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Conserved domains on  [gi|2126596142|gb|UDV19629|]
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magnesium transporter [Enterobacter hormaechei]

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];
49-477 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: 540.81  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2126596142  49 ADDIAEVGALVAHLPPPDLADTLEALPSEERHALWRLVQDHERGQVLLEASENVWDDLIDEMSDRDILDALQTLDIDEQI 128
Cdd:COG2239    15 EGDLEELRELLEELHPADIAELLEELPPEERLALFRLLPKELAAEVLEELDEEVQEELLEELSDEELAELLEELDPDDAA 94

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2126596142 129 YLVQHLPRNLTGRLLASLPAEERARVRQVMHYEKNSVGAIMEFGVITVRPDVTLGTVQRYLRRLGSMPDNTDKLFVTSRD 208
Cdd:COG2239    95 DLLEELPEEVVEELLALLDPEEREEIRELLSYPEDSAGRLMTTEFVAVREDWTVGEALRYLRRQAEDPETIYYIYVVDDD 174

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2126596142 209 KTLLGELELKTILLNSTQQRVSEVMETEPMVFSPEDDAEKAARTFERDDLVSAAVVDSVGKLMGRLTIDEIVDVVYEETD 288
Cdd:COG2239   175 GRLVGVVSLRDLLLADPDTKVSDIMDTDVISVPADDDQEEVARLFERYDLLALPVVDEEGRLVGIITVDDVVDVIEEEAT 254

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2126596142 289 NDLRALGGISAEDDVHASVGKAVKTRWAWLAINLCTAFVASRVIDGFEHTISQLVALASLMPIVAGIGGNTGNQTITMIV 368
Cdd:COG2239   255 EDILKLAGVSEDEDLFASVLKLARKRLPWLLILLLTAFLAASVIGLFEDTLEQVVALAVFMPLVAGMGGNAGSQSLTVVV 334

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2126596142 369 RALALENIQPGNFSWLIFREMGVALINGLVWGGIMGGITWWLYDDMALGGVMMLAMVLNLLVAAMMGVIIPLTMTRLGRD 448
Cdd:COG2239   335 RGLALGEITLSDWWRVLLKELLVGLLNGLILGLVVGLVAYLWFGNPLLGLVVGLALVINVLVAALAGSLLPLLLKRLGID 414

                         410       420
                  ....*....|....*....|....*....
gi 2126596142 449 PAVGSSVMITAITDTGGFFIFLGLATIFL 477
Cdd:COG2239   415 PAVASGPFITTITDVVGFFIYLGLATLFL 443
 
Name Accession Description Interval E-value
MgtE COG2239
Mg/Co/Ni transporter MgtE (contains CBS domain) [Inorganic ion transport and metabolism];
49-477 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: 540.81  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2126596142  49 ADDIAEVGALVAHLPPPDLADTLEALPSEERHALWRLVQDHERGQVLLEASENVWDDLIDEMSDRDILDALQTLDIDEQI 128
Cdd:COG2239    15 EGDLEELRELLEELHPADIAELLEELPPEERLALFRLLPKELAAEVLEELDEEVQEELLEELSDEELAELLEELDPDDAA 94

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2126596142 129 YLVQHLPRNLTGRLLASLPAEERARVRQVMHYEKNSVGAIMEFGVITVRPDVTLGTVQRYLRRLGSMPDNTDKLFVTSRD 208
Cdd:COG2239    95 DLLEELPEEVVEELLALLDPEEREEIRELLSYPEDSAGRLMTTEFVAVREDWTVGEALRYLRRQAEDPETIYYIYVVDDD 174

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2126596142 209 KTLLGELELKTILLNSTQQRVSEVMETEPMVFSPEDDAEKAARTFERDDLVSAAVVDSVGKLMGRLTIDEIVDVVYEETD 288
Cdd:COG2239   175 GRLVGVVSLRDLLLADPDTKVSDIMDTDVISVPADDDQEEVARLFERYDLLALPVVDEEGRLVGIITVDDVVDVIEEEAT 254

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2126596142 289 NDLRALGGISAEDDVHASVGKAVKTRWAWLAINLCTAFVASRVIDGFEHTISQLVALASLMPIVAGIGGNTGNQTITMIV 368
Cdd:COG2239   255 EDILKLAGVSEDEDLFASVLKLARKRLPWLLILLLTAFLAASVIGLFEDTLEQVVALAVFMPLVAGMGGNAGSQSLTVVV 334

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2126596142 369 RALALENIQPGNFSWLIFREMGVALINGLVWGGIMGGITWWLYDDMALGGVMMLAMVLNLLVAAMMGVIIPLTMTRLGRD 448
Cdd:COG2239   335 RGLALGEITLSDWWRVLLKELLVGLLNGLILGLVVGLVAYLWFGNPLLGLVVGLALVINVLVAALAGSLLPLLLKRLGID 414

                         410       420
                  ....*....|....*....|....*....
gi 2126596142 449 PAVGSSVMITAITDTGGFFIFLGLATIFL 477
Cdd:COG2239   415 PAVASGPFITTITDVVGFFIYLGLATLFL 443
mgtE TIGR00400
Mg2+ transporter (mgtE); This family of prokaryotic proteins models a class of Mg++ ...
 64-477 6.76e-66

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: 218.93  E-value: 6.76e-66
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2126596142  64 PPDLADTLEALPSEERHALWRLVQDHERGQVLLEASENVWDDLIDEMSDRDILDALQTLDIDEQIYLVQHLPRNLTGRLL 143
Cdd:TIGR00400  32 P*DIAEALKRLPGTELILLYRFLPKKIAVDTFSNLDQSTQNKLLNSFTNKEISEMINEMNLDDVIDLLEEVPANVVQQLL 111

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2126596142 144 ASLPAEERARVRQVMHYEKNSVGAIMEFGVITVRPDVTLGTVQRYLRRLGSMPDNTDKLFVTSRDKTLLGELELKTILLN 223
Cdd:TIGR00400 112 ASSTEEERKAINLLLSYSDDSAGRIMTIEYVELKEDYTVGKALDYIRRVAKTKEDIYTLYVTNESKHLKGVLSIRDLILA 191

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2126596142 224 STQQRVSEVMETEPMVFSPEDDAEKAARTFERDDLVSAAVVDSVGKLMGRLTIDEIVDVVYEETDNDLRALGGISAEDDV 303
Cdd:TIGR00400 192 KPEEILSSIMRSSVFSIVGVNDQEEVARLIQKYDFLAVPVVDNEGRLVGIVTVDDIIDVIQSEATEDFYMIAAVKPLDDS 271

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2126596142 304 H--ASVGKAVKTRWAWLAINLCTAFVASRVIDGFEHTISQLVALASLMPIVAGIGGNTGNQTITMIVRALALENIQPGNF 381
Cdd:TIGR00400 272 YfdTSILVMAKNRIIWLLVLLVSSTFTATIISNYEDLLLSLVALANFIPLLMDTSGNAGSQSSAVVIRGLALETVKVKDF 351

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2126596142 382 SWLIFREMGVALINGLVWGGIMGGITWWLYDDMALGGVMMLAMVLNLLVAAMMGVIIPLTMTRLGRDPAVGSSVMITAIT 461
Cdd:TIGR00400 352 FKVILREICVSILVGAILASVNFLRIVFFQGKLLIAFVVSSSLFVSLTVAKILGGLLPIVAKLLKLDPALMSGPLITTIA 431

                         410
                  ....*....|....*.
gi 2126596142 462 DTGGFFIFLGLATIFL 477
Cdd:TIGR00400 432 DALTLIIYFNIAKWVL 447
MgtE pfam01769
Divalent cation transporter; This region is the integral membrane part of the eubacterial MgtE ...
 349-472 1.12e-38

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: 136.42  E-value: 1.12e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2126596142 349 MPIVAGIGGNTGNQTITMIVRALALENIQPGNFSWLIFREMGVALINGLVWGGIMGGITWWLYDDMALGGVMMLAMVLNL 428
Cdd:pfam01769   1 IPVILGLGGNLGSQSASRLSRALALGEIEPRDAWRVLLKELLVGLLLGLVLGLIAGVLAFLWFGGLLLGLVVGLALLLAV 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 2126596142 429 LVAAMMGVIIPLTMTRLGRDPAVGSSVMITAITDTGGFFIFLGL 472
Cdd:pfam01769  81 LIALLLGTLLPLLLWRLGLDPDNASGPLITTLGDLLGLLILFGI 124
CBS_pair_Mg_transporter cd04606
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains in the magnesium ...
 163-283 3.83e-37

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: 132.46  E-value: 3.83e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2126596142 163 NSVGAIMEFGVITVRPDVTLGTVQRYLRRLGSMPDNTDKLFVTSRDKTLLGELELKTILLNSTQQRVSEVMETEPMVFSP 242
Cdd:cd04606     1 DSAGRLMTTEFVAVRPDWTVEEALEYLRRLAPDPETIYYIYVVDEDRRLLGVVSLRDLLLADPDTKVSDIMDTDVISVSA 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 2126596142 243 EDDAEKAARTFERDDLVSAAVVDSVGKLMGRLTIDEIVDVV 283
Cdd:cd04606    81 DDDQEEVARLFAKYDLLALPVVDEEGRLVGIITVDDVLDVI 121
MgtE_N smart00924
MgtE intracellular N domain; This region is the integral membrane part of the eubacterial MgtE ...
 62-165 1.45e-27

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: 106.06  E-value: 1.45e-27
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2126596142   62 LPPPDLADTLEALPSEERHALWRLVQDHERGQVLLEASENVWDDLIDEMSDRDIL-DALQTLDIDEQIYLVQHLPRNLTG 140
Cdd:smart00924   1 LHPADIADLLEELPPEERAELFRLLPPERAAEVLEELDEEVQAELLEALPPDERAaELLEELDPDDAADLLEELPEEVRE 80

                           90       100
                   ....*....|....*....|....*
gi 2126596142  141 RLLASLPAEERARVRQVMHYEKNSV 165
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];
49-477 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: 540.81  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2126596142  49 ADDIAEVGALVAHLPPPDLADTLEALPSEERHALWRLVQDHERGQVLLEASENVWDDLIDEMSDRDILDALQTLDIDEQI 128
Cdd:COG2239    15 EGDLEELRELLEELHPADIAELLEELPPEERLALFRLLPKELAAEVLEELDEEVQEELLEELSDEELAELLEELDPDDAA 94

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2126596142 129 YLVQHLPRNLTGRLLASLPAEERARVRQVMHYEKNSVGAIMEFGVITVRPDVTLGTVQRYLRRLGSMPDNTDKLFVTSRD 208
Cdd:COG2239    95 DLLEELPEEVVEELLALLDPEEREEIRELLSYPEDSAGRLMTTEFVAVREDWTVGEALRYLRRQAEDPETIYYIYVVDDD 174

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2126596142 209 KTLLGELELKTILLNSTQQRVSEVMETEPMVFSPEDDAEKAARTFERDDLVSAAVVDSVGKLMGRLTIDEIVDVVYEETD 288
Cdd:COG2239   175 GRLVGVVSLRDLLLADPDTKVSDIMDTDVISVPADDDQEEVARLFERYDLLALPVVDEEGRLVGIITVDDVVDVIEEEAT 254

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2126596142 289 NDLRALGGISAEDDVHASVGKAVKTRWAWLAINLCTAFVASRVIDGFEHTISQLVALASLMPIVAGIGGNTGNQTITMIV 368
Cdd:COG2239   255 EDILKLAGVSEDEDLFASVLKLARKRLPWLLILLLTAFLAASVIGLFEDTLEQVVALAVFMPLVAGMGGNAGSQSLTVVV 334

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2126596142 369 RALALENIQPGNFSWLIFREMGVALINGLVWGGIMGGITWWLYDDMALGGVMMLAMVLNLLVAAMMGVIIPLTMTRLGRD 448
Cdd:COG2239   335 RGLALGEITLSDWWRVLLKELLVGLLNGLILGLVVGLVAYLWFGNPLLGLVVGLALVINVLVAALAGSLLPLLLKRLGID 414

                         410       420
                  ....*....|....*....|....*....
gi 2126596142 449 PAVGSSVMITAITDTGGFFIFLGLATIFL 477
Cdd:COG2239   415 PAVASGPFITTITDVVGFFIYLGLATLFL 443
mgtE TIGR00400
Mg2+ transporter (mgtE); This family of prokaryotic proteins models a class of Mg++ ...
 64-477 6.76e-66

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: 218.93  E-value: 6.76e-66
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2126596142  64 PPDLADTLEALPSEERHALWRLVQDHERGQVLLEASENVWDDLIDEMSDRDILDALQTLDIDEQIYLVQHLPRNLTGRLL 143
Cdd:TIGR00400  32 P*DIAEALKRLPGTELILLYRFLPKKIAVDTFSNLDQSTQNKLLNSFTNKEISEMINEMNLDDVIDLLEEVPANVVQQLL 111

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2126596142 144 ASLPAEERARVRQVMHYEKNSVGAIMEFGVITVRPDVTLGTVQRYLRRLGSMPDNTDKLFVTSRDKTLLGELELKTILLN 223
Cdd:TIGR00400 112 ASSTEEERKAINLLLSYSDDSAGRIMTIEYVELKEDYTVGKALDYIRRVAKTKEDIYTLYVTNESKHLKGVLSIRDLILA 191

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2126596142 224 STQQRVSEVMETEPMVFSPEDDAEKAARTFERDDLVSAAVVDSVGKLMGRLTIDEIVDVVYEETDNDLRALGGISAEDDV 303
Cdd:TIGR00400 192 KPEEILSSIMRSSVFSIVGVNDQEEVARLIQKYDFLAVPVVDNEGRLVGIVTVDDIIDVIQSEATEDFYMIAAVKPLDDS 271

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2126596142 304 H--ASVGKAVKTRWAWLAINLCTAFVASRVIDGFEHTISQLVALASLMPIVAGIGGNTGNQTITMIVRALALENIQPGNF 381
Cdd:TIGR00400 272 YfdTSILVMAKNRIIWLLVLLVSSTFTATIISNYEDLLLSLVALANFIPLLMDTSGNAGSQSSAVVIRGLALETVKVKDF 351

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2126596142 382 SWLIFREMGVALINGLVWGGIMGGITWWLYDDMALGGVMMLAMVLNLLVAAMMGVIIPLTMTRLGRDPAVGSSVMITAIT 461
Cdd:TIGR00400 352 FKVILREICVSILVGAILASVNFLRIVFFQGKLLIAFVVSSSLFVSLTVAKILGGLLPIVAKLLKLDPALMSGPLITTIA 431

                         410
                  ....*....|....*.
gi 2126596142 462 DTGGFFIFLGLATIFL 477
Cdd:TIGR00400 432 DALTLIIYFNIAKWVL 447
MgtE pfam01769
Divalent cation transporter; This region is the integral membrane part of the eubacterial MgtE ...
 349-472 1.12e-38

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: 136.42  E-value: 1.12e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2126596142 349 MPIVAGIGGNTGNQTITMIVRALALENIQPGNFSWLIFREMGVALINGLVWGGIMGGITWWLYDDMALGGVMMLAMVLNL 428
Cdd:pfam01769   1 IPVILGLGGNLGSQSASRLSRALALGEIEPRDAWRVLLKELLVGLLLGLVLGLIAGVLAFLWFGGLLLGLVVGLALLLAV 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 2126596142 429 LVAAMMGVIIPLTMTRLGRDPAVGSSVMITAITDTGGFFIFLGL 472
Cdd:pfam01769  81 LIALLLGTLLPLLLWRLGLDPDNASGPLITTLGDLLGLLILFGI 124
CBS_pair_Mg_transporter cd04606
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains in the magnesium ...
 163-283 3.83e-37

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: 132.46  E-value: 3.83e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2126596142 163 NSVGAIMEFGVITVRPDVTLGTVQRYLRRLGSMPDNTDKLFVTSRDKTLLGELELKTILLNSTQQRVSEVMETEPMVFSP 242
Cdd:cd04606     1 DSAGRLMTTEFVAVRPDWTVEEALEYLRRLAPDPETIYYIYVVDEDRRLLGVVSLRDLLLADPDTKVSDIMDTDVISVSA 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 2126596142 243 EDDAEKAARTFERDDLVSAAVVDSVGKLMGRLTIDEIVDVV 283
Cdd:cd04606    81 DDDQEEVARLFAKYDLLALPVVDEEGRLVGIITVDDVLDVI 121
MgtE_N smart00924
MgtE intracellular N domain; This region is the integral membrane part of the eubacterial MgtE ...
 62-165 1.45e-27

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: 106.06  E-value: 1.45e-27
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2126596142   62 LPPPDLADTLEALPSEERHALWRLVQDHERGQVLLEASENVWDDLIDEMSDRDIL-DALQTLDIDEQIYLVQHLPRNLTG 140
Cdd:smart00924   1 LHPADIADLLEELPPEERAELFRLLPPERAAEVLEELDEEVQAELLEALPPDERAaELLEELDPDDAADLLEELPEEVRE 80

                           90       100
                   ....*....|....*....|....*
gi 2126596142  141 RLLASLPAEERARVRQVMHYEKNSV 165
Cdd:smart00924  81 ELLSLLDPEEREEIRELLSYPEDTA 105
MgtE_N pfam03448
MgtE intracellular N domain; This domain is found at the N-terminus of eubacterial magnesium ...
 62-163 7.57e-26

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: 101.09  E-value: 7.57e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2126596142  62 LPPPDLADTLEALPSEERHALWRLVQDHERGQVLLEASENVWDDLIDEMSDRDILDALQTLDIDEQIYLVQHLPRNLTGR 141
Cdd:pfam03448   1 LHPADIAELLEELPPEERLALLRLLPPETAAEVLEELDEDVQAELIEALDPEEAAELLEELDPDDAADLLEELPEEKVEE 80

                          90       100
                  ....*....|....*....|..
gi 2126596142 142 LLASLPAEERARVRQVMHYEKN 163
Cdd:pfam03448  81 ILSLLDPEERKEIRELLSYPED 102
CBS COG0517
CBS domain [Signal transduction mechanisms];
165-286 1.48e-11

CBS domain [Signal transduction mechanisms];


Pssm-ID: 440283 [Multi-domain]  Cd Length: 128  Bit Score: 61.42  E-value: 1.48e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2126596142 165 VGAIMEFGVITVRPDVTLGTVQRYLR--RLGSMP--DNTDKL--FVTSRDktLLGELELKTILLNSTqqRVSEVMETEPM 238
Cdd:COG0517     3 VKDIMTTDVVTVSPDATVREALELMSekRIGGLPvvDEDGKLvgIVTDRD--LRRALAAEGKDLLDT--PVSEVMTRPPV 78

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 2126596142 239 VFSPEDDAEKAARTFERDDLVSAAVVDSVGKLMGRLTIDEIVDVVYEE 286
Cdd:COG0517    79 TVSPDTSLEEAAELMEEHKIRRLPVVDDDGRLVGIITIKDLLKALLEP 126
COG3448 COG3448
CBS-domain-containing membrane protein [Signal transduction mechanisms];
165-290 1.43e-10

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


Pssm-ID: 442671 [Multi-domain]  Cd Length: 136  Bit Score: 59.11  E-value: 1.43e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2126596142 165 VGAIMEFGVITVRPDVTLGTVQRYLR--RLGSMP--DNTDKL--FVTSRD-KTLLGELELKTILLNSTQQRVSEVMETEP 237
Cdd:COG3448     4 VRDIMTRDVVTVSPDTTLREALELMRehGIRGLPvvDEDGRLvgIVTERDlLRALLPDRLDELEERLLDLPVEDVMTRPV 83

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 2126596142 238 MVFSPEDDAEKAARTFERDDLVSAAVVDSVGKLMGRLTIDEIVDVVYEETDND 290
Cdd:COG3448    84 VTVTPDTPLEEAAELMLEHGIHRLPVVDDDGRLVGIVTRTDLLRALARLLEEE 136
CBS_pair_SF cd02205
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains superfamily; The CBS ...
 173-281 6.33e-10

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: 56.48  E-value: 6.33e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2126596142 173 VITVRPDVTLGTVQRYLR--RLGSMP--DNTDKL--FVTSRDktLLGELELKTILLNSTqqrVSEVMETEPMVFSPEDDA 246
Cdd:cd02205     4 VVTVDPDTTVREALELMAenGIGALPvvDDDGKLvgIVTERD--ILRALVEGGLALDTP---VAEVMTPDVITVSPDTDL 78

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 2126596142 247 EKAARTFERDDLVSAAVVDSVGKLMGRLTIDEIVD 281
Cdd:cd02205    79 EEALELMLEHGIRRLPVVDDDGKLVGIVTRRDILR 113
COG2524 COG2524
Predicted transcriptional regulator, contains C-terminal CBS domains [Transcription];
148-283 5.01e-09

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


Pssm-ID: 442013 [Multi-domain]  Cd Length: 206  Bit Score: 56.05  E-value: 5.01e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2126596142 148 AEERARVRQVMHYEKNSVGAIMEFGVITVRPDVTLGTVQRYLR--RLGSMP--DNtDKL--FVTSRDktLLGELELKTIL 221
Cdd:COG2524    71 AVRVVAEKELGLVLKMKVKDIMTKDVITVSPDTTLEEALELMLekGISGLPvvDD-GKLvgIITERD--LLKALAEGRDL 147

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2126596142 222 LNSTqqrVSEVMETEPMVFSPEDDAEKAARTFERDDLVSAAVVDSVGKLMGRLTIDEIVDVV 283
Cdd:COG2524   148 LDAP---VSDIMTRDVVTVSEDDSLEEALRLMLEHGIGRLPVVDDDGKLVGIITRTDILRAL 206
COG2905 COG2905
Signal-transduction protein containing cAMP-binding, CBS, and nucleotidyltransferase domains ...
 165-286 3.51e-07

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


Pssm-ID: 442149 [Multi-domain]  Cd Length: 124  Bit Score: 49.06  E-value: 3.51e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2126596142 165 VGAIMEFGVITVRPDVTLGTVQRYL--RRLGSMP--DNTDKL--FVTSRDktLLGELELKTilLNSTQQRVSEVMETEPM 238
Cdd:COG2905     1 VKDIMSRDVVTVSPDATVREAARLMteKGVGSLVvvDDDGRLvgIITDRD--LRRRVLAEG--LDPLDTPVSEVMTRPPI 76

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 2126596142 239 VFSPEDDAEKAARTFERDDLVSAAVVDSvGKLMGRLTIDEIVDVVYEE 286
Cdd:COG2905    77 TVSPDDSLAEALELMEEHRIRHLPVVDD-GKLVGIVSITDLLRALSEE 123
YtoI COG4109
Predicted transcriptional regulator containing CBS domains [Transcription];
150-275 2.02e-06

Predicted transcriptional regulator containing CBS domains [Transcription];


Pssm-ID: 443285 [Multi-domain]  Cd Length: 135  Bit Score: 47.21  E-value: 2.02e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2126596142 150 ERARVRQVMHYEKnsvgaimefgVITVRPDVTLGTVQRYLR--RLGSMPdntdklfVTSRDKTLLGELELKTILLNSTQQ 227
Cdd:COG4109    14 EILLVEDIMTLED----------VATLSEDDTVEDALELLEktGHSRFP-------VVDENGRLVGIVTSKDILGKDDDT 76

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 2126596142 228 RVSEVMETEPMVFSPEDDAEKAARTFERDDLVSAAVVDSVGKLMGRLT 275
Cdd:COG4109    77 PIEDVMTKNPITVTPDTSLASAAHKMIWEGIELLPVVDDDGRLLGIIS 124
CBS pfam00571
CBS domain; CBS domains are small intracellular modules that pair together to form a stable ...
 229-285 3.72e-06

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


Pssm-ID: 425756 [Multi-domain]  Cd Length: 57  Bit Score: 44.13  E-value: 3.72e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 2126596142 229 VSEVMETEPMVFSPEDDAEKAARTFERDDLVSAAVVDSVGKLMGRLTIDEIVDVVYE 285
Cdd:pfam00571   1 VKDIMTKDVVTVSPDTTLEEALELMREHGISRLPVVDEDGKLVGIVTLKDLLRALLG 57
CBS_pair_ParBc_assoc cd04610
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with a ...
 169-280 5.15e-06

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: 45.39  E-value: 5.15e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2126596142 169 MEFGVITVRPDVTLGTVQRYLRRLGSmpdntdKLFVTSRDKTLLGELELKTILLNSTQQRVSEVMETEPMVFSPEDDAEK 248
Cdd:cd04610     1 MTRDVITVSPDDTVKDVIKLIKETGH------DGFPVVDDGKVVGYVTAKDLLGKDDDEKVSEIMSRDTVVADPDMDITD 74

                          90       100       110
                  ....*....|....*....|....*....|..
gi 2126596142 249 AARTFERDDLVSAAVVDSVGKLMGRLTIDEIV 280
Cdd:cd04610    75 AARVIFRSGISKLPVVDDEGNLVGIITNMDVI 106
CBS_pair_ABC_OpuCA_assoc cd04583
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains found associated with ...
 174-283 8.12e-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: 8.12e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2126596142 174 ITVRPDVTLgtvqryLRRLGSMPDN-TDKLFVTSRDKTLLGELELKTILLN-STQQRVSEVMETEPMVFSPEDDAEKAAR 251
Cdd:cd04583     5 VTITPERTL------AQAIEIMREKrVDSLLVVDKDNVLLGIVDIEDINRNyRKAKKVGEIMERDVFTVKEDSLLRDTVD 78

                          90       100       110
                  ....*....|....*....|....*....|..
gi 2126596142 252 TFERDDLVSAAVVDSVGKLMGRLTIDEIVDVV 283
Cdd:cd04583    79 RILKRGLKYVPVVDEQGRLVGLVTRASLVDIV 110
CBS_pair_HRP1_like cd04622
CBS pair domain found in Hypoxic Response Protein 1 (HRP1) -like proteinds; Mycobacterium ...
 172-279 4.14e-05

CBS pair domain found in Hypoxic Response Protein 1 (HRP1) -like proteinds; Mycobacterium tuberculosis adapts to cellular stresses by upregulation of the dormancy survival regulon. Hypoxic response protein 1 (HRP1) is encoded by one of the most strongly upregulated genes in the dormancy survival regulon. HRP1 is a 'CBS-domain-only protein; however unlike other CBS containing proteins it does not appear to bind AMP. The biological function of the protein remains unclear, but is thought to contribute to the modulation of the host immune response. The CBS domain, named after human CBS, is a small domain originally identified in cystathionine beta-synthase and is subsequently found in a wide range of different proteins. CBS domains usually occur in tandem repeats. They associate to form a so-called Bateman domain or a CBS pair based on crystallographic studies in bacteria. The CBS pair was used as a basis for this cd hierarchy since the human CBS proteins can adopt the typical core structure and form an intramolecular CBS pair. The interface between the two CBS domains forms a cleft that is a potential ligand binding site. The CBS pair coexists with a variety of other functional domains and this has been used to help in its classification here. It has been proposed that the CBS domain may play a regulatory role, although its exact function is unknown. Mutations of conserved residues within this domain are associated with a variety of human hereditary diseases, including congenital myotonia, idiopathic generalized epilepsy, hypercalciuric nephrolithiasis, and classic Bartter syndrome (CLC chloride channel family members), Wolff-Parkinson-White syndrome (gamma 2 subunit of AMP-activated protein kinase), retinitis pigmentosa (IMP dehydrogenase-1), and homocystinuria (cystathionine beta-synthase).


Pssm-ID: 341390 [Multi-domain]  Cd Length: 115  Bit Score: 42.79  E-value: 4.14e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2126596142 172 GVITVRPDVTLGTVQRYLRRL--GSMP--DNtDKLF--VTSRDKTLLGELELKtillNSTQQRVSEVMETEPMVFSPEDD 245
Cdd:cd04622     4 DVVTVSPDTTLREAARLMRDLdiGALPvcEG-DRLVgmVTDRDIVVRAVAEGK----DPNTTTVREVMTGDVVTCSPDDD 78

                          90       100       110
                  ....*....|....*....|....*....|....
gi 2126596142 246 AEKAARTFERDDLVSAAVVDSVGKLMGRLTIDEI 279
Cdd:cd04622    79 VEEAARLMAEHQVRRLPVVDDDGRLVGIVSLGDL 112
IMPDH pfam00478
IMP dehydrogenase / GMP reductase domain; This family is involved in biosynthesis of guanosine ...
 145-280 4.34e-05

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


Pssm-ID: 459826 [Multi-domain]  Cd Length: 463  Bit Score: 45.84  E-value: 4.34e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2126596142 145 SLPAEERAR-VRQVMHYEknsvgAIMEFGVITVRPDVTLGTVQRYLRRLG--SMPDNTDKLFV---TSRDktllgeLELK 218
Cdd:pfam00478  66 NMSIEEQAEeVRKVKRSE-----SGMITDPVTLSPDATVADALALMERYGisGVPVVDDGKLVgivTNRD------LRFE 134

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2126596142 219 TillnSTQQRVSEVMETEPMVFSPED-DAEKAARTFERDDLVSAAVVDSVGKLMGRLTIDEIV 280
Cdd:pfam00478 135 T----DLSQPVSEVMTKENLVTAPEGtTLEEAKEILHKHKIEKLPVVDDNGRLVGLITIKDIE 193
CBS_pair_CBS cd04608
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with the ...
 173-277 5.62e-05

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: 42.52  E-value: 5.62e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2126596142 173 VITVRPDVTLGTVQRYLRRLGsmpdnTDKLFVTSRDKTLLG---ELELKTILLNSTQQR---VSEVMETEPMVFSPEDDA 246
Cdd:cd04608    12 PVTVLPDDTLGEAIEIMREYG-----VDQLPVVDEDGRVVGmvtEGNLLSSLLAGRAQPsdpVSKAMYKQFKQVDLDTPL 86

                          90       100       110
                  ....*....|....*....|....*....|..
gi 2126596142 247 EKAARTFERDDlvSAAVVDSVGKLMGRLT-ID 277
Cdd:cd04608    87 GALSRILERDH--FALVVDGQGKVLGIVTrID 116
MgtE2 COG1824
Permease, similar to cation transporters [Inorganic ion transport and metabolism];
302-478 1.06e-04

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


Pssm-ID: 441429  Cd Length: 188  Bit Score: 42.93  E-value: 1.06e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2126596142 302 DVHASVGKAVKTRWAWLAINLCTAFVASRVIDGFEHTISQLVALASLMPIVAGIGGNTGNQTITMIVRALALENIQPgNF 381
Cdd:COG1824     2 TVRWTVRRIVRESLPVLLVLAVGGIIAGLVLEGMEELLLAYPGLLVLVPAFLGTRGNLGGILGARLSTALHLGLLEP-RL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2126596142 382 SW--LIFREMGVALINGLVWGGIMGGITWWL-----YDDMALGGVMMLAMVLNLLVAAMM---GVIIPLTMTRLGRDPAV 451
Cdd:COG1824    81 RPdrRLLNNILATLILALLISPLIGVLAWLVavllgRGSLGLLTLVGIALLAGLLLALLLivvTYYVAIASYRFGLDPDN 160

                         170       180
                  ....*....|....*....|....*..
gi 2126596142 452 GSSVMITAITDTGGFFIFLGLATIFLL 478
Cdd:COG1824   161 VVIPVVTTLGDVFGVLFLILVARLVLG 187
CBS_arch_repeat2 cd17778
CBS pair domains found in archeal proteins, repeat 2; CBS pair domains found in archeal ...
 165-275 2.49e-04

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


Pssm-ID: 341414 [Multi-domain]  Cd Length: 131  Bit Score: 40.78  E-value: 2.49e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2126596142 165 VGAIMEFGVITVRPDVTLG-----TVQRYLRRLGSMPDNTDKLFVTSRD--KTLLGELELKTILLNSTQQ----RVSEVM 233
Cdd:cd17778     2 VKEFMTTPVVTIYPDDTLKeamelMVTRGFRRLPVVSGGKLVGIVTAMDivKYFGSHEAKKRLTTGDIDEaystPVEEIM 81

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 2126596142 234 ETEPMVFSPEDDAEKAARTFERDDLVSAAVVDSVGKLMGRLT 275
Cdd:cd17778    82 SKEVVTIEPDADIAEAARLMIKKNVGSLLVVDDEGELKGIIT 123
CBS_pair_AcuB_like cd04584
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with the ...
 165-282 1.89e-03

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


Pssm-ID: 341361 [Multi-domain]  Cd Length: 130  Bit Score: 38.17  E-value: 1.89e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2126596142 165 VGAIMEFGVITVRPDVTLGTVQRYL-----RRLgsmP--DNtDKL--FVTSRD--------KTLLGELELKTILLnstQQ 227
Cdd:cd04584     2 VKDIMTKNVVTVTPDTSLAEARELMkehkiRHL---PvvDD-GKLvgIVTDRDllraspskATSLSIYELNYLLS---KI 74

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 2126596142 228 RVSEVMETEPMVFSPEDDAEKAARTFERDDLVSAAVVDSvGKLMGRLTIDEIVDV 282
Cdd:cd04584    75 PVKDIMTKDVITVSPDDTVEEAALLMLENKIGCLPVVDG-GKLVGIITETDILRA 128
COG3448 COG3448
CBS-domain-containing membrane protein [Signal transduction mechanisms];
228-301 5.39e-03

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


Pssm-ID: 442671 [Multi-domain]  Cd Length: 136  Bit Score: 37.15  E-value: 5.39e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2126596142 228 RVSEVMETEPMVFSPEDDAEKAARTFERDDLVSAAVVDSVGKLMGRLTIDEIVDVVYEETDNDL-RALGGISAED 301
Cdd:COG3448     3 TVRDIMTRDVVTVSPDTTLREALELMREHGIRGLPVVDEDGRLVGIVTERDLLRALLPDRLDELeERLLDLPVED 77
CBS_pair_plant_CBSX cd17789
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains from plant CBSX ...
 216-280 5.77e-03

Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains from plant CBSX proteins; This cd contains two tandem repeats of the cystathionine beta-synthase (CBS pair) domains of plant single cystathionine beta-synthase (CBS) pair proteins (CBSX). CBSX1 and CBSX2 have been identified as redox regulators of the thioredoxin (Trx) system. 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: 341425 [Multi-domain]  Cd Length: 141  Bit Score: 37.07  E-value: 5.77e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2126596142 216 ELKTILLNSTQQRVSEVMETEPMVFSPEDDAEKAARTFERDDLVSAAVVDSVGKLMGRLTIDEIV 280
Cdd:cd17789    75 EVQKLLSKTNGKVVGDVMTPSPLVVREKTNLEDAARILLETKFRRLPVVDSDGKLVGIITRGNVV 139
CBS_pair_arch_MET2_assoc cd04605
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with the ...
 165-279 6.07e-03

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


Pssm-ID: 341379 [Multi-domain]  Cd Length: 116  Bit Score: 36.45  E-value: 6.07e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2126596142 165 VGAIMEFGVITVRPDVTLGTVQRYLrrlgsMPDNTDKLFVTSRDKTLLGELEL----KTILLNSTqqRVSEVMETEPMVF 240
Cdd:cd04605     2 VEDIMSKDVATIREDISIEEAAKIM-----IDKNVTHLPVVSEDGKLIGIVTSwdisKAVALKKD--SLEEIMTRNVITA 74

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 2126596142 241 SPEDDAEKAARTFERDDLVSAAVVDSVGKLMGRLTIDEI 279
Cdd:cd04605    75 RPDEPIELAARKMEKHNISALPVVDDDRRVIGIITSDDI 113
CBS COG0517
CBS domain [Signal transduction mechanisms];
228-291 8.43e-03

CBS domain [Signal transduction mechanisms];


Pssm-ID: 440283 [Multi-domain]  Cd Length: 128  Bit Score: 36.38  E-value: 8.43e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2126596142 228 RVSEVMETEPMVFSPEDDAEKAARTFERDDLVSAAVVDSVGKLMGRLTIDEIVDVVYEETDNDL 291
Cdd:COG0517     2 KVKDIMTTDVVTVSPDATVREALELMSEKRIGGLPVVDEDGKLVGIVTDRDLRRALAAEGKDLL 65
 
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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