NCBI Conserved Domain Search

HPP family; These proteins are integral membrane proteins with four transmembrane spanning helices. The most conserved region of the alignment is a motif HPP. The function of these proteins is uncertain but they may be transporters.

Pssm-ID: 461506 Cd Length: 122 Bit Score: 161.14 E-value: 5.15e-49

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736698752   54 IAPMGASSVLLFAVPASPLAQPWNILVGNTIAAVVGVTCALFIASPTEAFS--LAVALAIILMMTTDSLHPPSGAVAITA 131
Cdd:pfam04982   2 IASFGASAVLLFGAPESPLAQPRNVVGGHLISALIGVAIAKLFGLSLLWLAaaLAVALAIALMQLTRTLHPPAGATALLA 81

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 736698752  132 VLGGnAVHELGYAFVFYPVLLNSILLMVIAIVFNRMIGKRYP 173
Cdd:pfam04982  82 VLGG-PIHALGWWFVLVPVLLGSLLLVLVALLVNNLTGRRYP 122

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

Pssm-ID: 442671 [Multi-domain] Cd Length: 136 Bit Score: 121.13 E-value: 1.66e-33

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736698752 236 TCQDIMTKDVVTLHANDNIQHALDKFKEMNLMSLPVVNAEGKLVGTLAMYQVVEWFKRAADVRSSWE---HQVKHIMTRK 312
Cdd:COG3448    3 TVRDIMTRDVVTVSPDTTLREALELMREHGIRGLPVVDEDGRLVGIVTERDLLRALLPDRLDELEERlldLPVEDVMTRP 82

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|...
gi 736698752 313 VVTVQPLQPIQDLVPYFVERSFNYIPVVSEQ-RLVGIISRADIIAALNQELNH 364
Cdd:COG3448   83 VVTVTPDTPLEEAAELMLEHGIHRLPVVDDDgRLVGIVTRTDLLRALARLLEE 135

CBS domain [Signal transduction mechanisms];

Pssm-ID: 440283 [Multi-domain] Cd Length: 128 Bit Score: 102.25 E-value: 1.95e-26

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736698752 238 QDIMTKDVVTLHANDNIQHALDKFKEMNLMSLPVVNAEGKLVGTLAMYQVVewFKRAADVRSSWEHQVKHIMTRKVVTVQ 317
Cdd:COG0517    4 KDIMTTDVVTVSPDATVREALELMSEKRIGGLPVVDEDGKLVGIVTDRDLR--RALAAEGKDLLDTPVSEVMTRPPVTVS 81

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 736698752 318 PLQPIQDLVPYFVERSFNYIPVVSEQ-RLVGIISRADIIAALNQEL 362
Cdd:COG0517   82 PDTSLEEAAELMEEHKIRRLPVVDDDgRLVGIITIKDLLKALLEPL 127

Predicted transcriptional regulator containing CBS domains [Transcription];

Pssm-ID: 443285 [Multi-domain] Cd Length: 135 Bit Score: 96.91 E-value: 2.13e-24

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736698752 239 DIMT-KDVVTLHANDNIQHALDKFKEMNLMSLPVVNAEGKLVGTLAMyqvvewfkraADVRSSWEH-QVKHIMTRKVVTV 316
Cdd:COG4109   20 DIMTlEDVATLSEDDTVEDALELLEKTGHSRFPVVDENGRLVGIVTS----------KDILGKDDDtPIEDVMTKNPITV 89

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 736698752 317 QPLQPIQDLVPYFVERSFNYIPVVSEQ-RLVGIISRADIIAALNQ 360
Cdd:COG4109   90 TPDTSLASAAHKMIWEGIELLPVVDDDgRLLGIISRQDVLKALQK 134

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: 95.71 E-value: 5.14e-24

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736698752 241 MTKDVVTLHANDNIQHALDKFKEMNLMSLPVVNAEGKLVG-----------TLAMYQVVEWFKRAADVRSSWEHQ-VKHI 308
Cdd:cd04600    1 MSRDVVTVTPDTSLEEAWRLLRRHRIKALPVVDRARRLVGivtladllkhaDLDPPRGLRGRLRRTLGLRRDRPEtVGDI 80

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|.
gi 736698752 309 MTRKVVTVQPLQPIQDLVPYFVERSFNYIPVV-SEQRLVGIISRADIIAAL 358
Cdd:cd04600   81 MTRPVVTVRPDTPIAELVPLFSDGGLHHIPVVdADGRLVGIVTQSDLIAAL 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: 95.57 E-value: 6.09e-24

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736698752 241 MTKDVVTLHANDNIQHALDKFKEMNLMSLPVVNAEGKLVG------------TLAMYQVVEWF--------KRAADVRSS 300
Cdd:cd04586    1 MTTDVVTVTPDTSVREAARLLLEHRISGLPVVDDDGKLVGivsegdllrreePGTEPRRVWWLdallespeRLAEEYVKA 80

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 736698752 301 WEHQVKHIMTRKVVTVQPLQPIQDLVPYFVERSFNYIPVVSEQRLVGIISRADIIAA 357
Cdd:cd04586   81 HGRTVGDVMTRPVVTVSPDTPLEEAARLMERHRIKRLPVVDDGKLVGIVSRADLLRA 137

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: 94.80 E-value: 1.22e-23

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736698752 239 DIMTKDVVTLHANDNIQHALDKFKEMNLMSLPVVNaEGKLVGTL-------AMYQVVEWFKRAADVRSSWEHQVKHIMTR 311
Cdd:cd04584    4 DIMTKNVVTVTPDTSLAEARELMKEHKIRHLPVVD-DGKLVGIVtdrdllrASPSKATSLSIYELNYLLSKIPVKDIMTK 82

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 736698752 312 KVVTVQPLQPIQDLVPYFVERSFNYIPVVSEQRLVGIISRADIIAAL 358
Cdd:cd04584   83 DVITVSPDDTVEEAALLMLENKIGCLPVVDGGKLVGIITETDILRAF 129

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

Pssm-ID: 442013 [Multi-domain] Cd Length: 206 Bit Score: 94.95 E-value: 6.16e-23

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736698752 216 LQKIILEAQDRANARAVNQFTCQDIMTKDVVTLHANDNIQHALDKFKEMNLMSLPVVNaEGKLVGTLAMYQVVEWFkraA 295
Cdd:COG2524   67 LQAAAVRVVAEKELGLVLKMKVKDIMTKDVITVSPDTTLEEALELMLEKGISGLPVVD-DGKLVGIITERDLLKAL---A 142

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 736698752 296 DVRSSWEHQVKHIMTRKVVTVQPLQPIQDLVPYFVERSFNYIPVV-SEQRLVGIISRADIIAAL 358
Cdd:COG2524  143 EGRDLLDAPVSDIMTRDVVTVSEDDSLEEALRLMLEHGIGRLPVVdDDGKLVGIITRTDILRAL 206

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

Pssm-ID: 341358 [Multi-domain] Cd Length: 113 Bit Score: 88.07 E-value: 2.47e-21

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736698752 242 TKDVVTLHANDNIQHALDKFKEMNLMSLPVVNAEGKLVGTLAMYQVVewfKRAADVRSSWEHQVKHIMTRKVVTVQPLQP 321
Cdd:cd02205    1 TRDVVTVDPDTTVREALELMAENGIGALPVVDDDGKLVGIVTERDIL---RALVEGGLALDTPVAEVMTPDVITVSPDTD 77

                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 736698752 322 IQDLVPYFVERSFNYIPVVSEQ-RLVGIISRADIIA 356
Cdd:cd02205   78 LEEALELMLEHGIRRLPVVDDDgKLVGIVTRRDILR 113

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

Pssm-ID: 442149 [Multi-domain] Cd Length: 124 Bit Score: 87.58 E-value: 4.19e-21

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736698752 238 QDIMTKDVVTLHANDNIQHALDKFKEMNLMSLPVVNAEGKLVGTLAMYQVVEwfKRAADVRSSWEHQVKHIMTRKVVTVQ 317
Cdd:COG2905    2 KDIMSRDVVTVSPDATVREAARLMTEKGVGSLVVVDDDGRLVGIITDRDLRR--RVLAEGLDPLDTPVSEVMTRPPITVS 79

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 736698752 318 PLQPIQDLVPYFVERSFNYIPVVSEQRLVGIISRADIIAALNQEL 362
Cdd:COG2905   80 PDDSLAEALELMEEHRIRHLPVVDDGKLVGIVSITDLLRALSEEL 124

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: 87.11 E-value: 4.95e-21

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736698752 241 MTKDVVTLHANDNIQHALDKFKEMNLMSLPVVNAEGKLVGTL-----------AMYQvvewfkraadvrSSWEHQVKHIM 309
Cdd:cd04629    1 MTRNPVTLTPDTSILEAVELLLEHKISGAPVVDEQGRLVGFLseqdclkalleASYH------------CEPGGTVADYM 68

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 736698752 310 TRKVVTVQPLQPIQDLVPYFVERSFNYIPVVSEQRLVGIISRADIIAA 357
Cdd:cd04629   69 STEVLTVSPDTSIVDLAQLFLKNKPRRYPVVEDGKLVGQISRRDVLRA 116

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: 71.98 E-value: 1.75e-15

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736698752 240 IMTKDVVTLHANDNIQHALDKFKEM-----NLMSLPVVNAEGKLVGTLAMYQVVewfkRAADvrsswEHQVKHIMTRKVV 314
Cdd:cd04606    6 LMTTEFVAVRPDWTVEEALEYLRRLapdpeTIYYIYVVDEDRRLLGVVSLRDLL----LADP-----DTKVSDIMDTDVI 76

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 736698752 315 TVQPLQPIQDLVPYFVERSFNYIPVV-SEQRLVGIISRADII 355
Cdd:cd04606   77 SVSADDDQEEVARLFAKYDLLALPVVdEEGRLVGIITVDDVL 118

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: 70.14 E-value: 6.59e-15

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736698752 243 KDVVTLHANDNIQHALDKFKEMNLMSLPVVNAEGKLVGTLA----MYQVVEwfkRAADVRsswEHQVKHIMTRKVVTVQP 318
Cdd:cd04623    2 RDVVTVSPDATVAEALRLLAEKNIGALVVVDDGGRLVGILSerdyVRKLAL---RGASSL---DTPVSEIMTRDVVTCTP 75

                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 736698752 319 LQPIQDLVPYFVERSFNYIPVVSEQRLVGIISRADII 355
Cdd:cd04623   76 DDTVEECMALMTERRIRHLPVVEDGKLVGIVSIGDVV 112

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: 69.28 E-value: 1.69e-14

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736698752 242 TKDVVTLHANDNIQHALDKFKEMNLMSLPVVNAEGKLVGTLAMYQVVEWFKR------AADVRSSWEHQ----VKHIMTR 311
Cdd:cd04632    1 TEEVITVNEDDTIGKAINLLREHGISRLPVVDDNGKLVGIVTTYDIVDFVVRpgtktrGGDRGGEKERMldlpVYDIMSS 80

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 736698752 312 KVVTVQPLQPIQDLVPYFVERSFNYIPVVSEQRLV-GIISRADIIAA 357
Cdd:cd04632   81 PVVTVTRDATVADAVERMLENDISGLVVTPDDNMViGILTKTDVLRA 127

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

Pssm-ID: 441840 [Multi-domain] Cd Length: 443 Bit Score: 73.95 E-value: 2.08e-14

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736698752 195 PQDIQEVL-----DQQTELLDISEYDLQKIILEAQDRANARAVNQF------TCQDIMTKDVVTLHANDNIQHALDKFKE 263
Cdd:COG2239   78 DEELAELLeeldpDDAADLLEELPEEVVEELLALLDPEEREEIRELlsypedSAGRLMTTEFVAVREDWTVGEALRYLRR 157

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736698752 264 M-----NLMSLPVVNAEGKLVGTLAMYQVvewfkraadVRSSWEHQVKHIMTRKVVTVQPLQPIQDLVPYFVERSFNYIP 338
Cdd:COG2239  158 QaedpeTIYYIYVVDDDGRLVGVVSLRDL---------LLADPDTKVSDIMDTDVISVPADDDQEEVARLFERYDLLALP 228

                        170       180
                 ....*....|....*....|....
gi 736698752 339 VV-SEQRLVGIISRADIIAALNQE 361
Cdd:COG2239  229 VVdEEGRLVGIITVDDVVDVIEEE 252

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: 68.52 E-value: 2.66e-14

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736698752 241 MTKDVVTLHANDNIQHALDKFKEMNLMSLPVVNAE-GKLVGTLAmyqvvewfkRAADVRSSWEHQVKHIMTRKVVTVQPL 319
Cdd:cd04638    1 MTKDVVTVTLPGTRDDVLEILKKKAISGVPVVKKEtGKLVGIVT---------RKDLLRNPDEEQIALLMSRDPITISPD 71

                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 736698752 320 QPIQDLVPYFVERSFNYIPVVSEQRLVGIISRADIIAA 357
Cdd:cd04638   72 DTLSEAAELMLEHNIRRVPVVDDDKLVGIVTVADLVRA 109

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: 67.99 E-value: 4.20e-14

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736698752 241 MTKDVVTLHANDNIQHALDKFKEMNLMSLPVVNAEGKLVGTLAMYqvvewfkraaDVRS-----SWEHQV--KHIMTRKV 313
Cdd:cd04613    1 MPRKVTVLPEGMTFRQFTEFIAGTRQHYFPVVDEQGRLTGILSIQ----------DVRGvlfeeELWDLVvvKDLATTDV 70

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*....
gi 736698752 314 VTVQPLQPIQDLVPYFVERSFNYIPVVSEQ---RLVGIISRADIIAALN 359
Cdd:cd04613   71 ITVTPDDDLYTALLKFTSTNLDQLPVVDDDdpgKVLGMLSRRDVIAAYN 119

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: 67.93 E-value: 4.37e-14

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736698752 241 MTKDVVTLHANDNIQHALDKFKEMNLMSLPVVNAEGKLVGTLAMYQVVewfkRAADVRSSWEHQVKHIMTRKVVTVQPLQ 320
Cdd:cd09836    1 MSKPVVTVPPETTIREAAKLMAENNIGSVVVVDDDGKPVGIVTERDIV----RAVAEGIDLDTPVEEIMTKNLVTVSPDE 76

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 736698752 321 PIQDLVPYFVERSFNYIPVV-SEQRLVGIISRADIIAALN 359
Cdd:cd09836   77 SIYEAAELMREHNIRHLPVVdGGGKLVGVISIRDLARELS 116

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

Pssm-ID: 442671 [Multi-domain] Cd Length: 136 Bit Score: 67.97 E-value: 7.74e-14

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736698752 201 VLDQQTELL-DISEYDLQKIILEAQDRANARAVNQFTCQDIMTKDVVTLHANDNIQHALDKFKEMNLMSLPVVNAEGKLV 279
Cdd:COG3448   38 VVDEDGRLVgIVTERDLLRALLPDRLDELEERLLDLPVEDVMTRPVVTVTPDTPLEEAAELMLEHGIHRLPVVDDDGRLV 117


                 .
gi 736698752 280 G 280
Cdd:COG3448  118 G 118

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

Pssm-ID: 442013 [Multi-domain] Cd Length: 206 Bit Score: 67.60 E-value: 4.57e-13

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736698752  95 FIASPTEAFSLAVALAIILMMTTDSLHPPSGAVAITAVLGGNAVHELGYAFVFYPVLLNSILLMVIAIVFNRMIGKRYPQ 174
Cdd:COG2524    1 LLVLLLLALSLLLPLLAVVLAALLLLAALVLALTAAAAATVLLLAAAAAAAGAGGLGLLLLLLLIVLQAAAVRVVAEKEL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736698752 175 QAQLNTRSKDPTPTQKVTIQPQD-IQEVLDQQTEL-------LD-------ISEYDLQKIILEAQDRANARAvnqftcQD 239
Cdd:COG2524   81 GLVLKMKVKDIMTKDVITVSPDTtLEEALELMLEKgisglpvVDdgklvgiITERDLLKALAEGRDLLDAPV------SD 154

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|...
gi 736698752 240 IMTKDVVTLHANDNIQHALDKFKEMNLMSLPVVNAEGKLVGTL 282
Cdd:COG2524  155 IMTRDVVTVSEDDSLEEALRLMLEHGIGRLPVVDDDGKLVGII 197

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: 64.83 E-value: 4.74e-13

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736698752 245 VVTLHANDNIQHALDKFKEMNLMSLPVVNaEGKLVGTLAmyqvvewfKRaaDVRSSWEHQ-----VKHIMTRKVVTVQPL 319
Cdd:cd04595    4 VKTVSPDTTIEEARKIMLRYGHTGLPVVE-DGKLVGIIS--------RR--DVDKAKHHGlghapVKGYMSTNVITIDPD 72

                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 736698752 320 QPIQDLVPYFVERSFNYIPVVSEQRLVGIISRADII 355
Cdd:cd04595   73 TSLEEAQELMVEHDIGRLPVVEEGKLVGIVTRSDVL 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: 64.51 E-value: 6.39e-13

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736698752 239 DIMTKDVVTLHANDNIQHALDKFKEMNLMSLPVVNaEGKLVG--TLAMYQVVEWFKRAAdvrssweHQVKHIMTRKVVTV 316
Cdd:cd04801    1 DIMTPEVVTVTPEMTVSELLDRMFEEKHLGYPVVE-NGRLVGivTLEDIRKVPEVEREA-------TRVRDVMTKDVITV 72

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 736698752 317 QPLQPIQDLVPYFVERSFNYIPVVSEQRLVGIISRADIIAA 357
Cdd:cd04801   73 SPDADAMEALKLMSQNNIGRLPVVEDGELVGIISRTDLMRA 113

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: 64.75 E-value: 6.43e-13

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736698752 241 MTKDVVTLHANDNIQHALDKFKEMNLMSLPVVNaEGKLVGTL-----AMyqvvewfkRA-ADVRSSWEHQVKHIMTRKVV 314
Cdd:cd04622    1 MTRDVVTVSPDTTLREAARLMRDLDIGALPVCE-GDRLVGMVtdrdiVV--------RAvAEGKDPNTTTVREVMTGDVV 71

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 736698752 315 TVQPLQPIQDLVPYFVERSFNYIPVV-SEQRLVGIISRADI 354
Cdd:cd04622   72 TCSPDDDVEEAARLMAEHQVRRLPVVdDDGRLVGIVSLGDL 112

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: 64.26 E-value: 7.53e-13

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736698752 241 MTKDVVTLHANDNIQHALDKFKEMNLMSLPVVNaEGKLVGtlamyqvvewFKRAAD-VRSSWEHQVKHIMTRKVVTVQPL 319
Cdd:cd04610    1 MTRDVITVSPDDTVKDVIKLIKETGHDGFPVVD-DGKVVG----------YVTAKDlLGKDDDEKVSEIMSRDTVVADPD 69

                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 736698752 320 QPIQDLVPYFVERSFNYIPVV-SEQRLVGIISRADII 355
Cdd:cd04610   70 MDITDAARVIFRSGISKLPVVdDEGNLVGIITNMDVI 106

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: 64.08 E-value: 8.93e-13

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736698752 243 KDVVTLHANDNIQHALDKFKEMNLMSLPVVNAEGKLVGtlamYQVVEWFKRAADvrssWEHQVKHIMTRKVVTVQPLQPI 322
Cdd:cd04583    2 TNPVTITPERTLAQAIEIMREKRVDSLLVVDKDNVLLG----IVDIEDINRNYR----KAKKVGEIMERDVFTVKEDSLL 73

                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 736698752 323 QDLVPYFVERSFNYIPVVSEQ-RLVGIISRADIIAAL 358
Cdd:cd04583   74 RDTVDRILKRGLKYVPVVDEQgRLVGLVTRASLVDIV 110

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: 63.80 E-value: 1.47e-12

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736698752 239 DIMTKDVVTLHANDNIQHALDKFKEMNLMSLPVVNAEGKLVGTlamyqVVEW--FKRAADVRSSwehqVKHIMTRKVVTV 316
Cdd:cd04605    4 DIMSKDVATIREDISIEEAAKIMIDKNVTHLPVVSEDGKLIGI-----VTSWdiSKAVALKKDS----LEEIMTRNVITA 74

                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 736698752 317 QPLQPIQDLVPYFVERSFNYIPVVSEQ-RLVGIISRADI 354
Cdd:cd04605   75 RPDEPIELAARKMEKHNISALPVVDDDrRVIGIITSDDI 113

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: 63.40 E-value: 2.83e-12

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736698752 236 TCQDIMTKDVVTLHANDNIQHALdkfKEM---NLMSLPVVNaEGKLVGTLAMYQVVEWF--KRA------ADVRSSWEHQ 304
Cdd:cd04631    1 VVEDYMTKNVITATPGTPIEDVA---KIMvrnGFRRLPVVS-DGKLVGIVTSTDIMRYLgsGEAfeklktGNIHEVLNVP 76

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....
gi 736698752 305 VKHIMTRKVVTVQPLQPIQDLVPYFVERSFNYIPVVSEQRLVGIISRADIIAAL 358
Cdd:cd04631   77 ISSIMKRDIITTTPDTDLGEAAELMLEKNIGALPVVDDGKLVGIITERDILRAI 130

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

Pssm-ID: 341374 [Multi-domain] Cd Length: 107 Bit Score: 61.20 E-value: 9.31e-12

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736698752 241 MTKDVVTLHANDNIQHALDKFKEMNLMSLPVVNaEGKLVGTLAmyqvvewfkrAADVRSSWEHQ-VKHIMTRKVVTVQP- 318
Cdd:cd04599    1 MTRNPITISPLDSVARAAALMERQRIGGLPVVE-NGKLVGIIT----------SRDVRRAHPNRlVADAMSRNVVTISPe 69

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 736698752 319 ---LQPIQDLVPYFVERsfnyIPVVSEQRLVGIISRADIIAA 357
Cdd:cd04599   70 aslWEAKELMEEHGIER----LVVVEEGRLVGIITKSTLYLE 107

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: 60.66 E-value: 1.62e-11

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736698752 242 TKDVVTLHANDNIQHALDKFKEMNLMSLPVVN-AEGKLVGTLAmYQVVEwfkRAA-----DVrsswehQVKHIMTRKVVT 315
Cdd:cd17772    1 SSPVISVEPDTTIAEAAELMTRYNINALPVVDgGTGRLVGIIT-RQVAE---KAIyhglgDL------PVSEYMTTEFAT 70

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 736698752 316 VQPLQPIQDLVPYFVERSFNYIPVVSEQRLVGIISRADII 355
Cdd:cd17772   71 VTPDAPLSEIQEIIVEQRQRLVPVVEDGRLVGVITRTDLL 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: 59.85 E-value: 3.09e-11

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736698752 236 TCQDIMTKDVVTLHANDNIQHALDKFKEMNLMSLPVVNAEGKLVGTLA----MYQVVEwfkraadVRSSWEHQVKHIMTR 311
Cdd:cd04608    3 IVRRLDLGAPVTVLPDDTLGEAIEIMREYGVDQLPVVDEDGRVVGMVTegnlLSSLLA-------GRAQPSDPVSKAMYK 75

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 736698752 312 KVVTVQPLQPIQDLVPYFvERSFNYIPVVSEQRLVGIISRADIIAA 357
Cdd:cd04608   76 QFKQVDLDTPLGALSRIL-ERDHFALVVDGQGKVLGIVTRIDLLNY 120

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: 60.32 E-value: 3.71e-11

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736698752 239 DIMTKDVVTLHANDNIQHALDKFKEMNLMSLPVVNA-EGKLVGTLAMYQVVEWF---KRAADVRSSWEH--------QVK 306
Cdd:cd17779    4 AIATKDVITIPPTTTIIGAIKTMTEKGFRRLPVADAgTKRLEGIVTSMDIVDFLgggSKYNLVEKKHNGnllaainePVR 83

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|...
gi 736698752 307 HIMTRKVVTVQPLQPIQDLVPYFVERSFNYIPVV-SEQRLVGIISRADIIAAL 358
Cdd:cd17779   84 EIMTRDVISVKENASIDDAIELMLEKNVGGLPIVdKDGKVIGIVTERDFLKFL 136

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

Pssm-ID: 442013 [Multi-domain] Cd Length: 206 Bit Score: 61.82 E-value: 3.75e-11

                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 736698752 304 QVKHIMTRKVVTVQPLQPIQDLVPYFVERSFNYIPVVSEQRLVGIISRADIIAALNQELNHFKMRA 369
Cdd:COG2524   87 KVKDIMTKDVITVSPDTTLEEALELMLEKGISGLPVVDDGKLVGIITERDLLKALAEGRDLLDAPV 152

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: 59.74 E-value: 4.64e-11

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736698752 242 TKDVVTLHANDNIQHALDKFKEMNLMSLPVVNAEGKLVGTLAmyqvvewfkrAADV-------RSSWEHQVKHIMTRKVV 314
Cdd:cd17784    1 TKNVITAKPNEGVVEAFEKMLKHKISALPVVDDEGKLIGIVT----------ATDLghnlildKYELGTTVEEVMVKDVA 70

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*....
gi 736698752 315 TVQPLQPIQDLVPYFVERS-----FNYIPVVSEQRLVGIISRADIIAAL 358
Cdd:cd17784   71 TVHPDETLLEAIKKMDSNApdeeiINQLPVVDDGKLVGIISDGDIIRAI 119

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

Pssm-ID: 425756 [Multi-domain] Cd Length: 57 Bit Score: 55.30 E-value: 2.88e-10

                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 736698752  305 VKHIMTRKVVTVQPLQPIQDLVPYFVERSFNYIPVVSEQ-RLVGIISRADIIAAL 358
Cdd:pfam00571   1 VKDIMTKDVVTVSPDTTLEEALELMREHGISRLPVVDEDgKLVGIVTLKDLLRAL 55

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

Pssm-ID: 341371 [Multi-domain] Cd Length: 108 Bit Score: 56.71 E-value: 3.05e-10

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736698752 243 KDVVTLHANDNIQHALDKFKEMNLMSLPVVNAEGKLVGTLAMYQVVEwfkRAADVRsswehqVKHIMTRKVVTVQPlqpi 322
Cdd:cd04596    2 EETGYLRETDTVRDYKQLSEETGHSRFPVVDEENRVVGIVTAKDVIG---KEDDTP------IEKVMTKNPITVKP---- 68

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 736698752 323 QDLVPYFVER----SFNYIPVVSEQR-LVGIISRADIIAA 357
Cdd:cd04596   69 KTSVASAAHMmiweGIELLPVVDENRkLLGVISRQDVLKA 108

CBS domain [Signal transduction mechanisms];

Pssm-ID: 440283 [Multi-domain] Cd Length: 128 Bit Score: 57.57 E-value: 3.06e-10

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736698752 201 VLDQQTELLDI-SEYDLQKIILEAQDRANARAVnqftcQDIMTKDVVTLHANDNIQHALDKFKEMNLMSLPVVNAEGKLV 279
Cdd:COG0517   37 VVDEDGKLVGIvTDRDLRRALAAEGKDLLDTPV-----SEVMTRPPVTVSPDTSLEEAAELMEEHKIRRLPVVDDDGRLV 111

                         90
                 ....*....|....*..
gi 736698752 280 GTLAMYQVVEWFKRAAD 296
Cdd:COG0517  112 GIITIKDLLKALLEPLA 128

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: 56.19 E-value: 6.52e-10

                         10        20        30        40
                 ....*....|....*....|....*....|....*....|..
gi 736698752 239 DIMTKDVVTLHANDNIQHALDKFKEMNLMSLPVVNAEGKLVG 280
Cdd:cd04606   69 DIMDTDVISVSADDDQEEVARLFAKYDLLALPVVDEEGRLVG 110

CBS domain [Signal transduction mechanisms];

Pssm-ID: 440283 [Multi-domain] Cd Length: 128 Bit Score: 56.41 E-value: 6.72e-10

                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 736698752 304 QVKHIMTRKVVTVQPLQPIQDLVPYFVERSFNYIPVVSEQ-RLVGIISRADIIAALNQE 361
Cdd:COG0517    2 KVKDIMTTDVVTVSPDATVREALELMSEKRIGGLPVVDEDgKLVGIVTDRDLRRALAAE 60

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: 55.89 E-value: 7.31e-10

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736698752 240 IMTKDVVTLHANDNIQHALDKFKEMNLMSLPVVNaEGKLVGTLAMyqvvewfkraADVRS-------SWEHQVKHIMTRK 312
Cdd:cd04587    1 LMSRPPVTVPPDATIQEAAQLMSEERVSSLLVVD-DGRLVGIVTD----------RDLRNrvvaeglDPDTPVSEIMTPP 69

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 736698752 313 VVTVQPLQPIQDLVPYFVERSFNYIPVVSEQRLVGIISRADII 355
Cdd:cd04587   70 PVTIDADALVFEALLLMLERNIHHLPVVDDGRVVGVVTATDLM 112

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: 55.89 E-value: 1.04e-09

                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....
gi 736698752 305 VKHIMTRKVVTVQPLQPIQDLVPYFVERSFNYIPVVSEQRLVGIISRADIIAAL 358
Cdd:cd04584    2 VKDIMTKNVVTVTPDTSLAEARELMKEHKIRHLPVVDDGKLVGIVTDRDLLRAS 55

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

Pssm-ID: 341400 [Multi-domain] Cd Length: 130 Bit Score: 55.97 E-value: 1.11e-09

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736698752 243 KDVVTLHANDNIQHALDKFKEMNLMSLPVVNAEGKLVGTLAMYQVVEW--------FKRAAdvrsswEHQVKHIMTRKVV 314
Cdd:cd04643    7 EKVAHVQDTNNLEHALLVLTKSGYSRIPVLDKDYKLVGLISLSMILDAilglerieFEKLS------ELKVEEVMNTDVP 80

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 736698752 315 TVQPLQPIQDLVPYFVERSFnyIPVVSE-QRLVGIISRADIIAALN 359
Cdd:cd04643   81 TVSPDDDLEEVLHLLVDHPF--LCVVDEdGYFLGIITRREILKAVN 124

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: 53.76 E-value: 1.15e-09

                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 736698752  239 DIMTKDVVTLHANDNIQHALDKFKEMNLMSLPVVNAEGKLVGTLAMYQVVEWFKR 293
Cdd:pfam00571   3 DIMTKDVVTVSPDTTLEEALELMREHGISRLPVVDEDGKLVGIVTLKDLLRALLG 57

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: 55.33 E-value: 1.35e-09

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736698752 201 VLDQQTELLDI-SEYDLQKIILEAQDRANARAvnqftcQDIMTKDVVTLHANDNIQHALDKFKEMNLMSLPVVNAEGKLV 279
Cdd:cd02205   30 VVDDDGKLVGIvTERDILRALVEGGLALDTPV------AEVMTPDVITVSPDTDLEEALELMLEHGIRRLPVVDDDGKLV 103


                 ...
gi 736698752 280 GTL 282
Cdd:cd02205  104 GIV 106

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: 55.42 E-value: 1.52e-09

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736698752 239 DIMTKDVVTLHANDNIQHAldkfkeMNLMS------LPVVNaEGKLVGTLAMYQVVEWFKRAADVRSSWEHQ-------- 304
Cdd:cd17778    4 EFMTTPVVTIYPDDTLKEA------MELMVtrgfrrLPVVS-GGKLVGIVTAMDIVKYFGSHEAKKRLTTGDideaystp 76

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 736698752 305 VKHIMTRKVVTVQPLQPIQDLVPYFVERSFNYIPVVSEQ-RLVGIISRADIIAAL 358
Cdd:cd17778   77 VEEIMSKEVVTIEPDADIAEAARLMIKKNVGSLLVVDDEgELKGIITERDVLIAL 131

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: 54.17 E-value: 3.46e-09

                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 736698752 220 ILEAQDRANARAVNQFTCQDIMTKDVVTLHANDNIQHALDKFKEMNLMSLPVVNAEGKLVG 280
Cdd:cd04605   46 IVTSWDISKAVALKKDSLEEIMTRNVITARPDEPIELAARKMEKHNISALPVVDDDRRVIG 106

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: 53.19 E-value: 6.66e-09

                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 736698752 227 ANARAVNQFTCQDIMTKDVVTLHANDNIQHALDKFKEMNLMSLPVVNAEGKLVGTLAM 284
Cdd:cd04622   52 AEGKDPNTTTVREVMTGDVVTCSPDDDVEEAARLMAEHQVRRLPVVDDDGRLVGIVSL 109

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

Pssm-ID: 341376 [Multi-domain] Cd Length: 110 Bit Score: 53.19 E-value: 6.77e-09

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736698752 244 DVVTLHANDNIQHALDKFKEMNLMSLPVVNAEGKLVGTLAmyqvvewfKRAADVRSSWEHQVKHIMTR--KVVTVQP--- 318
Cdd:cd04601    3 DPVTLSPDATVADVLELKAEYGISGVPVTEDGGKLVGIVT--------SRDIRFETDLSTPVSEVMTPdeRLVTAPEgit 74

                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 736698752 319 LQPIQDLvpyFVERSFNYIPVVSEQ-RLVGIISRADI 354
Cdd:cd04601   75 LEEAKEI---LHKHKIEKLPIVDDNgELVGLITRKDI 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: 341397 [Multi-domain] Cd Length: 120 Bit Score: 52.96 E-value: 8.89e-09

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736698752 239 DIMTKDVVTLHANDNIQHALDKFKEMNL--MSLPVVNAEGKLVGTLAmyqvVEWFKRAAdvRSSWEHQ-VKHIMTRK--V 313
Cdd:cd04639    1 DAMVTEFPIVDADLTLREFADDYLIGKKswREFLVTDEAGRLVGLIT----VDDLRAIP--TSQWPDTpVRELMKPLeeI 74

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 736698752 314 VTVQPLQPIQDLVPYFVERSFNYIPVVSE-QRLVGIISRADIIAAL 358
Cdd:cd04639   75 PTVAADQSLLEVVKLLEEQQLPALAVVSEnGTLVGLIEKEDIIELL 120

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: 52.53 E-value: 9.60e-09

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736698752 242 TKDVVTLHANDNIQHALDKFKEMNLMSLPVVNaEGKLVGTLAMYQVVEwfkraADVRSSWEHQVKHIMTRKVVTVQPLQP 321
Cdd:cd04588    1 SKDLITLKPDATIKDAAKLLSENNIHGAPVVD-DGKLVGIVTLTDIAK-----ALAEGKENAKVKDIMTKDVITIDKDEK 74

                         90       100       110
                 ....*....|....*....|....*....|....*
gi 736698752 322 IQDLVPYFVERSFNYIPVVSEQ-RLVGIISRADII 355
Cdd:cd04588   75 IYDAIRLMNKHNIGRLIVVDDNgKPVGIITRTDIL 109

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: 52.14 E-value: 1.68e-08

                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736698752 211 ISEYDLQKIIleAQDRANARAVNqftcqDIMTKDVVTLHANDNIQHALDKFKEMNLMSLPVVNAEGKLVG 280
Cdd:cd09836   42 VTERDIVRAV--AEGIDLDTPVE-----EIMTKNLVTVSPDESIYEAAELMREHNIRHLPVVDGGGKLVG 104

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: 51.39 E-value: 3.24e-08

                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....
gi 736698752 236 TCQDIMTKDVVTLHANDNIQHALDKFKEMNLMSLPVVNAEGKLVGTLAMYQVVE 289
Cdd:cd17775   62 TVGDIMSADLITAREDDGLFEALERMREKGVRRLPVVDDDGELVGIVTLDDILE 115

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: 50.27 E-value: 7.85e-08

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736698752 201 VLDQQTELLDI-SEYDLQKIILEA--QDRANARavnqftcqDIMTKDVVTLHANDNIQHALDKFKEMNLMSLPVVNAE-- 275
Cdd:cd04613   31 VVDEQGRLTGIlSIQDVRGVLFEEelWDLVVVK--------DLATTDVITVTPDDDLYTALLKFTSTNLDQLPVVDDDdp 102


                 ....*...
gi 736698752 276 GKLVGTLA 283
Cdd:cd04613  103 GKVLGMLS 110

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: 50.21 E-value: 8.72e-08

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736698752 236 TCQDIMTKDVVTLHANDNIQHALDKFKEMNLMSLPVVNA--EGKLVGTLamyqvvewfKRAaDVRSSWEHQVKHIMTRKV 313
Cdd:cd04591    1 TAEDVMRPPLTVLARDETVGDIVSVLKTTDHNGFPVVDSteSQTLVGFI---------LRS-QLILLLEADLRPIMDPSP 70

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 736698752 314 VTVQPLQPIQDLVPYFVERSFNYIPVVSEQRLVGIISRADIIAA 357
Cdd:cd04591   71 FTVTEETSLEKVHDLFRLLGLRHLLVTNNGRLVGIVTRKDLLRA 114

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: 49.33 E-value: 1.51e-07

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736698752 241 MTKDVVTLHANDNIQHALDKFKEMNLMSLpVVNAEGKLVGTLAMYQVVeWFKRAADvRSSWEHQVKHIMTRKVVTVQPLQ 320
Cdd:cd17776    1 MTTDVVTVDADASLEDAAERMLRNRVGSV-VVTDDGTPAGILTETDAL-HAGYATD-DPFSEIPVRAVASRPLVTISPTA 77

                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 736698752 321 PIQDLVPYFVERSFNYIPVVSEQRLVGIISRADIIAA 357
Cdd:cd17776   78 TLREAAERMVDEGVKKLPVVDGLDLVGILTATDIIRA 114

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: 47.12 E-value: 1.91e-07

                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*..
gi 736698752   313 VVTVQPLQPIQDLVPYFVERSFNYIPVV-SEQRLVGIISRADIIAAL 358
Cdd:smart00116   2 VVTVSPDTTLEEALELLRENGIRRLPVVdEEGRLVGIVTRRDIIKAL 48

Predicted transcriptional regulator containing CBS domains [Transcription];

Pssm-ID: 443285 [Multi-domain] Cd Length: 135 Bit Score: 49.53 E-value: 2.11e-07

                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 736698752 303 HQVKHIMTR-KVVTVQPLQPIQDLVPYFVERSFNYIPVVSEQ-RLVGIISRADIIAALNQEL 362
Cdd:COG4109   16 LLVEDIMTLeDVATLSEDDTVEDALELLEKTGHSRFPVVDENgRLVGIVTSKDILGKDDDTP 77

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: 48.11 E-value: 3.54e-07

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736698752 246 VTLHANDNIQHALDKFKEMNLMSLPVVNAEGKLVGTLAMYQVVEwfkraadvRSSweHQVKHIMTRKVVTVQPLQPIQDL 325
Cdd:cd04594    5 IKVSAYDTVERALKIMRENNLLSLPVVDNDSNFLGAVYLRDIEN--------KSP--GKVGKYVVRGSPYVTPTSSLEEA 74

                         90       100       110
                 ....*....|....*....|....*....|..
gi 736698752 326 VPYFVERSFNYIPVVSEQRLVGIISRADIIAA 357
Cdd:cd04594   75 WEIMMRNKSRWVAVVEKGKFLGIITLDDLLEA 106

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: 48.87 E-value: 3.75e-07

                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 736698752 304 QVKHIMTRKVVTVQPLQPIQDLVPYFVERSFNYIPVVSEQRLVGIISRADIIAAL 358
Cdd:cd17778    1 KVKEFMTTPVVTIYPDDTLKEAMELMVTRGFRRLPVVSGGKLVGIVTAMDIVKYF 55

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: 5.17e-07

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736698752 197 DIQEVLDQQTELLDISE--YDLQKIileaqdranaravnqfTCQDIMTKDVVTLHANDNIQHALDKFKEMNLMSLPVVNa 274
Cdd:cd04584   50 DLLRASPSKATSLSIYElnYLLSKI----------------PVKDIMTKDVITVSPDDTVEEAALLMLENKIGCLPVVD- 112


                 ....*.
gi 736698752 275 EGKLVG 280
Cdd:cd04584  113 GGKLVG 118

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: 47.54 E-value: 8.13e-07

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736698752 241 MTKDVVTLHANDNIQHALDKFKEMNLMSLPVVNAEGKLVGTLA----MYQVVewfkrAADVRSSwEHQVKHIMTRKVVTV 316
Cdd:cd17775    1 CRREVVTASPDTSVLEAARLMRDHHVGSVVVVEEDGKPVGIVTdrdiVVEVV-----AKGLDPK-DVTVGDIMSADLITA 74

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 736698752 317 QPLQPIQDLVPYFVERSFNYIPVVSEQ-RLVGIISRADIIAAL 358
Cdd:cd17775   75 REDDGLFEALERMREKGVRRLPVVDDDgELVGIVTLDDILELL 117

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

Pssm-ID: 442149 [Multi-domain] Cd Length: 124 Bit Score: 47.52 E-value: 9.44e-07

                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 736698752 305 VKHIMTRKVVTVQPLQPIQDLVPYFVERSFNYIPVVSEQ-RLVGIISRADIIAAL 358
Cdd:COG2905    1 VKDIMSRDVVTVSPDATVREAARLMTEKGVGSLVVVDDDgRLVGIITDRDLRRRV 55

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: 46.55 E-value: 1.01e-06

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736698752 239 DIMTKDVVTLHANDNIQHALDKF-KEMNLMSLPVVnaegKLVGtLAMYQVVEWFKRAADVRsswehqvkhimtrkvvtvq 317
Cdd:COG3620    3 DLMSRDVVTVSPDDTLGEALRLMrKELGLSQLPVA----ELVG-VSQSDILRIESGKRDPT------------------- 58

                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 736698752 318 pLQPIQDLVPYFvERSFNYIPVVSEQRLVGIISRADIIA 356
Cdd:COG3620   59 -VSTLEKIAEAL-GKELSAVLVVDDGKLVGIITRRDLLK 95

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: 49.69 E-value: 1.65e-06

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736698752  241 MTKDVVTLHANDNIQHALDKFKEMNLMSLPVVNaEGKLVGTLAmyqvvewfKRAADVRSSWEHQVKHIMTR-KVVTVQPL 319
Cdd:pfam00478  86 MITDPVTLSPDATVADALALMERYGISGVPVVD-DGKLVGIVT--------NRDLRFETDLSQPVSEVMTKeNLVTAPEG 156

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 736698752  320 QPIQD----LVPYFVERsfnyIPVVSEQ-RLVGIISRADI 354
Cdd:pfam00478 157 TTLEEakeiLHKHKIEK----LPVVDDNgRLVGLITIKDI 192

Predicted transcriptional regulator containing CBS domains [Transcription];

Pssm-ID: 443285 [Multi-domain] Cd Length: 135 Bit Score: 46.83 E-value: 1.66e-06

                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*
gi 736698752 238 QDIMTKDVVTLHANDNIQHALDKFKEMNLMSLPVVNAEGKLVGTL 282
Cdd:COG4109   79 EDVMTKNPITVTPDTSLASAAHKMIWEGIELLPVVDDDGRLLGII 123

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: 47.27 E-value: 1.68e-06

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736698752 240 IMTKDVVTLHANDNIQHALDKFKEMNLMSLPVVNAEGKLVGTL------AMYQVVEWFKR----AADVRSSW-------- 301
Cdd:cd04614    1 YAGKGVVPVWDETPLPVALRAMRLANVPAAPVLDSEGKLVGIVterdliDVSRIVESEEEsgmsIADDEDEWswegirdv 80

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736698752 302 -------------EHQVKHIMTRKVVTVQPLQPIQDLVPYFVERSFNYIPVVS-EQRLVGIISRADIIAA 357
Cdd:cd04614   81 mslyyptsnvelpDKPVKDVMTKDVVTAFPSSTVSEAAKKMIRNDIEQLPVVSgEGDLAGMLRDVDLLKA 150

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: 47.08 E-value: 1.81e-06

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736698752 251 NDNIQHALDKFKEMNLMSLPVVNAEGKLVGTLAMYQVVewfkrAADVRSSWEHQ-------------------------- 304
Cdd:cd17789   11 NTTVDEALELLVENRITGLPVIDEDWRLVGVVSDYDLL-----ALDSISGRSQTdnnfppadstwktfnevqkllsktng 85

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 736698752 305 --VKHIMTRKVVTVQPLQPIQDLVPYFVERSFNYIPVV-SEQRLVGIISRADIIAA 357
Cdd:cd17789   86 kvVGDVMTPSPLVVREKTNLEDAARILLETKFRRLPVVdSDGKLVGIITRGNVVRA 141

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: 43.66 E-value: 3.45e-06

                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*
gi 736698752   244 DVVTLHANDNIQHALDKFKEMNLMSLPVVNAEGKLVGTLAMYQVV 288
Cdd:smart00116   1 DVVTVSPDTTLEEALELLRENGIRRLPVVDEEGRLVGIVTRRDII 45

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: 44.65 E-value: 6.27e-06

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736698752 239 DIMTKDVVTLHANDNIQHALDKFKEMNLMSLPVVNAEGKLVGTLAMYQVvewfkrAADVRsswehqvkHIMTRKVVTVQP 318
Cdd:cd04597    1 DLEYDKVEPLSPETSIKDAWNLMDENNLKTLPVTDDNGKLIGLLSISDI------ARTVD--------YIMTKDNLIVFK 66

                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 736698752 319 LQPIQDLVPYFVERS-FNYIPVVSEQ-RLVGIISRADII 355
Cdd:cd04597   67 EDDYLDEVKEIMLNTnFRNYPVVDENnKFLGTISRKHLI 105

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: 44.74 E-value: 6.75e-06

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736698752 201 VLDQQTELLD-ISEYDLQKIILEA---QDRANaravnqfTCQDIMTKDVVTLHANDNIQHALDKFKEMNLMSLPVVNaEG 276
Cdd:cd04629   31 VVDEQGRLVGfLSEQDCLKALLEAsyhCEPGG-------TVADYMSTEVLTVSPDTSIVDLAQLFLKNKPRRYPVVE-DG 102


                 ....*.
gi 736698752 277 KLVGTL 282
Cdd:cd04629  103 KLVGQI 108

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

Pssm-ID: 341393 [Multi-domain] Cd Length: 120 Bit Score: 43.36 E-value: 1.96e-05

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736698752 237 CQDIMTKDVVTLHANDNIQHALDKFKEMNLMSLPVV-----NAEGKLVGTLAMYQVVewfkrAADvRSSWEHQVKHIMTR 311
Cdd:cd04630    1 VRDVMKTNVVTIDGLATVREALQLMKEHNVKSLIVEkrhehDAYGIVTYTDILKKVI-----AED-RDPDLVNVYEIMTK 74

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 736698752 312 KVVTVQPLQPIQDLVPYFVERSFNYIPVVSEQRLVGIISRADIIAA 357
Cdd:cd04630   75 PAISVSPDLDIKYAARLMARFNLKRAPVIENNELIGIVSMTDLVLD 120

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: 43.39 E-value: 1.96e-05

                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|
gi 736698752 310 TRKVVTVQPLQPIQDLVPYFVERSFNYIPVV-SEQRLVGIISRADIIAAL 358
Cdd:cd02205    1 TRDVVTVDPDTTVREALELMAENGIGALPVVdDDGKLVGIVTERDILRAL 50

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: 43.17 E-value: 2.30e-05

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736698752 201 VLDQQTELLDI-SEYD-LQKIILeaqdraNARAVNQFTCQDIMTKDVVTLHANDNIQHAldkfkeMNLMS------LPVV 272
Cdd:cd04623   30 VVDDGGRLVGIlSERDyVRKLAL------RGASSLDTPVSEIMTRDVVTCTPDDTVEEC------MALMTerrirhLPVV 97

                         90
                 ....*....|....*.
gi 736698752 273 nAEGKLVGTLAMYQVV 288
Cdd:cd04623   98 -EDGKLVGIVSIGDVV 112

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: 42.89 E-value: 2.54e-05

                         10        20        30        40
                 ....*....|....*....|....*....|....*....|...
gi 736698752 238 QDIMTKDVVTLHANDNIQHALDKFKEMNLMSLPVVNAEGKLVG 280
Cdd:cd04583   57 GEIMERDVFTVKEDSLLRDTVDRILKRGLKYVPVVDEQGRLVG 99

Mg2+ transporter (mgtE); This family of prokaryotic proteins models a class of Mg++ transporter first described in Bacillus firmus. May form a homodimer. [Transport and binding proteins, Cations and iron carrying compounds]

Pssm-ID: 129495 [Multi-domain] Cd Length: 449 Bit Score: 45.97 E-value: 2.55e-05

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736698752  202 LDQQTELLDISEYDLQKIILEAQDRANARAVNQF------TCQDIMTKDVVTLHANDNIQHALDKFKEM-----NLMSLP 270
Cdd:TIGR00400  92 LDDVIDLLEEVPANVVQQLLASSTEEERKAINLLlsysddSAGRIMTIEYVELKEDYTVGKALDYIRRVaktkeDIYTLY 171

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736698752  271 VVNAEGKLVGTLAMYQVVewfkRAADvrsswEHQVKHIMTRKVVTVQPLQPIQDLVPYFVERSFNYIPVV-SEQRLVGII 349
Cdd:TIGR00400 172 VTNESKHLKGVLSIRDLI----LAKP-----EEILSSIMRSSVFSIVGVNDQEEVARLIQKYDFLAVPVVdNEGRLVGIV 242

                         170
                  ....*....|..
gi 736698752  350 SRADIIAALNQE 361
Cdd:TIGR00400 243 TVDDIIDVIQSE 254

putative manganese-dependent inorganic diphosphatase;

Pssm-ID: 237843 [Multi-domain] Cd Length: 546 Bit Score: 45.98 E-value: 2.70e-05

                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|.
gi 736698752 239 DIMTKDVVTLHANDNIQHALDKFKEMNLMSLPVVNAEGKLVGTLAMYQVVE 289
Cdd:PRK14869  72 DLEIDKPVTVSPDTSLKEAWNLMDENNVKTLPVVDEEGKLLGLVSLSDLAR 122

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: 42.90 E-value: 2.97e-05

                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....
gi 736698752 239 DIMTKDVVTLHANDNIQHALDKFKEMNLMSLPVVNAEGKLVGTL 282
Cdd:cd04588   60 DIMTKDVITIDKDEKIYDAIRLMNKHNIGRLIVVDDNGKPVGII 103

CBS pair domains found in archeal proteins, repeat 1; CBS pair domains found in archeal proteins that contain 2 repeats. The CBS domain, named after human CBS, is a small domain originally identified in cystathionine beta-synthase and is subsequently found in a wide range of different proteins. CBS domains usually occur in tandem repeats. They associate to form a so-called Bateman domain or a CBS pair based on crystallographic studies in bacteria. The CBS pair was used as a basis for this cd hierarchy since the human CBS proteins can adopt the typical core structure and form an intramolecular CBS pair. The interface between the two CBS domains forms a cleft that is a potential ligand binding site. The CBS pair coexists with a variety of other functional domains and this has been used to help in its classification here.

Pssm-ID: 341413 [Multi-domain] Cd Length: 137 Bit Score: 42.71 E-value: 4.75e-05

                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 736698752 218 KIILEAQDRANA-RAVNQFTCQDIMTKDVVTLHANDNIQHALDKFKEMNLMSLPVVNAEGKLVG 280
Cdd:cd17777   63 FKIVESRHQGDLySALNREVVETIMTPNPVYVYEDSDLIEALTIMVTRGIGSLPVVDRDGRPVG 126

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: 42.17 E-value: 5.61e-05

                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 736698752 228 NARAVNQ-----FTCQDIMTKDVVTLHANDNIQHALDKFKEMNLMSLPVVNaEGKLVG 280
Cdd:cd04801   47 DIRKVPEvereaTRVRDVMTKDVITVSPDADAMEALKLMSQNNIGRLPVVE-DGELVG 103

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: 42.16 E-value: 6.20e-05

                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|..
gi 736698752 309 MTRKVVTVQPLQPIQDLVPYFVERSFNYIPVV-SEQRLVGIISRADIIAALN 359
Cdd:cd04600    1 MSRDVVTVTPDTSLEEAWRLLRRHRIKALPVVdRARRLVGIVTLADLLKHAD 52

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: 41.74 E-value: 6.78e-05

                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 736698752 305 VKHIMTRKVVTVQPLQPIQDLVPYFVERSFNYIPVVS---EQRLVGIISRADIIAALNQELNHF 365
Cdd:cd04591    2 AEDVMRPPLTVLARDETVGDIVSVLKTTDHNGFPVVDsteSQTLVGFILRSQLILLLEADLRPI 65

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

Pssm-ID: 341421 [Multi-domain] Cd Length: 136 Bit Score: 42.26 E-value: 7.49e-05

                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....
gi 736698752 236 TCQDIMtKDVVTLHANDNIQHALDKFKEMNLMSLPVVNAEGKLVGTLAMYQVVE 289
Cdd:cd17785   84 KAKDIM-LSPIYVKKEDTLEEALELMVKNRLQELPVVDENGKVIGDLNSLELLK 136

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: 341404 [Multi-domain] Cd Length: 118 Bit Score: 41.71 E-value: 7.59e-05

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736698752 243 KDVVTLHANDNIQHALDKFKEMNLMSLPVVNAEGKLVGTLAmyqvvE----WF---KRAADVRSSWEHQVKHI-MTRKVV 314
Cdd:cd09834    2 SEVAYLYDDSTLRQALEKMEYHRYTAIPILNRDGKYVGTIT-----EgdllWYiknKPNLDLKDAEKISIKDIpRRRDNK 76

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 736698752 315 TVQPLQPIQDLVPYFVERsfNYIPVVSEQ-RLVGIISRADII 355
Cdd:cd09834   77 PVNINANMEDLLDLAMNQ--NFVPVVDDRgVFIGIVTRKDII 116

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: 41.54 E-value: 7.63e-05

                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*....
gi 736698752 309 MTRKVVTVQPLQPIQDLVPYFVERSFNYIPVVSEQRLVGIISRADIIAA 357
Cdd:cd04610    1 MTRDVITVSPDDTVKDVIKLIKETGHDGFPVVDDGKVVGYVTAKDLLGK 49

2 tandem repeats of the CBS domain in the two-component sensor histidine kinase and related-proteins, repeat 1; This cd contains 2 tandem repeats of the CBS domain in the two-component sensor histidine kinase and related-proteins. Two-component regulation is the predominant form of signal recognition and response coupling mechanism used by bacteria to sense and respond to diverse environmental stresses and cues ranging from common environmental stimuli to host signals recognized by pathogens and bacterial cell-cell communication signals. The structures of both sensors and regulators are modular, and numerous variations in domain architecture and composition have evolved to tailor to specific needs in signal perception and signal transduction. The simplest histidine kinase sensors consists of only sensing and kinase domains. The more complex hybrid sensors contain an additional REC domain typical of two-component regulators and in some cases a C-terminal histidine phosphotransferase (HPT) domain. The CBS domain, named after human CBS, is a small domain originally identified in cystathionine beta-synthase and is subsequently found in a wide range of different proteins. CBS domains usually occur in tandem repeats. They associate to form a so-called Bateman domain or a CBS pair based on crystallographic studies in bacteria. The CBS pair was used as a basis for this cd hierarchy since the human CBS proteins can adopt the typical core structure and form an intramolecular CBS pair. The interface between the two CBS domains forms a cleft that is a potential ligand binding site. The CBS pair coexists with a variety of other functional domains and this has been used to help in its classification here. It has been proposed that the CBS domain may play a regulatory role, although its exact function is unknown. Mutations of conserved residues within this domain are associated with a variety of human hereditary diseases, including congenital myotonia, idiopathic generalized epilepsy, hypercalciuric nephrolithiasis, and classic Bartter syndrome (CLC chloride channel family members), Wolff-Parkinson-White syndrome (gamma 2 subunit of AMP-activated protein kinase), retinitis pigmentosa (IMP dehydrogenase-1), and homocystinuria (cystathionine beta-synthase).

Pssm-ID: 341389 [Multi-domain] Cd Length: 136 Bit Score: 42.14 E-value: 7.89e-05

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736698752 204 QQTELLDI-SEYDLQKIIleaqdrANARAVNQFTCQDIMTKDVVTLHAND--NIQHALDKFKEMNLMSLPVVNAEGKLVG 280
Cdd:cd04620   53 ENQQLVGIfTERDVVRLT------ASGIDLSGVTIAEVMTQPVITLKESEfqDIFTVLSLLRQHQIRHLPIVDDQGQLVG 126


                 ..
gi 736698752 281 TL 282
Cdd:cd04620  127 LI 128

Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains found associated with the glycine betaine/L-proline ABC transporter; 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: 341402 [Multi-domain] Cd Length: 116 Bit Score: 41.39 E-value: 9.82e-05

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736698752 239 DIMTKDVVTL--HANDNIQHALDKFKEMNLMSLPVVNAEGKLVGTLAMYQVVEwfKRAADVRSswehqVKHIMTRKVVTV 316
Cdd:cd09831    1 DIARKTQVTVieKTGDGPRAALQLLREHDREYGYVVDKKRRFLGVVSVDSLRA--ALKENAQS-----LEDAFLTDVETV 73

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 736698752 317 QPLQPIQDLVPYFVERSFNyIPVVSE-QRLVGIISRADIIAALN 359
Cdd:cd09831   74 PADTSLSDILGLVASAPCP-LPVVDEdGRYLGVISKASLLETLD 116

Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with the MET2 domain; This cd contains two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with the MET2 domain. Met2 is a key enzyme in the biosynthesis of methionine. It encodes a homoserine transacetylase involved in converting homoserine to O-acetyl homoserine. The CBS domain, named after human CBS, is a small domain originally identified in cystathionine beta-synthase and is subsequently found in a wide range of different proteins. CBS domains usually occur in tandem repeats. They associate to form a so-called Bateman domain or a CBS pair based on crystallographic studies in bacteria. The CBS pair was used as a basis for this cd hierarchy since the human CBS proteins can adopt the typical core structure and form an intramolecular CBS pair. The interface between the two CBS domains forms a cleft that is a potential ligand binding site. The CBS pair coexists with a variety of other functional domains and this has been used to help in its classification here. It has been proposed that the CBS domain may play a regulatory role, although its exact function is unknown. Mutations of conserved residues within this domain are associated with a variety of human hereditary diseases, including congenital myotonia, idiopathic generalized epilepsy, hypercalciuric nephrolithiasis, and classic Bartter syndrome (CLC chloride channel family members), Wolff-Parkinson-White syndrome (gamma 2 subunit of AMP-activated protein kinase), retinitis pigmentosa (IMP dehydrogenase-1), and homocystinuria (cystathionine beta-synthase).

Pssm-ID: 341379 [Multi-domain] Cd Length: 116 Bit Score: 40.68 E-value: 1.51e-04

                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 736698752 305 VKHIMTRKVVTVQPLQPIQDLVPYFVERSFNYIPVVSEQ-RLVGIISRADIIAALNQELNHFKM 367
Cdd:cd04605    2 VEDIMSKDVATIREDISIEEAAKIMIDKNVTHLPVVSEDgKLIGIVTSWDISKAVALKKDSLEE 65

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: 40.11 E-value: 2.53e-04

                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|.
gi 736698752 309 MTRKVVTVQPLQPIQDLVPYFVERSFNYIPVVSEQ-RLVGIISRADIIAAL 358
Cdd:cd04629    1 MTRNPVTLTPDTSILEAVELLLEHKISGAPVVDEQgRLVGFLSEQDCLKAL 51

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: 40.11 E-value: 3.61e-04

                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 736698752 223 AQDRANARAVnqfTCQDIMTKDVVTLHANDNIQHALDKFKEMNLMSLPVVNaEGKLVG 280
Cdd:cd04586   74 AEEYVKAHGR---TVGDVMTRPVVTVSPDTPLEEAARLMERHRIKRLPVVD-DGKLVG 127

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: 39.44 E-value: 4.08e-04

                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|...
gi 736698752 310 TRKVVTVQPLQPIQDLVPYFVERSFNYIPVVSEQRLVGIISRADIIAALNQEL 362
Cdd:cd04588    1 SKDLITLKPDATIKDAAKLLSENNIHGAPVVDDGKLVGIVTLTDIAKALAEGK 53

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: 39.14 E-value: 9.13e-04

                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|...
gi 736698752 305 VKHIMTRKVVTVQPLQPIQDLVPYFVERSFNYIPVVS--EQRLVGIISRADII 355
Cdd:cd17779    2 IMAIATKDVITIPPTTTIIGAIKTMTEKGFRRLPVADagTKRLEGIVTSMDIV 54

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

Pssm-ID: 341420 [Multi-domain] Cd Length: 120 Bit Score: 38.17 E-value: 1.22e-03

                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 736698752 236 TCQDIMTKDVVTLHANDNIQHALDKFKEMNLMS-----LPVVNaEGKLVGTLAMYQVVEWFK 292
Cdd:cd17784   60 TVEEVMVKDVATVHPDETLLEAIKKMDSNAPDEeiinqLPVVD-DGKLVGIISDGDIIRAIK 120

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: 37.86 E-value: 1.45e-03

                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736698752 211 ISEYDLQKIILEAQDRANARAvnqftcqdIMTKDVVTLHANDNIQHALDKFKEMNLMSLPVVNaEGKLVG 280
Cdd:cd04595   40 ISRRDVDKAKHHGLGHAPVKG--------YMSTNVITIDPDTSLEEAQELMVEHDIGRLPVVE-EGKLVG 100

putative manganese-dependent inorganic diphosphatase;

Pssm-ID: 237843 [Multi-domain] Cd Length: 546 Bit Score: 40.59 E-value: 1.56e-03

                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 736698752 229 ARAVNQ-FTCQDIMTK-DVVTLHANDNIQHALDKFKEMNLMSLPVVNAEGKLVGTLAMYQVV 288
Cdd:PRK14869 239 ARLINQsIPVSYIMTTeDLVTFSKDDYLEDVKEVMLKSRYRSYPVVDEDGKVVGVISRYHLL 300

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: 1.83e-03

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gi 736698752 238 QDIMTKDVVTLHANDNIQHALDKFKEMNLMSLPVVNAEGKLVGTLAMY 285
Cdd:cd04604   73 KDVMTRNPKTISPDALAAEALELMEEHKITVLPVVDEDGKPVGILHLH 120

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: 38.41 E-value: 1.88e-03

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gi 736698752 239 DIMTKDVVTLHANDNIQHALDKFKEMNLMSLPVVNAEGKLVGTL 282
Cdd:cd04614   99 DVMTKDVVTAFPSSTVSEAAKKMIRNDIEQLPVVSGEGDLAGML 142

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: 37.96 E-value: 1.89e-03

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gi 736698752 216 LQKIIleAQDRaNARAVNQFtcqDIMTKDVVTLHANDNIQHALDKFKEMNLMSLPVVNAeGKLVGTLAMYQVV 288
Cdd:cd04630   53 LKKVI--AEDR-DPDLVNVY---EIMTKPAISVSPDLDIKYAARLMARFNLKRAPVIEN-NELIGIVSMTDLV 118

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

Pssm-ID: 341381 [Multi-domain] Cd Length: 112 Bit Score: 37.42 E-value: 2.34e-03

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gi 736698752 239 DIMTKDVVTLHANDNIQHALDKFKEMNLMSLPVVNAEGKLVG 280
Cdd:cd04607   62 EVMNKNPITASPSTSREELLALMRAKKILQLPIVDEQGRVVG 103

GuaB1 family IMP dehydrogenase-related protein;

Pssm-ID: 181127 [Multi-domain] Cd Length: 479 Bit Score: 39.12 E-value: 3.30e-03

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                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 736698752 227 ANARAVNQFT-CQDIMTKDVVTLHANDNIQHALDKFKEMNLMSLPVVNAEGKLVGTL 282
Cdd:PRK07807 139 ADCAGVDRFTqVRDVMSTDLVTLPAGTDPREAFDLLEAARVKLAPVVDADGRLVGVL 195

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: 38.91 E-value: 4.06e-03

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                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 736698752  294 AADVRsswehQVK---HIMTRKVVTVQPLQPIQDLVPYFVERSFNYIPVVSEQRLVGIISRADI 354
Cdd:pfam00478  73 AEEVR-----KVKrseSGMITDPVTLSPDATVADALALMERYGISGVPVVDDGKLVGIVTNRDL 131

Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains similar to MUG70 repeat1; Two tandem repeats of the cystathionine beta-synthase (CBS pair) domain, present in MUG70. The MUG70 protein, encoded by the Meiotically Up-regulated Gene 70, plays a role in meiosis and contains, beside the two CBS pairs, a PB1 domain. The CBS domain, named after human CBS, is a small domain originally identified in cystathionine beta-synthase and is subsequently found in a wide range of different proteins. CBS domains usually occur in tandem repeats. They associate to form a so-called Bateman domain or a CBS pair based on crystallographic studies in bacteria. The CBS pair was used as a basis for this cd hierarchy since the human CBS proteins can adopt the typical core structure and form an intramolecular CBS pair. The interface between the two CBS domains forms a cleft that is a potential ligand binding site. The CBS pair coexists with a variety of other functional domains and this has been used to help in its classification here. It has been proposed that the CBS domain may play a regulatory role, although its exact function is unknown. Mutations of conserved residues within this domain are associated with a variety of human hereditary diseases, including congenital myotonia, idiopathic generalized epilepsy, hypercalciuric nephrolithiasis, and classic Bartter syndrome (CLC chloride channel family members), Wolff-Parkinson-White syndrome (gamma 2 subunit of AMP-activated protein kinase), retinitis pigmentosa (IMP dehydrogenase-1), and homocystinuria (cystathionine beta-synthase).

Pssm-ID: 341417 [Multi-domain] Cd Length: 118 Bit Score: 36.80 E-value: 4.21e-03

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gi 736698752 236 TCQDIMTKDVVTLHANDNIQHALDKFKEMNLMSLPVVNAEGKLVGTL 282
Cdd:cd17781   61 LVSSVMTPNPLCVTMDTSATDALDLMVEGKFRHLPVVDDDGDVVGVL 107

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

Pssm-ID: 341423 [Multi-domain] Cd Length: 111 Bit Score: 36.63 E-value: 4.24e-03

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                 ....*....|....*....|....*....|....*....|.
gi 736698752 249 HANDNIQHALDKFKEMNLMSLPVVNAEGKLVGTLAMYQVVE 289
Cdd:cd17787   67 HEEDYIEDAALLLIESHEFVLPVVNSDMKVKGVLTVFEILE 107

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

Pssm-ID: 341381 [Multi-domain] Cd Length: 112 Bit Score: 36.65 E-value: 4.65e-03

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gi 736698752 271 VVNAEGKLVGTLAmyqvvewfkrAADVR------SSWEHQVKHIMTRKVVTVQPLQPIQDLVPYFVERSFNYIPVVSEQ- 343
Cdd:cd04607   30 VVDENRKLLGTVT----------DGDIRrgllkgLSLDAPVEEVMNKNPITASPSTSREELLALMRAKKILQLPIVDEQg 99

                         90
                 ....*....|...
gi 736698752 344 RLVGIISRADIIA 356
Cdd:cd04607  100 RVVGLETLDDLLA 112

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: 36.70 E-value: 4.66e-03

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gi 736698752 305 VKHIMT--RKVVTVQPLQPIQDLVPYFVERSFNYIPVVSEQR--LVGIISRADIIAALNQELNHFKMRA 369
Cdd:cd04590    2 VREVMTprTDVVALDADATLEELLELILESGYSRFPVYEGDLdnIIGVLHVKDLLAALLEGREKLDLRA 70

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: 5.78e-03

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gi 736698752 313 VVTVQPLQPIQDLVPYFVERSFNYIPVVSEQRLVGIISRADIIAALNQELNH 364
Cdd:cd04595    4 VKTVSPDTTIEEARKIMLRYGHTGLPVVEDGKLVGIISRRDVDKAKHHGLGH 55

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: 36.68 E-value: 7.33e-03

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gi 736698752 239 DIMTKDVVTLHANDNIQHALDKFKEMNLMSLPVVNAEGKLVGTLAMYQVV 288
Cdd:cd17789   90 DVMTPSPLVVREKTNLEDAARILLETKFRRLPVVDSDGKLVGIITRGNVV 139

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: 35.76 E-value: 8.79e-03

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gi 736698752 240 IMTKDVVTLHANDNIQHALDKFKEMNLMSLPVVNAEGKLVG 280
Cdd:cd04610   58 IMSRDTVVADPDMDITDAARVIFRSGISKLPVVDDEGNLVG 98

IMP dehydrogenase / GMP reductase domain; This family is involved in biosynthesis of guanosine nucleotide. Members of this family contain a TIM barrel structure. In the inosine monophosphate dehydrogenases 2 CBS domains pfam00571 are inserted in the TIM barrel. This family is a member of the common phosphate binding site TIM barrel family.

Pssm-ID: 459826 [Multi-domain] Cd Length: 463 Bit Score: 37.75 E-value: 9.67e-03

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                  ....*....|....*....|....*....|....*....|...
gi 736698752  239 DIMTKD-VVTLHANDNIQHALDKFKEMNLMSLPVVNAEGKLVG 280
Cdd:pfam00478 143 EVMTKEnLVTAPEGTTLEEAKEILHKHKIEKLPVVDDNGRLVG 185