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Conserved domains on  [gi|1705233313|ref|WP_142589626|]
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cyclic nucleotide-binding/CBS domain-containing protein [Pseudorhizobium halotolerans]

Protein Classification

cyclic nucleotide-binding/CBS domain-containing protein( domain architecture ID 11458464)

uncharacterized cyclic nucleotide-binding/CBS (cystathione beta synthase) domain-containing protein

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
COG2905 COG2905
Signal-transduction protein containing cAMP-binding, CBS, and nucleotidyltransferase domains ...
 9-129 1.99e-20

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


:

Pssm-ID: 442149 [Multi-domain]  Cd Length: 124  Bit Score: 80.26  E-value: 1.99e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1705233313   9 VARERLLIVNQDAPVIEAARLLRDGRSDLVIACDAAGHLSGVVTKSDIVAQISHCLGASCTTGISAVMSRDVTFCRPEDW 88
Cdd:COG2905     4 IMSRDVVTVSPDATVREAARLMTEKGVGSLVVVDDDGRLVGIITDRDLRRRVLAEGLDPLDTPVSEVMTRPPITVSPDDS 83

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 1705233313  89 LHDIWGIMKERQLKNVPITDDAsRPIGILNARDALQALMQE 129
Cdd:COG2905    84 LAEALELMEEHRIRHLPVVDDG-KLVGIVSITDLLRALSEE 123
 
Name Accession Description Interval E-value
COG2905 COG2905
Signal-transduction protein containing cAMP-binding, CBS, and nucleotidyltransferase domains ...
 9-129 1.99e-20

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


Pssm-ID: 442149 [Multi-domain]  Cd Length: 124  Bit Score: 80.26  E-value: 1.99e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1705233313   9 VARERLLIVNQDAPVIEAARLLRDGRSDLVIACDAAGHLSGVVTKSDIVAQISHCLGASCTTGISAVMSRDVTFCRPEDW 88
Cdd:COG2905     4 IMSRDVVTVSPDATVREAARLMTEKGVGSLVVVDDDGRLVGIITDRDLRRRVLAEGLDPLDTPVSEVMTRPPITVSPDDS 83

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 1705233313  89 LHDIWGIMKERQLKNVPITDDAsRPIGILNARDALQALMQE 129
Cdd:COG2905    84 LAEALELMEEHRIRHLPVVDDG-KLVGIVSITDLLRALSEE 123
CBS_pair_arch cd09836
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains; The CBS domain, ...
 10-127 5.29e-16

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: 68.70  E-value: 5.29e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1705233313  10 ARERLLIVNQDAPVIEAARLLRDGRSDLVIACDAAGHLSGVVTKSDIVAQISHclGASCTTGISAVMSRDVTFCRPEDWL 89
Cdd:cd09836     1 MSKPVVTVPPETTIREAAKLMAENNIGSVVVVDDDGKPVGIVTERDIVRAVAE--GIDLDTPVEEIMTKNLVTVSPDESI 78

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 1705233313  90 HDIWGIMKERQLKNVPITDDASRPIGILNARDALQALM 127
Cdd:cd09836    79 YEAAELMREHNIRHLPVVDGGGKLVGVISIRDLARELS 116
CBS pfam00571
CBS domain; CBS domains are small intracellular modules that pair together to form a stable ...
 72-127 1.20e-07

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: 45.28  E-value: 1.20e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1705233313  72 ISAVMSRDVTFCRPEDWLHDIWGIMKERQLKNVPITDDASRPIGILNARDALQALM 127
Cdd:pfam00571   1 VKDIMTKDVVTVSPDTTLEEALELMREHGISRLPVVDEDGKLVGIVTLKDLLRALL 56
PRK14869 PRK14869
putative manganese-dependent inorganic diphosphatase;
72-127 2.30e-06

putative manganese-dependent inorganic diphosphatase;


Pssm-ID: 237843 [Multi-domain]  Cd Length: 546  Bit Score: 45.21  E-value: 2.30e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1705233313  72 ISAVMSRDVTFCRPEDWLHDIWGIMKERQLKNVPITDDASRPIGILNARDALQALM 127
Cdd:PRK14869   70 VRDLEIDKPVTVSPDTSLKEAWNLMDENNVKTLPVVDEEGKLLGLVSLSDLARAYM 125
CBS smart00116
Domain in cystathionine beta-synthase and other proteins; Domain present in all 3 forms of ...
 13-60 8.22e-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: 32.48  E-value: 8.22e-03
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*...
gi 1705233313   13 RLLIVNQDAPVIEAARLLRDGRSDLVIACDAAGHLSGVVTKSDIVAQI 60
Cdd:smart00116   1 DVVTVSPDTTLEEALELLRENGIRRLPVVDEEGRLVGIVTRRDIIKAL 48
 
Name Accession Description Interval E-value
COG2905 COG2905
Signal-transduction protein containing cAMP-binding, CBS, and nucleotidyltransferase domains ...
 9-129 1.99e-20

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


Pssm-ID: 442149 [Multi-domain]  Cd Length: 124  Bit Score: 80.26  E-value: 1.99e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1705233313   9 VARERLLIVNQDAPVIEAARLLRDGRSDLVIACDAAGHLSGVVTKSDIVAQISHCLGASCTTGISAVMSRDVTFCRPEDW 88
Cdd:COG2905     4 IMSRDVVTVSPDATVREAARLMTEKGVGSLVVVDDDGRLVGIITDRDLRRRVLAEGLDPLDTPVSEVMTRPPITVSPDDS 83

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 1705233313  89 LHDIWGIMKERQLKNVPITDDAsRPIGILNARDALQALMQE 129
Cdd:COG2905    84 LAEALELMEEHRIRHLPVVDDG-KLVGIVSITDLLRALSEE 123
CBS COG0517
CBS domain [Signal transduction mechanisms];
1-131 8.59e-20

CBS domain [Signal transduction mechanisms];


Pssm-ID: 440283 [Multi-domain]  Cd Length: 128  Bit Score: 78.75  E-value: 8.59e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1705233313   1 MLVENItavARERLLIVNQDAPVIEAARLLRDGRSDLVIACDAAGHLSGVVTKSDIVAQISHCLGASCTTGISAVMSRDV 80
Cdd:COG0517     1 MKVKDI---MTTDVVTVSPDATVREALELMSEKRIGGLPVVDEDGKLVGIVTDRDLRRALAAEGKDLLDTPVSEVMTRPP 77

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1705233313  81 TFCRPEDWLHDIWGIMKERQLKNVPITDDASRPIGILNARDALQALMQEVE 131
Cdd:COG0517    78 VTVSPDTSLEEAAELMEEHKIRRLPVVDDDGRLVGIITIKDLLKALLEPLA 128
CBS_pair_arch cd09836
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains; The CBS domain, ...
 10-127 5.29e-16

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: 68.70  E-value: 5.29e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1705233313  10 ARERLLIVNQDAPVIEAARLLRDGRSDLVIACDAAGHLSGVVTKSDIVAQISHclGASCTTGISAVMSRDVTFCRPEDWL 89
Cdd:cd09836     1 MSKPVVTVPPETTIREAAKLMAENNIGSVVVVDDDGKPVGIVTERDIVRAVAE--GIDLDTPVEEIMTKNLVTVSPDESI 78

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 1705233313  90 HDIWGIMKERQLKNVPITDDASRPIGILNARDALQALM 127
Cdd:cd09836    79 YEAAELMREHNIRHLPVVDGGGKLVGVISIRDLARELS 116
CBS_pair_SF cd02205
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains superfamily; The CBS ...
 11-124 6.38e-16

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: 68.43  E-value: 6.38e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1705233313  11 RERLLIVNQDAPVIEAARLLRDGRSDLVIACDAAGHLSGVVTKSDIVAQISHcLGASCTTGISAVMSRDVTFCRPEDWLH 90
Cdd:cd02205     1 TRDVVTVDPDTTVREALELMAENGIGALPVVDDDGKLVGIVTERDILRALVE-GGLALDTPVAEVMTPDVITVSPDTDLE 79

                          90       100       110
                  ....*....|....*....|....*....|....
gi 1705233313  91 DIWGIMKERQLKNVPITDDASRPIGILNARDALQ 124
Cdd:cd02205    80 EALELMLEHGIRRLPVVDDDGKLVGIVTRRDILR 113
COG3448 COG3448
CBS-domain-containing membrane protein [Signal transduction mechanisms];
1-131 1.24e-15

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


Pssm-ID: 442671 [Multi-domain]  Cd Length: 136  Bit Score: 67.97  E-value: 1.24e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1705233313   1 MLVENItavARERLLIVNQDAPVIEAARLLRDGRSDLVIACDAAGHLSGVVTKSDIVAQISHCLGASCTTGISA-----V 75
Cdd:COG3448     2 MTVRDI---MTRDVVTVSPDTTLREALELMREHGIRGLPVVDEDGRLVGIVTERDLLRALLPDRLDELEERLLDlpvedV 78

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1705233313  76 MSRDVTFCRPEDWLHDIWGIMKERQLKNVPITDDASRPIGILNARDALQALMQEVE 131
Cdd:COG3448    79 MTRPVVTVTPDTPLEEAAELMLEHGIHRLPVVDDDGRLVGIVTRTDLLRALARLLE 134
COG2524 COG2524
Predicted transcriptional regulator, contains C-terminal CBS domains [Transcription];
1-126 4.03e-14

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


Pssm-ID: 442013 [Multi-domain]  Cd Length: 206  Bit Score: 65.68  E-value: 4.03e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1705233313   1 MLVENItavARERLLIVNQDAPVIEAARLLRDGRSDLVIACDAaGHLSGVVTKSDIVAQISHCLGAScTTGISAVMSRDV 80
Cdd:COG2524    86 MKVKDI---MTKDVITVSPDTTLEEALELMLEKGISGLPVVDD-GKLVGIITERDLLKALAEGRDLL-DAPVSDIMTRDV 160

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 1705233313  81 TFCRPEDWLHDIWGIMKERQLKNVPITDDASRPIGILNARDALQAL 126
Cdd:COG2524   161 VTVSEDDSLEEALRLMLEHGIGRLPVVDDDGKLVGIITRTDILRAL 206
CBS_pair_HRP1_like cd04622
CBS pair domain found in Hypoxic Response Protein 1 (HRP1) -like proteinds; Mycobacterium ...
 17-117 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: 59.36  E-value: 1.66e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1705233313  17 VNQDAPVIEAARLLRDGRSDLVIACDAaGHLSGVVTKSDIVAQISHCLGASCTTGISAVMSRDVTFCRPEDWLHDIWGIM 96
Cdd:cd04622     8 VSPDTTLREAARLMRDLDIGALPVCEG-DRLVGMVTDRDIVVRAVAEGKDPNTTTVREVMTGDVVTCSPDDDVEEAARLM 86

                          90       100
                  ....*....|....*....|.
gi 1705233313  97 KERQLKNVPITDDASRPIGIL 117
Cdd:cd04622    87 AEHQVRRLPVVDDDGRLVGIV 107
CBS_pair_MUG70_1 cd17781
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains similar to MUG70 ...
 15-118 1.07e-11

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: 57.60  E-value: 1.07e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1705233313  15 LIVNQDAPVIEAARLLRDGRSDLVIACDAAGHLSGVVTKSDI----VAQishCLGASCTTgISAVMSRDVTFCRPEDWLH 90
Cdd:cd17781     5 LTVPETTTVAEAAQLMAAKRTDAVLVVDDDGGLSGIFTDKDLarrvVAS---GLDPRSTL-VSSVMTPNPLCVTMDTSAT 80

                          90       100
                  ....*....|....*....|....*...
gi 1705233313  91 DIWGIMKERQLKNVPITDDASRPIGILN 118
Cdd:cd17781    81 DALDLMVEGKFRHLPVVDDDGDVVGVLD 108
CBS_pair_bac_euk cd04623
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains present in bacteria ...
 20-121 2.28e-11

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: 56.66  E-value: 2.28e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1705233313  20 DAPVIEAARLLRDGRSDLVIACDAAGHLSGVVTKSDIVAQISHcLGASC-TTGISAVMSRDVTFCRPEDWLHDIWGIMKE 98
Cdd:cd04623    10 DATVAEALRLLAEKNIGALVVVDDGGRLVGILSERDYVRKLAL-RGASSlDTPVSEIMTRDVVTCTPDDTVEECMALMTE 88

                          90       100
                  ....*....|....*....|...
gi 1705233313  99 RQLKNVPITDDaSRPIGILNARD 121
Cdd:cd04623    89 RRIRHLPVVED-GKLVGIVSIGD 110
YtoI COG4109
Predicted transcriptional regulator containing CBS domains [Transcription];
1-128 4.11e-10

Predicted transcriptional regulator containing CBS domains [Transcription];


Pssm-ID: 443285 [Multi-domain]  Cd Length: 135  Bit Score: 53.76  E-value: 4.11e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1705233313   1 MLVENItaVARERLLIVNQDAPVIEAARLLRDGRSDLVIACDAAGHLSGVVTKSDIvaqishcLGASCTTGISAVMSRDV 80
Cdd:COG4109    16 LLVEDI--MTLEDVATLSEDDTVEDALELLEKTGHSRFPVVDENGRLVGIVTSKDI-------LGKDDDTPIEDVMTKNP 86

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 1705233313  81 TFCRPEDWLHDIWGIMKERQLKNVPITDDASRPIGILNARDALQALMQ 128
Cdd:COG4109    87 ITVTPDTSLASAAHKMIWEGIELLPVVDDDGRLLGIISRQDVLKALQK 134
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 ...
 9-121 1.17e-09

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: 52.04  E-value: 1.17e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1705233313   9 VARERLLIVNQDAPVIEAARLLRDGR-SDLVIAcdAAGHLSGVVTKSDI----VAQishclGASCTTGISAVMSRDVTFC 83
Cdd:cd04587     1 LMSRPPVTVPPDATIQEAAQLMSEERvSSLLVV--DDGRLVGIVTDRDLrnrvVAE-----GLDPDTPVSEIMTPPPVTI 73

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 1705233313  84 RPEDWLHDIWGIMKERQLKNVPITDDaSRPIGILNARD 121
Cdd:cd04587    74 DADALVFEALLLMLERNIHHLPVVDD-GRVVGVVTATD 110
CBS_pair_ABC_OpuCA_assoc cd04583
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains found associated with ...
 17-117 1.41e-09

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: 51.75  E-value: 1.41e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1705233313  17 VNQDAPVIEAARLLRDGRSDLVIACDAAGHLSGVVTKSDIVAQISHclgascTTGISAVMSRDVTFCRPEDWLHDIWGIM 96
Cdd:cd04583     7 ITPERTLAQAIEIMREKRVDSLLVVDKDNVLLGIVDIEDINRNYRK------AKKVGEIMERDVFTVKEDSLLRDTVDRI 80

                          90       100
                  ....*....|....*....|.
gi 1705233313  97 KERQLKNVPITDDASRPIGIL 117
Cdd:cd04583    81 LKRGLKYVPVVDEQGRLVGLV 101
CBS_pair_BON_assoc cd04586
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with the ...
 17-125 1.86e-09

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: 1.86e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1705233313  17 VNQDAPVIEAARLLRDGR-SDL-VIacDAAGHLSGVVTKSDIVAQIS-------HCLGASCTTGISA------------- 74
Cdd:cd04586     8 VTPDTSVREAARLLLEHRiSGLpVV--DDDGKLVGIVSEGDLLRREEpgteprrVWWLDALLESPERlaeeyvkahgrtv 85

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1705233313  75 --VMSRDVTFCRPEDWLHDIWGIMKERQLKNVPITDDaSRPIGILNARDALQA 125
Cdd:cd04586    86 gdVMTRPVVTVSPDTPLEEAARLMERHRIKRLPVVDD-GKLVGIVSRADLLRA 137
CBS_pair_bact_arch cd17775
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains present in bacteria ...
 10-126 2.11e-09

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


Pssm-ID: 341411 [Multi-domain]  Cd Length: 117  Bit Score: 51.39  E-value: 2.11e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1705233313  10 ARERLLIVNQDAPVIEAARLLRDGRSDLVIACDAAGHLSGVVTKSDIVAQI-SHCLGASCTTgISAVMSRDVTFCRPEDW 88
Cdd:cd17775     1 CRREVVTASPDTSVLEAARLMRDHHVGSVVVVEEDGKPVGIVTDRDIVVEVvAKGLDPKDVT-VGDIMSADLITAREDDG 79

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 1705233313  89 LHDIWGIMKERQLKNVPITDDASRPIGILNARDALQAL 126
Cdd:cd17775    80 LFEALERMREKGVRRLPVVDDDGELVGIVTLDDILELL 117
CBS_pair_arch1_repeat2 cd04632
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains present in archaea, ...
 12-125 8.97e-09

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: 50.02  E-value: 8.97e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1705233313  12 ERLLIVNQDAPVIEAARLLRDGRSDLVIACDAAGHLSGVVTKSDIVAQISHcLGASCTTG-------------ISAVMSR 78
Cdd:cd04632     2 EEVITVNEDDTIGKAINLLREHGISRLPVVDDNGKLVGIVTTYDIVDFVVR-PGTKTRGGdrggekermldlpVYDIMSS 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 1705233313  79 DVTFCRPEDWLHDIWGIMKERQLKNVPITDDASRPIGILNARDALQA 125
Cdd:cd04632    81 PVVTVTRDATVADAVERMLENDISGLVVTPDDNMVIGILTKTDVLRA 127
CBS pfam00571
CBS domain; CBS domains are small intracellular modules that pair together to form a stable ...
 72-127 1.20e-07

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: 45.28  E-value: 1.20e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1705233313  72 ISAVMSRDVTFCRPEDWLHDIWGIMKERQLKNVPITDDASRPIGILNARDALQALM 127
Cdd:pfam00571   1 VKDIMTKDVVTVSPDTTLEEALELMREHGISRLPVVDEDGKLVGIVTLKDLLRALL 56
CBS_pair_MUG70_2 cd17782
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains similar to MUG70 ...
 12-124 1.24e-07

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: 46.86  E-value: 1.24e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1705233313  12 ERLLIVNQDAPVIEAARLLRDGRSDLVIACDAAGHLSGVVTKSDIVAQIshcLGASC---TTGISAVMSRDVTFCRPEDW 88
Cdd:cd17782     2 TPPPLVSPKTTVREAARLMKENRTTAVLVMDNSGKVIGIFTSKDVVLRV---LAAGLdpaTTSVVRVMTPNPETAPPSTT 78

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 1705233313  89 LHDIWGIMKERQLKNVPITDDASRPIGILnarDALQ 124
Cdd:cd17782    79 ILDALHKMHEGKFLNLPVVDDEGEIVGLV---DVLQ 111
CBS_pair_bac cd04629
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains present in bacteria; ...
 13-125 2.96e-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: 341392 [Multi-domain]  Cd Length: 116  Bit Score: 45.89  E-value: 2.96e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1705233313  13 RLLIVNQDAPVIEAARLLRDGRsdlvIAC----DAAGHLSGVVTKSDIVAQIshcLGAS--CTTG--ISAVMSRDVTFCR 84
Cdd:cd04629     4 NPVTLTPDTSILEAVELLLEHK----ISGapvvDEQGRLVGFLSEQDCLKAL---LEASyhCEPGgtVADYMSTEVLTVS 76

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 1705233313  85 PEDWLHDIWGIMKERQLKNVPITDDAsRPIGILNARDALQA 125
Cdd:cd04629    77 PDTSIVDLAQLFLKNKPRRYPVVEDG-KLVGQISRRDVLRA 116
CBS_pair_DHH_polyA_Pol_assoc cd04595
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with the ...
 17-125 5.25e-07

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: 45.18  E-value: 5.25e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1705233313  17 VNQDAPVIEAAR-LLRDGRSDLVIACDaaGHLSGVVTKSDIVAQISHCLGAScttGISAVMSRDVTFCRPEDWLHDIWGI 95
Cdd:cd04595     7 VSPDTTIEEARKiMLRYGHTGLPVVED--GKLVGIISRRDVDKAKHHGLGHA---PVKGYMSTNVITIDPDTSLEEAQEL 81

                          90       100       110
                  ....*....|....*....|....*....|
gi 1705233313  96 MKERQLKNVPITDDAsRPIGILNARDALQA 125
Cdd:cd04595    82 MVEHDIGRLPVVEEG-KLVGIVTRSDVLRY 110
CBS_pair_archHTH_assoc cd04588
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains found in archaea and ...
 11-124 9.68e-07

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


Pssm-ID: 341364 [Multi-domain]  Cd Length: 111  Bit Score: 44.45  E-value: 9.68e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1705233313  11 RERLLIVNQDAPVIEAARLLrdgrSDLVIacDAA-----GHLSGVVTKSDIVAQISHCLGascTTGISAVMSRDVTFCRP 85
Cdd:cd04588     1 SKDLITLKPDATIKDAAKLL----SENNI--HGApvvddGKLVGIVTLTDIAKALAEGKE---NAKVKDIMTKDVITIDK 71

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 1705233313  86 EDWLHDIWGIMKERQLKNVPITDDASRPIGILNARDALQ 124
Cdd:cd04588    72 DEKIYDAIRLMNKHNIGRLIVVDDNGKPVGIITRTDILK 110
CBS_pair_ACT cd17787
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains found in Thermatoga ...
 17-128 1.15e-06

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


Pssm-ID: 341423 [Multi-domain]  Cd Length: 111  Bit Score: 44.33  E-value: 1.15e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1705233313  17 VNQDAPVIEAARLLRDGRSDLVIACDAAGHLSGVVTKSDIvaqishcLGASCTTGISAVMSRDVTFCRPEDWLHDIWGIM 96
Cdd:cd17787     7 FEESATVGEVLHEMRKYETDYCIVVDEEGKFAGMVRKSKI-------MDEDLDKKVKEYVVEPDFYCHEEDYIEDAALLL 79

                          90       100       110
                  ....*....|....*....|....*....|..
gi 1705233313  97 KERQLKNVPITDDASRPIGILNARDALQALMQ 128
Cdd:cd17787    80 IESHEFVLPVVNSDMKVKGVLTVFEILEALME 111
CBS_arch_repeat2 cd17778
CBS pair domains found in archeal proteins, repeat 2; CBS pair domains found in archeal ...
 12-126 1.27e-06

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: 44.63  E-value: 1.27e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1705233313  12 ERLLIVNQDAPVIEAARL--LRDGRSDLVIAcdaAGHLSGVVTKSDIVAQI-SHCLGASCTTG---------ISAVMSRD 79
Cdd:cd17778     8 TPVVTIYPDDTLKEAMELmvTRGFRRLPVVS---GGKLVGIVTAMDIVKYFgSHEAKKRLTTGdideaystpVEEIMSKE 84

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 1705233313  80 VTFCRPEDWLHDIWGIMKERQLKNVPITDDASRPIGILNARDALQAL 126
Cdd:cd17778    85 VVTIEPDADIAEAARLMIKKNVGSLLVVDDEGELKGIITERDVLIAL 131
PRK14869 PRK14869
putative manganese-dependent inorganic diphosphatase;
72-127 2.30e-06

putative manganese-dependent inorganic diphosphatase;


Pssm-ID: 237843 [Multi-domain]  Cd Length: 546  Bit Score: 45.21  E-value: 2.30e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1705233313  72 ISAVMSRDVTFCRPEDWLHDIWGIMKERQLKNVPITDDASRPIGILNARDALQALM 127
Cdd:PRK14869   70 VRDLEIDKPVTVSPDTSLKEAWNLMDENNVKTLPVVDEEGKLLGLVSLSDLARAYM 125
CBS_archAMPK_gamma-repeat1 cd17779
signal transduction protein with CBS domains; Archeal gamma-subunit of 5'-AMP-activated ...
 6-126 2.49e-06

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: 43.76  E-value: 2.49e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1705233313   6 ITAVARERLLIVNQDAPVIEAAR-LLRDGRSDLVIACDAAGHLSGVVTKSDIVAQI-------------SHCLGASCTTG 71
Cdd:cd17779     2 IMAIATKDVITIPPTTTIIGAIKtMTEKGFRRLPVADAGTKRLEGIVTSMDIVDFLgggskynlvekkhNGNLLAAINEP 81

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1705233313  72 ISAVMSRDVTFCRPEDWLHDIWGIMKERQLKNVPITDDASRPIGILNARDALQAL 126
Cdd:cd17779    82 VREIMTRDVISVKENASIDDAIELMLEKNVGGLPIVDKDGKVIGIVTERDFLKFL 136
CBS_pair_NTP_transferase_assoc cd04607
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domain associated with the ...
 15-124 3.35e-06

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: 42.82  E-value: 3.35e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1705233313  15 LIVNQDAPVIEAARLLRDGRSDLVIACDAAGHLSGVVTKSDIVAQIshcL-GASCTTGISAVMSRDVTFCRPEDWLHDIW 93
Cdd:cd04607     5 VLVSPDTTIREAIEVIDKGALQIALVVDENRKLLGTVTDGDIRRGL---LkGLSLDAPVEEVMNKNPITASPSTSREELL 81

                          90       100       110
                  ....*....|....*....|....*....|.
gi 1705233313  94 GIMKERQLKNVPITDDASRPIGILNARDALQ 124
Cdd:cd04607    82 ALMRAKKILQLPIVDEQGRVVGLETLDDLLA 112
CBS_pair_arch_MET2_assoc cd04605
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with the ...
 16-121 3.41e-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: 43.00  E-value: 3.41e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1705233313  16 IVNQDAPVIEAARLLRDGRSDLVIACDAAGHLSGVVTKSDIVAQIshclgASCTTGISAVMSRDVTFCRPEDWLHDIWGI 95
Cdd:cd04605    12 TIREDISIEEAAKIMIDKNVTHLPVVSEDGKLIGIVTSWDISKAV-----ALKKDSLEEIMTRNVITARPDEPIELAARK 86

                          90       100
                  ....*....|....*....|....*.
gi 1705233313  96 MKERQLKNVPITDDASRPIGILNARD 121
Cdd:cd04605    87 MEKHNISALPVVDDDRRVIGIITSDD 112
COG2905 COG2905
Signal-transduction protein containing cAMP-binding, CBS, and nucleotidyltransferase domains ...
 72-129 4.69e-06

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


Pssm-ID: 442149 [Multi-domain]  Cd Length: 124  Bit Score: 42.89  E-value: 4.69e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1705233313  72 ISAVMSRDVTFCRPEDWLHDIWGIMKERQLKNVPITDDASRPIGILNARDALQALMQE 129
Cdd:COG2905     1 VKDIMSRDVVTVSPDATVREAARLMTEKGVGSLVVVDDDGRLVGIITDRDLRRRVLAE 58
CBS_pair_SIS_assoc cd04604
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with the ...
 12-118 5.62e-06

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: 42.37  E-value: 5.62e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1705233313  12 ERLLIVNQDAPVIEAARLLRDGRSDLVIACDAAGHLSGVVTKSDIVAQISHCLGASCTTgISAVMSRDVTFCRPEDWLHD 91
Cdd:cd04604    13 DELPLVSPDTSLKEALLEMTRKGLGCTAVVDEDGRLVGIITDGDLRRALEKGLDILNLP-AKDVMTRNPKTISPDALAAE 91

                          90       100
                  ....*....|....*....|....*..
gi 1705233313  92 IWGIMKERQLKNVPITDDASRPIGILN 118
Cdd:cd04604    92 ALELMEEHKITVLPVVDEDGKPVGILH 118
CBS_arch_repeat1 cd17777
CBS pair domains found in archeal proteins, repeat 1; CBS pair domains found in archeal ...
 3-126 6.22e-06

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


Pssm-ID: 341413 [Multi-domain]  Cd Length: 137  Bit Score: 42.71  E-value: 6.22e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1705233313   3 VENITAVARERLLIVNQDAPVIEAARLLRDGRSDLVIACDAaGHLSGVVTKSDIVAqishCLGASCTTGI---------- 72
Cdd:cd17777     1 EKELMIIASPPVLSISPSAPILSAFEKMNRRGIRRLVVVDE-NKLEGILSARDLVS----YLGGGCLFKIvesrhqgdly 75

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1705233313  73 --------SAVMSRDVTFCRPEDWLHDIWGIMKERQLKNVPITDDASRPIGILNARDALQAL 126
Cdd:cd17777    76 salnrevvETIMTPNPVYVYEDSDLIEALTIMVTRGIGSLPVVDRDGRPVGIVTERDLVLYL 137
CBS_archAMPK_gamma-repeat2 cd04631
CBS pair domains found in archeal 5'-AMP-activated protein kinase gamma subunit-like proteins; ...
 17-126 7.87e-06

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: 42.21  E-value: 7.87e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1705233313  17 VNQDAPVIEAAR-LLRDGRSDLVIACDaaGHLSGVVTKSDIVaqisHCLGA-----SCTTG---------ISAVMSRDVT 81
Cdd:cd04631    13 ATPGTPIEDVAKiMVRNGFRRLPVVSD--GKLVGIVTSTDIM----RYLGSgeafeKLKTGnihevlnvpISSIMKRDII 86

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 1705233313  82 FCRPEDWLHDIWGIMKERQLKNVPITDDaSRPIGILNARDALQAL 126
Cdd:cd04631    87 TTTPDTDLGEAAELMLEKNIGALPVVDD-GKLVGIITERDILRAI 130
CBS_pair_HPP_assoc cd04600
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with the ...
 76-117 9.94e-06

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


Pssm-ID: 341375 [Multi-domain]  Cd Length: 133  Bit Score: 42.16  E-value: 9.94e-06
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 1705233313  76 MSRDVTFCRPEDWLHDIWGIMKERQLKNVPITDDASRPIGIL 117
Cdd:cd04600     1 MSRDVVTVTPDTSLEEAWRLLRRHRIKALPVVDRARRLVGIV 42
CBS_pair_inorgPPase cd04597
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with ...
 17-123 1.03e-05

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: 41.56  E-value: 1.03e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1705233313  17 VNQDAPVIEAARLLRDGRSDLVIACDAAGHLSGVVTKSDIvaqishclgascTTGISAVMSRD-VTFCRPEDWLHDIWGI 95
Cdd:cd04597    10 LSPETSIKDAWNLMDENNLKTLPVTDDNGKLIGLLSISDI------------ARTVDYIMTKDnLIVFKEDDYLDEVKEI 77

                          90       100
                  ....*....|....*....|....*...
gi 1705233313  96 MKERQLKNVPITDDASRPIGILNARDAL 123
Cdd:cd04597    78 MLNTNFRNYPVVDENNKFLGTISRKHLI 105
gutQ PRK11543
arabinose-5-phosphate isomerase GutQ;
12-125 1.31e-05

arabinose-5-phosphate isomerase GutQ;


Pssm-ID: 183186 [Multi-domain]  Cd Length: 321  Bit Score: 42.83  E-value: 1.31e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1705233313  12 ERLLIVNQDAPVIEAA-RLLRDGRSdLVIACDAAGHLSGVVTKSDIVAQISHclGASCTTGISAVMSRDvTFCRPEDW-L 89
Cdd:PRK11543  207 DAIPQVALTASVMDAMlELSRTGLG-LVAVCDAQQQVQGVFTDGDLRRWLVG--GGALTTPVNEAMTRG-GTTLQAQSrA 282

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 1705233313  90 HDIWGIMKERQLKNVPITDDASRPIGILNARDALQA 125
Cdd:PRK11543  283 IDAKEILMKRKITAAPVVDENGKLTGAINLQDFYQA 318
PRK07807 PRK07807
GuaB1 family IMP dehydrogenase-related protein;
15-125 3.20e-05

GuaB1 family IMP dehydrogenase-related protein;


Pssm-ID: 181127 [Multi-domain]  Cd Length: 479  Bit Score: 41.81  E-value: 3.20e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1705233313  15 LIVNQDAPVIEAARLLRDGRSDLVIACDAAGHLSGVVTKSDivaqishCLGASCTTGISAVMSRDVTFCRPEDWLHDIWG 94
Cdd:PRK07807  100 VTLSPDDTVGDALALLPKRAHGAVVVVDEEGRPVGVVTEAD-------CAGVDRFTQVRDVMSTDLVTLPAGTDPREAFD 172

                          90       100       110
                  ....*....|....*....|....*....|.
gi 1705233313  95 IMKERQLKNVPITDDASRPIGILNARDALQA 125
Cdd:PRK07807  173 LLEAARVKLAPVVDADGRLVGVLTRTGALRA 203
CBS_pair_ParBc_assoc cd04610
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with a ...
 17-121 6.15e-05

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: 39.61  E-value: 6.15e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1705233313  17 VNQDAPVIEAARLLRDGRSDLVIACDAaGHLSGVVTKSDIVAQISHclgasctTGISAVMSRDVTFCRPEDWLHDIWGIM 96
Cdd:cd04610     8 VSPDDTVKDVIKLIKETGHDGFPVVDD-GKVVGYVTAKDLLGKDDD-------EKVSEIMSRDTVVADPDMDITDAARVI 79

                          90       100
                  ....*....|....*....|....*
gi 1705233313  97 KERQLKNVPITDDASRPIGILNARD 121
Cdd:cd04610    80 FRSGISKLPVVDDEGNLVGIITNMD 104
CBS_pair_HPP_assoc cd04600
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with the ...
 14-126 7.51e-05

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


Pssm-ID: 341375 [Multi-domain]  Cd Length: 133  Bit Score: 39.85  E-value: 7.51e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1705233313  14 LLIVNQDAPVIEAARLLRDGR--SDLVIacDAAGHLSGVVTKSDIVAQI--------------SHCLGASCTTGISAVMS 77
Cdd:cd04600     5 VVTVTPDTSLEEAWRLLRRHRikALPVV--DRARRLVGIVTLADLLKHAdldpprglrgrlrrTLGLRRDRPETVGDIMT 82

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 1705233313  78 RDVTFCRPEDWLHDIWGIMKERQLKNVPITDDASRPIGILNARDALQAL 126
Cdd:cd04600    83 RPVVTVRPDTPIAELVPLFSDGGLHHIPVVDADGRLVGIVTQSDLIAAL 131
CBS_pair_inorgPPase cd04597
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with ...
 80-121 9.51e-05

Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with family II inorganic pyrophosphatase; This cd contains two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with a subgroup of family II inorganic pyrophosphatases (PPases) that also contain a DRTGG domain. The homolog from Clostridium has been shown to be inhibited by AMP and activated by a novel effector, diadenosine 5',5-P1,P4-tetraphosphate (AP(4)A), which has been shown to bind to the CBS domain. The CBS domain, named after human CBS, is a small domain originally identified in cystathionine beta-synthase and is subsequently found in a wide range of different proteins. CBS domains usually occur in tandem repeats. They associate to form a so-called Bateman domain or a CBS pair based on crystallographic studies in bacteria. The CBS pair was used as a basis for this cd hierarchy since the human CBS proteins can adopt the typical core structure and form an intramolecular CBS pair. The interface between the two CBS domains forms a cleft that is a potential ligand binding site. The CBS pair coexists with a variety of other functional domains and this has been used to help in its classification here.


Pssm-ID: 341372 [Multi-domain]  Cd Length: 106  Bit Score: 38.87  E-value: 9.51e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 1705233313  80 VTFCRPEDWLHDIWGIMKERQLKNVPITDDASRPIGILNARD 121
Cdd:cd04597     7 VEPLSPETSIKDAWNLMDENNLKTLPVTDDNGKLIGLLSISD 48
CBS_pair_AcuB_like cd04584
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with the ...
 17-126 1.35e-04

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: 38.94  E-value: 1.35e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1705233313  17 VNQDAPVIEAARLLRDGR-SDLVIACDaaGHLSGVVTKSDIVAQISHCLGASCTTG---------ISAVMSRDVTFCRPE 86
Cdd:cd04584    13 VTPDTSLAEARELMKEHKiRHLPVVDD--GKLVGIVTDRDLLRASPSKATSLSIYElnyllskipVKDIMTKDVITVSPD 90

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 1705233313  87 DWLHDIWGIMKERQLKNVPITDDaSRPIGILNARDALQAL 126
Cdd:cd04584    91 DTVEEAALLMLENKIGCLPVVDG-GKLVGIITETDILRAF 129
COG3448 COG3448
CBS-domain-containing membrane protein [Signal transduction mechanisms];
9-67 2.02e-04

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


Pssm-ID: 442671 [Multi-domain]  Cd Length: 136  Bit Score: 38.69  E-value: 2.02e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1705233313   9 VARERLLIVNQDAPVIEAARLLRDGRSDLVIACDAAGHLSGVVTKSDIVAQISHCLGAS 67
Cdd:COG3448    78 VMTRPVVTVTPDTPLEEAAELMLEHGIHRLPVVDDDGRLVGIVTRTDLLRALARLLEEE 136
CBS pfam00571
CBS domain; CBS domains are small intracellular modules that pair together to form a stable ...
 6-62 2.66e-04

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: 36.81  E-value: 2.66e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1705233313   6 ITAVARERLLIVNQDAPVIEAARLLRDGRSDLVIACDAAGHLSGVVTKSDIVAQISH 62
Cdd:pfam00571   1 VKDIMTKDVVTVSPDTTLEEALELMREHGISRLPVVDEDGKLVGIVTLKDLLRALLG 57
CBS_pair_GGDEF_PAS_repeat2 cd04611
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains found in diguanylate ...
 15-132 3.12e-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: 38.09  E-value: 3.12e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1705233313  15 LIVNQDAPVIEAARLLRDGRSD-LVIACDAAGHlsGVVTKSDIVAQISHCLGascTTGISAVMSRDVTFCRPEDWLHDIW 93
Cdd:cd04611    16 LVLPGDASLAEAARRMRSHRADaAVIECPDGGL--GILTERDLVRFIARHPG---NTPVGELASRPLLTVGAEDSLIHAR 90

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 1705233313  94 GIMKERQLKNVPITDDASRPIGILNARDalqaLMQEVEQ 132
Cdd:cd04611    91 DLLIDHRIRHLAVVDEDGQVTGLLGFAD----LLAGVEH 125
CBS_pair_SF cd02205
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains superfamily; The CBS ...
 77-127 3.48e-04

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: 37.61  E-value: 3.48e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1705233313  77 SRDVTFCRPEDWLHDIWGIMKERQLKNVPITDDASRPIGILNARDALQALM 127
Cdd:cd02205     1 TRDVVTVDPDTTVREALELMAENGIGALPVVDDDGKLVGIVTERDILRALV 51
CBS_two-component_sensor_histidine_kinase_repeat2 cd17774
2 tandem repeats of the CBS domain in the two-component sensor histidine kinase and ...
 20-126 5.22e-04

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: 37.52  E-value: 5.22e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1705233313  20 DAPVIEAARLLRDGR-SDLVIA------CDAAGHLSGVVTKSDIVaQIsHCLGASC-TTGISAVMSRDVTFCRPEDWLHD 91
Cdd:cd17774    13 TASVLELAQLMAEHRvSCVVIVeedeqqEKNKLIPVGIVTERDIV-QF-QALGLDLsQTQAQTVMSSPLFSLRPDDSLWT 90

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 1705233313  92 IWGIMKERQLKNVPITDDASRPIGILNARDALQAL 126
Cdd:cd17774    91 AHQLMQQRRIRRLVVVGEQGELLGIVTQTSLLQAL 125
CBS_pair_arch2_repeat1 cd04638
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains present in archaea, ...
 45-125 6.27e-04

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


Pssm-ID: 341396 [Multi-domain]  Cd Length: 109  Bit Score: 36.94  E-value: 6.27e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1705233313  45 GHLSGVVTKSDIVAQishclgaSCTTGISAVMSRDVTFCRPEDWLHDIWGIMKERQLKNVPITDDaSRPIGILNARDALQ 124
Cdd:cd04638    37 GKLVGIVTRKDLLRN-------PDEEQIALLMSRDPITISPDDTLSEAAELMLEHNIRRVPVVDD-DKLVGIVTVADLVR 108


                  .
gi 1705233313 125 A 125
Cdd:cd04638   109 A 109
MgtE COG2239
Mg/Co/Ni transporter MgtE (contains CBS domain) [Inorganic ion transport and metabolism];
14-131 1.33e-03

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


Pssm-ID: 441840 [Multi-domain]  Cd Length: 443  Bit Score: 37.35  E-value: 1.33e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1705233313  14 LLIVNQDAPVIEAARLLRDGRSDL-------VIacDAAGHLSGVVTKSDIVAqishclgASCTTGISAVMSRDVTFCRPE 86
Cdd:COG2239   139 FVAVREDWTVGEALRYLRRQAEDPetiyyiyVV--DDDGRLVGVVSLRDLLL-------ADPDTKVSDIMDTDVISVPAD 209

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 1705233313  87 DWLHDIWGIMKERQLKNVPITDDASRPIGILNARDALQALMQEVE 131
Cdd:COG2239   210 DDQEEVARLFERYDLLALPVVDEEGRLVGIITVDDVVDVIEEEAT 254
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 ...
 15-123 1.46e-03

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: 36.01  E-value: 1.46e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1705233313  15 LIVNQDAPVIEAARLLRDGRSDLVIACDAAGHLsGVVTKSDIVAQISHcLGASCTTGISAVMSRDVTFCRPEDWLHDIWG 94
Cdd:cd04589     6 LFVDAETSIREATRLMKENGADSLLVRDGDGRV-GIVTRTDLRDAVVL-DGQPVDTPVGEIATFPLISVEPDDFLFNALL 83

                          90       100
                  ....*....|....*....|....*....
gi 1705233313  95 IMKERQLKNVPITDDAsRPIGILNARDAL 123
Cdd:cd04589    84 LMTRHRVKRVVVREGE-EIVGVLEQTDLL 111
CBS_euAMPK_gamma-like_repeat2 cd04641
CBS pair domain found in 5'-AMP (adenosine monophosphate)-activated protein kinase; The 5'-AMP ...
 17-127 4.57e-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: 34.79  E-value: 4.57e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1705233313  17 VNQDAPVIEAARLLRDGRSDLVIACDAAGHLSGVVTKSDIVAQIS----HCLGASCTtgiSAVMSRDVTF-----CRPED 87
Cdd:cd04641     8 ASMDTPVIDALNLFVERRVSALPIVDEDGRVVDIYAKFDVINLAAektyNNLDLTVG---EALQHRSEDFegvhtCTLND 84

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 1705233313  88 WLHDIWGIMKERQLKNVPITDDASRPIGILNARDALQALM 127
Cdd:cd04641    85 TLETIIDRIVKAEVHRLVVVDEEDRLEGIVSLSDILKYLV 124
COG2524 COG2524
Predicted transcriptional regulator, contains C-terminal CBS domains [Transcription];
72-131 4.72e-03

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


Pssm-ID: 442013 [Multi-domain]  Cd Length: 206  Bit Score: 35.24  E-value: 4.72e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1705233313  72 ISAVMSRDVTFCRPEDWLHDIWGIMKERQLKNVPITDDaSRPIGILNARDALQALMQEVE 131
Cdd:COG2524    88 VKDIMTKDVITVSPDTTLEEALELMLEKGISGLPVVDD-GKLVGIITERDLLKALAEGRD 146
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 ...
 76-124 5.29e-03

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: 34.22  E-value: 5.29e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 1705233313  76 MSRDVTFCRPEDWLHDIWGIMKERQLKNVPITDDASRPIGILNARDALQ 124
Cdd:cd17771     2 IRREPVTCSPDTPLRAALETMHERRVGSMVVVDANRRPVGIFTLRDLLS 50
CBS_pair_IMPDH cd04601
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains in the inosine 5' ...
 78-121 5.69e-03

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: 34.31  E-value: 5.69e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....
gi 1705233313  78 RDVTFCRPEDWLHDIWGIMKERQLKNVPITDDASRPIGILNARD 121
Cdd:cd04601     2 TDPVTLSPDATVADVLELKAEYGISGVPVTEDGGKLVGIVTSRD 45
CBS_pair_CorC_HlyC_assoc cd04590
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains the majority of which ...
 4-57 8.04e-03

Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains the majority of which are associated with the CorC_HlyC domain; This cd contains two tandem repeats of the cystathionine beta-synthase (CBS pair) domains the majority of which are associated with the CorC_HlyC domain. CorC_HlyC is a transporter associated domain. This small domain is found in Na+/H+ antiporters, in proteins involved in magnesium and cobalt efflux, and in association with some proteins of unknown function. The function of the CorC_HlyC domain is uncertain but it might be involved in modulating transport of ion substrates. These CBS domains are found in highly conserved proteins that either have unknown function or are puported to be hemolysins, exotoxins involved in lysis of red blood cells in vitro. The CBS domain, named after human CBS, is a small domain originally identified in cystathionine beta-synthase and is subsequently found in a wide range of different proteins. CBS domains usually occur in tandem repeats. They associate to form a so-called Bateman domain or a CBS pair based on crystallographic studies in bacteria. The CBS pair was used as a basis for this cd hierarchy since the human CBS proteins can adopt the typical core structure and form an intramolecular CBS pair. The interface between the two CBS domains forms a cleft that is a potential ligand binding site. The CBS pair coexists with a variety of other functional domains and this has been used to help in its classification here. It has been proposed that the CBS domain may play a regulatory role, although its exact function is unknown. Mutations of conserved residues within this domain are associated with a variety of human hereditary diseases, including congenital myotonia, idiopathic generalized epilepsy, hypercalciuric nephrolithiasis, and classic Bartter syndrome (CLC chloride channel family members), Wolff-Parkinson-White syndrome (gamma 2 subunit of AMP-activated protein kinase), retinitis pigmentosa (IMP dehydrogenase-1), and homocystinuria (cystathionine beta-synthase).


Pssm-ID: 341366 [Multi-domain]  Cd Length: 119  Bit Score: 34.01  E-value: 8.04e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1705233313   4 ENITAVARErLLIVNQDAPVIEAARLLRDGRSDLVIACDAAGHLSGVVTKSDIV 57
Cdd:cd04590    66 LDLRALLRP-PLFVPETTPLDDLLEEFRKERSHMAIVVDEYGGTAGIVTLEDIL 118
CBS smart00116
Domain in cystathionine beta-synthase and other proteins; Domain present in all 3 forms of ...
 13-60 8.22e-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: 32.48  E-value: 8.22e-03
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*...
gi 1705233313   13 RLLIVNQDAPVIEAARLLRDGRSDLVIACDAAGHLSGVVTKSDIVAQI 60
Cdd:smart00116   1 DVVTVSPDTTLEEALELLRENGIRRLPVVDEEGRLVGIVTRRDIIKAL 48
CBS_two-component_sensor_histidine_kinase_repeat1 cd04620
2 tandem repeats of the CBS domain in the two-component sensor histidine kinase and ...
 15-117 8.61e-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: 34.05  E-value: 8.61e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1705233313  15 LIVNQDAPVIEAARLL----------------RDGRSDLVIACDAAGHLsGVVTKSDIVAQISHclGASCT-TGISAVMS 77
Cdd:cd04620    10 LTVSPDTPVIEAIALMsqtrssccllsedsiiTEARSSCVLVVENQQLV-GIFTERDVVRLTAS--GIDLSgVTIAEVMT 86

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 1705233313  78 RDVTFCRPEDwLHDI---WGIMKERQLKNVPITDDASRPIGIL 117
Cdd:cd04620    87 QPVITLKESE-FQDIftvLSLLRQHQIRHLPIVDDQGQLVGLI 128
CBS_pair_HRP1_like cd04622
CBS pair domain found in Hypoxic Response Protein 1 (HRP1) -like proteinds; Mycobacterium ...
 76-121 8.92e-03

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: 33.55  E-value: 8.92e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*.
gi 1705233313  76 MSRDVTFCRPEDWLHDIWGIMKERQLKNVPITDDaSRPIGILNARD 121
Cdd:cd04622     1 MTRDVVTVSPDTTLREAARLMRDLDIGALPVCEG-DRLVGMVTDRD 45
CBS smart00116
Domain in cystathionine beta-synthase and other proteins; Domain present in all 3 forms of ...
 79-126 9.12e-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: 32.48  E-value: 9.12e-03
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*...
gi 1705233313   79 DVTFCRPEDWLHDIWGIMKERQLKNVPITDDASRPIGILNARDALQAL 126
Cdd:smart00116   1 DVVTVSPDTTLEEALELLRENGIRRLPVVDEEGRLVGIVTRRDIIKAL 48
 
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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