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Conserved domains on  [gi|1402841403|ref|WP_110711405|]
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MULTISPECIES: magnesium transporter [Stenotrophomonas]

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 0e+00

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


:

Pssm-ID: 441840 [Multi-domain]  Cd Length: 443  Bit Score: 523.48  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1402841403   9 KTARQLRMLSDALDSGRLGPVRRLVNTLAPAEIGNLLESLPPGKREVVWGLVDPEDDGEVLVHVGEDVRESLLADMDPDE 88
Cdd:COG2239     1 ETEELLEELRELLEEGDLEELRELLEELHPADIAELLEELPPEERLALFRLLPKELAAEVLEELDEEVQEELLEELSDEE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1402841403  89 IIAAVEDLDIDDLADLVEDLPDTVIDEVLKSMDRENRERLEQVLSYPEDSAGRLMNPDVVTVRADVNVDVVLRYLRLRGE 168
Cdd:COG2239    81 LAELLEELDPDDAADLLEELPEEVVEELLALLDPEEREEIRELLSYPEDSAGRLMTTEFVAVREDWTVGEALRYLRRQAE 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1402841403 169 LPDHTDHLFVVSRRHQYLGRVSLAALVTHEDTTPINRLIDDEQPAIDVGESDQEVARQFSDHDWISAPVVDENNILVGRI 248
Cdd:COG2239   161 DPETIYYIYVVDDDGRLVGVVSLRDLLLADPDTKVSDIMDTDVISVPADDDQEEVARLFERYDLLALPVVDEEGRLVGII 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1402841403 249 TIDDVVDIIRGQAEHQALGAAGLDEDEDLFSPVWRAMRRRLMWLSVNLCTAFLASSVVGHFEGTIDKLVALAVLMPIVAG 328
Cdd:COG2239   241 TVDDVVDVIEEEATEDILKLAGVSEDEDLFASVLKLARKRLPWLLILLLTAFLAASVIGLFEDTLEQVVALAVFMPLVAG 320

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1402841403 329 LGGNAGTQVLALMVRGLALGQVGASNARTLLWKEVRVAALNGLLLGSILGLIVLAWFHSPGLSAVIAIALTCNLLFAALA 408
Cdd:COG2239   321 MGGNAGSQSLTVVVRGLALGEITLSDWWRVLLKELLVGLLNGLILGLVVGLVAYLWFGNPLLGLVVGLALVINVLVAALA 400

                         410       420       430       440
                  ....*....|....*....|....*....|....*....|...
gi 1402841403 409 GVLVPLTLKRFGFDPALASGIFLTAVTDSMGFFTFLGLATLVL 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 0e+00

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


Pssm-ID: 441840 [Multi-domain]  Cd Length: 443  Bit Score: 523.48  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1402841403   9 KTARQLRMLSDALDSGRLGPVRRLVNTLAPAEIGNLLESLPPGKREVVWGLVDPEDDGEVLVHVGEDVRESLLADMDPDE 88
Cdd:COG2239     1 ETEELLEELRELLEEGDLEELRELLEELHPADIAELLEELPPEERLALFRLLPKELAAEVLEELDEEVQEELLEELSDEE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1402841403  89 IIAAVEDLDIDDLADLVEDLPDTVIDEVLKSMDRENRERLEQVLSYPEDSAGRLMNPDVVTVRADVNVDVVLRYLRLRGE 168
Cdd:COG2239    81 LAELLEELDPDDAADLLEELPEEVVEELLALLDPEEREEIRELLSYPEDSAGRLMTTEFVAVREDWTVGEALRYLRRQAE 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1402841403 169 LPDHTDHLFVVSRRHQYLGRVSLAALVTHEDTTPINRLIDDEQPAIDVGESDQEVARQFSDHDWISAPVVDENNILVGRI 248
Cdd:COG2239   161 DPETIYYIYVVDDDGRLVGVVSLRDLLLADPDTKVSDIMDTDVISVPADDDQEEVARLFERYDLLALPVVDEEGRLVGII 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1402841403 249 TIDDVVDIIRGQAEHQALGAAGLDEDEDLFSPVWRAMRRRLMWLSVNLCTAFLASSVVGHFEGTIDKLVALAVLMPIVAG 328
Cdd:COG2239   241 TVDDVVDVIEEEATEDILKLAGVSEDEDLFASVLKLARKRLPWLLILLLTAFLAASVIGLFEDTLEQVVALAVFMPLVAG 320

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1402841403 329 LGGNAGTQVLALMVRGLALGQVGASNARTLLWKEVRVAALNGLLLGSILGLIVLAWFHSPGLSAVIAIALTCNLLFAALA 408
Cdd:COG2239   321 MGGNAGSQSLTVVVRGLALGEITLSDWWRVLLKELLVGLLNGLILGLVVGLVAYLWFGNPLLGLVVGLALVINVLVAALA 400

                         410       420       430       440
                  ....*....|....*....|....*....|....*....|...
gi 1402841403 409 GVLVPLTLKRFGFDPALASGIFLTAVTDSMGFFTFLGLATLVL 451
Cdd:COG2239   401 GSLLPLLLKRLGIDPAVASGPFITTITDVVGFFIYLGLATLFL 443
mgtE TIGR00400
Mg2+ transporter (mgtE); This family of prokaryotic proteins models a class of Mg++ ...
 21-451 3.61e-63

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: 210.84  E-value: 3.61e-63
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1402841403  21 LDSGRLGPVRRLVNTLAPAEIGNLLESLPPGKREVVWGLVDPEDDGEVLVHVGEDVRESLLADMDPDEIIAAVEDLDIDD 100
Cdd:TIGR00400  15 LKEKSYSKIKEKFLK*QP*DIAEALKRLPGTELILLYRFLPKKIAVDTFSNLDQSTQNKLLNSFTNKEISEMINEMNLDD 94

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1402841403 101 LADLVEDLPDTVIDEVLKSMDRENRERLEQVLSYPEDSAGRLMNPDVVTVRADVNVDVVLRYLRLRGELPDHTDHLFVVS 180
Cdd:TIGR00400  95 VIDLLEEVPANVVQQLLASSTEEERKAINLLLSYSDDSAGRIMTIEYVELKEDYTVGKALDYIRRVAKTKEDIYTLYVTN 174

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1402841403 181 RRHQYLGRVSLAALVTHEDTTPINRLIDDEQPAIDVGESDQEVARQFSDHDWISAPVVDENNILVGRITIDDVVDIIRGQ 260
Cdd:TIGR00400 175 ESKHLKGVLSIRDLILAKPEEILSSIMRSSVFSIVGVNDQEEVARLIQKYDFLAVPVVDNEGRLVGIVTVDDIIDVIQSE 254

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1402841403 261 A--EHQALGAAGLDEDEDLFSPVWRAMRRRLMWLSVNLCTAFLASSVVGHFEGTIDKLVALAVLMPIVAGLGGNAGTQVL 338
Cdd:TIGR00400 255 AteDFYMIAAVKPLDDSYFDTSILVMAKNRIIWLLVLLVSSTFTATIISNYEDLLLSLVALANFIPLLMDTSGNAGSQSS 334

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1402841403 339 ALMVRGLALGQVGASNARTLLWKEVRVAALNGLLLGSILGLIVLAWFHSPGLSAVIAIALTCNLLFAALAGVLVPLTLKR 418
Cdd:TIGR00400 335 AVVIRGLALETVKVKDFFKVILREICVSILVGAILASVNFLRIVFFQGKLLIAFVVSSSLFVSLTVAKILGGLLPIVAKL 414

                         410       420       430
                  ....*....|....*....|....*....|...
gi 1402841403 419 FGFDPALASGIFLTAVTDSMGFFTFLGLATLVL 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 2.13e-43

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: 148.64  E-value: 2.13e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1402841403 137 DSAGRLMNPDVVTVRADVNVDVVLRYLRLRGELPDHTDHLFVVSRRHQYLGRVSLAALVTHEDTTPINRLIDDEQPAIDV 216
Cdd:cd04606     1 DSAGRLMTTEFVAVRPDWTVEEALEYLRRLAPDPETIYYIYVVDEDRRLLGVVSLRDLLLADPDTKVSDIMDTDVISVSA 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 1402841403 217 GESDQEVARQFSDHDWISAPVVDENNILVGRITIDDVVDII 257
Cdd:cd04606    81 DDDQEEVARLFAKYDLLALPVVDEEGRLVGIITVDDVLDVI 121
MgtE pfam01769
Divalent cation transporter; This region is the integral membrane part of the eubacterial MgtE ...
 323-446 3.24e-35

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: 126.79  E-value: 3.24e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1402841403 323 MPIVAGLGGNAGTQVLALMVRGLALGQVGASNARTLLWKEVRVAALNGLLLGSILGLIVLAWFHSPGLSAVIAIALTCNL 402
Cdd:pfam01769   1 IPVILGLGGNLGSQSASRLSRALALGEIEPRDAWRVLLKELLVGLLLGLVLGLIAGVLAFLWFGGLLLGLVVGLALLLAV 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 1402841403 403 LFAALAGVLVPLTLKRFGFDPALASGIFLTAVTDSMGFFTFLGL 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 4.47e-25

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: 98.74  E-value: 4.47e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1402841403   36 LAPAEIGNLLESLPPGKREVVWGLVDPEDDGEVLVHVGEDVRESLLADMDPDEIIA-AVEDLDIDDLADLVEDLPDTVID 114
Cdd:smart00924   1 LHPADIADLLEELPPEERAELFRLLPPERAAEVLEELDEEVQAELLEALPPDERAAeLLEELDPDDAADLLEELPEEVRE 80

                           90       100
                   ....*....|....*....|....*
gi 1402841403  115 EVLKSMDRENRERLEQVLSYPEDSA 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 0e+00

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


Pssm-ID: 441840 [Multi-domain]  Cd Length: 443  Bit Score: 523.48  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1402841403   9 KTARQLRMLSDALDSGRLGPVRRLVNTLAPAEIGNLLESLPPGKREVVWGLVDPEDDGEVLVHVGEDVRESLLADMDPDE 88
Cdd:COG2239     1 ETEELLEELRELLEEGDLEELRELLEELHPADIAELLEELPPEERLALFRLLPKELAAEVLEELDEEVQEELLEELSDEE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1402841403  89 IIAAVEDLDIDDLADLVEDLPDTVIDEVLKSMDRENRERLEQVLSYPEDSAGRLMNPDVVTVRADVNVDVVLRYLRLRGE 168
Cdd:COG2239    81 LAELLEELDPDDAADLLEELPEEVVEELLALLDPEEREEIRELLSYPEDSAGRLMTTEFVAVREDWTVGEALRYLRRQAE 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1402841403 169 LPDHTDHLFVVSRRHQYLGRVSLAALVTHEDTTPINRLIDDEQPAIDVGESDQEVARQFSDHDWISAPVVDENNILVGRI 248
Cdd:COG2239   161 DPETIYYIYVVDDDGRLVGVVSLRDLLLADPDTKVSDIMDTDVISVPADDDQEEVARLFERYDLLALPVVDEEGRLVGII 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1402841403 249 TIDDVVDIIRGQAEHQALGAAGLDEDEDLFSPVWRAMRRRLMWLSVNLCTAFLASSVVGHFEGTIDKLVALAVLMPIVAG 328
Cdd:COG2239   241 TVDDVVDVIEEEATEDILKLAGVSEDEDLFASVLKLARKRLPWLLILLLTAFLAASVIGLFEDTLEQVVALAVFMPLVAG 320

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1402841403 329 LGGNAGTQVLALMVRGLALGQVGASNARTLLWKEVRVAALNGLLLGSILGLIVLAWFHSPGLSAVIAIALTCNLLFAALA 408
Cdd:COG2239   321 MGGNAGSQSLTVVVRGLALGEITLSDWWRVLLKELLVGLLNGLILGLVVGLVAYLWFGNPLLGLVVGLALVINVLVAALA 400

                         410       420       430       440
                  ....*....|....*....|....*....|....*....|...
gi 1402841403 409 GVLVPLTLKRFGFDPALASGIFLTAVTDSMGFFTFLGLATLVL 451
Cdd:COG2239   401 GSLLPLLLKRLGIDPAVASGPFITTITDVVGFFIYLGLATLFL 443
mgtE TIGR00400
Mg2+ transporter (mgtE); This family of prokaryotic proteins models a class of Mg++ ...
 21-451 3.61e-63

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: 210.84  E-value: 3.61e-63
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1402841403  21 LDSGRLGPVRRLVNTLAPAEIGNLLESLPPGKREVVWGLVDPEDDGEVLVHVGEDVRESLLADMDPDEIIAAVEDLDIDD 100
Cdd:TIGR00400  15 LKEKSYSKIKEKFLK*QP*DIAEALKRLPGTELILLYRFLPKKIAVDTFSNLDQSTQNKLLNSFTNKEISEMINEMNLDD 94

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1402841403 101 LADLVEDLPDTVIDEVLKSMDRENRERLEQVLSYPEDSAGRLMNPDVVTVRADVNVDVVLRYLRLRGELPDHTDHLFVVS 180
Cdd:TIGR00400  95 VIDLLEEVPANVVQQLLASSTEEERKAINLLLSYSDDSAGRIMTIEYVELKEDYTVGKALDYIRRVAKTKEDIYTLYVTN 174

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1402841403 181 RRHQYLGRVSLAALVTHEDTTPINRLIDDEQPAIDVGESDQEVARQFSDHDWISAPVVDENNILVGRITIDDVVDIIRGQ 260
Cdd:TIGR00400 175 ESKHLKGVLSIRDLILAKPEEILSSIMRSSVFSIVGVNDQEEVARLIQKYDFLAVPVVDNEGRLVGIVTVDDIIDVIQSE 254

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1402841403 261 A--EHQALGAAGLDEDEDLFSPVWRAMRRRLMWLSVNLCTAFLASSVVGHFEGTIDKLVALAVLMPIVAGLGGNAGTQVL 338
Cdd:TIGR00400 255 AteDFYMIAAVKPLDDSYFDTSILVMAKNRIIWLLVLLVSSTFTATIISNYEDLLLSLVALANFIPLLMDTSGNAGSQSS 334

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1402841403 339 ALMVRGLALGQVGASNARTLLWKEVRVAALNGLLLGSILGLIVLAWFHSPGLSAVIAIALTCNLLFAALAGVLVPLTLKR 418
Cdd:TIGR00400 335 AVVIRGLALETVKVKDFFKVILREICVSILVGAILASVNFLRIVFFQGKLLIAFVVSSSLFVSLTVAKILGGLLPIVAKL 414

                         410       420       430
                  ....*....|....*....|....*....|...
gi 1402841403 419 FGFDPALASGIFLTAVTDSMGFFTFLGLATLVL 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 2.13e-43

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: 148.64  E-value: 2.13e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1402841403 137 DSAGRLMNPDVVTVRADVNVDVVLRYLRLRGELPDHTDHLFVVSRRHQYLGRVSLAALVTHEDTTPINRLIDDEQPAIDV 216
Cdd:cd04606     1 DSAGRLMTTEFVAVRPDWTVEEALEYLRRLAPDPETIYYIYVVDEDRRLLGVVSLRDLLLADPDTKVSDIMDTDVISVSA 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 1402841403 217 GESDQEVARQFSDHDWISAPVVDENNILVGRITIDDVVDII 257
Cdd:cd04606    81 DDDQEEVARLFAKYDLLALPVVDEEGRLVGIITVDDVLDVI 121
MgtE pfam01769
Divalent cation transporter; This region is the integral membrane part of the eubacterial MgtE ...
 323-446 3.24e-35

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: 126.79  E-value: 3.24e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1402841403 323 MPIVAGLGGNAGTQVLALMVRGLALGQVGASNARTLLWKEVRVAALNGLLLGSILGLIVLAWFHSPGLSAVIAIALTCNL 402
Cdd:pfam01769   1 IPVILGLGGNLGSQSASRLSRALALGEIEPRDAWRVLLKELLVGLLLGLVLGLIAGVLAFLWFGGLLLGLVVGLALLLAV 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 1402841403 403 LFAALAGVLVPLTLKRFGFDPALASGIFLTAVTDSMGFFTFLGL 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 4.47e-25

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: 98.74  E-value: 4.47e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1402841403   36 LAPAEIGNLLESLPPGKREVVWGLVDPEDDGEVLVHVGEDVRESLLADMDPDEIIA-AVEDLDIDDLADLVEDLPDTVID 114
Cdd:smart00924   1 LHPADIADLLEELPPEERAELFRLLPPERAAEVLEELDEEVQAELLEALPPDERAAeLLEELDPDDAADLLEELPEEVRE 80

                           90       100
                   ....*....|....*....|....*
gi 1402841403  115 EVLKSMDRENRERLEQVLSYPEDSA 139
Cdd:smart00924  81 ELLSLLDPEEREEIRELLSYPEDTA 105
MgtE_N pfam03448
MgtE intracellular N domain; This domain is found at the N-terminus of eubacterial magnesium ...
 38-137 2.45e-21

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: 88.38  E-value: 2.45e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1402841403  38 PAEIGNLLESLPPGKREVVWGLVDPEDDGEVLVHVGEDVRESLLADMDPDEIIAAVEDLDIDDLADLVEDLPDTVIDEVL 117
Cdd:pfam03448   3 PADIAELLEELPPEERLALLRLLPPETAAEVLEELDEDVQAELIEALDPEEAAELLEELDPDDAADLLEELPEEKVEEIL 82

                          90       100
                  ....*....|....*....|
gi 1402841403 118 KSMDRENRERLEQVLSYPED 137
Cdd:pfam03448  83 SLLDPEERKEIRELLSYPED 102
COG3448 COG3448
CBS-domain-containing membrane protein [Signal transduction mechanisms];
142-264 3.65e-09

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


Pssm-ID: 442671 [Multi-domain]  Cd Length: 136  Bit Score: 54.87  E-value: 3.65e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1402841403 142 LMNPDVVTVRADVNVDVVLRYLRLRgelpdHTDHLFVVSRRHQYLGRVSLAALVTHEDTTPINRLIDDEQ---------- 211
Cdd:COG3448     7 IMTRDVVTVSPDTTLREALELMREH-----GIRGLPVVDEDGRLVGIVTERDLLRALLPDRLDELEERLLdlpvedvmtr 81

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1402841403 212 PAIDVGESD--QEVARQFSDHDWISAPVVDENNILVGRITIDDVVDIIRGQAEHQ 264
Cdd:COG3448    82 PVVTVTPDTplEEAAELMLEHGIHRLPVVDDDGRLVGIVTRTDLLRALARLLEEE 136
YtoI COG4109
Predicted transcriptional regulator containing CBS domains [Transcription];
142-254 1.07e-07

Predicted transcriptional regulator containing CBS domains [Transcription];


Pssm-ID: 443285 [Multi-domain]  Cd Length: 135  Bit Score: 50.68  E-value: 1.07e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1402841403 142 LMNPDVVTVRADVNVDVVLRYLRlrgelpdHTDHLF--VVSRRHQYLGRVSLAALVTHEDTTPINRLIDDEQPAIDVGES 219
Cdd:COG4109    22 MTLEDVATLSEDDTVEDALELLE-------KTGHSRfpVVDENGRLVGIVTSKDILGKDDDTPIEDVMTKNPITVTPDTS 94

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 1402841403 220 DQEVARQFSDHDWISAPVVDENNILVGRITIDDVV 254
Cdd:COG4109    95 LASAAHKMIWEGIELLPVVDDDGRLLGIISRQDVL 129
CBS COG0517
CBS domain [Signal transduction mechanisms];
142-262 7.73e-07

CBS domain [Signal transduction mechanisms];


Pssm-ID: 440283 [Multi-domain]  Cd Length: 128  Bit Score: 47.94  E-value: 7.73e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1402841403 142 LMNPDVVTVRADVNVDVVLRYLRLRgelpdHTDHLFVVSRRHQYLG-------RVSLAALVTHEDTTPINRLIDDEQPAI 214
Cdd:COG0517     6 IMTTDVVTVSPDATVREALELMSEK-----RIGGLPVVDEDGKLVGivtdrdlRRALAAEGKDLLDTPVSEVMTRPPVTV 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 1402841403 215 DVGESDQEVARQFSDHDWISAPVVDENNILVGRITIDDVVDIIRGQAE 262
Cdd:COG0517    81 SPDTSLEEAAELMEEHKIRRLPVVDDDGRLVGIITIKDLLKALLEPLA 128
COG2524 COG2524
Predicted transcriptional regulator, contains C-terminal CBS domains [Transcription];
138-257 1.48e-06

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


Pssm-ID: 442013 [Multi-domain]  Cd Length: 206  Bit Score: 48.73  E-value: 1.48e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1402841403 138 SAGRLMNPDVVTVRADVNVDVVLRYLRLRGElpdhtdHLFVVSRRHQYLGRVSLAALV------THEDTTPINRLIDDEQ 211
Cdd:COG2524    87 KVKDIMTKDVITVSPDTTLEEALELMLEKGI------SGLPVVDDGKLVGIITERDLLkalaegRDLLDAPVSDIMTRDV 160

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 1402841403 212 PAIDVGESDQEVARQFSDHDWISAPVVDENNILVGRITIDDVVDII 257
Cdd:COG2524   161 VTVSEDDSLEEALRLMLEHGIGRLPVVDDDGKLVGIITRTDILRAL 206
CBS_pair_SF cd02205
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains superfamily; The CBS ...
 144-255 2.12e-06

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: 46.47  E-value: 2.12e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1402841403 144 NPDVVTVRADVNVDVVLRYLRLRGelpdhTDHLFVVSRRHQYLGRVSLAALVTH------EDTTPINRLIDDEQPAIDVG 217
Cdd:cd02205     1 TRDVVTVDPDTTVREALELMAENG-----IGALPVVDDDGKLVGIVTERDILRAlvegglALDTPVAEVMTPDVITVSPD 75

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 1402841403 218 ESDQEVARQFSDHDWISAPVVDENNILVGRITIDDVVD 255
Cdd:cd02205    76 TDLEEALELMLEHGIRRLPVVDDDGKLVGIVTRRDILR 113
MgtE2 COG1824
Permease, similar to cation transporters [Inorganic ion transport and metabolism];
281-452 2.29e-05

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


Pssm-ID: 441429  Cd Length: 188  Bit Score: 44.86  E-value: 2.29e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1402841403 281 VWRAMRRRLMWLSVNLCTAFLASSVVGHFEGTIDKLVALAVLMPIVAGLGGNAGTQVLALMVRGLALGQVGAS-NARTLL 359
Cdd:COG1824     7 VRRIVRESLPVLLVLAVGGIIAGLVLEGMEELLLAYPGLLVLVPAFLGTRGNLGGILGARLSTALHLGLLEPRlRPDRRL 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1402841403 360 WKEVrvAALNGLLLGSILGLIVLAWF-------HSPGLSAVIAIALTCNLLFAALA---GVLVPLTLKRFGFDPALASGI 429
Cdd:COG1824    87 LNNI--LATLILALLISPLIGVLAWLvavllgrGSLGLLTLVGIALLAGLLLALLLivvTYYVAIASYRFGLDPDNVVIP 164

                         170       180
                  ....*....|....*....|...
gi 1402841403 430 FLTAVTDSMGFFTFLGLATLVLL 452
Cdd:COG1824   165 VVTTLGDVFGVLFLILVARLVLG 187
CBS_pair_ParBc_assoc cd04610
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with a ...
 143-254 1.83e-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: 40.77  E-value: 1.83e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1402841403 143 MNPDVVTVRADVNVDVVLRYLRlrgelpdHTDHL-FVVSRRHQYLGRVSLAALVTHEDTTPINRLIDDEQPAIDVGESDQ 221
Cdd:cd04610     1 MTRDVITVSPDDTVKDVIKLIK-------ETGHDgFPVVDDGKVVGYVTAKDLLGKDDDEKVSEIMSRDTVVADPDMDIT 73

                          90       100       110
                  ....*....|....*....|....*....|...
gi 1402841403 222 EVARQFSDHDWISAPVVDENNILVGRITIDDVV 254
Cdd:cd04610    74 DAARVIFRSGISKLPVVDDEGNLVGIITNMDVI 106
CBS_pair_arch2_repeat1 cd04638
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains present in archaea, ...
 143-254 2.77e-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: 40.40  E-value: 2.77e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1402841403 143 MNPDVVTVRADVNVDVVLRYLRLRgelpdHTDHLFVVSR-RHQYLGRVSLAALVTHEDTTPINRLIDDEQPAIDVGESDQ 221
Cdd:cd04638     1 MTKDVVTVTLPGTRDDVLEILKKK-----AISGVPVVKKeTGKLVGIVTRKDLLRNPDEEQIALLMSRDPITISPDDTLS 75

                          90       100       110
                  ....*....|....*....|....*....|...
gi 1402841403 222 EVARQFSDHDWISAPVVDENNiLVGRITIDDVV 254
Cdd:cd04638    76 EAAELMLEHNIRRVPVVDDDK-LVGIVTVADLV 107
CBS smart00116
Domain in cystathionine beta-synthase and other proteins; Domain present in all 3 forms of ...
 221-257 3.15e-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: 38.26  E-value: 3.15e-04
                           10        20        30
                   ....*....|....*....|....*....|....*..
gi 1402841403  221 QEVARQFSDHDWISAPVVDENNILVGRITIDDVVDII 257
Cdd:smart00116  12 EEALELLRENGIRRLPVVDEEGRLVGIVTRRDIIKAL 48
CBS_pair_ABC_Gly_Pro_assoc cd09831
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains found associated with ...
 173-249 1.26e-03

Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains found associated with the glycine betaine/L-proline ABC transporter; 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: 341402 [Multi-domain]  Cd Length: 116  Bit Score: 38.31  E-value: 1.26e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1402841403 173 TDHLFVVSRRHQYLGRVSLAALVT--HEDTTPINRLIDDEQPAIDVGESDQEVARQFSDHDWiSAPVVDENNILVGRIT 249
Cdd:cd09831    30 REYGYVVDKKRRFLGVVSVDSLRAalKENAQSLEDAFLTDVETVPADTSLSDILGLVASAPC-PLPVVDEDGRYLGVIS 107
CBS pfam00571
CBS domain; CBS domains are small intracellular modules that pair together to form a stable ...
 212-259 2.08e-03

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


Pssm-ID: 425756 [Multi-domain]  Cd Length: 57  Bit Score: 36.42  E-value: 2.08e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 1402841403 212 PAIDVGESDQEVARQFSDHDWISAPVVDENNILVGRITIDDVVDIIRG 259
Cdd:pfam00571  10 VTVSPDTTLEEALELMREHGISRLPVVDEDGKLVGIVTLKDLLRALLG 57
 
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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