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Conserved domains on  [gi|1443048451|ref|XP_015616615|]
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CBS domain-containing protein CBSCBSPB5 [Oryza sativa Japonica Group]

Protein Classification

CBS_pair_SF and PB1_MUG70 domain-containing protein( domain architecture ID 10333855)

protein containing domains CBS_pair_SF, and PB1_MUG70

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
CBS_pair_SF super family cl15354
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains superfamily; The CBS ...
60-176 3.22e-42

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).


The actual alignment was detected with superfamily member cd17781:

Pssm-ID: 449531 [Multi-domain]  Cd Length: 118  Bit Score: 146.96  E-value: 3.22e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443048451  60 LSKALTVPESTTVLEACRRMAARRADAALLTDSNALLCGILTDKDIATRVIARELKIEETPAWKVMTRHPVFVPSETLAV 139
Cdd:cd17781     1 PSPALTVPETTTVAEAAQLMAAKRTDAVLVVDDDGGLSGIFTDKDLARRVVASGLDPRSTLVSSVMTPNPLCVTMDTSAT 80
                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 1443048451 140 EALHKMVQGKFRHLPVVE-NGEVIAMLDIAKCLYDAIA 176
Cdd:cd17781    81 DALDLMVEGKFRHLPVVDdDGDVVGVLDITKCLYDAIE 118
CBS_pair_SF super family cl15354
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains superfamily; The CBS ...
227-343 2.83e-39

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).


The actual alignment was detected with superfamily member cd17782:

Pssm-ID: 449531 [Multi-domain]  Cd Length: 118  Bit Score: 139.30  E-value: 2.83e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443048451 227 ESTVVIVSPGDSVLTATQKMVEVHASSAVVAVGNKA-QGILTSRDILMRMIAKNLPADSTPVEKVMTLDPECATVDMPIL 305
Cdd:cd17782     1 GTPPPLVSPKTTVREAARLMKENRTTAVLVMDNSGKvIGIFTSKDVVLRVLAAGLDPATTSVVRVMTPNPETAPPSTTIL 80
                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 1443048451 306 DALRIMQERKFLHLPVMDRDGSIVSILDVIDITHAAFS 343
Cdd:cd17782    81 DALHKMHEGKFLNLPVVDDEGEIVGLVDVLQLTYATLQ 118
PB1_MUG70 cd06409
The MUG70 protein is a product of the meiotically up-regulated gene 70 which has a role in ...
403-487 3.30e-31

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


:

Pssm-ID: 99730  Cd Length: 86  Bit Score: 115.87  E-value: 3.30e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443048451 403 FSFKLQDRRGRMHRFSCEV-QSLTPLITCILQRLGPDLDRDHLPQILYEDEDRDKVVLASDDDLTAAVDHARLAGWKGLK 481
Cdd:cd06409     1 FAFKFKDPKGRVHRFRLRPsESLEELRTLISQRLGDDDFETHLYALSYVDDEGDIVLITSDSDLVAAVLVARSAGLKKLD 80

                  ....*.
gi 1443048451 482 LYLDYS 487
Cdd:cd06409    81 LHLHYP 86
 
Name Accession Description Interval E-value
CBS_pair_MUG70_1 cd17781
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains similar to MUG70 ...
60-176 3.22e-42

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: 146.96  E-value: 3.22e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443048451  60 LSKALTVPESTTVLEACRRMAARRADAALLTDSNALLCGILTDKDIATRVIARELKIEETPAWKVMTRHPVFVPSETLAV 139
Cdd:cd17781     1 PSPALTVPETTTVAEAAQLMAAKRTDAVLVVDDDGGLSGIFTDKDLARRVVASGLDPRSTLVSSVMTPNPLCVTMDTSAT 80
                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 1443048451 140 EALHKMVQGKFRHLPVVE-NGEVIAMLDIAKCLYDAIA 176
Cdd:cd17781    81 DALDLMVEGKFRHLPVVDdDGDVVGVLDITKCLYDAIE 118
CBS_pair_MUG70_2 cd17782
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains similar to MUG70 ...
227-343 2.83e-39

Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains similar to MUG70 repeat2; Two tandem repeats of the cystathionine beta-synthase (CBS pair) domain, present in MUG70. The MUG70 protein, encoded by the Meiotically Up-regulated Gene 70, plays a role in meiosis and contains, beside the two CBS pairs, a PB1 domain. The CBS domain, named after human CBS, is a small domain originally identified in cystathionine beta-synthase and is subsequently found in a wide range of different proteins. CBS domains usually occur in tandem repeats. They associate to form a so-called Bateman domain or a CBS pair based on crystallographic studies in bacteria. The CBS pair was used as a basis for this cd hierarchy since the human CBS proteins can adopt the typical core structure and form an intramolecular CBS pair. The interface between the two CBS domains forms a cleft that is a potential ligand binding site. The CBS pair coexists with a variety of other functional domains and this has been used to help in its classification here. It has been proposed that the CBS domain may play a regulatory role, although its exact function is unknown. Mutations of conserved residues within this domain are associated with a variety of human hereditary diseases, including congenital myotonia, idiopathic generalized epilepsy, hypercalciuric nephrolithiasis, and classic Bartter syndrome (CLC chloride channel family members), Wolff-Parkinson-White syndrome (gamma 2 subunit of AMP-activated protein kinase), retinitis pigmentosa (IMP dehydrogenase-1), and homocystinuria (cystathionine beta-synthase).


Pssm-ID: 341418 [Multi-domain]  Cd Length: 118  Bit Score: 139.30  E-value: 2.83e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443048451 227 ESTVVIVSPGDSVLTATQKMVEVHASSAVVAVGNKA-QGILTSRDILMRMIAKNLPADSTPVEKVMTLDPECATVDMPIL 305
Cdd:cd17782     1 GTPPPLVSPKTTVREAARLMKENRTTAVLVMDNSGKvIGIFTSKDVVLRVLAAGLDPATTSVVRVMTPNPETAPPSTTIL 80
                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 1443048451 306 DALRIMQERKFLHLPVMDRDGSIVSILDVIDITHAAFS 343
Cdd:cd17782    81 DALHKMHEGKFLNLPVVDDEGEIVGLVDVLQLTYATLQ 118
PB1_MUG70 cd06409
The MUG70 protein is a product of the meiotically up-regulated gene 70 which has a role in ...
403-487 3.30e-31

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


Pssm-ID: 99730  Cd Length: 86  Bit Score: 115.87  E-value: 3.30e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443048451 403 FSFKLQDRRGRMHRFSCEV-QSLTPLITCILQRLGPDLDRDHLPQILYEDEDRDKVVLASDDDLTAAVDHARLAGWKGLK 481
Cdd:cd06409     1 FAFKFKDPKGRVHRFRLRPsESLEELRTLISQRLGDDDFETHLYALSYVDDEGDIVLITSDSDLVAAVLVARSAGLKKLD 80

                  ....*.
gi 1443048451 482 LYLDYS 487
Cdd:cd06409    81 LHLHYP 86
COG2905 COG2905
Signal-transduction protein containing cAMP-binding, CBS, and nucleotidyltransferase domains ...
228-340 7.49e-24

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


Pssm-ID: 442149 [Multi-domain]  Cd Length: 124  Bit Score: 96.82  E-value: 7.49e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443048451 228 STVVIVSPGDSVLTATQKMVEVHASSA-VVAVGNKAQGILTSRDILMRMIAKNLPADSTPVEKVMTLDPECATVDMPILD 306
Cdd:COG2905     7 RDVVTVSPDATVREAARLMTEKGVGSLvVVDDDGRLVGIITDRDLRRRVLAEGLDPLDTPVSEVMTRPPITVSPDDSLAE 86
                          90       100       110
                  ....*....|....*....|....*....|....
gi 1443048451 307 ALRIMQERKFLHLPVMDrDGSIVSILDVIDITHA 340
Cdd:COG2905    87 ALELMEEHRIRHLPVVD-DGKLVGIVSITDLLRA 119
COG2905 COG2905
Signal-transduction protein containing cAMP-binding, CBS, and nucleotidyltransferase domains ...
55-167 6.03e-23

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


Pssm-ID: 442149 [Multi-domain]  Cd Length: 124  Bit Score: 94.13  E-value: 6.03e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443048451  55 VRRLRLSKALTVPESTTVLEACRRMAARRADAALLTDSNALLCGILTDKDIATRVIARELKIEETPAWKVMTRHPVFVPS 134
Cdd:COG2905     1 VKDIMSRDVVTVSPDATVREAARLMTEKGVGSLVVVDDDGRLVGIITDRDLRRRVLAEGLDPLDTPVSEVMTRPPITVSP 80
                          90       100       110
                  ....*....|....*....|....*....|...
gi 1443048451 135 ETLAVEALHKMVQGKFRHLPVVENGEVIAMLDI 167
Cdd:COG2905    81 DDSLAEALELMEEHRIRHLPVVDDGKLVGIVSI 113
PB1 pfam00564
PB1 domain;
402-487 2.85e-11

PB1 domain;


Pssm-ID: 395447  Cd Length: 84  Bit Score: 59.61  E-value: 2.85e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443048451 402 SFSFKLQDRRGRMHRFS-CEVQSLTPLITCILQRLGpdlDRDHLPQILYEDEDRDKVVLASDDDLTAAVDHARLAGWKGL 480
Cdd:pfam00564   1 TVRLKLRYGGGIRRFLSvSRGISFEELRALVEQRFG---LDDVDFKLKYPDEDGDLVSLTSDEDLEEALEEARSLGSKSL 77

                  ....*..
gi 1443048451 481 KLYLDYS 487
Cdd:pfam00564  78 RLHVFPT 84
PB1 smart00666
PB1 domain; Phox and Bem1p domain, present in many eukaryotic cytoplasmic signalling proteins. ...
402-485 1.14e-10

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


Pssm-ID: 214770  Cd Length: 81  Bit Score: 57.98  E-value: 1.14e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443048451  402 SFSFKLQDRrGRMHRFSCEVQ-SLTPLITCILQRLGpdLDRDHlPQILYEDEDRDKVVLASDDDLTAAVDHARLAGWKGL 480
Cdd:smart00666   1 TVDVKLRYG-GETRRLSVPRDiSFEDLRSKVAKRFG--LDNQS-FTLKYQDEDGDLVSLTSDEDLEEAIEEYDSLGSKKL 76

                   ....*
gi 1443048451  481 KLYLD 485
Cdd:smart00666  77 RLHVF 81
CBS pfam00571
CBS domain; CBS domains are small intracellular modules that pair together to form a stable ...
287-340 1.25e-08

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


Pssm-ID: 425756 [Multi-domain]  Cd Length: 57  Bit Score: 51.45  E-value: 1.25e-08
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1443048451 287 VEKVMTLDPECATVDMPILDALRIMQERKFLHLPVMDRDGSIVSILDVIDITHA 340
Cdd:pfam00571   1 VKDIMTKDVVTVSPDTTLEEALELMREHGISRLPVVDEDGKLVGIVTLKDLLRA 54
PRK14869 PRK14869
putative manganese-dependent inorganic diphosphatase;
124-332 1.62e-07

putative manganese-dependent inorganic diphosphatase;


Pssm-ID: 237843 [Multi-domain]  Cd Length: 546  Bit Score: 54.07  E-value: 1.62e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443048451 124 VMTRHPVFVPSETLAVEALHKMVQGKFRHLPVVENGE----VIAMLDIAKCL---------------YDAIARIErasdK 184
Cdd:PRK14869   73 LEIDKPVTVSPDTSLKEAWNLMDENNVKTLPVVDEEGkllgLVSLSDLARAYmdildpeilsksptsLENIIRTL----D 148
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443048451 185 GKAAAIASAVDAAAGNDPTASSMVEAFKEQMlrpslstittAESTVVIVspGDSVlTATQKMVEVHASSAVVAVGN---- 260
Cdd:PRK14869  149 GEVLVGAEEDKVEEGKVVVAAMAPESLLERI----------EEGDIVIV--GDRE-DIQLAAIEAGVRLLIITGGApvse 215
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443048451 261 ------KAQG---ILTSRD--ILMRMIakNLpadSTPVEKVMTL-DPECATVDMPILDALRIMQERKFLHLPVMDRDGSI 328
Cdd:PRK14869  216 dvlelaKENGvtvISTPYDtfTTARLI--NQ---SIPVSYIMTTeDLVTFSKDDYLEDVKEVMLKSRYRSYPVVDEDGKV 290

                  ....
gi 1443048451 329 VSIL 332
Cdd:PRK14869  291 VGVI 294
CBS pfam00571
CBS domain; CBS domains are small intracellular modules that pair together to form a stable ...
124-173 2.70e-06

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: 44.51  E-value: 2.70e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1443048451 124 VMTRHPVFVPSETLAVEALHKMVQGKFRHLPVV-ENGEVIAML---DIAKCLYD 173
Cdd:pfam00571   4 IMTKDVVTVSPDTTLEEALELMREHGISRLPVVdEDGKLVGIVtlkDLLRALLG 57
CBS smart00116
Domain in cystathionine beta-synthase and other proteins; Domain present in all 3 forms of ...
294-337 8.24e-04

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: 37.49  E-value: 8.24e-04
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....
gi 1443048451  294 DPECATVDMPILDALRIMQERKFLHLPVMDRDGSIVSILDVIDI 337
Cdd:smart00116   1 DVVTVSPDTTLEEALELLRENGIRRLPVVDEEGRLVGIVTRRDI 44
CBS smart00116
Domain in cystathionine beta-synthase and other proteins; Domain present in all 3 forms of ...
133-172 1.32e-03

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: 36.72  E-value: 1.32e-03
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....
gi 1443048451  133 PSETLAvEALHKMVQGKFRHLPVV-ENGEVIAML---DIAKCLY 172
Cdd:smart00116   7 PDTTLE-EALELLRENGIRRLPVVdEEGRLVGIVtrrDIIKALA 49
 
Name Accession Description Interval E-value
CBS_pair_MUG70_1 cd17781
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains similar to MUG70 ...
60-176 3.22e-42

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: 146.96  E-value: 3.22e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443048451  60 LSKALTVPESTTVLEACRRMAARRADAALLTDSNALLCGILTDKDIATRVIARELKIEETPAWKVMTRHPVFVPSETLAV 139
Cdd:cd17781     1 PSPALTVPETTTVAEAAQLMAAKRTDAVLVVDDDGGLSGIFTDKDLARRVVASGLDPRSTLVSSVMTPNPLCVTMDTSAT 80
                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 1443048451 140 EALHKMVQGKFRHLPVVE-NGEVIAMLDIAKCLYDAIA 176
Cdd:cd17781    81 DALDLMVEGKFRHLPVVDdDGDVVGVLDITKCLYDAIE 118
CBS_pair_MUG70_2 cd17782
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains similar to MUG70 ...
227-343 2.83e-39

Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains similar to MUG70 repeat2; Two tandem repeats of the cystathionine beta-synthase (CBS pair) domain, present in MUG70. The MUG70 protein, encoded by the Meiotically Up-regulated Gene 70, plays a role in meiosis and contains, beside the two CBS pairs, a PB1 domain. The CBS domain, named after human CBS, is a small domain originally identified in cystathionine beta-synthase and is subsequently found in a wide range of different proteins. CBS domains usually occur in tandem repeats. They associate to form a so-called Bateman domain or a CBS pair based on crystallographic studies in bacteria. The CBS pair was used as a basis for this cd hierarchy since the human CBS proteins can adopt the typical core structure and form an intramolecular CBS pair. The interface between the two CBS domains forms a cleft that is a potential ligand binding site. The CBS pair coexists with a variety of other functional domains and this has been used to help in its classification here. It has been proposed that the CBS domain may play a regulatory role, although its exact function is unknown. Mutations of conserved residues within this domain are associated with a variety of human hereditary diseases, including congenital myotonia, idiopathic generalized epilepsy, hypercalciuric nephrolithiasis, and classic Bartter syndrome (CLC chloride channel family members), Wolff-Parkinson-White syndrome (gamma 2 subunit of AMP-activated protein kinase), retinitis pigmentosa (IMP dehydrogenase-1), and homocystinuria (cystathionine beta-synthase).


Pssm-ID: 341418 [Multi-domain]  Cd Length: 118  Bit Score: 139.30  E-value: 2.83e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443048451 227 ESTVVIVSPGDSVLTATQKMVEVHASSAVVAVGNKA-QGILTSRDILMRMIAKNLPADSTPVEKVMTLDPECATVDMPIL 305
Cdd:cd17782     1 GTPPPLVSPKTTVREAARLMKENRTTAVLVMDNSGKvIGIFTSKDVVLRVLAAGLDPATTSVVRVMTPNPETAPPSTTIL 80
                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 1443048451 306 DALRIMQERKFLHLPVMDRDGSIVSILDVIDITHAAFS 343
Cdd:cd17782    81 DALHKMHEGKFLNLPVVDDEGEIVGLVDVLQLTYATLQ 118
PB1_MUG70 cd06409
The MUG70 protein is a product of the meiotically up-regulated gene 70 which has a role in ...
403-487 3.30e-31

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


Pssm-ID: 99730  Cd Length: 86  Bit Score: 115.87  E-value: 3.30e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443048451 403 FSFKLQDRRGRMHRFSCEV-QSLTPLITCILQRLGPDLDRDHLPQILYEDEDRDKVVLASDDDLTAAVDHARLAGWKGLK 481
Cdd:cd06409     1 FAFKFKDPKGRVHRFRLRPsESLEELRTLISQRLGDDDFETHLYALSYVDDEGDIVLITSDSDLVAAVLVARSAGLKKLD 80

                  ....*.
gi 1443048451 482 LYLDYS 487
Cdd:cd06409    81 LHLHYP 86
CBS_pair_MUG70_1 cd17781
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains similar to MUG70 ...
228-334 7.12e-27

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: 104.98  E-value: 7.12e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443048451 228 STVVIVSPGDSVLTATQKMVEVHASSAVVAVGNKA-QGILTSRDILMRMIAKNLPADSTPVEKVMTLDPECATVDMPILD 306
Cdd:cd17781     2 SPALTVPETTTVAEAAQLMAAKRTDAVLVVDDDGGlSGIFTDKDLARRVVASGLDPRSTLVSSVMTPNPLCVTMDTSATD 81
                          90       100
                  ....*....|....*....|....*...
gi 1443048451 307 ALRIMQERKFLHLPVMDRDGSIVSILDV 334
Cdd:cd17781    82 ALDLMVEGKFRHLPVVDDDGDVVGVLDI 109
COG2905 COG2905
Signal-transduction protein containing cAMP-binding, CBS, and nucleotidyltransferase domains ...
228-340 7.49e-24

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


Pssm-ID: 442149 [Multi-domain]  Cd Length: 124  Bit Score: 96.82  E-value: 7.49e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443048451 228 STVVIVSPGDSVLTATQKMVEVHASSA-VVAVGNKAQGILTSRDILMRMIAKNLPADSTPVEKVMTLDPECATVDMPILD 306
Cdd:COG2905     7 RDVVTVSPDATVREAARLMTEKGVGSLvVVDDDGRLVGIITDRDLRRRVLAEGLDPLDTPVSEVMTRPPITVSPDDSLAE 86
                          90       100       110
                  ....*....|....*....|....*....|....
gi 1443048451 307 ALRIMQERKFLHLPVMDrDGSIVSILDVIDITHA 340
Cdd:COG2905    87 ALELMEEHRIRHLPVVD-DGKLVGIVSITDLLRA 119
COG2905 COG2905
Signal-transduction protein containing cAMP-binding, CBS, and nucleotidyltransferase domains ...
55-167 6.03e-23

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


Pssm-ID: 442149 [Multi-domain]  Cd Length: 124  Bit Score: 94.13  E-value: 6.03e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443048451  55 VRRLRLSKALTVPESTTVLEACRRMAARRADAALLTDSNALLCGILTDKDIATRVIARELKIEETPAWKVMTRHPVFVPS 134
Cdd:COG2905     1 VKDIMSRDVVTVSPDATVREAARLMTEKGVGSLVVVDDDGRLVGIITDRDLRRRVLAEGLDPLDTPVSEVMTRPPITVSP 80
                          90       100       110
                  ....*....|....*....|....*....|...
gi 1443048451 135 ETLAVEALHKMVQGKFRHLPVVENGEVIAMLDI 167
Cdd:COG2905    81 DDSLAEALELMEEHRIRHLPVVDDGKLVGIVSI 113
CBS_pair_bact_arch cd17775
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains present in bacteria ...
230-341 7.22e-23

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


Pssm-ID: 341411 [Multi-domain]  Cd Length: 117  Bit Score: 93.76  E-value: 7.22e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443048451 230 VVIVSPGDSVLTATQKMVEVHASSAVVAVG-NKAQGILTSRDILMRMIAKNLPADSTPVEKVMTLDPECATVDMPILDAL 308
Cdd:cd17775     5 VVTASPDTSVLEAARLMRDHHVGSVVVVEEdGKPVGIVTDRDIVVEVVAKGLDPKDVTVGDIMSADLITAREDDGLFEAL 84
                          90       100       110
                  ....*....|....*....|....*....|...
gi 1443048451 309 RIMQERKFLHLPVMDRDGSIVSILDVIDITHAA 341
Cdd:cd17775    85 ERMREKGVRRLPVVDDDGELVGIVTLDDILELL 117
CBS_pair_MUG70_2 cd17782
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains similar to MUG70 ...
61-176 1.13e-22

Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains similar to MUG70 repeat2; Two tandem repeats of the cystathionine beta-synthase (CBS pair) domain, present in MUG70. The MUG70 protein, encoded by the Meiotically Up-regulated Gene 70, plays a role in meiosis and contains, beside the two CBS pairs, a PB1 domain. The CBS domain, named after human CBS, is a small domain originally identified in cystathionine beta-synthase and is subsequently found in a wide range of different proteins. CBS domains usually occur in tandem repeats. They associate to form a so-called Bateman domain or a CBS pair based on crystallographic studies in bacteria. The CBS pair was used as a basis for this cd hierarchy since the human CBS proteins can adopt the typical core structure and form an intramolecular CBS pair. The interface between the two CBS domains forms a cleft that is a potential ligand binding site. The CBS pair coexists with a variety of other functional domains and this has been used to help in its classification here. It has been proposed that the CBS domain may play a regulatory role, although its exact function is unknown. Mutations of conserved residues within this domain are associated with a variety of human hereditary diseases, including congenital myotonia, idiopathic generalized epilepsy, hypercalciuric nephrolithiasis, and classic Bartter syndrome (CLC chloride channel family members), Wolff-Parkinson-White syndrome (gamma 2 subunit of AMP-activated protein kinase), retinitis pigmentosa (IMP dehydrogenase-1), and homocystinuria (cystathionine beta-synthase).


Pssm-ID: 341418 [Multi-domain]  Cd Length: 118  Bit Score: 93.08  E-value: 1.13e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443048451  61 SKALTVPESTTVLEACRRMAARRADAALLTDSNALLCGILTDKDIATRVIARELKIEETPAWKVMTRHPVFVPSETLAVE 140
Cdd:cd17782     2 TPPPLVSPKTTVREAARLMKENRTTAVLVMDNSGKVIGIFTSKDVVLRVLAAGLDPATTSVVRVMTPNPETAPPSTTILD 81
                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 1443048451 141 ALHKMVQGKFRHLPVVEN-GEVIAMLDIAKCLYDAIA 176
Cdd:cd17782    82 ALHKMHEGKFLNLPVVDDeGEIVGLVDVLQLTYATLQ 118
CBS COG0517
CBS domain [Signal transduction mechanisms];
230-340 1.48e-22

CBS domain [Signal transduction mechanisms];


Pssm-ID: 440283 [Multi-domain]  Cd Length: 128  Bit Score: 93.39  E-value: 1.48e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443048451 230 VVIVSPGDSVLTATQKMVEVHASSA-VVAVGNKAQGILTSRDILMRMIAKNLPADSTPVEKVMTLDPECATVDMPILDAL 308
Cdd:COG0517    11 VVTVSPDATVREALELMSEKRIGGLpVVDEDGKLVGIVTDRDLRRALAAEGKDLLDTPVSEVMTRPPVTVSPDTSLEEAA 90
                          90       100       110
                  ....*....|....*....|....*....|..
gi 1443048451 309 RIMQERKFLHLPVMDRDGSIVSILDVIDITHA 340
Cdd:COG0517    91 ELMEEHKIRRLPVVDDDGRLVGIITIKDLLKA 122
CBS_pair_HRP1_like cd04622
CBS pair domain found in Hypoxic Response Protein 1 (HRP1) -like proteinds; Mycobacterium ...
230-337 4.20e-21

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: 88.63  E-value: 4.20e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443048451 230 VVIVSPGDSVLTATQKMVEVHASSAVVAVGNKAQGILTSRDILMRMIAKNLPADSTPVEKVMTLDPECATVDMPILDALR 309
Cdd:cd04622     5 VVTVSPDTTLREAARLMRDLDIGALPVCEGDRLVGMVTDRDIVVRAVAEGKDPNTTTVREVMTGDVVTCSPDDDVEEAAR 84
                          90       100
                  ....*....|....*....|....*...
gi 1443048451 310 IMQERKFLHLPVMDRDGSIVSILDVIDI 337
Cdd:cd04622    85 LMAEHQVRRLPVVDDDGRLVGIVSLGDL 112
CBS_pair_bac_euk cd04623
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains present in bacteria ...
228-335 1.80e-20

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: 86.70  E-value: 1.80e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443048451 228 STVVIVSPGDSVLTATQKMVEvHASSAVVAV--GNKAQGILTSRDILMRMIAKNLPADSTPVEKVMTLDPECATVDMPIL 305
Cdd:cd04623     2 RDVVTVSPDATVAEALRLLAE-KNIGALVVVddGGRLVGILSERDYVRKLALRGASSLDTPVSEIMTRDVVTCTPDDTVE 80
                          90       100       110
                  ....*....|....*....|....*....|...
gi 1443048451 306 DALRIMQERKFLHLPVMDrDGS---IVSILDVI 335
Cdd:cd04623    81 ECMALMTERRIRHLPVVE-DGKlvgIVSIGDVV 112
COG2524 COG2524
Predicted transcriptional regulator, contains C-terminal CBS domains [Transcription];
228-340 5.11e-19

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


Pssm-ID: 442013 [Multi-domain]  Cd Length: 206  Bit Score: 85.71  E-value: 5.11e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443048451 228 STVVIVSPGDSVLTATQKMVEVHASSAVVAVGNKAQGILTSRDILmRMIAKNLPADSTPVEKVMTLDPECATVDMPILDA 307
Cdd:COG2524    94 KDVITVSPDTTLEEALELMLEKGISGLPVVDDGKLVGIITERDLL-KALAEGRDLLDAPVSDIMTRDVVTVSEDDSLEEA 172
                          90       100       110
                  ....*....|....*....|....*....|...
gi 1443048451 308 LRIMQERKFLHLPVMDRDGSIVSILDVIDITHA 340
Cdd:COG2524   173 LRLMLEHGIGRLPVVDDDGKLVGIITRTDILRA 205
CBS_pair_CAP-ED_NT_Pol-beta-like_DUF294_assoc cd04587
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with the ...
230-340 7.39e-19

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: 82.09  E-value: 7.39e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443048451 230 VVIVSPGDSVLTATQKMVEVHASSAVVAVGNKAQGILTSRDILMRMIAKNLPADsTPVEKVMTLDPECATVDMPILDALR 309
Cdd:cd04587     6 PVTVPPDATIQEAAQLMSEERVSSLLVVDDGRLVGIVTDRDLRNRVVAEGLDPD-TPVSEIMTPPPVTIDADALVFEALL 84
                          90       100       110
                  ....*....|....*....|....*....|.
gi 1443048451 310 IMQERKFLHLPVMDrDGSIVSILDVIDITHA 340
Cdd:cd04587    85 LMLERNIHHLPVVD-DGRVVGVVTATDLMRL 114
CBS_pair_SF cd02205
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains superfamily; The CBS ...
230-337 7.80e-19

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: 82.29  E-value: 7.80e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443048451 230 VVIVSPGDSVLTATQKMVEVHASSA-VVAVGNKAQGILTSRDILmRMIAKNLPADSTPVEKVMTLDPECATVDMPILDAL 308
Cdd:cd02205     4 VVTVDPDTTVREALELMAENGIGALpVVDDDGKLVGIVTERDIL-RALVEGGLALDTPVAEVMTPDVITVSPDTDLEEAL 82
                          90       100
                  ....*....|....*....|....*....
gi 1443048451 309 RIMQERKFLHLPVMDRDGSIVSILDVIDI 337
Cdd:cd02205    83 ELMLEHGIRRLPVVDDDGKLVGIVTRRDI 111
CBS_pair_arch cd09836
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains; The CBS domain, ...
228-338 7.96e-19

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: 82.19  E-value: 7.96e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443048451 228 STVVIVSPGDSVLTATQKMVEVHASSAV-VAVGNKAQGILTSRDILmRMIAKNLPADsTPVEKVMTLDPECATVDMPILD 306
Cdd:cd09836     3 KPVVTVPPETTIREAAKLMAENNIGSVVvVDDDGKPVGIVTERDIV-RAVAEGIDLD-TPVEEIMTKNLVTVSPDESIYE 80
                          90       100       110
                  ....*....|....*....|....*....|..
gi 1443048451 307 ALRIMQERKFLHLPVMDRDGSIVSILDVIDIT 338
Cdd:cd09836    81 AAELMREHNIRHLPVVDGGGKLVGVISIRDLA 112
CBS_pair_CAP-ED_NT_Pol-beta-like_DUF294_assoc cd04587
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with the ...
96-165 2.10e-17

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: 78.24  E-value: 2.10e-17
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443048451  96 LCGILTDKDIATRVIARELKIEeTPAWKVMTRHPVFVPSETLAVEALHKMVQGKFRHLPVVENGEVIAML 165
Cdd:cd04587    38 LVGIVTDRDLRNRVVAEGLDPD-TPVSEIMTPPPVTIDADALVFEALLLMLERNIHHLPVVDDGRVVGVV 106
COG3448 COG3448
CBS-domain-containing membrane protein [Signal transduction mechanisms];
230-340 2.31e-17

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


Pssm-ID: 442671 [Multi-domain]  Cd Length: 136  Bit Score: 78.75  E-value: 2.31e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443048451 230 VVIVSPGDSVLTATQKMVEVHASSA-VVAVGNKAQGILTSRDILMRMIAKNLP-----ADSTPVEKVMTLDPECATVDMP 303
Cdd:COG3448    12 VVTVSPDTTLREALELMREHGIRGLpVVDEDGRLVGIVTERDLLRALLPDRLDeleerLLDLPVEDVMTRPVVTVTPDTP 91
                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 1443048451 304 ILDALRIMQERKFLHLPVMDRDGSIVSILDVIDITHA 340
Cdd:COG3448    92 LEEAAELMLEHGIHRLPVVDDDGRLVGIVTRTDLLRA 128
CBS COG0517
CBS domain [Signal transduction mechanisms];
54-176 4.14e-17

CBS domain [Signal transduction mechanisms];


Pssm-ID: 440283 [Multi-domain]  Cd Length: 128  Bit Score: 77.60  E-value: 4.14e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443048451  54 TVRRLRLSKALTVPESTTVLEACRRMAARRADAALLTDSNALLCGILTDKDIATRVIARELKIEETPAWKVMTRHPVFVP 133
Cdd:COG0517     2 KVKDIMTTDVVTVSPDATVREALELMSEKRIGGLPVVDEDGKLVGIVTDRDLRRALAAEGKDLLDTPVSEVMTRPPVTVS 81
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 1443048451 134 SETLAVEALHKMVQGKFRHLPVVENGE----VIAMLDIAKCLYDAIA 176
Cdd:COG0517    82 PDTSLEEAAELMEEHKIRRLPVVDDDGrlvgIITIKDLLKALLEPLA 128
CBS_pair_bac_euk cd04623
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains present in bacteria ...
88-167 1.71e-14

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: 69.75  E-value: 1.71e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443048451  88 LLTDSNALLCGILTDKDIATRVIARELKIEETPAWKVMTRHPVFVPSETLAVEALHKMVQGKFRHLPVVENGEVIAMLDI 167
Cdd:cd04623    29 VVVDDGGRLVGILSERDYVRKLALRGASSLDTPVSEIMTRDVVTCTPDDTVEECMALMTERRIRHLPVVEDGKLVGIVSI 108
YtoI COG4109
Predicted transcriptional regulator containing CBS domains [Transcription];
211-335 4.16e-13

Predicted transcriptional regulator containing CBS domains [Transcription];


Pssm-ID: 443285 [Multi-domain]  Cd Length: 135  Bit Score: 66.47  E-value: 4.16e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443048451 211 FKEQMLrpsLSTITTAESTVVIvSPGDSVLTATQKMVEVHASSA-VVAVGNKAQGILTSRDILMRMiaknlpaDSTPVEK 289
Cdd:COG4109    12 FKEILL---VEDIMTLEDVATL-SEDDTVEDALELLEKTGHSRFpVVDENGRLVGIVTSKDILGKD-------DDTPIED 80
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 1443048451 290 VMTLDPECATVDMPILDALRIMQERKFLHLPVMDRDGSIVSIL---DVI 335
Cdd:COG4109    81 VMTKNPITVTPDTSLASAAHKMIWEGIELLPVVDDDGRLLGIIsrqDVL 129
CBS_pair_SF cd02205
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains superfamily; The CBS ...
61-165 8.57e-13

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: 64.96  E-value: 8.57e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443048451  61 SKALTVPESTTVLEACRRMAARRADAALLTDSNALLCGILTDKDIAtRVIARELKIEETPAWKVMTRHPVFVPSETLAVE 140
Cdd:cd02205     2 RDVVTVDPDTTVREALELMAENGIGALPVVDDDGKLVGIVTERDIL-RALVEGGLALDTPVAEVMTPDVITVSPDTDLEE 80
                          90       100
                  ....*....|....*....|....*.
gi 1443048451 141 ALHKMVQGKFRHLPVV-ENGEVIAML 165
Cdd:cd02205    81 ALELMLEHGIRRLPVVdDDGKLVGIV 106
CBS_pair_HRP1_like cd04622
CBS pair domain found in Hypoxic Response Protein 1 (HRP1) -like proteinds; Mycobacterium ...
96-168 1.66e-12

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: 63.98  E-value: 1.66e-12
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1443048451  96 LCGILTDKDIATRVIARELKIEETPAWKVMTRHPVFVPSETLAVEALHKMVQGKFRHLPVVENGE----VIAMLDIA 168
Cdd:cd04622    37 LVGMVTDRDIVVRAVAEGKDPNTTTVREVMTGDVVTCSPDDDVEEAARLMAEHQVRRLPVVDDDGrlvgIVSLGDLA 113
CBS_pair_arch cd09836
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains; The CBS domain, ...
61-169 3.19e-12

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: 63.31  E-value: 3.19e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443048451  61 SKALTVPESTTVLEACRRMAARRADAALLTDSNALLCGILTDKDIaTRVIARElKIEETPAWKVMTRHPVFVPSETLAVE 140
Cdd:cd09836     3 KPVVTVPPETTIREAAKLMAENNIGSVVVVDDDGKPVGIVTERDI-VRAVAEG-IDLDTPVEEIMTKNLVTVSPDESIYE 80
                          90       100       110
                  ....*....|....*....|....*....|...
gi 1443048451 141 ALHKMVQGKFRHLPVVENGE----VIAMLDIAK 169
Cdd:cd09836    81 AAELMREHNIRHLPVVDGGGklvgVISIRDLAR 113
CBS_pair_AcuB_like cd04584
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with the ...
230-341 6.81e-12

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: 62.82  E-value: 6.81e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443048451 230 VVIVSPGDSVLTATQKMVEVHASSAVVAVGNKAQGILTSRDIL---------MRMIAKNLPADSTPVEKVMTLDPECATV 300
Cdd:cd04584    10 VVTVTPDTSLAEARELMKEHKIRHLPVVDDGKLVGIVTDRDLLraspskatsLSIYELNYLLSKIPVKDIMTKDVITVSP 89
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 1443048451 301 DMPILDALRIMQERKFLHLPVMDrDGSIVSILDVIDITHAA 341
Cdd:cd04584    90 DDTVEEAALLMLENKIGCLPVVD-GGKLVGIITETDILRAF 129
CBS_pair_SIS_assoc cd04604
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with the ...
90-167 6.86e-12

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: 62.78  E-value: 6.86e-12
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1443048451  90 TDSNALLCGILTDKDIAtRVIARELKIEETPAWKVMTRHPVFVPSETLAVEALHKMVQGKFRHLPVV-ENGEVIAMLDI 167
Cdd:cd04604    42 VDEDGRLVGIITDGDLR-RALEKGLDILNLPAKDVMTRNPKTISPDALAAEALELMEEHKITVLPVVdEDGKPVGILHL 119
CBS_arch_repeat1 cd17777
CBS pair domains found in archeal proteins, repeat 1; CBS pair domains found in archeal ...
230-332 6.90e-12

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: 63.13  E-value: 6.90e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443048451 230 VVIVSPGDSVLTATQKMVEVHASSAVVAVGNKAQGILTSRDIL-------MRMIAKNL-------PADSTPVEKVMTLDP 295
Cdd:cd17777    12 VLSISPSAPILSAFEKMNRRGIRRLVVVDENKLEGILSARDLVsylgggcLFKIVESRhqgdlysALNREVVETIMTPNP 91
                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 1443048451 296 ECATVDMPILDALRIMQERKFLHLPVMDRDGSIVSIL 332
Cdd:cd17777    92 VYVYEDSDLIEALTIMVTRGIGSLPVVDRDGRPVGIV 128
PB1 pfam00564
PB1 domain;
402-487 2.85e-11

PB1 domain;


Pssm-ID: 395447  Cd Length: 84  Bit Score: 59.61  E-value: 2.85e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443048451 402 SFSFKLQDRRGRMHRFS-CEVQSLTPLITCILQRLGpdlDRDHLPQILYEDEDRDKVVLASDDDLTAAVDHARLAGWKGL 480
Cdd:pfam00564   1 TVRLKLRYGGGIRRFLSvSRGISFEELRALVEQRFG---LDDVDFKLKYPDEDGDLVSLTSDEDLEEALEEARSLGSKSL 77

                  ....*..
gi 1443048451 481 KLYLDYS 487
Cdd:pfam00564  78 RLHVFPT 84
CBS_pair_ParBc_assoc cd04610
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with a ...
230-337 3.11e-11

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: 60.41  E-value: 3.11e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443048451 230 VVIVSPGDSVLTATQKMVEVHASSAVVAVGNKAQGILTSRDILMRMiaknlpaDSTPVEKVMTLDPECATVDMPILDALR 309
Cdd:cd04610     5 VITVSPDDTVKDVIKLIKETGHDGFPVVDDGKVVGYVTAKDLLGKD-------DDEKVSEIMSRDTVVADPDMDITDAAR 77
                          90       100
                  ....*....|....*....|....*...
gi 1443048451 310 IMQERKFLHLPVMDRDGSIVSILDVIDI 337
Cdd:cd04610    78 VIFRSGISKLPVVDDEGNLVGIITNMDV 105
PB1 smart00666
PB1 domain; Phox and Bem1p domain, present in many eukaryotic cytoplasmic signalling proteins. ...
402-485 1.14e-10

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


Pssm-ID: 214770  Cd Length: 81  Bit Score: 57.98  E-value: 1.14e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443048451  402 SFSFKLQDRrGRMHRFSCEVQ-SLTPLITCILQRLGpdLDRDHlPQILYEDEDRDKVVLASDDDLTAAVDHARLAGWKGL 480
Cdd:smart00666   1 TVDVKLRYG-GETRRLSVPRDiSFEDLRSKVAKRFG--LDNQS-FTLKYQDEDGDLVSLTSDEDLEEAIEEYDSLGSKKL 76

                   ....*
gi 1443048451  481 KLYLD 485
Cdd:smart00666  77 RLHVF 81
CBS_pair_bact_arch cd17775
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains present in bacteria ...
97-171 1.27e-10

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: 58.71  E-value: 1.27e-10
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1443048451  97 CGILTDKDIATRVIARELKIEETPAWKVMTRHPVFVPSETLAVEALHKMVQGKFRHLPVV-ENGE---VIAMLDIAKCL 171
Cdd:cd17775    39 VGIVTDRDIVVEVVAKGLDPKDVTVGDIMSADLITAREDDGLFEALERMREKGVRRLPVVdDDGElvgIVTLDDILELL 117
CBS_pair_SIS_assoc cd04604
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with the ...
232-337 1.75e-10

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: 58.55  E-value: 1.75e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443048451 232 IVSPGDSVLTA----TQK---MVevhassAVVAVGNKAQGILTSRDiLMRMIAKNLPADSTPVEKVMTLDPECATVDMPI 304
Cdd:cd04604    17 LVSPDTSLKEAllemTRKglgCT------AVVDEDGRLVGIITDGD-LRRALEKGLDILNLPAKDVMTRNPKTISPDALA 89
                          90       100       110
                  ....*....|....*....|....*....|...
gi 1443048451 305 LDALRIMQERKFLHLPVMDRDGSIVSILDVIDI 337
Cdd:cd04604    90 AEALELMEEHKITVLPVVDEDGKPVGILHLHDL 122
COG2524 COG2524
Predicted transcriptional regulator, contains C-terminal CBS domains [Transcription];
1-171 2.27e-10

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


Pssm-ID: 442013 [Multi-domain]  Cd Length: 206  Bit Score: 60.28  E-value: 2.27e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443048451   1 MAGRRSSPPRRTMSMGSGSLPRRPTAAAGGAGSMLPGLSRSMTMGGGGVGGER----------TVRRLRLSKALTVPEST 70
Cdd:COG2524    24 LLLAALVLALTAAAAATVLLLAAAAAAAGAGGLGLLLLLLLIVLQAAAVRVVAekelglvlkmKVKDIMTKDVITVSPDT 103
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443048451  71 TVLEACRRMAARRADAALLTDSNALLcGILTDKDIAtRVIARELKIEETPAWKVMTRHPVFVPSETLAVEALHKMVQGKF 150
Cdd:COG2524   104 TLEEALELMLEKGISGLPVVDDGKLV-GIITERDLL-KALAEGRDLLDAPVSDIMTRDVVTVSEDDSLEEALRLMLEHGI 181
                         170       180
                  ....*....|....*....|....*
gi 1443048451 151 RHLPVVE-NGEVIAML---DIAKCL 171
Cdd:COG2524   182 GRLPVVDdDGKLVGIItrtDILRAL 206
COG3448 COG3448
CBS-domain-containing membrane protein [Signal transduction mechanisms];
90-177 7.83e-10

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


Pssm-ID: 442671 [Multi-domain]  Cd Length: 136  Bit Score: 57.18  E-value: 7.83e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443048451  90 TDSNALLCGILTDKDIATRVIAREL-----KIEETPAWKVMTRHPVFVPSETLAVEALHKMVQGKFRHLPVV-ENGEVIA 163
Cdd:COG3448    39 VDEDGRLVGIVTERDLLRALLPDRLdeleeRLLDLPVEDVMTRPVVTVTPDTPLEEAAELMLEHGIHRLPVVdDDGRLVG 118
                          90
                  ....*....|....*..
gi 1443048451 164 ML---DIAKCLYDAIAR 177
Cdd:COG3448   119 IVtrtDLLRALARLLEE 135
CBS_arch_repeat2 cd17778
CBS pair domains found in archeal proteins, repeat 2; CBS pair domains found in archeal ...
120-275 9.68e-10

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: 56.57  E-value: 9.68e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443048451 120 PAWKVMTRHPVFVPSETLAVEALHKMVQGKFRHLPVVENGEVIAMLDIAkclyDAIARIERASDKgkaaaiasavdaaag 199
Cdd:cd17778     1 KVKEFMTTPVVTIYPDDTLKEAMELMVTRGFRRLPVVSGGKLVGIVTAM----DIVKYFGSHEAK--------------- 61
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443048451 200 NDPTASSMVEAF----KEQMLRPslstittaestVVIVSPGDSVLTATQKMVEVHASSAVVAVG-NKAQGILTSRDILMR 274
Cdd:cd17778    62 KRLTTGDIDEAYstpvEEIMSKE-----------VVTIEPDADIAEAARLMIKKNVGSLLVVDDeGELKGIITERDVLIA 130

                  .
gi 1443048451 275 M 275
Cdd:cd17778   131 L 131
CBS_pair_NTP_transferase_assoc cd04607
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domain associated with the ...
231-329 1.24e-09

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: 55.91  E-value: 1.24e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443048451 231 VIVSPGDSVLTAtqkmVEVHASSA-----VVAVGNKAQGILTSRDIlMRMIAKNLPADStPVEKVMTLDPECATVDMPIL 305
Cdd:cd04607     5 VLVSPDTTIREA----IEVIDKGAlqialVVDENRKLLGTVTDGDI-RRGLLKGLSLDA-PVEEVMNKNPITASPSTSRE 78
                          90       100
                  ....*....|....*....|....
gi 1443048451 306 DALRIMQERKFLHLPVMDRDGSIV 329
Cdd:cd04607    79 ELLALMRAKKILQLPIVDEQGRVV 102
CBS_pair_archHTH_assoc cd04588
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains found in archaea and ...
230-336 6.46e-09

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: 53.69  E-value: 6.46e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443048451 230 VVIVSPGDSVLTATQKMVEVHASSAVVAVGNKAQGILTSRDIlMRMIAKNLPadSTPVEKVMTLDPECATVDMPILDALR 309
Cdd:cd04588     4 LITLKPDATIKDAAKLLSENNIHGAPVVDDGKLVGIVTLTDI-AKALAEGKE--NAKVKDIMTKDVITIDKDEKIYDAIR 80
                          90       100       110
                  ....*....|....*....|....*....|
gi 1443048451 310 IMQERKFLHLPVMDRDGSIVSIL---DVID 336
Cdd:cd04588    81 LMNKHNIGRLIVVDDNGKPVGIItrtDILK 110
PB1 cd05992
The PB1 domain is a modular domain mediating specific protein-protein interactions which play ...
411-485 7.15e-09

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


Pssm-ID: 99716 [Multi-domain]  Cd Length: 81  Bit Score: 52.67  E-value: 7.15e-09
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1443048451 411 RGRMHRFSCEVQSLT--PLITCILQRLGpdlDRDHLPQILYEDEDRDKVVLASDDDLTAAVDHARLAGWKGLKLYLD 485
Cdd:cd05992     8 GGEIRRFVVVSRSISfeDLRSKIAEKFG---LDAVSFKLKYPDEDGDLVTISSDEDLEEAIEEARRSGSKKLRLFVF 81
CBS_pair_AcuB_like cd04584
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with the ...
125-272 1.12e-08

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: 53.58  E-value: 1.12e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443048451 125 MTRHPVFVPSETLAVEALHKMVQGKFRHLPVVENGEVIAML---DIAkclydaiarieRASdkgkaaaiasavdaaagnd 201
Cdd:cd04584     6 MTKNVVTVTPDTSLAEARELMKEHKIRHLPVVDDGKLVGIVtdrDLL-----------RAS------------------- 55
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1443048451 202 ptaSSMVEAFKEQMLRPSLSTITTAE---STVVIVSPGDSVLTATQKMVEVHASSAVVAVGNKAQGILTSRDIL 272
Cdd:cd04584    56 ---PSKATSLSIYELNYLLSKIPVKDimtKDVITVSPDDTVEEAALLMLENKIGCLPVVDGGKLVGIITETDIL 126
CBS pfam00571
CBS domain; CBS domains are small intracellular modules that pair together to form a stable ...
287-340 1.25e-08

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


Pssm-ID: 425756 [Multi-domain]  Cd Length: 57  Bit Score: 51.45  E-value: 1.25e-08
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1443048451 287 VEKVMTLDPECATVDMPILDALRIMQERKFLHLPVMDRDGSIVSILDVIDITHA 340
Cdd:pfam00571   1 VKDIMTKDVVTVSPDTTLEEALELMREHGISRLPVVDEDGKLVGIVTLKDLLRA 54
CBS_pair_CAP-ED_NT_Pol-beta-like_DUF294_assoc cd17771
CBS domain protein; This cd contains two tandem repeats of the cystathionine beta-synthase ...
231-325 2.10e-08

CBS domain protein; This cd contains two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with the bacterial CAP_ED (cAMP receptor protein effector domain) family of transcription factors, the NT_Pol-beta-like domain, and the DUF294 domain. Members of CAP_ED, include CAP which binds cAMP, FNR (fumarate and nitrate reductase) which uses an iron-sulfur cluster to sense oxygen, and CooA a heme containing CO sensor. In all cases binding of the effector leads to conformational changes and the ability to activate transcription. The NT_Pol-beta-like domain includes the Nucleotidyltransferase (NT) domains of DNA polymerase beta and other family X DNA polymerases, as well as the NT domains of class I and class II CCA-adding enzymes, RelA- and SpoT-like ppGpp synthetases and hydrolases, 2'5'-oligoadenylate (2-5A)synthetases, Escherichia coli adenylyltransferase (GlnE), Escherichia coli uridylyl transferase (GlnD), poly (A) polymerases, terminal uridylyl transferases, Staphylococcus aureus kanamycin nucleotidyltransferase, and similar proteins. DUF294 is a putative nucleotidyltransferase with a conserved DxD motif. CBS is a small domain originally identified in cystathionine beta-synthase and subsequently found in a wide range of different proteins. The CBS domain, named after human CBS, is a small domain originally identified in cystathionine beta-synthase and is subsequently found in a wide range of different proteins. CBS domains usually occur in tandem repeats. They associate to form a so-called Bateman domain or a CBS pair based on crystallographic studies in bacteria. The CBS pair was used as a basis for this cd hierarchy since the human CBS proteins can adopt the typical core structure and form an intramolecular CBS pair. The interface between the two CBS domains forms a cleft that is a potential ligand binding site. The CBS pair coexists with a variety of other functional domains and this has been used to help in its classification here. It has been proposed that the CBS domain may play a regulatory role, although its exact function is unknown. Mutations of conserved residues within this domain are associated with a variety of human hereditary diseases, including congenital myotonia, idiopathic generalized epilepsy, hypercalciuric nephrolithiasis, and classic Bartter syndrome (CLC chloride channel family members), Wolff-Parkinson-White syndrome (gamma 2 subunit of AMP-activated protein kinase), retinitis pigmentosa (IMP dehydrogenase-1), and homocystinuria (cystathionine beta-synthase).


Pssm-ID: 341407 [Multi-domain]  Cd Length: 115  Bit Score: 52.32  E-value: 2.10e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443048451 231 VIVSPGDSVLTATQKMVEVHASSAVVAVGN-KAQGILTSRDILMRMIAKNLPADsTPVEKVMTLDPECATVDMPILDALR 309
Cdd:cd17771     7 VTCSPDTPLRAALETMHERRVGSMVVVDANrRPVGIFTLRDLLSRVALPQIDLD-APISEVMTPDPVRLPPSASAFEAAL 85
                          90
                  ....*....|....*.
gi 1443048451 310 IMQERKFLHLPVMDRD 325
Cdd:cd17771    86 LMAEHGFRHVCVVDNG 101
CBS_archAMPK_gamma-repeat2 cd04631
CBS pair domains found in archeal 5'-AMP-activated protein kinase gamma subunit-like proteins; ...
230-340 2.14e-08

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: 53.00  E-value: 2.14e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443048451 230 VVIVSPGDSVLTATQKMVEVHASSAVVAVGNKAQGILTSRDILM---------RMIAKNL-PADSTPVEKVMTLDPECAT 299
Cdd:cd04631    10 VITATPGTPIEDVAKIMVRNGFRRLPVVSDGKLVGIVTSTDIMRylgsgeafeKLKTGNIhEVLNVPISSIMKRDIITTT 89
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 1443048451 300 VDMPILDALRIMQERKFLHLPVMDrDGSIVSILDVIDITHA 340
Cdd:cd04631    90 PDTDLGEAAELMLEKNIGALPVVD-DGKLVGIITERDILRA 129
YtoI COG4109
Predicted transcriptional regulator containing CBS domains [Transcription];
91-165 2.77e-08

Predicted transcriptional regulator containing CBS domains [Transcription];


Pssm-ID: 443285 [Multi-domain]  Cd Length: 135  Bit Score: 52.61  E-value: 2.77e-08
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1443048451  91 DSNALLCGILTDKDIATrviarelKIEETPAWKVMTRHPVFV-PSETLAvEALHKMVQGKFRHLPVV-ENGEVIAML 165
Cdd:COG4109    55 DENGRLVGIVTSKDILG-------KDDDTPIEDVMTKNPITVtPDTSLA-SAAHKMIWEGIELLPVVdDDGRLLGII 123
CBS_pair_IMPDH cd04601
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains in the inosine 5' ...
231-337 3.82e-08

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: 51.65  E-value: 3.82e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443048451 231 VIVSPGDSVLTATQKMVEVHASS-AVVAVGNKAQGILTSRDIlmrmiaKNLPADSTPVEKVMTLDPECATVDMPI--LDA 307
Cdd:cd04601     5 VTLSPDATVADVLELKAEYGISGvPVTEDGGKLVGIVTSRDI------RFETDLSTPVSEVMTPDERLVTAPEGItlEEA 78
                          90       100       110
                  ....*....|....*....|....*....|
gi 1443048451 308 LRIMQERKFLHLPVMDRDGSIVSILDVIDI 337
Cdd:cd04601    79 KEILHKHKIEKLPIVDDNGELVGLITRKDI 108
CBS_pair_CAP-ED_NT_Pol-beta-like_DUF294_assoc cd17771
CBS domain protein; This cd contains two tandem repeats of the cystathionine beta-synthase ...
90-165 4.89e-08

CBS domain protein; This cd contains two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with the bacterial CAP_ED (cAMP receptor protein effector domain) family of transcription factors, the NT_Pol-beta-like domain, and the DUF294 domain. Members of CAP_ED, include CAP which binds cAMP, FNR (fumarate and nitrate reductase) which uses an iron-sulfur cluster to sense oxygen, and CooA a heme containing CO sensor. In all cases binding of the effector leads to conformational changes and the ability to activate transcription. The NT_Pol-beta-like domain includes the Nucleotidyltransferase (NT) domains of DNA polymerase beta and other family X DNA polymerases, as well as the NT domains of class I and class II CCA-adding enzymes, RelA- and SpoT-like ppGpp synthetases and hydrolases, 2'5'-oligoadenylate (2-5A)synthetases, Escherichia coli adenylyltransferase (GlnE), Escherichia coli uridylyl transferase (GlnD), poly (A) polymerases, terminal uridylyl transferases, Staphylococcus aureus kanamycin nucleotidyltransferase, and similar proteins. DUF294 is a putative nucleotidyltransferase with a conserved DxD motif. CBS is a small domain originally identified in cystathionine beta-synthase and subsequently found in a wide range of different proteins. The CBS domain, named after human CBS, is a small domain originally identified in cystathionine beta-synthase and is subsequently found in a wide range of different proteins. CBS domains usually occur in tandem repeats. They associate to form a so-called Bateman domain or a CBS pair based on crystallographic studies in bacteria. The CBS pair was used as a basis for this cd hierarchy since the human CBS proteins can adopt the typical core structure and form an intramolecular CBS pair. The interface between the two CBS domains forms a cleft that is a potential ligand binding site. The CBS pair coexists with a variety of other functional domains and this has been used to help in its classification here. It has been proposed that the CBS domain may play a regulatory role, although its exact function is unknown. Mutations of conserved residues within this domain are associated with a variety of human hereditary diseases, including congenital myotonia, idiopathic generalized epilepsy, hypercalciuric nephrolithiasis, and classic Bartter syndrome (CLC chloride channel family members), Wolff-Parkinson-White syndrome (gamma 2 subunit of AMP-activated protein kinase), retinitis pigmentosa (IMP dehydrogenase-1), and homocystinuria (cystathionine beta-synthase).


Pssm-ID: 341407 [Multi-domain]  Cd Length: 115  Bit Score: 51.55  E-value: 4.89e-08
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1443048451  90 TDSNALLCGILTDKDIATRVIARELKIEeTPAWKVMTRHPVFVPSETLAVEALHKMVQGKFRHLPVVENGEVIAML 165
Cdd:cd17771    33 VDANRRPVGIFTLRDLLSRVALPQIDLD-APISEVMTPDPVRLPPSASAFEAALLMAEHGFRHVCVVDNGRLVGVV 107
CBS_two-component_sensor_histidine_kinase_repeat1 cd04620
2 tandem repeats of the CBS domain in the two-component sensor histidine kinase and ...
223-332 5.09e-08

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: 51.77  E-value: 5.09e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443048451 223 ITTAESTV--VI-----VSPGDSVLTATQKMVEVHASSAVVAVGNKAQGILTSRDILmRMIAKNLPADSTPVEKVMTLDP 295
Cdd:cd04620    11 TVSPDTPVieAIalmsqTRSSCCLLSEDSIITEARSSCVLVVENQQLVGIFTERDVV-RLTASGIDLSGVTIAEVMTQPV 89
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 1443048451 296 ----ECATVDmpILDALRIMQERKFLHLPVMDRDGSIVSIL 332
Cdd:cd04620    90 itlkESEFQD--IFTVLSLLRQHQIRHLPIVDDQGQLVGLI 128
CBS_pair_BON_assoc cd04586
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with the ...
230-340 5.13e-08

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: 52.05  E-value: 5.13e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443048451 230 VVIVSPGDSVLTATQKMVEVHASSA-VVAVGNKAQGILTSRDILMRMIAKNLP----------------------ADSTP 286
Cdd:cd04586     5 VVTVTPDTSVREAARLLLEHRISGLpVVDDDGKLVGIVSEGDLLRREEPGTEPrrvwwldallesperlaeeyvkAHGRT 84
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1443048451 287 VEKVMTLDPECATVDMPILDALRIMQERKFLHLPVMDrDGSIVSILDVIDITHA 340
Cdd:cd04586    85 VGDVMTRPVVTVSPDTPLEEAARLMERHRIKRLPVVD-DGKLVGIVSRADLLRA 137
CBS_pair_CAP-ED_NT_Pol-beta-like_DUF294_assoc cd04589
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with the ...
231-337 7.12e-08

Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with the bacterial CAP_ED (cAMP receptor protein effector domain) family of transcription factors, the NT (Nucleotidyltransferase) Pol-beta-like domain, and the DUF294 dom; This cd contains two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with the bacterial CAP_ED (cAMP receptor protein effector domain) family of transcription factors, the NT_Pol-beta-like domain, and the DUF294 domain. Members of CAP_ED, include CAP which binds cAMP, FNR (fumarate and nitrate reductase) which uses an iron-sulfur cluster to sense oxygen, and CooA a heme containing CO sensor. In all cases binding of the effector leads to conformational changes and the ability to activate transcription. The NT_Pol-beta-like domain includes the Nucleotidyltransferase (NT) domains of DNA polymerase beta and other family X DNA polymerases, as well as the NT domains of class I and class II CCA-adding enzymes, RelA- and SpoT-like ppGpp synthetases and hydrolases, 2'5'-oligoadenylate (2-5A)synthetases, Escherichia coli adenylyltransferase (GlnE), Escherichia coli uridylyl transferase (GlnD), poly (A) polymerases, terminal uridylyl transferases, Staphylococcus aureus kanamycin nucleotidyltransferase, and similar proteins. DUF294 is a putative nucleotidyltransferase with a conserved DxD motif. CBS is a small domain originally identified in cystathionine beta-synthase and subsequently found in a wide range of different proteins. The CBS domain, named after human CBS, is a small domain originally identified in cystathionine beta-synthase and is subsequently found in a wide range of different proteins. CBS domains usually occur in tandem repeats. They associate to form a so-called Bateman domain or a CBS pair based on crystallographic studies in bacteria. The CBS pair was used as a basis for this cd hierarchy since the human CBS proteins can adopt the typical core structure and form an intramolecular CBS pair. The interface between the two CBS domains forms a cleft that is a potential ligand binding site. The CBS pair coexists with a variety of other functional domains and this has been used to help in its classification here. It has been proposed that the CBS domain may play a regulatory role, although its exact function is unknown. Mutations of conserved residues within this domain are associated with a variety of human hereditary diseases, including congenital myotonia, idiopathic generalized epilepsy, hypercalciuric nephrolithiasis, and classic Bartter syndrome (CLC chloride channel family members), Wolff-Parkinson-White syndrome (gamma 2 subunit of AMP-activated protein kinase), retinitis pigmentosa (IMP dehydrogenase-1), and homocystinuria (cystathionine beta-synthase).


Pssm-ID: 341365 [Multi-domain]  Cd Length: 113  Bit Score: 51.03  E-value: 7.12e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443048451 231 VIVSPGDSVLTATQKMVEVHASSAVVAVGNKAQGILTSRDILMRMIAKNLPADsTPVEKVMTLDPECATVDMPILDALRI 310
Cdd:cd04589     6 LFVDAETSIREATRLMKENGADSLLVRDGDGRVGIVTRTDLRDAVVLDGQPVD-TPVGEIATFPLISVEPDDFLFNALLL 84
                          90       100
                  ....*....|....*....|....*..
gi 1443048451 311 MQERKFLHLPVMDrDGSIVSILDVIDI 337
Cdd:cd04589    85 MTRHRVKRVVVRE-GEEIVGVLEQTDL 110
CBS_two-component_sensor_histidine_kinase_repeat2 cd17774
2 tandem repeats of the CBS domain in the two-component sensor histidine kinase and ...
228-336 8.10e-08

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


Pssm-ID: 341410 [Multi-domain]  Cd Length: 137  Bit Score: 51.38  E-value: 8.10e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443048451 228 STVVIVSPGDSVLTATQKMVEVHASSAVVAVGNKAQ--------GILTSRDILmRMIAKNLPADSTPVEKVMTLDPECAT 299
Cdd:cd17774     5 TRVIHAPPTASVLELAQLMAEHRVSCVVIVEEDEQQeknklipvGIVTERDIV-QFQALGLDLSQTQAQTVMSSPLFSLR 83
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 1443048451 300 VDMPILDALRIMQERKFLHLPVMDRDG---SIV---SILDVID 336
Cdd:cd17774    84 PDDSLWTAHQLMQQRRIRRLVVVGEQGellGIVtqtSLLQALD 126
PRK14869 PRK14869
putative manganese-dependent inorganic diphosphatase;
124-332 1.62e-07

putative manganese-dependent inorganic diphosphatase;


Pssm-ID: 237843 [Multi-domain]  Cd Length: 546  Bit Score: 54.07  E-value: 1.62e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443048451 124 VMTRHPVFVPSETLAVEALHKMVQGKFRHLPVVENGE----VIAMLDIAKCL---------------YDAIARIErasdK 184
Cdd:PRK14869   73 LEIDKPVTVSPDTSLKEAWNLMDENNVKTLPVVDEEGkllgLVSLSDLARAYmdildpeilsksptsLENIIRTL----D 148
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443048451 185 GKAAAIASAVDAAAGNDPTASSMVEAFKEQMlrpslstittAESTVVIVspGDSVlTATQKMVEVHASSAVVAVGN---- 260
Cdd:PRK14869  149 GEVLVGAEEDKVEEGKVVVAAMAPESLLERI----------EEGDIVIV--GDRE-DIQLAAIEAGVRLLIITGGApvse 215
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443048451 261 ------KAQG---ILTSRD--ILMRMIakNLpadSTPVEKVMTL-DPECATVDMPILDALRIMQERKFLHLPVMDRDGSI 328
Cdd:PRK14869  216 dvlelaKENGvtvISTPYDtfTTARLI--NQ---SIPVSYIMTTeDLVTFSKDDYLEDVKEVMLKSRYRSYPVVDEDGKV 290

                  ....
gi 1443048451 329 VSIL 332
Cdd:PRK14869  291 VGVI 294
CBS_pair_voltage-gated_CLC_euk_bac cd04592
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with the ...
230-326 3.37e-07

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


Pssm-ID: 341368 [Multi-domain]  Cd Length: 128  Bit Score: 49.29  E-value: 3.37e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443048451 230 VVIVSPGDSVLTATQKMVEVHASSA-VVAVGNKAQGILTSRDI---LMRMIAKNLPADSTPVEKVMTLD------PECAT 299
Cdd:cd04592     5 YITVLMSTTLKEAVLLMLEEKQSCAlIVDSDDFLIGILTLGDIqrfLKRAKADNEDPKTILVSSICTRNggycrgLWTCT 84
                          90       100
                  ....*....|....*....|....*..
gi 1443048451 300 VDMPILDALRIMQERKFLHLPVMDRDG 326
Cdd:cd04592    85 PDMDLLTAKMLMEARGINQLPVVKRGG 111
COG3448 COG3448
CBS-domain-containing membrane protein [Signal transduction mechanisms];
287-343 3.83e-07

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


Pssm-ID: 442671 [Multi-domain]  Cd Length: 136  Bit Score: 49.48  E-value: 3.83e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1443048451 287 VEKVMTLDPECATVDMPILDALRIMQERKFLHLPVMDRDGSIVSILDVIDITHAAFS 343
Cdd:COG3448     4 VRDIMTRDVVTVSPDTTLREALELMREHGIRGLPVVDEDGRLVGIVTERDLLRALLP 60
IMPDH pfam00478
IMP dehydrogenase / GMP reductase domain; This family is involved in biosynthesis of guanosine ...
230-337 4.46e-07

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: 52.39  E-value: 4.46e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443048451 230 VVIVSPGDSVLTATQKMVEVHASSAVVAVGNKAQGILTSRDIlmrmiaKNLPADSTPVEKVMTLDPEC-ATVDMPILDAL 308
Cdd:pfam00478  90 PVTLSPDATVADALALMERYGISGVPVVDDGKLVGIVTNRDL------RFETDLSQPVSEVMTKENLVtAPEGTTLEEAK 163
                          90       100
                  ....*....|....*....|....*....
gi 1443048451 309 RIMQERKFLHLPVMDRDGSIVSILDVIDI 337
Cdd:pfam00478 164 EILHKHKIEKLPVVDDNGRLVGLITIKDI 192
CBS_archAMPK_gamma-repeat1 cd17779
signal transduction protein with CBS domains; Archeal gamma-subunit of 5'-AMP-activated ...
221-332 6.02e-07

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: 48.77  E-value: 6.02e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443048451 221 STITTAESTVVIVSPGDSVLTATQKMVEVHASS-AVVAVG-NKAQGILTSRDILMRM-------IAKN------LPADST 285
Cdd:cd17779     1 SIMAIATKDVITIPPTTTIIGAIKTMTEKGFRRlPVADAGtKRLEGIVTSMDIVDFLgggskynLVEKkhngnlLAAINE 80
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 1443048451 286 PVEKVMTLDPECATVDMPILDALRIMQERKFLHLPVMDRDGSIVSIL 332
Cdd:cd17779    81 PVREIMTRDVISVKENASIDDAIELMLEKNVGGLPIVDKDGKVIGIV 127
CBS_pair_bac cd04630
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains present in bacteria; ...
98-165 6.22e-07

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


Pssm-ID: 341393 [Multi-domain]  Cd Length: 120  Bit Score: 48.36  E-value: 6.22e-07
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1443048451  98 GILTDKDIATRVIARELKIEETPAWKVMTRhPVFVPSETLAVE-ALHKMVQGKFRHLPVVENGEVIAML 165
Cdd:cd04630    45 GIVTYTDILKKVIAEDRDPDLVNVYEIMTK-PAISVSPDLDIKyAARLMARFNLKRAPVIENNELIGIV 112
CBS_pair_AcuB_like cd04584
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with the ...
96-171 7.60e-07

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: 7.60e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443048451  96 LCGILTDKDI--ATRVIARELKIEE-------TPAWKVMTRHPVFVPSETLAVEALHKMVQGKFRHLPVVENGEVIAML- 165
Cdd:cd04584    42 LVGIVTDRDLlrASPSKATSLSIYElnyllskIPVKDIMTKDVITVSPDDTVEEAALLMLENKIGCLPVVDGGKLVGIIt 121

                  ....*...
gi 1443048451 166 --DIAKCL 171
Cdd:cd04584   122 etDILRAF 129
CBS_pair_arch cd17776
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains present in archaea; ...
230-340 9.23e-07

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: 47.79  E-value: 9.23e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443048451 230 VVIVSPGDSVLTATQKMVEVHASSAVVAVGNKAQGILTSRDILMRMIAKNLPADSTPVEKVMTLDPECATVDMPILDALR 309
Cdd:cd17776     5 VVTVDADASLEDAAERMLRNRVGSVVVTDDGTPAGILTETDALHAGYATDDPFSEIPVRAVASRPLVTISPTATLREAAE 84
                          90       100       110
                  ....*....|....*....|....*....|.
gi 1443048451 310 IMQERKFLHLPVMDRDgSIVSILDVIDITHA 340
Cdd:cd17776    85 RMVDEGVKKLPVVDGL-DLVGILTATDIIRA 114
CBS_pair_Mg_transporter cd04606
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains in the magnesium ...
255-337 1.04e-06

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: 47.71  E-value: 1.04e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443048451 255 VVAVGNKAQGILTSRDILMRmiaknlpADSTPVEKVMTLDPECATVDMPILDALRIMQERKFLHLPVMDRDGSIVSIL-- 332
Cdd:cd04606    42 VVDEDRRLLGVVSLRDLLLA-------DPDTKVSDIMDTDVISVSADDDQEEVARLFAKYDLLALPVVDEEGRLVGIItv 114

                  ....*.
gi 1443048451 333 -DVIDI 337
Cdd:cd04606   115 dDVLDV 120
CBS_pair_arch2_repeat2 cd04614
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains present in archaea, ...
91-165 1.12e-06

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: 48.43  E-value: 1.12e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443048451  91 DSNALLCGILTDKDI--ATRVI-------------------------------ARELKIEETPAWKVMTRHPVFVPSETL 137
Cdd:cd04614    34 DSEGKLVGIVTERDLidVSRIVeseeesgmsiaddedewswegirdvmslyypTSNVELPDKPVKDVMTKDVVTAFPSST 113
                          90       100
                  ....*....|....*....|....*....
gi 1443048451 138 AVEALHKMVQGKFRHLPVVE-NGEVIAML 165
Cdd:cd04614   114 VSEAAKKMIRNDIEQLPVVSgEGDLAGML 142
CBS_pair_bac cd04630
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains present in bacteria; ...
230-340 1.53e-06

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: 47.21  E-value: 1.53e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443048451 230 VVIVSPGDSVLTATQKMVEVHASSAVVavgNK-----AQGILTSRDILMRMIAKNLPADSTPVEKVMTlDPeCATV--DM 302
Cdd:cd04630     9 VVTIDGLATVREALQLMKEHNVKSLIV---EKrhehdAYGIVTYTDILKKVIAEDRDPDLVNVYEIMT-KP-AISVspDL 83
                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 1443048451 303 PILDALRIMQERKFLHLPVMDrDGSIVSILDVIDITHA 340
Cdd:cd04630    84 DIKYAARLMARFNLKRAPVIE-NNELIGIVSMTDLVLD 120
CBS_pair_arch_MET2_assoc cd04605
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with the ...
228-339 1.53e-06

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: 47.23  E-value: 1.53e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443048451 228 STVVIVSPGDSVLTATQKMVEVHASS-AVVAVGNKAQGILTSRDIlmrmiAKNLPADSTPVEKVMTLDPECATVDMPILD 306
Cdd:cd04605     8 KDVATIREDISIEEAAKIMIDKNVTHlPVVSEDGKLIGIVTSWDI-----SKAVALKKDSLEEIMTRNVITARPDEPIEL 82
                          90       100       110
                  ....*....|....*....|....*....|...
gi 1443048451 307 ALRIMQERKFLHLPVMDRDGSIVSILDVIDITH 339
Cdd:cd04605    83 AARKMEKHNISALPVVDDDRRVIGIITSDDISR 115
COG2524 COG2524
Predicted transcriptional regulator, contains C-terminal CBS domains [Transcription];
215-343 1.84e-06

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


Pssm-ID: 442013 [Multi-domain]  Cd Length: 206  Bit Score: 48.73  E-value: 1.84e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443048451 215 MLRPSLSTITTAESTVVIVSPGDSVLTATQKMVEVHASSAVVAVGNKAQGILTSRDILMRMIAKNLPADSTPVEKVMTLD 294
Cdd:COG2524    16 LAVVLAALLLLAALVLALTAAAAATVLLLAAAAAAAGAGGLGLLLLLLLIVLQAAAVRVVAEKELGLVLKMKVKDIMTKD 95
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 1443048451 295 PECATVDMPILDALRIMQERKFLHLPVMDrDGSIVSILDVIDITHAAFS 343
Cdd:COG2524    96 VITVSPDTTLEEALELMLEKGISGLPVVD-DGKLVGIITERDLLKALAE 143
CBS_pair_bac cd04629
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains present in bacteria; ...
231-332 2.35e-06

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: 46.66  E-value: 2.35e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443048451 231 VIVSPGDSVLTATQKMVEVHASSA-VVAVGNKAQGILTSRDILMRMIaknlpaDST-------PVEKVMTLDPECATVDM 302
Cdd:cd04629     6 VTLTPDTSILEAVELLLEHKISGApVVDEQGRLVGFLSEQDCLKALL------EASyhcepggTVADYMSTEVLTVSPDT 79
                          90       100       110
                  ....*....|....*....|....*....|
gi 1443048451 303 PILDALRIMQERKFLHLPVMDrDGSIVSIL 332
Cdd:cd04629    80 SIVDLAQLFLKNKPRRYPVVE-DGKLVGQI 108
CBS_pair_GGDEF_PAS_repeat1 cd09833
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains found in diguanylate ...
234-335 2.44e-06

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


Pssm-ID: 341403 [Multi-domain]  Cd Length: 116  Bit Score: 46.45  E-value: 2.44e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443048451 234 SPGDSVLTATQKMVEVHASSAVVAVGNKAQGILTSRDILmrMIAKNLP-ADSTPVEKVMTLDPECATVDMPILDALRIMQ 312
Cdd:cd09833    11 SPDTPLADAAARMAERRCSSILIVENGEIVGIWTERDAL--KLDFSDPdAFRRPISEVMSSPVLTIPQDTTLGEAAVRFR 88
                          90       100
                  ....*....|....*....|....*.
gi 1443048451 313 ERKFLHLPVMDRDG---SIVSILDVI 335
Cdd:cd09833    89 QEGVRHLLVVDDDGrpvGIVSQTDVV 114
CBS pfam00571
CBS domain; CBS domains are small intracellular modules that pair together to form a stable ...
124-173 2.70e-06

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: 44.51  E-value: 2.70e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1443048451 124 VMTRHPVFVPSETLAVEALHKMVQGKFRHLPVV-ENGEVIAML---DIAKCLYD 173
Cdd:pfam00571   4 IMTKDVVTVSPDTTLEEALELMREHGISRLPVVdEDGKLVGIVtlkDLLRALLG 57
CBS COG0517
CBS domain [Signal transduction mechanisms];
287-355 3.08e-06

CBS domain [Signal transduction mechanisms];


Pssm-ID: 440283 [Multi-domain]  Cd Length: 128  Bit Score: 46.40  E-value: 3.08e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1443048451 287 VEKVMTLDPECATVDMPILDALRIMQERKFLHLPVMDRDGSIVSILDVIDITHAAFSIVEGNGDGAVND 355
Cdd:COG0517     3 VKDIMTTDVVTVSPDATVREALELMSEKRIGGLPVVDEDGKLVGIVTDRDLRRALAAEGKDLLDTPVSE 71
CBS_pair_peptidase_M50 cd04801
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains found in the ...
228-340 3.53e-06

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: 46.02  E-value: 3.53e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443048451 228 STVVIVSPGDSVLTATQKMVEV-HASSAVVAvGNKAQGILTSRDIlmRMIAKNLpADSTPVEKVMTLDPECATVDMPILD 306
Cdd:cd04801     5 PEVVTVTPEMTVSELLDRMFEEkHLGYPVVE-NGRLVGIVTLEDI--RKVPEVE-REATRVRDVMTKDVITVSPDADAME 80
                          90       100       110
                  ....*....|....*....|....*....|....
gi 1443048451 307 ALRIMQERKFLHLPVMDrDGSIVSILDVIDITHA 340
Cdd:cd04801    81 ALKLMSQNNIGRLPVVE-DGELVGIISRTDLMRA 113
CBS_pair_AcuB_like cd04584
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with the ...
287-346 4.75e-06

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: 45.88  E-value: 4.75e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443048451 287 VEKVMTLDPECATVDMPILDALRIMQERKFLHLPVMDrDGSIVSILDVIDITHAAFSIVE 346
Cdd:cd04584     2 VKDIMTKNVVTVTPDTSLAEARELMKEHKIRHLPVVD-DGKLVGIVTDRDLLRASPSKAT 60
CBS_pair_GGDEF_assoc cd04599
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with the ...
230-340 1.08e-05

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: 44.64  E-value: 1.08e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443048451 230 VVIVSPGDSVLTATQKMVEVHASSAVVAVGNKAQGILTSRDIlmRMIAKN-LPADSTpVEKVMTLDPECAtvdmpILDAL 308
Cdd:cd04599     5 PITISPLDSVARAAALMERQRIGGLPVVENGKLVGIITSRDV--RRAHPNrLVADAM-SRNVVTISPEAS-----LWEAK 76
                          90       100       110
                  ....*....|....*....|....*....|..
gi 1443048451 309 RIMQERKFLHLPVMDrDGSIVSILDVIDITHA 340
Cdd:cd04599    77 ELMEEHGIERLVVVE-EGRLVGIITKSTLYLE 107
MgtE COG2239
Mg/Co/Ni transporter MgtE (contains CBS domain) [Inorganic ion transport and metabolism];
263-337 1.82e-05

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


Pssm-ID: 441840 [Multi-domain]  Cd Length: 443  Bit Score: 47.37  E-value: 1.82e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1443048451 263 QGILTSRDILmrmiaknLPADSTPVEKVMTLDPECATVDMPILDALRIMQERKFLHLPVMDRDGSIVSIL---DVIDI 337
Cdd:COG2239   178 VGVVSLRDLL-------LADPDTKVSDIMDTDVISVPADDDQEEVARLFERYDLLALPVVDEEGRLVGIItvdDVVDV 248
CBS_arch_repeat2 cd17778
CBS pair domains found in archeal proteins, repeat 2; CBS pair domains found in archeal ...
286-339 2.93e-05

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: 43.86  E-value: 2.93e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1443048451 286 PVEKVMTLDPECATVDMPILDALRIMQERKFLHLPVMDrDGSIVSILDVIDITH 339
Cdd:cd17778     1 KVKEFMTTPVVTIYPDDTLKEAMELMVTRGFRRLPVVS-GGKLVGIVTAMDIVK 53
CBS_pair_Thermoplasmatales cd17786
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains present in ...
233-338 3.08e-05

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


Pssm-ID: 341422 [Multi-domain]  Cd Length: 114  Bit Score: 43.29  E-value: 3.08e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443048451 233 VSPGDSVLTATQKMVEVHASSAVVAVGN-KAQGILTSRDILMRMIAKNLPADSTPVEKVMTLDPECATVDMPILDALRIM 311
Cdd:cd17786     7 INWNATVFDAVKIMNENHLYGLVVKDDDgNYVGLISERSIIKRFIPRNVKPDEVPVKLVMRKPIPKVKSDYDVKDVAAFL 86
                          90       100
                  ....*....|....*....|....*..
gi 1443048451 312 QERKFLHLPVMDRDGSIVSILDVIDIT 338
Cdd:cd17786    87 SENGLERCAVVDDNGRVVGIVTITDLS 113
CBS_pair_SF cd02205
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains superfamily; The CBS ...
292-343 3.25e-05

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: 3.25e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1443048451 292 TLDPECATVDMPILDALRIMQERKFLHLPVMDRDGSIVSILDVIDITHAAFS 343
Cdd:cd02205     1 TRDVVTVDPDTTVREALELMAENGIGALPVVDDDGKLVGIVTERDILRALVE 52
PTZ00314 PTZ00314
inosine-5'-monophosphate dehydrogenase; Provisional
258-331 3.74e-05

inosine-5'-monophosphate dehydrogenase; Provisional


Pssm-ID: 240355 [Multi-domain]  Cd Length: 495  Bit Score: 46.50  E-value: 3.74e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1443048451 258 VGNKAQGILTSRDIlmrmiaKNLPADSTPVEKVMTLDPECATVDMPIL--DALRIMQERKFLHLPVMDRDGSIVSI 331
Cdd:PTZ00314  138 VGGKLLGIVTSRDI------DFVKDKSTPVSEVMTPREKLVVGNTPISleEANEVLRESRKGKLPIVNDNGELVAL 207
CBS_pair_peptidase_M50 cd04639
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains found in the ...
284-337 4.10e-05

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: 43.33  E-value: 4.10e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1443048451 284 STPVEKVMTLDPECATV--DMPILDALRIMQERKFLHLPVMDRDGSIVSILDVIDI 337
Cdd:cd04639    61 DTPVRELMKPLEEIPTVaaDQSLLEVVKLLEEQQLPALAVVSENGTLVGLIEKEDI 116
CBS_archAMPK_gamma-repeat2 cd04631
CBS pair domains found in archeal 5'-AMP-activated protein kinase gamma subunit-like proteins; ...
125-273 6.00e-05

CBS pair domains found in archeal 5'-AMP-activated protein kinase gamma subunit-like proteins; Archeal gamma-subunit of 5'-AMP-activated protein kinase (AMPK) contains four CBS domains in tandem repeats, similar to eukaryotic homologs. AMPK is an important regulator of metabolism and of energy homeostasis. It is a heterotrimeric protein composed of a catalytic serine/threonine kinase subunit (alpha) and two regulatory subunits (beta and gamma). The gamma subunit senses the intracellular energy status by competitively binding AMP and ATP and is believed to be responsible for allosteric regulation of the whole complex. In humans mutations in gamma- subunit of AMPK are associated with hypertrophic cardiomiopathy, Wolff-Parkinson-White syndrome and glycogen storage in the skeletal muscle. The CBS domain, named after human CBS, is a small domain originally identified in cystathionine beta-synthase and is subsequently found in a wide range of different proteins. CBS domains usually occur in tandem repeats. They associate to form a so-called Bateman domain or a CBS pair based on crystallographic studies in bacteria. The CBS pair was used as a basis for this cd hierarchy since the human CBS proteins can adopt the typical core structure and form an intramolecular CBS pair. The interface between the two CBS domains forms a cleft that is a potential ligand binding site. The CBS pair coexists with a variety of other functional domains and this has been used to help in its classification here.


Pssm-ID: 341394 [Multi-domain]  Cd Length: 130  Bit Score: 42.98  E-value: 6.00e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443048451 125 MTRHPVFVPSETLAVEALHKMVQGKFRHLPVVENGEVIAML---DIAKCLydaiarierasdkgkaaaiasavdaaaGND 201
Cdd:cd04631     6 MTKNVITATPGTPIEDVAKIMVRNGFRRLPVVSDGKLVGIVtstDIMRYL---------------------------GSG 58
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1443048451 202 PTASSMV-----EAFKEQMlrpslSTITTAEstVVIVSPGDSVLTATQKMVEVHASSAVVAVGNKAQGILTSRDILM 273
Cdd:cd04631    59 EAFEKLKtgnihEVLNVPI-----SSIMKRD--IITTTPDTDLGEAAELMLEKNIGALPVVDDGKLVGIITERDILR 128
CBS_pair_peptidase_M50 cd04801
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains found in the ...
96-165 6.36e-05

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: 42.56  E-value: 6.36e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443048451  96 LCGILTDKDIATrviARELKIEETPAWKVMTRHPVFVPSETLAVEALHKMVQGKFRHLPVVENGEVIAML 165
Cdd:cd04801    39 LVGIVTLEDIRK---VPEVEREATRVRDVMTKDVITVSPDADAMEALKLMSQNNIGRLPVVEDGELVGII 105
CBS_pair_DHH_polyA_Pol_assoc cd04595
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with the ...
228-335 7.12e-05

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: 42.10  E-value: 7.12e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443048451 228 STVVIVSPGDSVLTATQKMVEVHASSAVVAVGNKAQGILTSRDIlmrMIAKNLPADSTPVEKVMTLDPECATVDMPILDA 307
Cdd:cd04595     2 SPVKTVSPDTTIEEARKIMLRYGHTGLPVVEDGKLVGIISRRDV---DKAKHHGLGHAPVKGYMSTNVITIDPDTSLEEA 78
                          90       100       110
                  ....*....|....*....|....*....|.
gi 1443048451 308 LRIMQERKFLHLPVMDrDGSIVSIL---DVI 335
Cdd:cd04595    79 QELMVEHDIGRLPVVE-EGKLVGIVtrsDVL 108
CBS_pair_NTP_transferase_assoc cd04607
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domain associated with the ...
88-162 9.81e-05

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: 41.66  E-value: 9.81e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1443048451  88 LLTDSNALLCGILTDKDIaTRVIARELKIEeTPAWKVMTRHPVFVPSETLAVEALHKMVQGKFRHLPVV-ENGEVI 162
Cdd:cd04607    29 LVVDENRKLLGTVTDGDI-RRGLLKGLSLD-APVEEVMNKNPITASPSTSREELLALMRAKKILQLPIVdEQGRVV 102
CBS_pair_CcpN cd04617
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains of CcpN repressor; ...
60-160 1.22e-04

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


Pssm-ID: 341387 [Multi-domain]  Cd Length: 125  Bit Score: 41.70  E-value: 1.22e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443048451  60 LSKALTVPESTTVLEACRRMAARRADAALLTDSNALLCGILTDKDIATRVIARElKIEETPAWKVMTRHP--VFVPSETL 137
Cdd:cd04617     3 MSVPVVVDETTSVYDAIVTLFLEDVGSLFVVDEEGYLVGVVSRKDLLKATLGGQ-DLEKTPVSMIMTRMPniVTVTPDDS 81
                          90       100
                  ....*....|....*....|...
gi 1443048451 138 AVEALHKMVQGKFRHLPVVENGE 160
Cdd:cd04617    82 VLEAARKLIEHEIDSLPVVEKED 104
CBS_pair_DHH_polyA_Pol_assoc cd04595
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with the ...
96-162 1.34e-04

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: 41.33  E-value: 1.34e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1443048451  96 LCGILTDKDIatrVIARELKIEETPAWKVMTRHPVFVPSETLAVEALHKMVQGKFRHLPVVENGEVI 162
Cdd:cd04595    36 LVGIISRRDV---DKAKHHGLGHAPVKGYMSTNVITIDPDTSLEEAQELMVEHDIGRLPVVEEGKLV 99
CBS_pair_arch_MET2_assoc cd04605
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with the ...
287-340 1.67e-04

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: 41.46  E-value: 1.67e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1443048451 287 VEKVMTLDPECATVDMPILDALRIMQERKFLHLPVMDRDGSIVSILDVIDITHA 340
Cdd:cd04605     2 VEDIMSKDVATIREDISIEEAAKIMIDKNVTHLPVVSEDGKLIGIVTSWDISKA 55
COG2905 COG2905
Signal-transduction protein containing cAMP-binding, CBS, and nucleotidyltransferase domains ...
287-332 2.13e-04

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


Pssm-ID: 442149 [Multi-domain]  Cd Length: 124  Bit Score: 41.35  E-value: 2.13e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*.
gi 1443048451 287 VEKVMTLDPECATVDMPILDALRIMQERKFLHLPVMDRDGSIVSIL 332
Cdd:COG2905     1 VKDIMSRDVVTVSPDATVREAARLMTEKGVGSLVVVDDDGRLVGII 46
CBS_pair_bac cd04629
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains present in bacteria; ...
124-165 2.21e-04

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: 40.88  E-value: 2.21e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 1443048451 124 VMTRHPVFVPSETLAVEALHKMVQGKFRHLPVVENGEVIAML 165
Cdd:cd04629    67 YMSTEVLTVSPDTSIVDLAQLFLKNKPRRYPVVEDGKLVGQI 108
CBS_pair_CBS cd04608
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with the ...
227-337 2.45e-04

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: 40.98  E-value: 2.45e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443048451 227 ESTVVIVSPGDSVLTATQKMVEVHASSA-VVAVGNKAQGILTSRDIlMRMIAKNLPADSTPVEKVMTLDPECATVDMPIL 305
Cdd:cd04608     9 LGAPVTVLPDDTLGEAIEIMREYGVDQLpVVDEDGRVVGMVTEGNL-LSSLLAGRAQPSDPVSKAMYKQFKQVDLDTPLG 87
                          90       100       110
                  ....*....|....*....|....*....|..
gi 1443048451 306 DALRIMQERKFlhLPVMDRDGSIVSILDVIDI 337
Cdd:cd04608    88 ALSRILERDHF--ALVVDGQGKVLGIVTRIDL 117
CBS_pair_DRTGG_assoc cd04596
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with the ...
90-159 2.48e-04

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: 40.53  E-value: 2.48e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443048451  90 TDSNALLCGILTDKDIATRviARELKIEetpawKVMTRHPVFVPSETLAVEALHKMVQGKFRHLPVVENG 159
Cdd:cd04596    31 VDEENRVVGIVTAKDVIGK--EDDTPIE-----KVMTKNPITVKPKTSVASAAHMMIWEGIELLPVVDEN 93
CBS_pair_arch cd17776
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains present in archaea; ...
97-165 2.65e-04

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: 40.85  E-value: 2.65e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1443048451  97 CGILTDKDIATRVIARELKIEETPAWKVMTRHPVFVPSETLAVEALHKMVQGKFRHLPVVENGEVIAML 165
Cdd:cd17776    38 AGILTETDALHAGYATDDPFSEIPVRAVASRPLVTISPTATLREAAERMVDEGVKKLPVVDGLDLVGIL 106
CBS_pair_ABC_OpuCA_assoc cd04583
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains found associated with ...
231-332 3.61e-04

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: 40.19  E-value: 3.61e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443048451 231 VIVSPGDSVLTATQKMVEVHASSA-VVAVGNKAQGILTSRDIlmrmiaKNLPADSTPVEKVMTLDPECATVDMPILDALR 309
Cdd:cd04583     5 VTITPERTLAQAIEIMREKRVDSLlVVDKDNVLLGIVDIEDI------NRNYRKAKKVGEIMERDVFTVKEDSLLRDTVD 78
                          90       100
                  ....*....|....*....|...
gi 1443048451 310 IMQERKFLHLPVMDRDGSIVSIL 332
Cdd:cd04583    79 RILKRGLKYVPVVDEQGRLVGLV 101
CBS_pair_BON_assoc cd04586
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with the ...
91-162 4.07e-04

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: 40.49  E-value: 4.07e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443048451  91 DSNALLCGILTDKDI---------------------ATRVIAREL-KIEETPAWKVMTRHPVFVPSETLAVEALHKMVQG 148
Cdd:cd04586    33 DDDGKLVGIVSEGDLlrreepgteprrvwwldalleSPERLAEEYvKAHGRTVGDVMTRPVVTVSPDTPLEEAARLMERH 112
                          90
                  ....*....|....
gi 1443048451 149 KFRHLPVVENGEVI 162
Cdd:cd04586   113 RIKRLPVVDDGKLV 126
CBS_pair_voltage-gated_CLC_bac cd04613
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with the ...
62-165 4.36e-04

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: 40.25  E-value: 4.36e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443048451  62 KALTVPESTTVLEACRRMAARRADAALLTDSNALLCGILTDKDIatRVIARELKIEE-TPAWKVMTRHPVFV-PSETLAv 139
Cdd:cd04613     4 KVTVLPEGMTFRQFTEFIAGTRQHYFPVVDEQGRLTGILSIQDV--RGVLFEEELWDlVVVKDLATTDVITVtPDDDLY- 80
                          90       100
                  ....*....|....*....|....*....
gi 1443048451 140 EALHKMVQGKFRHLPVVE---NGEVIAML 165
Cdd:cd04613    81 TALLKFTSTNLDQLPVVDdddPGKVLGML 109
CBS_pair_ABC_OpuCA_assoc cd04583
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains found associated with ...
88-158 5.12e-04

Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains found associated with the ABC transporter OpuCA; This cd contains two tandem repeats of the cystathionine beta-synthase (CBS pair) domains found in association with the ABC transporter OpuCA. OpuCA is the ATP binding component of a bacterial solute transporter that serves a protective role to cells growing in a hyperosmolar environment but the function of the CBS domains in OpuCA remains unknown. In the related ABC transporter, OpuA, the tandem CBS domains have been shown to function as sensors for ionic strength, whereby they control the transport activity through an electronic switching mechanism. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. They are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins. The CBS domain, named after human CBS, is a small domain originally identified in cystathionine beta-synthase and is subsequently found in a wide range of different proteins. CBS domains usually occur in tandem repeats. They associate to form a so-called Bateman domain or a CBS pair based on crystallographic studies in bacteria. The CBS pair was used as a basis for this cd hierarchy since the human CBS proteins can adopt the typical core structure and form an intramolecular CBS pair. The interface between the two CBS domains forms a cleft that is a potential ligand binding site. The CBS pair coexists with a variety of other functional domains and this has been used to help in its classification here. It has been proposed that the CBS domain may play a regulatory role, although its exact function is unknown. Mutations of conserved residues within this domain are associated with a variety of human hereditary diseases, including congenital myotonia, idiopathic generalized epilepsy, hypercalciuric nephrolithiasis, and classic Bartter syndrome (CLC chloride channel family members), Wolff-Parkinson-White syndrome (gamma 2 subunit of AMP-activated protein kinase), retinitis pigmentosa (IMP dehydrogenase-1), and homocystinuria (cystathionine beta-synthase).


Pssm-ID: 341360 [Multi-domain]  Cd Length: 110  Bit Score: 39.81  E-value: 5.12e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1443048451  88 LLTDSNALLCGILTDKDIaTRVIARELKIEEtpawkVMTRHPVFVPSETLAVEALHKMVQGKFRHLPVVEN 158
Cdd:cd04583    29 LVVDKDNVLLGIVDIEDI-NRNYRKAKKVGE-----IMERDVFTVKEDSLLRDTVDRILKRGLKYVPVVDE 93
CBS_arch_repeat1 cd17777
CBS pair domains found in archeal proteins, repeat 1; CBS pair domains found in archeal ...
63-156 5.89e-04

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: 40.40  E-value: 5.89e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443048451  63 ALTVPESTTVLEACRRMAARRADAALLTDSNALLcGILTDKDIATRVIARELKI--------------EETPAWKVMTRH 128
Cdd:cd17777    12 VLSISPSAPILSAFEKMNRRGIRRLVVVDENKLE-GILSARDLVSYLGGGCLFKivesrhqgdlysalNREVVETIMTPN 90
                          90       100
                  ....*....|....*....|....*...
gi 1443048451 129 PVFVPSETLAVEALHKMVQGKFRHLPVV 156
Cdd:cd17777    91 PVYVYEDSDLIEALTIMVTRGIGSLPVV 118
CBS_pair_GGDEF_PAS_repeat2 cd04611
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains found in diguanylate ...
219-337 7.10e-04

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


Pssm-ID: 341384 [Multi-domain]  Cd Length: 131  Bit Score: 40.01  E-value: 7.10e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443048451 219 SLSTITTAESTVVIVSPGDSVLT-ATQKMVEVHASSAVVAVGNKAQGILTSRDiLMRMIAKNLPadSTPVEKVMTLDPEC 297
Cdd:cd04611     3 RLREVGSAMNRSPLVLPGDASLAeAARRMRSHRADAAVIECPDGGLGILTERD-LVRFIARHPG--NTPVGELASRPLLT 79
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 1443048451 298 ATVDMPILDALRIMQERKFLHLPVMDRDGSIVSILDVIDI 337
Cdd:cd04611    80 VGAEDSLIHARDLLIDHRIRHLAVVDEDGQVTGLLGFADL 119
CBS_archAMPK_gamma-repeat2 cd04631
CBS pair domains found in archeal 5'-AMP-activated protein kinase gamma subunit-like proteins; ...
287-354 7.75e-04

CBS pair domains found in archeal 5'-AMP-activated protein kinase gamma subunit-like proteins; Archeal gamma-subunit of 5'-AMP-activated protein kinase (AMPK) contains four CBS domains in tandem repeats, similar to eukaryotic homologs. AMPK is an important regulator of metabolism and of energy homeostasis. It is a heterotrimeric protein composed of a catalytic serine/threonine kinase subunit (alpha) and two regulatory subunits (beta and gamma). The gamma subunit senses the intracellular energy status by competitively binding AMP and ATP and is believed to be responsible for allosteric regulation of the whole complex. In humans mutations in gamma- subunit of AMPK are associated with hypertrophic cardiomiopathy, Wolff-Parkinson-White syndrome and glycogen storage in the skeletal muscle. The CBS domain, named after human CBS, is a small domain originally identified in cystathionine beta-synthase and is subsequently found in a wide range of different proteins. CBS domains usually occur in tandem repeats. They associate to form a so-called Bateman domain or a CBS pair based on crystallographic studies in bacteria. The CBS pair was used as a basis for this cd hierarchy since the human CBS proteins can adopt the typical core structure and form an intramolecular CBS pair. The interface between the two CBS domains forms a cleft that is a potential ligand binding site. The CBS pair coexists with a variety of other functional domains and this has been used to help in its classification here.


Pssm-ID: 341394 [Multi-domain]  Cd Length: 130  Bit Score: 39.90  E-value: 7.75e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1443048451 287 VEKVMTLDPECATVDMPILDALRIMQERKFLHLPVMdRDGSIVSILDVIDITH-----AAFS-IVEGNGDGAVN 354
Cdd:cd04631     2 VEDYMTKNVITATPGTPIEDVAKIMVRNGFRRLPVV-SDGKLVGIVTSTDIMRylgsgEAFEkLKTGNIHEVLN 74
CBS_pair_Euryarchaeota cd17784
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains present in ...
230-340 7.90e-04

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: 39.33  E-value: 7.90e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443048451 230 VVIVSPGDSVLTATQKMVEVHASS-AVVAVGNKAQGILTSRDILMRMIAKNLPADSTpVEKVMTLDPECATVDMPILDAL 308
Cdd:cd17784     4 VITAKPNEGVVEAFEKMLKHKISAlPVVDDEGKLIGIVTATDLGHNLILDKYELGTT-VEEVMVKDVATVHPDETLLEAI 82
                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 1443048451 309 RIMQ-----ERKFLHLPVMDrDGSIVSILDVIDITHA 340
Cdd:cd17784    83 KKMDsnapdEEIINQLPVVD-DGKLVGIISDGDIIRA 118
CBS smart00116
Domain in cystathionine beta-synthase and other proteins; Domain present in all 3 forms of ...
294-337 8.24e-04

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: 37.49  E-value: 8.24e-04
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....
gi 1443048451  294 DPECATVDMPILDALRIMQERKFLHLPVMDRDGSIVSILDVIDI 337
Cdd:smart00116   1 DVVTVSPDTTLEEALELLRENGIRRLPVVDEEGRLVGIVTRRDI 44
CBS_arch_repeat2 cd17778
CBS pair domains found in archeal proteins, repeat 2; CBS pair domains found in archeal ...
228-340 1.19e-03

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


Pssm-ID: 341414 [Multi-domain]  Cd Length: 131  Bit Score: 39.24  E-value: 1.19e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443048451 228 STVVIVSPGDSVLTATQKMVEVHASSAVVAVGNKAQGILTSRDIL---MRMIAKNLP-------ADSTPVEKVMTLDPEC 297
Cdd:cd17778     8 TPVVTIYPDDTLKEAMELMVTRGFRRLPVVSGGKLVGIVTAMDIVkyfGSHEAKKRLttgdideAYSTPVEEIMSKEVVT 87
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 1443048451 298 ATVDMPILDALRIMQERKFLHLPVMDRDGSIVSILDVIDITHA 340
Cdd:cd17778    88 IEPDADIAEAARLMIKKNVGSLLVVDDEGELKGIITERDVLIA 130
CBS smart00116
Domain in cystathionine beta-synthase and other proteins; Domain present in all 3 forms of ...
133-172 1.32e-03

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: 36.72  E-value: 1.32e-03
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....
gi 1443048451  133 PSETLAvEALHKMVQGKFRHLPVV-ENGEVIAML---DIAKCLY 172
Cdd:smart00116   7 PDTTLE-EALELLRENGIRRLPVVdEEGRLVGIVtrrDIIKALA 49
PRK14869 PRK14869
putative manganese-dependent inorganic diphosphatase;
287-338 1.45e-03

putative manganese-dependent inorganic diphosphatase;


Pssm-ID: 237843 [Multi-domain]  Cd Length: 546  Bit Score: 41.36  E-value: 1.45e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1443048451 287 VEKVMTLDPECATVDMPILDALRIMQERKFLHLPVMDRDGSIVSILDVIDIT 338
Cdd:PRK14869   70 VRDLEIDKPVTVSPDTSLKEAWNLMDENNVKTLPVVDEEGKLLGLVSLSDLA 121
CBS_pair_bac cd04629
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains present in bacteria; ...
125-272 1.55e-03

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: 38.57  E-value: 1.55e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443048451 125 MTRHPVFVPSETLAVEALHKMVQGKFRHLPVV-ENGEVIAMLDIAKCLydaiarierasdkgkaaaiasavdaaagndpt 203
Cdd:cd04629     1 MTRNPVTLTPDTSILEAVELLLEHKISGAPVVdEQGRLVGFLSEQDCL-------------------------------- 48
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1443048451 204 aSSMVEAFKEQMLRPSLSTITTAEstVVIVSPGDSVLTATQKMVEVHASSAVVAVGNKAQGILTSRDIL 272
Cdd:cd04629    49 -KALLEASYHCEPGGTVADYMSTE--VLTVSPDTSIVDLAQLFLKNKPRRYPVVEDGKLVGQISRRDVL 114
CBS_two-component_sensor_histidine_kinase_repeat1 cd04620
2 tandem repeats of the CBS domain in the two-component sensor histidine kinase and ...
64-165 1.82e-03

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: 38.67  E-value: 1.82e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443048451  64 LTVPESTTVLE--------ACRRMAARRADAALLTDS-------NALLCGILTDKDIaTRVIARELKIEETPAWKVMTRH 128
Cdd:cd04620    10 LTVSPDTPVIEaialmsqtRSSCCLLSEDSIITEARSscvlvveNQQLVGIFTERDV-VRLTASGIDLSGVTIAEVMTQP 88
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 1443048451 129 PVFVPSETL--AVEALHKMVQGKFRHLPVV-ENGEVIAML 165
Cdd:cd04620    89 VITLKESEFqdIFTVLSLLRQHQIRHLPIVdDQGQLVGLI 128
CBS_pair_voltage-gated_CLC_bac cd04613
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with the ...
255-340 1.93e-03

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: 38.33  E-value: 1.93e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443048451 255 VVAVGNKAQGILTSRDILMRMIAKNLpADSTPVEKVMTLDPECATVDMPILDALRIMQERKFLHLPVMDRD--GSIVSIL 332
Cdd:cd04613    31 VVDEQGRLTGILSIQDVRGVLFEEEL-WDLVVVKDLATTDVITVTPDDDLYTALLKFTSTNLDQLPVVDDDdpGKVLGML 109

                  ....*...
gi 1443048451 333 DVIDITHA 340
Cdd:cd04613   110 SRRDVIAA 117
CBS_pair_NeuB cd17773
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domain present in ...
232-331 2.34e-03

Two tandem repeats of the cystathionine beta-synthase (CBS pair) domain present in N-acylneuraminate-9-phosphate synthase; This CD contains two tandem repeats of the cystathionine beta-synthase (CBS pair) domain present in N-acylneuraminate-9-phosphate synthase NeuB. NeuB catalyzes the condensation of phosphoenolpyruvate (PEP) and N-acetylmannosamine, directly forming N-acetylneuraminic acid (or sialic acid). The CBS domain, named after human CBS, is a small domain originally identified in cystathionine beta-synthase and is subsequently found in a wide range of different proteins. CBS domains usually occur in tandem repeats. They associate to form a so-called Bateman domain or a CBS pair based on crystallographic studies in bacteria. The CBS pair was used as a basis for this cd hierarchy since the human CBS proteins can adopt the typical core structure and form an intramolecular CBS pair. The interface between the two CBS domains forms a cleft that is a potential ligand binding site. The CBS pair coexists with a variety of other functional domains and this has been used to help in its classification here. It has been proposed that the CBS domain may play a regulatory role, although its exact function is unknown. Mutations of conserved residues within this domain are associated with a variety of human hereditary diseases, including congenital myotonia, idiopathic generalized epilepsy, hypercalciuric nephrolithiasis, and classic Bartter syndrome (CLC chloride channel family members), Wolff-Parkinson-White syndrome (gamma 2 subunit of AMP-activated protein kinase), retinitis pigmentosa (IMP dehydrogenase-1), and homocystinuria (cystathionine beta-synthase).


Pssm-ID: 341409 [Multi-domain]  Cd Length: 118  Bit Score: 38.00  E-value: 2.34e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443048451 232 IVSPGDSVLTATQKMVEVHASSA-VVAVGNKAQGILTSRDIlMRMIAKNLPAD-STPVEKVMTLDPECATVDMPiLDALR 309
Cdd:cd17773    10 VVFAEDSILNALQKISDNKSRIVfCVDEHGVLEGVLTDGDF-RRWLLENPNADlSQPVSHVANTNFVSAPEGES-PEKIE 87
                          90       100
                  ....*....|....*....|..
gi 1443048451 310 IMQERKFLHLPVMDRDGSIVSI 331
Cdd:cd17773    88 ALFSSRISYIPLVDERGRLVAV 109
CBS_pair_DRTGG_assoc cd04596
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with the ...
260-335 2.52e-03

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: 37.83  E-value: 2.52e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1443048451 260 NKAQGILTSRDILMRmiaknlpADSTPVEKVMTLDPECATVDMPILDALRIMQERKFLHLPVMDRDGSIVSIL---DVI 335
Cdd:cd04596    35 NRVVGIVTAKDVIGK-------EDDTPIEKVMTKNPITVKPKTSVASAAHMMIWEGIELLPVVDENRKLLGVIsrqDVL 106
CBS_pair_DHH_polyA_Pol_assoc cd17772
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with the ...
96-162 2.89e-03

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: 37.55  E-value: 2.89e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1443048451  96 LCGILTdKDIATRVIARELkiEETPAWKVMTRHPVFVPSETLAVEALHKMVQGKFRHLPVVENGEVI 162
Cdd:cd17772    38 LVGIIT-RQVAEKAIYHGL--GDLPVSEYMTTEFATVTPDAPLSEIQEIIVEQRQRLVPVVEDGRLV 101
YtoI COG4109
Predicted transcriptional regulator containing CBS domains [Transcription];
283-337 3.96e-03

Predicted transcriptional regulator containing CBS domains [Transcription];


Pssm-ID: 443285 [Multi-domain]  Cd Length: 135  Bit Score: 37.58  E-value: 3.96e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1443048451 283 DSTPVEKVMTL-DPECATVDMPILDALRIMQERKFLHLPVMDRDGSIVSILDVIDI 337
Cdd:COG4109    14 EILLVEDIMTLeDVATLSEDDTVEDALELLEKTGHSRFPVVDENGRLVGIVTSKDI 69
CBS_euAMPK_gamma-like_repeat2 cd04641
CBS pair domain found in 5'-AMP (adenosine monophosphate)-activated protein kinase; The 5'-AMP ...
296-341 4.78e-03

CBS pair domain found in 5'-AMP (adenosine monophosphate)-activated protein kinase; The 5'-AMP (adenosine monophosphate)-activated protein kinase (AMPK) coordinates metabolic function with energy availability by responding to changes in intracellular ATP (adenosine triphosphate) and AMP concentrations. Most of the members of this cd contain two Bateman domains, each of which is composed of a tandem pair of cystathionine beta-synthase (CBS) motifs. The CBS domain, named after human CBS, is a small domain originally identified in cystathionine beta-synthase and is subsequently found in a wide range of different proteins. CBS domains usually occur in tandem repeats. They associate to form a so-called Bateman domain or a CBS pair based on crystallographic studies in bacteria. The CBS pair was used as a basis for this cd hierarchy since the human CBS proteins can adopt the typical core structure and form an intramolecular CBS pair. The interface between the two CBS domains forms a cleft that is a potential ligand binding site. The CBS pair coexists with a variety of other functional domains and this has been used to help in its classification here. It has been proposed that the CBS domain may play a regulatory role, although its exact function is unknown. Mutations of conserved residues within this domain are associated with a variety of human hereditary diseases, including congenital myotonia, idiopathic generalized epilepsy, hypercalciuric nephrolithiasis, and classic Bartter syndrome (CLC chloride channel family members), Wolff-Parkinson-White syndrome (gamma 2 subunit of AMP-activated protein kinase), retinitis pigmentosa (IMP dehydrogenase-1), and homocystinuria (cystathionine beta-synthase).


Pssm-ID: 341399 [Multi-domain]  Cd Length: 124  Bit Score: 37.11  E-value: 4.78e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*.
gi 1443048451 296 ECATVDMPILDALRIMQERKFLHLPVMDRDGSIVSILDVIDITHAA 341
Cdd:cd04641     6 ATASMDTPVIDALNLFVERRVSALPIVDEDGRVVDIYAKFDVINLA 51
CBS_pair_arch2_repeat2 cd04614
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains present in archaea, ...
279-332 4.95e-03

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: 37.64  E-value: 4.95e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1443048451 279 NLPAdsTPVEKVMTLDPECATVDMPILDALRIMQERKFLHLPVMDRDGSIVSIL 332
Cdd:cd04614    91 ELPD--KPVKDVMTKDVVTAFPSSTVSEAAKKMIRNDIEQLPVVSGEGDLAGML 142
CBS_pair_arch1_repeat2 cd04632
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains present in archaea, ...
126-272 5.24e-03

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: 37.31  E-value: 5.24e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443048451 126 TRHPVFVPSETLAVEALHKMVQGKFRHLPVV-ENGEVIAMLDiakcLYDAIARIERASDKGKaaaiasavdaaaGNDPTA 204
Cdd:cd04632     1 TEEVITVNEDDTIGKAINLLREHGISRLPVVdDNGKLVGIVT----TYDIVDFVVRPGTKTR------------GGDRGG 64
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1443048451 205 SsmveafKEQMLRPSLSTITTaeSTVVIVSPGDSVLTATQKMVEVHASSAVVAVGNKA-QGILTSRDIL 272
Cdd:cd04632    65 E------KERMLDLPVYDIMS--SPVVTVTRDATVADAVERMLENDISGLVVTPDDNMvIGILTKTDVL 125
CBS_pair_inorgPPase cd04597
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with ...
295-344 5.43e-03

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: 36.56  E-value: 5.43e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 1443048451 295 PECATVDMPILDALRIMQERKFLHLPVMDRDGSIVSILDVIDITHAAFSI 344
Cdd:cd04597     7 VEPLSPETSIKDAWNLMDENNLKTLPVTDDNGKLIGLLSISDIARTVDYI 56
CBS_pair_arch1_repeat2 cd04632
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains present in archaea, ...
230-340 7.26e-03

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


Pssm-ID: 341395 [Multi-domain]  Cd Length: 127  Bit Score: 36.93  E-value: 7.26e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443048451 230 VVIVSPGDSVLTATQKMVEvHASSAVVAV--GNKAQGILTSRDIL---MRMIAKNLPAD---------STPVEKVMTLDP 295
Cdd:cd04632     4 VITVNEDDTIGKAINLLRE-HGISRLPVVddNGKLVGIVTTYDIVdfvVRPGTKTRGGDrggekermlDLPVYDIMSSPV 82
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 1443048451 296 ECATVDMPILDALRIMQERKFLHLPVMDRDGSIVSILDVIDITHA 340
Cdd:cd04632    83 VTVTRDATVADAVERMLENDISGLVVTPDDNMVIGILTKTDVLRA 127
CBS_pair_bac_arch cd17785
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains present in bacteria ...
232-337 8.26e-03

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: 36.86  E-value: 8.26e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443048451 232 IVSPGDSVLTATQKMVE--VHASSAVVAVGNKAQGILTSRDILM-----------RMIAKNLP---ADSTPVEKVMtLDP 295
Cdd:cd17785    14 VVHENTSIRDVIDKMIEdpKTRSVYVVDDDEKLLGIITLMELLKyigyrfgvtiyKGVSFGLLlriSLKEKAKDIM-LSP 92
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 1443048451 296 ECATVDMPILDALRIMQERKFLHLPVMDRDGSIVSILDVIDI 337
Cdd:cd17785    93 IYVKKEDTLEEALELMVKNRLQELPVVDENGKVIGDLNSLEL 134
CBS_pair_archHTH_assoc cd04588
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains found in archaea and ...
92-165 9.84e-03

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: 35.97  E-value: 9.84e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1443048451  92 SNALLCGILTDKDIAtRVIARELkiEETPAWKVMTRHPVFVPSETLAVEALHKMVQGKFRHLPVV-ENGEVIAML 165
Cdd:cd04588    32 DDGKLVGIVTLTDIA-KALAEGK--ENAKVKDIMTKDVITIDKDEKIYDAIRLMNKHNIGRLIVVdDNGKPVGII 103
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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