTRNPIFVMGDTLAVDALQKMVQGKFRHLPVVENGEVVALLDIT 171
Cdd:cd04638    39 LVGIVTRKDLLR-------NPDEEQIALLMSRDPITISPDDTLSEAAELMLEHNIRRVPVVDDDKLVGIVTVA 104

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: 46.98 E-value: 2.27e-06

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044790120  64 SKALTIPDGTTVADACRRMATRRVDAALLTDASALLCGIITDKDV---ATRVIAEGFKPEETSVSKVMTRN------PIF 134
Cdd:cd04592     3 TRYITVLMSTTLKEAVLLMLEEKQSCALIVDSDDFLIGILTLGDIqrfLKRAKADNEDPKTILVSSICTRNggycrgLWT 82

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 2044790120 135 VMGDTLAVDALQKMVQGKFRHLPVVENGE------VVALLDitkclYDAI 178
Cdd:cd04592    83 CTPDMDLLTAKMLMEARGINQLPVVKRGGeerrrrVVGLLD-----RDSI 127

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: 46.18 E-value: 3.03e-06

                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2044790120  99 LCGIITDKDVAtrviaegFKPEETSVSKVMTRNPIFVMGDTLAVDALQKMVQGKFRHLPVVENGEVVALldITK-CLY 175
Cdd:cd04599    37 LVGIITSRDVR-------RAHPNRLVADAMSRNVVTISPEASLWEAKELMEEHGIERLVVVEEGRLVGI--ITKsTLY 105

Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains found in diguanylate cyclase/phosphodiesterase proteins with PAS sensors, repeat 2; This cd contains two tandem repeats of the cystathionine beta-synthase (CBS pair) domains found in diguanylate cyclase/phosphodiesterase proteins with PAS sensors. PAS domains have been found to bind ligands, and to act as sensors for light and oxygen in signal transduction. 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: 341384 [Multi-domain] Cd Length: 131 Bit Score: 46.56 E-value: 3.20e-06

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044790120  67 LTIPDGTTVADACRRMATRRVDAALLTDASALLcGIITDKDVaTRVIAEgfKPEETSVSKVMTRNPIFVMGDTLAVDALQ 146
Cdd:cd04611    16 LVLPGDASLAEAARRMRSHRADAAVIECPDGGL-GILTERDL-VRFIAR--HPGNTPVGELASRPLLTVGAEDSLIHARD 91

                          90       100
                  ....*....|....*....|...
gi 2044790120 147 KMVQGKFRHLPVV-ENGEVVALL 168
Cdd:cd04611    92 LLIDHRIRHLAVVdEDGQVTGLL 114

inosine-5'-monophosphate dehydrogenase; Provisional

Pssm-ID: 240355 [Multi-domain] Cd Length: 495 Bit Score: 49.58 E-value: 3.63e-06

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044790120 238 TVGLSDTVYTATKKMRDLRVNSVVITTNNKPQ----GILTSKDVLMrvvavgLPPDTTPVEKVMTP--NPECASLDTTIV 311
Cdd:PTZ00314  108 VLSPNHTVADVLEIKEKKGFSSILITVDGKVGgkllGIVTSRDIDF------VKDKSTPVSEVMTPreKLVVGNTPISLE 181

                          90       100
                  ....*....|....*....|....*..
gi 2044790120 312 DALHTMHDGKFLHLPVVDRDGQVVACV 338
Cdd:PTZ00314  182 EANEVLRESRKGKLPIVNDNGELVALV 208

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: 45.89 E-value: 3.98e-06

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044790120 261 VITTNNKPQGILTSKDVLmRVVAVG----LPPDTtpVEKVMTPNPECASLDTTIVDALHTMHDGKFLHLPVVDrDGQVVA 336
Cdd:cd04629    31 VVDEQGRLVGFLSEQDCL-KALLEAsyhcEPGGT--VADYMSTEVLTVSPDTSIVDLAQLFLKNKPRRYPVVE-DGKLVG 106


                  ....*....
gi 2044790120 337 CV---DVLQ 342
Cdd:cd04629   107 QIsrrDVLR 115

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: 45.40 E-value: 6.13e-06

                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2044790120 261 VITTNNKPQGILTSKDVLMRvvavglpPDTTPVEKVMTPNPECASLDTTIVDALHTMHDGKFLHLPVVDRDGQVV 335
Cdd:cd04606    42 VVDEDRRLLGVVSLRDLLLA-------DPDTKVSDIMDTDVISVSADDDQEEVARLFAKYDLLALPVVDEEGRLV 109

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: 45.68 E-value: 6.45e-06

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044790120 123 SVSKVMTRNPIFVMGDTLAVDALQKMVQGKFRHLPVVENGEVVALL---DITKCLYDaiarmeraaekGNAIAAAVEGve 199
Cdd:cd04631     1 VVEDYMTKNVITATPGTPIEDVAKIMVRNGFRRLPVVSDGKLVGIVtstDIMRYLGS-----------GEAFEKLKTG-- 67

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044790120 200 rqwgnNANAAPSNFIETLRERMFRPTlgsllsegakVATVGLSDtvytATKKMRDLRVNSVVITTNNKPQGILTSKDVLM 279
Cdd:cd04631    68 -----NIHEVLNVPISSIMKRDIITT----------TPDTDLGE----AAELMLEKNIGALPVVDDGKLVGIITERDILR 128

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: 45.31 E-value: 6.58e-06

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044790120  57 TVKRLRLSKALTIPDGTTVADACRRMATRRVDAALLTDASALLCGIITDKDVAtRVIAEGFKpeetSVSKVMTRNPIFVM 136
Cdd:cd04605     1 LVEDIMSKDVATIREDISIEEAAKIMIDKNVTHLPVVSEDGKLIGIVTSWDIS-KAVALKKD----SLEEIMTRNVITAR 75

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 2044790120 137 GDTLAVDALQKMVQGKFRHLPVV-ENGEVVALL---DITK 172
Cdd:cd04605    76 PDEPIELAARKMEKHNISALPVVdDDRRVIGIItsdDISR 115

Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains found in diguanylate cyclase/phosphodiesterase proteins with PAS sensors, repeat 1; This cd contains two tandem repeats of the cystathionine beta-synthase (CBS pair) domains found in diguanylate cyclase/phosphodiesterase proteins with PAS sensors. PAS domains have been found to bind ligands, and to act as sensors for light and oxygen in signal transduction. 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: 341403 [Multi-domain] Cd Length: 116 Bit Score: 44.91 E-value: 1.02e-05

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044790120  70 PDgTTVADACRRMATRRVDAALLTDASALLcGIITDKDvatrVIAEGFKPEE---TSVSKVMTRNPIFVMGDTLAVDALQ 146
Cdd:cd09833    12 PD-TPLADAAARMAERRCSSILIVENGEIV-GIWTERD----ALKLDFSDPDafrRPISEVMSSPVLTIPQDTTLGEAAV 85

                          90       100
                  ....*....|....*....|....*...
gi 2044790120 147 KMVQGKFRHLPVVENGE----VVALLDI 170
Cdd:cd09833    86 RFRQEGVRHLLVVDDDGrpvgIVSQTDV 113

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: 44.05 E-value: 1.75e-05

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044790120 235 KVATVGLSDTVYTATKKMRDLRVNSVVIT-TNNKPQGILTSKDV--LMRvvavglppDTTPVEKVMTPNPECASLDTTIV 311
Cdd:cd04583     3 NPVTITPERTLAQAIEIMREKRVDSLLVVdKDNVLLGIVDIEDInrNYR--------KAKKVGEIMERDVFTVKEDSLLR 74

                          90       100
                  ....*....|....*....|....
gi 2044790120 312 DALHTMHDGKFLHLPVVDRDGQVV 335
Cdd:cd04583    75 DTVDRILKRGLKYVPVVDEQGRLV 98

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: 47.38 E-value: 1.94e-05

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044790120  56 RTVKRlrlSKALTIPD------GTTVADACRRMATRRVDAALLTDaSALLCGIITDKDVatRVIaegfKPEETSVSKVMT 129
Cdd:pfam00478  77 RKVKR---SESGMITDpvtlspDATVADALALMERYGISGVPVVD-DGKLVGIVTNRDL--RFE----TDLSQPVSEVMT 146

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 2044790120 130 R-NPIFVMGDTLAVDALQKMVQGKFRHLPVV-ENGEVVALL---DITK 172
Cdd:pfam00478 147 KeNLVTAPEGTTLEEAKEILHKHKIEKLPVVdDNGRLVGLItikDIEK 194

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: 43.77 E-value: 2.34e-05

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044790120 235 KVATVGLSDTVYTATKKMRDLRVNSV-VITTNNKPQGILTSKDVlMRVVAVglppDTTPVEKVMTPNPECASLDTTIVDA 313
Cdd:cd04605     9 DVATIREDISIEEAAKIMIDKNVTHLpVVSEDGKLIGIVTSWDI-SKAVAL----KKDSLEEIMTRNVITARPDEPIELA 83

                          90       100
                  ....*....|....*....|....*
gi 2044790120 314 LHTMHDGKFLHLPVVDRDGQVVACV 338
Cdd:cd04605    84 ARKMEKHNISALPVVDDDRRVIGII 108

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: 41.04 E-value: 4.84e-05

                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 2044790120  58 VKRLRLSKALTIPDGTTVADACRRMATRRVDAALLTDASALLCGIITDKDVATRVI 113
Cdd:pfam00571   1 VKDIMTKDVVTVSPDTTLEEALELMREHGISRLPVVDEDGKLVGIVTLKDLLRALL 56

Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with the voltage gated CLC (chloride channel) in 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 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: 341385 [Multi-domain] Cd Length: 119 Bit Score: 42.95 E-value: 5.42e-05

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044790120  65 KALTIPDGTTVADACRRMATRRVDAALLTDASALLCGIITDKDVATRVIAEGFKpEETSVSKVMTRNPIFVMG-DTLAvD 143
Cdd:cd04613     4 KVTVLPEGMTFRQFTEFIAGTRQHYFPVVDEQGRLTGILSIQDVRGVLFEEELW-DLVVVKDLATTDVITVTPdDDLY-T 81

                          90       100
                  ....*....|....*....|....*...
gi 2044790120 144 ALQKMVQGKFRHLPVVE---NGEVVALL 168
Cdd:cd04613    82 ALLKFTSTNLDQLPVVDdddPGKVLGML 109

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: 42.60 E-value: 7.81e-05

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044790120  68 TIPDGTTVADACRRMAT---RRVdaALLTDAsaLLCGIITDKD-------------VATRVIAEGFKpeeTSVSKVMTRN 131
Cdd:cd04631    12 TATPGTPIEDVAKIMVRngfRRL--PVVSDG--KLVGIVTSTDimrylgsgeafekLKTGNIHEVLN---VPISSIMKRD 84

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 2044790120 132 PIFVMGDTLAVDALQKMVQGKFRHLPVVENGEVVALL---DITKCL 174
Cdd:cd04631    85 IITTTPDTDLGEAAELMLEKNIGALPVVDDGKLVGIIterDILRAI 130

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: 341365 [Multi-domain] Cd Length: 113 Bit Score: 41.79 E-value: 1.12e-04

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044790120 242 SDTVYTATKKMRDLRVNSVVITTNNKPQGILTSKDVLMRVVAVGLPPDtTPVEKVMTPNPECASLDTTIVDALHTM--HD 319
Cdd:cd04589    11 ETSIREATRLMKENGADSLLVRDGDGRVGIVTRTDLRDAVVLDGQPVD-TPVGEIATFPLISVEPDDFLFNALLLMtrHR 89

                          90       100
                  ....*....|....*....|....
gi 2044790120 320 GKFLhlpVVDRDGQVVACVDVLQL 343
Cdd:cd04589    90 VKRV---VVREGEEIVGVLEQTDL 110

Signal-transduction protein containing cAMP-binding, CBS, and nucleotidyltransferase domains [Signal transduction mechanisms];

Pssm-ID: 442149 [Multi-domain] Cd Length: 124 Bit Score: 41.74 E-value: 1.48e-04

                          10        20        30        40
                  ....*....|....*....|....*....|....*....|...
gi 2044790120 293 VEKVMTPNPECASLDTTIVDALHTMHDGKFLHLPVVDRDGQVV 335
Cdd:COG2905     1 VKDIMSRDVVTVSPDATVREAARLMTEKGVGSLVVVDDDGRLV 43

Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains present in Thermoplasmatales; 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: 341422 [Multi-domain] Cd Length: 114 Bit Score: 41.37 E-value: 1.62e-04

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044790120 238 TVGLSDTVYTATKKMRDLRVNSVVITT-NNKPQGILTSKDVLMRVVAVGLPPDTTPVEKVM-TPNPECASlDTTIVDALH 315
Cdd:cd17786     6 TINWNATVFDAVKIMNENHLYGLVVKDdDGNYVGLISERSIIKRFIPRNVKPDEVPVKLVMrKPIPKVKS-DYDVKDVAA 84

                          90       100
                  ....*....|....*....|....*....
gi 2044790120 316 TMHDGKFLHLPVVDRDGQVVACVDVLQLT 344
Cdd:cd17786    85 FLSENGLERCAVVDDNGRVVGIVTITDLS 113

Mg/Co/Ni transporter MgtE (contains CBS domain) [Inorganic ion transport and metabolism];

Pssm-ID: 441840 [Multi-domain] Cd Length: 443 Bit Score: 43.52 E-value: 2.90e-04

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044790120 244 TVYTATKKMRDL-----RVNSV-VITTNNKPQGILTSKDVLmrvvavgLPPDTTPVEKVMTPNPECASLDTTIVDALHTM 317
Cdd:COG2239   147 TVGEALRYLRRQaedpeTIYYIyVVDDDGRLVGVVSLRDLL-------LADPDTKVSDIMDTDVISVPADDDQEEVARLF 219

                          90
                  ....*....|....*...
gi 2044790120 318 HDGKFLHLPVVDRDGQVV 335
Cdd:COG2239   220 ERYDLLALPVVDEEGRLV 237

CBS domain [Signal transduction mechanisms];

Pssm-ID: 440283 [Multi-domain] Cd Length: 128 Bit Score: 41.00 E-value: 3.12e-04

                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2044790120  51 TSPGERTVKRLRLSKALTIPDGTTVADACRRMATRRVDAALLTDASALLCGIITDKDVATRVIAE 115
Cdd:COG0517    62 KDLLDTPVSEVMTRPPVTVSPDTSLEEAAELMEEHKIRRLPVVDDDGRLVGIITIKDLLKALLEP 126

Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains present in Thermoplasmatales; 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: 341422 [Multi-domain] Cd Length: 114 Bit Score: 40.59 E-value: 3.38e-04

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044790120  68 TIPDGTTVADACRRMATRRVDAALLTDASALLCGIITDKDVATRVIAEGFKPEETSVSKVMtRNPI-FVMGDTLAVDALQ 146
Cdd:cd17786     6 TINWNATVFDAVKIMNENHLYGLVVKDDDGNYVGLISERSIIKRFIPRNVKPDEVPVKLVM-RKPIpKVKSDYDVKDVAA 84

                          90       100
                  ....*....|....*....|....*.
gi 2044790120 147 KMVQGKFRHLPVVE-NGEVVALLDIT 171
Cdd:cd17786    85 FLSENGLERCAVVDdNGRVVGIVTIT 110

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: 40.21 E-value: 3.42e-04

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044790120 238 TVGLSDTVYTATKKMRDLRVNSVVITTNNKPQGILTSKDVlMRVVAVGLPpdTTPVEKVMTPNPECASLDTTIVDALHTM 317
Cdd:cd04588     6 TLKPDATIKDAAKLLSENNIHGAPVVDDGKLVGIVTLTDI-AKALAEGKE--NAKVKDIMTKDVITIDKDEKIYDAIRLM 82

                          90       100
                  ....*....|....*....|....*....
gi 2044790120 318 HDGKFLHLPVVDRDGQVVACV---DVLQL 343
Cdd:cd04588    83 NKHNIGRLIVVDDNGKPVGIItrtDILKV 111

Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains found in diguanylate cyclase/phosphodiesterase proteins with PAS sensors, repeat 2; This cd contains two tandem repeats of the cystathionine beta-synthase (CBS pair) domains found in diguanylate cyclase/phosphodiesterase proteins with PAS sensors. PAS domains have been found to bind ligands, and to act as sensors for light and oxygen in signal transduction. 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: 341384 [Multi-domain] Cd Length: 131 Bit Score: 40.78 E-value: 3.57e-04

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044790120 248 ATKKMRDLRVNSVVITTNNKPQGILTSKDVLmRVVAvGLPPDtTPVEKVMTPNPECASLDTTIVDALHTMHDGKFLHLPV 327
Cdd:cd04611    27 AARRMRSHRADAAVIECPDGGLGILTERDLV-RFIA-RHPGN-TPVGELASRPLLTVGAEDSLIHARDLLIDHRIRHLAV 103

                          90       100
                  ....*....|....*....|
gi 2044790120 328 VDRDGQVVACVDVLQLTHGA 347
Cdd:cd04611   104 VDEDGQVTGLLGFADLLAGV 123

arabinose-5-phosphate isomerase KdsD;

Pssm-ID: 182814 [Multi-domain] Cd Length: 326 Bit Score: 42.79 E-value: 3.65e-04

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044790120  43 PGGA-GRPLTspgertvkrLRLSKALTIPD-------GTTVADACRRMATRRVDAALLTDASALLCGIITDKDVaTRVIA 114
Cdd:PRK10892  192 PGGAlGRKLL---------LRVSDIMHTGDeiphvskTASLRDALLEITRKNLGMTVICDDNMKIEGIFTDGDL-RRVFD 261

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 2044790120 115 EGFKPEETSVSKVMTRNPIFVMGDTLAVDALQKMVQGKFRHLPVVENGEVVALL 168
Cdd:PRK10892  262 MGIDLRQASIADVMTPGGIRVRPGILAVDALNLMQSRHITSVLVADGDHLLGVL 315

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: 38.26 E-value: 3.89e-04

                           10        20        30        40
                   ....*....|....*....|....*....|....*....|.
gi 2044790120   68 TIPDGTTVADACRRMATRRVDAALLTDASALLCGIITDKDV 108
Cdd:smart00116   4 TVSPDTTLEEALELLRENGIRRLPVVDEEGRLVGIVTRRDI 44

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: 40.62 E-value: 4.17e-04

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044790120 236 VATVGLSDTVYTATKKMRDLRVNSV-VITTNNKPQGILTSKDVL--------------MRVVAVGLPPDTTPVEKVMTPN 300
Cdd:cd04600     5 VVTVTPDTSLEEAWRLLRRHRIKALpVVDRARRLVGIVTLADLLkhadldpprglrgrLRRTLGLRRDRPETVGDIMTRP 84

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 2044790120 301 PECASLDTTIVDALHTMHDGKFLHLPVVDRDGQVV 335
Cdd:cd04600    85 VVTVRPDTPIAELVPLFSDGGLHHIPVVDADGRLV 119

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: 38.35 E-value: 4.25e-04

                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 2044790120 235 KVATVGLSDTVYTATKKMRDLRVNSV-VITTNNKPQGILTSKDVLMRVV 282
Cdd:pfam00571   8 DVVTVSPDTTLEEALELMREHGISRLpVVDEDGKLVGIVTLKDLLRALL 56

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: 39.91 E-value: 4.61e-04

                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*.
gi 2044790120 293 VEKVMTPNPECASLDTTIVDALHTMHDGKFLHLPVVDRDGQVVACV 338
Cdd:cd04605     2 VEDIMSKDVATIREDISIEEAAKIMIDKNVTHLPVVSEDGKLIGIV 47

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: 39.61 E-value: 5.51e-04

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044790120  68 TIPDGTTVADACRRMATRRVDAALLTDASALLcGIITDKDVATrviaegfKPEETSVSKVMTRNPIFVMGDTLAVDALQK 147
Cdd:cd04610     7 TVSPDDTVKDVIKLIKETGHDGFPVVDDGKVV-GYVTAKDLLG-------KDDDEKVSEIMSRDTVVADPDMDITDAARV 78

                          90       100
                  ....*....|....*....|..
gi 2044790120 148 MVQGKFRHLPVV-ENGEVVALL 168
Cdd:cd04610    79 IFRSGISKLPVVdDEGNLVGII 100

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: 39.64 E-value: 5.72e-04

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044790120 235 KVATVGLSDTVYTATKKMRDLRVNSV-VITTNNKPQGILTSKDVlmrvvavglppdTTPVEKVMTP-NPECASLDTTIVD 312
Cdd:cd04597     6 KVEPLSPETSIKDAWNLMDENNLKTLpVTDDNGKLIGLLSISDI------------ARTVDYIMTKdNLIVFKEDDYLDE 73

                          90       100
                  ....*....|....*....|...
gi 2044790120 313 ALHTMHDGKFLHLPVVDRDGQVV 335
Cdd:cd04597    74 VKEIMLNTNFRNYPVVDENNKFL 96

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: 40.01 E-value: 5.74e-04

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044790120 234 AKVATVGLSDTVYTATKKMRDLRVNSVVITTNNKPQGILTSKDVLMRV-------VAVGLPPDT---TPVEKVMTPNPEC 303
Cdd:cd17778     8 TPVVTIYPDDTLKEAMELMVTRGFRRLPVVSGGKLVGIVTAMDIVKYFgsheakkRLTTGDIDEaysTPVEEIMSKEVVT 87

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 2044790120 304 ASLDTTIVDALHTMHDGKFLHLPVVDRDGQVVACV---DVL 341
Cdd:cd17778    88 IEPDADIAEAARLMIKKNVGSLLVVDDEGELKGIIterDVL 128

Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains present in archaea, repeat 2; This cd contains two tandem repeats of the cystathionine beta-synthase (CBS pair) domains found in Inosine monophosphate (IMP) dehydrogenases and related proteins including IMP dehydrogenase IX from Methanothermobacter. IMP dehydrogenase is an essential enzyme in the de novo biosynthesis of Guanosine monophosphate (GMP), catalyzing the NAD-dependent oxidation of IMP to xanthosine monophosphate (XMP). 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: 341386 [Multi-domain] Cd Length: 150 Bit Score: 40.73 E-value: 5.77e-04

                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 2044790120 288 PDTtPVEKVMTPNPECASLDTTIVDALHTMHDGKFLHLPVVDRDGQ---VVACVDVL 341
Cdd:cd04614    93 PDK-PVKDVMTKDVVTAFPSSTVSEAAKKMIRNDIEQLPVVSGEGDlagMLRDVDLL 148

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: 341421 [Multi-domain] Cd Length: 136 Bit Score: 39.95 E-value: 6.85e-04

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044790120 235 KVATVGLSDTVYTATKKM-RDLRVNSV-VITTNNKPQGILTSKDvLMRVVAVGLPPDT---------------TPVEKVM 297
Cdd:cd17785    11 KPSVVHENTSIRDVIDKMiEDPKTRSVyVVDDDEKLLGIITLME-LLKYIGYRFGVTIykgvsfglllrislkEKAKDIM 89

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 2044790120 298 TPnPECASLDTTIVDALHTMHDGKFLHLPVVDRDGQVVACVDVLQL 343
Cdd:cd17785    90 LS-PIYVKKEDTLEEALELMVKNRLQELPVVDENGKVIGDLNSLEL 134

Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains from plant CBSX proteins; This cd contains two tandem repeats of the cystathionine beta-synthase (CBS pair) domains of plant single cystathionine beta-synthase (CBS) pair proteins (CBSX). CBSX1 and CBSX2 have been identified as redox regulators of the thioredoxin (Trx) system. 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: 341425 [Multi-domain] Cd Length: 141 Bit Score: 40.15 E-value: 7.84e-04

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044790120  73 TTVADACRRMATRRVDAALLTDASALLCGIITDKDV-------ATRVIAEGFKPEETS------------------VSKV 127
Cdd:cd17789    12 TTVDEALELLVENRITGLPVIDEDWRLVGVVSDYDLlaldsisGRSQTDNNFPPADSTwktfnevqkllsktngkvVGDV 91

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 2044790120 128 MTRNPIFVMGDTLAVDALQKMVQGKFRHLPVVE-NGEVVALL 168
Cdd:cd17789    92 MTPSPLVVREKTNLEDAARILLETKFRRLPVVDsDGKLVGII 133

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: 39.54 E-value: 8.03e-04

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044790120 243 DTVYTATKKMRDLRVNSV-VITTNNKPQGILTSKDVLMRVVAVGLPPDTTPVEKVMTPNPECASLDTTiVDALHTMHDGK 321
Cdd:cd17773    15 DSILNALQKISDNKSRIVfCVDEHGVLEGVLTDGDFRRWLLENPNADLSQPVSHVANTNFVSAPEGES-PEKIEALFSSR 93

                          90
                  ....*....|....*
gi 2044790120 322 FLHLPVVDRDGQVVA 336
Cdd:cd17773    94 ISYIPLVDERGRLVA 108

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: 39.34 E-value: 8.85e-04

                          10        20        30
                  ....*....|....*....|....*....|....*....
gi 2044790120 297 MTPNPECASLDTTIVDALHTMHDGKFLHLPVVDRDGQVV 335
Cdd:cd04629     1 MTRNPVTLTPDTSILEAVELLLEHKISGAPVVDEQGRLV 39

Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains from plant CBSX proteins; This cd contains two tandem repeats of the cystathionine beta-synthase (CBS pair) domains of plant single cystathionine beta-synthase (CBS) pair proteins (CBSX). CBSX1 and CBSX2 have been identified as redox regulators of the thioredoxin (Trx) system. 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: 341425 [Multi-domain] Cd Length: 141 Bit Score: 39.38 E-value: 1.15e-03

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044790120 242 SDTVYTATKKMRDLRVNSV-VITTNNKPQGILTSKDVL--------MRVVAVGLPPDTT-----PVEK------------ 295
Cdd:cd17789    11 NTTVDEALELLVENRITGLpVIDEDWRLVGVVSDYDLLaldsisgrSQTDNNFPPADSTwktfnEVQKllsktngkvvgd 90

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 2044790120 296 VMTPNPECASLDTTIVDALHTMHDGKFLHLPVVDRDGQVV 335
Cdd:cd17789    91 VMTPSPLVVREKTNLEDAARILLETKFRRLPVVDSDGKLV 130

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: 38.86 E-value: 1.16e-03

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044790120 235 KVATVGLSDTVYTATKKMRDLRVNSVVITTNNKPQGILTSKDVlmrvvaVGLPPDTTpVEKVMTPNPECASLDTTIVDAL 314
Cdd:cd04599     4 NPITISPLDSVARAAALMERQRIGGLPVVENGKLVGIITSRDV------RRAHPNRL-VADAMSRNVVTISPEASLWEAK 76

                          90
                  ....*....|....*..
gi 2044790120 315 HTMHDGKFLHLPVVDRD 331
Cdd:cd04599    77 ELMEEHGIERLVVVEEG 93

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: 38.76 E-value: 1.31e-03

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044790120 124 VSKVMTRNPIFVMGDTLAVDALQKMVQGKFRHLPVV-ENGEVVALL---DITKclydAIArmeraaekgnaiaaavegve 199
Cdd:cd04605     2 VEDIMSKDVATIREDISIEEAAKIMIDKNVTHLPVVsEDGKLIGIVtswDISK----AVA-------------------- 57

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2044790120 200 rqwgnnanaapsNFIETLRERMFRptlgsllsegaKVATVGLSDTVYTATKKMRDLRVNSV-VITTNNKPQGILTSKDV 277
Cdd:cd04605    58 ------------LKKDSLEEIMTR-----------NVITARPDEPIELAARKMEKHNISALpVVDDDRRVIGIITSDDI 113

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: 39.08 E-value: 1.61e-03

                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2044790120  61 LRLSKALTIPDGTTVADACRRMATRRVDAALLTDASALLCGIITDKDVA-----TRVIAEGFKPEETSVSKVMT 129
Cdd:cd04640     2 FRRVPPVTIDPDVSADEALEKMIRRGVRLLLVVDANNRVIGLITARDILgekplKIVQERGIPREELLVADVMT 75

inosine-5'-monophosphate dehydrogenase; Provisional

Pssm-ID: 240355 [Multi-domain] Cd Length: 495 Bit Score: 41.11 E-value: 1.72e-03

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044790120  56 RTVKRLR---LSKALTIPDGTTVADACRRMATRRVDAALLTD---ASALLCGIITDKDVATRviaegfKPEETSVSKVMT 129
Cdd:PTZ00314   93 RKVKRFEngfIMDPYVLSPNHTVADVLEIKEKKGFSSILITVdgkVGGKLLGIVTSRDIDFV------KDKSTPVSEVMT 166

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 2044790120 130 RNPIFVMGD---TLAvDALQKMVQGKFRHLPVV-ENGEVVAL 167
Cdd:PTZ00314  167 PREKLVVGNtpiSLE-EANEVLRESRKGKLPIVnDNGELVAL 207

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: 38.38 E-value: 1.96e-03

                          10        20        30
                  ....*....|....*....|....*....|....*...
gi 2044790120 298 TPNPECASLDTTIVDALHTMHDGKFLHLPVVDRDGQVV 335
Cdd:cd02205     1 TRDVVTVDPDTTVREALELMAENGIGALPVVDDDGKLV 38

CBS pair domain found in 5'-AMP (adenosine monophosphate)-activated protein kinase; The 5'-AMP (adenosine monophosphate)-activated protein kinase (AMPK) coordinates metabolic function with energy availability by responding to changes in intracellular ATP (adenosine triphosphate) and AMP concentrations. Most of the members of this cd contain two Bateman domains, each of which is composed of a tandem pair of cystathionine beta-synthase (CBS) motifs. 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: 341399 [Multi-domain] Cd Length: 124 Bit Score: 38.26 E-value: 2.04e-03

                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*..
gi 2044790120 300 NPECASLDTTIVDALHTMHDGKFLHLPVVDRDGQVV---ACVDVLQL 343
Cdd:cd04641     4 NIATASMDTPVIDALNLFVERRVSALPIVDEDGRVVdiyAKFDVINL 50

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: 38.17 E-value: 2.38e-03

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044790120 236 VATVGLSDTVYTATKKMRDLRVNSV-VITTNNKPQGILTSKDVLMRVVAVGLPPDTTpVEKVMTPNPECASLDTTIVDAL 314
Cdd:cd17784     4 VITAKPNEGVVEAFEKMLKHKISALpVVDDEGKLIGIVTATDLGHNLILDKYELGTT-VEEVMVKDVATVHPDETLLEAI 82

                          90       100
                  ....*....|....*....|....*.
gi 2044790120 315 HTMHD-----GKFLHLPVVDrDGQVV 335
Cdd:cd17784    83 KKMDSnapdeEIINQLPVVD-DGKLV 107

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: 38.37 E-value: 2.54e-03

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044790120 232 EGAKVATVGLSDTVYTATKKM--RDLRVNSVVITTNNKPQGILTSKDVL--------MRVVAVG-----LPPDTTPVEKV 296
Cdd:cd17779     6 ATKDVITIPPTTTIIGAIKTMteKGFRRLPVADAGTKRLEGIVTSMDIVdflgggskYNLVEKKhngnlLAAINEPVREI 85

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 2044790120 297 MTPNPECASLDTTIVDALHTMHDGKFLHLPVVDRDGQVVACV---DVLQL 343
Cdd:cd17779    86 MTRDVISVKENASIDDAIELMLEKNVGGLPIVDKDGKVIGIVterDFLKF 135

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: 341400 [Multi-domain] Cd Length: 130 Bit Score: 38.25 E-value: 2.56e-03

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044790120 228 SLLSEGAKVATVGLSDTVYTAT---KKMRDLRVNsvVITTNNKPQGILTSKDVLMRVVAVGL----PPDTTPVEKVMTPN 300
Cdd:cd04643     1 DFLIPAEKVAHVQDTNNLEHALlvlTKSGYSRIP--VLDKDYKLVGLISLSMILDAILGLERiefeKLSELKVEEVMNTD 78

                          90       100       110
                  ....*....|....*....|....*....|..
gi 2044790120 301 PECASLDTTIVDALHTMHDGKFlhLPVVDRDG 332
Cdd:cd04643    79 VPTVSPDDDLEEVLHLLVDHPF--LCVVDEDG 108

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: 38.31 E-value: 2.60e-03

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044790120  72 GTTVADACRRMATRRVDAALLTDASALLCGIITDKD---------------VATRVIAEGFKPEETsVSKVMTRNPIFVM 136
Cdd:cd04600    11 DTSLEEAWRLLRRHRIKALPVVDRARRLVGIVTLADllkhadldpprglrgRLRRTLGLRRDRPET-VGDIMTRPVVTVR 89

                          90       100       110
                  ....*....|....*....|....*....|
gi 2044790120 137 GDTLAVDALQKMVQGKFRHLPVVENGEVVA 166
Cdd:cd04600    90 PDTPIAELVPLFSDGGLHHIPVVDADGRLV 119

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: 35.95 E-value: 2.71e-03

                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*....
gi 2044790120  131 NPIFVMGDTLAVDALQKMVQGKFRHLPVV-ENGEVVALL---DITKCLY 175
Cdd:smart00116   1 DVVTVSPDTTLEEALELLRENGIRRLPVVdEEGRLVGIVtrrDIIKALA 49

IMP dehydrogenase;

Pssm-ID: 180842 [Multi-domain] Cd Length: 502 Bit Score: 40.45 E-value: 3.16e-03

                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2044790120 263 TTNNKPQGILTSKDvlMRVVAvgLPPDTtPVEKVMTPNPE--CASLDTTIVDALHTMHDGKFLHLPVVDRDGQVVACV 338
Cdd:PRK07107  138 TAHGKLLGIVTSRD--YRISR--MSLDT-KVKDFMTPFEKlvTANEGTTLKEANDIIWDHKLNTLPIVDKNGNLVYLV 210

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: 37.51 E-value: 3.52e-03

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044790120 230 LSEGAKVaTVGLSDTVYTATKKMRDLRVNSV-VITTNNKPQGILTSKDVLMRVVAvGLPPDTTPVEKVMTPNPECASLDT 308
Cdd:cd04608     7 LDLGAPV-TVLPDDTLGEAIEIMREYGVDQLpVVDEDGRVVGMVTEGNLLSSLLA-GRAQPSDPVSKAMYKQFKQVDLDT 84

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 2044790120 309 TIVDALHTMHDGKFlhLPVVDRDGQVVACV---DVL 341
Cdd:cd04608    85 PLGALSRILERDHF--ALVVDGQGKVLGIVtriDLL 118

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: 37.70 E-value: 3.62e-03

                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 2044790120  58 VKRLRLSKALTIPDGTTVADACRRMATRRVDAALLTDASALLCGIITDKDV 108
Cdd:cd17778    77 VEEIMSKEVVTIEPDADIAEAARLMIKKNVGSLLVVDDEGELKGIITERDV 127

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: 35.18 E-value: 4.71e-03

                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....
gi 2044790120  236 VATVGLSDTVYTATKKMRDLRVNSV-VITTNNKPQGILTSKDVL 278
Cdd:smart00116   2 VVTVSPDTTLEEALELLRENGIRRLpVVDEEGRLVGIVTRRDII 45

putative manganese-dependent inorganic diphosphatase;

Pssm-ID: 237843 [Multi-domain] Cd Length: 546 Bit Score: 39.81 E-value: 4.94e-03

                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 2044790120 293 VEKVMTPNPECASLDTTIVDALHTMHDGKFLHLPVVDRDGQVVACVDVLQLT 344
Cdd:PRK14869   70 VRDLEIDKPVTVSPDTSLKEAWNLMDENNVKTLPVVDEEGKLLGLVSLSDLA 121

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: 36.94 E-value: 4.96e-03

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044790120 236 VATVGLSDTVYTATKKMRDLRVNS--VVITTNNKPQGILTSKDVLMRvvavglpPDTTPVEKVMTPNPECASLDTTIVDA 313
Cdd:cd04638     5 VVTVTLPGTRDDVLEILKKKAISGvpVVKKETGKLVGIVTRKDLLRN-------PDEEQIALLMSRDPITISPDDTLSEA 77

                          90
                  ....*....|....*...
gi 2044790120 314 LHTMHDGKFLHLPVVDRD 331
Cdd:cd04638    78 AELMLEHNIRRVPVVDDD 95

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: 37.13 E-value: 5.81e-03

                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2044790120  57 TVKRLRLSKALTIPDGTTVADACRRMATRRVDAALLTDASALLCGIITDKDVATRVIAEGFKPEETsVSKVMTR 130
Cdd:cd04608     3 IVRRLDLGAPVTVLPDDTLGEAIEIMREYGVDQLPVVDEDGRVVGMVTEGNLLSSLLAGRAQPSDP-VSKAMYK 75

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: 37.21 E-value: 6.54e-03

                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*.
gi 2044790120 293 VEKVMTPNPECASLDTTIVDALHTMHDGKFLHLPVVdRDGQVVACV 338
Cdd:cd04631     2 VEDYMTKNVITATPGTPIEDVAKIMVRNGFRRLPVV-SDGKLVGIV 46

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: 341393 [Multi-domain] Cd Length: 120 Bit Score: 36.81 E-value: 6.61e-03

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044790120 235 KVATVGLSDTVYTATKKMRDLRVNSVVIttnNKPQ-----GILTSKDVLMRVVAVGLPPDTTPVEKVMT-P----NPEca 304
Cdd:cd04630     8 NVVTIDGLATVREALQLMKEHNVKSLIV---EKRHehdayGIVTYTDILKKVIAEDRDPDLVNVYEIMTkPaisvSPD-- 82

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 2044790120 305 sLDTTIVDALhtMHDGKFLHLPVVDrDGQVVACVDVLQLTH 345
Cdd:cd04630    83 -LDIKYAARL--MARFNLKRAPVIE-NNELIGIVSMTDLVL 119

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: 37.02 E-value: 7.55e-03

                          10        20        30
                  ....*....|....*....|....*....|....*....
gi 2044790120 297 MTPNPECASLDTTIVDALHTMHDGKFLHLPVVDRDGQVV 335
Cdd:cd04586     1 MTTDVVTVTPDTSVREAARLLLEHRISGLPVVDDDGKLV 39

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: 36.32 E-value: 8.10e-03

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044790120 236 VATVGLSDTVYTATKKMRDLRVNSVVITTNNKPQGILTSKDVlMRVVAVGLppDTTPVEKVMTPNPECASLDTTIVDALH 315
Cdd:cd04595     4 VKTVSPDTTIEEARKIMLRYGHTGLPVVEDGKLVGIISRRDV-DKAKHHGL--GHAPVKGYMSTNVITIDPDTSLEEAQE 80

                          90       100       110
                  ....*....|....*....|....*....|
gi 2044790120 316 TMHDGKFLHLPVVDrDGQVVACV---DVLQ 342
Cdd:cd04595    81 LMVEHDIGRLPVVE-EGKLVGIVtrsDVLR 109

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: 36.45 E-value: 8.20e-03

                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 2044790120  52 SPGERTVKRLRLSKALTIPDGTTVADACRRMATRRVDAALLTDASALLCGIITDKDV 108
Cdd:cd02205    55 LALDTPVAEVMTPDVITVSPDTDLEEALELMLEHGIRRLPVVDDDGKLVGIVTRRDI 111

Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains present in archaea, repeat 2; 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: 341395 [Multi-domain] Cd Length: 127 Bit Score: 36.54 E-value: 9.62e-03

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2044790120  68 TIPDGTTVADACRRMATRRVDAALLTDASALLCGIITDKDVATRVIAEGFKPEETSVSK------------VMTRNPIFV 135
Cdd:cd04632     6 TVNEDDTIGKAINLLREHGISRLPVVDDNGKLVGIVTTYDIVDFVVRPGTKTRGGDRGGekermldlpvydIMSSPVVTV 85

                          90       100       110
                  ....*....|....*....|....*....|.
gi 2044790120 136 MGDTLAVDALQKMVQGKFRHLPVVENGEVVA 166
Cdd:cd04632    86 TRDATVADAVERMLENDISGLVVTPDDNMVI 116