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Conserved domains on  [gi|503249015|ref|WP_013483676|]
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MULTISPECIES: magnesium transporter [Ruminococcus]

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];
30-481 3.67e-127

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


:

Pssm-ID: 441840 [Multi-domain]  Cd Length: 443  Bit Score: 377.10  E-value: 3.67e-127
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503249015  30 KPDYEGEIISVIRSNDSPRVmLKKLEDYHGNDIAGVMADLSKQERQKLYRVCNGDMLAEAFEYLDEDDAGIYLNEMDLNK 109
Cdd:COG2239    2 TEELLEELRELLEEGDLEEL-RELLEELHPADIAELLEELPPEERLALFRLLPKELAAEVLEELDEEVQEELLEELSDEE 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503249015 110 AAAVVSLMETDTAVNVLREIEREKRGLIIDALSAEVRKEIRLIASFDEDEIGSKMTTNCIIIKEDLTIKQAMSELVRQAE 189
Cdd:COG2239   81 LAELLEELDPDDAADLLEELPEEVVEELLALLDPEEREEIRELLSYPEDSAGRLMTTEFVAVREDWTVGEALRYLRRQAE 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503249015 190 DNDNITTIFVVDDNDEFYGAIDLKELITARSTRSLESLIMTSFPYVYANEEIDECIEKLKDYSEDLIPVLDNSSRLLGVI 269
Cdd:COG2239  161 DPETIYYIYVVDDDGRLVGVVSLRDLLLADPDTKVSDIMDTDVISVPADDDQEEVARLFERYDLLALPVVDEEGRLVGII 240

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503249015 270 TAKSLIEVVDDEMGEDYVMFAGLTAEEDLQEPLLQSMKKRLPWLLVLLGLGLVVSGVVGVFEKVISQLTLIMAFQSLILD 349
Cdd:COG2239  241 TVDDVVDVIEEEATEDILKLAGVSEDEDLFASVLKLARKRLPWLLILLLTAFLAASVIGLFEDTLEQVVALAVFMPLVAG 320

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503249015 350 MAGNVGTQSLAVTIRVLTDENLTFRQKMHLVAKETRVGLSNGILLGLmsfaMVGLYIMFFKHrtagfSFAVSGCIGVSLM 429
Cdd:COG2239  321 MGGNAGSQSLTVVVRGLALGEITLSDWWRVLLKELLVGLLNGLILGL----VVGLVAYLWFG-----NPLLGLVVGLALV 391

                        410       420       430       440       450
                 ....*....|....*....|....*....|....*....|....*....|..
gi 503249015 430 LAMLISSAVGTIIPLFFKKIKVDPAVASGPLITTVNDLVAVVTYYGLSWLLL 481
Cdd:COG2239  392 INVLVAALAGSLLPLLLKRLGIDPAVASGPFITTITDVVGFFIYLGLATLFL 443
 
Name Accession Description Interval E-value
MgtE COG2239
Mg/Co/Ni transporter MgtE (contains CBS domain) [Inorganic ion transport and metabolism];
30-481 3.67e-127

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


Pssm-ID: 441840 [Multi-domain]  Cd Length: 443  Bit Score: 377.10  E-value: 3.67e-127
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503249015  30 KPDYEGEIISVIRSNDSPRVmLKKLEDYHGNDIAGVMADLSKQERQKLYRVCNGDMLAEAFEYLDEDDAGIYLNEMDLNK 109
Cdd:COG2239    2 TEELLEELRELLEEGDLEEL-RELLEELHPADIAELLEELPPEERLALFRLLPKELAAEVLEELDEEVQEELLEELSDEE 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503249015 110 AAAVVSLMETDTAVNVLREIEREKRGLIIDALSAEVRKEIRLIASFDEDEIGSKMTTNCIIIKEDLTIKQAMSELVRQAE 189
Cdd:COG2239   81 LAELLEELDPDDAADLLEELPEEVVEELLALLDPEEREEIRELLSYPEDSAGRLMTTEFVAVREDWTVGEALRYLRRQAE 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503249015 190 DNDNITTIFVVDDNDEFYGAIDLKELITARSTRSLESLIMTSFPYVYANEEIDECIEKLKDYSEDLIPVLDNSSRLLGVI 269
Cdd:COG2239  161 DPETIYYIYVVDDDGRLVGVVSLRDLLLADPDTKVSDIMDTDVISVPADDDQEEVARLFERYDLLALPVVDEEGRLVGII 240

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503249015 270 TAKSLIEVVDDEMGEDYVMFAGLTAEEDLQEPLLQSMKKRLPWLLVLLGLGLVVSGVVGVFEKVISQLTLIMAFQSLILD 349
Cdd:COG2239  241 TVDDVVDVIEEEATEDILKLAGVSEDEDLFASVLKLARKRLPWLLILLLTAFLAASVIGLFEDTLEQVVALAVFMPLVAG 320

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503249015 350 MAGNVGTQSLAVTIRVLTDENLTFRQKMHLVAKETRVGLSNGILLGLmsfaMVGLYIMFFKHrtagfSFAVSGCIGVSLM 429
Cdd:COG2239  321 MGGNAGSQSLTVVVRGLALGEITLSDWWRVLLKELLVGLLNGLILGL----VVGLVAYLWFG-----NPLLGLVVGLALV 391

                        410       420       430       440       450
                 ....*....|....*....|....*....|....*....|....*....|..
gi 503249015 430 LAMLISSAVGTIIPLFFKKIKVDPAVASGPLITTVNDLVAVVTYYGLSWLLL 481
Cdd:COG2239  392 INVLVAALAGSLLPLLLKRLGIDPAVASGPFITTITDVVGFFIYLGLATLFL 443
mgtE TIGR00400
Mg2+ transporter (mgtE); This family of prokaryotic proteins models a class of Mg++ ...
 53-480 4.42e-61

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: 206.60  E-value: 4.42e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503249015   53 KLEDYHGNDIAGVMADLSKQERQKLYRVCNGDMLAEAFEYLDEDDAGIYLNEMDLNKAAAVVSLMETDTAVNVLREIERE 132
Cdd:TIGR00400  26 KFLK*QP*DIAEALKRLPGTELILLYRFLPKKIAVDTFSNLDQSTQNKLLNSFTNKEISEMINEMNLDDVIDLLEEVPAN 105

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503249015  133 KRGLIIDALSAEVRKEIRLIASFDEDEIGSKMTTNCIIIKEDLTIKQAMSELVRQAEDNDNITTIFVVDDNDEFYGAIDL 212
Cdd:TIGR00400 106 VVQQLLASSTEEERKAINLLLSYSDDSAGRIMTIEYVELKEDYTVGKALDYIRRVAKTKEDIYTLYVTNESKHLKGVLSI 185

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503249015  213 KELITARSTRSLESLIMTSFPYVYANEEIDECIEKLKDYSEDLIPVLDNSSRLLGVITAKSLIEVVDDEMGEDYVMFAGL 292
Cdd:TIGR00400 186 RDLILAKPEEILSSIMRSSVFSIVGVNDQEEVARLIQKYDFLAVPVVDNEGRLVGIVTVDDIIDVIQSEATEDFYMIAAV 265

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503249015  293 TAEED--LQEPLLQSMKKRLPWLLVLLGLGLVVSGVVGVFEKVISQLTLIMAFQSLILDMAGNVGTQSLAVTIRVLTDEN 370
Cdd:TIGR00400 266 KPLDDsyFDTSILVMAKNRIIWLLVLLVSSTFTATIISNYEDLLLSLVALANFIPLLMDTSGNAGSQSSAVVIRGLALET 345

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503249015  371 LTFRQKMHLVAKETRVglsnGILLGLMSFAMVGLYIMFFKHRtAGFSFAVSGCigvsLMLAMLISSAVGTIIPLFFKKIK 450
Cdd:TIGR00400 346 VKVKDFFKVILREICV----SILVGAILASVNFLRIVFFQGK-LLIAFVVSSS----LFVSLTVAKILGGLLPIVAKLLK 416

                         410       420       430
                  ....*....|....*....|....*....|.
gi 503249015  451 VDPAVASGPLITTVNDLVAVVTYYGLS-WLL 480
Cdd:TIGR00400 417 LDPALMSGPLITTIADALTLIIYFNIAkWVL 447
MgtE pfam01769
Divalent cation transporter; This region is the integral membrane part of the eubacterial MgtE ...
 346-476 4.95e-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: 127.17  E-value: 4.95e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503249015  346 LILDMAGNVGTQSLAVTIRVLTDENLTFRQKMHLVAKETRVGLSNGILLGLMSFAMVGLYIMFFKhrtagfsfaVSGCIG 425
Cdd:pfam01769   3 VILGLGGNLGSQSASRLSRALALGEIEPRDAWRVLLKELLVGLLLGLVLGLIAGVLAFLWFGGLL---------LGLVVG 73

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 503249015  426 VSLMLAMLISSAVGTIIPLFFKKIKVDPAVASGPLITTVNDLVAVVTYYGL 476
Cdd:pfam01769  74 LALLLAVLIALLLGTLLPLLLWRLGLDPDNASGPLITTLGDLLGLLILFGI 124
CBS_pair_Mg_transporter cd04606
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains in the magnesium ...
 158-280 2.15e-24

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: 97.79  E-value: 2.15e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503249015 158 DEIGSKMTTNCIIIKEDLTIKQAMSELVRQAEDNDNITTIFVVDDNDEFYGAIDLKELITARSTRSLESLIMTSFPYVYA 237
Cdd:cd04606    1 DSAGRLMTTEFVAVRPDWTVEEALEYLRRLAPDPETIYYIYVVDEDRRLLGVVSLRDLLLADPDTKVSDIMDTDVISVSA 80

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 503249015 238 NEEIDECIEKLKDYseDL--IPVLDNSSRLLGVITakslievVDD 280
Cdd:cd04606   81 DDDQEEVARLFAKY--DLlaLPVVDEEGRLVGIIT-------VDD 116
MgtE_N smart00924
MgtE intracellular N domain; This region is the integral membrane part of the eubacterial MgtE ...
 57-160 3.42e-15

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: 71.39  E-value: 3.42e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503249015    57 YHGNDIAGVMADLSKQERQKLYRVCNGDMLAEAFEYLDEDDAGIYLNEMDLNKAAA-VVSLMETDTAVNVLREIEREKRG 135
Cdd:smart00924   1 LHPADIADLLEELPPEERAELFRLLPPERAAEVLEELDEEVQAELLEALPPDERAAeLLEELDPDDAADLLEELPEEVRE 80

                           90       100
                   ....*....|....*....|....*
gi 503249015   136 LIIDALSAEVRKEIRLIASFDEDEI 160
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];
30-481 3.67e-127

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


Pssm-ID: 441840 [Multi-domain]  Cd Length: 443  Bit Score: 377.10  E-value: 3.67e-127
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503249015  30 KPDYEGEIISVIRSNDSPRVmLKKLEDYHGNDIAGVMADLSKQERQKLYRVCNGDMLAEAFEYLDEDDAGIYLNEMDLNK 109
Cdd:COG2239    2 TEELLEELRELLEEGDLEEL-RELLEELHPADIAELLEELPPEERLALFRLLPKELAAEVLEELDEEVQEELLEELSDEE 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503249015 110 AAAVVSLMETDTAVNVLREIEREKRGLIIDALSAEVRKEIRLIASFDEDEIGSKMTTNCIIIKEDLTIKQAMSELVRQAE 189
Cdd:COG2239   81 LAELLEELDPDDAADLLEELPEEVVEELLALLDPEEREEIRELLSYPEDSAGRLMTTEFVAVREDWTVGEALRYLRRQAE 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503249015 190 DNDNITTIFVVDDNDEFYGAIDLKELITARSTRSLESLIMTSFPYVYANEEIDECIEKLKDYSEDLIPVLDNSSRLLGVI 269
Cdd:COG2239  161 DPETIYYIYVVDDDGRLVGVVSLRDLLLADPDTKVSDIMDTDVISVPADDDQEEVARLFERYDLLALPVVDEEGRLVGII 240

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503249015 270 TAKSLIEVVDDEMGEDYVMFAGLTAEEDLQEPLLQSMKKRLPWLLVLLGLGLVVSGVVGVFEKVISQLTLIMAFQSLILD 349
Cdd:COG2239  241 TVDDVVDVIEEEATEDILKLAGVSEDEDLFASVLKLARKRLPWLLILLLTAFLAASVIGLFEDTLEQVVALAVFMPLVAG 320

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503249015 350 MAGNVGTQSLAVTIRVLTDENLTFRQKMHLVAKETRVGLSNGILLGLmsfaMVGLYIMFFKHrtagfSFAVSGCIGVSLM 429
Cdd:COG2239  321 MGGNAGSQSLTVVVRGLALGEITLSDWWRVLLKELLVGLLNGLILGL----VVGLVAYLWFG-----NPLLGLVVGLALV 391

                        410       420       430       440       450
                 ....*....|....*....|....*....|....*....|....*....|..
gi 503249015 430 LAMLISSAVGTIIPLFFKKIKVDPAVASGPLITTVNDLVAVVTYYGLSWLLL 481
Cdd:COG2239  392 INVLVAALAGSLLPLLLKRLGIDPAVASGPFITTITDVVGFFIYLGLATLFL 443
mgtE TIGR00400
Mg2+ transporter (mgtE); This family of prokaryotic proteins models a class of Mg++ ...
 53-480 4.42e-61

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: 206.60  E-value: 4.42e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503249015   53 KLEDYHGNDIAGVMADLSKQERQKLYRVCNGDMLAEAFEYLDEDDAGIYLNEMDLNKAAAVVSLMETDTAVNVLREIERE 132
Cdd:TIGR00400  26 KFLK*QP*DIAEALKRLPGTELILLYRFLPKKIAVDTFSNLDQSTQNKLLNSFTNKEISEMINEMNLDDVIDLLEEVPAN 105

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503249015  133 KRGLIIDALSAEVRKEIRLIASFDEDEIGSKMTTNCIIIKEDLTIKQAMSELVRQAEDNDNITTIFVVDDNDEFYGAIDL 212
Cdd:TIGR00400 106 VVQQLLASSTEEERKAINLLLSYSDDSAGRIMTIEYVELKEDYTVGKALDYIRRVAKTKEDIYTLYVTNESKHLKGVLSI 185

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503249015  213 KELITARSTRSLESLIMTSFPYVYANEEIDECIEKLKDYSEDLIPVLDNSSRLLGVITAKSLIEVVDDEMGEDYVMFAGL 292
Cdd:TIGR00400 186 RDLILAKPEEILSSIMRSSVFSIVGVNDQEEVARLIQKYDFLAVPVVDNEGRLVGIVTVDDIIDVIQSEATEDFYMIAAV 265

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503249015  293 TAEED--LQEPLLQSMKKRLPWLLVLLGLGLVVSGVVGVFEKVISQLTLIMAFQSLILDMAGNVGTQSLAVTIRVLTDEN 370
Cdd:TIGR00400 266 KPLDDsyFDTSILVMAKNRIIWLLVLLVSSTFTATIISNYEDLLLSLVALANFIPLLMDTSGNAGSQSSAVVIRGLALET 345

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503249015  371 LTFRQKMHLVAKETRVglsnGILLGLMSFAMVGLYIMFFKHRtAGFSFAVSGCigvsLMLAMLISSAVGTIIPLFFKKIK 450
Cdd:TIGR00400 346 VKVKDFFKVILREICV----SILVGAILASVNFLRIVFFQGK-LLIAFVVSSS----LFVSLTVAKILGGLLPIVAKLLK 416

                         410       420       430
                  ....*....|....*....|....*....|.
gi 503249015  451 VDPAVASGPLITTVNDLVAVVTYYGLS-WLL 480
Cdd:TIGR00400 417 LDPALMSGPLITTIADALTLIIYFNIAkWVL 447
MgtE pfam01769
Divalent cation transporter; This region is the integral membrane part of the eubacterial MgtE ...
 346-476 4.95e-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: 127.17  E-value: 4.95e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503249015  346 LILDMAGNVGTQSLAVTIRVLTDENLTFRQKMHLVAKETRVGLSNGILLGLMSFAMVGLYIMFFKhrtagfsfaVSGCIG 425
Cdd:pfam01769   3 VILGLGGNLGSQSASRLSRALALGEIEPRDAWRVLLKELLVGLLLGLVLGLIAGVLAFLWFGGLL---------LGLVVG 73

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 503249015  426 VSLMLAMLISSAVGTIIPLFFKKIKVDPAVASGPLITTVNDLVAVVTYYGL 476
Cdd:pfam01769  74 LALLLAVLIALLLGTLLPLLLWRLGLDPDNASGPLITTLGDLLGLLILFGI 124
CBS_pair_Mg_transporter cd04606
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains in the magnesium ...
 158-280 2.15e-24

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: 97.79  E-value: 2.15e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503249015 158 DEIGSKMTTNCIIIKEDLTIKQAMSELVRQAEDNDNITTIFVVDDNDEFYGAIDLKELITARSTRSLESLIMTSFPYVYA 237
Cdd:cd04606    1 DSAGRLMTTEFVAVRPDWTVEEALEYLRRLAPDPETIYYIYVVDEDRRLLGVVSLRDLLLADPDTKVSDIMDTDVISVSA 80

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 503249015 238 NEEIDECIEKLKDYseDL--IPVLDNSSRLLGVITakslievVDD 280
Cdd:cd04606   81 DDDQEEVARLFAKY--DLlaLPVVDEEGRLVGIIT-------VDD 116
MgtE_N pfam03448
MgtE intracellular N domain; This domain is found at the N-terminus of eubacterial magnesium ...
 57-158 2.64e-19

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: 82.98  E-value: 2.64e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503249015   57 YHGNDIAGVMADLSKQERQKLYRVCNGDMLAEAFEYLDEDDAGIYLNEMDLNKAAAVVSLMETDTAVNVLREIEREKRGL 136
Cdd:pfam03448   1 LHPADIAELLEELPPEERLALLRLLPPETAAEVLEELDEDVQAELIEALDPEEAAELLEELDPDDAADLLEELPEEKVEE 80

                          90       100
                  ....*....|....*....|..
gi 503249015  137 IIDALSAEVRKEIRLIASFDED 158
Cdd:pfam03448  81 ILSLLDPEERKEIRELLSYPED 102
MgtE_N smart00924
MgtE intracellular N domain; This region is the integral membrane part of the eubacterial MgtE ...
 57-160 3.42e-15

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: 71.39  E-value: 3.42e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503249015    57 YHGNDIAGVMADLSKQERQKLYRVCNGDMLAEAFEYLDEDDAGIYLNEMDLNKAAA-VVSLMETDTAVNVLREIEREKRG 135
Cdd:smart00924   1 LHPADIADLLEELPPEERAELFRLLPPERAAEVLEELDEEVQAELLEALPPDERAAeLLEELDPDDAADLLEELPEEVRE 80

                           90       100
                   ....*....|....*....|....*
gi 503249015   136 LIIDALSAEVRKEIRLIASFDEDEI 160
Cdd:smart00924  81 ELLSLLDPEEREEIRELLSYPEDTA 105
CBS COG0517
CBS domain [Signal transduction mechanisms];
164-282 1.97e-12

CBS domain [Signal transduction mechanisms];


Pssm-ID: 440283 [Multi-domain]  Cd Length: 128  Bit Score: 64.12  E-value: 1.97e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503249015 164 MTTNCIIIKEDLTIKQAMSELVRQaedndNITTIFVVDDNDEFYGAI---DLKELITARSTRSLE---SLIMTSFP-YVY 236
Cdd:COG0517    7 MTTDVVTVSPDATVREALELMSEK-----RIGGLPVVDEDGKLVGIVtdrDLRRALAAEGKDLLDtpvSEVMTRPPvTVS 81

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 503249015 237 ANEEIDECIEKLKDYSEDLIPVLDNSSRLLGVITAKSLIEVVDDEM 282
Cdd:COG0517   82 PDTSLEEAAELMEEHKIRRLPVVDDDGRLVGIITIKDLLKALLEPL 127
COG3448 COG3448
CBS-domain-containing membrane protein [Signal transduction mechanisms];
164-285 2.74e-11

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


Pssm-ID: 442671 [Multi-domain]  Cd Length: 136  Bit Score: 61.03  E-value: 2.74e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503249015 164 MTTNCIIIKEDLTIKQAMSELVRQaedndNITTIFVVDDNDEFYGAIDLKELITARSTRSLESL-----------IMTS- 231
Cdd:COG3448    8 MTRDVVTVSPDTTLREALELMREH-----GIRGLPVVDEDGRLVGIVTERDLLRALLPDRLDELeerlldlpvedVMTRp 82

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....
gi 503249015 232 FPYVYANEEIDECIEKLKDYSEDLIPVLDNSSRLLGVITAKSLIEVVDDEMGED 285
Cdd:COG3448   83 VVTVTPDTPLEEAAELMLEHGIHRLPVVDDDGRLVGIVTRTDLLRALARLLEEE 136
CBS_pair_SF cd02205
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains superfamily; The CBS ...
 169-275 7.30e-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: 7.30e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503249015 169 IIIKEDLTIKQAMSELVRqaednDNITTIFVVDDNDEFYGAIDLKELITAR------STRSLESLIMTSFPYVYANEEID 242
Cdd:cd02205    5 VTVDPDTTVREALELMAE-----NGIGALPVVDDDGKLVGIVTERDILRALvegglaLDTPVAEVMTPDVITVSPDTDLE 79

                         90       100       110
                 ....*....|....*....|....*....|...
gi 503249015 243 ECIEKLKDYSEDLIPVLDNSSRLLGVITAKSLI 275
Cdd:cd02205   80 EALELMLEHGIRRLPVVDDDGKLVGIVTRRDIL 112
COG2524 COG2524
Predicted transcriptional regulator, contains C-terminal CBS domains [Transcription];
110-278 3.58e-09

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


Pssm-ID: 442013 [Multi-domain]  Cd Length: 206  Bit Score: 56.82  E-value: 3.58e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503249015 110 AAAVVSLMETDTAVNVLREIEREKRGLIIDALSAEVRKEIRLIASFDEDEIGSKMTTNCIIIKEDLTIKQAMSELVRQae 189
Cdd:COG2524   38 AATVLLLAAAAAAAGAGGLGLLLLLLLIVLQAAAVRVVAEKELGLVLKMKVKDIMTKDVITVSPDTTLEEALELMLEK-- 115

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503249015 190 dndNITTIFVVDDnDEFYGAIDLKELITA-RSTRSLESL----IMTS-FPYVYANEEIDECIEKLKDYSEDLIPVLDNSS 263
Cdd:COG2524  116 ---GISGLPVVDD-GKLVGIITERDLLKAlAEGRDLLDApvsdIMTRdVVTVSEDDSLEEALRLMLEHGIGRLPVVDDDG 191

                        170
                 ....*....|....*
gi 503249015 264 RLLGVITAKSLIEVV 278
Cdd:COG2524  192 KLVGIITRTDILRAL 206
COG2905 COG2905
Signal-transduction protein containing cAMP-binding, CBS, and nucleotidyltransferase domains ...
 164-282 4.46e-08

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


Pssm-ID: 442149 [Multi-domain]  Cd Length: 124  Bit Score: 51.37  E-value: 4.46e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503249015 164 MTTNCIIIKEDLTIKQAMSELVRQaedndNITTIFVVDDNDEFYGAI---DLKELITARSTRSLE---SLIMTSFP-YVY 236
Cdd:COG2905    5 MSRDVVTVSPDATVREAARLMTEK-----GVGSLVVVDDDGRLVGIItdrDLRRRVLAEGLDPLDtpvSEVMTRPPiTVS 79

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 503249015 237 ANEEIDECIEKLKDYSEDLIPVLDNsSRLLGVITAKSLIEVVDDEM 282
Cdd:COG2905   80 PDDSLAEALELMEEHRIRHLPVVDD-GKLVGIVSITDLLRALSEEL 124
CBS_pair_ABC_OpuCA_assoc cd04583
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains found associated with ...
 166-278 6.73e-08

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: 50.59  E-value: 6.73e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503249015 166 TNCIIIKEDLTIKQAMSELVRQAEDndnitTIFVVDDNDEFYGAIDLKEL-ITARSTRSLESLIMTSFPYVYANEEIDEC 244
Cdd:cd04583    2 TNPVTITPERTLAQAIEIMREKRVD-----SLLVVDKDNVLLGIVDIEDInRNYRKAKKVGEIMERDVFTVKEDSLLRDT 76

                         90       100       110
                 ....*....|....*....|....*....|....
gi 503249015 245 IEKLKDYSEDLIPVLDNSSRLLGVITAKSLIEVV 278
Cdd:cd04583   77 VDRILKRGLKYVPVVDEQGRLVGLVTRASLVDIV 110
CBS_pair_arch_MET2_assoc cd04605
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with the ...
 164-274 8.73e-06

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: 44.92  E-value: 8.73e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503249015 164 MTTNCIIIKEDLTIKQAMSELVrqaedNDNITTIFVVDDNDEFYGAI---DLKELItARSTRSLESlIMT-SFPYVYANE 239
Cdd:cd04605    6 MSKDVATIREDISIEEAAKIMI-----DKNVTHLPVVSEDGKLIGIVtswDISKAV-ALKKDSLEE-IMTrNVITARPDE 78

                         90       100       110
                 ....*....|....*....|....*....|....*
gi 503249015 240 EIDECIEKLKDYSEDLIPVLDNSSRLLGVITAKSL 274
Cdd:cd04605   79 PIELAARKMEKHNISALPVVDDDRRVIGIITSDDI 113
YtoI COG4109
Predicted transcriptional regulator containing CBS domains [Transcription];
165-276 9.78e-06

Predicted transcriptional regulator containing CBS domains [Transcription];


Pssm-ID: 443285 [Multi-domain]  Cd Length: 135  Bit Score: 45.29  E-value: 9.78e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503249015 165 TTNCIIIKEDLTIKQAMSELVRQAEDndnittIF-VVDDNDEFYGAIDLKELITARSTRSLESLIMTSFPYVYANEEIDE 243
Cdd:COG4109   24 LEDVATLSEDDTVEDALELLEKTGHS------RFpVVDENGRLVGIVTSKDILGKDDDTPIEDVMTKNPITVTPDTSLAS 97

                         90       100       110
                 ....*....|....*....|....*....|...
gi 503249015 244 CIEKLKDYSEDLIPVLDNSSRLLGVITAKSLIE 276
Cdd:COG4109   98 AAHKMIWEGIELLPVVDDDGRLLGIISRQDVLK 130
CBS_pair_peptidase_M50 cd04639
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains found in the ...
 164-276 1.61e-05

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


Pssm-ID: 341397 [Multi-domain]  Cd Length: 120  Bit Score: 44.10  E-value: 1.61e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503249015 164 MTTNCIIIKEDLTIKQAMSELVRQaedNDNITTIFVVDDNDEFYGAIDLKELITARS----TRSLESLIMT--SFPYVYA 237
Cdd:cd04639    3 MVTEFPIVDADLTLREFADDYLIG---KKSWREFLVTDEAGRLVGLITVDDLRAIPTsqwpDTPVRELMKPleEIPTVAA 79

                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 503249015 238 NEEIDECIEKLKDYSEDLIPVLDNSSRLLGVITAKSLIE 276
Cdd:cd04639   80 DQSLLEVVKLLEEQQLPALAVVSENGTLVGLIEKEDIIE 118
CBS_pair_CcpN cd04617
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains of CcpN repressor; ...
 169-269 2.83e-05

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


Pssm-ID: 341387 [Multi-domain]  Cd Length: 125  Bit Score: 43.63  E-value: 2.83e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503249015 169 IIIKEDLTIKQAMSELVrqaedNDNITTIFVVDDNDEFYGAIDLKELI-TARSTRSLE----SLIMTSFP---YVYANEE 240
Cdd:cd04617    7 VVVDETTSVYDAIVTLF-----LEDVGSLFVVDEEGYLVGVVSRKDLLkATLGGQDLEktpvSMIMTRMPnivTVTPDDS 81

                         90       100
                 ....*....|....*....|....*....
gi 503249015 241 IDECIEKLKDYSEDLIPVLDNSSRLLGVI 269
Cdd:cd04617   82 VLEAARKLIEHEIDSLPVVEKEDGKLKVV 110
CBS_pair_bac cd17783
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains present in bacteria; ...
 199-276 7.90e-05

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


Pssm-ID: 341419 [Multi-domain]  Cd Length: 108  Bit Score: 41.79  E-value: 7.90e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503249015 199 VVDDNdEFYGAIDLKELITARSTRSLESLIMTSF--PYVYANEEIDECIEKLKDYSEDLIPVLDNSSRLLGVITAKSLIE 276
Cdd:cd17783   30 VVDNG-QYLGLISEDDLLELNDPEAPLSNLPLSLkdVFVYEDQHFYDVIRLASEYKLEVVPVLDEENEYLGVITVNDLLA 108
CBS_pair_arch cd09836
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains; The CBS domain, ...
 164-278 1.11e-04

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


Pssm-ID: 341405 [Multi-domain]  Cd Length: 116  Bit Score: 41.74  E-value: 1.11e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503249015 164 MTTNCIIIKEDLTIKQAMSELVRQaedndNITTIFVVDDNDEFYGAI---DLKELITAR-STRSLESLIMTSFP-YVYAN 238
Cdd:cd09836    1 MSKPVVTVPPETTIREAAKLMAEN-----NIGSVVVVDDDGKPVGIVterDIVRAVAEGiDLDTPVEEIMTKNLvTVSPD 75

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 503249015 239 EEIDECIEKLKDYSEDLIPVLDNSSRLLGVITAKSLIEVV 278
Cdd:cd09836   76 ESIYEAAELMREHNIRHLPVVDGGGKLVGVISIRDLAREL 115
CBS pfam00571
CBS domain; CBS domains are small intracellular modules that pair together to form a stable ...
 224-280 3.78e-04

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


Pssm-ID: 425756 [Multi-domain]  Cd Length: 57  Bit Score: 38.35  E-value: 3.78e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 503249015  224 LESLIMTSFPYVYANEEIDECIEKLKDYSEDLIPVLDNSSRLLGVITAKSLIEVVDD 280
Cdd:pfam00571   1 VKDIMTKDVVTVSPDTTLEEALELMREHGISRLPVVDEDGKLVGIVTLKDLLRALLG 57
YtoI COG4109
Predicted transcriptional regulator containing CBS domains [Transcription];
211-288 4.55e-04

Predicted transcriptional regulator containing CBS domains [Transcription];


Pssm-ID: 443285 [Multi-domain]  Cd Length: 135  Bit Score: 40.28  E-value: 4.55e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 503249015 211 DLKELITARstrslESLIMTSFPYVYANEEIDECIEKLKDYSEDLIPVLDNSSRLLGVITAKSLIEVVDDEMGEDyVM 288
Cdd:COG4109   11 TFKEILLVE-----DIMTLEDVATLSEDDTVEDALELLEKTGHSRFPVVDENGRLVGIVTSKDILGKDDDTPIED-VM 82
CBS pfam00571
CBS domain; CBS domains are small intracellular modules that pair together to form a stable ...
 164-218 5.55e-04

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


Pssm-ID: 425756 [Multi-domain]  Cd Length: 57  Bit Score: 37.96  E-value: 5.55e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 503249015  164 MTTNCIIIKEDLTIKQAMSELVRQaedndNITTIFVVDDNDEFYGAIDLKELITA 218
Cdd:pfam00571   5 MTKDVVTVSPDTTLEEALELMREH-----GISRLPVVDEDGKLVGIVTLKDLLRA 54
CBS_pair_inorgPPase cd04597
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with ...
 190-276 9.91e-04

Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with family II inorganic pyrophosphatase; This cd contains two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with a subgroup of family II inorganic pyrophosphatases (PPases) that also contain a DRTGG domain. The homolog from Clostridium has been shown to be inhibited by AMP and activated by a novel effector, diadenosine 5',5-P1,P4-tetraphosphate (AP(4)A), which has been shown to bind to the CBS domain. The CBS domain, named after human CBS, is a small domain originally identified in cystathionine beta-synthase and is subsequently found in a wide range of different proteins. CBS domains usually occur in tandem repeats. They associate to form a so-called Bateman domain or a CBS pair based on crystallographic studies in bacteria. The CBS pair was used as a basis for this cd hierarchy since the human CBS proteins can adopt the typical core structure and form an intramolecular CBS pair. The interface between the two CBS domains forms a cleft that is a potential ligand binding site. The CBS pair coexists with a variety of other functional domains and this has been used to help in its classification here.


Pssm-ID: 341372 [Multi-domain]  Cd Length: 106  Bit Score: 38.87  E-value: 9.91e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503249015 190 DNDNITTIFVVDDNDEFYGAIDLKELitarsTRSLESLIMTSFPYVYANEE-IDECIEKLKDYSEDLIPVLDNSSRLLGV 268
Cdd:cd04597   24 DENNLKTLPVTDDNGKLIGLLSISDI-----ARTVDYIMTKDNLIVFKEDDyLDEVKEIMLNTNFRNYPVVDENNKFLGT 98


                 ....*...
gi 503249015 269 ITAKSLIE 276
Cdd:cd04597   99 ISRKHLIN 106
CBS_pair_bac_arch cd17785
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains present in bacteria ...
 159-267 1.11e-03

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


Pssm-ID: 341421 [Multi-domain]  Cd Length: 136  Bit Score: 39.18  E-value: 1.11e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503249015 159 EIGSKMTTNCIIIKEDLTIKQamselVRQAEDNDNIT-TIFVVDDNDEFYGAIDLKELI--------------------T 217
Cdd:cd17785    3 DIYNLITKKPSVVHENTSIRD-----VIDKMIEDPKTrSVYVVDDDEKLLGIITLMELLkyigyrfgvtiykgvsfgllL 77

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|
gi 503249015 218 ARSTRSLESLIMTSFPYVYANEEIDECIEKLKDYSEDLIPVLDNSSRLLG 267
Cdd:cd17785   78 RISLKEKAKDIMLSPIYVKKEDTLEEALELMVKNRLQELPVVDENGKVIG 127
CBS_pair_ABC_Gly_Pro_assoc cd09831
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains found associated with ...
 197-279 2.21e-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: 37.92  E-value: 2.21e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503249015 197 IFVVDDNDEFYGAIDLKELITARS--TRSLESLIMTSFPYVYANEEIDECIEKLKD--YSedlIPVLDNSSRLLGVITAK 272
Cdd:cd09831   33 GYVVDKKRRFLGVVSVDSLRAALKenAQSLEDAFLTDVETVPADTSLSDILGLVASapCP---LPVVDEDGRYLGVISKA 109


                 ....*..
gi 503249015 273 SLIEVVD 279
Cdd:cd09831  110 SLLETLD 116
CBS_pair_ACT cd17787
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains found in Thermatoga ...
 171-276 2.65e-03

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


Pssm-ID: 341423 [Multi-domain]  Cd Length: 111  Bit Score: 37.78  E-value: 2.65e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503249015 171 IKEDLTIKQAMSELvRQAEdndnITTIFVVDDNDEFYGAIDLKELITARSTRSLESLIMTSFPYVYANEEIDECIEKLKD 250
Cdd:cd17787    7 FEESATVGEVLHEM-RKYE----TDYCIVVDEEGKFAGMVRKSKIMDEDLDKKVKEYVVEPDFYCHEEDYIEDAALLLIE 81

                         90       100
                 ....*....|....*....|....*.
gi 503249015 251 YSEDLIPVLDNSSRLLGVITAKSLIE 276
Cdd:cd17787   82 SHEFVLPVVNSDMKVKGVLTVFEILE 107
MgtE2 COG1824
Permease, similar to cation transporters [Inorganic ion transport and metabolism];
392-482 3.10e-03

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


Pssm-ID: 441429  Cd Length: 188  Bit Score: 38.69  E-value: 3.10e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503249015 392 ILLGLMSFAMVGLYIMFFKHRTAGFSFAVSGCIGVSL---MLAMLISSAVGTIIPLFFKKIKVDPAVASGPLITTVNDLV 468
Cdd:COG1824   94 LILALLISPLIGVLAWLVAVLLGRGSLGLLTLVGIALlagLLLALLLIVVTYYVAIASYRFGLDPDNVVIPVVTTLGDVF 173

                         90
                 ....*....|....
gi 503249015 469 AVVTYYGLSWLLLL 482
Cdd:COG1824  174 GVLFLILVARLVLG 187
CBS_pair_voltage-gated_CLC_archaea cd04594
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with the ...
 169-277 3.95e-03

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


Pssm-ID: 341369 [Multi-domain]  Cd Length: 107  Bit Score: 36.94  E-value: 3.95e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503249015 169 IIIKEDLTIKQAMSELVRqaednDNITTIFVVDDNDEFYGAIDLKElITARSTRSLESLIMTSFPYVYANEEIDECIEKL 248
Cdd:cd04594    5 IKVSAYDTVERALKIMRE-----NNLLSLPVVDNDSNFLGAVYLRD-IENKSPGKVGKYVVRGSPYVTPTSSLEEAWEIM 78

                         90       100
                 ....*....|....*....|....*....
gi 503249015 249 KDYSEDLIPVLDNsSRLLGVITAKSLIEV 277
Cdd:cd04594   79 MRNKSRWVAVVEK-GKFLGIITLDDLLEA 106
CBS_pair_bac cd04629
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains present in bacteria; ...
 164-270 7.08e-03

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


Pssm-ID: 341392 [Multi-domain]  Cd Length: 116  Bit Score: 36.26  E-value: 7.08e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503249015 164 MTTNCIIIKEDLTIKQAMSELVRQaedndNITTIFVVDDNDEFYGAI---D-LKELITAR---STRSLESLIMTSFPY-V 235
Cdd:cd04629    1 MTRNPVTLTPDTSILEAVELLLEH-----KISGAPVVDEQGRLVGFLseqDcLKALLEASyhcEPGGTVADYMSTEVLtV 75

                         90       100       110
                 ....*....|....*....|....*....|....*
gi 503249015 236 YANEEIDECIEKLKDYSEDLIPVLDNsSRLLGVIT 270
Cdd:cd04629   76 SPDTSIVDLAQLFLKNKPRRYPVVED-GKLVGQIS 109
 
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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