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Conserved domains on  [gi|328772605|gb|EGF82643|]
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hypothetical protein BATDEDRAFT_86123 [Batrachochytrium dendrobatidis JAM81]

Protein Classification

CBS domain-containing protein( domain architecture ID 10333671)

CBS (cystathione beta synthase) domain-containing protein may bind ligands with an adenosyl group such as AMP, ATP and S-AdoMet; similar to Arabidopsis thaliana SNF1-related protein kinase regulatory subunit gamma-1, a regulatory subunit of the probable trimeric SNF1-related protein kinase (SnRK) complex, which may play a role in a signal transduction cascade regulating gene expression and carbohydrate metabolism in higher plants

CATH:  3.10.580.10
PubMed:  16275737|24161944|21958115
SCOP:  4000247

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
COG3448 COG3448
CBS-domain-containing membrane protein [Signal transduction mechanisms];
259-384 1.28e-13

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


:

Pssm-ID: 442671 [Multi-domain]  Cd Length: 136  Bit Score: 67.20  E-value: 1.28e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 328772605 259 KQLVCVESSMSALAALRSLYLHQVSAVAVVDTNGRLVANLSASDLRGvnfsnlEMLLGSVFEFLEAEKRTP-NQLKSDQL 337
Cdd:COG3448   10 RDVVTVSPDTTLREALELMREHGIRGLPVVDEDGRLVGIVTERDLLR------ALLPDRLDELEERLLDLPvEDVMTRPV 83

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 328772605 338 KSVEPGSVVGEVGVSMMEHMIHHLWVVDDDDHPIGVVSMSDVLALFV 384
Cdd:COG3448   84 VTVTPDTPLEEAAELMLEHGIHRLPVVDDDGRLVGIVTRTDLLRALA 130
COG3448 super family cl34614
CBS-domain-containing membrane protein [Signal transduction mechanisms];
34-201 1.40e-05

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


The actual alignment was detected with superfamily member COG3448:

Pssm-ID: 442671 [Multi-domain]  Cd Length: 136  Bit Score: 44.47  E-value: 1.40e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 328772605  34 KPLISVHQDTTLDNVLSIMHTSQILAIPVykvpKDEpDGKVfTGIVSVFDILaNTVFQSVFDDMSGNVKNpitmskdefq 113
Cdd:COG3448   10 RDVVTVSPDTTLREALELMREHGIRGLPV----VDE-DGRL-VGIVTERDLL-RALLPDRLDELEERLLD---------- 72

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 328772605 114 qyirmvkeehayfsTKIGELLgqtseSAESWTLHSSDPLTSLLQILTYANRHRALIIDDDVNLAtvappsGssirLVTQT 193
Cdd:COG3448   73 --------------LPVEDVM-----TRPVVTVTPDTPLEEAAELMLEHGIHRLPVVDDDGRLV------G----IVTRT 123


                 ....*...
gi 328772605 194 DLLRYLLD 201
Cdd:COG3448  124 DLLRALAR 131
 
Name Accession Description Interval E-value
COG3448 COG3448
CBS-domain-containing membrane protein [Signal transduction mechanisms];
259-384 1.28e-13

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


Pssm-ID: 442671 [Multi-domain]  Cd Length: 136  Bit Score: 67.20  E-value: 1.28e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 328772605 259 KQLVCVESSMSALAALRSLYLHQVSAVAVVDTNGRLVANLSASDLRGvnfsnlEMLLGSVFEFLEAEKRTP-NQLKSDQL 337
Cdd:COG3448   10 RDVVTVSPDTTLREALELMREHGIRGLPVVDEDGRLVGIVTERDLLR------ALLPDRLDELEERLLDLPvEDVMTRPV 83

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 328772605 338 KSVEPGSVVGEVGVSMMEHMIHHLWVVDDDDHPIGVVSMSDVLALFV 384
Cdd:COG3448   84 VTVTPDTPLEEAAELMLEHGIHRLPVVDDDGRLVGIVTRTDLLRALA 130
CBS_pair_SF cd02205
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains superfamily; The CBS ...
 258-381 9.31e-13

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: 64.19  E-value: 9.31e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 328772605 258 KKQLVCVESSMSALAALRSLYLHQVSAVAVVDTNGRLVANLSASDLRGVNFSNLEMLLGSVFEFLeaekrtpnqlkSDQL 337
Cdd:cd02205    1 TRDVVTVDPDTTVREALELMAENGIGALPVVDDDGKLVGIVTERDILRALVEGGLALDTPVAEVM-----------TPDV 69

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 328772605 338 KSVEPGSVVGEVGVSMMEHMIHHLWVVDDDDHPIGVVSMSDVLA 381
Cdd:cd02205   70 ITVSPDTDLEEALELMLEHGIRRLPVVDDDGKLVGIVTRRDILR 113
CBS pfam00571
CBS domain; CBS domains are small intracellular modules that pair together to form a stable ...
 331-384 3.73e-06

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


Pssm-ID: 425756 [Multi-domain]  Cd Length: 57  Bit Score: 43.74  E-value: 3.73e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 328772605  331 QLKSDQLKSVEPGSVVGEVGVSMMEHMIHHLWVVDDDDHPIGVVSMSDVLALFV 384
Cdd:pfam00571   3 DIMTKDVVTVSPDTTLEEALELMREHGISRLPVVDEDGKLVGIVTLKDLLRALL 56
COG3448 COG3448
CBS-domain-containing membrane protein [Signal transduction mechanisms];
34-201 1.40e-05

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


Pssm-ID: 442671 [Multi-domain]  Cd Length: 136  Bit Score: 44.47  E-value: 1.40e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 328772605  34 KPLISVHQDTTLDNVLSIMHTSQILAIPVykvpKDEpDGKVfTGIVSVFDILaNTVFQSVFDDMSGNVKNpitmskdefq 113
Cdd:COG3448   10 RDVVTVSPDTTLREALELMREHGIRGLPV----VDE-DGRL-VGIVTERDLL-RALLPDRLDELEERLLD---------- 72

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 328772605 114 qyirmvkeehayfsTKIGELLgqtseSAESWTLHSSDPLTSLLQILTYANRHRALIIDDDVNLAtvappsGssirLVTQT 193
Cdd:COG3448   73 --------------LPVEDVM-----TRPVVTVTPDTPLEEAAELMLEHGIHRLPVVDDDGRLV------G----IVTRT 123


                 ....*...
gi 328772605 194 DLLRYLLD 201
Cdd:COG3448  124 DLLRALAR 131
CBS smart00116
Domain in cystathionine beta-synthase and other proteins; Domain present in all 3 forms of ...
 337-380 3.39e-05

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: 40.96  E-value: 3.39e-05
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....
gi 328772605   337 LKSVEPGSVVGEVGVSMMEHMIHHLWVVDDDDHPIGVVSMSDVL 380
Cdd:smart00116   2 VVTVSPDTTLEEALELLRENGIRRLPVVDEEGRLVGIVTRRDII 45
CBS_pair_SF cd02205
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains superfamily; The CBS ...
 33-197 1.70e-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: 1.70e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 328772605  33 KKPLISVHQDTTLDNVLSIMHTSQILAIPVykvpkDEPDGKVfTGIVSVFDILantvfqsvfddmsgnvknpitmskdef 112
Cdd:cd02205    1 TRDVVTVDPDTTVREALELMAENGIGALPV-----VDDDGKL-VGIVTERDIL--------------------------- 47

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 328772605 113 qqyiRMVKEEHAYFSTKIGELLgqtseSAESWTLHSSDPLTSLLQILTYANRHRALIIDDDVNLatvappsgssIRLVTQ 192
Cdd:cd02205   48 ----RALVEGGLALDTPVAEVM-----TPDVITVSPDTDLEEALELMLEHGIRRLPVVDDDGKL----------VGIVTR 108


                 ....*
gi 328772605 193 TDLLR 197
Cdd:cd02205  109 RDILR 113
CBS pfam00571
CBS domain; CBS domains are small intracellular modules that pair together to form a stable ...
 33-85 3.50e-04

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


Pssm-ID: 425756 [Multi-domain]  Cd Length: 57  Bit Score: 38.35  E-value: 3.50e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 328772605   33 KKPLISVHQDTTLDNVLSIMHTSQILAIPVYkvpkdEPDGKVfTGIVSVFDIL 85
Cdd:pfam00571   6 TKDVVTVSPDTTLEEALELMREHGISRLPVV-----DEDGKL-VGIVTLKDLL 52
 
Name Accession Description Interval E-value
COG3448 COG3448
CBS-domain-containing membrane protein [Signal transduction mechanisms];
259-384 1.28e-13

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


Pssm-ID: 442671 [Multi-domain]  Cd Length: 136  Bit Score: 67.20  E-value: 1.28e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 328772605 259 KQLVCVESSMSALAALRSLYLHQVSAVAVVDTNGRLVANLSASDLRGvnfsnlEMLLGSVFEFLEAEKRTP-NQLKSDQL 337
Cdd:COG3448   10 RDVVTVSPDTTLREALELMREHGIRGLPVVDEDGRLVGIVTERDLLR------ALLPDRLDELEERLLDLPvEDVMTRPV 83

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 328772605 338 KSVEPGSVVGEVGVSMMEHMIHHLWVVDDDDHPIGVVSMSDVLALFV 384
Cdd:COG3448   84 VTVTPDTPLEEAAELMLEHGIHRLPVVDDDGRLVGIVTRTDLLRALA 130
CBS_pair_SF cd02205
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains superfamily; The CBS ...
 258-381 9.31e-13

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: 64.19  E-value: 9.31e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 328772605 258 KKQLVCVESSMSALAALRSLYLHQVSAVAVVDTNGRLVANLSASDLRGVNFSNLEMLLGSVFEFLeaekrtpnqlkSDQL 337
Cdd:cd02205    1 TRDVVTVDPDTTVREALELMAENGIGALPVVDDDGKLVGIVTERDILRALVEGGLALDTPVAEVM-----------TPDV 69

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 328772605 338 KSVEPGSVVGEVGVSMMEHMIHHLWVVDDDDHPIGVVSMSDVLA 381
Cdd:cd02205   70 ITVSPDTDLEEALELMLEHGIRRLPVVDDDGKLVGIVTRRDILR 113
CBS COG0517
CBS domain [Signal transduction mechanisms];
258-387 2.36e-12

CBS domain [Signal transduction mechanisms];


Pssm-ID: 440283 [Multi-domain]  Cd Length: 128  Bit Score: 63.73  E-value: 2.36e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 328772605 258 KKQLVCVESSMSALAALRSLYLHQVSAVAVVDTNGRLVANLSASDLRGVnfsnlemllgsvfefLEAEKRTPNQLK---- 333
Cdd:COG0517    8 TTDVVTVSPDATVREALELMSEKRIGGLPVVDEDGKLVGIVTDRDLRRA---------------LAAEGKDLLDTPvsev 72

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 328772605 334 -SDQLKSVEPGSVVGEVGVSMMEHMIHHLWVVDDDDHPIGVVSMSDVLALFVPEN 387
Cdd:COG0517   73 mTRPPVTVSPDTSLEEAAELMEEHKIRRLPVVDDDGRLVGIITIKDLLKALLEPL 127
COG2905 COG2905
Signal-transduction protein containing cAMP-binding, CBS, and nucleotidyltransferase domains ...
 259-386 1.07e-11

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


Pssm-ID: 442149 [Multi-domain]  Cd Length: 124  Bit Score: 61.38  E-value: 1.07e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 328772605 259 KQLVCVESSMSALAALRSLYLHQVSAVAVVDTNGRLVANLSASDLRGVNFSNLEMLLG-SVFEFLeaekrTPNqlksdqL 337
Cdd:COG2905    7 RDVVTVSPDATVREAARLMTEKGVGSLVVVDDDGRLVGIITDRDLRRRVLAEGLDPLDtPVSEVM-----TRP------P 75

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*....
gi 328772605 338 KSVEPGSVVGEVGVSMMEHMIHHLWVVdDDDHPIGVVSMSDVLALFVPE 386
Cdd:COG2905   76 ITVSPDDSLAEALELMEEHRIRHLPVV-DDGKLVGIVSITDLLRALSEE 123
COG2524 COG2524
Predicted transcriptional regulator, contains C-terminal CBS domains [Transcription];
259-383 1.25e-10

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


Pssm-ID: 442013 [Multi-domain]  Cd Length: 206  Bit Score: 60.67  E-value: 1.25e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 328772605 259 KQLVCVESSMSALAALRSLYLHQVSAVAVVDtNGRLVANLSASDLRGVNFSNLEMLLGSVFEFLeaekrtpnqlkSDQLK 338
Cdd:COG2524   94 KDVITVSPDTTLEEALELMLEKGISGLPVVD-DGKLVGIITERDLLKALAEGRDLLDAPVSDIM-----------TRDVV 161

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 328772605 339 SVEPGSVVGEVGVSMMEHMIHHLWVVDDDDHPIGVVSMSDVLALF 383
Cdd:COG2524  162 TVSEDDSLEEALRLMLEHGIGRLPVVDDDGKLVGIITRTDILRAL 206
CBS_pair_arch cd09836
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains; The CBS domain, ...
 258-381 1.81e-09

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: 54.84  E-value: 1.81e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 328772605 258 KKQLVCVESSMSALAALRSLYLHQVSAVAVVDTNGRLVANLSASDL-RGVnfsnlemllgsvfefleAEKRTPN----QL 332
Cdd:cd09836    2 SKPVVTVPPETTIREAAKLMAENNIGSVVVVDDDGKPVGIVTERDIvRAV-----------------AEGIDLDtpveEI 64

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*....
gi 328772605 333 KSDQLKSVEPGSVVGEVGVSMMEHMIHHLWVVDDDDHPIGVVSMSDVLA 381
Cdd:cd09836   65 MTKNLVTVSPDESIYEAAELMREHNIRHLPVVDGGGKLVGVISIRDLAR 113
CBS_pair_BON_assoc cd04586
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with the ...
 259-380 1.80e-08

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: 52.82  E-value: 1.80e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 328772605 259 KQLVCVESSMSALAALRSLYLHQVSAVAVVDTNGRLVANLSASDL----RGVNFSNLEMLLGSVF--------EFLEAEK 326
Cdd:cd04586    3 TDVVTVTPDTSVREAARLLLEHRISGLPVVDDDGKLVGIVSEGDLlrreEPGTEPRRVWWLDALLesperlaeEYVKAHG 82

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....
gi 328772605 327 RTPNQLKSDQLKSVEPGSVVGEVGVSMMEHMIHHLWVVdDDDHPIGVVSMSDVL 380
Cdd:cd04586   83 RTVGDVMTRPVVTVSPDTPLEEAARLMERHRIKRLPVV-DDGKLVGIVSRADLL 135
CBS_euAMPK_gamma-like_repeat2 cd04641
CBS pair domain found in 5'-AMP (adenosine monophosphate)-activated protein kinase; The 5'-AMP ...
 257-380 4.78e-08

CBS pair domain found in 5'-AMP (adenosine monophosphate)-activated protein kinase; The 5'-AMP (adenosine monophosphate)-activated protein kinase (AMPK) coordinates metabolic function with energy availability by responding to changes in intracellular ATP (adenosine triphosphate) and AMP concentrations. Most of the members of this cd contain two Bateman domains, each of which is composed of a tandem pair of cystathionine beta-synthase (CBS) motifs. 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: 341399 [Multi-domain]  Cd Length: 124  Bit Score: 50.97  E-value: 4.78e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 328772605 257 TKKQLVCVESSMSALAALRSLYLHQVSAVAVVDTNGRLVANLSASDL----RGVNFSNLEMllgSVFEFLEAEKRTPNQ- 331
Cdd:cd04641    1 TYENIATASMDTPVIDALNLFVERRVSALPIVDEDGRVVDIYAKFDVinlaAEKTYNNLDL---TVGEALQHRSEDFEGv 77

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 328772605 332 ---LKSDQLKSVEPGSVVGEVgvsmmehmiHHLWVVDDDDHPIGVVSMSDVL 380
Cdd:cd04641   78 htcTLNDTLETIIDRIVKAEV---------HRLVVVDEEDRLEGIVSLSDIL 120
CBS_pair_HPP_assoc cd04600
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with the ...
 261-381 2.63e-07

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: 49.10  E-value: 2.63e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 328772605 261 LVCVESSMSALAALRSLYLHQVSAVAVVDTNGRLVANLSASDL-RGVNFSNLEMLLGSVFEFLEAEKRTPN---QLKSDQ 336
Cdd:cd04600    5 VVTVTPDTSLEEAWRLLRRHRIKALPVVDRARRLVGIVTLADLlKHADLDPPRGLRGRLRRTLGLRRDRPEtvgDIMTRP 84

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 328772605 337 LKSVEPGSVVGEVgVSMM-EHMIHHLWVVDDDDHPIGVVSMSDVLA 381
Cdd:cd04600   85 VVTVRPDTPIAEL-VPLFsDGGLHHIPVVDADGRLVGIVTQSDLIA 129
CBS_pair_CAP-ED_NT_Pol-beta-like_DUF294_assoc cd04587
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with the ...
 258-380 8.57e-07

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 (Nucleotidyltransferase) Pol-beta-like domain, and the DUF294 dom; 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: 341363 [Multi-domain]  Cd Length: 114  Bit Score: 47.42  E-value: 8.57e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 328772605 258 KKQLVCVESSMSALAALRSLYLHQVSAVAVVDtNGRLVANLSASDLRG-VnfsnlemllgsVFEFLEAEkrTP-NQLKSD 335
Cdd:cd04587    3 SRPPVTVPPDATIQEAAQLMSEERVSSLLVVD-DGRLVGIVTDRDLRNrV-----------VAEGLDPD--TPvSEIMTP 68

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 328772605 336 QLKSVEPGSVVGEVGVSMMEHMIHHLWVVDDDDhPIGVVSMSDVL 380
Cdd:cd04587   69 PPVTIDADALVFEALLLMLERNIHHLPVVDDGR-VVGVVTATDLM 112
CBS_pair_GGDEF_PAS_repeat1 cd09833
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains found in diguanylate ...
 280-379 1.17e-06

Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains found in diguanylate cyclase/phosphodiesterase proteins with PAS sensors, repeat 1; This cd contains two tandem repeats of the cystathionine beta-synthase (CBS pair) domains found in diguanylate cyclase/phosphodiesterase proteins with PAS sensors. PAS domains have been found to bind ligands, and to act as sensors for light and oxygen in signal transduction. The GGDEF domain has been suggested to be homologous to the adenylyl cyclase catalytic domain and is thought to be involved in regulating cell surface adhesiveness 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: 341403 [Multi-domain]  Cd Length: 116  Bit Score: 46.83  E-value: 1.17e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 328772605 280 HQVSAVAVVDtNGRLVANLSASDLRGVNFSNLEMLlgsvfefleaekRTP-NQLKSDQLKSVEPGSVVGEVGVSMMEHMI 358
Cdd:cd09833   26 RRCSSILIVE-NGEIVGIWTERDALKLDFSDPDAF------------RRPiSEVMSSPVLTIPQDTTLGEAAVRFRQEGV 92

                         90       100
                 ....*....|....*....|.
gi 328772605 359 HHLWVVDDDDHPIGVVSMSDV 379
Cdd:cd09833   93 RHLLVVDDDGRPVGIVSQTDV 113
CBS pfam00571
CBS domain; CBS domains are small intracellular modules that pair together to form a stable ...
 331-384 3.73e-06

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


Pssm-ID: 425756 [Multi-domain]  Cd Length: 57  Bit Score: 43.74  E-value: 3.73e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 328772605  331 QLKSDQLKSVEPGSVVGEVGVSMMEHMIHHLWVVDDDDHPIGVVSMSDVLALFV 384
Cdd:pfam00571   3 DIMTKDVVTVSPDTTLEEALELMREHGISRLPVVDEDGKLVGIVTLKDLLRALL 56
COG3448 COG3448
CBS-domain-containing membrane protein [Signal transduction mechanisms];
34-201 1.40e-05

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


Pssm-ID: 442671 [Multi-domain]  Cd Length: 136  Bit Score: 44.47  E-value: 1.40e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 328772605  34 KPLISVHQDTTLDNVLSIMHTSQILAIPVykvpKDEpDGKVfTGIVSVFDILaNTVFQSVFDDMSGNVKNpitmskdefq 113
Cdd:COG3448   10 RDVVTVSPDTTLREALELMREHGIRGLPV----VDE-DGRL-VGIVTERDLL-RALLPDRLDELEERLLD---------- 72

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 328772605 114 qyirmvkeehayfsTKIGELLgqtseSAESWTLHSSDPLTSLLQILTYANRHRALIIDDDVNLAtvappsGssirLVTQT 193
Cdd:COG3448   73 --------------LPVEDVM-----TRPVVTVTPDTPLEEAAELMLEHGIHRLPVVDDDGRLV------G----IVTRT 123


                 ....*...
gi 328772605 194 DLLRYLLD 201
Cdd:COG3448  124 DLLRALAR 131
CBS smart00116
Domain in cystathionine beta-synthase and other proteins; Domain present in all 3 forms of ...
 337-380 3.39e-05

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: 40.96  E-value: 3.39e-05
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....
gi 328772605   337 LKSVEPGSVVGEVGVSMMEHMIHHLWVVDDDDHPIGVVSMSDVL 380
Cdd:smart00116   2 VVTVSPDTTLEEALELLRENGIRRLPVVDEEGRLVGIVTRRDII 45
CBS_pair_HRP1_like cd04622
CBS pair domain found in Hypoxic Response Protein 1 (HRP1) -like proteinds; Mycobacterium ...
 259-379 6.58e-05

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


Pssm-ID: 341390 [Multi-domain]  Cd Length: 115  Bit Score: 42.02  E-value: 6.58e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 328772605 259 KQLVCVESSMSALAALRSLYLHQVSAVAVVDtNGRLVANLSASD--LRGVnfsnlemllgsvfefleAEKRTPNQLK--- 333
Cdd:cd04622    3 RDVVTVSPDTTLREAARLMRDLDIGALPVCE-GDRLVGMVTDRDivVRAV-----------------AEGKDPNTTTvre 64

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 328772605 334 --SDQLKSVEPGSVVGEVGVSMMEHMIHHLWVVDDDDHPIGVVSMSDV 379
Cdd:cd04622   65 vmTGDVVTCSPDDDVEEAARLMAEHQVRRLPVVDDDGRLVGIVSLGDL 112
CBS_pair_SF cd02205
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains superfamily; The CBS ...
 33-197 1.70e-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: 1.70e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 328772605  33 KKPLISVHQDTTLDNVLSIMHTSQILAIPVykvpkDEPDGKVfTGIVSVFDILantvfqsvfddmsgnvknpitmskdef 112
Cdd:cd02205    1 TRDVVTVDPDTTVREALELMAENGIGALPV-----VDDDGKL-VGIVTERDIL--------------------------- 47

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 328772605 113 qqyiRMVKEEHAYFSTKIGELLgqtseSAESWTLHSSDPLTSLLQILTYANRHRALIIDDDVNLatvappsgssIRLVTQ 192
Cdd:cd02205   48 ----RALVEGGLALDTPVAEVM-----TPDVITVSPDTDLEEALELMLEHGIRRLPVVDDDGKL----------VGIVTR 108


                 ....*
gi 328772605 193 TDLLR 197
Cdd:cd02205  109 RDILR 113
CBS COG0517
CBS domain [Signal transduction mechanisms];
17-85 2.32e-04

CBS domain [Signal transduction mechanisms];


Pssm-ID: 440283 [Multi-domain]  Cd Length: 128  Bit Score: 40.62  E-value: 2.32e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 328772605  17 LSHIPISQVLNhahgskKPLISVHQDTTLDNVLSIMHTSQILAIPVYKvpkdepDGKVFTGIVSVFDIL 85
Cdd:COG0517   64 LLDTPVSEVMT------RPPVTVSPDTSLEEAAELMEEHKIRRLPVVD------DDGRLVGIITIKDLL 120
CBS_pair_arch1_repeat2 cd04632
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains present in archaea, ...
 270-380 3.24e-04

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: 40.39  E-value: 3.24e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 328772605 270 ALAALRSlylHQVSAVAVVDTNGRLVANLSASDLrgVNF---SNLEMLLGSVFEflEAEKRTPNQLK---SDQLKSVEPG 343
Cdd:cd04632   16 AINLLRE---HGISRLPVVDDNGKLVGIVTTYDI--VDFvvrPGTKTRGGDRGG--EKERMLDLPVYdimSSPVVTVTRD 88

                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 328772605 344 SVVGEVGVSMMEHMIHHLWVVDDDDHPIGVVSMSDVL 380
Cdd:cd04632   89 ATVADAVERMLENDISGLVVTPDDNMVIGILTKTDVL 125
CBS pfam00571
CBS domain; CBS domains are small intracellular modules that pair together to form a stable ...
 33-85 3.50e-04

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


Pssm-ID: 425756 [Multi-domain]  Cd Length: 57  Bit Score: 38.35  E-value: 3.50e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 328772605   33 KKPLISVHQDTTLDNVLSIMHTSQILAIPVYkvpkdEPDGKVfTGIVSVFDIL 85
Cdd:pfam00571   6 TKDVVTVSPDTTLEEALELMREHGISRLPVV-----DEDGKL-VGIVTLKDLL 52
COG3448 COG3448
CBS-domain-containing membrane protein [Signal transduction mechanisms];
334-386 3.61e-04

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


Pssm-ID: 442671 [Multi-domain]  Cd Length: 136  Bit Score: 40.23  E-value: 3.61e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|...
gi 328772605 334 SDQLKSVEPGSVVGEVGVSMMEHMIHHLWVVDDDDHPIGVVSMSDVLALFVPE 386
Cdd:COG3448    9 TRDVVTVSPDTTLREALELMREHGIRGLPVVDEDGRLVGIVTERDLLRALLPD 61
YtoI COG4109
Predicted transcriptional regulator containing CBS domains [Transcription];
257-380 4.21e-04

Predicted transcriptional regulator containing CBS domains [Transcription];


Pssm-ID: 443285 [Multi-domain]  Cd Length: 135  Bit Score: 39.90  E-value: 4.21e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 328772605 257 TKKQLVCVESSMSALAALRSLYLHQVSAVAVVDTNGRLVANLSASDLRGVnfsnlemllgsvfefleaEKRTP-NQLKSD 335
Cdd:COG4109   23 TLEDVATLSEDDTVEDALELLEKTGHSRFPVVDENGRLVGIVTSKDILGK------------------DDDTPiEDVMTK 84

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 328772605 336 QLKSVEPGSVVGEVGVSMMEHMIHHLWVVDDDDHPIGVVSMSDVL 380
Cdd:COG4109   85 NPITVTPDTSLASAAHKMIWEGIELLPVVDDDGRLLGIISRQDVL 129
CBS COG0517
CBS domain [Signal transduction mechanisms];
334-389 6.49e-04

CBS domain [Signal transduction mechanisms];


Pssm-ID: 440283 [Multi-domain]  Cd Length: 128  Bit Score: 39.46  E-value: 6.49e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 328772605 334 SDQLKSVEPGSVVGEVGVSMMEHMIHHLWVVDDDDHPIGVVSMSDVLALFVPENGA 389
Cdd:COG0517    8 TTDVVTVSPDATVREALELMSEKRIGGLPVVDEDGKLVGIVTDRDLRRALAAEGKD 63
COG2524 COG2524
Predicted transcriptional regulator, contains C-terminal CBS domains [Transcription];
34-199 6.87e-04

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


Pssm-ID: 442013 [Multi-domain]  Cd Length: 206  Bit Score: 40.64  E-value: 6.87e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 328772605  34 KPLISVHQDTTLDNVLSIMHTSQILAIPVYkvpkdepDGKVFTGIVSVFDIlantvfqsvfddmsgnvknpitmskdefq 113
Cdd:COG2524   94 KDVITVSPDTTLEEALELMLEKGISGLPVV-------DDGKLVGIITERDL----------------------------- 137

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 328772605 114 qyIRMVKEEHAYFSTKIGELLgqtseSAESWTLHSSDPLTSLLQILTYANRHRALIIDDDVNLAtvappsGssirLVTQT 193
Cdd:COG2524  138 --LKALAEGRDLLDAPVSDIM-----TRDVVTVSEDDSLEEALRLMLEHGIGRLPVVDDDGKLV------G----IITRT 200


                 ....*.
gi 328772605 194 DLLRYL 199
Cdd:COG2524  201 DILRAL 206
CBS_pair_bac_euk cd04623
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains present in bacteria ...
 259-379 7.21e-04

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: 38.94  E-value: 7.21e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 328772605 259 KQLVCVESSMSALAALRSLYLHQVSAVAVVDTNGRLVANLSASD------LRGVnfSNLEMLLGSVFefleaekrtpnql 332
Cdd:cd04623    2 RDVVTVSPDATVAEALRLLAEKNIGALVVVDDGGRLVGILSERDyvrklaLRGA--SSLDTPVSEIM------------- 66

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 328772605 333 kSDQLKSVEPGSVVGEVGVSMMEHMIHHLWVVDDDdHPIGVVSMSDV 379
Cdd:cd04623   67 -TRDVVTCTPDDTVEECMALMTERRIRHLPVVEDG-KLVGIVSIGDV 111
COG2524 COG2524
Predicted transcriptional regulator, contains C-terminal CBS domains [Transcription];
270-380 8.33e-04

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


Pssm-ID: 442013 [Multi-domain]  Cd Length: 206  Bit Score: 40.25  E-value: 8.33e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 328772605 270 ALAALRSLYLHQVSAVAVVDTNGRLVANLSASDLRGVNFSNLEMLLGSVFEFLEAEKRTPNQLK-------SDQLKSVEP 342
Cdd:COG2524   22 ALLLLAALVLALTAAAAATVLLLAAAAAAAGAGGLGLLLLLLLIVLQAAAVRVVAEKELGLVLKmkvkdimTKDVITVSP 101

                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 328772605 343 GSVVGEVGVSMMEHMIHHLWVVdDDDHPIGVVSMSDVL 380
Cdd:COG2524  102 DTTLEEALELMLEKGISGLPVV-DDGKLVGIITERDLL 138
CBS_pair_bac cd04629
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains present in bacteria; ...
 259-381 8.61e-04

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: 38.57  E-value: 8.61e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 328772605 259 KQLVCVESSMSALAALRSLYLHQVSAVAVVDTNGRLVANLSASD-LRGvnfsnleMLLGSVFeflEAEKRTPNQLKSDQL 337
Cdd:cd04629    3 RNPVTLTPDTSILEAVELLLEHKISGAPVVDEQGRLVGFLSEQDcLKA-------LLEASYH---CEPGGTVADYMSTEV 72

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 328772605 338 KSVEPGSVVGEVGVSMMEHMIHHLWVVdDDDHPIGVVSMSDVLA 381
Cdd:cd04629   73 LTVSPDTSIVDLAQLFLKNKPRRYPVV-EDGKLVGQISRRDVLR 115
CBS pfam00571
CBS domain; CBS domains are small intracellular modules that pair together to form a stable ...
 258-304 1.01e-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: 36.81  E-value: 1.01e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*..
gi 328772605  258 KKQLVCVESSMSALAALRSLYLHQVSAVAVVDTNGRLVANLSASDLR 304
Cdd:pfam00571   6 TKDVVTVSPDTTLEEALELMREHGISRLPVVDEDGKLVGIVTLKDLL 52
COG2905 COG2905
Signal-transduction protein containing cAMP-binding, CBS, and nucleotidyltransferase domains ...
 331-380 2.35e-03

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


Pssm-ID: 442149 [Multi-domain]  Cd Length: 124  Bit Score: 37.50  E-value: 2.35e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|
gi 328772605 331 QLKSDQLKSVEPGSVVGEVGVSMMEHMIHHLWVVDDDDHPIGVVSMSDVL 380
Cdd:COG2905    3 DIMSRDVVTVSPDATVREAARLMTEKGVGSLVVVDDDGRLVGIITDRDLR 52
CBS_pair_arch1_repeat2 cd04632
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains present in archaea, ...
 339-380 3.42e-03

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: 37.31  E-value: 3.42e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|..
gi 328772605 339 SVEPGSVVGEVGVSMMEHMIHHLWVVDDDDHPIGVVSMSDVL 380
Cdd:cd04632    6 TVNEDDTIGKAINLLREHGISRLPVVDDNGKLVGIVTTYDIV 47
CBS_pair_SF cd02205
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains superfamily; The CBS ...
 334-387 4.23e-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: 36.84  E-value: 4.23e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....
gi 328772605 334 SDQLKSVEPGSVVGEVGVSMMEHMIHHLWVVDDDDHPIGVVSMSDVLALFVPEN 387
Cdd:cd02205    1 TRDVVTVDPDTTVREALELMAENGIGALPVVDDDGKLVGIVTERDILRALVEGG 54
CBS_pair_SF cd02205
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains superfamily; The CBS ...
 17-86 4.94e-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: 36.45  E-value: 4.94e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 328772605  17 LSHIPISQVLNhahgskKPLISVHQDTTLDNVLSIMHTSQILAIPVYKvpkdepDGKVFTGIVSVFDILA 86
Cdd:cd02205   56 ALDTPVAEVMT------PDVITVSPDTDLEEALELMLEHGIRRLPVVD------DDGKLVGIVTRRDILR 113
CBS_pair_BON_assoc cd04586
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with the ...
 339-381 5.47e-03

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: 37.02  E-value: 5.47e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|...
gi 328772605 339 SVEPGSVVGEVGVSMMEHMIHHLWVVDDDDHPIGVVSMSDVLA 381
Cdd:cd04586    7 TVTPDTSVREAARLLLEHRISGLPVVDDDGKLVGIVSEGDLLR 49
COG2524 COG2524
Predicted transcriptional regulator, contains C-terminal CBS domains [Transcription];
17-85 5.69e-03

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


Pssm-ID: 442013 [Multi-domain]  Cd Length: 206  Bit Score: 37.94  E-value: 5.69e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 328772605  17 LSHIPISQVLNhahgskKPLISVHQDTTLDNVLSIMHTSQILAIPVykVpkdEPDGKVfTGIVSVFDIL 85
Cdd:COG2524  147 LLDAPVSDIMT------RDVVTVSEDDSLEEALRLMLEHGIGRLPV--V---DDDGKL-VGIITRTDIL 203
COG3448 COG3448
CBS-domain-containing membrane protein [Signal transduction mechanisms];
13-86 7.22e-03

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


Pssm-ID: 442671 [Multi-domain]  Cd Length: 136  Bit Score: 36.38  E-value: 7.22e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 328772605  13 IYAHLSHIPISQVLNhahgskKPLISVHQDTTLDNVLSIMHTSQILAIPVykVpkdEPDGKVfTGIVSVFDILA 86
Cdd:COG3448   66 LEERLLDLPVEDVMT------RPVVTVTPDTPLEEAAELMLEHGIHRLPV--V---DDDGRL-VGIVTRTDLLR 127
CBS smart00116
Domain in cystathionine beta-synthase and other proteins; Domain present in all 3 forms of ...
 261-303 9.95e-03

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: 34.03  E-value: 9.95e-03
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|...
gi 328772605   261 LVCVESSMSALAALRSLYLHQVSAVAVVDTNGRLVANLSASDL 303
Cdd:smart00116   2 VVTVSPDTTLEEALELLRENGIRRLPVVDEEGRLVGIVTRRDI 44
 
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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