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Conserved domains on  [gi|1838346481|ref|WP_169405066|]
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KpsF/GutQ family sugar-phosphate isomerase [Rouxiella aceris]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
gutQ super family cl32701
arabinose-5-phosphate isomerase GutQ;
1-320 4.26e-157

arabinose-5-phosphate isomerase GutQ;


The actual alignment was detected with superfamily member PRK11543:

Pssm-ID: 183186 [Multi-domain]  Cd Length: 321  Bit Score: 441.90  E-value: 4.26e-157
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838346481   1 MQELLLTAARETIETELREAANLAERLNNDFIQACLLIQACRGKVIVSGIGKSGHIGRKIAATLASTGTPAFYVHPAEAL 80
Cdd:PRK11543    1 MSEALLNAGRQTLMLELQEASRLPERLGDDFVRAANIILHCEGKVVVSGIGKSGHIGKKIAATLASTGTPAFFVHPAEAL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838346481  81 HGDLGMITAGDVVILISSSGHAAEFRLIVPLLKALPVGIIAFTGNPHSPLGEAADYCINIHANKEACPLGLAPTSSAVNT 160
Cdd:PRK11543   81 HGDLGMIESRDVMLFISYSGGAKELDLIIPRLEDKSIALLAMTGKPTSPLGLAAKAVLDISVEREACPMHLAPTSSTVNT 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838346481 161 LIMGDAMAVALMRARNFSEHDFARSHPAGSLGTRLLCRVGDIMRNAEKIPCVSDRATVTDALFELTRTGLGLVAITNADN 240
Cdd:PRK11543  161 LMMGDALAMAVMQARGFNEEDFARSHPAGALGARLLNKVHHLMRRDDAIPQVALTASVMDAMLELSRTGLGLVAVCDAQQ 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838346481 241 KLKGVFTDGDLRRWLMKGGVITAAVQDAMTVPGFTLSAGQLAAEAQALFQQYKISAAPVVTEDGTLSGAINAHDIREAGI 320
Cdd:PRK11543  241 QVQGVFTDGDLRRWLVGGGALTTPVNEAMTRGGTTLQAQSRAIDAKEILMKRKITAAPVVDENGKLTGAINLQDFYQAGI 320
 
Name Accession Description Interval E-value
gutQ PRK11543
arabinose-5-phosphate isomerase GutQ;
1-320 4.26e-157

arabinose-5-phosphate isomerase GutQ;


Pssm-ID: 183186 [Multi-domain]  Cd Length: 321  Bit Score: 441.90  E-value: 4.26e-157
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838346481   1 MQELLLTAARETIETELREAANLAERLNNDFIQACLLIQACRGKVIVSGIGKSGHIGRKIAATLASTGTPAFYVHPAEAL 80
Cdd:PRK11543    1 MSEALLNAGRQTLMLELQEASRLPERLGDDFVRAANIILHCEGKVVVSGIGKSGHIGKKIAATLASTGTPAFFVHPAEAL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838346481  81 HGDLGMITAGDVVILISSSGHAAEFRLIVPLLKALPVGIIAFTGNPHSPLGEAADYCINIHANKEACPLGLAPTSSAVNT 160
Cdd:PRK11543   81 HGDLGMIESRDVMLFISYSGGAKELDLIIPRLEDKSIALLAMTGKPTSPLGLAAKAVLDISVEREACPMHLAPTSSTVNT 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838346481 161 LIMGDAMAVALMRARNFSEHDFARSHPAGSLGTRLLCRVGDIMRNAEKIPCVSDRATVTDALFELTRTGLGLVAITNADN 240
Cdd:PRK11543  161 LMMGDALAMAVMQARGFNEEDFARSHPAGALGARLLNKVHHLMRRDDAIPQVALTASVMDAMLELSRTGLGLVAVCDAQQ 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838346481 241 KLKGVFTDGDLRRWLMKGGVITAAVQDAMTVPGFTLSAGQLAAEAQALFQQYKISAAPVVTEDGTLSGAINAHDIREAGI 320
Cdd:PRK11543  241 QVQGVFTDGDLRRWLVGGGALTTPVNEAMTRGGTTLQAQSRAIDAKEILMKRKITAAPVVDENGKLTGAINLQDFYQAGI 320
GutQ COG0794
D-arabinose 5-phosphate isomerase GutQ [Carbohydrate transport and metabolism, Cell wall ...
 5-315 1.03e-126

D-arabinose 5-phosphate isomerase GutQ [Carbohydrate transport and metabolism, Cell wall/membrane/envelope biogenesis];


Pssm-ID: 440557 [Multi-domain]  Cd Length: 317  Bit Score: 364.68  E-value: 1.03e-126
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838346481   5 LLTAARETIETELREAANLAERLNNDFIQACLLIQACRGKVIVSGIGKSGHIGRKIAATLASTGTPAFYVHPAEALHGDL 84
Cdd:COG0794     7 ILESAREVLEIEAEALAALAERLDESFEKAVELILNCKGRVVVTGMGKSGHIARKIAATLASTGTPAFFLHPAEASHGDL 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838346481  85 GMITAGDVVILISSSGHAAEFRLIVPLLKALPVGIIAFTGNPHSPLGEAADYCINIHANKEACPLGLAPTSSAVNTLIMG 164
Cdd:COG0794    87 GMITPGDVVIAISNSGETEELLALLPLLKRLGVPLIAITGNPDSTLARAADVVLDLPVEREACPLNLAPTTSTTATLALG 166

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838346481 165 DAMAVALMRARNFSEHDFARSHPAGSLGTRLLCRVGDIMRNAEKIPCVSDRATVTDALFELTRTGLGLVAITNADNKLKG 244
Cdd:COG0794   167 DALAVALLEARGFTAEDFARFHPGGSLGRRLLLRVSDLMMPGVEPPVVVPDALLEEALKELGMTGVGGGAVVDDGGGLDG 246

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1838346481 245 VFTDGDLRRWLMKGGVITAAVQDAMTVPGFTLSAGQLAAEAQALFQQYKISAAPVVTEDGTLSGAINAHDI 315
Cdd:COG0794   247 DLTDGDLRRRLLDDLDLTDVMTTTMTTPTTPPLAAAAAAAAAALLIEEIIVVVVVVVVVGVLVGGLLLLLL 317
kpsF TIGR00393
KpsF/GutQ family protein; This model describes a number of closely related proteins with the ...
 43-311 1.78e-123

KpsF/GutQ family protein; This model describes a number of closely related proteins with the phosphosugar-binding domain SIS (Sugar ISomerase) followed by two copies of the CBS (named after Cystathionine Beta Synthase) domain. One is GutQ, a protein of the glucitol operon. Another is KpsF, a virulence factor involved in capsular polysialic acid biosynthesis in some pathogenic strains of E. coli. [Energy metabolism, Sugars]


Pssm-ID: 129488 [Multi-domain]  Cd Length: 268  Bit Score: 354.50  E-value: 1.78e-123
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838346481  43 GKVIVSGIGKSGHIGRKIAATLASTGTPAFYVHPAEALHGDLGMITAGDVVILISSSGHAAEFRLIVPLLKALPVGIIAF 122
Cdd:TIGR00393   1 GKLVIVGIGKSGLIGKKIVATFASTGTPSFFLHPTEAMHGDLGMVEPNDVVLMISYSGESLELLNLIPHLKRLSHKIIAF 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838346481 123 TGNPHSPLGEAADYCINIHANKEACPLGLAPTSSAVNTLIMGDAMAVALMRARNFSEHDFARSHPAGSLGTRLLCRVGDI 202
Cdd:TIGR00393  81 TGSPNSSLARAADYVLDIKVEKEACPINLAPTTSTTLTLALGDALAVALMRARNFSQEDFASFHPGGALGRKLLVKVKDL 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838346481 203 MRNAEkIPCVSDRATVTDALFELTRTGLGLVAITNADNKLKGVFTDGDLRRWLMKGGVITAAVQDAMTVPGFTLSAGQLA 282
Cdd:TIGR00393 161 MQTTD-LPLIAPTTSFKDALLEMSEKRLGSAIVCDENNQLVGVFTDGDLRRALLGGGSLKSEVRDFMTLGPKTFKLDALL 239

                         250       260
                  ....*....|....*....|....*....
gi 1838346481 283 AEAQALFQQYKISAAPVVTEDGTLSGAIN 311
Cdd:TIGR00393 240 LEALEFLERRKITSLVVVDDHNKVLGVLH 268
SIS_Kpsf cd05014
KpsF-like protein. KpsF is an arabinose-5-phosphate isomerase which contains SIS (Sugar ...
 43-170 9.21e-65

KpsF-like protein. KpsF is an arabinose-5-phosphate isomerase which contains SIS (Sugar ISomerase) domains. SIS domains are found in many phosphosugar isomerases and phosphosugar binding proteins. KpsF catalyzes the reversible reaction of ribulose 5-phosphate to arabinose 5-phosphate. This is the second step in the CMP-Kdo biosynthesis pathway.


Pssm-ID: 240145 [Multi-domain]  Cd Length: 128  Bit Score: 200.08  E-value: 9.21e-65
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838346481  43 GKVIVSGIGKSGHIGRKIAATLASTGTPAFYVHPAEALHGDLGMITAGDVVILISSSGHAAEFRLIVPLLKALPVGIIAF 122
Cdd:cd05014     1 GKVVVTGVGKSGHIARKIAATLSSTGTPAFFLHPTEALHGDLGMVTPGDVVIAISNSGETDELLNLLPHLKRRGAPIIAI 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 1838346481 123 TGNPHSPLGEAADYCINIHANKEACPLGLAPTSSAVNTLIMGDAMAVA 170
Cdd:cd05014    81 TGNPNSTLAKLSDVVLDLPVEEEACPLGLAPTTSTTAMLALGDALAVA 128
SIS pfam01380
SIS domain; SIS (Sugar ISomerase) domains are found in many phosphosugar isomerases and ...
 40-170 1.11e-28

SIS domain; SIS (Sugar ISomerase) domains are found in many phosphosugar isomerases and phosphosugar binding proteins. SIS domains are also found in proteins that regulate the expression of genes involved in synthesis of phosphosugars. Presumably the SIS domains bind to the end-product of the pathway.


Pssm-ID: 426230 [Multi-domain]  Cd Length: 131  Bit Score: 107.38  E-value: 1.11e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838346481  40 ACRGKVIVSGIGKSGHIGRKIAATLASTGTPAFYVHPAEAL-HGDLGMITAGDVVILISSSGHAAEFRLIVPLLKALPVG 118
Cdd:pfam01380   3 AKAKRIFVIGRGTSYAIALELALKFEEIGYKVVEVELASELrHGVLALVDEDDLVIAISYSGETKDLLAAAELAKARGAK 82

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1838346481 119 IIAFTGNPHSPLGEAADYCINIHANKEAcplGLAPTSSAVNTLIMGDAMAVA 170
Cdd:pfam01380  83 IIAITDSPGSPLAREADHVLYINAGPET---GVASTKSITAQLAALDALAVA 131
CBS smart00116
Domain in cystathionine beta-synthase and other proteins; Domain present in all 3 forms of ...
 209-251 4.40e-04

Domain in cystathionine beta-synthase and other proteins; Domain present in all 3 forms of cellular life. Present in two copies in inosine monophosphate dehydrogenase, of which one is disordered in the crystal structure. A number of disease states are associated with CBS-containing proteins including homocystinuria, Becker's and Thomsen disease.


Pssm-ID: 214522 [Multi-domain]  Cd Length: 49  Bit Score: 37.49  E-value: 4.40e-04
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|...
gi 1838346481  209 IPCVSDRATVTDALFELTRTGLGLVAITNADNKLKGVFTDGDL 251
Cdd:smart00116   2 VVTVSPDTTLEEALELLRENGIRRLPVVDEEGRLVGIVTRRDI 44
 
Name Accession Description Interval E-value
gutQ PRK11543
arabinose-5-phosphate isomerase GutQ;
1-320 4.26e-157

arabinose-5-phosphate isomerase GutQ;


Pssm-ID: 183186 [Multi-domain]  Cd Length: 321  Bit Score: 441.90  E-value: 4.26e-157
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838346481   1 MQELLLTAARETIETELREAANLAERLNNDFIQACLLIQACRGKVIVSGIGKSGHIGRKIAATLASTGTPAFYVHPAEAL 80
Cdd:PRK11543    1 MSEALLNAGRQTLMLELQEASRLPERLGDDFVRAANIILHCEGKVVVSGIGKSGHIGKKIAATLASTGTPAFFVHPAEAL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838346481  81 HGDLGMITAGDVVILISSSGHAAEFRLIVPLLKALPVGIIAFTGNPHSPLGEAADYCINIHANKEACPLGLAPTSSAVNT 160
Cdd:PRK11543   81 HGDLGMIESRDVMLFISYSGGAKELDLIIPRLEDKSIALLAMTGKPTSPLGLAAKAVLDISVEREACPMHLAPTSSTVNT 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838346481 161 LIMGDAMAVALMRARNFSEHDFARSHPAGSLGTRLLCRVGDIMRNAEKIPCVSDRATVTDALFELTRTGLGLVAITNADN 240
Cdd:PRK11543  161 LMMGDALAMAVMQARGFNEEDFARSHPAGALGARLLNKVHHLMRRDDAIPQVALTASVMDAMLELSRTGLGLVAVCDAQQ 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838346481 241 KLKGVFTDGDLRRWLMKGGVITAAVQDAMTVPGFTLSAGQLAAEAQALFQQYKISAAPVVTEDGTLSGAINAHDIREAGI 320
Cdd:PRK11543  241 QVQGVFTDGDLRRWLVGGGALTTPVNEAMTRGGTTLQAQSRAIDAKEILMKRKITAAPVVDENGKLTGAINLQDFYQAGI 320
GutQ COG0794
D-arabinose 5-phosphate isomerase GutQ [Carbohydrate transport and metabolism, Cell wall ...
 5-315 1.03e-126

D-arabinose 5-phosphate isomerase GutQ [Carbohydrate transport and metabolism, Cell wall/membrane/envelope biogenesis];


Pssm-ID: 440557 [Multi-domain]  Cd Length: 317  Bit Score: 364.68  E-value: 1.03e-126
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838346481   5 LLTAARETIETELREAANLAERLNNDFIQACLLIQACRGKVIVSGIGKSGHIGRKIAATLASTGTPAFYVHPAEALHGDL 84
Cdd:COG0794     7 ILESAREVLEIEAEALAALAERLDESFEKAVELILNCKGRVVVTGMGKSGHIARKIAATLASTGTPAFFLHPAEASHGDL 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838346481  85 GMITAGDVVILISSSGHAAEFRLIVPLLKALPVGIIAFTGNPHSPLGEAADYCINIHANKEACPLGLAPTSSAVNTLIMG 164
Cdd:COG0794    87 GMITPGDVVIAISNSGETEELLALLPLLKRLGVPLIAITGNPDSTLARAADVVLDLPVEREACPLNLAPTTSTTATLALG 166

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838346481 165 DAMAVALMRARNFSEHDFARSHPAGSLGTRLLCRVGDIMRNAEKIPCVSDRATVTDALFELTRTGLGLVAITNADNKLKG 244
Cdd:COG0794   167 DALAVALLEARGFTAEDFARFHPGGSLGRRLLLRVSDLMMPGVEPPVVVPDALLEEALKELGMTGVGGGAVVDDGGGLDG 246

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1838346481 245 VFTDGDLRRWLMKGGVITAAVQDAMTVPGFTLSAGQLAAEAQALFQQYKISAAPVVTEDGTLSGAINAHDI 315
Cdd:COG0794   247 DLTDGDLRRRLLDDLDLTDVMTTTMTTPTTPPLAAAAAAAAAALLIEEIIVVVVVVVVVGVLVGGLLLLLL 317
kpsF TIGR00393
KpsF/GutQ family protein; This model describes a number of closely related proteins with the ...
 43-311 1.78e-123

KpsF/GutQ family protein; This model describes a number of closely related proteins with the phosphosugar-binding domain SIS (Sugar ISomerase) followed by two copies of the CBS (named after Cystathionine Beta Synthase) domain. One is GutQ, a protein of the glucitol operon. Another is KpsF, a virulence factor involved in capsular polysialic acid biosynthesis in some pathogenic strains of E. coli. [Energy metabolism, Sugars]


Pssm-ID: 129488 [Multi-domain]  Cd Length: 268  Bit Score: 354.50  E-value: 1.78e-123
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838346481  43 GKVIVSGIGKSGHIGRKIAATLASTGTPAFYVHPAEALHGDLGMITAGDVVILISSSGHAAEFRLIVPLLKALPVGIIAF 122
Cdd:TIGR00393   1 GKLVIVGIGKSGLIGKKIVATFASTGTPSFFLHPTEAMHGDLGMVEPNDVVLMISYSGESLELLNLIPHLKRLSHKIIAF 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838346481 123 TGNPHSPLGEAADYCINIHANKEACPLGLAPTSSAVNTLIMGDAMAVALMRARNFSEHDFARSHPAGSLGTRLLCRVGDI 202
Cdd:TIGR00393  81 TGSPNSSLARAADYVLDIKVEKEACPINLAPTTSTTLTLALGDALAVALMRARNFSQEDFASFHPGGALGRKLLVKVKDL 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838346481 203 MRNAEkIPCVSDRATVTDALFELTRTGLGLVAITNADNKLKGVFTDGDLRRWLMKGGVITAAVQDAMTVPGFTLSAGQLA 282
Cdd:TIGR00393 161 MQTTD-LPLIAPTTSFKDALLEMSEKRLGSAIVCDENNQLVGVFTDGDLRRALLGGGSLKSEVRDFMTLGPKTFKLDALL 239

                         250       260
                  ....*....|....*....|....*....
gi 1838346481 283 AEAQALFQQYKISAAPVVTEDGTLSGAIN 311
Cdd:TIGR00393 240 LEALEFLERRKITSLVVVDDHNKVLGVLH 268
PRK10892 PRK10892
arabinose-5-phosphate isomerase KdsD;
8-320 5.81e-118

arabinose-5-phosphate isomerase KdsD;


Pssm-ID: 182814 [Multi-domain]  Cd Length: 326  Bit Score: 342.86  E-value: 5.81e-118
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838346481   8 AARETIETELREAANLAERLNNDFIQACLLIQACRGKVIVSGIGKSGHIGRKIAATLASTGTPAFYVHPAEALHGDLGMI 87
Cdd:PRK10892   13 AGKEVLAIEREGLAELDQYINQDFTLACEKMFWCKGKVVVMGMGKSGHIGRKMAATFASTGTPSFFVHPGEAAHGDLGMV 92

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838346481  88 TAGDVVILISSSGHAAEFRLIVPLLKALPVGIIAFTGNPHSPLGEAADYCINIHANKEACPLGLAPTSSAVNTLIMGDAM 167
Cdd:PRK10892   93 TPQDVVIAISNSGESSEILALIPVLKRLHVPLICITGRPESSMARAADIHLCVKVPKEACPLGLAPTSSTTATLVMGDAL 172

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838346481 168 AVALMRARNFSEHDFARSHPAGSLGTRLLCRVGDIMRNAEKIPCVSDRATVTDALFELTRTGLGLVAITNADNKLKGVFT 247
Cdd:PRK10892  173 AVALLKARGFTAEDFALSHPGGALGRKLLLRVSDIMHTGDEIPHVSKTASLRDALLEITRKNLGMTVICDDNMKIEGIFT 252

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1838346481 248 DGDLRRWL-MKGGVITAAVQDAMTVPGFTLSAGQLAAEAQALFQQYKISAApVVTEDGTLSGAINAHDIREAGI 320
Cdd:PRK10892  253 DGDLRRVFdMGIDLRQASIADVMTPGGIRVRPGILAVDALNLMQSRHITSV-LVADGDHLLGVLHMHDLLRAGV 325
SIS_Kpsf cd05014
KpsF-like protein. KpsF is an arabinose-5-phosphate isomerase which contains SIS (Sugar ...
 43-170 9.21e-65

KpsF-like protein. KpsF is an arabinose-5-phosphate isomerase which contains SIS (Sugar ISomerase) domains. SIS domains are found in many phosphosugar isomerases and phosphosugar binding proteins. KpsF catalyzes the reversible reaction of ribulose 5-phosphate to arabinose 5-phosphate. This is the second step in the CMP-Kdo biosynthesis pathway.


Pssm-ID: 240145 [Multi-domain]  Cd Length: 128  Bit Score: 200.08  E-value: 9.21e-65
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838346481  43 GKVIVSGIGKSGHIGRKIAATLASTGTPAFYVHPAEALHGDLGMITAGDVVILISSSGHAAEFRLIVPLLKALPVGIIAF 122
Cdd:cd05014     1 GKVVVTGVGKSGHIARKIAATLSSTGTPAFFLHPTEALHGDLGMVTPGDVVIAISNSGETDELLNLLPHLKRRGAPIIAI 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 1838346481 123 TGNPHSPLGEAADYCINIHANKEACPLGLAPTSSAVNTLIMGDAMAVA 170
Cdd:cd05014    81 TGNPNSTLAKLSDVVLDLPVEEEACPLGLAPTTSTTAMLALGDALAVA 128
CBS_pair_SIS_assoc cd04604
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with the ...
 195-315 1.05e-43

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: 145.99  E-value: 1.05e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838346481 195 LLCRVGDIMRNAEKIPCVSDRATVTDALFELTRTGLGLVAITNADNKLKGVFTDGDLRRWLMKGGVITAA-VQDAMTVPG 273
Cdd:cd04604     1 LLLRVSDLMHTGDELPLVSPDTSLKEALLEMTRKGLGCTAVVDEDGRLVGIITDGDLRRALEKGLDILNLpAKDVMTRNP 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 1838346481 274 FTLSAGQLAAEAQALFQQYKISAAPVVTEDGTLSGAINAHDI 315
Cdd:cd04604    81 KTISPDALAAEALELMEEHKITVLPVVDEDGKPVGILHLHDL 122
SIS pfam01380
SIS domain; SIS (Sugar ISomerase) domains are found in many phosphosugar isomerases and ...
 40-170 1.11e-28

SIS domain; SIS (Sugar ISomerase) domains are found in many phosphosugar isomerases and phosphosugar binding proteins. SIS domains are also found in proteins that regulate the expression of genes involved in synthesis of phosphosugars. Presumably the SIS domains bind to the end-product of the pathway.


Pssm-ID: 426230 [Multi-domain]  Cd Length: 131  Bit Score: 107.38  E-value: 1.11e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838346481  40 ACRGKVIVSGIGKSGHIGRKIAATLASTGTPAFYVHPAEAL-HGDLGMITAGDVVILISSSGHAAEFRLIVPLLKALPVG 118
Cdd:pfam01380   3 AKAKRIFVIGRGTSYAIALELALKFEEIGYKVVEVELASELrHGVLALVDEDDLVIAISYSGETKDLLAAAELAKARGAK 82

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1838346481 119 IIAFTGNPHSPLGEAADYCINIHANKEAcplGLAPTSSAVNTLIMGDAMAVA 170
Cdd:pfam01380  83 IIAITDSPGSPLAREADHVLYINAGPET---GVASTKSITAQLAALDALAVA 131
CBS COG0517
CBS domain [Signal transduction mechanisms];
198-320 8.45e-28

CBS domain [Signal transduction mechanisms];


Pssm-ID: 440283 [Multi-domain]  Cd Length: 128  Bit Score: 104.95  E-value: 8.45e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838346481 198 RVGDIMRNaeKIPCVSDRATVTDALFELTRTGLGLVAITNADNKLKGVFTDGDLRRWLMKGGVITAA--VQDAMTVPGFT 275
Cdd:COG0517     2 KVKDIMTT--DVVTVSPDATVREALELMSEKRIGGLPVVDEDGKLVGIVTDRDLRRALAAEGKDLLDtpVSEVMTRPPVT 79

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 1838346481 276 LSAGQLAAEAQALFQQYKISAAPVVTEDGTLSGAINAHDIREAGI 320
Cdd:COG0517    80 VSPDTSLEEAAELMEEHKIRRLPVVDDDGRLVGIITIKDLLKALL 124
COG2905 COG2905
Signal-transduction protein containing cAMP-binding, CBS, and nucleotidyltransferase domains ...
 199-315 1.60e-25

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


Pssm-ID: 442149 [Multi-domain]  Cd Length: 124  Bit Score: 98.75  E-value: 1.60e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838346481 199 VGDIMRnaEKIPCVSDRATVTDALFELTRTGLGLVAITNADNKLKGVFTDGDLRRWLMKGG--VITAAVQDAMTVPGFTL 276
Cdd:COG2905     1 VKDIMS--RDVVTVSPDATVREAARLMTEKGVGSLVVVDDDGRLVGIITDRDLRRRVLAEGldPLDTPVSEVMTRPPITV 78

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 1838346481 277 SAGQLAAEAQALFQQYKISAAPVVtEDGTLSGAINAHDI 315
Cdd:COG2905    79 SPDDSLAEALELMEEHRIRHLPVV-DDGKLVGIVSITDL 116
CBS_pair_SF cd02205
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains superfamily; The CBS ...
 207-315 5.35e-18

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: 78.06  E-value: 5.35e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838346481 207 EKIPCVSDRATVTDALFELTRTGLGLVAITNADNKLKGVFTDGDLRRWLMKGGVI-TAAVQDAMTVPGFTLSAGQLAAEA 285
Cdd:cd02205     2 RDVVTVDPDTTVREALELMAENGIGALPVVDDDGKLVGIVTERDILRALVEGGLAlDTPVAEVMTPDVITVSPDTDLEEA 81

                          90       100       110
                  ....*....|....*....|....*....|
gi 1838346481 286 QALFQQYKISAAPVVTEDGTLSGAINAHDI 315
Cdd:cd02205    82 LELMLEHGIRRLPVVDDDGKLVGIVTRRDI 111
COG2524 COG2524
Predicted transcriptional regulator, contains C-terminal CBS domains [Transcription];
119-318 2.34e-17

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


Pssm-ID: 442013 [Multi-domain]  Cd Length: 206  Bit Score: 79.16  E-value: 2.34e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838346481 119 IIAFTGNPHSPLGEAADYCINIHANKEACPLGLAPTSSAVNTLIMGDAMAVALMRARNFSEHDF-------ARSHPAGSL 191
Cdd:COG2524     1 LLVLLLLALSLLLPLLAVVLAALLLLAALVLALTAAAAATVLLLAAAAAAAGAGGLGLLLLLLLivlqaaaVRVVAEKEL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838346481 192 GTRLLCRVGDIMRnaEKIPCVSDRATVTDALFELTRTGLGLVAITNaDNKLKGVFTDGDLRRWLMKGGVITAA-VQDAMT 270
Cdd:COG2524    81 GLVLKMKVKDIMT--KDVITVSPDTTLEEALELMLEKGISGLPVVD-DGKLVGIITERDLLKALAEGRDLLDApVSDIMT 157

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 1838346481 271 VPGFTLSAGQLAAEAQALFQQYKISAAPVVTEDGTLSGAINAHDIREA 318
Cdd:COG2524   158 RDVVTVSEDDSLEEALRLMLEHGIGRLPVVDDDGKLVGIITRTDILRA 205
SIS_PHI cd05005
Hexulose-6-phosphate isomerase (PHI). PHI is a member of the SIS (Sugar ISomerase domain) ...
 11-186 1.28e-15

Hexulose-6-phosphate isomerase (PHI). PHI is a member of the SIS (Sugar ISomerase domain) superfamily. In the ribulose monophosphate pathway of formaldehyde fixation, hexulose-6-phosphate synthase catalyzes the condensation of ribulose-5-phosphate with formadelhyde to become hexulose-6-phosphate, which is then isomerized to fructose-6-phosphate by PHI.


Pssm-ID: 240138 [Multi-domain]  Cd Length: 179  Bit Score: 73.38  E-value: 1.28e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838346481  11 ETIETELREAANLAERLNND----FIQAclLIQAcrGKVIVSGIGKSGHIGRKIAATLASTGTPAFYV----HPAealhg 82
Cdd:cd05005     2 EYLSLILEEIENVADKIDEEeldkLISA--ILNA--KRIFVYGAGRSGLVAKAFAMRLMHLGLNVYVVgettTPA----- 72

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838346481  83 dlgmITAGDVVILISSSGhaaEFRLIVPLL-KALPVG--IIAFTGNPHSPLGEAADYCINIHANKEACPLG----LAPTS 155
Cdd:cd05005    73 ----IGPGDLLIAISGSG---ETSSVVNAAeKAKKAGakVVLITSNPDSPLAKLADVVVVIPAATKDDHGGehksIQPLG 145

                         170       180       190
                  ....*....|....*....|....*....|...
gi 1838346481 156 SA--VNTLIMGDAMAVALMRARNFSEHDFARSH 186
Cdd:cd05005   146 TLfeQSALVFLDAVIAKLMEELGVSEEEMKKRH 178
RpiR COG1737
DNA-binding transcriptional regulator, MurR/RpiR family, contains HTH and SIS domains ...
 7-175 1.41e-14

DNA-binding transcriptional regulator, MurR/RpiR family, contains HTH and SIS domains [Transcription];


Pssm-ID: 441343 [Multi-domain]  Cd Length: 286  Bit Score: 72.65  E-value: 1.41e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838346481   7 TAARETIETELREAANLAERLNND-FIQACLLIQACRgKVIVSGIGKSGHIGRKIAATLASTGTPAFYV-HPAEALHGDL 84
Cdd:COG1737    99 DILAKVLEAEIANLEETLELLDEEaLERAVDLLAKAR-RIYIFGVGASAPVAEDLAYKLLRLGKNVVLLdGDGHLQAESA 177

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838346481  85 GMITAGDVVILISSSGHAAEFRLIVPLLKALPVGIIAFTGNPHSPLGEAADYCINIHANKEacPLGLAPTSSAVNTLIMG 164
Cdd:COG1737   178 ALLGPGDVVIAISFSGYTRETLEAARLAKERGAKVIAITDSPLSPLAKLADVVLYVPSEEP--TLRSSAFSSRVAQLALI 255

                         170
                  ....*....|.
gi 1838346481 165 DAMAVALMRAR 175
Cdd:COG1737   256 DALAAAVAQRD 266
SIS_RpiR cd05013
RpiR-like protein. RpiR contains a SIS (Sugar ISomerase) domain, which is found in many ...
 29-170 3.52e-14

RpiR-like protein. RpiR contains a SIS (Sugar ISomerase) domain, which is found in many phosphosugar isomerases and phosphosugar binding proteins. In E. coli, rpiR negatively regulates the expression of rpiB gene. Both rpiB and rpiA are ribose phosphate isomerases that catalyze the reversible reactions of ribose 5-phosphate into ribulose 5-phosphate.


Pssm-ID: 240144 [Multi-domain]  Cd Length: 139  Bit Score: 68.41  E-value: 3.52e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838346481  29 NDFIQACLLIQACRgKVIVSGIGKSGHIGRKIAATLASTGTPAFYVHPAEALHGDLGMITAGDVVILISSSGHAAEFRLI 108
Cdd:cd05013     1 EALEKAVDLLAKAR-RIYIFGVGSSGLVAEYLAYKLLRLGKPVVLLSDPHLQLMSAANLTPGDVVIAISFSGETKETVEA 79

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1838346481 109 VPLLKALPVGIIAFTGNPHSPLGEAADYCINIHANKEacPLGLAPTSSAVNTLIMGDAMAVA 170
Cdd:cd05013    80 AEIAKERGAKVIAITDSANSPLAKLADIVLLVSSEEG--DFRSSAFSSRIAQLALIDALFLA 139
COG3448 COG3448
CBS-domain-containing membrane protein [Signal transduction mechanisms];
198-315 7.29e-14

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


Pssm-ID: 442671 [Multi-domain]  Cd Length: 136  Bit Score: 67.58  E-value: 7.29e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838346481 198 RVGDIMRnaEKIPCVSDRATVTDALFELTRTGLGLVAITNADNKLKGVFTDGDLRRWLMKGGVITAA-------VQDAMT 270
Cdd:COG3448     3 TVRDIMT--RDVVTVSPDTTLREALELMREHGIRGLPVVDEDGRLVGIVTERDLLRALLPDRLDELEerlldlpVEDVMT 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 1838346481 271 VPGFTLSAGQLAAEAQALFQQYKISAAPVVTEDGTLSGAINAHDI 315
Cdd:COG3448    81 RPVVTVTPDTPLEEAAELMLEHGIHRLPVVDDDGRLVGIVTRTDL 125
CBS_pair_NTP_transferase_assoc cd04607
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domain associated with the ...
 205-315 7.36e-14

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: 66.70  E-value: 7.36e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838346481 205 NAEKIpCVSDRATVTDALFELTRTGLGLVAITNADNKLKGVFTDGDLRRWLMKGGVITAAVQDAM-TVPgFTLSAGQLAA 283
Cdd:cd04607     1 NWKKV-LVSPDTTIREAIEVIDKGALQIALVVDENRKLLGTVTDGDIRRGLLKGLSLDAPVEEVMnKNP-ITASPSTSRE 78

                          90       100       110
                  ....*....|....*....|....*....|..
gi 1838346481 284 EAQALFQQYKISAAPVVTEDGTLSGAINAHDI 315
Cdd:cd04607    79 ELLALMRAKKILQLPIVDEQGRVVGLETLDDL 110
AgaS COG2222
Fructoselysine-6-P-deglycase FrlB or related protein, duplicated sugar isomerase (SIS) domain ...
 8-179 3.38e-13

Fructoselysine-6-P-deglycase FrlB or related protein, duplicated sugar isomerase (SIS) domain [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 441824 [Multi-domain]  Cd Length: 336  Bit Score: 69.16  E-value: 3.38e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838346481   8 AARETIETELREAANLAERLNNDFiqaclliqacRGKVIVSGIGKSGHIGRKIAATLAS-TGTPAFYVHPAEALHGDLGM 86
Cdd:COG2222    10 AWRRALAALAAAIAALLARLRAKP----------PRRVVLVGAGSSDHAAQAAAYLLERlLGIPVAALAPSELVVYPAYL 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838346481  87 ITAGDVVILISSSGHAAEFRLIVPLLKALPVGIIAFTGNPHSPLGEAADYCINIHANKEacpLGLAPTSSAVNTLimgdA 166
Cdd:COG2222    80 KLEGTLVVAISRSGNSPEVVAALELAKARGARTLAITNNPDSPLAEAADRVLPLPAGPE---KSVAATKSFTTML----L 152

                         170
                  ....*....|...
gi 1838346481 167 MAVALMRARNFSE 179
Cdd:COG2222   153 ALLALLAAWGGDD 165
YtoI COG4109
Predicted transcriptional regulator containing CBS domains [Transcription];
198-315 1.51e-11

Predicted transcriptional regulator containing CBS domains [Transcription];


Pssm-ID: 443285 [Multi-domain]  Cd Length: 135  Bit Score: 61.08  E-value: 1.51e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838346481 198 RVGDIMRNaEKIPCVSDRATVTDALFELTRTGLGLVAITNADNKLKGVFTDGDLRRWLMkggviTAAVQDAMTVPGFTLS 277
Cdd:COG4109    17 LVEDIMTL-EDVATLSEDDTVEDALELLEKTGHSRFPVVDENGRLVGIVTSKDILGKDD-----DTPIEDVMTKNPITVT 90

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 1838346481 278 AGQLAAEAQALFQQYKISAAPVVTEDGTLSGAINAHDI 315
Cdd:COG4109    91 PDTSLASAAHKMIWEGIELLPVVDDDGRLLGIISRQDV 128
CBS_pair_arch cd09836
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains; The CBS domain, ...
 211-315 3.35e-08

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: 50.98  E-value: 3.35e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838346481 211 CVSDRATVTDALFELTRTGLGLVAITNADNKLKGVFTDGDLRRWLMKGGVITAAVQDAMTVPGFTLSAGQLAAEAQALFQ 290
Cdd:cd09836     7 TVPPETTIREAAKLMAENNIGSVVVVDDDGKPVGIVTERDIVRAVAEGIDLDTPVEEIMTKNLVTVSPDESIYEAAELMR 86

                          90       100
                  ....*....|....*....|....*
gi 1838346481 291 QYKISAAPVVTEDGTLSGAINAHDI 315
Cdd:cd09836    87 EHNIRHLPVVDGGGKLVGVISIRDL 111
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 ...
 239-315 7.43e-08

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


Pssm-ID: 341363 [Multi-domain]  Cd Length: 114  Bit Score: 50.12  E-value: 7.43e-08
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1838346481 239 DNKLKGVFTDGDLR-RWLMKGGVITAAVQDAMTVPGFTLSAGQLAAEAQALFQQYKISAAPVVtEDGTLSGAINAHDI 315
Cdd:cd04587    35 DGRLVGIVTDRDLRnRVVAEGLDPDTPVSEIMTPPPVTIDADALVFEALLLMLERNIHHLPVV-DDGRVVGVVTATDL 111
CBS_pair_AcuB_like cd04584
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with the ...
 198-315 2.05e-07

Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with the ACT domain; The putative Acetoin Utilization Protein (Acub) from Vibrio Cholerae contains a CBS pair domain. The acetoin utilization protein plays a role in growth and sporulation on acetoin or butanediol for use as a carbon source. Acetoin is an important physiological metabolite excreted by many microorganisms. It is used as an external energy store by a number of fermentive bacteria. Acetoin is produced by the decarboxylation of alpha-acetolactate. Once superior carbon sources are exhausted, and the culture enters stationary phase, acetoin can be utilised in order to maintain the culture density. The conversion of acetoin into acetyl-CoA or 2,3-butanediol is catalysed by the acetoin dehydrogenase complex and acetoin reductase/2,3-butanediol dehydrogenase, respectively. Acetoin utilization proteins, acetylpolyamine amidohydrolases, and histone deacetylases are members of an ancient protein superfamily.This cd contains two tandem repeats of the cystathionine beta-synthase (CBS pair) domains in the acetoin utilization proteins in bacteria. Acetoin is a product of fermentative metabolism in many prokaryotic and eukaryotic microorganisms. They produce acetoin as an external carbon storage compound and then later reuse it as a carbon and energy source during their stationary phase and sporulation. In addition these CBS domains are associated with a downstream ACT (aspartate kinase/chorismate mutase/TyrA) domain, which is linked to a wide range of metabolic enzymes that are regulated by amino acid concentration. Pairs of ACT domains bind specifically to a particular amino acid leading to regulation of the linked enzyme. The CBS domain, named after human CBS, is a small domain originally identified in cystathionine beta-synthase and is subsequently found in a wide range of different proteins. CBS domains usually occur in tandem repeats. They associate to form a so-called Bateman domain or a CBS pair based on crystallographic studies in bacteria. The CBS pair was used as a basis for this cd hierarchy since the human CBS proteins can adopt the typical core structure and form an intramolecular CBS pair. The interface between the two CBS domains forms a cleft that is a potential ligand binding site. The CBS pair coexists with a variety of other functional domains and this has been used to help in its classification here. It has been proposed that the CBS domain may play a regulatory role, although its exact function is unknown. Mutations of conserved residues within this domain are associated with a variety of human hereditary diseases, including congenital myotonia, idiopathic generalized epilepsy, hypercalciuric nephrolithiasis, and classic Bartter syndrome (CLC chloride channel family members), Wolff-Parkinson-White syndrome (gamma 2 subunit of AMP-activated protein kinase), retinitis pigmentosa (IMP dehydrogenase-1), and homocystinuria (cystathionine beta-synthase).


Pssm-ID: 341361 [Multi-domain]  Cd Length: 130  Bit Score: 48.96  E-value: 2.05e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838346481 198 RVGDIMRnaEKIPCVSDRATVTDALFELTRTGLGLVAITNaDNKLKGVFTDGDLRR-----------WLMKGGVITAAVQ 266
Cdd:cd04584     1 LVKDIMT--KNVVTVTPDTSLAEARELMKEHKIRHLPVVD-DGKLVGIVTDRDLLRaspskatslsiYELNYLLSKIPVK 77

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 1838346481 267 DAMTVPGFTLSAGQLAAEAQALFQQYKISAAPVVtEDGTLSGAINAHDI 315
Cdd:cd04584    78 DIMTKDVITVSPDDTVEEAALLMLENKIGCLPVV-DGGKLVGIITETDI 125
SIS_GmhA cd05006
Phosphoheptose isomerase is a member of the SIS (Sugar ISomerase) superfamily. Phosphoheptose ...
 10-146 2.72e-07

Phosphoheptose isomerase is a member of the SIS (Sugar ISomerase) superfamily. Phosphoheptose isomerase catalyzes the isomerization of sedoheptulose 7-phosphate into D-glycero-D-mannoheptose 7-phosphate. This is the first step of the biosynthesis of gram-negative bacteria inner core lipopolysaccharide precursor, L-glycero-D-mannoheptose (Gmh).


Pssm-ID: 240139 [Multi-domain]  Cd Length: 177  Bit Score: 49.82  E-value: 2.72e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838346481  10 RETIETELREAANLAERLnndfIQACLLIQACR---GKVIVSGIGKSGHIGRKIAATLAS---TGTPAFyvhPAEALHGD 83
Cdd:cd05006     2 QESIQLKEALLELLAEAI----EQAAQLLAEALlngGKILICGNGGSAADAQHFAAELVKrfeKERPGL---PAIALTTD 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838346481  84 LGMITA---------------------GDVVILISSSGHAAEfrlivpLLKALPVG------IIAFTGNPHSPLGEAADY 136
Cdd:cd05006    75 TSILTAiandygyeevfsrqvealgqpGDVLIGISTSGNSPN------VLKALEAAkergmkTIALTGRDGGKLLELADI 148

                         170
                  ....*....|
gi 1838346481 137 CINIHANKEA 146
Cdd:cd05006   149 EIHVPSDDTP 158
CBS_pair_IMPDH cd04601
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains in the inosine 5' ...
 211-315 7.14e-07

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: 47.02  E-value: 7.14e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838346481 211 CVSDRATVTDALFELTRTGLGLVAITNADNKLKGVFTDGDLRrwlmkggVIT---AAVQDAMT--------VPGFTLSag 279
Cdd:cd04601     6 TLSPDATVADVLELKAEYGISGVPVTEDGGKLVGIVTSRDIR-------FETdlsTPVSEVMTpderlvtaPEGITLE-- 76

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 1838346481 280 qlaaEAQALFQQYKISAAPVVTEDGTLSGAINAHDI 315
Cdd:cd04601    77 ----EAKEILHKHKIEKLPIVDDNGELVGLITRKDI 108
CBS pfam00571
CBS domain; CBS domains are small intracellular modules that pair together to form a stable ...
 265-318 7.60e-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: 45.67  E-value: 7.60e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1838346481 265 VQDAMTVPGFTLSAGQLAAEAQALFQQYKISAAPVVTEDGTLSGAINAHDIREA 318
Cdd:pfam00571   1 VKDIMTKDVVTVSPDTTLEEALELMREHGISRLPVVDEDGKLVGIVTLKDLLRA 54
CBS pfam00571
CBS domain; CBS domains are small intracellular modules that pair together to form a stable ...
 199-257 9.92e-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: 9.92e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1838346481 199 VGDIMRnaEKIPCVSDRATVTDALFELTRTGLGLVAITNADNKLKGVFTDGDLRRWLMK 257
Cdd:pfam00571   1 VKDIMT--KDVVTVSPDTTLEEALELMREHGISRLPVVDEDGKLVGIVTLKDLLRALLG 57
COG3448 COG3448
CBS-domain-containing membrane protein [Signal transduction mechanisms];
168-257 4.14e-06

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


Pssm-ID: 442671 [Multi-domain]  Cd Length: 136  Bit Score: 45.63  E-value: 4.14e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838346481 168 AVALMRARNF----------------SEHDFARSHPAGSLGTRLL----CRVGDIMRnaEKIPCVSDRATVTDALFELTR 227
Cdd:COG3448    24 ALELMREHGIrglpvvdedgrlvgivTERDLLRALLPDRLDELEErlldLPVEDVMT--RPVVTVTPDTPLEEAAELMLE 101

                          90       100       110
                  ....*....|....*....|....*....|
gi 1838346481 228 TGLGLVAITNADNKLKGVFTDGDLRRWLMK 257
Cdd:COG3448   102 HGIHRLPVVDDDGRLVGIVTRTDLLRALAR 131
COG3448 COG3448
CBS-domain-containing membrane protein [Signal transduction mechanisms];
265-318 5.32e-06

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


Pssm-ID: 442671 [Multi-domain]  Cd Length: 136  Bit Score: 45.24  E-value: 5.32e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1838346481 265 VQDAMTVPGFTLSAGQLAAEAQALFQQYKISAAPVVTEDGTLSGAINAHDIREA 318
Cdd:COG3448     4 VRDIMTRDVVTVSPDTTLREALELMREHGIRGLPVVDEDGRLVGIVTERDLLRA 57
SIS cd04795
SIS domain. SIS (Sugar ISomerase) domains are found in many phosphosugar isomerases and ...
 45-123 7.89e-06

SIS domain. SIS (Sugar ISomerase) domains are found in many phosphosugar isomerases and phosphosugar binding proteins. SIS domains are also found in proteins that regulate the expression of genes involved in synthesis of phosphosugars.


Pssm-ID: 240112 [Multi-domain]  Cd Length: 87  Bit Score: 43.52  E-value: 7.89e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838346481  45 VIVSGIGKSGHIGRKIAATLAS-TGTPAFYVHPAEALHGD-LGMITAGDVVILISSSGHAAEFRLIVPLLKALPVGIIAF 122
Cdd:cd04795     1 IFVIGIGGSGAIAAYFALELLElTGIEVVALIATELEHASlLSLLRKGDVVIALSYSGRTEELLAALEIAKELGIPVIAI 80


                  .
gi 1838346481 123 T 123
Cdd:cd04795    81 T 81
IMPDH pfam00478
IMP dehydrogenase / GMP reductase domain; This family is involved in biosynthesis of guanosine ...
 211-315 1.72e-05

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


Pssm-ID: 459826 [Multi-domain]  Cd Length: 463  Bit Score: 46.23  E-value: 1.72e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838346481 211 CVSDRATVTDALFELTRTGLGLVAITNaDNKLKGVFTDGDLR--RWLmkggviTAAVQDAMTVPG-FTLSAGQLAAEAQA 287
Cdd:pfam00478  92 TLSPDATVADALALMERYGISGVPVVD-DGKLVGIVTNRDLRfeTDL------SQPVSEVMTKENlVTAPEGTTLEEAKE 164

                          90       100
                  ....*....|....*....|....*...
gi 1838346481 288 LFQQYKISAAPVVTEDGTLSGAINAHDI 315
Cdd:pfam00478 165 ILHKHKIEKLPVVDDNGRLVGLITIKDI 192
CBS_two-component_sensor_histidine_kinase_repeat1 cd04620
2 tandem repeats of the CBS domain in the two-component sensor histidine kinase and ...
 239-318 2.12e-05

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: 43.68  E-value: 2.12e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838346481 239 DNKLKGVFTDGDLRRWLMKGGVITA-AVQDAMTVPGFTLSAGQL--AAEAQALFQQYKISAAPVVTEDGTLSGAINAHDI 315
Cdd:cd04620    54 NQQLVGIFTERDVVRLTASGIDLSGvTIAEVMTQPVITLKESEFqdIFTVLSLLRQHQIRHLPIVDDQGQLVGLITPESL 133


                  ...
gi 1838346481 316 REA 318
Cdd:cd04620   134 RQV 136
CBS_pair_SF cd02205
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains superfamily; The CBS ...
 177-253 2.19e-05

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


Pssm-ID: 341358 [Multi-domain]  Cd Length: 113  Bit Score: 43.00  E-value: 2.19e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1838346481 177 FSEHDFARSHPAGSLGTRLlcRVGDIMRNaeKIPCVSDRATVTDALFELTRTGLGLVAITNADNKLKGVFTDGDLRR 253
Cdd:cd02205    41 VTERDILRALVEGGLALDT--PVAEVMTP--DVITVSPDTDLEEALELMLEHGIRRLPVVDDDGKLVGIVTRRDILR 113
SIS_GlmS_GlmD_1 cd05008
SIS (Sugar ISomerase) domain repeat 1 found in Glucosamine 6-phosphate synthase (GlmS) and ...
 44-145 3.73e-05

SIS (Sugar ISomerase) domain repeat 1 found in Glucosamine 6-phosphate synthase (GlmS) and Glucosamine-6-phosphate deaminase (GlmD). The SIS domain is found in many phosphosugar isomerases and phosphosugar binding proteins. GlmS contains a N-terminal glutaminase domain and two C-terminal SIS domains and catalyzes the first step in hexosamine metabolism, converting fructose 6-phosphate into glucosamine 6-phosphate using glutamine as nitrogen source. The glutaminase domain hydrolyzes glutamine to glutamate and ammonia. Ammonia is transferred through a channel to the isomerase domain for glucosamine 6-phosphate synthesis. The end product of the pathway is N-acetylglucosamine, which plays multiple roles in eukaryotic cells including being a building block of bacterial and fungal cell walls. In the absence of glutamine, GlmS catalyzes the isomerization of fructose 6-phosphate into glucose 6- phosphate (PGI-like activity). Glucosamine-6-phosphate deaminase (GlmD) contains two SIS domains and catalyzes the deamination and isomerization of glucosamine-6-phosphate into fructose-6-phosphate with the release of ammonia; in presence of high ammonia concentration, GlmD can catalyze the reverse reaction.


Pssm-ID: 240141 [Multi-domain]  Cd Length: 126  Bit Score: 42.48  E-value: 3.73e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838346481  44 KVIVSGIGKSGHIGRKIAATLASTGTPAFYVHPAEALHGDLGMITAGDVVILISSSGHAAEFRLIVPLLKALPVGIIAFT 123
Cdd:cd05008     1 RILIVGCGTSYHAALVAKYLLERLAGIPVEVEAASEFRYRRPLLDEDTLVIAISQSGETADTLAALRLAKEKGAKTVAIT 80

                          90       100
                  ....*....|....*....|..
gi 1838346481 124 GNPHSPLGEAADYCINIHANKE 145
Cdd:cd05008    81 NVVGSTLAREADYVLYLRAGPE 102
CBS_pair_NeuB cd17773
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domain present in ...
 217-306 8.39e-05

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


Pssm-ID: 341409 [Multi-domain]  Cd Length: 118  Bit Score: 41.47  E-value: 8.39e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838346481 217 TVTDALFELTRTGLGLVAITNADNKLKGVFTDGDLRRWLMKGGVI--TAAVQDAMTVPGFTLSAGQLAAEAQALFQQyKI 294
Cdd:cd17773    16 SILNALQKISDNKSRIVFCVDEHGVLEGVLTDGDFRRWLLENPNAdlSQPVSHVANTNFVSAPEGESPEKIEALFSS-RI 94

                          90
                  ....*....|..
gi 1838346481 295 SAAPVVTEDGTL 306
Cdd:cd17773    95 SYIPLVDERGRL 106
COG2524 COG2524
Predicted transcriptional regulator, contains C-terminal CBS domains [Transcription];
168-255 1.30e-04

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


Pssm-ID: 442013 [Multi-domain]  Cd Length: 206  Bit Score: 42.18  E-value: 1.30e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838346481 168 AVALMRARNF---------------SEHDFARSHPAGSLGTRLlcRVGDIMRnaEKIPCVSDRATVTDALFELTRTGLGL 232
Cdd:COG2524   108 ALELMLEKGIsglpvvddgklvgiiTERDLLKALAEGRDLLDA--PVSDIMT--RDVVTVSEDDSLEEALRLMLEHGIGR 183

                          90       100
                  ....*....|....*....|...
gi 1838346481 233 VAITNADNKLKGVFTDGDLRRWL 255
Cdd:COG2524   184 LPVVDDDGKLVGIITRTDILRAL 206
CBS_pair_bac_euk cd04623
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains present in bacteria ...
 216-315 1.48e-04

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: 40.48  E-value: 1.48e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838346481 216 ATVTDALFELTRTGLGLVAITNADNKLKGVFTDGDLRRWLMKGG--VITAAVQDAMTVPGFTLSAGQLAAEAQALFQQYK 293
Cdd:cd04623    11 ATVAEALRLLAEKNIGALVVVDDGGRLVGILSERDYVRKLALRGasSLDTPVSEIMTRDVVTCTPDDTVEECMALMTERR 90

                          90       100
                  ....*....|....*....|..
gi 1838346481 294 ISAAPVVtEDGTLSGAINAHDI 315
Cdd:cd04623    91 IRHLPVV-EDGKLVGIVSIGDV 111
CBS_pair_Mg_transporter cd04606
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains in the magnesium ...
 212-315 1.91e-04

Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains in the magnesium transporter, MgtE; This cd contains two tandem repeats of the cystathionine beta-synthase (CBS pair) domain in the magnesium transporter, MgtE. MgtE and its homologs are found in eubacteria, archaebacteria, and eukaryota. Members of this family transport Mg2+ or other divalent cations into the cell via two highly conserved aspartates. The CBS domain, named after human CBS, is a small domain originally identified in cystathionine beta-synthase and is subsequently found in a wide range of different proteins. CBS domains usually occur in tandem repeats. They associate to form a so-called Bateman domain or a CBS pair based on crystallographic studies in bacteria. The CBS pair was used as a basis for this cd hierarchy since the human CBS proteins can adopt the typical core structure and form an intramolecular CBS pair. The interface between the two CBS domains forms a cleft that is a potential ligand binding site. The CBS pair coexists with a variety of other functional domains and this has been used to help in its classification here. It has been proposed that the CBS domain may play a regulatory role, although its exact function is unknown. Mutations of conserved residues within this domain are associated with a variety of human hereditary diseases, including congenital myotonia, idiopathic generalized epilepsy, hypercalciuric nephrolithiasis, and classic Bartter syndrome (CLC chloride channel family members), Wolff-Parkinson-White syndrome (gamma 2 subunit of AMP-activated protein kinase), retinitis pigmentosa (IMP dehydrogenase-1), and homocystinuria (cystathionine beta-synthase).


Pssm-ID: 341380 [Multi-domain]  Cd Length: 121  Bit Score: 40.39  E-value: 1.91e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838346481 212 VSDRATVTDALFELTRTGLGL-----VAITNADNKLKGVFTdgdLRRwlmkggVITAA----VQDAMTVPGFTLSAGQLA 282
Cdd:cd04606    14 VRPDWTVEEALEYLRRLAPDPetiyyIYVVDEDRRLLGVVS---LRD------LLLADpdtkVSDIMDTDVISVSADDDQ 84

                          90       100       110
                  ....*....|....*....|....*....|...
gi 1838346481 283 AEAQALFQQYKISAAPVVTEDGTLSGAINAHDI 315
Cdd:cd04606    85 EEVARLFAKYDLLALPVVDEEGRLVGIITVDDV 117
PRK07807 PRK07807
GuaB1 family IMP dehydrogenase-related protein;
212-320 2.41e-04

GuaB1 family IMP dehydrogenase-related protein;


Pssm-ID: 181127 [Multi-domain]  Cd Length: 479  Bit Score: 42.58  E-value: 2.41e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838346481 212 VSDRATVTDALFELTRTGLGLVAITNADNKLKGVFTDGDLRrwlmkgGVIT-AAVQDAMTVPGFTLSAGQLAAEAQALFQ 290
Cdd:PRK07807  102 LSPDDTVGDALALLPKRAHGAVVVVDEEGRPVGVVTEADCA------GVDRfTQVRDVMSTDLVTLPAGTDPREAFDLLE 175

                          90       100       110
                  ....*....|....*....|....*....|
gi 1838346481 291 QYKISAAPVVTEDGTLSGAINAHDIREAGI 320
Cdd:PRK07807  176 AARVKLAPVVDADGRLVGVLTRTGALRATI 205
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 ...
 202-315 3.29e-04

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: 39.61  E-value: 3.29e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838346481 202 IMRNAekIPCVSDrATVTDALFELTRTGLGLVAITNADNKLKGVFTDGDLRRWLMKGGV-ITAAVQDAMTVPGFTLSAGQ 280
Cdd:cd17771     2 IRREP--VTCSPD-TPLRAALETMHERRVGSMVVVDANRRPVGIFTLRDLLSRVALPQIdLDAPISEVMTPDPVRLPPSA 78

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 1838346481 281 LAAEAQALFQQYKIsAAPVVTEDGTLSGAINAHDI 315
Cdd:cd17771    79 SAFEAALLMAEHGF-RHVCVVDNGRLVGVVSERDL 112
CBS smart00116
Domain in cystathionine beta-synthase and other proteins; Domain present in all 3 forms of ...
 209-251 4.40e-04

Domain in cystathionine beta-synthase and other proteins; Domain present in all 3 forms of cellular life. Present in two copies in inosine monophosphate dehydrogenase, of which one is disordered in the crystal structure. A number of disease states are associated with CBS-containing proteins including homocystinuria, Becker's and Thomsen disease.


Pssm-ID: 214522 [Multi-domain]  Cd Length: 49  Bit Score: 37.49  E-value: 4.40e-04
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|...
gi 1838346481  209 IPCVSDRATVTDALFELTRTGLGLVAITNADNKLKGVFTDGDL 251
Cdd:smart00116   2 VVTVSPDTTLEEALELLRENGIRRLPVVDEEGRLVGIVTRRDI 44
YtoI COG4109
Predicted transcriptional regulator containing CBS domains [Transcription];
265-318 4.78e-04

Predicted transcriptional regulator containing CBS domains [Transcription];


Pssm-ID: 443285 [Multi-domain]  Cd Length: 135  Bit Score: 39.51  E-value: 4.78e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1838346481 265 VQDAMTVPGF-TLSAGQLAAEAQALFQQYKISAAPVVTEDGTLSGAINAHDIREA 318
Cdd:COG4109    18 VEDIMTLEDVaTLSEDDTVEDALELLEKTGHSRFPVVDENGRLVGIVTSKDILGK 72
PRK11557 PRK11557
MurR/RpiR family transcriptional regulator;
22-138 4.85e-04

MurR/RpiR family transcriptional regulator;


Pssm-ID: 183195 [Multi-domain]  Cd Length: 278  Bit Score: 41.29  E-value: 4.85e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838346481  22 NLAERLnndfIQACLLIQACRgKVIVSGIGKSGHIGRKIAATLASTGTPAFYVHPAEALHGDLGMITAGDVVILISSSGH 101
Cdd:PRK11557  113 NSEEKL----HECVTMLRSAR-RIILTGIGASGLVAQNFAWKLMKIGINAVAERDMHALLATVQALSPDDLLLAISYSGE 187

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 1838346481 102 AAEFRLIVPllKALPVG--IIAFTGNPHSPLGEAADYCI 138
Cdd:PRK11557  188 RRELNLAAD--EALRVGakVLAITGFTPNALQQRASHCL 224
CBS_pair_HRP1_like cd04622
CBS pair domain found in Hypoxic Response Protein 1 (HRP1) -like proteinds; Mycobacterium ...
 211-310 4.92e-04

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: 38.94  E-value: 4.92e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838346481 211 CVSDRATVTDALFELTRTGLGLVAITNaDNKLKGVFTDGD--LRRWLMKGGVITAAVQDAMTVPGFTLSAGQLAAEAQAL 288
Cdd:cd04622     7 TVSPDTTLREAARLMRDLDIGALPVCE-GDRLVGMVTDRDivVRAVAEGKDPNTTTVREVMTGDVVTCSPDDDVEEAARL 85

                          90       100
                  ....*....|....*....|..
gi 1838346481 289 FQQYKISAAPVVTEDGTLSGAI 310
Cdd:cd04622    86 MAEHQVRRLPVVDDDGRLVGIV 107
CBS_pair_peptidase_M50 cd04639
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains found in the ...
 235-318 5.08e-04

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


Pssm-ID: 341397 [Multi-domain]  Cd Length: 120  Bit Score: 39.09  E-value: 5.08e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838346481 235 ITNADNKLKGVFTDGDLRRWLMKGGVITAaVQDAMTvPG---FTLSAGQLAAEAQALFQQYKISAAPVVTEDGTLSGAIN 311
Cdd:cd04639    35 VTDEAGRLVGLITVDDLRAIPTSQWPDTP-VRELMK-PLeeiPTVAADQSLLEVVKLLEEQQLPALAVVSENGTLVGLIE 112


                  ....*..
gi 1838346481 312 AHDIREA 318
Cdd:cd04639   113 KEDIIEL 119
CBS_pair_bact_arch cd17775
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains present in bacteria ...
 211-315 9.96e-04

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: 38.29  E-value: 9.96e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838346481 211 CVSDRATVTDALFELTRTGLGLVAITNADNKLKGVFTDGDLRRWLMKGGVITAA--VQDAMTVPGFTLSAGQLAAEAQAL 288
Cdd:cd17775     7 TASPDTSVLEAARLMRDHHVGSVVVVEEDGKPVGIVTDRDIVVEVVAKGLDPKDvtVGDIMSADLITAREDDGLFEALER 86

                          90       100
                  ....*....|....*....|....*..
gi 1838346481 289 FQQYKISAAPVVTEDGTLSGAINAHDI 315
Cdd:cd17775    87 MREKGVRRLPVVDDDGELVGIVTLDDI 113
MgtE COG2239
Mg/Co/Ni transporter MgtE (contains CBS domain) [Inorganic ion transport and metabolism];
235-315 1.05e-03

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


Pssm-ID: 441840 [Multi-domain]  Cd Length: 443  Bit Score: 40.44  E-value: 1.05e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838346481 235 ITNADNKLKGVFTdgdLRRwlmkggVITAA----VQDAMTVPGFTLSAGQLAAEAQALFQQYKISAAPVVTEDGTLSGAI 310
Cdd:COG2239   170 VVDDDGRLVGVVS---LRD------LLLADpdtkVSDIMDTDVISVPADDDQEEVARLFERYDLLALPVVDEEGRLVGII 240


                  ....*
gi 1838346481 311 NAHDI 315
Cdd:COG2239   241 TVDDV 245
PRK02947 PRK02947
sugar isomerase domain-containing protein;
87-177 1.21e-03

sugar isomerase domain-containing protein;


Pssm-ID: 179510 [Multi-domain]  Cd Length: 246  Bit Score: 39.85  E-value: 1.21e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838346481  87 ITAGDVVILISSSGHAA---EFRLIVpllKALPVGIIAFTGNPHSP-----------LGEAADYCINIHANK-------E 145
Cdd:PRK02947  104 IRPGDVLIVVSNSGRNPvpiEMALEA---KERGAKVIAVTSLAYSAsvasrhssgkrLAEVADVVLDNGAPKgdavleiP 180

                          90       100       110
                  ....*....|....*....|....*....|....
gi 1838346481 146 ACPLGLAPTSSAVNTLIMGDAMA--VALMRARNF 177
Cdd:PRK02947  181 GLEAPVGPVSTVVGAAILNAIFAevAERLVERGI 214
mgtE TIGR00400
Mg2+ transporter (mgtE); This family of prokaryotic proteins models a class of Mg++ ...
 217-317 1.25e-03

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


Pssm-ID: 129495 [Multi-domain]  Cd Length: 449  Bit Score: 40.19  E-value: 1.25e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838346481 217 TVTDAL-----FELTRTGLGLVAITNADNKLKGVFTDGDLrrWLMKGGVItaaVQDAMTVPGFTLSAGQLAAEAQALFQQ 291
Cdd:TIGR00400 149 TVGKALdyirrVAKTKEDIYTLYVTNESKHLKGVLSIRDL--ILAKPEEI---LSSIMRSSVFSIVGVNDQEEVARLIQK 223

                          90       100
                  ....*....|....*....|....*.
gi 1838346481 292 YKISAAPVVTEDGTLSGAINAHDIRE 317
Cdd:TIGR00400 224 YDFLAVPVVDNEGRLVGIVTVDDIID 249
CBS_pair_ACT cd17787
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains found in Thermatoga ...
 210-318 1.50e-03

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: 37.78  E-value: 1.50e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838346481 210 PCVSDRATVTDALFELTRTGLGLVAITNADNKLKGVftdgdLRRWLMKGGVITAAVQDAMTVPGFTLSAGQLAAEAQALF 289
Cdd:cd17787     5 PTFEESATVGEVLHEMRKYETDYCIVVDEEGKFAGM-----VRKSKIMDEDLDKKVKEYVVEPDFYCHEEDYIEDAALLL 79

                          90       100
                  ....*....|....*....|....*....
gi 1838346481 290 QQYKISAAPVVTEDGTLSGAINAHDIREA 318
Cdd:cd17787    80 IESHEFVLPVVNSDMKVKGVLTVFEILEA 108
CBS_pair_bac cd04629
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains present in bacteria; ...
 269-314 1.66e-03

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


Pssm-ID: 341392 [Multi-domain]  Cd Length: 116  Bit Score: 37.80  E-value: 1.66e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*.
gi 1838346481 269 MTVPGFTLSAGQLAAEAQALFQQYKISAAPVVTEDGTLSGAINAHD 314
Cdd:cd04629     1 MTRNPVTLTPDTSILEAVELLLEHKISGAPVVDEQGRLVGFLSEQD 46
PRK11337 PRK11337
MurR/RpiR family transcriptional regulator;
49-171 2.36e-03

MurR/RpiR family transcriptional regulator;


Pssm-ID: 183089 [Multi-domain]  Cd Length: 292  Bit Score: 38.97  E-value: 2.36e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838346481  49 GIGKSGHIGRKIAATLASTGTPAFYVHPAEALHGDLGMITAGDVVILISSSGHAAEFRLIVPLLKALPVGIIAFTGNPHS 128
Cdd:PRK11337  147 GAGGSAAIARDVQHKFLRIGVRCQAYDDAHIMLMSAALLQEGDVVLVVSHSGRTSDVIEAVELAKKNGAKIICITNSYHS 226

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 1838346481 129 PLGEAADYCINIHAnkEACPLGLAPTSSAVNTLIMGDAMAVAL 171
Cdd:PRK11337  227 PIAKLADYVICSTA--QGSPLLGENAAARIAQLNILDAFFVSV 267
SIS_1 cd05710
A subgroup of the SIS domain. SIS (Sugar ISomerase) domains are found in many phosphosugar ...
 70-138 2.91e-03

A subgroup of the SIS domain. SIS (Sugar ISomerase) domains are found in many phosphosugar isomerases and phosphosugar binding proteins. SIS domains are also found in proteins that regulate the expression of genes involved in synthesis of phosphosugars.


Pssm-ID: 240214 [Multi-domain]  Cd Length: 120  Bit Score: 37.17  E-value: 2.91e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1838346481  70 PAFYVHPAEALHGDLGMITAGDVVILISSSGHAAEFRLIVPLLKALPVGIIAFTGNPHSPLGEAADYCI 138
Cdd:cd05710    28 PVFVYNAAEFLHTGPKRLTEKSVVILASHSGNTKETVAAAKFAKEKGATVIGLTDDEDSPLAKLADYVI 96
CBS smart00116
Domain in cystathionine beta-synthase and other proteins; Domain present in all 3 forms of ...
 274-315 3.42e-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: 34.80  E-value: 3.42e-03
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|..
gi 1838346481  274 FTLSAGQLAAEAQALFQQYKISAAPVVTEDGTLSGAINAHDI 315
Cdd:smart00116   3 VTVSPDTTLEEALELLRENGIRRLPVVDEEGRLVGIVTRRDI 44
CBS_pair_GGDEF_assoc cd04599
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with the ...
 269-318 3.65e-03

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


Pssm-ID: 341374 [Multi-domain]  Cd Length: 107  Bit Score: 36.55  E-value: 3.65e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 1838346481 269 MTVPGFTLSAGQLAAEAQALFQQYKISAAPVVtEDGTLSGAINAHDIREA 318
Cdd:cd04599     1 MTRNPITISPLDSVARAAALMERQRIGGLPVV-ENGKLVGIITSRDVRRA 49
CBS_pair_arch_MET2_assoc cd04605
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with the ...
 199-315 3.83e-03

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


Pssm-ID: 341379 [Multi-domain]  Cd Length: 116  Bit Score: 36.45  E-value: 3.83e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838346481 199 VGDIMrnAEKIPCVSDRATVTDALFELTRTGLGLVAITNADNKLKGVFTDGDLRRWLMKGgviTAAVQDAMTVPGFTLSA 278
Cdd:cd04605     2 VEDIM--SKDVATIREDISIEEAAKIMIDKNVTHLPVVSEDGKLIGIVTSWDISKAVALK---KDSLEEIMTRNVITARP 76

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 1838346481 279 GQLAAEAQALFQQYKISAAPVVTEDGTLSGAINAHDI 315
Cdd:cd04605    77 DEPIELAARKMEKHNISALPVVDDDRRVIGIITSDDI 113
CBS_pair_voltage-gated_CLC_bac cd04613
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with the ...
 237-318 5.20e-03

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


Pssm-ID: 341385 [Multi-domain]  Cd Length: 119  Bit Score: 36.40  E-value: 5.20e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838346481 237 NADNKLKGVFTDGDLRRWLMKGGVIT-AAVQDAMTVPGFTLSAGQLAAEAQALFQQYKISAAPVVTED--GTLSGAINAH 313
Cdd:cd04613    33 DEQGRLTGILSIQDVRGVLFEEELWDlVVVKDLATTDVITVTPDDDLYTALLKFTSTNLDQLPVVDDDdpGKVLGMLSRR 112


                  ....*
gi 1838346481 314 DIREA 318
Cdd:cd04613   113 DVIAA 117
CBS_arch_repeat2 cd17778
CBS pair domains found in archeal proteins, repeat 2; CBS pair domains found in archeal ...
 175-251 5.23e-03

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


Pssm-ID: 341414 [Multi-domain]  Cd Length: 131  Bit Score: 36.54  E-value: 5.23e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1838346481 175 RNFSEHDFARSHPAGSLGTRLLCRVGDIMRnaEKIPCVSDRATVTDALFELTRTGLGLVAITNADNKLKGVFTDGDL 251
Cdd:cd17778    53 KYFGSHEAKKRLTTGDIDEAYSTPVEEIMS--KEVVTIEPDADIAEAARLMIKKNVGSLLVVDDEGELKGIITERDV 127
CBS_pair_SF cd02205
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains superfamily; The CBS ...
 274-320 5.38e-03

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: 36.07  E-value: 5.38e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*..
gi 1838346481 274 FTLSAGQLAAEAQALFQQYKISAAPVVTEDGTLSGAINAHDIREAGI 320
Cdd:cd02205     5 VTVDPDTTVREALELMAENGIGALPVVDDDGKLVGIVTERDILRALV 51
CBS_pair_IMPDH cd04601
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains in the inosine 5' ...
 274-316 6.47e-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: 35.85  E-value: 6.47e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|...
gi 1838346481 274 FTLSAGQLAAEAQALFQQYKISAAPVVTEDGTLSGAINAHDIR 316
Cdd:cd04601     5 VTLSPDATVADVLELKAEYGISGVPVTEDGGKLVGIVTSRDIR 47
COG2905 COG2905
Signal-transduction protein containing cAMP-binding, CBS, and nucleotidyltransferase domains ...
 265-320 6.64e-03

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


Pssm-ID: 442149 [Multi-domain]  Cd Length: 124  Bit Score: 35.96  E-value: 6.64e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1838346481 265 VQDAMTVPGFTLSAGQLAAEAQALFQQYKISAAPVVTEDGTLSGAINAHDIREAGI 320
Cdd:COG2905     1 VKDIMSRDVVTVSPDATVREAARLMTEKGVGSLVVVDDDGRLVGIITDRDLRRRVL 56
CBS_pair_bac cd04630
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains present in bacteria; ...
 199-315 7.88e-03

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


Pssm-ID: 341393 [Multi-domain]  Cd Length: 120  Bit Score: 35.65  E-value: 7.88e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838346481 199 VGDIMRNaeKIPCVSDRATVTDALFELTRTGL--GLVAITNADNKLkGVFTDGD-LRRWLMKGGVITAA-VQDAMTVPGF 274
Cdd:cd04630     1 VRDVMKT--NVVTIDGLATVREALQLMKEHNVksLIVEKRHEHDAY-GIVTYTDiLKKVIAEDRDPDLVnVYEIMTKPAI 77

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 1838346481 275 TLSAgQLAAE-AQALFQQYKISAAPVVtEDGTLSGAINAHDI 315
Cdd:cd04630    78 SVSP-DLDIKyAARLMARFNLKRAPVI-ENNELIGIVSMTDL 117
CBS_pair_BON_assoc cd04586
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with the ...
 211-315 9.44e-03

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: 35.87  E-value: 9.44e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838346481 211 CVSDRATVTDALFELTRTGLGLVAITNADNKLKGVFTDGDL-----------RRWLMKGGVITAA-------------VQ 266
Cdd:cd04586     7 TVTPDTSVREAARLLLEHRISGLPVVDDDGKLVGIVSEGDLlrreepgteprRVWWLDALLESPErlaeeyvkahgrtVG 86

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 1838346481 267 DAMTVPGFTLSAGQLAAEAQALFQQYKISAAPVVtEDGTLSGAINAHDI 315
Cdd:cd04586    87 DVMTRPVVTVSPDTPLEEAARLMERHRIKRLPVV-DDGKLVGIVSRADL 134
CBS COG0517
CBS domain [Signal transduction mechanisms];
177-257 9.91e-03

CBS domain [Signal transduction mechanisms];


Pssm-ID: 440283 [Multi-domain]  Cd Length: 128  Bit Score: 35.61  E-value: 9.91e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838346481 177 FSEHD--FARSHPAGSLGTRllcRVGDIMRnaEKIPCVSDRATVTDALFELTRTGLGLVAITNADNKLKGVFTDGDLRRW 254
Cdd:COG0517    48 VTDRDlrRALAAEGKDLLDT---PVSEVMT--RPPVTVSPDTSLEEAAELMEEHKIRRLPVVDDDGRLVGIITIKDLLKA 122


                  ...
gi 1838346481 255 LMK 257
Cdd:COG0517   123 LLE 125
 
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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