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Conserved domains on  [gi|974335151|gb|KUO93992|]
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MAG: sodium:proton antiporter [Caldivirga sp. JCHS_4]

Protein Classification

KefB and CBS_pair_SF domain-containing protein( domain architecture ID 10001519)

KefB and CBS_pair_SF domain-containing protein

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
KefB COG0475
Kef-type K+ transport system, membrane component KefB [Inorganic ion transport and metabolism]; ...
 4-367 9.39e-29

Kef-type K+ transport system, membrane component KefB [Inorganic ion transport and metabolism];


:

Pssm-ID: 440243 [Multi-domain]  Cd Length: 384  Bit Score: 117.17  E-value: 9.39e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 974335151   4 VTLTLLYLGVMLILAKLLEELFSRIRLVPFVGAVVAGVVLGNGVLGFVKVNSIIQFISLLGITLLLFLSGAeEFEVGR-G 82
Cdd:COG0475    2 LASLLLQLGLLLLAAVLAGLLARRLGLPSVLGYILAGILLGPSGLGLIEDSEALELLAELGVVLLLFLIGL-ELDLKRlR 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 974335151  83 SLNARVTAAAAVELALPFTLIYLSLRALNVSITP--LLAIPLIMTSVGPLARLLMDINLSRTELGNMLFRQGALVEVASV 160
Cdd:COG0475   81 KMGRRALGIGLLQVLLPFLLGFLLALLLGLSLAAalFLGAALAATSTAIVLKVLKELGLLKTPLGQLILGVALFDDIAAI 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 974335151 161 VAFAILVTVRLGGS-----LLTLIGIAVLIAAIFTVGRWVSRALEWVEGYVKAREAEFAAAIFLVLVISFLPEAVNFNPA 235
Cdd:COG0475  161 LLLALVPALAGGGSvagslLLALLKALLFLALLLLVGRYLLRRLFRLVARTRSRELFLLFALLLVLLAAALAELLGLSAA 240

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 974335151 236 MAALFLGILLRDyLKDRPELLEKLHGFTYgFFEPLFFVSIGLYF-VRLSPDLLMTSLLIALILLSSKVAAGALASMVVGG 314
Cdd:COG0475  241 LGAFLAGLVLAE-SEYRHELEEKIEPFGD-LFLPLFFVSVGLSLdLSALLSNPLLALLLVLAAIVGKLLGAYLAARLFGL 318

                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 974335151 315 SP---IINGLGTSTKGGVDVSLLLALLTTGLITRLTYSYLTLAITVNSVVTPLLVR 367
Cdd:COG0475  319 SRreaLRIGLLLAPRGEFALVLASLGLSAGLISPELFAALVLVVLLTTLLTPLLLR 374
CBS_pair_SF super family cl15354
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains superfamily; The CBS ...
 397-504 1.95e-27

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).


The actual alignment was detected with superfamily member cd04603:

Pssm-ID: 449531 [Multi-domain]  Cd Length: 112  Bit Score: 106.00  E-value: 1.95e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 974335151 397 PLTVTCSDNLRIVIDRMVERGVRAVVVVNSEGKPLGYLTMQQLLEIDPATYGMTPACDLPLNELTTVTTKARIIDVLRRI 476
Cdd:cd04603    4 LVFVNKNEPLREIIKKITELNARAIVIVNNNMSVLGQITVSDLLEIGPSQYETLTAYDLILVPLIRVNCDAPITDLLRKF 83

                         90       100
                 ....*....|....*....|....*...
gi 974335151 477 RGFEDPVIGVVNDDGVLVATIYERELLR 504
Cdd:cd04603   84 RETDPPIIAVIDDESKFIGTIYERELLK 111
 
Name Accession Description Interval E-value
KefB COG0475
Kef-type K+ transport system, membrane component KefB [Inorganic ion transport and metabolism]; ...
 4-367 9.39e-29

Kef-type K+ transport system, membrane component KefB [Inorganic ion transport and metabolism];


Pssm-ID: 440243 [Multi-domain]  Cd Length: 384  Bit Score: 117.17  E-value: 9.39e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 974335151   4 VTLTLLYLGVMLILAKLLEELFSRIRLVPFVGAVVAGVVLGNGVLGFVKVNSIIQFISLLGITLLLFLSGAeEFEVGR-G 82
Cdd:COG0475    2 LASLLLQLGLLLLAAVLAGLLARRLGLPSVLGYILAGILLGPSGLGLIEDSEALELLAELGVVLLLFLIGL-ELDLKRlR 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 974335151  83 SLNARVTAAAAVELALPFTLIYLSLRALNVSITP--LLAIPLIMTSVGPLARLLMDINLSRTELGNMLFRQGALVEVASV 160
Cdd:COG0475   81 KMGRRALGIGLLQVLLPFLLGFLLALLLGLSLAAalFLGAALAATSTAIVLKVLKELGLLKTPLGQLILGVALFDDIAAI 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 974335151 161 VAFAILVTVRLGGS-----LLTLIGIAVLIAAIFTVGRWVSRALEWVEGYVKAREAEFAAAIFLVLVISFLPEAVNFNPA 235
Cdd:COG0475  161 LLLALVPALAGGGSvagslLLALLKALLFLALLLLVGRYLLRRLFRLVARTRSRELFLLFALLLVLLAAALAELLGLSAA 240

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 974335151 236 MAALFLGILLRDyLKDRPELLEKLHGFTYgFFEPLFFVSIGLYF-VRLSPDLLMTSLLIALILLSSKVAAGALASMVVGG 314
Cdd:COG0475  241 LGAFLAGLVLAE-SEYRHELEEKIEPFGD-LFLPLFFVSVGLSLdLSALLSNPLLALLLVLAAIVGKLLGAYLAARLFGL 318

                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 974335151 315 SP---IINGLGTSTKGGVDVSLLLALLTTGLITRLTYSYLTLAITVNSVVTPLLVR 367
Cdd:COG0475  319 SRreaLRIGLLLAPRGEFALVLASLGLSAGLISPELFAALVLVVLLTTLLTPLLLR 374
CBS_pair_KefB_assoc cd04603
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with the ...
 397-504 1.95e-27

Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with the KefB (Kef-type K+ transport systems) domain; This cd contains two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with the KefB (Kef-type K+ transport systems) domain which is involved in inorganic ion transport and metabolism. 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: 341377 [Multi-domain]  Cd Length: 112  Bit Score: 106.00  E-value: 1.95e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 974335151 397 PLTVTCSDNLRIVIDRMVERGVRAVVVVNSEGKPLGYLTMQQLLEIDPATYGMTPACDLPLNELTTVTTKARIIDVLRRI 476
Cdd:cd04603    4 LVFVNKNEPLREIIKKITELNARAIVIVNNNMSVLGQITVSDLLEIGPSQYETLTAYDLILVPLIRVNCDAPITDLLRKF 83

                         90       100
                 ....*....|....*....|....*...
gi 974335151 477 RGFEDPVIGVVNDDGVLVATIYERELLR 504
Cdd:cd04603   84 RETDPPIIAVIDDESKFIGTIYERELLK 111
Na_H_Exchanger pfam00999
Sodium/hydrogen exchanger family; Na/H antiporters are key transporters in maintaining the pH ...
 11-277 7.68e-13

Sodium/hydrogen exchanger family; Na/H antiporters are key transporters in maintaining the pH of actively metabolising cells. The molecular mechanisms of antiport are unclear. These antiporters contain 10-12 transmembrane regions (M) at the amino-terminus and a large cytoplasmic region at the carboxyl terminus. The transmembrane regions M3-M12 share identity with other members of the family. The M6 and M7 regions are highly conserved. Thus, this is thought to be the region that is involved in the transport of sodium and hydrogen ions. The cytoplasmic region has little similarity throughout the family.


Pssm-ID: 425982 [Multi-domain]  Cd Length: 377  Bit Score: 69.98  E-value: 7.68e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 974335151   11 LGVMLILAKLLEELFSRIRLVPFVGAVVAGVVLGNGVLGFVK-VNSIIQFISLLGITLLLFLSGAE----EFEVGRGSLN 85
Cdd:pfam00999   1 IVLLILLALLAPLLARRLKLPPIVGLIIAGILLGPSGLGLISeVDEDLEVLSNLGLPPLLFLAGLEldlrELRKNGGSIL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 974335151   86 ARVTAAAAVELALPFTLIYLSLRALNVSITPLLAIPLIMTSVGPLARLLMDINLSRTELGNMLFRQGALVEVASVVAFAI 165
Cdd:pfam00999  81 LLALLGVLIPFVLIGLLLYLLGLGIPLLEALLFGAILSATSPVVVLAILKELGRVPERLGTLLLGESVLNDGVAVVLLAV 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 974335151  166 LVTVRLGGSLLTLIGIAVLIAAIFTVGRWVSRALEWVEGYVKAR------EAEFAAAIFLVLVISFLPEAVNFNPAMAAL 239
Cdd:pfam00999 161 LLALAQGVGGGSDLGWLLLIFLVVAVGGLLLGLLIGWLLRLITRftdddrELEVLLVLLLALLAALLAEALGVSGILGAF 240

                         250       260       270
                  ....*....|....*....|....*....|....*...
gi 974335151  240 FLGILLRDYLKdRPELLEKLHGFTYGFFEPLFFVSIGL 277
Cdd:pfam00999 241 LAGLVLSEYPF-ANKLSEKLEPFGYGLFNPLFFVLVGL 277
COG3448 COG3448
CBS-domain-containing membrane protein [Signal transduction mechanisms];
389-507 3.82e-10

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


Pssm-ID: 442671 [Multi-domain]  Cd Length: 136  Bit Score: 57.95  E-value: 3.82e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 974335151 389 MSISEY--AKPLTVTCSDNLRIVIDRMVERGVRAVVVVNSEGKPLGYLTMQQLLEIDPATY--------GMTPACDLPLN 458
Cdd:COG3448    2 MTVRDImtRDVVTVSPDTTLREALELMREHGIRGLPVVDEDGRLVGIVTERDLLRALLPDRldeleerlLDLPVEDVMTR 81

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*....
gi 974335151 459 ELTTVTTKARIIDVLRRIRGFEDPVIGVVNDDGVLVATIYERELLRLLI 507
Cdd:COG3448   82 PVVTVTPDTPLEEAAELMLEHGIHRLPVVDDDGRLVGIVTRTDLLRALA 130
CBS pfam00571
CBS domain; CBS domains are small intracellular modules that pair together to form a stable ...
 396-441 6.84e-05

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


Pssm-ID: 425756 [Multi-domain]  Cd Length: 57  Bit Score: 40.66  E-value: 6.84e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*.
gi 974335151  396 KPLTVTCSDNLRIVIDRMVERGVRAVVVVNSEGKPLGYLTMQQLLE 441
Cdd:pfam00571   8 DVVTVSPDTTLEEALELMREHGISRLPVVDEDGKLVGIVTLKDLLR 53
PRK07807 PRK07807
GuaB1 family IMP dehydrogenase-related protein;
397-507 1.33e-04

GuaB1 family IMP dehydrogenase-related protein;


Pssm-ID: 181127 [Multi-domain]  Cd Length: 479  Bit Score: 44.51  E-value: 1.33e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 974335151 397 PLTVTCSDNLRIVIDRMVERGVRAVVVVNSEGKPLGYLTMQQLLEIDPatygMTPACDLPLNELTTVTTKARIIDVLRRI 476
Cdd:PRK07807  99 PVTLSPDDTVGDALALLPKRAHGAVVVVDEEGRPVGVVTEADCAGVDR----FTQVRDVMSTDLVTLPAGTDPREAFDLL 174

                         90       100       110
                 ....*....|....*....|....*....|.
gi 974335151 477 RGFEDPVIGVVNDDGVLVATIYERELLRLLI 507
Cdd:PRK07807 175 EAARVKLAPVVDADGRLVGVLTRTGALRATI 205
CBS smart00116
Domain in cystathionine beta-synthase and other proteins; Domain present in all 3 forms of ...
 397-440 4.58e-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: 37.88  E-value: 4.58e-04
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....
gi 974335151   397 PLTVTCSDNLRIVIDRMVERGVRAVVVVNSEGKPLGYLTMQQLL 440
Cdd:smart00116   2 VVTVSPDTTLEEALELLRENGIRRLPVVDEEGRLVGIVTRRDII 45
PRK03562 PRK03562
glutathione-regulated potassium-efflux system protein KefC; Provisional
 171-277 2.13e-03

glutathione-regulated potassium-efflux system protein KefC; Provisional


Pssm-ID: 235131 [Multi-domain]  Cd Length: 621  Bit Score: 40.75  E-value: 2.13e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 974335151 171 LGGSLLTLIGIAVLIAAIFTVGRWVSR-ALEWVeGYVKAREAEFAAAIFLVLVISFLPEAVNFNPAMAALFLGILLRD-- 247
Cdd:PRK03562 179 LGAFALSALKVAGALALVVLGGRYVTRpALRFV-ARSGLREVFTAVALFLVFGFGLLMEEVGLSMALGAFLAGVLLASse 257

                         90       100       110
                 ....*....|....*....|....*....|...
gi 974335151 248 YlkdRPEL---LEKLHGFTYGffepLFFVSIGL 277
Cdd:PRK03562 258 Y---RHALesdIEPFKGLLLG----LFFIAVGM 283
 
Name Accession Description Interval E-value
KefB COG0475
Kef-type K+ transport system, membrane component KefB [Inorganic ion transport and metabolism]; ...
 4-367 9.39e-29

Kef-type K+ transport system, membrane component KefB [Inorganic ion transport and metabolism];


Pssm-ID: 440243 [Multi-domain]  Cd Length: 384  Bit Score: 117.17  E-value: 9.39e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 974335151   4 VTLTLLYLGVMLILAKLLEELFSRIRLVPFVGAVVAGVVLGNGVLGFVKVNSIIQFISLLGITLLLFLSGAeEFEVGR-G 82
Cdd:COG0475    2 LASLLLQLGLLLLAAVLAGLLARRLGLPSVLGYILAGILLGPSGLGLIEDSEALELLAELGVVLLLFLIGL-ELDLKRlR 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 974335151  83 SLNARVTAAAAVELALPFTLIYLSLRALNVSITP--LLAIPLIMTSVGPLARLLMDINLSRTELGNMLFRQGALVEVASV 160
Cdd:COG0475   81 KMGRRALGIGLLQVLLPFLLGFLLALLLGLSLAAalFLGAALAATSTAIVLKVLKELGLLKTPLGQLILGVALFDDIAAI 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 974335151 161 VAFAILVTVRLGGS-----LLTLIGIAVLIAAIFTVGRWVSRALEWVEGYVKAREAEFAAAIFLVLVISFLPEAVNFNPA 235
Cdd:COG0475  161 LLLALVPALAGGGSvagslLLALLKALLFLALLLLVGRYLLRRLFRLVARTRSRELFLLFALLLVLLAAALAELLGLSAA 240

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 974335151 236 MAALFLGILLRDyLKDRPELLEKLHGFTYgFFEPLFFVSIGLYF-VRLSPDLLMTSLLIALILLSSKVAAGALASMVVGG 314
Cdd:COG0475  241 LGAFLAGLVLAE-SEYRHELEEKIEPFGD-LFLPLFFVSVGLSLdLSALLSNPLLALLLVLAAIVGKLLGAYLAARLFGL 318

                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 974335151 315 SP---IINGLGTSTKGGVDVSLLLALLTTGLITRLTYSYLTLAITVNSVVTPLLVR 367
Cdd:COG0475  319 SRreaLRIGLLLAPRGEFALVLASLGLSAGLISPELFAALVLVVLLTTLLTPLLLR 374
CBS_pair_KefB_assoc cd04603
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with the ...
 397-504 1.95e-27

Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with the KefB (Kef-type K+ transport systems) domain; This cd contains two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with the KefB (Kef-type K+ transport systems) domain which is involved in inorganic ion transport and metabolism. 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: 341377 [Multi-domain]  Cd Length: 112  Bit Score: 106.00  E-value: 1.95e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 974335151 397 PLTVTCSDNLRIVIDRMVERGVRAVVVVNSEGKPLGYLTMQQLLEIDPATYGMTPACDLPLNELTTVTTKARIIDVLRRI 476
Cdd:cd04603    4 LVFVNKNEPLREIIKKITELNARAIVIVNNNMSVLGQITVSDLLEIGPSQYETLTAYDLILVPLIRVNCDAPITDLLRKF 83

                         90       100
                 ....*....|....*....|....*...
gi 974335151 477 RGFEDPVIGVVNDDGVLVATIYERELLR 504
Cdd:cd04603   84 RETDPPIIAVIDDESKFIGTIYERELLK 111
Na_H_Exchanger pfam00999
Sodium/hydrogen exchanger family; Na/H antiporters are key transporters in maintaining the pH ...
 11-277 7.68e-13

Sodium/hydrogen exchanger family; Na/H antiporters are key transporters in maintaining the pH of actively metabolising cells. The molecular mechanisms of antiport are unclear. These antiporters contain 10-12 transmembrane regions (M) at the amino-terminus and a large cytoplasmic region at the carboxyl terminus. The transmembrane regions M3-M12 share identity with other members of the family. The M6 and M7 regions are highly conserved. Thus, this is thought to be the region that is involved in the transport of sodium and hydrogen ions. The cytoplasmic region has little similarity throughout the family.


Pssm-ID: 425982 [Multi-domain]  Cd Length: 377  Bit Score: 69.98  E-value: 7.68e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 974335151   11 LGVMLILAKLLEELFSRIRLVPFVGAVVAGVVLGNGVLGFVK-VNSIIQFISLLGITLLLFLSGAE----EFEVGRGSLN 85
Cdd:pfam00999   1 IVLLILLALLAPLLARRLKLPPIVGLIIAGILLGPSGLGLISeVDEDLEVLSNLGLPPLLFLAGLEldlrELRKNGGSIL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 974335151   86 ARVTAAAAVELALPFTLIYLSLRALNVSITPLLAIPLIMTSVGPLARLLMDINLSRTELGNMLFRQGALVEVASVVAFAI 165
Cdd:pfam00999  81 LLALLGVLIPFVLIGLLLYLLGLGIPLLEALLFGAILSATSPVVVLAILKELGRVPERLGTLLLGESVLNDGVAVVLLAV 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 974335151  166 LVTVRLGGSLLTLIGIAVLIAAIFTVGRWVSRALEWVEGYVKAR------EAEFAAAIFLVLVISFLPEAVNFNPAMAAL 239
Cdd:pfam00999 161 LLALAQGVGGGSDLGWLLLIFLVVAVGGLLLGLLIGWLLRLITRftdddrELEVLLVLLLALLAALLAEALGVSGILGAF 240

                         250       260       270
                  ....*....|....*....|....*....|....*...
gi 974335151  240 FLGILLRDYLKdRPELLEKLHGFTYGFFEPLFFVSIGL 277
Cdd:pfam00999 241 LAGLVLSEYPF-ANKLSEKLEPFGYGLFNPLFFVLVGL 277
COG3448 COG3448
CBS-domain-containing membrane protein [Signal transduction mechanisms];
389-507 3.82e-10

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


Pssm-ID: 442671 [Multi-domain]  Cd Length: 136  Bit Score: 57.95  E-value: 3.82e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 974335151 389 MSISEY--AKPLTVTCSDNLRIVIDRMVERGVRAVVVVNSEGKPLGYLTMQQLLEIDPATY--------GMTPACDLPLN 458
Cdd:COG3448    2 MTVRDImtRDVVTVSPDTTLREALELMREHGIRGLPVVDEDGRLVGIVTERDLLRALLPDRldeleerlLDLPVEDVMTR 81

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*....
gi 974335151 459 ELTTVTTKARIIDVLRRIRGFEDPVIGVVNDDGVLVATIYERELLRLLI 507
Cdd:COG3448   82 PVVTVTPDTPLEEAAELMLEHGIHRLPVVDDDGRLVGIVTRTDLLRALA 130
CBS_pair_SF cd02205
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains superfamily; The CBS ...
 396-504 4.18e-10

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


Pssm-ID: 341358 [Multi-domain]  Cd Length: 113  Bit Score: 57.25  E-value: 4.18e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 974335151 396 KPLTVTCSDNLRIVIDRMVERGVRAVVVVNSEGKPLGYLTMQQLLE--IDPATYGMTPACDLPLNELTTVTTKARIIDVL 473
Cdd:cd02205    3 DVVTVDPDTTVREALELMAENGIGALPVVDDDGKLVGIVTERDILRalVEGGLALDTPVAEVMTPDVITVSPDTDLEEAL 82

                         90       100       110
                 ....*....|....*....|....*....|.
gi 974335151 474 RRIRGFEDPVIGVVNDDGVLVATIYERELLR 504
Cdd:cd02205   83 ELMLEHGIRRLPVVDDDGKLVGIVTRRDILR 113
COG2524 COG2524
Predicted transcriptional regulator, contains C-terminal CBS domains [Transcription];
389-506 6.96e-09

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


Pssm-ID: 442013 [Multi-domain]  Cd Length: 206  Bit Score: 56.05  E-value: 6.96e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 974335151 389 MSISEY--AKPLTVTCSDNLRIVIDRMVERGVRAVVVVNsEGKPLGYLTMQQLLEIDPATYGM--TPACDLPLNELTTVT 464
Cdd:COG2524   86 MKVKDImtKDVITVSPDTTLEEALELMLEKGISGLPVVD-DGKLVGIITERDLLKALAEGRDLldAPVSDIMTRDVVTVS 164

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 974335151 465 TKARIIDVLRRIRGFEDPVIGVVNDDGVLVATIYERELLRLL 506
Cdd:COG2524  165 EDDSLEEALRLMLEHGIGRLPVVDDDGKLVGIITRTDILRAL 206
CBS COG0517
CBS domain [Signal transduction mechanisms];
389-507 9.41e-08

CBS domain [Signal transduction mechanisms];


Pssm-ID: 440283 [Multi-domain]  Cd Length: 128  Bit Score: 50.63  E-value: 9.41e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 974335151 389 MSISEY--AKPLTVTCSDNLRIVIDRMVERGVRAVVVVNSEGKPLGYLT---MQQLLEIDPATYGMTPACDLPLNELTTV 463
Cdd:COG0517    1 MKVKDImtTDVVTVSPDATVREALELMSEKRIGGLPVVDEDGKLVGIVTdrdLRRALAAEGKDLLDTPVSEVMTRPPVTV 80

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 974335151 464 TTKARIIDVLRRIRGFEDPVIGVVNDDGVLVATIYERELLRLLI 507
Cdd:COG0517   81 SPDTSLEEAAELMEEHKIRRLPVVDDDGRLVGIITIKDLLKALL 124
YtoI COG4109
Predicted transcriptional regulator containing CBS domains [Transcription];
396-504 9.59e-08

Predicted transcriptional regulator containing CBS domains [Transcription];


Pssm-ID: 443285 [Multi-domain]  Cd Length: 135  Bit Score: 51.07  E-value: 9.59e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 974335151 396 KPLTVTCSDNLRIVIDRMVERGVRAVVVVNSEGKPLGYLTMQQLLEIDPATygmtPACDLPLNELTTVTTKARIIDVLRR 475
Cdd:COG4109   26 DVATLSEDDTVEDALELLEKTGHSRFPVVDENGRLVGIVTSKDILGKDDDT----PIEDVMTKNPITVTPDTSLASAAHK 101

                         90       100       110
                 ....*....|....*....|....*....|.
gi 974335151 476 I--RGFEdpVIGVVNDDGVLVATIYERELLR 504
Cdd:COG4109  102 MiwEGIE--LLPVVDDDGRLLGIISRQDVLK 130
CBS_pair_ABC_OpuCA_assoc cd04583
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains found associated with ...
 396-494 7.91e-06

Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains found associated with the ABC transporter OpuCA; This cd contains two tandem repeats of the cystathionine beta-synthase (CBS pair) domains found in association with the ABC transporter OpuCA. OpuCA is the ATP binding component of a bacterial solute transporter that serves a protective role to cells growing in a hyperosmolar environment but the function of the CBS domains in OpuCA remains unknown. In the related ABC transporter, OpuA, the tandem CBS domains have been shown to function as sensors for ionic strength, whereby they control the transport activity through an electronic switching mechanism. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. They are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins. The CBS domain, named after human CBS, is a small domain originally identified in cystathionine beta-synthase and is subsequently found in a wide range of different proteins. CBS domains usually occur in tandem repeats. They associate to form a so-called Bateman domain or a CBS pair based on crystallographic studies in bacteria. The CBS pair was used as a basis for this cd hierarchy since the human CBS proteins can adopt the typical core structure and form an intramolecular CBS pair. The interface between the two CBS domains forms a cleft that is a potential ligand binding site. The CBS pair coexists with a variety of other functional domains and this has been used to help in its classification here. It has been proposed that the CBS domain may play a regulatory role, although its exact function is unknown. Mutations of conserved residues within this domain are associated with a variety of human hereditary diseases, including congenital myotonia, idiopathic generalized epilepsy, hypercalciuric nephrolithiasis, and classic Bartter syndrome (CLC chloride channel family members), Wolff-Parkinson-White syndrome (gamma 2 subunit of AMP-activated protein kinase), retinitis pigmentosa (IMP dehydrogenase-1), and homocystinuria (cystathionine beta-synthase).


Pssm-ID: 341360 [Multi-domain]  Cd Length: 110  Bit Score: 44.82  E-value: 7.91e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 974335151 396 KPLTVTCSDNLRIVIDRMVERGVRAVVVVNSEGKPLGYLTMQqllEIDPATYGMTPACDLPLNELTTVTTKARIIDVLRR 475
Cdd:cd04583    3 NPVTITPERTLAQAIEIMREKRVDSLLVVDKDNVLLGIVDIE---DINRNYRKAKKVGEIMERDVFTVKEDSLLRDTVDR 79

                         90       100
                 ....*....|....*....|.
gi 974335151 476 I--RGFEdpVIGVVNDDGVLV 494
Cdd:cd04583   80 IlkRGLK--YVPVVDEQGRLV 98
COG2905 COG2905
Signal-transduction protein containing cAMP-binding, CBS, and nucleotidyltransferase domains ...
 396-508 1.43e-05

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


Pssm-ID: 442149 [Multi-domain]  Cd Length: 124  Bit Score: 44.43  E-value: 1.43e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 974335151 396 KPLTVTCSDNLRIVIDRMVERGVRAVVVVNSEGKPLGYLTMQQLL------EIDPATygmTPACDLPLNELTTVTTKARI 469
Cdd:COG2905    8 DVVTVSPDATVREAARLMTEKGVGSLVVVDDDGRLVGIITDRDLRrrvlaeGLDPLD---TPVSEVMTRPPITVSPDDSL 84

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 974335151 470 IDVL-----RRIRGFedPVIgvvnDDGVLVATIYERELLRLLIT 508
Cdd:COG2905   85 AEALelmeeHRIRHL--PVV----DDGKLVGIVSITDLLRALSE 122
CBS_arch_repeat1 cd17777
CBS pair domains found in archeal proteins, repeat 1; CBS pair domains found in archeal ...
 397-506 5.83e-05

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: 43.10  E-value: 5.83e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 974335151 397 PLTVTCSDNLRIVIDRMVERGVRAVVVVNsEGKPLGYLTMQQL------------------------LEIDPATYGMTPa 452
Cdd:cd17777   12 VLSISPSAPILSAFEKMNRRGIRRLVVVD-ENKLEGILSARDLvsylgggclfkivesrhqgdlysaLNREVVETIMTP- 89

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 974335151 453 cdlplnELTTVTTKARIIDVLRRI--RGFEdpVIGVVNDDGVLVATIYERELLRLL 506
Cdd:cd17777   90 ------NPVYVYEDSDLIEALTIMvtRGIG--SLPVVDRDGRPVGIVTERDLVLYL 137
CBS_pair_bac cd04629
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains present in bacteria; ...
 396-504 6.67e-05

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


Pssm-ID: 341392 [Multi-domain]  Cd Length: 116  Bit Score: 42.42  E-value: 6.67e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 974335151 396 KPLTVTCSDNLRIVIDRMVERGVRAVVVVNSEGKPLGYLT----MQQLLEidpATY-GMTPA--CDLPLNELTTVTTKAR 468
Cdd:cd04629    4 NPVTLTPDTSILEAVELLLEHKISGAPVVDEQGRLVGFLSeqdcLKALLE---ASYhCEPGGtvADYMSTEVLTVSPDTS 80

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 974335151 469 IIDV--------LRRIrgfedPVIgvvnDDGVLVATIYERELLR 504
Cdd:cd04629   81 IVDLaqlflknkPRRY-----PVV----EDGKLVGQISRRDVLR 115
CBS pfam00571
CBS domain; CBS domains are small intracellular modules that pair together to form a stable ...
 396-441 6.84e-05

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


Pssm-ID: 425756 [Multi-domain]  Cd Length: 57  Bit Score: 40.66  E-value: 6.84e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*.
gi 974335151  396 KPLTVTCSDNLRIVIDRMVERGVRAVVVVNSEGKPLGYLTMQQLLE 441
Cdd:pfam00571   8 DVVTVSPDTTLEEALELMREHGISRLPVVDEDGKLVGIVTLKDLLR 53
CBS_pair_bact_arch cd17775
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains present in bacteria ...
 399-506 7.84e-05

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: 42.14  E-value: 7.84e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 974335151 399 TVTCSDNLRIVIDRMVERGVRAVVVVNSEGKPLGYLTMQQLL------EIDPATygmTPACDLPLNELTTVTTKARIIDV 472
Cdd:cd17775    7 TASPDTSVLEAARLMRDHHVGSVVVVEEDGKPVGIVTDRDIVvevvakGLDPKD---VTVGDIMSADLITAREDDGLFEA 83

                         90       100       110
                 ....*....|....*....|....*....|....
gi 974335151 473 LRRIRGFEDPVIGVVNDDGVLVATIYERELLRLL 506
Cdd:cd17775   84 LERMREKGVRRLPVVDDDGELVGIVTLDDILELL 117
PRK07807 PRK07807
GuaB1 family IMP dehydrogenase-related protein;
397-507 1.33e-04

GuaB1 family IMP dehydrogenase-related protein;


Pssm-ID: 181127 [Multi-domain]  Cd Length: 479  Bit Score: 44.51  E-value: 1.33e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 974335151 397 PLTVTCSDNLRIVIDRMVERGVRAVVVVNSEGKPLGYLTMQQLLEIDPatygMTPACDLPLNELTTVTTKARIIDVLRRI 476
Cdd:PRK07807  99 PVTLSPDDTVGDALALLPKRAHGAVVVVDEEGRPVGVVTEADCAGVDR----FTQVRDVMSTDLVTLPAGTDPREAFDLL 174

                         90       100       110
                 ....*....|....*....|....*....|.
gi 974335151 477 RGFEDPVIGVVNDDGVLVATIYERELLRLLI 507
Cdd:PRK07807 175 EAARVKLAPVVDADGRLVGVLTRTGALRATI 205
CBS_pair_chlorobiales cd09837
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains present in ...
 409-504 1.84e-04

Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains present in chlorobiales; 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: 341406 [Multi-domain]  Cd Length: 111  Bit Score: 40.82  E-value: 1.84e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 974335151 409 VIDRMVERGVRAVVVVnSEGKPLGYLTMQQLLEID--PATYGMTPAcDLPLNELTTVTTKARIIDVLRRIRGFEDPVIGV 486
Cdd:cd09837   16 VLAFMQAKELSCAPVL-HDGRYVAMVTLADLLPARqgTPTAGLKLG-ELSLEEVGSIGPHEHLFDLFSRLALFPCSIIPV 93

                         90
                 ....*....|....*...
gi 974335151 487 VNDDGVLVATIYERELLR 504
Cdd:cd09837   94 SDEDGRYIGVVSKKRVLE 111
COG3448 COG3448
CBS-domain-containing membrane protein [Signal transduction mechanisms];
388-435 2.08e-04

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


Pssm-ID: 442671 [Multi-domain]  Cd Length: 136  Bit Score: 41.39  E-value: 2.08e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*...
gi 974335151 388 VMSiseyAKPLTVTCSDNLRIVIDRMVERGVRAVVVVNSEGKPLGYLT 435
Cdd:COG3448   78 VMT----RPVVTVTPDTPLEEAAELMLEHGIHRLPVVDDDGRLVGIVT 121
CBS_pair_SF cd02205
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains superfamily; The CBS ...
 387-440 2.67e-04

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: 40.69  E-value: 2.67e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....
gi 974335151 387 NVMSiseyAKPLTVTCSDNLRIVIDRMVERGVRAVVVVNSEGKPLGYLTMQQLL 440
Cdd:cd02205   63 EVMT----PDVITVSPDTDLEEALELMLEHGIRRLPVVDDDGKLVGIVTRRDIL 112
CBS COG0517
CBS domain [Signal transduction mechanisms];
388-441 2.67e-04

CBS domain [Signal transduction mechanisms];


Pssm-ID: 440283 [Multi-domain]  Cd Length: 128  Bit Score: 41.00  E-value: 2.67e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....
gi 974335151 388 VMSiseyAKPLTVTCSDNLRIVIDRMVERGVRAVVVVNSEGKPLGYLTMQQLLE 441
Cdd:COG0517   72 VMT----RPPVTVSPDTSLEEAAELMEEHKIRRLPVVDDDGRLVGIITIKDLLK 121
CBS_pair_peptidase_M50 cd04639
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains found in the ...
 419-506 4.34e-04

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


Pssm-ID: 341397 [Multi-domain]  Cd Length: 120  Bit Score: 40.25  E-value: 4.34e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 974335151 419 RAVVVVNSEGKPLGYLTMQQLLEIDPATYGMTPACDL--PLNELTTVTTKARIIDVLRRIRGFEDPVIGVVNDDGVLVAT 496
Cdd:cd04639   31 REFLVTDEAGRLVGLITVDDLRAIPTSQWPDTPVRELmkPLEEIPTVAADQSLLEVVKLLEEQQLPALAVVSENGTLVGL 110

                         90
                 ....*....|
gi 974335151 497 IYERELLRLL 506
Cdd:cd04639  111 IEKEDIIELL 120
CBS smart00116
Domain in cystathionine beta-synthase and other proteins; Domain present in all 3 forms of ...
 397-440 4.58e-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: 37.88  E-value: 4.58e-04
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....
gi 974335151   397 PLTVTCSDNLRIVIDRMVERGVRAVVVVNSEGKPLGYLTMQQLL 440
Cdd:smart00116   2 VVTVSPDTTLEEALELLRENGIRRLPVVDEEGRLVGIVTRRDII 45
YtoI COG4109
Predicted transcriptional regulator containing CBS domains [Transcription];
375-441 6.36e-04

Predicted transcriptional regulator containing CBS domains [Transcription];


Pssm-ID: 443285 [Multi-domain]  Cd Length: 135  Bit Score: 39.90  E-value: 6.36e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 974335151 375 GVNPLIRVKlnnNVMSiseyAKPLTVTCSDNLRIVIDRMVERGVRAVVVVNSEGKPLGYLTMQQLLE 441
Cdd:COG4109   71 GKDDDTPIE---DVMT----KNPITVTPDTSLASAAHKMIWEGIELLPVVDDDGRLLGIISRQDVLK 130
CBS_pair_CAP-ED_NT_Pol-beta-like_DUF294_assoc cd17771
CBS domain protein; This cd contains two tandem repeats of the cystathionine beta-synthase ...
 400-440 6.61e-04

CBS domain protein; This cd contains two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with the bacterial CAP_ED (cAMP receptor protein effector domain) family of transcription factors, the NT_Pol-beta-like domain, and the DUF294 domain. Members of CAP_ED, include CAP which binds cAMP, FNR (fumarate and nitrate reductase) which uses an iron-sulfur cluster to sense oxygen, and CooA a heme containing CO sensor. In all cases binding of the effector leads to conformational changes and the ability to activate transcription. The NT_Pol-beta-like domain includes the Nucleotidyltransferase (NT) domains of DNA polymerase beta and other family X DNA polymerases, as well as the NT domains of class I and class II CCA-adding enzymes, RelA- and SpoT-like ppGpp synthetases and hydrolases, 2'5'-oligoadenylate (2-5A)synthetases, Escherichia coli adenylyltransferase (GlnE), Escherichia coli uridylyl transferase (GlnD), poly (A) polymerases, terminal uridylyl transferases, Staphylococcus aureus kanamycin nucleotidyltransferase, and similar proteins. DUF294 is a putative nucleotidyltransferase with a conserved DxD motif. CBS is a small domain originally identified in cystathionine beta-synthase and subsequently found in a wide range of different 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: 341407 [Multi-domain]  Cd Length: 115  Bit Score: 39.61  E-value: 6.61e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|...
gi 974335151 400 VTCSDN--LRIVIDRMVERGVRAVVVVNSEGKPLGYLTMQQLL 440
Cdd:cd17771    7 VTCSPDtpLRAALETMHERRVGSMVVVDANRRPVGIFTLRDLL 49
CBS_pair_arch cd09836
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains; The CBS domain, ...
 396-506 1.08e-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: 38.66  E-value: 1.08e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 974335151 396 KPLTVTCSDNLRIVIDRMVERGVRAVVVVNSEGKPLGYLTMQQLLEI--------DPATYGMTPacdlplnELTTVTTKA 467
Cdd:cd09836    4 PVVTVPPETTIREAAKLMAENNIGSVVVVDDDGKPVGIVTERDIVRAvaegidldTPVEEIMTK-------NLVTVSPDE 76

                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 974335151 468 RIIDVLRRIRGFEDPVIGVVNDDGVLVATIYERELLRLL 506
Cdd:cd09836   77 SIYEAAELMREHNIRHLPVVDGGGKLVGVISIRDLAREL 115
CBS_arch_repeat1 cd17777
CBS pair domains found in archeal proteins, repeat 1; CBS pair domains found in archeal ...
 387-440 1.42e-03

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: 38.86  E-value: 1.42e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 974335151 387 NVMSISEYAK--PLTVTCSDNLRIVIDRMVERGVRAVVVVNSEGKPLGYLTMQQLL 440
Cdd:cd17777   79 NREVVETIMTpnPVYVYEDSDLIEALTIMVTRGIGSLPVVDRDGRPVGIVTERDLV 134
PRK03562 PRK03562
glutathione-regulated potassium-efflux system protein KefC; Provisional
 171-277 2.13e-03

glutathione-regulated potassium-efflux system protein KefC; Provisional


Pssm-ID: 235131 [Multi-domain]  Cd Length: 621  Bit Score: 40.75  E-value: 2.13e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 974335151 171 LGGSLLTLIGIAVLIAAIFTVGRWVSR-ALEWVeGYVKAREAEFAAAIFLVLVISFLPEAVNFNPAMAALFLGILLRD-- 247
Cdd:PRK03562 179 LGAFALSALKVAGALALVVLGGRYVTRpALRFV-ARSGLREVFTAVALFLVFGFGLLMEEVGLSMALGAFLAGVLLASse 257

                         90       100       110
                 ....*....|....*....|....*....|...
gi 974335151 248 YlkdRPEL---LEKLHGFTYGffepLFFVSIGL 277
Cdd:PRK03562 258 Y---RHALesdIEPFKGLLLG----LFFIAVGM 283
CBS_two-component_sensor_histidine_kinase_repeat2 cd17774
2 tandem repeats of the CBS domain in the two-component sensor histidine kinase and ...
 388-444 2.60e-03

2 tandem repeats of the CBS domain in the two-component sensor histidine kinase and related-proteins, repeat 2; This cd contains 2 tandem repeats of the CBS domain in the two-component sensor histidine kinase and related-proteins. Two-component regulation is the predominant form of signal recognition and response coupling mechanism used by bacteria to sense and respond to diverse environmental stresses and cues ranging from common environmental stimuli to host signals recognized by pathogens and bacterial cell-cell communication signals. The structures of both sensors and regulators are modular, and numerous variations in domain architecture and composition have evolved to tailor to specific needs in signal perception and signal transduction. The simplest histidine kinase sensors consists of only sensing and kinase domains. The more complex hybrid sensors contain an additional REC domain typical of two-component regulators and in some cases a C-terminal histidine phosphotransferase (HPT) domain. The CBS domain, named after human CBS, is a small domain originally identified in cystathionine beta-synthase and is subsequently found in a wide range of different proteins. CBS domains usually occur in tandem repeats. They associate to form a so-called Bateman domain or a CBS pair based on crystallographic studies in bacteria. The CBS pair was used as a basis for this cd hierarchy since the human CBS proteins can adopt the typical core structure and form an intramolecular CBS pair. The interface between the two CBS domains forms a cleft that is a potential ligand binding site. The CBS pair coexists with a variety of other functional domains and this has been used to help in its classification here. It has been proposed that the CBS domain may play a regulatory role, although its exact function is unknown. Mutations of conserved residues within this domain are associated with a variety of human hereditary diseases, including congenital myotonia, idiopathic generalized epilepsy, hypercalciuric nephrolithiasis, and classic Bartter syndrome (CLC chloride channel family members), Wolff-Parkinson-White syndrome (gamma 2 subunit of AMP-activated protein kinase), retinitis pigmentosa (IMP dehydrogenase-1), and homocystinuria (cystathionine beta-synthase).


Pssm-ID: 341410 [Multi-domain]  Cd Length: 137  Bit Score: 38.29  E-value: 2.60e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 974335151 388 VMSISeyakPLTVTCSDNLRIVIDRMVERGVRAVVVVNSEGKPLGYLTMQQLLE-IDP 444
Cdd:cd17774   74 VMSSP----LFSLRPDDSLWTAHQLMQQRRIRRLVVVGEQGELLGIVTQTSLLQaLDP 127
CBS_pair_bac_arch cd17785
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains present in bacteria ...
 396-474 4.56e-03

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


Pssm-ID: 341421 [Multi-domain]  Cd Length: 136  Bit Score: 37.64  E-value: 4.56e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 974335151 396 KPLTVTCSDNLRIVIDRMVERGV-RAVVVVNSEGKPLGYLTMQQLLEIDPATYGMTPACDLPLNELTTVTTKARIIDVLR 474
Cdd:cd17785   11 KPSVVHENTSIRDVIDKMIEDPKtRSVYVVDDDEKLLGIITLMELLKYIGYRFGVTIYKGVSFGLLLRISLKEKAKDIML 90
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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