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).

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447143256  10 KREVLFCSSSITIGEALEHLNKTGYRCVPVLDEkKEKYLGNVYKVDIL----EYKGSLEESVVQLLNDKEGYVREDSSFF 85
Cdd:cd02205    1 TRDVVTVDPDTTVREALELMAENGIGALPVVDD-DGKLVGIVTERDILralvEGGLALDTPVAEVMTPDVITVSPDTDLE 79

                         90       100       110
                 ....*....|....*....|....*....|...
gi 447143256  86 KVFFTI--KKLPYLSVVDENGVFLGILTHKKVF 116
Cdd:cd02205   80 EALELMleHGIRRLPVVDDDGKLVGIVTRRDIL 112

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.

                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 447143256    8 VPKREVLFCSSSITIGEALEHLNKTGYRCVPVLDEkKEKYLGNVYKVDILEY 59
Cdd:pfam00571   4 IMTKDVVTVSPDTTLEEALELMREHGISRLPVVDE-DGKLVGIVTLKDLLRA 54

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).

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447143256  10 KREVLFCSSSITIGEALEHLNKTGYRCVPVLDEkKEKYLGNVYKVDIL----EYKGSLEESVVQLLNDKEGYVREDSSFF 85
Cdd:cd02205    1 TRDVVTVDPDTTVREALELMAENGIGALPVVDD-DGKLVGIVTERDILralvEGGLALDTPVAEVMTPDVITVSPDTDLE 79

                         90       100       110
                 ....*....|....*....|....*....|...
gi 447143256  86 KVFFTI--KKLPYLSVVDENGVFLGILTHKKVF 116
Cdd:cd02205   80 EALELMleHGIRRLPVVDDDGKLVGIVTRRDIL 112

Predicted transcriptional regulator containing CBS domains [Transcription];

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447143256   5 GNYVPKREVLFCSSSITIGEALEHLNKTGYRCVPVLDEKKeKYLGNVYKVDILEYkgSLEESVVQLLNDKEGYVREDSSF 84
Cdd:COG4109   19 EDIMTLEDVATLSEDDTVEDALELLEKTGHSRFPVVDENG-RLVGIVTSKDILGK--DDDTPIEDVMTKNPITVTPDTSL 95

                         90       100       110
                 ....*....|....*....|....*....|....*
gi 447143256  85 FKVF--FTIKKLPYLSVVDENGVFLGILTHKKVFE 117
Cdd:COG4109   96 ASAAhkMIWEGIELLPVVDDDGRLLGIISRQDVLK 130

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

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447143256  11 REVLFCSSSITIGEALEHLNKTGYRCVPVLDEKKeKYLGNVYKVDILE--YKGSLEESVVQLLNDKEG--------YVRE 80
Cdd:COG3448   10 RDVVTVSPDTTLREALELMREHGIRGLPVVDEDG-RLVGIVTERDLLRalLPDRLDELEERLLDLPVEdvmtrpvvTVTP 88

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 447143256  81 DSSFFKVFFTI--KKLPYLSVVDENGVFLGILTHKKVFELLEDAWGVH 126
Cdd:COG3448   89 DTPLEEAAELMleHGIHRLPVVDDDGRLVGIVTRTDLLRALARLLEEE 136

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.

                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 447143256    8 VPKREVLFCSSSITIGEALEHLNKTGYRCVPVLDEkKEKYLGNVYKVDILEY 59
Cdd:pfam00571   4 IMTKDVVTVSPDTTLEEALELMREHGISRLPVVDE-DGKLVGIVTLKDLLRA 54

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).

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447143256  10 KREVLFCSSSITIGEALEHLNKTGYRCVPVLDeKKEKYLGNVYKVDILEYkgsLEESVVQLLNDKEGY------------ 77
Cdd:cd09834    1 KSEVAYLYDDSTLRQALEKMEYHRYTAIPILN-RDGKYVGTITEGDLLWY---IKNKPNLDLKDAEKIsikdiprrrdnk 76

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 447143256  78 -VREDSSFFKVFFTIKKLPYLSVVDENGVFLGILTHKKVFE 117
Cdd:cd09834   77 pVNINANMEDLLDLAMNQNFVPVVDDRGVFIGIVTRKDIIK 117

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.

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447143256   8 VPKREVLFCSSSITIGEALEHLNKTGYRCVPVLDEKKEKYLGNVYKVDILE--------------YKGSL----EESVVQ 69
Cdd:cd17779    5 IATKDVITIPPTTTIIGAIKTMTEKGFRRLPVADAGTKRLEGIVTSMDIVDflgggskynlvekkHNGNLlaaiNEPVRE 84

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 447143256  70 LLNDKEGYVREDSSFFKVFFTI--KKLPYLSVVDENGVFLGILTHKKVFELL 119
Cdd:cd17779   85 IMTRDVISVKENASIDDAIELMleKNVGGLPIVDKDGKVIGIVTERDFLKFL 136

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).

                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....
gi 447143256  78 VREDSSFFKVF--FTIKKLPYLSVVDENGVFLGILTHKKVFELL 119
Cdd:cd04639   77 VAADQSLLEVVklLEEQQLPALAVVSENGTLVGLIEKEDIIELL 120

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).

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447143256  17 SSSITIGEALEHLNKTGYRCVPVLDEKKeKYLGNVYKVDI----LeyKG-SLEESVVQLLNDKEGYVREDSSFFKVFFTI 91
Cdd:cd04607    8 SPDTTIREAIEVIDKGALQIALVVDENR-KLLGTVTDGDIrrglL--KGlSLDAPVEEVMNKNPITASPSTSREELLALM 84

                         90       100
                 ....*....|....*....|..
gi 447143256  92 --KKLPYLSVVDENGVFLGILT 111
Cdd:cd04607   85 raKKILQLPIVDEQGRVVGLET 106