NCBI Conserved Domain Search

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: 160.68 E-value: 3.59e-52

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983192395  10 MTKQVVTFTPDMPLSLALDKVMRSPHMGGPVIDDNEQVIGFLSEQDLLDKLVKVSYFCQDTHIVRDCMYQEVLSVSPELS 89
Cdd:cd04629    1 MTRNPVTLTPDTSILEAVELLLEHKISGAPVVDEQGRLVGFLSEQDCLKALLEASYHCEPGGTVADYMSTEVLTVSPDTS 80

                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 983192395  90 IIELADMMQVGKPKAYPVIDNKKLVGMITRSDVLRA 125
Cdd:cd04629   81 IVDLAQLFLKNKPRRYPVVEDGKLVGQISRRDVLRA 116

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

Pssm-ID: 442671 [Multi-domain] Cd Length: 136 Bit Score: 110.34 E-value: 5.06e-32

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983192395   3 SIKVKDYMTKQVVTFTPDMPLSLALDKVMRSPHMGGPVIDDNEQVIGFLSEQDLLDKLVKVSYFCQDTHI----VRDCMY 78
Cdd:COG3448    1 AMTVRDIMTRDVVTVSPDTTLREALELMREHGIRGLPVVDEDGRLVGIVTERDLLRALLPDRLDELEERLldlpVEDVMT 80

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 983192395  79 QEVLSVSPELSIIELADMMQVGKPKAYPVID-NKKLVGMITRSDVLRAIGKNLNE 132
Cdd:COG3448   81 RPVVTVTPDTPLEEAAELMLEHGIHRLPVVDdDGRLVGIVTRTDLLRALARLLEE 135

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

Pssm-ID: 442013 [Multi-domain] Cd Length: 206 Bit Score: 105.74 E-value: 2.02e-29

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983192395   1 MHSIKVKDYMTKQVVTFTPDMPLSLALDKVMRSPHMGGPVIDDNEqVIGFLSEQDLLDKLVKVSYFcqDTHIVRDCMYQE 80
Cdd:COG2524   83 VLKMKVKDIMTKDVITVSPDTTLEEALELMLEKGISGLPVVDDGK-LVGIITERDLLKALAEGRDL--LDAPVSDIMTRD 159

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 983192395  81 VLSVSPELSIIELADMMQVGKPKAYPVID-NKKLVGMITRSDVLRAI 126
Cdd:COG2524  160 VVTVSEDDSLEEALRLMLEHGIGRLPVVDdDGKLVGIITRTDILRAL 206

CBS domain [Signal transduction mechanisms];

Pssm-ID: 440283 [Multi-domain] Cd Length: 128 Bit Score: 99.94 E-value: 5.00e-28

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983192395   4 IKVKDYMTKQVVTFTPDMPLSLALDKVMRSPHMGGPVIDDNEQVIGFLSEQDLLDKLVKVSYFCQDTHiVRDCMYQEVLS 83
Cdd:COG0517    1 MKVKDIMTTDVVTVSPDATVREALELMSEKRIGGLPVVDEDGKLVGIVTDRDLRRALAAEGKDLLDTP-VSEVMTRPPVT 79

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 983192395  84 VSPELSIIELADMMQVGKPKAYPVID-NKKLVGMITRSDVLRAI 126
Cdd:COG0517   80 VSPDTSLEEAAELMEEHKIRRLPVVDdDGRLVGIITIKDLLKAL 123

Predicted transcriptional regulator containing CBS domains [Transcription];

Pssm-ID: 443285 [Multi-domain] Cd Length: 135 Bit Score: 93.44 E-value: 1.80e-25

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983192395   3 SIKVKDYMT-KQVVTFTPDMPLSLALDKVMRSPHMGGPVIDDNEQVIGFLSEQDLLDKlvkvsyfcQDTHIVRDCMYQEV 81
Cdd:COG4109   15 ILLVEDIMTlEDVATLSEDDTVEDALELLEKTGHSRFPVVDENGRLVGIVTSKDILGK--------DDDTPIEDVMTKNP 86

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 983192395  82 LSVSPELSIIELADMMQVGKPKAYPVID-NKKLVGMITRSDVLRA 125
Cdd:COG4109   87 ITVTPDTSLASAAHKMIWEGIELLPVVDdDGRLLGIISRQDVLKA 131

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: 90.95 E-value: 1.72e-24

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983192395  10 MTKQVVTFTPDMPLSLALdKVMRSPHMGG-PVIDDNEQVIGFLSEQDLLDKLVKVS-----------------YFCQDTH 71
Cdd:cd04586    1 MTTDVVTVTPDTSVREAA-RLLLEHRISGlPVVDDDGKLVGIVSEGDLLRREEPGTeprrvwwldallesperLAEEYVK 79

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 983192395  72 I----VRDCMYQEVLSVSPELSIIELADMMQVGKPKAYPVIDNKKLVGMITRSDVLRA 125
Cdd:cd04586   80 AhgrtVGDVMTRPVVTVSPDTPLEEAARLMERHRIKRLPVVDDGKLVGIVSRADLLRA 137

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

Pssm-ID: 442149 [Multi-domain] Cd Length: 124 Bit Score: 88.73 E-value: 1.02e-23

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983192395   6 VKDYMTKQVVTFTPDMPLSLALdKVMRSPHMGG-PVIDDNEQVIGFLSEQDLLDKLVKVSYFCQDThIVRDCMYQEVLSV 84
Cdd:COG2905    1 VKDIMSRDVVTVSPDATVREAA-RLMTEKGVGSlVVVDDDGRLVGIITDRDLRRRVLAEGLDPLDT-PVSEVMTRPPITV 78

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 983192395  85 SPELSIIELADMMQVGKPKAYPVIDNKKLVGMITRSDVLRAIGKNL 130
Cdd:COG2905   79 SPDDSLAEALELMEEHRIRHLPVVDDGKLVGIVSITDLLRALSEEL 124

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: 83.83 E-value: 6.60e-22

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983192395  11 TKQVVTFTPDMPLSLALDKVMRSPHMGGPVIDDNEQVIGFLSEQDLLDKLvkVSYFCQDTHIVRDCMYQEVLSVSPELSI 90
Cdd:cd02205    1 TRDVVTVDPDTTVREALELMAENGIGALPVVDDDGKLVGIVTERDILRAL--VEGGLALDTPVAEVMTPDVITVSPDTDL 78

                         90       100       110
                 ....*....|....*....|....*....|....*
gi 983192395  91 IELADMMQVGKPKAYPVID-NKKLVGMITRSDVLR 124
Cdd:cd02205   79 EEALELMLEHGIRRLPVVDdDGKLVGIVTRRDILR 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: 80.54 E-value: 1.71e-20

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983192395   5 KVKDYMTKQVVTFTPDMPLSLALDkVMRSPHMGG-PVIDDNeQVIGFLSEQDLLD----KLVKVSYFCQDTHI----VRD 75
Cdd:cd04584    1 LVKDIMTKNVVTVTPDTSLAEARE-LMKEHKIRHlPVVDDG-KLVGIVTDRDLLRaspsKATSLSIYELNYLLskipVKD 78

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|.
gi 983192395  76 CMYQEVLSVSPELSIIELADMMQVGKPKAYPVIDNKKLVGMITRSDVLRAI 126
Cdd:cd04584   79 IMTKDVITVSPDDTVEEAALLMLENKIGCLPVVDGGKLVGIITETDILRAF 129

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: 70.68 E-value: 9.99e-17

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983192395   8 DYMTKQVVTFTPDMPLSLALDKVMRSPHMGGPVIDDNEqVIGFLSeqdlLDKLVKVSYFCQDTHIVRDCMYQEVLSVSPE 87
Cdd:cd04801    1 DIMTPEVVTVTPEMTVSELLDRMFEEKHLGYPVVENGR-LVGIVT----LEDIRKVPEVEREATRVRDVMTKDVITVSPD 75

                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 983192395  88 LSIIELADMMQVGKPKAYPVIDNKKLVGMITRSDVLRA 125
Cdd:cd04801   76 ADAMEALKLMSQNNIGRLPVVEDGELVGIISRTDLMRA 113

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: 67.20 E-value: 3.58e-15

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983192395  10 MTKQVVTFTPDMPLSLALDkVMRSPHMGG-PVIDDNEQVIGFLSEQDLL------------DKLVKVSYFCQDTHI-VRD 75
Cdd:cd04600    1 MSRDVVTVTPDTSLEEAWR-LLRRHRIKAlPVVDRARRLVGIVTLADLLkhadldpprglrGRLRRTLGLRRDRPEtVGD 79

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|.
gi 983192395  76 CMYQEVLSVSPELSIIELADMMQVGKPKAYPVIDN-KKLVGMITRSDVLRA 125
Cdd:cd04600   80 IMTRPVVTVRPDTPIAELVPLFSDGGLHHIPVVDAdGRLVGIVTQSDLIAA 130

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: 65.71 E-value: 1.22e-14

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983192395   5 KVKDYMTKQVVTFTPDMPLSLALDKVMRSPHMGGPVIDDNEQV--------IGFLSEQDLLDKLVKVSYFCQDTHIVRDC 76
Cdd:cd04631    1 VVEDYMTKNVITATPGTPIEDVAKIMVRNGFRRLPVVSDGKLVgivtstdiMRYLGSGEAFEKLKTGNIHEVLNVPISSI 80

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|
gi 983192395  77 MYQEVLSVSPELSIIELADMMQVGKPKAYPVIDNKKLVGMITRSDVLRAI 126
Cdd:cd04631   81 MKRDIITTTPDTDLGEAAELMLEKNIGALPVVDDGKLVGIITERDILRAI 130

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: 62.90 E-value: 9.93e-14

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983192395  14 VVTFTPDMPLSLALDKVMRSPHMGGPVIDDNeQVIGFLSEQDLlDKLVKVSYfcqdTHI-VRDCMYQEVLSVSPELSIIE 92
Cdd:cd04595    4 VKTVSPDTTIEEARKIMLRYGHTGLPVVEDG-KLVGIISRRDV-DKAKHHGL----GHApVKGYMSTNVITIDPDTSLEE 77

                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 983192395  93 LADMM---QVGKpkaYPVIDNKKLVGMITRSDVLRA 125
Cdd:cd04595   78 AQELMvehDIGR---LPVVEEGKLVGIVTRSDVLRY 110

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: 62.72 E-value: 1.15e-13

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983192395  10 MTKQVVTFTPDMPLSLALDKVMRSPHMGGPVIDDNeQVIGFLSEQDLLDKlvkvsyfcQDTHIVRDCMYQEVLSVSPELS 89
Cdd:cd04610    1 MTRDVITVSPDDTVKDVIKLIKETGHDGFPVVDDG-KVVGYVTAKDLLGK--------DDDEKVSEIMSRDTVVADPDMD 71

                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 983192395  90 IIELADMM-QVGKPKaYPVIDN-KKLVGMITRSDVLR 124
Cdd:cd04610   72 ITDAARVIfRSGISK-LPVVDDeGNLVGIITNMDVIR 107

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: 62.36 E-value: 1.28e-13

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983192395  10 MTKQVVTFTPDMPLSLALDkVMRSPHMGG-PVIDdNEQVIGFLSEQDLLdklvkvsyFCQDTHIVRDCMYQEVLSVSPEL 88
Cdd:cd04599    1 MTRNPITISPLDSVARAAA-LMERQRIGGlPVVE-NGKLVGIITSRDVR--------RAHPNRLVADAMSRNVVTISPEA 70

                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 983192395  89 SIIELADMMQVGKPKAYPVIDNKKLVGMITRSDVLRA 125
Cdd:cd04599   71 SLWEAKELMEEHGIERLVVVEEGRLVGIITKSTLYLE 107

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: 62.43 E-value: 1.41e-13

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983192395  12 KQVVTFTPDMPLSLALdKVMRSPHMGG-PVIDDNEQVIGFLSEQDLLDKLVKVSYFCQDTHiVRDCMYQEVLSVSPELSI 90
Cdd:cd04623    2 RDVVTVSPDATVAEAL-RLLAEKNIGAlVVVDDGGRLVGILSERDYVRKLALRGASSLDTP-VSEIMTRDVVTCTPDDTV 79

                         90       100       110
                 ....*....|....*....|....*....|....
gi 983192395  91 IELADMMQVGKPKAYPVIDNKKLVGMITRSDVLR 124
Cdd:cd04623   80 EECMALMTERRIRHLPVVEDGKLVGIVSIGDVVK 113

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: 58.97 E-value: 3.70e-12

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983192395  11 TKQVVTFTPDMPLSLALDKVMRSPHMGGPVIDDNEQVIGFLSEQDLLDKLVKVSYFCQDThiVRDCMYQEVLSVSPELSI 90
Cdd:cd17784    1 TKNVITAKPNEGVVEAFEKMLKHKISALPVVDDEGKLIGIVTATDLGHNLILDKYELGTT--VEEVMVKDVATVHPDETL 78

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 983192395  91 IELADMMQVGKPKA-----YPVIDNKKLVGMITRSDVLRAI 126
Cdd:cd17784   79 LEAIKKMDSNAPDEeiinqLPVVDDGKLVGIISDGDIIRAI 119

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

Pssm-ID: 441840 [Multi-domain] Cd Length: 443 Bit Score: 60.85 E-value: 1.04e-11

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983192395   9 YMTKQVVTFTPDMPLSLALDKVMRSPHMGG-----PVIDDNEQVIGFLSEQDLLdklvkvsyFCQDTHIVRDCMYQEVLS 83
Cdd:COG2239  134 LMTTEFVAVREDWTVGEALRYLRRQAEDPEtiyyiYVVDDDGRLVGVVSLRDLL--------LADPDTKVSDIMDTDVIS 205

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 983192395  84 VSPELSIIELADMMQvgkpK----AYPVID-NKKLVGMITRSDVLRAI 126
Cdd:COG2239  206 VPADDDQEEVARLFE----RydllALPVVDeEGRLVGIITVDDVVDVI 249

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: 56.78 E-value: 2.39e-11

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983192395  10 MTKQVVTFTPDMPLsLALDKVMRSPHMGG-PVIDDNEQVIGFLSEQDLLDKLVKVSYFCQDThIVRDCMYQEVLSVSPEL 88
Cdd:cd17775    1 CRREVVTASPDTSV-LEAARLMRDHHVGSvVVVEEDGKPVGIVTDRDIVVEVVAKGLDPKDV-TVGDIMSADLITAREDD 78

                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 983192395  89 SIIELADMMQVGKPKAYPVIDNK-KLVGMITRSDVLRAI 126
Cdd:cd17775   79 GLFEALERMREKGVRRLPVVDDDgELVGIVTLDDILELL 117

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: 341367 [Multi-domain] Cd Length: 114 Bit Score: 55.22 E-value: 7.25e-11

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983192395   6 VKDYMTKQVVTFTPDMPLSLALDKVMRSPHMGGPVIDDNE--QVIGFLSEQDLLDKLvkvsyfcqdTHIVRDCMYQEVLS 83
Cdd:cd04591    2 AEDVMRPPLTVLARDETVGDIVSVLKTTDHNGFPVVDSTEsqTLVGFILRSQLILLL---------EADLRPIMDPSPFT 72

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 983192395  84 VSPELSIIELADMMQVGKPKAYPVIDNKKLVGMITRSDVLRA 125
Cdd:cd04591   73 VTEETSLEKVHDLFRLLGLRHLLVTNNGRLVGIVTRKDLLRA 114

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

Pssm-ID: 442013 [Multi-domain] Cd Length: 206 Bit Score: 56.43 E-value: 1.42e-10

                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 983192395  73 VRDCMYQEVLSVSPELSIIELADMMQVGKPKAYPVIDNKKLVGMITRSDVLRAIGKNL 130
Cdd:COG2524   88 VKDIMTKDVITVSPDTTLEEALELMLEKGISGLPVVDDGKLVGIITERDLLKALAEGR 145

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: 52.91 E-value: 7.39e-10

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983192395  10 MTKQVVTFTPDMPLSLALdKVMRSPHMGGPVI-DDNEQVIGFLSEQDLLDKlvkVSYFCQDTHIVRDCMYQEVLSVSPEL 88
Cdd:cd09836    1 MSKPVVTVPPETTIREAA-KLMAENNIGSVVVvDDDGKPVGIVTERDIVRA---VAEGIDLDTPVEEIMTKNLVTVSPDE 76

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 983192395  89 SIIELADMMQVGKPKAYPVIDN-KKLVGMITRSDVLRAIG 127
Cdd:cd09836   77 SIYEAAELMREHNIRHLPVVDGgGKLVGVISIRDLARELS 116

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: 55.09 E-value: 9.09e-10

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983192395    5 KVKDY---MTKQVVTFTPDMPLSLALDKVMRSPHMGGPVIDDNeQVIGFLSEQDLldklvkvsYFCQDTHI-VRDCMYQE 80
Cdd:pfam00478  78 KVKRSesgMITDPVTLSPDATVADALALMERYGISGVPVVDDG-KLVGIVTNRDL--------RFETDLSQpVSEVMTKE 148

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 983192395   81 VLSVSPELSIIELA-DMMQVGKPKAYPVIDNK-KLVGMITRSDVLRAIgKNLNEC 133
Cdd:pfam00478 149 NLVTAPEGTTLEEAkEILHKHKIEKLPVVDDNgRLVGLITIKDIEKAK-EYPNAA 202

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: 51.06 E-value: 1.07e-09

                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 983192395   73 VRDCMYQEVLSVSPELSIIELADMMQVGKPKAYPVID-NKKLVGMITRSDVLRAI 126
Cdd:pfam00571   1 VKDIMTKDVVTVSPDTTLEEALELMREHGISRLPVVDeDGKLVGIVTLKDLLRAL 55

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: 51.95 E-value: 1.53e-09

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983192395  10 MTKQVVTFTPDMPLSLALDKVMRSPHMGG-----PVIDDNEQVIGFLSEQDLLdklvkvsyFCQDTHIVRDCMYQEVLSV 84
Cdd:cd04606    7 MTTEFVAVRPDWTVEEALEYLRRLAPDPEtiyyiYVVDEDRRLLGVVSLRDLL--------LADPDTKVSDIMDTDVISV 78

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 983192395  85 SPELSIIELADMMQvgkpK----AYPVID-NKKLVGMITRSDVLRAI 126
Cdd:cd04606   79 SADDDQEEVARLFA----KydllALPVVDeEGRLVGIITVDDVLDVI 121

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: 51.70 E-value: 1.87e-09

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983192395  39 PVIDDNEQVIGFLSEQDLLDKlvkvsyfcQDTHIVRDCMYQEVLSVSPELSIIELADMMqvgkpkAY------PVID-NK 111
Cdd:cd04596   29 PVVDEENRVVGIVTAKDVIGK--------EDDTPIEKVMTKNPITVKPKTSVASAAHMM------IWegiellPVVDeNR 94

                         90
                 ....*....|....
gi 983192395 112 KLVGMITRSDVLRA 125
Cdd:cd04596   95 KLLGVISRQDVLKA 108

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

Pssm-ID: 442671 [Multi-domain] Cd Length: 136 Bit Score: 51.79 E-value: 2.90e-09

                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 983192395   1 MHSIKVKDYMTKQVVTFTPDMPLSLALDKVMRSPHMGGPVIDDNEQVIGFLSEQDLLDKLVK 62
Cdd:COG3448   70 LLDLPVEDVMTRPVVTVTPDTPLEEAAELMLEHGIHRLPVVDDDGRLVGIVTRTDLLRALAR 131

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: 49.52 E-value: 3.30e-09

                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 983192395    6 VKDYMTKQVVTFTPDMPLSLALDKVMRSPHMGGPVIDDNEQVIGFLSEQDLLDKLVK 62
Cdd:pfam00571   1 VKDIMTKDVVTVSPDTTLEEALELMREHGISRLPVVDEDGKLVGIVTLKDLLRALLG 57

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: 51.18 E-value: 3.65e-09

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983192395   5 KVKDYMTKQVVTFTPDMPLSLALDKVMRSPHMGGPVIDDNEqVIGFLSEQDLL-------DKLVKVSYFCQDTH--IVRD 75
Cdd:cd17778    1 KVKEFMTTPVVTIYPDDTLKEAMELMVTRGFRRLPVVSGGK-LVGIVTAMDIVkyfgsheAKKRLTTGDIDEAYstPVEE 79

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 983192395  76 CMYQEVLSVSPELSIIELADMMQVGKPKAYPVIDNK-KLVGMITRSDVLRAI 126
Cdd:cd17778   80 IMSKEVVTIEPDADIAEAARLMIKKNVGSLLVVDDEgELKGIITERDVLIAL 131

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: 50.64 E-value: 4.11e-09

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983192395  11 TKQVVTFTPDMPLSLALDKVMRSPHMGGPVIDDN-EQVIGFLSEQDLLdklvKVSYFCQDTHIVRDCMYQEVLSVSPELS 89
Cdd:cd17772    1 SSPVISVEPDTTIAEAAELMTRYNINALPVVDGGtGRLVGIITRQVAE----KAIYHGLGDLPVSEYMTTEFATVTPDAP 76

                         90       100       110
                 ....*....|....*....|....*....|....*
gi 983192395  90 IIELADMMQVGKPKAYPVIDNKKLVGMITRSDVLR 124
Cdd:cd17772   77 LSEIQEIIVEQRQRLVPVVEDGRLVGVITRTDLLN 111

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: 51.13 E-value: 6.98e-09

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983192395   9 YMTKQVVTFTPDMPLSLALdKVMR-SPHMGGPVIDDNEQVIGFLSEQDLLDKLVKV------------------------ 63
Cdd:cd04614    1 YAGKGVVPVWDETPLPVAL-RAMRlANVPAAPVLDSEGKLVGIVTERDLIDVSRIVeseeesgmsiaddedewswegird 79

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 983192395  64 --SYFCQDTHI------VRDCMYQEVLSVSPELSIIELADMMQVGKPKAYPVID-NKKLVGMITRSDVLRA 125
Cdd:cd04614   80 vmSLYYPTSNVelpdkpVKDVMTKDVVTAFPSSTVSEAAKKMIRNDIEQLPVVSgEGDLAGMLRDVDLLKA 150

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: 49.34 E-value: 1.27e-08

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983192395  10 MTKQVVTFTPDMPLSLALdKVMRSPHMGG-PVIDDNeQVIGFLSEQDLLDKLVKVSYFCQDTHiVRDCMYQEVLSVSPEL 88
Cdd:cd04622    1 MTRDVVTVSPDTTLREAA-RLMRDLDIGAlPVCEGD-RLVGMVTDRDIVVRAVAEGKDPNTTT-VREVMTGDVVTCSPDD 77

                         90       100       110
                 ....*....|....*....|....*....|....*
gi 983192395  89 SIIELADMMQVGKPKAYPVIDN-KKLVGMITRSDV 122
Cdd:cd04622   78 DVEEAARLMAEHQVRRLPVVDDdGRLVGIVSLGDL 112

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: 48.75 E-value: 2.52e-08

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983192395   6 VKDYMTKQVVTFTPDMPLSLALdKVMRSPHMGGPVIDDNEQ--VIGFLSEQDLLDKLVkvsyfCQDTHI----VRDCMYQ 79
Cdd:cd04630    1 VRDVMKTNVVTIDGLATVREAL-QLMKEHNVKSLIVEKRHEhdAYGIVTYTDILKKVI-----AEDRDPdlvnVYEIMTK 74

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 983192395  80 EVLSVSPELSIIELADMMQVGKPKAYPVIDNKKLVGMITRSDVLRA 125
Cdd:cd04630   75 PAISVSPDLDIKYAARLMARFNLKRAPVIENNELIGIVSMTDLVLD 120

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

Pssm-ID: 442671 [Multi-domain] Cd Length: 136 Bit Score: 49.09 E-value: 2.73e-08

                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 983192395  73 VRDCMYQEVLSVSPELSIIELADMMQVGKPKAYPVID-NKKLVGMITRSDVLRAIGKNLNECFKHQ 137
Cdd:COG3448    4 VRDIMTRDVVTVSPDTTLREALELMREHGIRGLPVVDeDGRLVGIVTERDLLRALLPDRLDELEER 69

CBS domain [Signal transduction mechanisms];

Pssm-ID: 440283 [Multi-domain] Cd Length: 128 Bit Score: 48.71 E-value: 2.89e-08

                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 983192395   2 HSIKVKDYMTKQVVTFTPDMPLSLALDKVMRSPHMGGPVIDDNEQVIGFLSEQDLLDKLVK 62
Cdd:COG0517   65 LDTPVSEVMTRPPVTVSPDTSLEEAAELMEEHKIRRLPVVDDDGRLVGIITIKDLLKALLE 125

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: 48.19 E-value: 4.84e-08

                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 983192395   1 MHSIKVKDYMTKQVVTFTPDMPLSLALdKVMRSPHMGG-PVIDDNeQVIGFLSEQDLLDKLV 61
Cdd:cd04584   71 LSKIPVKDIMTKDVITVSPDDTVEEAA-LLMLENKIGClPVVDGG-KLVGIITETDILRAFI 130

putative manganese-dependent inorganic diphosphatase;

Pssm-ID: 237843 [Multi-domain] Cd Length: 546 Bit Score: 49.06 E-value: 1.18e-07

                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....
gi 983192395  73 VRDCMYQEVLSVSPELSIIELADMMQVGKPKAYPVIDNK-KLVGMITRSDVLRA 125
Cdd:PRK14869  70 VRDLEIDKPVTVSPDTSLKEAWNLMDENNVKTLPVVDEEgKLLGLVSLSDLARA 123

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: 46.80 E-value: 1.40e-07

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983192395  10 MTKQVVTFTPDMPLSLALDKVMRSPHMGGPVIDDNEQVIGFLSEQDLLDKLvkvsyFCQDTH---IVRDCMYQEVLSVSP 86
Cdd:cd04613    1 MPRKVTVLPEGMTFRQFTEFIAGTRQHYFPVVDEQGRLTGILSIQDVRGVL-----FEEELWdlvVVKDLATTDVITVTP 75

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 983192395  87 ELSIIELADMMQVGKPKAYPVI---DNKKLVGMITRSDVLRA 125
Cdd:cd04613   76 DDDLYTALLKFTSTNLDQLPVVdddDPGKVLGMLSRRDVIAA 117

GuaB1 family IMP dehydrogenase-related protein;

Pssm-ID: 181127 [Multi-domain] Cd Length: 479 Bit Score: 48.36 E-value: 2.14e-07

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983192395  15 VTFTPDMPLSLALDKVMRSPHMGGPVIDDNEQVIGFLSEQDLLDklvkVSYFCQdthiVRDCMYQEVLSVSPELSIIELA 94
Cdd:PRK07807 100 VTLSPDDTVGDALALLPKRAHGAVVVVDEEGRPVGVVTEADCAG----VDRFTQ----VRDVMSTDLVTLPAGTDPREAF 171

                         90       100       110
                 ....*....|....*....|....*....|..
gi 983192395  95 DMMQVGKPKAYPVID-NKKLVGMITRSDVLRA 125
Cdd:PRK07807 172 DLLEAARVKLAPVVDaDGRLVGVLTRTGALRA 203

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: 45.10 E-value: 5.90e-07

                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 983192395  77 MYQEVLSVSPELSIIELADMMQ---VGkpkAYPVIDNKKLVGMITRSD-VLRAI--GKNLNEC 133
Cdd:cd04622    1 MTRDVVTVSPDTTLREAARLMRdldIG---ALPVCEGDRLVGMVTDRDiVVRAVaeGKDPNTT 60

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: 45.09 E-value: 6.17e-07

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983192395  10 MTKQVVTFTPDMPLSLALDKVMRSpHMGGPVIDDNEQVIGFLSEQDLLDKLVKVSYfCQDTHIVRDCMYQEVLSVSPELS 89
Cdd:cd17776    1 MTTDVVTVDADASLEDAAERMLRN-RVGSVVVTDDGTPAGILTETDALHAGYATDD-PFSEIPVRAVASRPLVTISPTAT 78

                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 983192395  90 IIELADMMQVGKPKAYPVIDNKKLVGMITRSDVLRA 125
Cdd:cd17776   79 LREAAERMVDEGVKKLPVVDGLDLVGILTATDIIRA 114

Predicted transcriptional regulator, contains an XRE-type HTH domain (archaeal members contain CBS pair) [Transcription];

Pssm-ID: 442838 [Multi-domain] Cd Length: 95 Bit Score: 44.63 E-value: 6.57e-07

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983192395   6 VKDYMTKQVVTFTPDMPLSLALDKVMRSPHMGG-PVIddneQVIGfLSEQDLLDKlvkvsyfcqdthivrdcmyqEVLSV 84
Cdd:COG3620    1 VRDLMSRDVVTVSPDDTLGEALRLMRKELGLSQlPVA----ELVG-VSQSDILRI--------------------ESGKR 55

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 983192395  85 SPELS-IIELADMMQvGKPKAYPVIDNKKLVGMITRSDVLR 124
Cdd:COG3620   56 DPTVStLEKIAEALG-KELSAVLVVDDGKLVGIITRRDLLK 95

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: 44.93 E-value: 7.62e-07

                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 983192395   3 SIKVKDYMTKQVVTFTPDMPLSLALDKVMRS--PHMggPVIDDNEQVIGFLSEQDLLD 58
Cdd:cd02205   58 DTPVAEVMTPDVITVSPDTDLEEALELMLEHgiRRL--PVVDDDGKLVGIVTRRDILR 113

Predicted transcriptional regulator containing CBS domains [Transcription];

Pssm-ID: 443285 [Multi-domain] Cd Length: 135 Bit Score: 44.90 E-value: 1.19e-06

                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 983192395   1 MHSIKVKDYMTKQVVTFTPDMPLSLALDKVMRSPHMGGPVIDDNEQVIGFLSEQDLL 57
Cdd:COG4109   73 DDDTPIEDVMTKNPITVTPDTSLASAAHKMIWEGIELLPVVDDDGRLLGIISRQDVL 129

Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains found in archaea and associated with helix turn helix domain; This cd contains two tandem repeats of the cystathionine beta-synthase (CBS pair) domains in the inosine 5' monophosphate dehydrogenase (IMPDH) protein. IMPDH is an essential enzyme that catalyzes the first step unique to GTP synthesis, playing a key role in the regulation of cell proliferation and differentiation. The CBS domain, named after human CBS, is a small domain originally identified in cystathionine beta-synthase and is subsequently found in a wide range of different proteins. CBS domains usually occur in tandem repeats. They associate to form a so-called Bateman domain or a CBS pair based on crystallographic studies in bacteria. The CBS pair was used as a basis for this cd hierarchy since the human CBS proteins can adopt the typical core structure and form an intramolecular CBS pair. The interface between the two CBS domains forms a cleft that is a potential ligand binding site. The CBS pair coexists with a variety of other functional domains and this has been used to help in its classification here. It has been proposed that the CBS domain may play a regulatory role, although its exact function is unknown. Mutations of conserved residues within this domain are associated with a variety of human hereditary diseases, including congenital myotonia, idiopathic generalized epilepsy, hypercalciuric nephrolithiasis, and classic Bartter syndrome (CLC chloride channel family members), Wolff-Parkinson-White syndrome (gamma 2 subunit of AMP-activated protein kinase), retinitis pigmentosa (IMP dehydrogenase-1), and homocystinuria (cystathionine beta-synthase).

Pssm-ID: 341364 [Multi-domain] Cd Length: 111 Bit Score: 44.06 E-value: 1.35e-06

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983192395  11 TKQVVTFTPDMPLSLALDKVMRSPHMGGPVIDDNEqVIGFLSEQDLLDKLVKVSYFCQdthiVRDCMYQEVLSVSPELSI 90
Cdd:cd04588    1 SKDLITLKPDATIKDAAKLLSENNIHGAPVVDDGK-LVGIVTLTDIAKALAEGKENAK----VKDIMTKDVITIDKDEKI 75

                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 983192395  91 IELADMMQ---VGKPKAypVIDNKKLVGMITRSDVLR 124
Cdd:cd04588   76 YDAIRLMNkhnIGRLIV--VDDNGKPVGIITRTDILK 110

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: 44.77 E-value: 1.55e-06

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983192395  37 GGPVIDDNEQVIGFLSEQDLLdKLVKVSYFCQDTH-------------------------IVRDCMYQEVLSVSPELSII 91
Cdd:cd17789   28 GLPVIDEDWRLVGVVSDYDLL-ALDSISGRSQTDNnfppadstwktfnevqkllsktngkVVGDVMTPSPLVVREKTNLE 106

                         90       100       110
                 ....*....|....*....|....*....|....*
gi 983192395  92 ELADMMQVGKPKAYPVIDNK-KLVGMITRSDVLRA 125
Cdd:cd17789  107 DAARILLETKFRRLPVVDSDgKLVGIITRGNVVRA 141

putative manganese-dependent inorganic diphosphatase;

Pssm-ID: 237843 [Multi-domain] Cd Length: 546 Bit Score: 45.59 E-value: 2.02e-06

                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 983192395   3 SIKVKDYMTKQ-VVTFTPDMPLSLALDKVMRSPHMGGPVIDDNEQVIGFLSEQDLLD 58
Cdd:PRK14869 245 SIPVSYIMTTEdLVTFSKDDYLEDVKEVMLKSRYRSYPVVDEDGKVVGVISRYHLLS 301

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: 43.49 E-value: 2.31e-06

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983192395  10 MTKQVVTFTPDMPLSLALDkVMRSPHMGG-PVI-DDNEQVIGFLSEQDLLDKlvkvsyfcQDTHIVRDCMYQEVLSVSPE 87
Cdd:cd04638    1 MTKDVVTVTLPGTRDDVLE-ILKKKAISGvPVVkKETGKLVGIVTRKDLLRN--------PDEEQIALLMSRDPITISPD 71

                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 983192395  88 LSIIELADMMQVGKPKAYPVIDNKKLVGMITRSDVLRA 125
Cdd:cd04638   72 DTLSEAAELMLEHNIRRVPVVDDDKLVGIVTVADLVRA 109

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: 42.11 E-value: 2.36e-06

                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*...
gi 983192395    80 EVLSVSPELSIIELADMMQVGKPKAYPVIDNK-KLVGMITRSDVLRAI 126
Cdd:smart00116   1 DVVTVSPDTTLEEALELLRENGIRRLPVVDEEgRLVGIVTRRDIIKAL 48

Hemolysin-related protein, contains CBS domains, UPF0053 family [General function prediction only];

Pssm-ID: 440865 [Multi-domain] Cd Length: 435 Bit Score: 44.34 E-value: 5.32e-06

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983192395   4 IKVKDYMT--KQVVTFTPDMPLSLALDKVMRSPHMGGPVIDDN-EQVIGFLSEQDLLDKLVKvsyfcQDTHIVRDCMyQE 80
Cdd:COG1253  214 RTVREVMTprTDVVALDLDDTLEEALELILESGHSRIPVYEGDlDDIVGVVHVKDLLRALLE-----GEPFDLRDLL-RP 287

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 983192395  81 VLSVSPELSIIELADMMQVGKPKAYPVID-NKKLVGMITRSDVLRAI 126
Cdd:COG1253  288 PLFVPETKPLDDLLEEFRRERVHMAIVVDeYGGTAGLVTLEDILEEI 334

Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with the HPP motif domain; This cd contains two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with the HPP motif domain. These proteins are integral membrane proteins with four transmembrane spanning helices. The function of these proteins is uncertain, but they are thought to be transporters. The CBS domain, named after human CBS, is a small domain originally identified in cystathionine beta-synthase and is subsequently found in a wide range of different proteins. CBS domains usually occur in tandem repeats. They associate to form a so-called Bateman domain or a CBS pair based on crystallographic studies in bacteria. The CBS pair was used as a basis for this cd hierarchy since the human CBS proteins can adopt the typical core structure and form an intramolecular CBS pair. The interface between the two CBS domains forms a cleft that is a potential ligand binding site. The CBS pair coexists with a variety of other functional domains and this has been used to help in its classification here. It has been proposed that the CBS domain may play a regulatory role, although its exact function is unknown. Mutations of conserved residues within this domain are associated with a variety of human hereditary diseases, including congenital myotonia, idiopathic generalized epilepsy, hypercalciuric nephrolithiasis, and classic Bartter syndrome (CLC chloride channel family members), Wolff-Parkinson-White syndrome (gamma 2 subunit of AMP-activated protein kinase), retinitis pigmentosa (IMP dehydrogenase-1), and homocystinuria (cystathionine beta-synthase).

Pssm-ID: 341375 [Multi-domain] Cd Length: 133 Bit Score: 42.93 E-value: 5.40e-06

                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|.
gi 983192395  77 MYQEVLSVSPELSIIELADMMQVGKPKAYPVID-NKKLVGMITRSDVLRAI 126
Cdd:cd04600    1 MSRDVVTVTPDTSLEEAWRLLRRHRIKALPVVDrARRLVGIVTLADLLKHA 51

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: 42.70 E-value: 5.79e-06

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983192395  11 TKQVVTFTPDMPLSLALDkVMRSPHMGG-PVIDDNEQVIGFLSEQDLLDKLVK------VSYFCQDTH-----IVRDCMY 78
Cdd:cd04632    1 TEEVITVNEDDTIGKAIN-LLREHGISRlPVVDDNGKLVGIVTTYDIVDFVVRpgtktrGGDRGGEKErmldlPVYDIMS 79

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 983192395  79 QEVLSVSPELSIIE-LADMMQVGKPKAYPVIDNKKLVGMITRSDVLRA 125
Cdd:cd04632   80 SPVVTVTRDATVADaVERMLENDISGLVVTPDDNMVIGILTKTDVLRA 127

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: 42.23 E-value: 7.07e-06

                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*....
gi 983192395  79 QEVLSVSPELSIIELADMMQVGKPKAYPVID-NKKLVGMITRSDVLRAI 126
Cdd:cd02205    2 RDVVTVDPDTTVREALELMAENGIGALPVVDdDGKLVGIVTERDILRAL 50

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: 42.02 E-value: 7.25e-06

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983192395  15 VTFTPDMPLSLALDKVMRSPHMGGPVIDDNEQVIGFLSEQDLLdklvkvsyFCQDTHI-VRDCMY-QEVLSVSPE-LSII 91
Cdd:cd04601    5 VTLSPDATVADVLELKAEYGISGVPVTEDGGKLVGIVTSRDIR--------FETDLSTpVSEVMTpDERLVTAPEgITLE 76

                         90       100       110
                 ....*....|....*....|....*....|....
gi 983192395  92 ELADMMQVGKPKAYPVIDNK-KLVGMITRSDVLR 124
Cdd:cd04601   77 EAKEILHKHKIEKLPIVDDNgELVGLITRKDIEK 110

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: 42.13 E-value: 7.45e-06

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983192395   3 SIKVKDYMTKQVVTFTPDMPLSLALDkVMRS---PHMggPVIDDNEQVIGFLSEQDLLDKLVKVSYFCQDThiVRDCMYQ 79
Cdd:cd04608    1 DLIVRRLDLGAPVTVLPDDTLGEAIE-IMREygvDQL--PVVDEDGRVVGMVTEGNLLSSLLAGRAQPSDP--VSKAMYK 75

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 983192395  80 EVLSVSPELSIIELADMMQVGkPKAYPVIDNKKLVGMITRSDVL 123
Cdd:cd04608   76 QFKQVDLDTPLGALSRILERD-HFALVVDGQGKVLGIVTRIDLL 118

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: 41.92 E-value: 8.47e-06

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983192395   9 YMTKQVVTFTPDMPLSLALDKvMRSPHMGGPVI-DDNEQVIGFLSEQDLLDKLVKVSYFCqDTHIvRDCMYQEVLSVSPE 87
Cdd:cd17771    1 LIRREPVTCSPDTPLRAALET-MHERRVGSMVVvDANRRPVGIFTLRDLLSRVALPQIDL-DAPI-SEVMTPDPVRLPPS 77

                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 983192395  88 LSIIELADMMQVGKPKAYPVIDNKKLVGMITRSDVL 123
Cdd:cd17771   78 ASAFEAALLMAEHGFRHVCVVDNGRLVGVVSERDLF 113

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: 42.22 E-value: 1.08e-05

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983192395   6 VKDYMTKQVVTFTPDMPLSLALDKVMRSPHMGGPVID-DNEQVIGFLSEQDLLD--------KLVKVSYfcQDTHI---- 72
Cdd:cd17779    2 IMAIATKDVITIPPTTTIIGAIKTMTEKGFRRLPVADaGTKRLEGIVTSMDIVDflgggskyNLVEKKH--NGNLLaain 79

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 983192395  73 --VRDCMYQEVLSVSPELSIIELADMMQVGKPKAYPVID-NKKLVGMITRSDVLRAI 126
Cdd:cd17779   80 epVREIMTRDVISVKENASIDDAIELMLEKNVGGLPIVDkDGKVIGIVTERDFLKFL 136

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: 1.15e-05

                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 983192395   2 HSIKVKDYMTKQVVTFTPDMPLSLALDKVMRSP--HMggPVIDDNeQVIGFLSEQDLL 57
Cdd:COG2905   63 LDTPVSEVMTRPPITVSPDDSLAEALELMEEHRirHL--PVVDDG-KLVGIVSITDLL 117

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: 40.87 E-value: 2.02e-05

                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 983192395   3 SIKVKDYMTKQVVTFTPDMPLSLALDKvmrsphMGG------PVIDDNEQVIGFLSEQDL 56
Cdd:cd04622   59 TTTVREVMTGDVVTCSPDDDVEEAARL------MAEhqvrrlPVVDDDGRLVGIVSLGDL 112

putative manganese-dependent inorganic diphosphatase;

Pssm-ID: 237843 [Multi-domain] Cd Length: 546 Bit Score: 42.51 E-value: 2.23e-05

                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 983192395  79 QEVLSVSPELSIIELADMMQVGKPKAYPVID-NKKLVGMITRSDVLRAIGKNL-----NE 132
Cdd:PRK14869 255 EDLVTFSKDDYLEDVKEVMLKSRYRSYPVVDeDGKVVGVISRYHLLSPVRKKVilvdhNE 314

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: 40.98 E-value: 2.26e-05

                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 983192395   3 SIKVKDYMTKQVVTFTPDMPLSLALdKVMRSPHMGG-PVIDDNEQVIGFLSEQDLLDK 59
Cdd:cd04588   55 NAKVKDIMTKDVITIDKDEKIYDAI-RLMNKHNIGRlIVVDDNGKPVGIITRTDILKV 111

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: 41.06 E-value: 2.55e-05

                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 983192395  73 VRDCMYQEVLSVSPELSIIELADMMQVGKPKAYPVIDNKKLVGMITRSDVLRAIGKnlNECFKH 136
Cdd:cd04631    2 VEDYMTKNVITATPGTPIEDVAKIMVRNGFRRLPVVSDGKLVGIVTSTDIMRYLGS--GEAFEK 63

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: 40.58 E-value: 3.01e-05

                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 983192395   5 KVKDYMTKQVVTFTPDMPLSLALDKvMRS---PHMggPVIDDNEQVIGFLSEQDLLDKL 60
Cdd:cd09836   60 PVEEIMTKNLVTVSPDESIYEAAEL-MREhniRHL--PVVDGGGKLVGVISIRDLAREL 115

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: 38.65 E-value: 3.78e-05

                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*..
gi 983192395    14 VVTFTPDMPLSLALDKVMRSPHMGGPVIDDNEQVIGFLSEQDLLDKL 60
Cdd:smart00116   2 VVTVSPDTTLEEALELLRENGIRRLPVVDEEGRLVGIVTRRDIIKAL 48

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: 39.79 E-value: 4.65e-05

                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|
gi 983192395  81 VLSVSPELSIIELADMMQVGKPKAYPVIDNKKLVGMITRSDVLRAIGKNL 130
Cdd:cd04595    4 VKTVSPDTTIEEARKIMLRYGHTGLPVVEDGKLVGIISRRDVDKAKHHGL 53

Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with the voltage gated CLC (chloride channel) in archaea; This cd contains two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with the voltage gated CLC voltage-gated chloride channel. The CBS pairs here are found in the EriC CIC-type chloride channels in archaea. These ion channels are proteins with a seemingly simple task of allowing the passive flow of chloride ions across biological membranes. CIC-type chloride channels come from all kingdoms of life, have several gene families, and can be gated by voltage. The members of the CIC-type chloride channel are double-barreled: two proteins forming homodimers at a broad interface formed by four helices from each protein. The two pores are not found at this interface, but are completely contained within each subunit, as deduced from the mutational analyses, unlike many other channels, in which four or five identical or structurally related subunits jointly form one pore. The CBS domain, named after human CBS, is a small domain originally identified in cystathionine beta-synthase and is subsequently found in a wide range of different proteins. CBS domains usually occur in tandem repeats. They associate to form a so-called Bateman domain or a CBS pair based on crystallographic studies in bacteria. The CBS pair was used as a basis for this cd hierarchy since the human CBS proteins can adopt the typical core structure and form an intramolecular CBS pair. The interface between the two CBS domains forms a cleft that is a potential ligand binding site. The CBS pair coexists with a variety of other functional domains and this has been used to help in its classification here. It has been proposed that the CBS domain may play a regulatory role, although its exact function is unknown. Mutations of conserved residues within this domain are associated with a variety of human hereditary diseases, including congenital myotonia, idiopathic generalized epilepsy, hypercalciuric nephrolithiasis, and classic Bartter syndrome (CLC chloride channel family members), Wolff-Parkinson-White syndrome (gamma 2 subunit of AMP-activated protein kinase), retinitis pigmentosa (IMP dehydrogenase-1), and homocystinuria (cystathionine beta-synthase).

Pssm-ID: 341369 [Multi-domain] Cd Length: 107 Bit Score: 39.63 E-value: 5.93e-05

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983192395  19 PDMPLSLALDKVMRSPHMGGPVIDDNEQVIGFLSEQDLLDKlvkvsyfcqDTHIVRDCMYQEVLSVSPELSIIELADMMQ 98
Cdd:cd04594    9 AYDTVERALKIMRENNLLSLPVVDNDSNFLGAVYLRDIENK---------SPGKVGKYVVRGSPYVTPTSSLEEAWEIMM 79

                         90       100
                 ....*....|....*....|....*..
gi 983192395  99 VGKPKAYPVIDNKKLVGMITRSDVLRA 125
Cdd:cd04594   80 RNKSRWVAVVEKGKFLGIITLDDLLEA 106

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: 6.00e-05

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983192395  12 KQVVTFTPDMPLSLALdKVMRSPHMGG-PVIDDNEQVIGFLSEQDLldklvkvsyfcqdTHIVRDCMYQEVL-SVSPELS 89
Cdd:cd04597    5 DKVEPLSPETSIKDAW-NLMDENNLKTlPVTDDNGKLIGLLSISDI-------------ARTVDYIMTKDNLiVFKEDDY 70

                         90       100       110
                 ....*....|....*....|....*....|....*
gi 983192395  90 IIELADMMQVGKPKAYPVIDNK-KLVGMITRSDVL 123
Cdd:cd04597   71 LDEVKEIMLNTNFRNYPVVDENnKFLGTISRKHLI 105

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: 39.04 E-value: 1.06e-04

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983192395  12 KQVVTFTPDMPLSLALdKVMRSPHMGGP-VIDDNEQVIGFLSEQDLLDKLVKVSYfcqdthiVRDCMYQEVLSVSPELSI 90
Cdd:cd04583    2 TNPVTITPERTLAQAI-EIMREKRVDSLlVVDKDNVLLGIVDIEDINRNYRKAKK-------VGEIMERDVFTVKEDSLL 73

                         90       100       110
                 ....*....|....*....|....*....|.
gi 983192395  91 IELADMMQVGKPKAYPVIDN-KKLVGMITRS 120
Cdd:cd04583   74 RDTVDRILKRGLKYVPVVDEqGRLVGLVTRA 104

Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains found in the metalloprotease peptidase M50; This cd contains two tandem repeats of the cystathionine beta-synthase (CBS pair) domains in peptidase M50. Members of the M50 metallopeptidase family include mammalian sterol-regulatory element binding protein (SREBP) site 2 proteases and various hypothetical bacterial homologues. The CBS domain, named after human CBS, is a small domain originally identified in cystathionine beta-synthase and is subsequently found in a wide range of different proteins. CBS domains usually occur in tandem repeats. They associate to form a so-called Bateman domain or a CBS pair based on crystallographic studies in bacteria. The CBS pair was used as a basis for this cd hierarchy since the human CBS proteins can adopt the typical core structure and form an intramolecular CBS pair. The interface between the two CBS domains forms a cleft that is a potential ligand binding site. The CBS pair coexists with a variety of other functional domains and this has been used to help in its classification here. It has been proposed that the CBS domain may play a regulatory role, although its exact function is unknown. Mutations of conserved residues within this domain are associated with a variety of human hereditary diseases, including congenital myotonia, idiopathic generalized epilepsy, hypercalciuric nephrolithiasis, and classic Bartter syndrome (CLC chloride channel family members), Wolff-Parkinson-White syndrome (gamma 2 subunit of AMP-activated protein kinase), retinitis pigmentosa (IMP dehydrogenase-1), and homocystinuria (cystathionine beta-synthase).

Pssm-ID: 341397 [Multi-domain] Cd Length: 120 Bit Score: 39.09 E-value: 1.07e-04

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983192395  39 PVIDDNEQVIGFLSEQDLldKLVKVSYFcQDTHiVRDCM--YQEVLSVSPELSIIELADMMQVGKPKAYPVID-NKKLVG 115
Cdd:cd04639   34 LVTDEAGRLVGLITVDDL--RAIPTSQW-PDTP-VRELMkpLEEIPTVAADQSLLEVVKLLEEQQLPALAVVSeNGTLVG 109

                         90
                 ....*....|.
gi 983192395 116 MITRSDVLRAI 126
Cdd:cd04639  110 LIEKEDIIELL 120

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: 39.13 E-value: 1.18e-04

                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 983192395   3 SIKVKDYMTKQVVTFTPDMPLSLALDKvMRSPHMGG-PVIDDNEqVIGFLSEQDLL 57
Cdd:cd04631   74 NVPISSIMKRDIITTTPDTDLGEAAEL-MLEKNIGAlPVVDDGK-LVGIITERDIL 127

CBS pair domains found in archeal proteins, repeat 2; CBS pair domains found in archeal proteins that contain 2 repeats. The CBS domain, named after human CBS, is a small domain originally identified in cystathionine beta-synthase and is subsequently found in a wide range of different proteins. CBS domains usually occur in tandem repeats. They associate to form a so-called Bateman domain or a CBS pair based on crystallographic studies in bacteria. The CBS pair was used as a basis for this cd hierarchy since the human CBS proteins can adopt the typical core structure and form an intramolecular CBS pair. The interface between the two CBS domains forms a cleft that is a potential ligand binding site. The CBS pair coexists with a variety of other functional domains and this has been used to help in its classification here.

Pssm-ID: 341414 [Multi-domain] Cd Length: 131 Bit Score: 39.24 E-value: 1.45e-04

                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 983192395  73 VRDCMYQEVLSVSPELSIIELADMMQVGKPKAYPVIDNKKLVGMITRSDVLRAIGK 128
Cdd:cd17778    2 VKEFMTTPVVTIYPDDTLKEAMELMVTRGFRRLPVVSGGKLVGIVTAMDIVKYFGS 57

Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains the majority of which are associated with the CorC_HlyC domain; This cd contains two tandem repeats of the cystathionine beta-synthase (CBS pair) domains the majority of which are associated with the CorC_HlyC domain. CorC_HlyC is a transporter associated domain. This small domain is found in Na+/H+ antiporters, in proteins involved in magnesium and cobalt efflux, and in association with some proteins of unknown function. The function of the CorC_HlyC domain is uncertain but it might be involved in modulating transport of ion substrates. These CBS domains are found in highly conserved proteins that either have unknown function or are puported to be hemolysins, exotoxins involved in lysis of red blood cells in vitro. 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: 341366 [Multi-domain] Cd Length: 119 Bit Score: 38.63 E-value: 1.46e-04

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983192395   5 KVKDYMT--KQVVTFTPDMPLSLALDKVMRSPHMGGPVIDDN-EQVIGFLSEQDLLDKLVKvsyfCQDTHIVRDCMyQEV 81
Cdd:cd04590    1 TVREVMTprTDVVALDADATLEELLELILESGYSRFPVYEGDlDNIIGVLHVKDLLAALLE----GREKLDLRALL-RPP 75

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 983192395  82 LSVSPELSIIELADMMQVGKPKAYPVID-NKKLVGMITRSDVL 123
Cdd:cd04590   76 LFVPETTPLDDLLEEFRKERSHMAIVVDeYGGTAGIVTLEDIL 118

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: 38.46 E-value: 1.65e-04

                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|
gi 983192395  77 MYQEVLSVSPELSIIELADMMQVGKPKAYPVIDNKKLVGMITRSDVLRAI 126
Cdd:cd04610    1 MTRDVITVSPDDTVKDVIKLIKETGHDGFPVVDDGKVVGYVTAKDLLGKD 50

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: 38.48 E-value: 1.70e-04

                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....
gi 983192395  75 DCMYQEVLSVSPELSIIELADMMQVGKPKAYPVID-NKKLVGMITRSDVLRAIG 127
Cdd:cd04597    1 DLEYDKVEPLSPETSIKDAWNLMDENNLKTLPVTDdNGKLIGLLSISDIARTVD 54

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: 38.32 E-value: 2.12e-04

                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....
gi 983192395  81 VLSVSPELSIIELADMMQVGKPKAYPVID--NKKLVGMITRSDVLRAIGKNLNE 132
Cdd:cd17772    4 VISVEPDTTIAEAAELMTRYNINALPVVDggTGRLVGIITRQVAEKAIYHGLGD 57

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: 37.80 E-value: 2.79e-04

                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|.
gi 983192395  77 MYQEVLSVSPELSIIELADMMQVGKPKAYPVID-NKKLVGMITRSDVLRAI 126
Cdd:cd04629    1 MTRNPVTLTPDTSILEAVELLLEHKISGAPVVDeQGRLVGFLSEQDCLKAL 51

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: 37.99 E-value: 3.05e-04

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983192395   6 VKDYMTKQVVTFTPDMPLSLAlDKVM---RSPHMggPVIDDNEQVIGFLSEQDlLDKLVKVSYFCqdthiVRDCMYQEVL 82
Cdd:cd04605    2 VEDIMSKDVATIREDISIEEA-AKIMidkNVTHL--PVVSEDGKLIGIVTSWD-ISKAVALKKDS-----LEEIMTRNVI 72

                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 983192395  83 SVSPELSIIELADMMQVGKPKAYPVID-NKKLVGMIT 118
Cdd:cd04605   73 TARPDEPIELAARKMEKHNISALPVVDdDRRVIGIIT 109

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: 37.78 E-value: 3.06e-04

                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 983192395   3 SIKVKDYMTKQVVTFTPDMPLSLALdKVM---RSPHMggPVIDDNeQVIGFLSEQDL 56
Cdd:cd04623   59 DTPVSEIMTRDVVTCTPDDTVEECM-ALMterRIRHL--PVVEDG-KLVGIVSIGDV 111

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: 341367 [Multi-domain] Cd Length: 114 Bit Score: 37.50 E-value: 3.59e-04

                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 983192395  72 IVRDCMYQEVLSVSPELSIIELADMMQVGKPKAYPVIDN---KKLVGMITRSDVLRAIGKNLNEC 133
Cdd:cd04591    1 TAEDVMRPPLTVLARDETVGDIVSVLKTTDHNGFPVVDStesQTLVGFILRSQLILLLEADLRPI 65

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: 37.75 E-value: 3.72e-04

                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 983192395   2 HSIKVKDYMTKQVVTFTPDMPLSLALdKVMRSPHMGG-PVIDDNEQVIGFLSEQDLL 57
Cdd:cd04604   68 LNLPAKDVMTRNPKTISPDALAAEAL-ELMEEHKITVlPVVDEDGKPVGILHLHDLL 123

putative manganese-dependent inorganic diphosphatase;

Pssm-ID: 237843 [Multi-domain] Cd Length: 546 Bit Score: 38.66 E-value: 4.95e-04

                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 983192395   5 KVKDYMTKQVVTFTPDMPLSLALdKVMRSPHMGG-PVIDDNEQVIGFLSEQDLLDKLVKVSY 65
Cdd:PRK14869  69 QVRDLEIDKPVTVSPDTSLKEAW-NLMDENNVKTlPVVDEEGKLLGLVSLSDLARAYMDILD 129

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: 36.83 E-value: 6.89e-04

                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 983192395   3 SIKVKDYMTKQVVTFTPDMPLSLALDKvMRSPHMGG-PVIDDNEQVIGFLSEQDL 56
Cdd:cd04605   60 KDSLEEIMTRNVITARPDEPIELAARK-MEKHNISAlPVVDDDRRVIGIITSDDI 113

IMP dehydrogenase;

Pssm-ID: 180842 [Multi-domain] Cd Length: 502 Bit Score: 38.14 E-value: 8.32e-04

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983192395   5 KVKDYMTKQVV---TFTPDMPLSLALDKVMRSPHMGGPVIDD---NEQVIGFLSEQDLldklvKVSYFCQDTHiVRDCMY 78
Cdd:PRK07107  95 RVKNYKAGFVVsdsNLTPDNTLADVLDLKEKTGHSTVAVTEDgtaHGKLLGIVTSRDY-----RISRMSLDTK-VKDFMT 168

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 983192395  79 Q-EVLSVSPE-LSIIELADMMQVGKPKAYPVID-NKKLVGMITRSD 121
Cdd:PRK07107 169 PfEKLVTANEgTTLKEANDIIWDHKLNTLPIVDkNGNLVYLVFRKD 214

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: 36.36 E-value: 9.54e-04

                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|..
gi 983192395  79 QEVLSVSPELSIIELADMMQVGKPKAYPVIDNKKLVGMITRSDVLRAIGKNL 130
Cdd:cd04588    2 KDLITLKPDATIKDAAKLLSENNIHGAPVVDDGKLVGIVTLTDIAKALAEGK 53

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: 36.39 E-value: 1.02e-03

                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....
gi 983192395   4 IKVKDYMTKQVVTFTPDMPLSLALDKVMRSPHMGGPVIDDNeQVIGFLSEQDLL 57
Cdd:cd17772   58 LPVSEYMTTEFATVTPDAPLSEIQEIIVEQRQRLVPVVEDG-RLVGVITRTDLL 110

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: 1.12e-03

                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 983192395   1 MHSiKVKDYMTKQVVTFTPDMPLSLALDKVMRspHMGG--PVIDDNEqVIGFLSEQDLL 57
Cdd:cd04595   54 GHA-PVKGYMSTNVITIDPDTSLEEAQELMVE--HDIGrlPVVEEGK-LVGIVTRSDVL 108

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: 36.01 E-value: 1.29e-03

                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|...
gi 983192395   5 KVKDYMTKQVVTFTPDMPLSLALdKVMRSPHMGGPVIDDNEQVIGFLSEQDLL 57
Cdd:cd04801   60 RVRDVMTKDVITVSPDADAMEAL-KLMSQNNIGRLPVVEDGELVGIISRTDLM 111

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: 35.48 E-value: 2.00e-03

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983192395  10 MTKQVVTFTPDMPLSLALdKVMRSPHMGGPVIDDNEQVIGFLSEQDLLDKLV--KVSYfcqDTHiVRDCMYQEVLSVSPE 87
Cdd:cd04587    2 MSRPPVTVPPDATIQEAA-QLMSEERVSSLLVVDDGRLVGIVTDRDLRNRVVaeGLDP---DTP-VSEIMTPPPVTIDAD 76

                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 983192395  88 LSIIE-LADMMQVGKpKAYPVIDNKKLVGMITRSDVLRA 125
Cdd:cd04587   77 ALVFEaLLLMLERNI-HHLPVVDDGRVVGVVTATDLMRL 114

voltage-gated chloride channel ClcB;

Pssm-ID: 234987 [Multi-domain] Cd Length: 574 Bit Score: 37.03 E-value: 2.03e-03

                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 983192395   6 VKDYMTKQVVTFTPDMPLSLALDKVMRSPHMGGPVIDD--NEQVIGFLSEQDLLDKLVK 62
Cdd:PRK01862 514 AADYAHTPFPLLTPDMPLGDALEHFMAFQGERLPVVESeaSPTLAGVVYKTSLLDAYRR 572

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: 35.63 E-value: 2.49e-03

                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 983192395   4 IKVKDYMTKQVVTFTPDMPLSLALDKVMRSPHMGGPVID--DNEQVIGFLSEQDLL 57
Cdd:cd04613   60 VVVKDLATTDVITVTPDDDLYTALLKFTSTNLDQLPVVDddDPGKVLGMLSRRDVI 115

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: 341416 [Multi-domain] Cd Length: 106 Bit Score: 35.02 E-value: 2.67e-03

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983192395  11 TKQVVTFTPDMPLSlALDKVMRSPHMGGPVIDDNEQVIGFLSEQDLLDKLVKvsyfcQDTHIVrdCMYQEVLSVSPELSI 90
Cdd:cd17780    1 TTEFVEVDADTRLG-KVRGLFEDENPKGVVVTDDGEYEGVVTERQLLQSHVE-----DDAKVG--ALVRAAPKVDRTEDV 72

                         90       100       110
                 ....*....|....*....|....*....|...
gi 983192395  91 IELADMMQVGKPKAYPVIDNKKLVGMITRSDVL 123
Cdd:cd17780   73 REVARLLVEGGTKVAPVFEGGSLWGVVTADAIL 105

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: 35.33 E-value: 3.55e-03

                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|...
gi 983192395   6 VKDYMTKQVVTFTPDMPLSLALdKVMRSPHMGG-PVIDDNEQVIGFLSEQDLL 57
Cdd:cd04614   97 VKDVMTKDVVTAFPSSTVSEAA-KKMIRNDIEQlPVVSGEGDLAGMLRDVDLL 148

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: 34.23 E-value: 7.45e-03

                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 983192395   1 MHSIKVKDYMTKQVVTFTPDMPLSLALDKVMRSPHMGGPVIDDNEQVIGFLSEQDLLD 58
Cdd:cd04632   69 MLDLPVYDIMSSPVVTVTRDATVADAVERMLENDISGLVVTPDDNMVIGILTKTDVLR 126