NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|1304970003|gb|PKG36859|]
View 

magnesium transporter [Psychrobacter sp. Sarcosine-3u-12]

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

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

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];
8-447 2.34e-158

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


:

Pssm-ID: 441840 [Multi-domain]  Cd Length: 443  Bit Score: 454.91  E-value: 2.34e-158
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1304970003   8 ETFATKLSRAIEQQQFEQAINQVQELRPIDIADVLTLMASKLAWQLLERLPN--RSTVFAYLEPNIQVAMAYEFPRESMV 85
Cdd:COG2239     3 EELLEELRELLEEGDLEELRELLEELHPADIAELLEELPPEERLALFRLLPKelAAEVLEELDEEVQEELLEELSDEELA 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1304970003  86 ILVGEMPADERTDLYKHLNQDQRDALLPALAQAQREDIRRLSAYEERTAGALMTSDYSTLAAHMTVTEALAALRLEAPDA 165
Cdd:COG2239    83 ELLEELDPDDAADLLEELPEEVVEELLALLDPEEREEIRELLSYPEDSAGRLMTTEFVAVREDWTVGEALRYLRRQAEDP 162

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1304970003 166 ETIYHTYVIDDERKLSGVVSLRALILAAPEQLINDIMLSTVVSCNVNDDQEDVAKVVARYDLIALPITDDHGALVGIVTH 245
Cdd:COG2239   163 ETIYYIYVVDDDGRLVGVVSLRDLLLADPDTKVSDIMDTDVISVPADDDQEEVARLFERYDLLALPVVDEEGRLVGIITV 242

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1304970003 246 DDAMDVASDEATDDFHKSGGVTTMVGRlkDVSIKVLYRKRVFWLVFLVFGNLLSGFSIANFEEVIAANLVLVFFLPLLVD 325
Cdd:COG2239   243 DDVVDVIEEEATEDILKLAGVSEDEDL--FASVLKLARKRLPWLLILLLTAFLAASVIGLFEDTLEQVVALAVFMPLVAG 320

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1304970003 326 SGGNAGSQSATLMVRALATGDVVMRDWLSLLGREAIVALMLGATMAVAISIIGYV-RGDAIVSLVLALSMMSVVMIGCVI 404
Cdd:COG2239   321 MGGNAGSQSLTVVVRGLALGEITLSDWWRVLLKELLVGLLNGLILGLVVGLVAYLwFGNPLLGLVVGLALVINVLVAALA 400

                         410       420       430       440
                  ....*....|....*....|....*....|....*....|...
gi 1304970003 405 GMSLPFVLNKIGLDPATASAPLITSVCDASGVLIYLFIASQFL 447
Cdd:COG2239   401 GSLLPLLLKRLGIDPAVASGPFITTITDVVGFFIYLGLATLFL 443
 
Name Accession Description Interval E-value
MgtE COG2239
Mg/Co/Ni transporter MgtE (contains CBS domain) [Inorganic ion transport and metabolism];
8-447 2.34e-158

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


Pssm-ID: 441840 [Multi-domain]  Cd Length: 443  Bit Score: 454.91  E-value: 2.34e-158
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1304970003   8 ETFATKLSRAIEQQQFEQAINQVQELRPIDIADVLTLMASKLAWQLLERLPN--RSTVFAYLEPNIQVAMAYEFPRESMV 85
Cdd:COG2239     3 EELLEELRELLEEGDLEELRELLEELHPADIAELLEELPPEERLALFRLLPKelAAEVLEELDEEVQEELLEELSDEELA 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1304970003  86 ILVGEMPADERTDLYKHLNQDQRDALLPALAQAQREDIRRLSAYEERTAGALMTSDYSTLAAHMTVTEALAALRLEAPDA 165
Cdd:COG2239    83 ELLEELDPDDAADLLEELPEEVVEELLALLDPEEREEIRELLSYPEDSAGRLMTTEFVAVREDWTVGEALRYLRRQAEDP 162

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1304970003 166 ETIYHTYVIDDERKLSGVVSLRALILAAPEQLINDIMLSTVVSCNVNDDQEDVAKVVARYDLIALPITDDHGALVGIVTH 245
Cdd:COG2239   163 ETIYYIYVVDDDGRLVGVVSLRDLLLADPDTKVSDIMDTDVISVPADDDQEEVARLFERYDLLALPVVDEEGRLVGIITV 242

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1304970003 246 DDAMDVASDEATDDFHKSGGVTTMVGRlkDVSIKVLYRKRVFWLVFLVFGNLLSGFSIANFEEVIAANLVLVFFLPLLVD 325
Cdd:COG2239   243 DDVVDVIEEEATEDILKLAGVSEDEDL--FASVLKLARKRLPWLLILLLTAFLAASVIGLFEDTLEQVVALAVFMPLVAG 320

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1304970003 326 SGGNAGSQSATLMVRALATGDVVMRDWLSLLGREAIVALMLGATMAVAISIIGYV-RGDAIVSLVLALSMMSVVMIGCVI 404
Cdd:COG2239   321 MGGNAGSQSLTVVVRGLALGEITLSDWWRVLLKELLVGLLNGLILGLVVGLVAYLwFGNPLLGLVVGLALVINVLVAALA 400

                         410       420       430       440
                  ....*....|....*....|....*....|....*....|...
gi 1304970003 405 GMSLPFVLNKIGLDPATASAPLITSVCDASGVLIYLFIASQFL 447
Cdd:COG2239   401 GSLLPLLLKRLGIDPAVASGPFITTITDVVGFFIYLGLATLFL 443
mgtE TIGR00400
Mg2+ transporter (mgtE); This family of prokaryotic proteins models a class of Mg++ ...
 18-449 8.66e-90

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: 280.17  E-value: 8.66e-90
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1304970003  18 IEQQQFEQAINQVQELRPIDIADVLTLMASKLAWQLLERLPNRSTV--FAYLEPNIQVAMAYEFPRESMVILVGEMPADE 95
Cdd:TIGR00400  15 LKEKSYSKIKEKFLK*QP*DIAEALKRLPGTELILLYRFLPKKIAVdtFSNLDQSTQNKLLNSFTNKEISEMINEMNLDD 94

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1304970003  96 RTDLYKHLNQDQRDALLPALAQAQREDIRRLSAYEERTAGALMTSDYSTLAAHMTVTEALAALRLEAPDAETIYHTYVID 175
Cdd:TIGR00400  95 VIDLLEEVPANVVQQLLASSTEEERKAINLLLSYSDDSAGRIMTIEYVELKEDYTVGKALDYIRRVAKTKEDIYTLYVTN 174

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1304970003 176 DERKLSGVVSLRALILAAPEQLINDIMLSTVVSCNVNDDQEDVAKVVARYDLIALPITDDHGALVGIVTHDDAMDVASDE 255
Cdd:TIGR00400 175 ESKHLKGVLSIRDLILAKPEEILSSIMRSSVFSIVGVNDQEEVARLIQKYDFLAVPVVDNEGRLVGIVTVDDIIDVIQSE 254

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1304970003 256 ATDDFHKSGGVTTMVGRLKDVSIKVLYRKRVFWLVFLVFGNLLSGFSIANFEEVIAANLVLVFFLPLLVDSGGNAGSQSA 335
Cdd:TIGR00400 255 ATEDFYMIAAVKPLDDSYFDTSILVMAKNRIIWLLVLLVSSTFTATIISNYEDLLLSLVALANFIPLLMDTSGNAGSQSS 334

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1304970003 336 TLMVRALATGDVVMRDWLSLLGREAIVALMLGATMAVAISIIGYV-RGDAIVSLVLALSMMSVVMIGCVIGMSLPFVLNK 414
Cdd:TIGR00400 335 AVVIRGLALETVKVKDFFKVILREICVSILVGAILASVNFLRIVFfQGKLLIAFVVSSSLFVSLTVAKILGGLLPIVAKL 414

                         410       420       430
                  ....*....|....*....|....*....|....*
gi 1304970003 415 IGLDPATASAPLITSVCDASGVLIYLFIASQFLSI 449
Cdd:TIGR00400 415 LKLDPALMSGPLITTIADALTLIIYFNIAKWVLVS 449
CBS_pair_Mg_transporter cd04606
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains in the magnesium ...
 133-252 2.62e-55

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: 179.45  E-value: 2.62e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1304970003 133 TAGALMTSDYSTLAAHMTVTEALAALRLEAPDAETIYHTYVIDDERKLSGVVSLRALILAAPEQLINDIMLSTVVSCNVN 212
Cdd:cd04606     2 SAGRLMTTEFVAVRPDWTVEEALEYLRRLAPDPETIYYIYVVDEDRRLLGVVSLRDLLLADPDTKVSDIMDTDVISVSAD 81

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 1304970003 213 DDQEDVAKVVARYDLIALPITDDHGALVGIVTHDDAMDVA 252
Cdd:cd04606    82 DDQEEVARLFAKYDLLALPVVDEEGRLVGIITVDDVLDVI 121
MgtE pfam01769
Divalent cation transporter; This region is the integral membrane part of the eubacterial MgtE ...
 325-442 2.13e-34

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: 124.86  E-value: 2.13e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1304970003 325 DSGGNAGSQSATLMVRALATGDVVMRDWLSLLGREAIVALMLGATMAVAISIIGYV-RGDAIVSLVLALSMMSVVMIGCV 403
Cdd:pfam01769   6 GLGGNLGSQSASRLSRALALGEIEPRDAWRVLLKELLVGLLLGLVLGLIAGVLAFLwFGGLLLGLVVGLALLLAVLIALL 85

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 1304970003 404 IGMSLPFVLNKIGLDPATASAPLITSVCDASGVLIYLFI 442
Cdd:pfam01769  86 LGTLLPLLLWRLGLDPDNASGPLITTLGDLLGLLILFGI 124
MgtE_N smart00924
MgtE intracellular N domain; This region is the integral membrane part of the eubacterial MgtE ...
 33-134 2.85e-16

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: 74.09  E-value: 2.85e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1304970003   33 LRPIDIADVLTLMASKLAWQLLERLPN--RSTVFAYLEPNIQVAMAYEF-PRESMVILVGEMPADERTDLYKHLNQDQRD 109
Cdd:smart00924   1 LHPADIADLLEELPPEERAELFRLLPPerAAEVLEELDEEVQAELLEALpPDERAAELLEELDPDDAADLLEELPEEVRE 80

                           90       100
                   ....*....|....*....|....*
gi 1304970003  110 ALLPALAQAQREDIRRLSAYEERTA 134
Cdd:smart00924  81 ELLSLLDPEEREEIRELLSYPEDTA 105
PRK07807 PRK07807
GuaB1 family IMP dehydrogenase-related protein;
144-248 3.38e-03

GuaB1 family IMP dehydrogenase-related protein;


Pssm-ID: 181127 [Multi-domain]  Cd Length: 479  Bit Score: 39.50  E-value: 3.38e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1304970003 144 TLAAHMTVTEALAALRLEAPDAetiyhTYVIDDERKLSGVVSLRALILAAPEQLINDIMLSTVVSCNVNDDQEDVAKVVA 223
Cdd:PRK07807  101 TLSPDDTVGDALALLPKRAHGA-----VVVVDEEGRPVGVVTEADCAGVDRFTQVRDVMSTDLVTLPAGTDPREAFDLLE 175

                          90       100
                  ....*....|....*....|....*
gi 1304970003 224 RYDLIALPITDDHGALVGIVTHDDA 248
Cdd:PRK07807  176 AARVKLAPVVDADGRLVGVLTRTGA 200
 
Name Accession Description Interval E-value
MgtE COG2239
Mg/Co/Ni transporter MgtE (contains CBS domain) [Inorganic ion transport and metabolism];
8-447 2.34e-158

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


Pssm-ID: 441840 [Multi-domain]  Cd Length: 443  Bit Score: 454.91  E-value: 2.34e-158
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1304970003   8 ETFATKLSRAIEQQQFEQAINQVQELRPIDIADVLTLMASKLAWQLLERLPN--RSTVFAYLEPNIQVAMAYEFPRESMV 85
Cdd:COG2239     3 EELLEELRELLEEGDLEELRELLEELHPADIAELLEELPPEERLALFRLLPKelAAEVLEELDEEVQEELLEELSDEELA 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1304970003  86 ILVGEMPADERTDLYKHLNQDQRDALLPALAQAQREDIRRLSAYEERTAGALMTSDYSTLAAHMTVTEALAALRLEAPDA 165
Cdd:COG2239    83 ELLEELDPDDAADLLEELPEEVVEELLALLDPEEREEIRELLSYPEDSAGRLMTTEFVAVREDWTVGEALRYLRRQAEDP 162

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1304970003 166 ETIYHTYVIDDERKLSGVVSLRALILAAPEQLINDIMLSTVVSCNVNDDQEDVAKVVARYDLIALPITDDHGALVGIVTH 245
Cdd:COG2239   163 ETIYYIYVVDDDGRLVGVVSLRDLLLADPDTKVSDIMDTDVISVPADDDQEEVARLFERYDLLALPVVDEEGRLVGIITV 242

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1304970003 246 DDAMDVASDEATDDFHKSGGVTTMVGRlkDVSIKVLYRKRVFWLVFLVFGNLLSGFSIANFEEVIAANLVLVFFLPLLVD 325
Cdd:COG2239   243 DDVVDVIEEEATEDILKLAGVSEDEDL--FASVLKLARKRLPWLLILLLTAFLAASVIGLFEDTLEQVVALAVFMPLVAG 320

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1304970003 326 SGGNAGSQSATLMVRALATGDVVMRDWLSLLGREAIVALMLGATMAVAISIIGYV-RGDAIVSLVLALSMMSVVMIGCVI 404
Cdd:COG2239   321 MGGNAGSQSLTVVVRGLALGEITLSDWWRVLLKELLVGLLNGLILGLVVGLVAYLwFGNPLLGLVVGLALVINVLVAALA 400

                         410       420       430       440
                  ....*....|....*....|....*....|....*....|...
gi 1304970003 405 GMSLPFVLNKIGLDPATASAPLITSVCDASGVLIYLFIASQFL 447
Cdd:COG2239   401 GSLLPLLLKRLGIDPAVASGPFITTITDVVGFFIYLGLATLFL 443
mgtE TIGR00400
Mg2+ transporter (mgtE); This family of prokaryotic proteins models a class of Mg++ ...
 18-449 8.66e-90

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: 280.17  E-value: 8.66e-90
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1304970003  18 IEQQQFEQAINQVQELRPIDIADVLTLMASKLAWQLLERLPNRSTV--FAYLEPNIQVAMAYEFPRESMVILVGEMPADE 95
Cdd:TIGR00400  15 LKEKSYSKIKEKFLK*QP*DIAEALKRLPGTELILLYRFLPKKIAVdtFSNLDQSTQNKLLNSFTNKEISEMINEMNLDD 94

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1304970003  96 RTDLYKHLNQDQRDALLPALAQAQREDIRRLSAYEERTAGALMTSDYSTLAAHMTVTEALAALRLEAPDAETIYHTYVID 175
Cdd:TIGR00400  95 VIDLLEEVPANVVQQLLASSTEEERKAINLLLSYSDDSAGRIMTIEYVELKEDYTVGKALDYIRRVAKTKEDIYTLYVTN 174

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1304970003 176 DERKLSGVVSLRALILAAPEQLINDIMLSTVVSCNVNDDQEDVAKVVARYDLIALPITDDHGALVGIVTHDDAMDVASDE 255
Cdd:TIGR00400 175 ESKHLKGVLSIRDLILAKPEEILSSIMRSSVFSIVGVNDQEEVARLIQKYDFLAVPVVDNEGRLVGIVTVDDIIDVIQSE 254

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1304970003 256 ATDDFHKSGGVTTMVGRLKDVSIKVLYRKRVFWLVFLVFGNLLSGFSIANFEEVIAANLVLVFFLPLLVDSGGNAGSQSA 335
Cdd:TIGR00400 255 ATEDFYMIAAVKPLDDSYFDTSILVMAKNRIIWLLVLLVSSTFTATIISNYEDLLLSLVALANFIPLLMDTSGNAGSQSS 334

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1304970003 336 TLMVRALATGDVVMRDWLSLLGREAIVALMLGATMAVAISIIGYV-RGDAIVSLVLALSMMSVVMIGCVIGMSLPFVLNK 414
Cdd:TIGR00400 335 AVVIRGLALETVKVKDFFKVILREICVSILVGAILASVNFLRIVFfQGKLLIAFVVSSSLFVSLTVAKILGGLLPIVAKL 414

                         410       420       430
                  ....*....|....*....|....*....|....*
gi 1304970003 415 IGLDPATASAPLITSVCDASGVLIYLFIASQFLSI 449
Cdd:TIGR00400 415 LKLDPALMSGPLITTIADALTLIIYFNIAKWVLVS 449
CBS_pair_Mg_transporter cd04606
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains in the magnesium ...
 133-252 2.62e-55

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: 179.45  E-value: 2.62e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1304970003 133 TAGALMTSDYSTLAAHMTVTEALAALRLEAPDAETIYHTYVIDDERKLSGVVSLRALILAAPEQLINDIMLSTVVSCNVN 212
Cdd:cd04606     2 SAGRLMTTEFVAVRPDWTVEEALEYLRRLAPDPETIYYIYVVDEDRRLLGVVSLRDLLLADPDTKVSDIMDTDVISVSAD 81

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 1304970003 213 DDQEDVAKVVARYDLIALPITDDHGALVGIVTHDDAMDVA 252
Cdd:cd04606    82 DDQEEVARLFAKYDLLALPVVDEEGRLVGIITVDDVLDVI 121
MgtE pfam01769
Divalent cation transporter; This region is the integral membrane part of the eubacterial MgtE ...
 325-442 2.13e-34

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: 124.86  E-value: 2.13e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1304970003 325 DSGGNAGSQSATLMVRALATGDVVMRDWLSLLGREAIVALMLGATMAVAISIIGYV-RGDAIVSLVLALSMMSVVMIGCV 403
Cdd:pfam01769   6 GLGGNLGSQSASRLSRALALGEIEPRDAWRVLLKELLVGLLLGLVLGLIAGVLAFLwFGGLLLGLVVGLALLLAVLIALL 85

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 1304970003 404 IGMSLPFVLNKIGLDPATASAPLITSVCDASGVLIYLFI 442
Cdd:pfam01769  86 LGTLLPLLLWRLGLDPDNASGPLITTLGDLLGLLILFGI 124
MgtE_N smart00924
MgtE intracellular N domain; This region is the integral membrane part of the eubacterial MgtE ...
 33-134 2.85e-16

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: 74.09  E-value: 2.85e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1304970003   33 LRPIDIADVLTLMASKLAWQLLERLPN--RSTVFAYLEPNIQVAMAYEF-PRESMVILVGEMPADERTDLYKHLNQDQRD 109
Cdd:smart00924   1 LHPADIADLLEELPPEERAELFRLLPPerAAEVLEELDEEVQAELLEALpPDERAAELLEELDPDDAADLLEELPEEVRE 80

                           90       100
                   ....*....|....*....|....*
gi 1304970003  110 ALLPALAQAQREDIRRLSAYEERTA 134
Cdd:smart00924  81 ELLSLLDPEEREEIRELLSYPEDTA 105
MgtE_N pfam03448
MgtE intracellular N domain; This domain is found at the N-terminus of eubacterial magnesium ...
 33-131 5.60e-16

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: 73.36  E-value: 5.60e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1304970003  33 LRPIDIADVLTLMASKLAWQLLERLPN--RSTVFAYLEPNIQVAMAYEFPRESMVILVGEMPADERTDLYKHLNQDQRDA 110
Cdd:pfam03448   1 LHPADIAELLEELPPEERLALLRLLPPetAAEVLEELDEDVQAELIEALDPEEAAELLEELDPDDAADLLEELPEEKVEE 80

                          90       100
                  ....*....|....*....|.
gi 1304970003 111 LLPALAQAQREDIRRLSAYEE 131
Cdd:pfam03448  81 ILSLLDPEERKEIRELLSYPE 101
YtoI COG4109
Predicted transcriptional regulator containing CBS domains [Transcription];
137-249 3.89e-15

Predicted transcriptional regulator containing CBS domains [Transcription];


Pssm-ID: 443285 [Multi-domain]  Cd Length: 135  Bit Score: 71.87  E-value: 3.89e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1304970003 137 LMTSDYSTLAAHMTVTEALAALrleapdAETIYHTY-VIDDERKLSGVVSLRALILAAPEQLINDIMLSTVVSCNVNDDQ 215
Cdd:COG4109    22 MTLEDVATLSEDDTVEDALELL------EKTGHSRFpVVDENGRLVGIVTSKDILGKDDDTPIEDVMTKNPITVTPDTSL 95

                          90       100       110
                  ....*....|....*....|....*....|....
gi 1304970003 216 EDVAKVVARYDLIALPITDDHGALVGIVTHDDAM 249
Cdd:COG4109    96 ASAAHKMIWEGIELLPVVDDDGRLLGIISRQDVL 129
CBS_pair_SF cd02205
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains superfamily; The CBS ...
 139-250 1.07e-14

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: 69.97  E-value: 1.07e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1304970003 139 TSDYSTLAAHMTVTEALAALRLEApdaetIYHTYVIDDERKLSGVVSLRALILA------APEQLINDIMLSTVVSCNVN 212
Cdd:cd02205     1 TRDVVTVDPDTTVREALELMAENG-----IGALPVVDDDGKLVGIVTERDILRAlvegglALDTPVAEVMTPDVITVSPD 75

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 1304970003 213 DDQEDVAKVVARYDLIALPITDDHGALVGIVTHDDAMD 250
Cdd:cd02205    76 TDLEEALELMLEHGIRRLPVVDDDGKLVGIVTRRDILR 113
CBS COG0517
CBS domain [Signal transduction mechanisms];
133-255 1.19e-14

CBS domain [Signal transduction mechanisms];


Pssm-ID: 440283 [Multi-domain]  Cd Length: 128  Bit Score: 70.28  E-value: 1.19e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1304970003 133 TAGALMTSDYSTLAAHMTVTEALAALRleapdAETIYHTYVIDDERKLSGVVSLRALILAA-------PEQLINDIMLST 205
Cdd:COG0517     2 KVKDIMTTDVVTVSPDATVREALELMS-----EKRIGGLPVVDEDGKLVGIVTDRDLRRALaaegkdlLDTPVSEVMTRP 76

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 1304970003 206 VVSCNVNDDQEDVAKVVARYDLIALPITDDHGALVGIVTHDDAMDVASDE 255
Cdd:COG0517    77 PVTVSPDTSLEEAAELMEEHKIRRLPVVDDDGRLVGIITIKDLLKALLEP 126
COG3448 COG3448
CBS-domain-containing membrane protein [Signal transduction mechanisms];
133-247 2.49e-14

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


Pssm-ID: 442671 [Multi-domain]  Cd Length: 136  Bit Score: 69.51  E-value: 2.49e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1304970003 133 TAGALMTSDYSTLAAHMTVTEALAALRleapdAETIYHTYVIDDERKLSGVVSLRALILAAP------------EQLIND 200
Cdd:COG3448     3 TVRDIMTRDVVTVSPDTTLREALELMR-----EHGIRGLPVVDEDGRLVGIVTERDLLRALLpdrldeleerllDLPVED 77

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 1304970003 201 IMLSTVVSCNVNDDQEDVAKVVARYDLIALPITDDHGALVGIVTHDD 247
Cdd:COG3448    78 VMTRPVVTVTPDTPLEEAAELMLEHGIHRLPVVDDDGRLVGIVTRTD 124
COG2524 COG2524
Predicted transcriptional regulator, contains C-terminal CBS domains [Transcription];
108-250 2.21e-13

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


Pssm-ID: 442013 [Multi-domain]  Cd Length: 206  Bit Score: 68.76  E-value: 2.21e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1304970003 108 RDALLPALAQAQREDIRRLSAYEERTAGALMTSDYSTLAAHMTVTEALAALRleapdAETIYHTYVIDDErKLSGVVSLR 187
Cdd:COG2524    62 LLLIVLQAAAVRVVAEKELGLVLKMKVKDIMTKDVITVSPDTTLEEALELML-----EKGISGLPVVDDG-KLVGIITER 135

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1304970003 188 ALILAAPEQL------INDIMLSTVVSCNVNDDQEDVAKVVARYDLIALPITDDHGALVGIVTHDDAMD 250
Cdd:COG2524   136 DLLKALAEGRdlldapVSDIMTRDVVTVSEDDSLEEALRLMLEHGIGRLPVVDDDGKLVGIITRTDILR 204
CBS_pair_ParBc_assoc cd04610
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with a ...
 138-247 1.46e-12

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: 63.88  E-value: 1.46e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1304970003 138 MTSDYSTLAAHMTVTEALAALRleapdaETIYHTYVIDDERKLSGVVSLRALILAAPEQLINDIMLSTVVSCNVNDDQED 217
Cdd:cd04610     1 MTRDVITVSPDDTVKDVIKLIK------ETGHDGFPVVDDGKVVGYVTAKDLLGKDDDEKVSEIMSRDTVVADPDMDITD 74

                          90       100       110
                  ....*....|....*....|....*....|
gi 1304970003 218 VAKVVARYDLIALPITDDHGALVGIVTHDD 247
Cdd:cd04610    75 AARVIFRSGISKLPVVDDEGNLVGIITNMD 104
COG2905 COG2905
Signal-transduction protein containing cAMP-binding, CBS, and nucleotidyltransferase domains ...
 137-255 2.61e-09

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


Pssm-ID: 442149 [Multi-domain]  Cd Length: 124  Bit Score: 54.84  E-value: 2.61e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1304970003 137 LMTSDYSTLAAHMTVTEALAALRleapdAETIYHTYVIDDERKLSGVVSLRALILAA-------PEQLINDIMLSTVVSC 209
Cdd:COG2905     4 IMSRDVVTVSPDATVREAARLMT-----EKGVGSLVVVDDDGRLVGIITDRDLRRRVlaegldpLDTPVSEVMTRPPITV 78

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 1304970003 210 NVNDDQEDVAKVVARYDLIALPITDDhGALVGIVTHDDAMDVASDE 255
Cdd:COG2905    79 SPDDSLAEALELMEEHRIRHLPVVDD-GKLVGIVSITDLLRALSEE 123
MgtE2 COG1824
Permease, similar to cation transporters [Inorganic ion transport and metabolism];
277-449 2.58e-08

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


Pssm-ID: 441429  Cd Length: 188  Bit Score: 53.72  E-value: 2.58e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1304970003 277 SIKVLYRKRVFWLVFLVFGNLLSGFSIANFEEVIAANLVLVFFLPLLVDSGGNAGSQSATLMVRALATGDVVMR-DWLSL 355
Cdd:COG1824     6 TVRRIVRESLPVLLVLAVGGIIAGLVLEGMEELLLAYPGLLVLVPAFLGTRGNLGGILGARLSTALHLGLLEPRlRPDRR 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1304970003 356 LGREAIVALMLGATMAVAISIIGYV------RGDAIVSLVLALSMMSVVMIG---CVIGMSLPFVLNKIGLDPATASAPL 426
Cdd:COG1824    86 LLNNILATLILALLISPLIGVLAWLvavllgRGSLGLLTLVGIALLAGLLLAlllIVVTYYVAIASYRFGLDPDNVVIPV 165

                         170       180
                  ....*....|....*....|...
gi 1304970003 427 ITSVCDASGVLIYLFIASQFLSI 449
Cdd:COG1824   166 VTTLGDVFGVLFLILVARLVLGL 188
CBS_pair_arch_MET2_assoc cd04605
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with the ...
 137-247 1.81e-07

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: 49.54  E-value: 1.81e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1304970003 137 LMTSDYSTLAAHMTVTEAlAALRLEapdaETIYHTYVIDDERKLSGVVSL----RALilAAPEQLINDIMLSTVVSCNVN 212
Cdd:cd04605     5 IMSKDVATIREDISIEEA-AKIMID----KNVTHLPVVSEDGKLIGIVTSwdisKAV--ALKKDSLEEIMTRNVITARPD 77

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 1304970003 213 DDQEDVAKVVARYDLIALPITDDHGALVGIVTHDD 247
Cdd:cd04605    78 EPIELAARKMEKHNISALPVVDDDRRVIGIITSDD 112
CBS_pair_NTP_transferase_assoc cd04607
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domain associated with the ...
 173-249 2.60e-07

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


Pssm-ID: 341381 [Multi-domain]  Cd Length: 112  Bit Score: 48.98  E-value: 2.60e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1304970003 173 VIDDERKLSGVVS--------LRALILAAPeqlINDIMLSTVVSCNVNDDQEDVAKVVARYDLIALPITDDHGALVGIVT 244
Cdd:cd04607    30 VVDENRKLLGTVTdgdirrglLKGLSLDAP---VEEVMNKNPITASPSTSREELLALMRAKKILQLPIVDEQGRVVGLET 106


                  ....*
gi 1304970003 245 HDDAM 249
Cdd:cd04607   107 LDDLL 111
CBS_pair_AcuB_like cd04584
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with the ...
 137-252 5.63e-07

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: 48.57  E-value: 5.63e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1304970003 137 LMTSDYSTLAAHMTVTEALAALRLEApdaetIYHTYVIDDeRKLSGVVSLRALILAAPEQL----------------IND 200
Cdd:cd04584     5 IMTKNVVTVTPDTSLAEARELMKEHK-----IRHLPVVDD-GKLVGIVTDRDLLRASPSKAtslsiyelnyllskipVKD 78

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1304970003 201 IMLSTVVSCNVNDDQEDVAKVVARYDLIALPITDDhGALVGIVTHDDAMDVA 252
Cdd:cd04584    79 IMTKDVITVSPDDTVEEAALLMLENKIGCLPVVDG-GKLVGIITETDILRAF 129
CBS pfam00571
CBS domain; CBS domains are small intracellular modules that pair together to form a stable ...
 198-254 8.50e-07

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: 45.67  E-value: 8.50e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1304970003 198 INDIMLSTVVSCNVNDDQEDVAKVVARYDLIALPITDDHGALVGIVTHDDAMDVASD 254
Cdd:pfam00571   1 VKDIMTKDVVTVSPDTTLEEALELMREHGISRLPVVDEDGKLVGIVTLKDLLRALLG 57
CBS_pair_bac cd04629
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains present in bacteria; ...
 138-244 1.55e-06

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


Pssm-ID: 341392 [Multi-domain]  Cd Length: 116  Bit Score: 46.66  E-value: 1.55e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1304970003 138 MTSDYSTLAAHMTVTEALAALrLE-----APdaetiyhtyVIDDERKLSGVVS----LRALILAA----PEQLINDIMLS 204
Cdd:cd04629     1 MTRNPVTLTPDTSILEAVELL-LEhkisgAP---------VVDEQGRLVGFLSeqdcLKALLEASyhcePGGTVADYMST 70

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 1304970003 205 TVVSCNVNDDQEDVAKVVARYDLIALPITDDhGALVGIVT 244
Cdd:cd04629    71 EVLTVSPDTSIVDLAQLFLKNKPRRYPVVED-GKLVGQIS 109
CBS_pair_DRTGG_assoc cd04596
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with the ...
 173-249 4.49e-06

Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with the DRTGG domain; This cd contains two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with a DRTGG domain upstream. The function of the DRTGG domain, named after its conserved residues, is unknown. 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: 341371 [Multi-domain]  Cd Length: 108  Bit Score: 45.15  E-value: 4.49e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1304970003 173 VIDDERKLSGVVSLRALILAAPEQLINDIMLSTVVSCNVNDDQEDVAKVVARYDLIALPITDDHGALVGIVTHDDAM 249
Cdd:cd04596    30 VVDEENRVVGIVTAKDVIGKEDDTPIEKVMTKNPITVKPKTSVASAAHMMIWEGIELLPVVDENRKLLGVISRQDVL 106
CBS_pair_HRP1_like cd04622
CBS pair domain found in Hypoxic Response Protein 1 (HRP1) -like proteinds; Mycobacterium ...
 138-247 1.06e-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: 44.33  E-value: 1.06e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1304970003 138 MTSDYSTLAAHMTVTEAlaALRLEAPDAETIyhtyVIDDERKLSGVVSLRALILAA------PEQL-INDIMLSTVVSCN 210
Cdd:cd04622     1 MTRDVVTVSPDTTLREA--ARLMRDLDIGAL----PVCEGDRLVGMVTDRDIVVRAvaegkdPNTTtVREVMTGDVVTCS 74

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 1304970003 211 VNDDQEDVAKVVARYDLIALPITDDHGALVGIVTHDD 247
Cdd:cd04622    75 PDDDVEEAARLMAEHQVRRLPVVDDDGRLVGIVSLGD 111
COG3448 COG3448
CBS-domain-containing membrane protein [Signal transduction mechanisms];
197-262 1.27e-05

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


Pssm-ID: 442671 [Multi-domain]  Cd Length: 136  Bit Score: 44.86  E-value: 1.27e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1304970003 197 LINDIMLSTVVSCNVNDDQEDVAKVVARYDLIALPITDDHGALVGIVTHDDAMDVASDEATDDFHK 262
Cdd:COG3448     3 TVRDIMTRDVVTVSPDTTLREALELMREHGIRGLPVVDEDGRLVGIVTERDLLRALLPDRLDELEE 68
CBS COG0517
CBS domain [Signal transduction mechanisms];
197-258 1.51e-05

CBS domain [Signal transduction mechanisms];


Pssm-ID: 440283 [Multi-domain]  Cd Length: 128  Bit Score: 44.47  E-value: 1.51e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1304970003 197 LINDIMLSTVVSCNVNDDQEDVAKVVARYDLIALPITDDHGALVGIVTHDDAMDVASDEATD 258
Cdd:COG0517     2 KVKDIMTTDVVTVSPDATVREALELMSEKRIGGLPVVDEDGKLVGIVTDRDLRRALAAEGKD 63
CBS_pair_DHH_polyA_Pol_assoc cd04595
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with the ...
 144-249 3.79e-05

Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with the DHH and nucleotidyltransferase (NT) domains; This cd contains two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with an upstream DHH domain which performs a phosphoesterase function and a downstream nucleotidyltransferase (NT) domain of family X DNA polymerases. 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: 341370 [Multi-domain]  Cd Length: 110  Bit Score: 42.87  E-value: 3.79e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1304970003 144 TLAAHMTVTEALAALRLEApdaetiyHT--YVIDDErKLSGVVSLRALILAAPEQL----INDIMLSTVVSCNVNDDQED 217
Cdd:cd04595     6 TVSPDTTIEEARKIMLRYG-------HTglPVVEDG-KLVGIISRRDVDKAKHHGLghapVKGYMSTNVITIDPDTSLEE 77

                          90       100       110
                  ....*....|....*....|....*....|..
gi 1304970003 218 VAKVVARYDLIALPITDDhGALVGIVTHDDAM 249
Cdd:cd04595    78 AQELMVEHDIGRLPVVEE-GKLVGIVTRSDVL 108
CBS_pair_bac_euk cd04623
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains present in bacteria ...
 144-243 5.76e-05

Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains present in bacteria and eukaryotes; 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: 341391 [Multi-domain]  Cd Length: 113  Bit Score: 42.40  E-value: 5.76e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1304970003 144 TLAAHMTVTEALAALRleapdAETIYHTYVIDDERKLSGVVS----LRALIL---AAPEQLINDIMLSTVVSCNVNDDQE 216
Cdd:cd04623     6 TVSPDATVAEALRLLA-----EKNIGALVVVDDGGRLVGILSerdyVRKLALrgaSSLDTPVSEIMTRDVVTCTPDDTVE 80

                          90       100
                  ....*....|....*....|....*..
gi 1304970003 217 DVAKVVARYDLIALPITDDhGALVGIV 243
Cdd:cd04623    81 ECMALMTERRIRHLPVVED-GKLVGIV 106
CBS_pair_peptidase_M50 cd04639
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains found in the ...
 138-247 7.29e-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: 42.17  E-value: 7.29e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1304970003 138 MTSDYSTLAAHMTVTEALAALRLEAPDAETIYhtyVIDDERKLSGVVSLRALILAA----PEQLINDIMLSTVVSCNVND 213
Cdd:cd04639     3 MVTEFPIVDADLTLREFADDYLIGKKSWREFL---VTDEAGRLVGLITVDDLRAIPtsqwPDTPVRELMKPLEEIPTVAA 79

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 1304970003 214 DQ--EDVAKVVARYDLIALPITDDHGALVGIVTHDD 247
Cdd:cd04639    80 DQslLEVVKLLEEQQLPALAVVSENGTLVGLIEKED 115
CBS_pair_ABC_Gly_Pro_assoc cd09831
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains found associated with ...
 172-244 7.41e-05

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: 42.16  E-value: 7.41e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1304970003 172 YVIDDERKLSGVVSLRALILA--APEQLINDIMLSTVVSCNVNDDQEDVAKVVARYDlIALPITDDHGALVGIVT 244
Cdd:cd09831    34 YVVDKKRRFLGVVSVDSLRAAlkENAQSLEDAFLTDVETVPADTSLSDILGLVASAP-CPLPVVDEDGRYLGVIS 107
CBS_pair_arch1_repeat2 cd04632
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains present in archaea, ...
 139-250 9.51e-05

Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains present in archaea, repeat 2; 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: 341395 [Multi-domain]  Cd Length: 127  Bit Score: 41.93  E-value: 9.51e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1304970003 139 TSDYSTLAAHMTVTEALAALRleapdAETIYHTYVIDDERKLSGVVSL----------------------RALILAAPeq 196
Cdd:cd04632     1 TEEVITVNEDDTIGKAINLLR-----EHGISRLPVVDDNGKLVGIVTTydivdfvvrpgtktrggdrggeKERMLDLP-- 73

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1304970003 197 lINDIMLSTVVSCNVNDDQEDVAKVVARYDLIALPITDDHGALVGIVTHDDAMD 250
Cdd:cd04632    74 -VYDIMSSPVVTVTRDATVADAVERMLENDISGLVVTPDDNMVIGILTKTDVLR 126
COG2905 COG2905
Signal-transduction protein containing cAMP-binding, CBS, and nucleotidyltransferase domains ...
 198-247 1.59e-04

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


Pssm-ID: 442149 [Multi-domain]  Cd Length: 124  Bit Score: 41.35  E-value: 1.59e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 1304970003 198 INDIMLSTVVSCNVNDDQEDVAKVVARYDLIALPITDDHGALVGIVTHDD 247
Cdd:COG2905     1 VKDIMSRDVVTVSPDATVREAARLMTEKGVGSLVVVDDDGRLVGIITDRD 50
CBS_pair_bact_arch cd17775
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains present in bacteria ...
 173-247 1.90e-04

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: 341411 [Multi-domain]  Cd Length: 117  Bit Score: 40.99  E-value: 1.90e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1304970003 173 VIDDERKLSGVVSLRALIL------AAPEQL-INDIMLSTVVSCNVNDDQEDVAKVVARYDLIALPITDDHGALVGIVTH 245
Cdd:cd17775    31 VVEEDGKPVGIVTDRDIVVevvakgLDPKDVtVGDIMSADLITAREDDGLFEALERMREKGVRRLPVVDDDGELVGIVTL 110


                  ..
gi 1304970003 246 DD 247
Cdd:cd17775   111 DD 112
IMPDH pfam00478
IMP dehydrogenase / GMP reductase domain; This family is involved in biosynthesis of guanosine ...
 116-247 1.90e-04

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: 43.53  E-value: 1.90e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1304970003 116 AQAQREDIRRLSAYEertagALMTSDYSTLAAHMTVTEALAALRleapdaETIYHTYVIDDERKLSGVVSLRAL-ILAAP 194
Cdd:pfam00478  69 IEEQAEEVRKVKRSE-----SGMITDPVTLSPDATVADALALME------RYGISGVPVVDDGKLVGIVTNRDLrFETDL 137

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1304970003 195 EQLINDIMLST-VVSCNVNDDQEDVAKVVARYDLIALPITDDHGALVGIVTHDD 247
Cdd:pfam00478 138 SQPVSEVMTKEnLVTAPEGTTLEEAKEILHKHKIEKLPVVDDNGRLVGLITIKD 191
CBS_pair_ABC_OpuCA_assoc cd04583
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains found associated with ...
 173-244 2.00e-04

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: 40.58  E-value: 2.00e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1304970003 173 VIDDERKLSGVVSLRAL-ILAAPEQLINDIMLSTVVSCNVNDDQEDVAKVVARYDLIALPITDDHGALVGIVT 244
Cdd:cd04583    30 VVDKDNVLLGIVDIEDInRNYRKAKKVGEIMERDVFTVKEDSLLRDTVDRILKRGLKYVPVVDEQGRLVGLVT 102
COG2524 COG2524
Predicted transcriptional regulator, contains C-terminal CBS domains [Transcription];
143-259 2.18e-04

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


Pssm-ID: 442013 [Multi-domain]  Cd Length: 206  Bit Score: 42.18  E-value: 2.18e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1304970003 143 STLAAHMTVTEALAALRLEAPDAETIYHTYVIDDERKLSGVVSLRALILAAPEQLINDIMLSTVVSCNVNDDQEDVAKVV 222
Cdd:COG2524    33 LTAAAAATVLLLAAAAAAAGAGGLGLLLLLLLIVLQAAAVRVVAEKELGLVLKMKVKDIMTKDVITVSPDTTLEEALELM 112

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 1304970003 223 ARYDLIALPITDDhGALVGIVTHDDAMDVASDEATDD 259
Cdd:COG2524   113 LEKGISGLPVVDD-GKLVGIITERDLLKALAEGRDLL 148
CBS_pair_archHTH_assoc cd04588
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains found in archaea and ...
 173-251 4.22e-04

Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains found in archaea and associated with helix turn helix domain; This cd contains two tandem repeats of the cystathionine beta-synthase (CBS pair) domains in the inosine 5' monophosphate dehydrogenase (IMPDH) protein. IMPDH is an essential enzyme that catalyzes the first step unique to GTP synthesis, playing a key role in the regulation of cell proliferation and differentiation. 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: 341364 [Multi-domain]  Cd Length: 111  Bit Score: 39.82  E-value: 4.22e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1304970003 173 VIDDErKLSGVVSL----RALILAAPEQLINDIMLSTVVSCNVNDDQEDVAKVVARYDLIALPITDDHGALVGIVTHDDA 248
Cdd:cd04588    30 VVDDG-KLVGIVTLtdiaKALAEGKENAKVKDIMTKDVITIDKDEKIYDAIRLMNKHNIGRLIVVDDNGKPVGIITRTDI 108


                  ...
gi 1304970003 249 MDV 251
Cdd:cd04588   109 LKV 111
CBS_pair_BON_assoc cd04586
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with the ...
 138-247 4.60e-04

Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with the BON (bacterial OsmY and nodulation domain) domain; This cd contains two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with the BON (bacterial OsmY and nodulation domain) domain. BON is a putative phospholipid-binding domain found in a family of osmotic shock protection proteins. It is also found in some secretins and a group of potential haemolysins. Its likely function is attachment to phospholipid membranes. 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: 341362 [Multi-domain]  Cd Length: 137  Bit Score: 40.11  E-value: 4.60e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1304970003 138 MTSDYSTLAAHMTVTEAlAALRLE-----APdaetiyhtyVIDDERKLSGVVS------------------LRALILAAP 194
Cdd:cd04586     1 MTTDVVTVTPDTSVREA-ARLLLEhrisgLP---------VVDDDGKLVGIVSegdllrreepgteprrvwWLDALLESP 70

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1304970003 195 EQLIN-----------DIMLSTVVSCNVNDDQEDVAKVVARYDLIALPITDDhGALVGIVTHDD 247
Cdd:cd04586    71 ERLAEeyvkahgrtvgDVMTRPVVTVSPDTPLEEAARLMERHRIKRLPVVDD-GKLVGIVSRAD 133
CBS_pair_HPP_assoc cd04600
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with the ...
 138-247 5.59e-04

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


Pssm-ID: 341375 [Multi-domain]  Cd Length: 133  Bit Score: 39.85  E-value: 5.59e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1304970003 138 MTSDYSTLAAHMTVTEALAALR---LEA-PdaetiyhtyVIDDERKLSGVVSL---------------------RALILA 192
Cdd:cd04600     1 MSRDVVTVTPDTSLEEAWRLLRrhrIKAlP---------VVDRARRLVGIVTLadllkhadldpprglrgrlrrTLGLRR 71

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1304970003 193 APEQLINDIMLSTVVSCNVNDDQEDVAKVVARYDLIALPITDDHGALVGIVTHDD 247
Cdd:cd04600    72 DRPETVGDIMTRPVVTVRPDTPIAELVPLFSDGGLHHIPVVDADGRLVGIVTQSD 126
CBS_arch_repeat1 cd17777
CBS pair domains found in archeal proteins, repeat 1; CBS pair domains found in archeal ...
 173-249 6.27e-04

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


Pssm-ID: 341413 [Multi-domain]  Cd Length: 137  Bit Score: 40.02  E-value: 6.27e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1304970003 173 VIDDERKLSGVVSLRALI---------------------LAAPEQLINDIMLSTVVSCNVNDDQEDVAKVVARYDLIALP 231
Cdd:cd17777    37 VVVDENKLEGILSARDLVsylgggclfkivesrhqgdlySALNREVVETIMTPNPVYVYEDSDLIEALTIMVTRGIGSLP 116

                          90
                  ....*....|....*...
gi 1304970003 232 ITDDHGALVGIVTHDDAM 249
Cdd:cd17777   117 VVDRDGRPVGIVTERDLV 134
CBS smart00116
Domain in cystathionine beta-synthase and other proteins; Domain present in all 3 forms of ...
 206-247 7.74e-04

Domain in cystathionine beta-synthase and other proteins; Domain present in all 3 forms of cellular life. Present in two copies in inosine monophosphate dehydrogenase, of which one is disordered in the crystal structure. A number of disease states are associated with CBS-containing proteins including homocystinuria, Becker's and Thomsen disease.


Pssm-ID: 214522 [Multi-domain]  Cd Length: 49  Bit Score: 37.11  E-value: 7.74e-04
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|..
gi 1304970003  206 VVSCNVNDDQEDVAKVVARYDLIALPITDDHGALVGIVTHDD 247
Cdd:smart00116   2 VVTVSPDTTLEEALELLRENGIRRLPVVDEEGRLVGIVTRRD 43
CBS_pair_bac_arch cd17785
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains present in bacteria ...
 137-241 9.24e-04

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: 9.24e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1304970003 137 LMTSDYSTLAAHMTVTEALAALrLEAPDAETIYhtyVIDDERKLSGVVSLRALI----------------LAAPEQLIN- 199
Cdd:cd17785     7 LITKKPSVVHENTSIRDVIDKM-IEDPKTRSVY---VVDDDEKLLGIITLMELLkyigyrfgvtiykgvsFGLLLRISLk 82

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 1304970003 200 ----DIMLStVVSCNVNDDQEDVAKVVARYDLIALPITDDHGALVG 241
Cdd:cd17785    83 ekakDIMLS-PIYVKKEDTLEEALELMVKNRLQELPVVDENGKVIG 127
CBS_pair_arch cd09836
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains; The CBS domain, ...
 173-253 2.50e-03

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


Pssm-ID: 341405 [Multi-domain]  Cd Length: 116  Bit Score: 37.50  E-value: 2.50e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1304970003 173 VIDDERKLSGVVSLRALILAAPEQLIND-----IMLSTVVSCNVNDDQEDVAKVVARYDLIALPITDDHGALVGIVTHDD 247
Cdd:cd09836    31 VVDDDGKPVGIVTERDIVRAVAEGIDLDtpveeIMTKNLVTVSPDESIYEAAELMREHNIRHLPVVDGGGKLVGVISIRD 110


                  ....*.
gi 1304970003 248 AMDVAS 253
Cdd:cd09836   111 LARELS 116
CBS pfam00571
CBS domain; CBS domains are small intracellular modules that pair together to form a stable ...
 134-195 2.69e-03

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


Pssm-ID: 425756 [Multi-domain]  Cd Length: 57  Bit Score: 36.04  E-value: 2.69e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1304970003 134 AGALMTSDYSTLAAHMTVTEALAALRleapdAETIYHTYVIDDERKLSGVVSLRALILAAPE 195
Cdd:pfam00571   1 VKDIMTKDVVTVSPDTTLEEALELMR-----EHGISRLPVVDEDGKLVGIVTLKDLLRALLG 57
CBS_pair_Thermoplasmatales cd17786
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains present in ...
 140-247 2.72e-03

Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains present in Thermoplasmatales; 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: 341422 [Multi-domain]  Cd Length: 114  Bit Score: 37.51  E-value: 2.72e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1304970003 140 SDYSTLAAHMTVTEALAALrleapDAETIYHTYVIDDERKLSGVVSLRALI-------LAAPEQLINDIMLSTVVSCNVN 212
Cdd:cd17786     2 KNFKTINWNATVFDAVKIM-----NENHLYGLVVKDDDGNYVGLISERSIIkrfiprnVKPDEVPVKLVMRKPIPKVKSD 76

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 1304970003 213 DDQEDVAKVVARYDLIALPITDDHGALVGIVTHDD 247
Cdd:cd17786    77 YDVKDVAAFLSENGLERCAVVDDNGRVVGIVTITD 111
CBS COG0517
CBS domain [Signal transduction mechanisms];
120-197 3.13e-03

CBS domain [Signal transduction mechanisms];


Pssm-ID: 440283 [Multi-domain]  Cd Length: 128  Bit Score: 37.54  E-value: 3.13e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1304970003 120 REDIRRLSA-----YEERTAGALMTSDYSTLAAHMTVTEALAALRleapdAETIYHTYVIDDERKLSGVVSLRALILAAP 194
Cdd:COG0517    50 DRDLRRALAaegkdLLDTPVSEVMTRPPVTVSPDTSLEEAAELME-----EHKIRRLPVVDDDGRLVGIITIKDLLKALL 124


                  ...
gi 1304970003 195 EQL 197
Cdd:COG0517   125 EPL 127
PRK07807 PRK07807
GuaB1 family IMP dehydrogenase-related protein;
144-248 3.38e-03

GuaB1 family IMP dehydrogenase-related protein;


Pssm-ID: 181127 [Multi-domain]  Cd Length: 479  Bit Score: 39.50  E-value: 3.38e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1304970003 144 TLAAHMTVTEALAALRLEAPDAetiyhTYVIDDERKLSGVVSLRALILAAPEQLINDIMLSTVVSCNVNDDQEDVAKVVA 223
Cdd:PRK07807  101 TLSPDDTVGDALALLPKRAHGA-----VVVVDEEGRPVGVVTEADCAGVDRFTQVRDVMSTDLVTLPAGTDPREAFDLLE 175

                          90       100
                  ....*....|....*....|....*
gi 1304970003 224 RYDLIALPITDDHGALVGIVTHDDA 248
Cdd:PRK07807  176 AARVKLAPVVDADGRLVGVLTRTGA 200
CBS_pair_IMPDH cd04601
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains in the inosine 5' ...
 216-257 4.52e-03

Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains in the inosine 5' monophosphate dehydrogenase (IMPDH) protein; This cd contains two tandem repeats of the cystathionine beta-synthase (CBS pair) domains in the inosine 5' monophosphate dehydrogenase (IMPDH) protein. IMPDH is an essential enzyme that catalyzes the first step unique to GTP synthesis, playing a key role in the regulation of cell proliferation and differentiation. 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: 341376 [Multi-domain]  Cd Length: 110  Bit Score: 36.62  E-value: 4.52e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 1304970003 216 EDVAKVVARYDLIALPITDDHGALVGIVTHDDaMDVASDEAT 257
Cdd:cd04601    14 ADVLELKAEYGISGVPVTEDGGKLVGIVTSRD-IRFETDLST 54
CBS_pair_bac cd04643
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains present in bacteria; ...
 173-244 4.89e-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: 341400 [Multi-domain]  Cd Length: 130  Bit Score: 37.09  E-value: 4.89e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1304970003 173 VIDDERKLSGVVSLrALILAA--------PEQL----INDIMLSTVVSCNVNDDQEDV-AKVVaryDLIALPITDDHGAL 239
Cdd:cd04643    35 VLDKDYKLVGLISL-SMILDAilglerieFEKLselkVEEVMNTDVPTVSPDDDLEEVlHLLV---DHPFLCVVDEDGYF 110


                  ....*
gi 1304970003 240 VGIVT 244
Cdd:cd04643   111 LGIIT 115
CBS_pair_peptidase_M50 cd04801
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains found in the ...
 137-249 5.16e-03

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: 341401 [Multi-domain]  Cd Length: 113  Bit Score: 36.78  E-value: 5.16e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1304970003 137 LMTSDYSTLAAHMTVTEALAALRLEApdaetiyHT-Y-VIDDERkLSGVVSLRALILAAPEQ----LINDIMLSTVVSCN 210
Cdd:cd04801     2 IMTPEVVTVTPEMTVSELLDRMFEEK-------HLgYpVVENGR-LVGIVTLEDIRKVPEVEreatRVRDVMTKDVITVS 73

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 1304970003 211 VNDDQEDVAKVVARYDLIALPITDDhGALVGIVTHDDAM 249
Cdd:cd04801    74 PDADAMEALKLMSQNNIGRLPVVED-GELVGIISRTDLM 111
CBS_pair_IMPDH cd04601
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains in the inosine 5' ...
 173-244 7.40e-03

Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains in the inosine 5' monophosphate dehydrogenase (IMPDH) protein; This cd contains two tandem repeats of the cystathionine beta-synthase (CBS pair) domains in the inosine 5' monophosphate dehydrogenase (IMPDH) protein. IMPDH is an essential enzyme that catalyzes the first step unique to GTP synthesis, playing a key role in the regulation of cell proliferation and differentiation. 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: 341376 [Multi-domain]  Cd Length: 110  Bit Score: 36.24  E-value: 7.40e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1304970003 173 VIDDERKLSGVVSLRAL-ILAAPEQLINDIM--LSTVVSCNVNDDQEDVAKVVARYDLIALPITDDHGALVGIVT 244
Cdd:cd04601    30 VTEDGGKLVGIVTSRDIrFETDLSTPVSEVMtpDERLVTAPEGITLEEAKEILHKHKIEKLPIVDDNGELVGLIT 104
CBS_pair_SF cd02205
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains superfamily; The CBS ...
 206-268 8.25e-03

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


Pssm-ID: 341358 [Multi-domain]  Cd Length: 113  Bit Score: 36.07  E-value: 8.25e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1304970003 206 VVSCNVNDDQEDVAKVVARYDLIALPITDDHGALVGIVTHDDAMDVASDEATDDFHKSGGVTT 268
Cdd:cd02205     4 VVTVDPDTTVREALELMAENGIGALPVVDDDGKLVGIVTERDILRALVEGGLALDTPVAEVMT 66
DOPA_deC_like cd06450
DOPA decarboxylase family. This family belongs to pyridoxal phosphate (PLP)-dependent ...
 108-295 9.02e-03

DOPA decarboxylase family. This family belongs to pyridoxal phosphate (PLP)-dependent aspartate aminotransferase superfamily (fold I). The major groups in this CD correspond to DOPA/tyrosine decarboxylase (DDC), histidine decarboxylase (HDC), and glutamate decarboxylase (GDC). DDC is active as a dimer and catalyzes the decarboxylation of tyrosine. GDC catalyzes the decarboxylation of glutamate and HDC catalyzes the decarboxylation of histidine.


Pssm-ID: 99743 [Multi-domain]  Cd Length: 345  Bit Score: 37.95  E-value: 9.02e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1304970003 108 RDALLPALAQAQREDIRRLSAYeertagalmTSDystlAAHMTVTEALAALRLEAPDAETiyhtyviDDERKLSgVVSLR 187
Cdd:cd06450    78 RDRARKRLKAGGGRGIDKLVIV---------CSD----QAHVSVEKAAAYLDVKVRLVPV-------DEDGRMD-PEALE 136

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1304970003 188 ALILAAPEQLINDIMLS----TVVSCNVnDDQEDVAKVVARYDLialPItddH------GALVGIVTHDDAMD----VAS 253
Cdd:cd06450   137 AAIDEDKAEGLNPIMVVatagTTDTGAI-DPLEEIADLAEKYDL---WL---HvdaaygGFLLPFPEPRHLDFgierVDS 209

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 1304970003 254 deATDDFHKSGGVTtmvgrlKDVSIkVLYRKRVFWLVFLVFG 295
Cdd:cd06450   210 --ISVDPHKYGLVP------LGCSA-VLVRALKLWATLRRFG 242
CBS_pair_arch_MET2_assoc cd04605
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with the ...
 197-244 9.09e-03

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


Pssm-ID: 341379 [Multi-domain]  Cd Length: 116  Bit Score: 36.06  E-value: 9.09e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 1304970003 197 LINDIMLSTVVSCNVNDDQEDVAKVVARYDLIALPITDDHGALVGIVT 244
Cdd:cd04605     1 LVEDIMSKDVATIREDISIEEAAKIMIDKNVTHLPVVSEDGKLIGIVT 48
CBS_pair_voltage-gated_CLC_bac cd04613
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with the ...
 165-247 9.26e-03

Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with the voltage gated CLC (chloride channel) in bacteria; 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 bacteria. 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: 341385 [Multi-domain]  Cd Length: 119  Bit Score: 36.01  E-value: 9.26e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1304970003 165 AETIYHTY-VIDDERKLSGVVSLRALILAAPEQ------LINDIMLSTVVSCNVNDDQEDVAKVVARYDLIALPITD--D 235
Cdd:cd04613    22 AGTRQHYFpVVDEQGRLTGILSIQDVRGVLFEEelwdlvVVKDLATTDVITVTPDDDLYTALLKFTSTNLDQLPVVDddD 101

                          90
                  ....*....|..
gi 1304970003 236 HGALVGIVTHDD 247
Cdd:cd04613   102 PGKVLGMLSRRD 113
CBS_archAMPK_gamma-repeat1 cd17779
signal transduction protein with CBS domains; Archeal gamma-subunit of 5'-AMP-activated ...
 191-249 9.77e-03

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


Pssm-ID: 341415 [Multi-domain]  Cd Length: 136  Bit Score: 36.44  E-value: 9.77e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1304970003 191 LAAPEQLINDIMLSTVVSCNVNDDQEDVAKVVARYDLIALPITDDHGALVGIVTHDDAM 249
Cdd:cd17779    75 LAAINEPVREIMTRDVISVKENASIDDAIELMLEKNVGGLPIVDKDGKVIGIVTERDFL 133
 
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH