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Conserved domains on  [gi|873899472|ref|WP_048605905|]
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MULTISPECIES: magnesium transporter [Vibrio]

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];
9-451 1.45e-180

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


:

Pssm-ID: 441840 [Multi-domain]  Cd Length: 443  Bit Score: 511.53  E-value: 1.45e-180
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 873899472   9 QAHQTLQEVSEALENGRFVHVRRQLQDMEPEDIAHLLEASPRKSRDVLWQLTDPEDYGEILDELNEDVKDALVSKMAPET 88
Cdd:COG2239    1 ETEELLEELRELLEEGDLEELRELLEELHPADIAELLEELPPEERLALFRLLPKELAAEVLEELDEEVQEELLEELSDEE 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 873899472  89 LAEATEGMETDDVAYVLRSLPDDVSREVLSQMDSVDRALVETALSYPEDSAGAIMNTDVITIRGDVDVDVVLRYMRMRGE 168
Cdd:COG2239   81 LAELLEELDPDDAADLLEELPEEVVEELLALLDPEEREEIRELLSYPEDSAGRLMTTEFVAVREDWTVGEALRYLRRQAE 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 873899472 169 LPDATDALYVIDEEERLIGNLSLTTLVTTQPDVAVSEVMEDADEAIAVETSASDIASLFERRNWVSAPVVDSNQHLVGRI 248
Cdd:COG2239  161 DPETIYYIYVVDDDGRLVGVVSLRDLLLADPDTKVSDIMDTDVISVPADDDQEEVARLFERYDLLALPVVDEEGRLVGII 240

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 873899472 249 TIDDVVDVIREDAEHSMMSMAGMDDDEDTFAPVVKSARRRSVWLGANVLAALAAASVSNMFEATLDQMAAIAVLMTIVPS 328
Cdd:COG2239  241 TVDDVVDVIEEEATEDILKLAGVSEDEDLFASVLKLARKRLPWLLILLLTAFLAASVIGLFEDTLEQVVALAVFMPLVAG 320

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 873899472 329 MGGVAGNQTVALVIRGLALGHIGDSNKRELLLKEAAIGFLNGVLWAVIIGGIVVAWKGNWILGGIISAAMMTNLIVAGIA 408
Cdd:COG2239  321 MGGNAGSQSLTVVVRGLALGEITLSDWWRVLLKELLVGLLNGLILGLVVGLVAYLWFGNPLLGLVVGLALVINVLVAALA 400

                        410       420       430       440
                 ....*....|....*....|....*....|....*....|...
gi 873899472 409 GVTIPVMLKKMNIDPALAGGMALTTVTDVIGLSVFLGLATILI 451
Cdd:COG2239  401 GSLLPLLLKRLGIDPAVASGPFITTITDVVGFFIYLGLATLFL 443
 
Name Accession Description Interval E-value
MgtE COG2239
Mg/Co/Ni transporter MgtE (contains CBS domain) [Inorganic ion transport and metabolism];
9-451 1.45e-180

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


Pssm-ID: 441840 [Multi-domain]  Cd Length: 443  Bit Score: 511.53  E-value: 1.45e-180
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 873899472   9 QAHQTLQEVSEALENGRFVHVRRQLQDMEPEDIAHLLEASPRKSRDVLWQLTDPEDYGEILDELNEDVKDALVSKMAPET 88
Cdd:COG2239    1 ETEELLEELRELLEEGDLEELRELLEELHPADIAELLEELPPEERLALFRLLPKELAAEVLEELDEEVQEELLEELSDEE 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 873899472  89 LAEATEGMETDDVAYVLRSLPDDVSREVLSQMDSVDRALVETALSYPEDSAGAIMNTDVITIRGDVDVDVVLRYMRMRGE 168
Cdd:COG2239   81 LAELLEELDPDDAADLLEELPEEVVEELLALLDPEEREEIRELLSYPEDSAGRLMTTEFVAVREDWTVGEALRYLRRQAE 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 873899472 169 LPDATDALYVIDEEERLIGNLSLTTLVTTQPDVAVSEVMEDADEAIAVETSASDIASLFERRNWVSAPVVDSNQHLVGRI 248
Cdd:COG2239  161 DPETIYYIYVVDDDGRLVGVVSLRDLLLADPDTKVSDIMDTDVISVPADDDQEEVARLFERYDLLALPVVDEEGRLVGII 240

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 873899472 249 TIDDVVDVIREDAEHSMMSMAGMDDDEDTFAPVVKSARRRSVWLGANVLAALAAASVSNMFEATLDQMAAIAVLMTIVPS 328
Cdd:COG2239  241 TVDDVVDVIEEEATEDILKLAGVSEDEDLFASVLKLARKRLPWLLILLLTAFLAASVIGLFEDTLEQVVALAVFMPLVAG 320

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 873899472 329 MGGVAGNQTVALVIRGLALGHIGDSNKRELLLKEAAIGFLNGVLWAVIIGGIVVAWKGNWILGGIISAAMMTNLIVAGIA 408
Cdd:COG2239  321 MGGNAGSQSLTVVVRGLALGEITLSDWWRVLLKELLVGLLNGLILGLVVGLVAYLWFGNPLLGLVVGLALVINVLVAALA 400

                        410       420       430       440
                 ....*....|....*....|....*....|....*....|...
gi 873899472 409 GVTIPVMLKKMNIDPALAGGMALTTVTDVIGLSVFLGLATILI 451
Cdd:COG2239  401 GSLLPLLLKRLGIDPAVASGPFITTITDVVGFFIYLGLATLFL 443
mgtE TIGR00400
Mg2+ transporter (mgtE); This family of prokaryotic proteins models a class of Mg++ ...
 21-451 1.05e-71

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: 233.18  E-value: 1.05e-71
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 873899472   21 LENGRFVHVRRQLQDMEPEDIAHLLEASPRKSRDVLWQLTDPEDYGEILDELNEDVKDALVSKMAPETLAEATEGMETDD 100
Cdd:TIGR00400  15 LKEKSYSKIKEKFLK*QP*DIAEALKRLPGTELILLYRFLPKKIAVDTFSNLDQSTQNKLLNSFTNKEISEMINEMNLDD 94

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 873899472  101 VAYVLRSLPDDVSREVLSQMDSVDRALVETALSYPEDSAGAIMNTDVITIRGDVDVDVVLRYMRMRGELPDATDALYVID 180
Cdd:TIGR00400  95 VIDLLEEVPANVVQQLLASSTEEERKAINLLLSYSDDSAGRIMTIEYVELKEDYTVGKALDYIRRVAKTKEDIYTLYVTN 174

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 873899472  181 EEERLIGNLSLTTLVTTQPDVAVSEVMEDADEAIAVETSASDIASLFERRNWVSAPVVDSNQHLVGRITIDDVVDVI-RE 259
Cdd:TIGR00400 175 ESKHLKGVLSIRDLILAKPEEILSSIMRSSVFSIVGVNDQEEVARLIQKYDFLAVPVVDNEGRLVGIVTVDDIIDVIqSE 254

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 873899472  260 DAEHSMMSMAGMDDDEDTF-APVVKSARRRSVWLGANVLAALAAASVSNMFEATLDQMAAIAVLMTIVPSMGGVAGNQTV 338
Cdd:TIGR00400 255 ATEDFYMIAAVKPLDDSYFdTSILVMAKNRIIWLLVLLVSSTFTATIISNYEDLLLSLVALANFIPLLMDTSGNAGSQSS 334

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 873899472  339 ALVIRGLALGHIGDSNKRELLLKEAAIGFLNGVLWAVIIGGIVVAWKGNWILGGIISAAMMTNLIVAGIAGVTIPVMLKK 418
Cdd:TIGR00400 335 AVVIRGLALETVKVKDFFKVILREICVSILVGAILASVNFLRIVFFQGKLLIAFVVSSSLFVSLTVAKILGGLLPIVAKL 414

                         410       420       430
                  ....*....|....*....|....*....|...
gi 873899472  419 MNIDPALAGGMALTTVTDVIGLSVFLGLATILI 451
Cdd:TIGR00400 415 LKLDPALMSGPLITTIADALTLIIYFNIAKWVL 447
CBS_pair_Mg_transporter cd04606
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains in the magnesium ...
 137-257 1.31e-41

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: 143.63  E-value: 1.31e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 873899472 137 DSAGAIMNTDVITIRGDVDVDVVLRYMRMRGELPDATDALYVIDEEERLIGNLSLTTLVTTQPDVAVSEVMEDADEAIAV 216
Cdd:cd04606    1 DSAGRLMTTEFVAVRPDWTVEEALEYLRRLAPDPETIYYIYVVDEDRRLLGVVSLRDLLLADPDTKVSDIMDTDVISVSA 80

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 873899472 217 ETSASDIASLFERRNWVSAPVVDSNQHLVGRITIDDVVDVI 257
Cdd:cd04606   81 DDDQEEVARLFAKYDLLALPVVDEEGRLVGIITVDDVLDVI 121
MgtE pfam01769
Divalent cation transporter; This region is the integral membrane part of the eubacterial MgtE ...
 323-446 3.08e-37

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: 132.18  E-value: 3.08e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 873899472  323 MTIVPSMGGVAGNQTVALVIRGLALGHIGDSNKRELLLKEAAIGFLNGVLWAVIIGGIVVAWKGNWILGGIISAAMMTNL 402
Cdd:pfam01769   1 IPVILGLGGNLGSQSASRLSRALALGEIEPRDAWRVLLKELLVGLLLGLVLGLIAGVLAFLWFGGLLLGLVVGLALLLAV 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 873899472  403 IVAGIAGVTIPVMLKKMNIDPALAGGMALTTVTDVIGLSVFLGL 446
Cdd:pfam01769  81 LIALLLGTLLPLLLWRLGLDPDNASGPLITTLGDLLGLLILFGI 124
MgtE_N smart00924
MgtE intracellular N domain; This region is the integral membrane part of the eubacterial MgtE ...
 36-139 5.42e-29

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: 109.53  E-value: 5.42e-29
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 873899472    36 MEPEDIAHLLEASPRKSRDVLWQLTDPEDYGEILDELNEDVKDALVSKMAP-ETLAEATEGMETDDVAYVLRSLPDDVSR 114
Cdd:smart00924   1 LHPADIADLLEELPPEERAELFRLLPPERAAEVLEELDEEVQAELLEALPPdERAAELLEELDPDDAADLLEELPEEVRE 80

                           90       100
                   ....*....|....*....|....*
gi 873899472   115 EVLSQMDSVDRALVETALSYPEDSA 139
Cdd:smart00924  81 ELLSLLDPEEREEIRELLSYPEDTA 105
 
Name Accession Description Interval E-value
MgtE COG2239
Mg/Co/Ni transporter MgtE (contains CBS domain) [Inorganic ion transport and metabolism];
9-451 1.45e-180

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


Pssm-ID: 441840 [Multi-domain]  Cd Length: 443  Bit Score: 511.53  E-value: 1.45e-180
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 873899472   9 QAHQTLQEVSEALENGRFVHVRRQLQDMEPEDIAHLLEASPRKSRDVLWQLTDPEDYGEILDELNEDVKDALVSKMAPET 88
Cdd:COG2239    1 ETEELLEELRELLEEGDLEELRELLEELHPADIAELLEELPPEERLALFRLLPKELAAEVLEELDEEVQEELLEELSDEE 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 873899472  89 LAEATEGMETDDVAYVLRSLPDDVSREVLSQMDSVDRALVETALSYPEDSAGAIMNTDVITIRGDVDVDVVLRYMRMRGE 168
Cdd:COG2239   81 LAELLEELDPDDAADLLEELPEEVVEELLALLDPEEREEIRELLSYPEDSAGRLMTTEFVAVREDWTVGEALRYLRRQAE 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 873899472 169 LPDATDALYVIDEEERLIGNLSLTTLVTTQPDVAVSEVMEDADEAIAVETSASDIASLFERRNWVSAPVVDSNQHLVGRI 248
Cdd:COG2239  161 DPETIYYIYVVDDDGRLVGVVSLRDLLLADPDTKVSDIMDTDVISVPADDDQEEVARLFERYDLLALPVVDEEGRLVGII 240

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 873899472 249 TIDDVVDVIREDAEHSMMSMAGMDDDEDTFAPVVKSARRRSVWLGANVLAALAAASVSNMFEATLDQMAAIAVLMTIVPS 328
Cdd:COG2239  241 TVDDVVDVIEEEATEDILKLAGVSEDEDLFASVLKLARKRLPWLLILLLTAFLAASVIGLFEDTLEQVVALAVFMPLVAG 320

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 873899472 329 MGGVAGNQTVALVIRGLALGHIGDSNKRELLLKEAAIGFLNGVLWAVIIGGIVVAWKGNWILGGIISAAMMTNLIVAGIA 408
Cdd:COG2239  321 MGGNAGSQSLTVVVRGLALGEITLSDWWRVLLKELLVGLLNGLILGLVVGLVAYLWFGNPLLGLVVGLALVINVLVAALA 400

                        410       420       430       440
                 ....*....|....*....|....*....|....*....|...
gi 873899472 409 GVTIPVMLKKMNIDPALAGGMALTTVTDVIGLSVFLGLATILI 451
Cdd:COG2239  401 GSLLPLLLKRLGIDPAVASGPFITTITDVVGFFIYLGLATLFL 443
mgtE TIGR00400
Mg2+ transporter (mgtE); This family of prokaryotic proteins models a class of Mg++ ...
 21-451 1.05e-71

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: 233.18  E-value: 1.05e-71
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 873899472   21 LENGRFVHVRRQLQDMEPEDIAHLLEASPRKSRDVLWQLTDPEDYGEILDELNEDVKDALVSKMAPETLAEATEGMETDD 100
Cdd:TIGR00400  15 LKEKSYSKIKEKFLK*QP*DIAEALKRLPGTELILLYRFLPKKIAVDTFSNLDQSTQNKLLNSFTNKEISEMINEMNLDD 94

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 873899472  101 VAYVLRSLPDDVSREVLSQMDSVDRALVETALSYPEDSAGAIMNTDVITIRGDVDVDVVLRYMRMRGELPDATDALYVID 180
Cdd:TIGR00400  95 VIDLLEEVPANVVQQLLASSTEEERKAINLLLSYSDDSAGRIMTIEYVELKEDYTVGKALDYIRRVAKTKEDIYTLYVTN 174

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 873899472  181 EEERLIGNLSLTTLVTTQPDVAVSEVMEDADEAIAVETSASDIASLFERRNWVSAPVVDSNQHLVGRITIDDVVDVI-RE 259
Cdd:TIGR00400 175 ESKHLKGVLSIRDLILAKPEEILSSIMRSSVFSIVGVNDQEEVARLIQKYDFLAVPVVDNEGRLVGIVTVDDIIDVIqSE 254

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 873899472  260 DAEHSMMSMAGMDDDEDTF-APVVKSARRRSVWLGANVLAALAAASVSNMFEATLDQMAAIAVLMTIVPSMGGVAGNQTV 338
Cdd:TIGR00400 255 ATEDFYMIAAVKPLDDSYFdTSILVMAKNRIIWLLVLLVSSTFTATIISNYEDLLLSLVALANFIPLLMDTSGNAGSQSS 334

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 873899472  339 ALVIRGLALGHIGDSNKRELLLKEAAIGFLNGVLWAVIIGGIVVAWKGNWILGGIISAAMMTNLIVAGIAGVTIPVMLKK 418
Cdd:TIGR00400 335 AVVIRGLALETVKVKDFFKVILREICVSILVGAILASVNFLRIVFFQGKLLIAFVVSSSLFVSLTVAKILGGLLPIVAKL 414

                         410       420       430
                  ....*....|....*....|....*....|...
gi 873899472  419 MNIDPALAGGMALTTVTDVIGLSVFLGLATILI 451
Cdd:TIGR00400 415 LKLDPALMSGPLITTIADALTLIIYFNIAKWVL 447
CBS_pair_Mg_transporter cd04606
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains in the magnesium ...
 137-257 1.31e-41

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: 143.63  E-value: 1.31e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 873899472 137 DSAGAIMNTDVITIRGDVDVDVVLRYMRMRGELPDATDALYVIDEEERLIGNLSLTTLVTTQPDVAVSEVMEDADEAIAV 216
Cdd:cd04606    1 DSAGRLMTTEFVAVRPDWTVEEALEYLRRLAPDPETIYYIYVVDEDRRLLGVVSLRDLLLADPDTKVSDIMDTDVISVSA 80

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 873899472 217 ETSASDIASLFERRNWVSAPVVDSNQHLVGRITIDDVVDVI 257
Cdd:cd04606   81 DDDQEEVARLFAKYDLLALPVVDEEGRLVGIITVDDVLDVI 121
MgtE pfam01769
Divalent cation transporter; This region is the integral membrane part of the eubacterial MgtE ...
 323-446 3.08e-37

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: 132.18  E-value: 3.08e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 873899472  323 MTIVPSMGGVAGNQTVALVIRGLALGHIGDSNKRELLLKEAAIGFLNGVLWAVIIGGIVVAWKGNWILGGIISAAMMTNL 402
Cdd:pfam01769   1 IPVILGLGGNLGSQSASRLSRALALGEIEPRDAWRVLLKELLVGLLLGLVLGLIAGVLAFLWFGGLLLGLVVGLALLLAV 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 873899472  403 IVAGIAGVTIPVMLKKMNIDPALAGGMALTTVTDVIGLSVFLGL 446
Cdd:pfam01769  81 LIALLLGTLLPLLLWRLGLDPDNASGPLITTLGDLLGLLILFGI 124
MgtE_N smart00924
MgtE intracellular N domain; This region is the integral membrane part of the eubacterial MgtE ...
 36-139 5.42e-29

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: 109.53  E-value: 5.42e-29
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 873899472    36 MEPEDIAHLLEASPRKSRDVLWQLTDPEDYGEILDELNEDVKDALVSKMAP-ETLAEATEGMETDDVAYVLRSLPDDVSR 114
Cdd:smart00924   1 LHPADIADLLEELPPEERAELFRLLPPERAAEVLEELDEEVQAELLEALPPdERAAELLEELDPDDAADLLEELPEEVRE 80

                           90       100
                   ....*....|....*....|....*
gi 873899472   115 EVLSQMDSVDRALVETALSYPEDSA 139
Cdd:smart00924  81 ELLSLLDPEEREEIRELLSYPEDTA 105
MgtE_N pfam03448
MgtE intracellular N domain; This domain is found at the N-terminus of eubacterial magnesium ...
 36-137 2.47e-27

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: 104.94  E-value: 2.47e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 873899472   36 MEPEDIAHLLEASPRKSRDVLWQLTDPEDYGEILDELNEDVKDALVSKMAPETLAEATEGMETDDVAYVLRSLPDDVSRE 115
Cdd:pfam03448   1 LHPADIAELLEELPPEERLALLRLLPPETAAEVLEELDEDVQAELIEALDPEEAAELLEELDPDDAADLLEELPEEKVEE 80

                          90       100
                  ....*....|....*....|..
gi 873899472  116 VLSQMDSVDRALVETALSYPED 137
Cdd:pfam03448  81 ILSLLDPEERKEIRELLSYPED 102
CBS_pair_SF cd02205
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains superfamily; The CBS ...
 144-255 1.77e-12

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: 63.80  E-value: 1.77e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 873899472 144 NTDVITIRGDVDVDVVLRYMRMRGelpdaTDALYVIDEEERLIGNLSLTTLVT------TQPDVAVSEVMEDADEAIAVE 217
Cdd:cd02205    1 TRDVVTVDPDTTVREALELMAENG-----IGALPVVDDDGKLVGIVTERDILRalveggLALDTPVAEVMTPDVITVSPD 75

                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 873899472 218 TSASDIASLFERRNWVSAPVVDSNQHLVGRITIDDVVD 255
Cdd:cd02205   76 TDLEEALELMLEHGIRRLPVVDDDGKLVGIVTRRDILR 113
COG3448 COG3448
CBS-domain-containing membrane protein [Signal transduction mechanisms];
142-264 4.39e-12

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


Pssm-ID: 442671 [Multi-domain]  Cd Length: 136  Bit Score: 63.35  E-value: 4.39e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 873899472 142 IMNTDVITIRGDVDVDVVLRYMRMRGelpdaTDALYVIDEEERLIGNLS------------LTTLVTTQPDVAVSEVMED 209
Cdd:COG3448    7 IMTRDVVTVSPDTTLREALELMREHG-----IRGLPVVDEDGRLVGIVTerdllrallpdrLDELEERLLDLPVEDVMTR 81

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 873899472 210 ADEAIAVETSASDIASLFERRNWVSAPVVDSNQHLVGRITIDDVVDVIREDAEHS 264
Cdd:COG3448   82 PVVTVTPDTPLEEAAELMLEHGIHRLPVVDDDGRLVGIVTRTDLLRALARLLEEE 136
CBS COG0517
CBS domain [Signal transduction mechanisms];
139-262 6.34e-11

CBS domain [Signal transduction mechanisms];


Pssm-ID: 440283 [Multi-domain]  Cd Length: 128  Bit Score: 59.88  E-value: 6.34e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 873899472 139 AGAIMNTDVITIRGDVDVDVVLRYMRMRGelpdaTDALYVIDEEERLIGNLSLTTLV-------TTQPDVAVSEVMEDAD 211
Cdd:COG0517    3 VKDIMTTDVVTVSPDATVREALELMSEKR-----IGGLPVVDEDGKLVGIVTDRDLRralaaegKDLLDTPVSEVMTRPP 77

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|.
gi 873899472 212 EAIAVETSASDIASLFERRNWVSAPVVDSNQHLVGRITIDDVVDVIREDAE 262
Cdd:COG0517   78 VTVSPDTSLEEAAELMEEHKIRRLPVVDDDGRLVGIITIKDLLKALLEPLA 128
COG2524 COG2524
Predicted transcriptional regulator, contains C-terminal CBS domains [Transcription];
119-257 3.76e-09

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


Pssm-ID: 442013 [Multi-domain]  Cd Length: 206  Bit Score: 56.43  E-value: 3.76e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 873899472 119 QMDSVDRALVETALSYPEDSAGAIMNTDVITIRGDVDVDVVLRYMRMRGelpdaTDALYVIDEEeRLIGNLSLTTLV--- 195
Cdd:COG2524   68 QAAAVRVVAEKELGLVLKMKVKDIMTKDVITVSPDTTLEEALELMLEKG-----ISGLPVVDDG-KLVGIITERDLLkal 141

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 873899472 196 ---TTQPDVAVSEVMEDADEAIAVETSASDIASLFERRNWVSAPVVDSNQHLVGRITIDDVVDVI 257
Cdd:COG2524  142 aegRDLLDAPVSDIMTRDVVTVSEDDSLEEALRLMLEHGIGRLPVVDDDGKLVGIITRTDILRAL 206
YtoI COG4109
Predicted transcriptional regulator containing CBS domains [Transcription];
140-254 2.11e-08

Predicted transcriptional regulator containing CBS domains [Transcription];


Pssm-ID: 443285 [Multi-domain]  Cd Length: 135  Bit Score: 52.61  E-value: 2.11e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 873899472 140 GAIM-NTDVITIRGDVDVDVVLRYMRMRGElpdatDALYVIDEEERLIGNLSLTTLVTTQPDVAVSEVMEDADEAIAVET 218
Cdd:COG4109   19 EDIMtLEDVATLSEDDTVEDALELLEKTGH-----SRFPVVDENGRLVGIVTSKDILGKDDDTPIEDVMTKNPITVTPDT 93

                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 873899472 219 SASDIASLFERRNWVSAPVVDSNQHLVGRITIDDVV 254
Cdd:COG4109   94 SLASAAHKMIWEGIELLPVVDDDGRLLGIISRQDVL 129
COG2905 COG2905
Signal-transduction protein containing cAMP-binding, CBS, and nucleotidyltransferase domains ...
 142-260 2.34e-08

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


Pssm-ID: 442149 [Multi-domain]  Cd Length: 124  Bit Score: 52.14  E-value: 2.34e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 873899472 142 IMNTDVITIRGDVDVDVVLRYMRMRGelpdaTDALYVIDEEERLIGNLSLTTLVT-------TQPDVAVSEVMEDADEAI 214
Cdd:COG2905    4 IMSRDVVTVSPDATVREAARLMTEKG-----VGSLVVVDDDGRLVGIITDRDLRRrvlaeglDPLDTPVSEVMTRPPITV 78

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 873899472 215 AVETSASDIASLFERRNWVSAPVVDsNQHLVGRITIDDVVDVIRED 260
Cdd:COG2905   79 SPDDSLAEALELMEEHRIRHLPVVD-DGKLVGIVSITDLLRALSEE 123
CBS_pair_ABC_OpuCA_assoc cd04583
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains found associated with ...
 144-256 7.31e-06

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: 44.82  E-value: 7.31e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 873899472 144 NTDVITIRGDVDVDVVLRYMRMRGelpdaTDALYVIDEEERLIGNLSLTTLVTT-QPDVAVSEVMEDADEAIAVETSASD 222
Cdd:cd04583    1 ITNPVTITPERTLAQAIEIMREKR-----VDSLLVVDKDNVLLGIVDIEDINRNyRKAKKVGEIMERDVFTVKEDSLLRD 75

                         90       100       110
                 ....*....|....*....|....*....|....
gi 873899472 223 IASLFERRNWVSAPVVDSNQHLVGRITIDDVVDV 256
Cdd:cd04583   76 TVDRILKRGLKYVPVVDEQGRLVGLVTRASLVDI 109
CBS pfam00571
CBS domain; CBS domains are small intracellular modules that pair together to form a stable ...
 203-259 1.32e-05

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: 42.59  E-value: 1.32e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 873899472  203 VSEVMEDADEAIAVETSASDIASLFERRNWVSAPVVDSNQHLVGRITIDDVVDVIRE 259
Cdd:pfam00571   1 VKDIMTKDVVTVSPDTTLEEALELMREHGISRLPVVDEDGKLVGIVTLKDLLRALLG 57
CBS_pair_HPP_assoc cd04600
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with the ...
 143-254 1.55e-04

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: 41.39  E-value: 1.55e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 873899472 143 MNTDVITIRGDVDVDVVLRYMRMRGelpdaTDALYVIDEEERLIGNLSLTTL---------------------VTTQPDV 201
Cdd:cd04600    1 MSRDVVTVTPDTSLEEAWRLLRRHR-----IKALPVVDRARRLVGIVTLADLlkhadldpprglrgrlrrtlgLRRDRPE 75

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|...
gi 873899472 202 AVSEVMEDADEAIAVETSASDIASLFERRNWVSAPVVDSNQHLVGRITIDDVV 254
Cdd:cd04600   76 TVGDIMTRPVVTVRPDTPIAELVPLFSDGGLHHIPVVDADGRLVGIVTQSDLI 128
CBS COG0517
CBS domain [Signal transduction mechanisms];
203-265 2.65e-04

CBS domain [Signal transduction mechanisms];


Pssm-ID: 440283 [Multi-domain]  Cd Length: 128  Bit Score: 40.62  E-value: 2.65e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 873899472 203 VSEVMEDADEAIAVETSASDIASLFERRNWVSAPVVDSNQHLVGRITIDDVVDVIREDAEHSM 265
Cdd:COG0517    3 VKDIMTTDVVTVSPDATVREALELMSEKRIGGLPVVDEDGKLVGIVTDRDLRRALAAEGKDLL 65
CBS_pair_NTP_transferase_assoc cd04607
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domain associated with the ...
 178-253 3.24e-04

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: 40.12  E-value: 3.24e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 873899472 178 VIDEEERLIG-------------NLSLttlvttqpDVAVSEVMEDADEAIAVETSASDIASLFERRNWVSAPVVDSNQHL 244
Cdd:cd04607   30 VVDENRKLLGtvtdgdirrgllkGLSL--------DAPVEEVMNKNPITASPSTSREELLALMRAKKILQLPIVDEQGRV 101


                 ....*....
gi 873899472 245 VGRITIDDV 253
Cdd:cd04607  102 VGLETLDDL 110
CBS pfam00571
CBS domain; CBS domains are small intracellular modules that pair together to form a stable ...
 139-195 3.25e-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: 38.35  E-value: 3.25e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 873899472  139 AGAIMNTDVITIRGDVDVDVVLRYMRMRGelpdaTDALYVIDEEERLIGNLSLTTLV 195
Cdd:pfam00571   1 VKDIMTKDVVTVSPDTTLEEALELMREHG-----ISRLPVVDEDGKLVGIVTLKDLL 52
CBS_pair_arch cd09836
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains; The CBS domain, ...
 143-257 3.28e-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: 40.20  E-value: 3.28e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 873899472 143 MNTDVITIRGDVDVDVVLRYMRMRGelpdaTDALYVIDEEERLIGNLSLTTLVT-----TQPDVAVSEVMEDADEAIAVE 217
Cdd:cd09836    1 MSKPVVTVPPETTIREAAKLMAENN-----IGSVVVVDDDGKPVGIVTERDIVRavaegIDLDTPVEEIMTKNLVTVSPD 75

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 873899472 218 TSASDIASLFERRNWVSAPVVDSNQHLVGRITIDDVVDVI 257
Cdd:cd09836   76 ESIYEAAELMREHNIRHLPVVDGGGKLVGVISIRDLAREL 115
CBS_pair_peptidase_M50 cd04639
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains found in the ...
 177-254 3.67e-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: 40.25  E-value: 3.67e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 873899472 177 YVIDEEERLIGNLSLTTL--VTTQ--PDVAVSEVMEDADEAIAVETSAS--DIASLFERRNWVSAPVVDSNQHLVGRITI 250
Cdd:cd04639   34 LVTDEAGRLVGLITVDDLraIPTSqwPDTPVRELMKPLEEIPTVAADQSllEVVKLLEEQQLPALAVVSENGTLVGLIEK 113


                 ....
gi 873899472 251 DDVV 254
Cdd:cd04639  114 EDII 117
CBS COG0517
CBS domain [Signal transduction mechanisms];
116-195 4.42e-04

CBS domain [Signal transduction mechanisms];


Pssm-ID: 440283 [Multi-domain]  Cd Length: 128  Bit Score: 40.23  E-value: 4.42e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 873899472 116 VLSQMDsVDRALVETALSYPEDSAGAIMNTDVITIRGDVDVDVVLRYMRMRGelpdaTDALYVIDEEERLIGNLSLTTLV 195
Cdd:COG0517   47 IVTDRD-LRRALAAEGKDLLDTPVSEVMTRPPVTVSPDTSLEEAAELMEEHK-----IRRLPVVDDDGRLVGIITIKDLL 120
MgtE2 COG1824
Permease, similar to cation transporters [Inorganic ion transport and metabolism];
308-451 5.77e-04

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


Pssm-ID: 441429  Cd Length: 188  Bit Score: 40.62  E-value: 5.77e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 873899472 308 MFEATLDQMAAIAVLMTIVPSMGGVAGNQTVALVIR---GLALGHIG---DSNKRelLLKEAAIGFLNGVLWAVIIGgiV 381
Cdd:COG1824   31 VLEGMEELLLAYPGLLVLVPAFLGTRGNLGGILGARlstALHLGLLEprlRPDRR--LLNNILATLILALLISPLIG--V 106

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 873899472 382 VAW----------KGNWILGGIISAAMMTNLIVAGIAGVTIPVMLKKMNIDPALAGGMALTTVTDVIGLSVFLGLATILI 451
Cdd:COG1824  107 LAWlvavllgrgsLGLLTLVGIALLAGLLLALLLIVVTYYVAIASYRFGLDPDNVVIPVVTTLGDVFGVLFLILVARLVL 186
CBS_pair_CBS cd04608
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with the ...
 146-249 6.48e-04

Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with the pyridoxal-phosphate (PALP) dependent enzyme domain; This cd contains two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with the pyridoxal-phosphate (PALP) dependent enzyme domain upstream. Cystathionine beta-synthase (CBS ) contains, besides the C-terminal regulatory CBS-pair, an N-terminal heme-binding module, followed by a pyridoxal phosphate (PLP) domain, which houses the active site. It is the first enzyme in the transsulfuration pathway, catalyzing the conversion of serine and homocysteine to cystathionine and water. In general, CBS domains usually occur in tandem repeats. They associate to form a so-called Bateman domain or a CBS pair based on crystallographic studies in bacteria. The CBS pair was used as a basis for this cd hierarchy since the human CBS proteins can adopt the typical core structure and form an intramolecular CBS pair. The interface between the two CBS domains forms a cleft that is a potential ligand binding site. The CBS pair coexists with a variety of other functional domains and this has been used to help in its classification here. It has been proposed that the CBS domain may play a regulatory role, although its exact function is unknown. Mutations of conserved residues within this domain are associated with a variety of human hereditary diseases, including congenital myotonia, idiopathic generalized epilepsy, hypercalciuric nephrolithiasis, and classic Bartter syndrome (CLC chloride channel family members), Wolff-Parkinson-White syndrome (gamma 2 subunit of AMP-activated protein kinase), retinitis pigmentosa (IMP dehydrogenase-1), and homocystinuria (cystathionine beta-synthase).


Pssm-ID: 341382 [Multi-domain]  Cd Length: 120  Bit Score: 39.44  E-value: 6.48e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 873899472 146 DVITIRGDVDVDVVLRYMRMRGelpdaTDALYVIDEEERLIGNLSLTTLVT------TQPDVAVSEVMEDADEAIAVETS 219
Cdd:cd04608   11 APVTVLPDDTLGEAIEIMREYG-----VDQLPVVDEDGRVVGMVTEGNLLSsllagrAQPSDPVSKAMYKQFKQVDLDTP 85

                         90       100       110
                 ....*....|....*....|....*....|
gi 873899472 220 ASDIASLFERRNwvSAPVVDSNQHLVGRIT 249
Cdd:cd04608   86 LGALSRILERDH--FALVVDGQGKVLGIVT 113
CBS_pair_ParBc_assoc cd04610
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with a ...
 143-254 6.77e-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: 6.77e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 873899472 143 MNTDVITIRGDVDVDVVLRYMRMRGElpdatDALYVIDEEeRLIGNLSLTTLVTTQPDVAVSEVMEDADEAIAVETSASD 222
Cdd:cd04610    1 MTRDVITVSPDDTVKDVIKLIKETGH-----DGFPVVDDG-KVVGYVTAKDLLGKDDDEKVSEIMSRDTVVADPDMDITD 74

                         90       100       110
                 ....*....|....*....|....*....|..
gi 873899472 223 IASLFERRNWVSAPVVDSNQHLVGRITIDDVV 254
Cdd:cd04610   75 AARVIFRSGISKLPVVDDEGNLVGIITNMDVI 106
CBS smart00116
Domain in cystathionine beta-synthase and other proteins; Domain present in all 3 forms of ...
 218-257 9.83e-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: 37.11  E-value: 9.83e-04
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|
gi 873899472   218 TSASDIASLFERRNWVSAPVVDSNQHLVGRITIDDVVDVI 257
Cdd:smart00116   9 TTLEEALELLRENGIRRLPVVDEEGRLVGIVTRRDIIKAL 48
CBS_pair_bac cd04629
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains present in bacteria; ...
 143-253 1.30e-03

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


Pssm-ID: 341392 [Multi-domain]  Cd Length: 116  Bit Score: 38.57  E-value: 1.30e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 873899472 143 MNTDVITIRGDVDVDVVLRYM---RMRGeLPdatdalyVIDEEERLIGNLS----LTTLVTT----QPDVAVSEVMEDAD 211
Cdd:cd04629    1 MTRNPVTLTPDTSILEAVELLlehKISG-AP-------VVDEQGRLVGFLSeqdcLKALLEAsyhcEPGGTVADYMSTEV 72

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 873899472 212 EAIAVETSASDIASLFERRNWVSAPVVDSNQhLVGRITIDDV 253
Cdd:cd04629   73 LTVSPDTSIVDLAQLFLKNKPRRYPVVEDGK-LVGQISRRDV 113
CBS_pair_SF cd02205
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains superfamily; The CBS ...
 125-195 1.46e-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: 38.38  E-value: 1.46e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 873899472 125 RALVETALSYPEDSAGAIMNTDVITIRGDVDVDVVLRYMRMRGelpdaTDALYVIDEEERLIGNLSLTTLV 195
Cdd:cd02205   47 LRALVEGGLALDTPVAEVMTPDVITVSPDTDLEEALELMLEHG-----IRRLPVVDDDGKLVGIVTRRDIL 112
COG3448 COG3448
CBS-domain-containing membrane protein [Signal transduction mechanisms];
116-187 2.89e-03

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


Pssm-ID: 442671 [Multi-domain]  Cd Length: 136  Bit Score: 37.92  E-value: 2.89e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 873899472 116 VLSQMD----SVDRALVETALSYPEDSAGAIMNTDVITIRGDVDVDVVLRYMRMRGElpdatDALYVIDEEERLIG 187
Cdd:COG3448   48 IVTERDllraLLPDRLDELEERLLDLPVEDVMTRPVVTVTPDTPLEEAAELMLEHGI-----HRLPVVDDDGRLVG 118
YtoI COG4109
Predicted transcriptional regulator containing CBS domains [Transcription];
203-267 3.67e-03

Predicted transcriptional regulator containing CBS domains [Transcription];


Pssm-ID: 443285 [Multi-domain]  Cd Length: 135  Bit Score: 37.58  E-value: 3.67e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 873899472 203 VSEVMEDAD-EAIAVETSASDIASLFERRNWVSAPVVDSNQHLVGRITIDDVVDVIREDAEHSMMS 267
Cdd:COG4109   18 VEDIMTLEDvATLSEDDTVEDALELLEKTGHSRFPVVDENGRLVGIVTSKDILGKDDDTPIEDVMT 83
CBS_pair_ACT cd17787
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains found in Thermatoga ...
 144-259 4.00e-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: 37.01  E-value: 4.00e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 873899472 144 NTDVITIRGDVDVDVVLRYMRMRGelpdaTDALYVIDEEERLIGNLSLTTLVTTQPDVAVSEVMEDADEAIAVETSASDI 223
Cdd:cd17787    1 NRDFPTFEESATVGEVLHEMRKYE-----TDYCIVVDEEGKFAGMVRKSKIMDEDLDKKVKEYVVEPDFYCHEEDYIEDA 75

                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 873899472 224 ASLFERRNWVSAPVVDSNQHLVGRITIDDVVDVIRE 259
Cdd:cd17787   76 ALLLIESHEFVLPVVNSDMKVKGVLTVFEILEALME 111
COG3448 COG3448
CBS-domain-containing membrane protein [Signal transduction mechanisms];
203-265 7.10e-03

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


Pssm-ID: 442671 [Multi-domain]  Cd Length: 136  Bit Score: 36.77  E-value: 7.10e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 873899472 203 VSEVMEDADEAIAVETSASDIASLFERRNWVSAPVVDSNQHLVGRITIDDVVDVIREDAEHSM 265
Cdd:COG3448    4 VRDIMTRDVVTVSPDTTLREALELMREHGIRGLPVVDEDGRLVGIVTERDLLRALLPDRLDEL 66
CBS_pair_arch_MET2_assoc cd04605
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with the ...
 142-253 8.04e-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: 36.06  E-value: 8.04e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 873899472 142 IMNTDVITIRGDVDVDVVLRYMrmrgeLPDATDALYVIDEEERLIGnlslttlVTTQPDV--AVSEVMEDADEAIA--VE 217
Cdd:cd04605    5 IMSKDVATIREDISIEEAAKIM-----IDKNVTHLPVVSEDGKLIG-------IVTSWDIskAVALKKDSLEEIMTrnVI 72

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 873899472 218 TSASD-----IASLFERRNWVSAPVVDSNQHLVGRITIDDV 253
Cdd:cd04605   73 TARPDepielAARKMEKHNISALPVVDDDRRVIGIITSDDI 113
CBS_pair_arch cd09836
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains; The CBS domain, ...
 135-195 9.22e-03

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: 35.96  E-value: 9.22e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 873899472 135 PEDSAGAIMNTDVITIRGDVDVDVVLRYMRMRG--ELPdatdalyVIDEEERLIGNLSLTTLV 195
Cdd:cd09836   57 LDTPVEEIMTKNLVTVSPDESIYEAAELMREHNirHLP-------VVDGGGKLVGVISIRDLA 112
 
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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