cyclic di-AMP binding protein CbpA; The founding member of this family, Lmo0553 from Listeria monocytogenes, now called CbpA, binds cyclic di-AMP, a signaling molecule, through its CBS (cystathionine-beta-synthase ) domain.

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489739771   1 MLLKTLVKPKERLVTITADATLEDALKVLEDSGFRCIPILDETGHIFRGNIYKMHIYRHKSRGGDMSLPVTTLLKNATKT 80
Cdd:NF038387   1 MLLKSLVKPKEDLTTVKEDATLEEALKILEDSGYRCVPILDETGKIFRGNIYKMHIYRHKSRGGDMSLPVTHLLKNATKF 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489739771  81 IQVDSAFYNIFFSIKDLPYIAVLDEHGYFYGILTHTRLLDMLSQSWNVNVGSYVLTVVSVGERGDLAAMAKIITKYTSIA 160
Cdd:NF038387  81 ISVNSSFFKVFFTIKDLPYIAVLDENNHFYGILTHSSLLNMLSQSWNVNTGSYVLTVASSGERGDLAKMAKIITKYTSIA 160

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
gi 489739771 161 GCLTLDVQNGTLGYRTLFTLPENVDSEKLKRIIDNLNRKQFKVIEVEDL 209
Cdd:NF038387 161 SCITLDEQSDELVRRTLFTLPAGVDEETLDKIVSRLERKGFRVVEIEDL 209

cyclic di-AMP binding protein CbpA; The founding member of this family, Lmo0553 from Listeria monocytogenes, now called CbpA, binds cyclic di-AMP, a signaling molecule, through its CBS (cystathionine-beta-synthase ) domain.

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489739771   1 MLLKTLVKPKERLVTITADATLEDALKVLEDSGFRCIPILDETGHIFRGNIYKMHIYRHKSRGGDMSLPVTTLLKNATKT 80
Cdd:NF038387   1 MLLKSLVKPKEDLTTVKEDATLEEALKILEDSGYRCVPILDETGKIFRGNIYKMHIYRHKSRGGDMSLPVTHLLKNATKF 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489739771  81 IQVDSAFYNIFFSIKDLPYIAVLDEHGYFYGILTHTRLLDMLSQSWNVNVGSYVLTVVSVGERGDLAAMAKIITKYTSIA 160
Cdd:NF038387  81 ISVNSSFFKVFFTIKDLPYIAVLDENNHFYGILTHSSLLNMLSQSWNVNTGSYVLTVASSGERGDLAKMAKIITKYTSIA 160

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
gi 489739771 161 GCLTLDVQNGTLGYRTLFTLPENVDSEKLKRIIDNLNRKQFKVIEVEDL 209
Cdd:NF038387 161 SCITLDEQSDELVRRTLFTLPAGVDEETLDKIVSRLERKGFRVVEIEDL 209

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

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489739771  10 KERLVTITADATLEDALKVLEDSGFRCIPILDETGHiFRGNIYKMHIYRHKSRGGD-MSLPVTTLLKNATKTIQVDSAFY 88
Cdd:cd02205    1 TRDVVTVDPDTTVREALELMAENGIGALPVVDDDGK-LVGIVTERDILRALVEGGLaLDTPVAEVMTPDVITVSPDTDLE 79

                         90       100       110
                 ....*....|....*....|....*....|....
gi 489739771  89 NIF--FSIKDLPYIAVLDEHGYFYGILTHTRLLD 120
Cdd:cd02205   80 EALelMLEHGIRRLPVVDDDGKLVGIVTRRDILR 113

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.

                           10        20        30
                   ....*....|....*....|....*....|....*
gi 489739771    12 RLVTITADATLEDALKVLEDSGFRCIPILDETGHI 46
Cdd:smart00116   1 DVVTVSPDTTLEEALELLRENGIRRLPVVDEEGRL 35

cyclic di-AMP binding protein CbpA; The founding member of this family, Lmo0553 from Listeria monocytogenes, now called CbpA, binds cyclic di-AMP, a signaling molecule, through its CBS (cystathionine-beta-synthase ) domain.

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489739771   1 MLLKTLVKPKERLVTITADATLEDALKVLEDSGFRCIPILDETGHIFRGNIYKMHIYRHKSRGGDMSLPVTTLLKNATKT 80
Cdd:NF038387   1 MLLKSLVKPKEDLTTVKEDATLEEALKILEDSGYRCVPILDETGKIFRGNIYKMHIYRHKSRGGDMSLPVTHLLKNATKF 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489739771  81 IQVDSAFYNIFFSIKDLPYIAVLDEHGYFYGILTHTRLLDMLSQSWNVNVGSYVLTVVSVGERGDLAAMAKIITKYTSIA 160
Cdd:NF038387  81 ISVNSSFFKVFFTIKDLPYIAVLDENNHFYGILTHSSLLNMLSQSWNVNTGSYVLTVASSGERGDLAKMAKIITKYTSIA 160

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
gi 489739771 161 GCLTLDVQNGTLGYRTLFTLPENVDSEKLKRIIDNLNRKQFKVIEVEDL 209
Cdd:NF038387 161 SCITLDEQSDELVRRTLFTLPAGVDEETLDKIVSRLERKGFRVVEIEDL 209

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

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489739771  10 KERLVTITADATLEDALKVLEDSGFRCIPILDETGHiFRGNIYKMHIYRHKSRGGD-MSLPVTTLLKNATKTIQVDSAFY 88
Cdd:cd02205    1 TRDVVTVDPDTTVREALELMAENGIGALPVVDDDGK-LVGIVTERDILRALVEGGLaLDTPVAEVMTPDVITVSPDTDLE 79

                         90       100       110
                 ....*....|....*....|....*....|....
gi 489739771  89 NIF--FSIKDLPYIAVLDEHGYFYGILTHTRLLD 120
Cdd:cd02205   80 EALelMLEHGIRRLPVVDDDGKLVGIVTRRDILR 113

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

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489739771  12 RLVTITADATLEDALKVLEDSGFRCIPILDetGHIFRGNIYKMHIYRHKSRGGD-MSLPVTTLLKNATKTIQVDSAFYNI 90
Cdd:COG2524   95 DVITVSPDTTLEEALELMLEKGISGLPVVD--DGKLVGIITERDLLKALAEGRDlLDAPVSDIMTRDVVTVSEDDSLEEA 172

                         90       100       110
                 ....*....|....*....|....*....|....
gi 489739771  91 F--FSIKDLPYIAVLDEHGYFYGILTHTRLLDML 122
Cdd:COG2524  173 LrlMLEHGIGRLPVVDDDGKLVGIITRTDILRAL 206

CBS domain; CBS domains are small intracellular modules that pair together to form a stable globular domain. This family represents a single CBS domain. Pairs of these domains have been termed a Bateman domain. CBS domains have been shown to bind ligands with an adenosyl group such as AMP, ATP and S-AdoMet. CBS domains are found attached to a wide range of other protein domains suggesting that CBS domains may play a regulatory role making proteins sensitive to adenosyl carrying ligands. The region containing the CBS domains in Cystathionine-beta synthase is involved in regulation by S-AdoMet. CBS domain pairs from AMPK bind AMP or ATP. The CBS domains from IMPDH and the chloride channel CLC2 bind ATP.

                          10        20        30
                  ....*....|....*....|....*....|....*...
gi 489739771    9 PKERLVTITADATLEDALKVLEDSGFRCIPILDETGHI 46
Cdd:pfam00571   5 MTKDVVTVSPDTTLEEALELMREHGISRLPVVDEDGKL 42

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

                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 489739771   1 MLLKTLVKPKERLVTITADATLEDALKVLEDSGFRCIPILDETGH----IFRGNIYKM 54
Cdd:cd04639   62 TPVRELMKPLEEIPTVAADQSLLEVVKLLEEQQLPALAVVSENGTlvglIEKEDIIEL 119

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).

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489739771  13 LVTITADATLEDALKVLEDSGFRCIPILDETGH----IFRGNIYKmHIYRHKSRggdMSLPVTTLLKNATKTIQVD---S 85
Cdd:cd04608   12 PVTVLPDDTLGEAIEIMREYGVDQLPVVDEDGRvvgmVTEGNLLS-SLLAGRAQ---PSDPVSKAMYKQFKQVDLDtplG 87

                         90       100       110
                 ....*....|....*....|....*....|....*
gi 489739771  86 AFYNIFfsiKDLPYIAVLDEHGYFYGILTHTRLLD 120
Cdd:cd04608   88 ALSRIL---ERDHFALVVDGQGKVLGIVTRIDLLN 119

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).

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489739771  13 LVTITADATLEDALKVLEDSGFRCIPILDETGHI--------------------FRGNIYKMHIYRHKSRG--GD-MSLP 69
Cdd:cd04600    5 VVTVTPDTSLEEAWRLLRRHRIKALPVVDRARRLvgivtladllkhadldpprgLRGRLRRTLGLRRDRPEtvGDiMTRP 84

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 489739771  70 VTTLLKNA--TKTIQVdsafynifFSIKDLPYIAVLDEHGYFYGILTHTRLL 119
Cdd:cd04600   85 VVTVRPDTpiAELVPL--------FSDGGLHHIPVVDADGRLVGIVTQSDLI 128

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

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489739771  11 ERLVTITADATLEDALKVLEDSGFRCIPILDETGH---IF-RGNIykmhIYRHKSRGGD---------MSLPVTTLLKNA 77
Cdd:COG2905    7 RDVVTVSPDATVREAARLMTEKGVGSLVVVDDDGRlvgIItDRDL----RRRVLAEGLDpldtpvsevMTRPPITVSPDD 82

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|
gi 489739771  78 TktiqVDSAFyNIF--FSIKDLPyiaVLDEhGYFYGILTHTRLLDMLSQS 125
Cdd:COG2905   83 S----LAEAL-ELMeeHRIRHLP---VVDD-GKLVGIVSITDLLRALSEE 123

inosine-5'-monophosphate dehydrogenase; Provisional

                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 489739771   1 MLLKTLVKPKERLVTITADATLEDALKVLEDSGFRCIPILDETGHIF----RGNIYKMHIYRHKSRGGDMSLPV 70
Cdd:PTZ00314 159 TPVSEVMTPREKLVVGNTPISLEEANEVLRESRKGKLPIVNDNGELValvsRSDLKKNRGYPNASLDSNGQLLV 232

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).

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489739771   9 PKERLVTITADATLEDALKVLEDSGFRCIPILDETGHIFRGNIYKMHIYRHkSRGGDMSLPVTTLLKNATK---TIQVDS 85
Cdd:cd04590    8 PRTDVVALDADATLEELLELILESGYSRFPVYEGDLDNIIGVLHVKDLLAA-LLEGREKLDLRALLRPPLFvpeTTPLDD 86

                         90       100
                 ....*....|....*....|....*....
gi 489739771  86 AFynIFFSIKDLPYIAVLDEHGYFYGILT 114
Cdd:cd04590   87 LL--EEFRKERSHMAIVVDEYGGTAGIVT 113