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Conserved domains on  [gi|496494511|ref|WP_009203047|]
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magnesium transporter [Anaerostipes hadrus]

Protein Classification

magnesium transporter( domain architecture ID 11454921)

MgtE family magnesium transporter is involved in the maintenance of cellular Mg(2+) homeostasis; may contain CBS domain(s)

CATH:  1.25.60.10|3.10.580.10
Gene Ontology:  GO:0000287|GO:0015095|GO:0015693|GO:0005524
PubMed:  19798051|21958115
SCOP:  4000203|4000290|4000247
TCDB:  1.A.26.1.1

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
MgtE COG2239
Mg/Co/Ni transporter MgtE (contains CBS domain) [Inorganic ion transport and metabolism];
9-459 4.89e-143

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


:

Pssm-ID: 441840 [Multi-domain]  Cd Length: 443  Bit Score: 416.78  E-value: 4.89e-143
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496494511   9 RTDYAKELVKIVQTTKDREELKKKIAAYHERDIANAIVESDKTVRKCIYDILDIADIAEIFSYIEEEP-GKYLEEMPIEQ 87
Cdd:COG2239    1 ETEELLEELRELLEEGDLEELRELLEELHPADIAELLEELPPEERLALFRLLPKELAAEVLEELDEEVqEELLEELSDEE 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496494511  88 AAKVVSNMDSDDAMDLFEELNEEDKYKLLKRLDKEAKEDVQKLLSYEEDQIGSCMTNNYIVVRNDVTIREAMSTLVKQAG 167
Cdd:COG2239   81 LAELLEELDPDDAADLLEELPEEVVEELLALLDPEEREEIRELLSYPEDSAGRLMTTEFVAVREDWTVGEALRYLRRQAE 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496494511 168 EHDNIQTLYVIDENGIFAGAIDLKDLIIAREHDNLQDIISSSYPYVYEHEKISECMEILTDYEEDSIPVLTQDKKIAGIL 247
Cdd:COG2239  161 DPETIYYIYVVDDDGRLVGVVSLRDLLLADPDTKVSDIMDTDVISVPADDDQEEVARLFERYDLLALPVVDEEGRLVGII 240

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496494511 248 TSSDIVELVDDEMGDDYAKLAGLTEEEDLNEPTIVSMKKRLPWLIALLFLGMAVSSVVGMFESIVAVLPIVICFQSLVLD 327
Cdd:COG2239  241 TVDDVVDVIEEEATEDILKLAGVSEDEDLFASVLKLARKRLPWLLILLLTAFLAASVIGLFEDTLEQVVALAVFMPLVAG 320

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496494511 328 MAGNVGTQSLAVTIRVLMDENLSGKKKIALLFKEMKIGFLNGASLAImaLVFLGVYIhlfkhyaWISSFLISGCVGISLI 407
Cdd:COG2239  321 MGGNAGSQSLTVVVRGLALGEITLSDWWRVLLKELLVGLLNGLILGL--VVGLVAYL-------WFGNPLLGLVVGLALV 391

                        410       420       430       440       450
                 ....*....|....*....|....*....|....*....|....*....|..
gi 496494511 408 VAMVISSLVGTIIPMFFHKINIDPAVASGPLITTINDLVAVITYYGLSGLVL 459
Cdd:COG2239  392 INVLVAALAGSLLPLLLKRLGIDPAVASGPFITTITDVVGFFIYLGLATLFL 443
 
Name Accession Description Interval E-value
MgtE COG2239
Mg/Co/Ni transporter MgtE (contains CBS domain) [Inorganic ion transport and metabolism];
9-459 4.89e-143

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


Pssm-ID: 441840 [Multi-domain]  Cd Length: 443  Bit Score: 416.78  E-value: 4.89e-143
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496494511   9 RTDYAKELVKIVQTTKDREELKKKIAAYHERDIANAIVESDKTVRKCIYDILDIADIAEIFSYIEEEP-GKYLEEMPIEQ 87
Cdd:COG2239    1 ETEELLEELRELLEEGDLEELRELLEELHPADIAELLEELPPEERLALFRLLPKELAAEVLEELDEEVqEELLEELSDEE 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496494511  88 AAKVVSNMDSDDAMDLFEELNEEDKYKLLKRLDKEAKEDVQKLLSYEEDQIGSCMTNNYIVVRNDVTIREAMSTLVKQAG 167
Cdd:COG2239   81 LAELLEELDPDDAADLLEELPEEVVEELLALLDPEEREEIRELLSYPEDSAGRLMTTEFVAVREDWTVGEALRYLRRQAE 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496494511 168 EHDNIQTLYVIDENGIFAGAIDLKDLIIAREHDNLQDIISSSYPYVYEHEKISECMEILTDYEEDSIPVLTQDKKIAGIL 247
Cdd:COG2239  161 DPETIYYIYVVDDDGRLVGVVSLRDLLLADPDTKVSDIMDTDVISVPADDDQEEVARLFERYDLLALPVVDEEGRLVGII 240

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496494511 248 TSSDIVELVDDEMGDDYAKLAGLTEEEDLNEPTIVSMKKRLPWLIALLFLGMAVSSVVGMFESIVAVLPIVICFQSLVLD 327
Cdd:COG2239  241 TVDDVVDVIEEEATEDILKLAGVSEDEDLFASVLKLARKRLPWLLILLLTAFLAASVIGLFEDTLEQVVALAVFMPLVAG 320

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496494511 328 MAGNVGTQSLAVTIRVLMDENLSGKKKIALLFKEMKIGFLNGASLAImaLVFLGVYIhlfkhyaWISSFLISGCVGISLI 407
Cdd:COG2239  321 MGGNAGSQSLTVVVRGLALGEITLSDWWRVLLKELLVGLLNGLILGL--VVGLVAYL-------WFGNPLLGLVVGLALV 391

                        410       420       430       440       450
                 ....*....|....*....|....*....|....*....|....*....|..
gi 496494511 408 VAMVISSLVGTIIPMFFHKINIDPAVASGPLITTINDLVAVITYYGLSGLVL 459
Cdd:COG2239  392 INVLVAALAGSLLPLLLKRLGIDPAVASGPFITTITDVVGFFIYLGLATLFL 443
mgtE TIGR00400
Mg2+ transporter (mgtE); This family of prokaryotic proteins models a class of Mg++ ...
 17-459 3.19e-68

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: 224.70  E-value: 3.19e-68
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496494511   17 VKIVQTTKDREELKKKIAAYHERDIANAIVESDKTVRKCIYDILDIADIAEIFSYIEEE-PGKYLEEMPIEQAAKVVSNM 95
Cdd:TIGR00400  11 IRILLKEKSYSKIKEKFLK*QP*DIAEALKRLPGTELILLYRFLPKKIAVDTFSNLDQStQNKLLNSFTNKEISEMINEM 90

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496494511   96 DSDDAMDLFEELNEEDKYKLLKRLDKEAKEDVQKLLSYEEDQIGSCMTNNYIVVRNDVTIREAMSTLVKQAGEHDNIQTL 175
Cdd:TIGR00400  91 NLDDVIDLLEEVPANVVQQLLASSTEEERKAINLLLSYSDDSAGRIMTIEYVELKEDYTVGKALDYIRRVAKTKEDIYTL 170

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496494511  176 YVIDENGIFAGAIDLKDLIIAREHDNLQDIISSSYPYVYEHEKISECMEILTDYEEDSIPVLTQDKKIAGILTSSDIVEL 255
Cdd:TIGR00400 171 YVTNESKHLKGVLSIRDLILAKPEEILSSIMRSSVFSIVGVNDQEEVARLIQKYDFLAVPVVDNEGRLVGIVTVDDIIDV 250

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496494511  256 VDDEMGDDYAKLAGLTEEED--LNEPTIVSMKKRLPWLIALLFLGMAVSSVVGMFESIVAVLPIVICFQSLVLDMAGNVG 333
Cdd:TIGR00400 251 IQSEATEDFYMIAAVKPLDDsyFDTSILVMAKNRIIWLLVLLVSSTFTATIISNYEDLLLSLVALANFIPLLMDTSGNAG 330

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496494511  334 TQSLAVTIRVLMDENLSGKKKIALLFKEMKIGFLNGASLAImaLVFLGVYIhlfkhyaWISSFLISGCVGISLIVAMVIS 413
Cdd:TIGR00400 331 SQSSAVVIRGLALETVKVKDFFKVILREICVSILVGAILAS--VNFLRIVF-------FQGKLLIAFVVSSSLFVSLTVA 401

                         410       420       430       440
                  ....*....|....*....|....*....|....*....|....*.
gi 496494511  414 SLVGTIIPMFFHKINIDPAVASGPLITTINDLVAVITYYGLSGLVL 459
Cdd:TIGR00400 402 KILGGLLPIVAKLLKLDPALMSGPLITTIADALTLIIYFNIAKWVL 447
MgtE pfam01769
Divalent cation transporter; This region is the integral membrane part of the eubacterial MgtE ...
 322-454 6.71e-36

Divalent cation transporter; This region is the integral membrane part of the eubacterial MgtE family of magnesium transporters. Related regions are found also in archaebacterial and eukaryotic proteins. All the archaebacterial and eukaryotic examples have two copies of the region. This suggests that the eubacterial examples may act as dimers. Members of this family probably transport Mg2+ or other divalent cations into the cell. The alignment contains two highly conserved aspartates that may be involved in cation binding (Bateman A unpubl.)


Pssm-ID: 460317 [Multi-domain]  Cd Length: 124  Bit Score: 129.10  E-value: 6.71e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496494511  322 QSLVLDMAGNVGTQSLAVTIRVLMDENLSGKKKIALLFKEMKIGFLNGASLAIMALVFLgvyihlfkhYAWISSFLISGC 401
Cdd:pfam01769   1 IPVILGLGGNLGSQSASRLSRALALGEIEPRDAWRVLLKELLVGLLLGLVLGLIAGVLA---------FLWFGGLLLGLV 71

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 496494511  402 VGISLIVAMVISSLVGTIIPMFFHKINIDPAVASGPLITTINDLVAVITYYGL 454
Cdd:pfam01769  72 VGLALLLAVLIALLLGTLLPLLLWRLGLDPDNASGPLITTLGDLLGLLILFGI 124
MgtE_N smart00924
MgtE intracellular N domain; This region is the integral membrane part of the eubacterial MgtE ...
 36-138 2.89e-21

MgtE intracellular N domain; This region is the integral membrane part of the eubacterial MgtE family of magnesium transporters. It is presumed to be an intracellular domain, that may be involved in magnesium binding.


Pssm-ID: 214915 [Multi-domain]  Cd Length: 105  Bit Score: 88.34  E-value: 2.89e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496494511    36 YHERDIANAIVESDKTVRKCIYDILDIADIAEIFSYIEEEP-GKYLEEM-PIEQAAKVVSNMDSDDAMDLFEELNEEDKY 113
Cdd:smart00924   1 LHPADIADLLEELPPEERAELFRLLPPERAAEVLEELDEEVqAELLEALpPDERAAELLEELDPDDAADLLEELPEEVRE 80

                           90       100
                   ....*....|....*....|....*
gi 496494511   114 KLLKRLDKEAKEDVQKLLSYEEDQI 138
Cdd:smart00924  81 ELLSLLDPEEREEIRELLSYPEDTA 105
CBS_pair_Mg_transporter cd04606
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains in the magnesium ...
 136-256 7.14e-21

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: 87.77  E-value: 7.14e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496494511 136 DQIGSCMTNNYIVVRNDVTIREAMSTLVKQAGEHDNIQTLYVIDENGIFAGAIDLKDLIIAREHDNLQDIISSSYPYVYE 215
Cdd:cd04606    1 DSAGRLMTTEFVAVRPDWTVEEALEYLRRLAPDPETIYYIYVVDEDRRLLGVVSLRDLLLADPDTKVSDIMDTDVISVSA 80

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 496494511 216 HEKISECMEILTDYEEDSIPVLTQDKKIAGILTSSDIVELV 256
Cdd:cd04606   81 DDDQEEVARLFAKYDLLALPVVDEEGRLVGIITVDDVLDVI 121
 
Name Accession Description Interval E-value
MgtE COG2239
Mg/Co/Ni transporter MgtE (contains CBS domain) [Inorganic ion transport and metabolism];
9-459 4.89e-143

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


Pssm-ID: 441840 [Multi-domain]  Cd Length: 443  Bit Score: 416.78  E-value: 4.89e-143
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496494511   9 RTDYAKELVKIVQTTKDREELKKKIAAYHERDIANAIVESDKTVRKCIYDILDIADIAEIFSYIEEEP-GKYLEEMPIEQ 87
Cdd:COG2239    1 ETEELLEELRELLEEGDLEELRELLEELHPADIAELLEELPPEERLALFRLLPKELAAEVLEELDEEVqEELLEELSDEE 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496494511  88 AAKVVSNMDSDDAMDLFEELNEEDKYKLLKRLDKEAKEDVQKLLSYEEDQIGSCMTNNYIVVRNDVTIREAMSTLVKQAG 167
Cdd:COG2239   81 LAELLEELDPDDAADLLEELPEEVVEELLALLDPEEREEIRELLSYPEDSAGRLMTTEFVAVREDWTVGEALRYLRRQAE 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496494511 168 EHDNIQTLYVIDENGIFAGAIDLKDLIIAREHDNLQDIISSSYPYVYEHEKISECMEILTDYEEDSIPVLTQDKKIAGIL 247
Cdd:COG2239  161 DPETIYYIYVVDDDGRLVGVVSLRDLLLADPDTKVSDIMDTDVISVPADDDQEEVARLFERYDLLALPVVDEEGRLVGII 240

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496494511 248 TSSDIVELVDDEMGDDYAKLAGLTEEEDLNEPTIVSMKKRLPWLIALLFLGMAVSSVVGMFESIVAVLPIVICFQSLVLD 327
Cdd:COG2239  241 TVDDVVDVIEEEATEDILKLAGVSEDEDLFASVLKLARKRLPWLLILLLTAFLAASVIGLFEDTLEQVVALAVFMPLVAG 320

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496494511 328 MAGNVGTQSLAVTIRVLMDENLSGKKKIALLFKEMKIGFLNGASLAImaLVFLGVYIhlfkhyaWISSFLISGCVGISLI 407
Cdd:COG2239  321 MGGNAGSQSLTVVVRGLALGEITLSDWWRVLLKELLVGLLNGLILGL--VVGLVAYL-------WFGNPLLGLVVGLALV 391

                        410       420       430       440       450
                 ....*....|....*....|....*....|....*....|....*....|..
gi 496494511 408 VAMVISSLVGTIIPMFFHKINIDPAVASGPLITTINDLVAVITYYGLSGLVL 459
Cdd:COG2239  392 INVLVAALAGSLLPLLLKRLGIDPAVASGPFITTITDVVGFFIYLGLATLFL 443
mgtE TIGR00400
Mg2+ transporter (mgtE); This family of prokaryotic proteins models a class of Mg++ ...
 17-459 3.19e-68

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: 224.70  E-value: 3.19e-68
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496494511   17 VKIVQTTKDREELKKKIAAYHERDIANAIVESDKTVRKCIYDILDIADIAEIFSYIEEE-PGKYLEEMPIEQAAKVVSNM 95
Cdd:TIGR00400  11 IRILLKEKSYSKIKEKFLK*QP*DIAEALKRLPGTELILLYRFLPKKIAVDTFSNLDQStQNKLLNSFTNKEISEMINEM 90

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496494511   96 DSDDAMDLFEELNEEDKYKLLKRLDKEAKEDVQKLLSYEEDQIGSCMTNNYIVVRNDVTIREAMSTLVKQAGEHDNIQTL 175
Cdd:TIGR00400  91 NLDDVIDLLEEVPANVVQQLLASSTEEERKAINLLLSYSDDSAGRIMTIEYVELKEDYTVGKALDYIRRVAKTKEDIYTL 170

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496494511  176 YVIDENGIFAGAIDLKDLIIAREHDNLQDIISSSYPYVYEHEKISECMEILTDYEEDSIPVLTQDKKIAGILTSSDIVEL 255
Cdd:TIGR00400 171 YVTNESKHLKGVLSIRDLILAKPEEILSSIMRSSVFSIVGVNDQEEVARLIQKYDFLAVPVVDNEGRLVGIVTVDDIIDV 250

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496494511  256 VDDEMGDDYAKLAGLTEEED--LNEPTIVSMKKRLPWLIALLFLGMAVSSVVGMFESIVAVLPIVICFQSLVLDMAGNVG 333
Cdd:TIGR00400 251 IQSEATEDFYMIAAVKPLDDsyFDTSILVMAKNRIIWLLVLLVSSTFTATIISNYEDLLLSLVALANFIPLLMDTSGNAG 330

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496494511  334 TQSLAVTIRVLMDENLSGKKKIALLFKEMKIGFLNGASLAImaLVFLGVYIhlfkhyaWISSFLISGCVGISLIVAMVIS 413
Cdd:TIGR00400 331 SQSSAVVIRGLALETVKVKDFFKVILREICVSILVGAILAS--VNFLRIVF-------FQGKLLIAFVVSSSLFVSLTVA 401

                         410       420       430       440
                  ....*....|....*....|....*....|....*....|....*.
gi 496494511  414 SLVGTIIPMFFHKINIDPAVASGPLITTINDLVAVITYYGLSGLVL 459
Cdd:TIGR00400 402 KILGGLLPIVAKLLKLDPALMSGPLITTIADALTLIIYFNIAKWVL 447
MgtE pfam01769
Divalent cation transporter; This region is the integral membrane part of the eubacterial MgtE ...
 322-454 6.71e-36

Divalent cation transporter; This region is the integral membrane part of the eubacterial MgtE family of magnesium transporters. Related regions are found also in archaebacterial and eukaryotic proteins. All the archaebacterial and eukaryotic examples have two copies of the region. This suggests that the eubacterial examples may act as dimers. Members of this family probably transport Mg2+ or other divalent cations into the cell. The alignment contains two highly conserved aspartates that may be involved in cation binding (Bateman A unpubl.)


Pssm-ID: 460317 [Multi-domain]  Cd Length: 124  Bit Score: 129.10  E-value: 6.71e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496494511  322 QSLVLDMAGNVGTQSLAVTIRVLMDENLSGKKKIALLFKEMKIGFLNGASLAIMALVFLgvyihlfkhYAWISSFLISGC 401
Cdd:pfam01769   1 IPVILGLGGNLGSQSASRLSRALALGEIEPRDAWRVLLKELLVGLLLGLVLGLIAGVLA---------FLWFGGLLLGLV 71

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 496494511  402 VGISLIVAMVISSLVGTIIPMFFHKINIDPAVASGPLITTINDLVAVITYYGL 454
Cdd:pfam01769  72 VGLALLLAVLIALLLGTLLPLLLWRLGLDPDNASGPLITTLGDLLGLLILFGI 124
MgtE_N pfam03448
MgtE intracellular N domain; This domain is found at the N-terminus of eubacterial magnesium ...
 36-136 4.80e-23

MgtE intracellular N domain; This domain is found at the N-terminus of eubacterial magnesium transporters of the MgtE family pfam01769. This domain is an intracellular domain that has an alpha-helical structure. The crystal structure of the MgtE transporter shows two of 5 magnesium ions are in the interface between the N domain and the CBS domains. In the absence of magnesium there is a large shift between the N and CBS domains.


Pssm-ID: 427299 [Multi-domain]  Cd Length: 102  Bit Score: 93.39  E-value: 4.80e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496494511   36 YHERDIANAIVESDKTVRKCIYDILDIADIAEIFSYIEEEPG-KYLEEMPIEQAAKVVSNMDSDDAMDLFEELNEEDKYK 114
Cdd:pfam03448   1 LHPADIAELLEELPPEERLALLRLLPPETAAEVLEELDEDVQaELIEALDPEEAAELLEELDPDDAADLLEELPEEKVEE 80

                          90       100
                  ....*....|....*....|..
gi 496494511  115 LLKRLDKEAKEDVQKLLSYEED 136
Cdd:pfam03448  81 ILSLLDPEERKEIRELLSYPED 102
MgtE_N smart00924
MgtE intracellular N domain; This region is the integral membrane part of the eubacterial MgtE ...
 36-138 2.89e-21

MgtE intracellular N domain; This region is the integral membrane part of the eubacterial MgtE family of magnesium transporters. It is presumed to be an intracellular domain, that may be involved in magnesium binding.


Pssm-ID: 214915 [Multi-domain]  Cd Length: 105  Bit Score: 88.34  E-value: 2.89e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496494511    36 YHERDIANAIVESDKTVRKCIYDILDIADIAEIFSYIEEEP-GKYLEEM-PIEQAAKVVSNMDSDDAMDLFEELNEEDKY 113
Cdd:smart00924   1 LHPADIADLLEELPPEERAELFRLLPPERAAEVLEELDEEVqAELLEALpPDERAAELLEELDPDDAADLLEELPEEVRE 80

                           90       100
                   ....*....|....*....|....*
gi 496494511   114 KLLKRLDKEAKEDVQKLLSYEEDQI 138
Cdd:smart00924  81 ELLSLLDPEEREEIRELLSYPEDTA 105
CBS_pair_Mg_transporter cd04606
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains in the magnesium ...
 136-256 7.14e-21

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: 87.77  E-value: 7.14e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496494511 136 DQIGSCMTNNYIVVRNDVTIREAMSTLVKQAGEHDNIQTLYVIDENGIFAGAIDLKDLIIAREHDNLQDIISSSYPYVYE 215
Cdd:cd04606    1 DSAGRLMTTEFVAVRPDWTVEEALEYLRRLAPDPETIYYIYVVDEDRRLLGVVSLRDLLLADPDTKVSDIMDTDVISVSA 80

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 496494511 216 HEKISECMEILTDYEEDSIPVLTQDKKIAGILTSSDIVELV 256
Cdd:cd04606   81 DDDQEEVARLFAKYDLLALPVVDEEGRLVGIITVDDVLDVI 121
CBS COG0517
CBS domain [Signal transduction mechanisms];
137-260 1.20e-13

CBS domain [Signal transduction mechanisms];


Pssm-ID: 440283 [Multi-domain]  Cd Length: 128  Bit Score: 67.58  E-value: 1.20e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496494511 137 QIGSCMTNNYIVVRNDVTIREAMSTLVKQagehdNIQTLYVIDENGIFAGAIDLKDLIIAREHDN-------LQDIISSS 209
Cdd:COG0517    2 KVKDIMTTDVVTVSPDATVREALELMSEK-----RIGGLPVVDEDGKLVGIVTDRDLRRALAAEGkdlldtpVSEVMTRP 76

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|.
gi 496494511 210 YPYVYEHEKISECMEILTDYEEDSIPVLTQDKKIAGILTSSDIVELVDDEM 260
Cdd:COG0517   77 PVTVSPDTSLEEAAELMEEHKIRRLPVVDDDGRLVGIITIKDLLKALLEPL 127
COG3448 COG3448
CBS-domain-containing membrane protein [Signal transduction mechanisms];
137-263 5.47e-13

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


Pssm-ID: 442671 [Multi-domain]  Cd Length: 136  Bit Score: 66.04  E-value: 5.47e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496494511 137 QIGSCMTNNYIVVRNDVTIREAMSTLVKQagehdNIQTLYVIDENGIFAGAIDLKDLIIAREHDNLQ------------D 204
Cdd:COG3448    3 TVRDIMTRDVVTVSPDTTLREALELMREH-----GIRGLPVVDEDGRLVGIVTERDLLRALLPDRLDeleerlldlpveD 77

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 496494511 205 IISSSYPYVYEHEKISECMEILTDYEEDSIPVLTQDKKIAGILTSSDIVELVDDEMGDD 263
Cdd:COG3448   78 VMTRPVVTVTPDTPLEEAAELMLEHGIHRLPVVDDDGRLVGIVTRTDLLRALARLLEEE 136
CBS_pair_SF cd02205
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains superfamily; The CBS ...
 143-253 7.24e-11

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: 59.18  E-value: 7.24e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496494511 143 TNNYIVVRNDVTIREAMSTLVKqagehDNIQTLYVIDENGIFAGAIDLKDLIIAREHDNLQ------DIISSSYPYVYEH 216
Cdd:cd02205    1 TRDVVTVDPDTTVREALELMAE-----NGIGALPVVDDDGKLVGIVTERDILRALVEGGLAldtpvaEVMTPDVITVSPD 75

                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 496494511 217 EKISECMEILTDYEEDSIPVLTQDKKIAGILTSSDIV 253
Cdd:cd02205   76 TDLEEALELMLEHGIRRLPVVDDDGKLVGIVTRRDIL 112
COG2524 COG2524
Predicted transcriptional regulator, contains C-terminal CBS domains [Transcription];
137-256 2.09e-10

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


Pssm-ID: 442013 [Multi-domain]  Cd Length: 206  Bit Score: 60.28  E-value: 2.09e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496494511 137 QIGSCMTNNYIVVRNDVTIREAMSTLVKQagehdNIQTLYVIDeNGIFAGAIDLKDLIIAREHDNLQ------DIISSSY 210
Cdd:COG2524   87 KVKDIMTKDVITVSPDTTLEEALELMLEK-----GISGLPVVD-DGKLVGIITERDLLKALAEGRDLldapvsDIMTRDV 160

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 496494511 211 PYVYEHEKISECMEILTDYEEDSIPVLTQDKKIAGILTSSDIVELV 256
Cdd:COG2524  161 VTVSEDDSLEEALRLMLEHGIGRLPVVDDDGKLVGIITRTDILRAL 206
COG2905 COG2905
Signal-transduction protein containing cAMP-binding, CBS, and nucleotidyltransferase domains ...
 138-260 8.65e-10

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


Pssm-ID: 442149 [Multi-domain]  Cd Length: 124  Bit Score: 56.38  E-value: 8.65e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496494511 138 IGSCMTNNYIVVRNDVTIREAMSTLVKQagehdNIQTLYVIDENGIFAGAI---DLKDLIIAREHDNLQ----DIISSSY 210
Cdd:COG2905    1 VKDIMSRDVVTVSPDATVREAARLMTEK-----GVGSLVVVDDDGRLVGIItdrDLRRRVLAEGLDPLDtpvsEVMTRPP 75

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|
gi 496494511 211 PYVYEHEKISECMEILTDYEEDSIPVlTQDKKIAGILTSSDIVELVDDEM 260
Cdd:COG2905   76 ITVSPDDSLAEALELMEEHRIRHLPV-VDDGKLVGIVSITDLLRALSEEL 124
CBS_pair_arch_MET2_assoc cd04605
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with the ...
 142-252 7.64e-09

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: 53.40  E-value: 7.64e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496494511 142 MTNNYIVVRNDVTIREAMSTLVKqagehDNIQTLYVIDENGIFAGAIDLKDL--IIAREHDNLQDIISSSYPYVYEHEKI 219
Cdd:cd04605    6 MSKDVATIREDISIEEAAKIMID-----KNVTHLPVVSEDGKLIGIVTSWDIskAVALKKDSLEEIMTRNVITARPDEPI 80

                         90       100       110
                 ....*....|....*....|....*....|...
gi 496494511 220 SECMEILTDYEEDSIPVLTQDKKIAGILTSSDI 252
Cdd:cd04605   81 ELAARKMEKHNISALPVVDDDRRVIGIITSDDI 113
MgtE2 COG1824
Permease, similar to cation transporters [Inorganic ion transport and metabolism];
288-459 5.17e-08

Permease, similar to cation transporters [Inorganic ion transport and metabolism];


Pssm-ID: 441429  Cd Length: 188  Bit Score: 52.94  E-value: 5.17e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496494511 288 LPWLIALLFLGMAVSSVVGMFESIVAVLPIVICFQSLVLDMAGNVGTqSLA-----------VTIRVLMDenlsgkkkia 356
Cdd:COG1824   15 LPVLLVLAVGGIIAGLVLEGMEELLLAYPGLLVLVPAFLGTRGNLGG-ILGarlstalhlglLEPRLRPD---------- 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496494511 357 llfKEMKIGFLNGASLAIMALVFLGVYIHLFKHYAWISSFLISGCVGISLIVAM---VISSLVGTIIPMFFHKINIDPAV 433
Cdd:COG1824   84 ---RRLLNNILATLILALLISPLIGVLAWLVAVLLGRGSLGLLTLVGIALLAGLllaLLLIVVTYYVAIASYRFGLDPDN 160

                        170       180
                 ....*....|....*....|....*.
gi 496494511 434 ASGPLITTINDLVAVITYYGLSGLVL 459
Cdd:COG1824  161 VVIPVVTTLGDVFGVLFLILVARLVL 186
YtoI COG4109
Predicted transcriptional regulator containing CBS domains [Transcription];
138-254 8.30e-08

Predicted transcriptional regulator containing CBS domains [Transcription];


Pssm-ID: 443285 [Multi-domain]  Cd Length: 135  Bit Score: 51.07  E-value: 8.30e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496494511 138 IGSCMTN-NYIVVRNDVTIREAMSTLVKQAgeHDNIQtlyVIDENGIFAGAIDLKDLIIAREHDNLQDIISSSYPYVYEH 216
Cdd:COG4109   18 VEDIMTLeDVATLSEDDTVEDALELLEKTG--HSRFP---VVDENGRLVGIVTSKDILGKDDDTPIEDVMTKNPITVTPD 92

                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 496494511 217 EKISECMEILTDYEEDSIPVLTQDKKIAGILTSSDIVE 254
Cdd:COG4109   93 TSLASAAHKMIWEGIELLPVVDDDGRLLGIISRQDVLK 130
CBS_pair_bac cd04629
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains present in bacteria; ...
 142-252 5.42e-07

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


Pssm-ID: 341392 [Multi-domain]  Cd Length: 116  Bit Score: 48.20  E-value: 5.42e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496494511 142 MTNNYIVVRNDVTIREAMSTLVKQagehdNIQTLYVIDENGIFAGAIDlkdliiarEHDNLQDIISSSYpYVYEHEKISE 221
Cdd:cd04629    1 MTRNPVTLTPDTSILEAVELLLEH-----KISGAPVVDEQGRLVGFLS--------EQDCLKALLEASY-HCEPGGTVAD 66

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 496494511 222 CM--EILTDYEEDSI---------------PVLtQDKKIAGILTSSDI 252
Cdd:cd04629   67 YMstEVLTVSPDTSIvdlaqlflknkprryPVV-EDGKLVGQISRRDV 113
CBS_pair_ABC_OpuCA_assoc cd04583
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains found associated with ...
 144-256 5.77e-07

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


Pssm-ID: 341360 [Multi-domain]  Cd Length: 110  Bit Score: 47.90  E-value: 5.77e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496494511 144 NNYIVVRNDVTIREAMSTLvkqageHDN-IQTLYVIDENGIFAGAIDLKDL-IIAREHDNLQDIISSSYPYVYEHEKISE 221
Cdd:cd04583    2 TNPVTITPERTLAQAIEIM------REKrVDSLLVVDKDNVLLGIVDIEDInRNYRKAKKVGEIMERDVFTVKEDSLLRD 75

                         90       100       110
                 ....*....|....*....|....*....|....*
gi 496494511 222 CMEILTDYEEDSIPVLTQDKKIAGILTSSDIVELV 256
Cdd:cd04583   76 TVDRILKRGLKYVPVVDEQGRLVGLVTRASLVDIV 110
CBS_pair_peptidase_M50 cd04639
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains found in the ...
 142-255 5.88e-07

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: 48.34  E-value: 5.88e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496494511 142 MTNNYIVVRNDVTIREAMSTLVkqAGEHDNiQTLYVIDENGIFAGAIDLKDLI-IAREHDN---LQDIISS--SYPYVYE 215
Cdd:cd04639    3 MVTEFPIVDADLTLREFADDYL--IGKKSW-REFLVTDEAGRLVGLITVDDLRaIPTSQWPdtpVRELMKPleEIPTVAA 79

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 496494511 216 HEKISECMEILTDYEEDSIPVLTQDKKIAGILTSSDIVEL 255
Cdd:cd04639   80 DQSLLEVVKLLEEQQLPALAVVSENGTLVGLIEKEDIIEL 119
CBS_pair_bac cd17783
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains present in bacteria; ...
 180-254 1.81e-06

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


Pssm-ID: 341419 [Multi-domain]  Cd Length: 108  Bit Score: 46.41  E-value: 1.81e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496494511 180 ENGIFAGAIDLKDLIiarEHDNLQDIISSS-----YPYVYEHEKISECMEILTDYEEDSIPVLTQDKKIAGILTSSDIVE 254
Cdd:cd17783   32 DNGQYLGLISEDDLL---ELNDPEAPLSNLplslkDVFVYEDQHFYDVIRLASEYKLEVVPVLDEENEYLGVITVNDLLA 108
CBS_pair_CcpN cd04617
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains of CcpN repressor; ...
 147-255 2.13e-06

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


Pssm-ID: 341387 [Multi-domain]  Cd Length: 125  Bit Score: 46.71  E-value: 2.13e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496494511 147 IVVRNDVTIREAMSTLVKQagehdNIQTLYVIDENGIFAGAIDLKDLI-IAREHDNLQDI----ISSSYP---YVYEHEK 218
Cdd:cd04617    7 VVVDETTSVYDAIVTLFLE-----DVGSLFVVDEEGYLVGVVSRKDLLkATLGGQDLEKTpvsmIMTRMPnivTVTPDDS 81

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 496494511 219 ISECMEILTDYEEDSIPVLTQDK---KIAGILTSSDIVEL 255
Cdd:cd04617   82 VLEAARKLIEHEIDSLPVVEKEDgklKVVGRITKTNITRL 121
CBS pfam00571
CBS domain; CBS domains are small intracellular modules that pair together to form a stable ...
 202-258 2.88e-06

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


Pssm-ID: 425756 [Multi-domain]  Cd Length: 57  Bit Score: 44.51  E-value: 2.88e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 496494511  202 LQDIISSSYPYVYEHEKISECMEILTDYEEDSIPVLTQDKKIAGILTSSDIVELVDD 258
Cdd:pfam00571   1 VKDIMTKDVVTVSPDTTLEEALELMREHGISRLPVVDEDGKLVGIVTLKDLLRALLG 57
CBS_pair_HPP_assoc cd04600
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with the ...
 142-253 3.83e-05

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


Pssm-ID: 341375 [Multi-domain]  Cd Length: 133  Bit Score: 43.32  E-value: 3.83e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496494511 142 MTNNYIVVRNDVTIREAMSTLVKQagehdNIQTLYVIDENGIFAGAIDLKDLIIAREHDNLQ------------------ 203
Cdd:cd04600    1 MSRDVVTVTPDTSLEEAWRLLRRH-----RIKALPVVDRARRLVGIVTLADLLKHADLDPPRglrgrlrrtlglrrdrpe 75

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|...
gi 496494511 204 ---DIISSSYPYVYEHEKISECMEILTDYEEDSIPVLTQDKKIAGILTSSDIV 253
Cdd:cd04600   76 tvgDIMTRPVVTVRPDTPIAELVPLFSDGGLHHIPVVDADGRLVGIVTQSDLI 128
CBS COG0517
CBS domain [Signal transduction mechanisms];
201-262 1.39e-04

CBS domain [Signal transduction mechanisms];


Pssm-ID: 440283 [Multi-domain]  Cd Length: 128  Bit Score: 41.39  E-value: 1.39e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 496494511 201 NLQDIISSSYPYVYEHEKISECMEILTDYEEDSIPVLTQDKKIAGILTSSDIVELVDDEMGD 262
Cdd:COG0517    2 KVKDIMTTDVVTVSPDATVREALELMSEKRIGGLPVVDEDGKLVGIVTDRDLRRALAAEGKD 63
CBS_pair_arch cd09836
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains; The CBS domain, ...
 142-256 1.87e-04

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: 40.97  E-value: 1.87e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496494511 142 MTNNYIVVRNDVTIREAMSTLVKQagehdNIQTLYVIDENGIFAGAIDLKDLI--IAREHDN---LQDIISSSYPYVYEH 216
Cdd:cd09836    1 MSKPVVTVPPETTIREAAKLMAEN-----NIGSVVVVDDDGKPVGIVTERDIVraVAEGIDLdtpVEEIMTKNLVTVSPD 75

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 496494511 217 EKISECMEILTDYEEDSIPVLTQDKKIAGILTSSDIVELV 256
Cdd:cd09836   76 ESIYEAAELMREHNIRHLPVVDGGGKLVGVISIRDLAREL 115
CBS pfam00571
CBS domain; CBS domains are small intracellular modules that pair together to form a stable ...
 138-199 3.16e-04

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


Pssm-ID: 425756 [Multi-domain]  Cd Length: 57  Bit Score: 38.73  E-value: 3.16e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 496494511  138 IGSCMTNNYIVVRNDVTIREAMSTLVKQagehdNIQTLYVIDENGIFAGAIDLKDLIIAREH 199
Cdd:pfam00571   1 VKDIMTKDVVTVSPDTTLEEALELMREH-----GISRLPVVDEDGKLVGIVTLKDLLRALLG 57
CBS_pair_ParBc_assoc cd04610
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with a ...
 142-253 7.07e-04

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


Pssm-ID: 341383 [Multi-domain]  Cd Length: 108  Bit Score: 39.23  E-value: 7.07e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496494511 142 MTNNYIVVRNDVTIREAMSTLVKqaGEHDNiqtlYVIDENGIFAGAIDLKDLIIAREHDNLQDIISSSYPYVYEHEKISE 221
Cdd:cd04610    1 MTRDVITVSPDDTVKDVIKLIKE--TGHDG----FPVVDDGKVVGYVTAKDLLGKDDDEKVSEIMSRDTVVADPDMDITD 74

                         90       100       110
                 ....*....|....*....|....*....|..
gi 496494511 222 CMEILTDYEEDSIPVLTQDKKIAGILTSSDIV 253
Cdd:cd04610   75 AARVIFRSGISKLPVVDDEGNLVGIITNMDVI 106
YtoI COG4109
Predicted transcriptional regulator containing CBS domains [Transcription];
194-259 7.85e-04

Predicted transcriptional regulator containing CBS domains [Transcription];


Pssm-ID: 443285 [Multi-domain]  Cd Length: 135  Bit Score: 39.51  E-value: 7.85e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 496494511 194 IIAREHDNLQDII-------SSSYPYVYEHEKISECMEILTDYEEDSIPVLTQDKKIAGILTSSDIVELVDDE 259
Cdd:COG4109    4 IISTSYDTFKEILlvedimtLEDVATLSEDDTVEDALELLEKTGHSRFPVVDENGRLVGIVTSKDILGKDDDT 76
CBS_pair_arch2_repeat1 cd04638
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains present in archaea, ...
 177-253 8.06e-04

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


Pssm-ID: 341396 [Multi-domain]  Cd Length: 109  Bit Score: 38.86  E-value: 8.06e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 496494511 177 VIDENGIFAGAIDLKDLIIAREHDNLQDIISSSYPYVYEHEKISECMEILTDYEEDSIPVLtQDKKIAGILTSSDIV 253
Cdd:cd04638   32 VKKETGKLVGIVTRKDLLRNPDEEQIALLMSRDPITISPDDTLSEAAELMLEHNIRRVPVV-DDDKLVGIVTVADLV 107
COG2905 COG2905
Signal-transduction protein containing cAMP-binding, CBS, and nucleotidyltransferase domains ...
 202-269 8.41e-04

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


Pssm-ID: 442149 [Multi-domain]  Cd Length: 124  Bit Score: 39.04  E-value: 8.41e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 496494511 202 LQDIISSSYPYVYEHEKISECMEILTDYEEDSIPVLTQDKKIAGILTSSDIVELVDDEMGDDYAKLAG 269
Cdd:COG2905    1 VKDIMSRDVVTVSPDATVREAARLMTEKGVGSLVVVDDDGRLVGIITDRDLRRRVLAEGLDPLDTPVS 68
COG3448 COG3448
CBS-domain-containing membrane protein [Signal transduction mechanisms];
98-194 1.21e-03

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


Pssm-ID: 442671 [Multi-domain]  Cd Length: 136  Bit Score: 39.08  E-value: 1.21e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496494511  98 DDAMDLFEE--------LNEEDKYK-------LLKRLDKEAKEDVQKLLSyeEDQIGSCMTNNYIVVRNDVTIREAMSTL 162
Cdd:COG3448   22 REALELMREhgirglpvVDEDGRLVgivterdLLRALLPDRLDELEERLL--DLPVEDVMTRPVVTVTPDTPLEEAAELM 99

                         90       100       110
                 ....*....|....*....|....*....|..
gi 496494511 163 VKQagehdNIQTLYVIDENGIFAGAIDLKDLI 194
Cdd:COG3448  100 LEH-----GIHRLPVVDDDGRLVGIVTRTDLL 126
CBS_pair_ACT cd17787
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains found in Thermatoga ...
 143-254 1.33e-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: 38.55  E-value: 1.33e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496494511 143 TNNYIVVRNDVTIREAMSTLVKQagEHDNIqtlYVIDENGIFAGAIDLKDLIIAREHDNLQDIISSSYPYVYEHEKISEC 222
Cdd:cd17787    1 NRDFPTFEESATVGEVLHEMRKY--ETDYC---IVVDEEGKFAGMVRKSKIMDEDLDKKVKEYVVEPDFYCHEEDYIEDA 75

                         90       100       110
                 ....*....|....*....|....*....|..
gi 496494511 223 MEILTDYEEDSIPVLTQDKKIAGILTSSDIVE 254
Cdd:cd17787   76 ALLLIESHEFVLPVVNSDMKVKGVLTVFEILE 107
YtoI COG4109
Predicted transcriptional regulator containing CBS domains [Transcription];
134-194 3.11e-03

Predicted transcriptional regulator containing CBS domains [Transcription];


Pssm-ID: 443285 [Multi-domain]  Cd Length: 135  Bit Score: 37.97  E-value: 3.11e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 496494511 134 EEDQIGSCMTNNYIVVRNDVTIREAMSTLVkqageHDNIQTLYVIDENGIFAGAIDLKDLI 194
Cdd:COG4109   74 DDTPIEDVMTKNPITVTPDTSLASAAHKMI-----WEGIELLPVVDDDGRLLGIISRQDVL 129
COG3448 COG3448
CBS-domain-containing membrane protein [Signal transduction mechanisms];
204-271 3.74e-03

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


Pssm-ID: 442671 [Multi-domain]  Cd Length: 136  Bit Score: 37.54  E-value: 3.74e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 496494511 204 DIISSSYPYVYEHEKISECMEILTDYEEDSIPVLTQDKKIAGILTSSDIVE-LVDDEMGDDYAKLAGLT 271
Cdd:COG3448    6 DIMTRDVVTVSPDTTLREALELMREHGIRGLPVVDEDGRLVGIVTERDLLRaLLPDRLDELEERLLDLP 74
CBS_arch_repeat1 cd17777
CBS pair domains found in archeal proteins, repeat 1; CBS pair domains found in archeal ...
 192-253 4.05e-03

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


Pssm-ID: 341413 [Multi-domain]  Cd Length: 137  Bit Score: 37.71  E-value: 4.05e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 496494511 192 DLIIAREHDNLQDIISSSYPYVYEHEKISECMEILTDYEEDSIPVLTQDKKIAGILTSSDIV 253
Cdd:cd17777   73 DLYSALNREVVETIMTPNPVYVYEDSDLIEALTIMVTRGIGSLPVVDRDGRPVGIVTERDLV 134
COG2524 COG2524
Predicted transcriptional regulator, contains C-terminal CBS domains [Transcription];
204-278 4.33e-03

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


Pssm-ID: 442013 [Multi-domain]  Cd Length: 206  Bit Score: 38.33  E-value: 4.33e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496494511 204 DIISSSYPYVYEHEKISECMEILTDYEEDSIPVLtQDKKIAGILTSSDIVELVDDEMGDDYAKLAGL--------TEEED 275
Cdd:COG2524   90 DIMTKDVITVSPDTTLEEALELMLEKGISGLPVV-DDGKLVGIITERDLLKALAEGRDLLDAPVSDImtrdvvtvSEDDS 168


                 ...
gi 496494511 276 LNE 278
Cdd:COG2524  169 LEE 171
CBS_archAMPK_gamma-repeat2 cd04631
CBS pair domains found in archeal 5'-AMP-activated protein kinase gamma subunit-like proteins; ...
 234-318 4.44e-03

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


Pssm-ID: 341394 [Multi-domain]  Cd Length: 130  Bit Score: 37.21  E-value: 4.44e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496494511 234 IPVLtQDKKIAGILTSSDIVELVDDemGDDYAKLAGLTEEEDLNEPTIVSMKKRLPWLIALLFLGMAVSSvvgMFESIVA 313
Cdd:cd04631   34 LPVV-SDGKLVGIVTSTDIMRYLGS--GEAFEKLKTGNIHEVLNVPISSIMKRDIITTTPDTDLGEAAEL---MLEKNIG 107


                 ....*
gi 496494511 314 VLPIV 318
Cdd:cd04631  108 ALPVV 112
CBS_pair_SF cd02205
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains superfamily; The CBS ...
 207-259 6.92e-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: 36.45  E-value: 6.92e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|...
gi 496494511 207 SSSYPYVYEHEKISECMEILTDYEEDSIPVLTQDKKIAGILTSSDIVELVDDE 259
Cdd:cd02205    1 TRDVVTVDPDTTVREALELMAENGIGALPVVDDDGKLVGIVTERDILRALVEG 53
COG2524 COG2524
Predicted transcriptional regulator, contains C-terminal CBS domains [Transcription];
125-196 7.78e-03

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


Pssm-ID: 442013 [Multi-domain]  Cd Length: 206  Bit Score: 37.56  E-value: 7.78e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 496494511 125 EDVQKLLS----YEEDQIGSCMTNNYIVVRNDVTIREAMSTLVKQagehdNIQTLYVIDENGIFAGAIDLKDLIIA 196
Cdd:COG2524  135 RDLLKALAegrdLLDAPVSDIMTRDVVTVSEDDSLEEALRLMLEH-----GIGRLPVVDDDGKLVGIITRTDILRA 205
 
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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