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Conserved domains on  [gi|1002253483|ref|XP_015630980|]
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sucrose nonfermenting 4-like protein [Oryza sativa Japonica Group]

Protein Classification

E_set_AMPKbeta_like_N and CBS_pair_SF domain-containing protein( domain architecture ID 11244020)

protein containing domains E_set_AMPKbeta_like_N, and CBS_pair_SF

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
CBS_pair_SF super family cl15354
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains superfamily; The CBS ...
 169-317 5.75e-42

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 cd04618:

Pssm-ID: 449531 [Multi-domain]  Cd Length: 138  Bit Score: 146.16  E-value: 5.75e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002253483 169 TGYDLLPDSGKVIALDVNLPVKQSFHILHEQGIPVAPLWDSFRGQFVGLLSPLDFILILRELETHGSnLTEEQLETHTIS 248
Cdd:cd04618     1 TCYDLLPTSSKLVVLDTKLPVKKAFFALVQNGIRSAPLWDSEKQDFVGMLTITDFINILQYYYKSPS-VQMEELEEHTIE 79

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1002253483 249 AWKEAKRQTYARnegswranhHLVHATPYESLREIAMKILQNGVSTVPIMfSSSPDGSYPQLLHLASLS 317
Cdd:cd04618    80 TWREIERQIGVP---------PLVSVHPEDSLYDAALLLLQNKIHRLPVI-DPLTGNVLSVLTHKRILK 138
CBS_pair_SF super family cl15354
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains superfamily; The CBS ...
 359-492 1.22e-41

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 cd04641:

Pssm-ID: 449531 [Multi-domain]  Cd Length: 124  Bit Score: 144.58  E-value: 1.22e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002253483 359 RPLAMLRPNTSLSAALNLLVQAGVSSIPIVDDNDSLLDTYSRSDITALAKDKVYTHirLDeMTIHQALQLGQDanspfgf 438
Cdd:cd04641     3 ENIATASMDTPVIDALNLFVERRVSALPIVDEDGRVVDIYAKFDVINLAAEKTYNN--LD-LTVGEALQHRSE------- 72

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1002253483 439 fNGQRCQMCLRSDTLLKVMERLANPGVRRVFIVEAgSKRVEGIISLSDIFKFLL 492
Cdd:cd04641    73 -DFEGVHTCTLNDTLETIIDRIVKAEVHRLVVVDE-EDRLEGIVSLSDILKYLV 124
AMPK1_CBM pfam16561
Glycogen recognition site of AMP-activated protein kinase; AMPK1_CBM is a family found in ...
 22-107 1.31e-37

Glycogen recognition site of AMP-activated protein kinase; AMPK1_CBM is a family found in close association with AMPKBI pfam04739. The surface of AMPK1_CBM reveals a carbohydrate-binding pocket.


:

Pssm-ID: 465176 [Multi-domain]  Cd Length: 85  Bit Score: 132.65  E-value: 1.31e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002253483  22 VPTRFVWPYGGKRVYLTGSFTRWTEHLPMSPvegCPTVFQAICSLSPGIHQYKFCVDGEWRHDERQPTITGDYGVVNTLC 101
Cdd:pfam16561   1 VPTVITWRGGGKKVYVTGSFDNWKKKIPLQK---SGGDFTTILDLPPGTHQYKFIVDGEWRHDPDLPTATDDMGNLNNYI 77


                  ....*.
gi 1002253483 102 LTRDFD 107
Cdd:pfam16561  78 EVKASD 83
 
Name Accession Description Interval E-value
CBS_euAMPK_gamma-like_repeat1 cd04618
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains found in ...
 169-317 5.75e-42

Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains found in AMP-activated protein kinase gamma-like proteins, repeat 1; AMP-activated protein kinase (AMPK) plays multiple roles in the body's overall metabolic balance and response to exercise, nutritional stress, hormonal stimulation, and the glucose-lowering drugs metformin and rosiglitazone. AMPK consists of a catalytic alpha subunit and two non-catalytic subunits, beta and gamma, each with multiple isoforms that form active 1:1:1 heterotrimers. This cd contains 2 tandem repeats of the CBS domains found in the gamma subunits of AMPK. 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: 341388 [Multi-domain]  Cd Length: 138  Bit Score: 146.16  E-value: 5.75e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002253483 169 TGYDLLPDSGKVIALDVNLPVKQSFHILHEQGIPVAPLWDSFRGQFVGLLSPLDFILILRELETHGSnLTEEQLETHTIS 248
Cdd:cd04618     1 TCYDLLPTSSKLVVLDTKLPVKKAFFALVQNGIRSAPLWDSEKQDFVGMLTITDFINILQYYYKSPS-VQMEELEEHTIE 79

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1002253483 249 AWKEAKRQTYARnegswranhHLVHATPYESLREIAMKILQNGVSTVPIMfSSSPDGSYPQLLHLASLS 317
Cdd:cd04618    80 TWREIERQIGVP---------PLVSVHPEDSLYDAALLLLQNKIHRLPVI-DPLTGNVLSVLTHKRILK 138
CBS_euAMPK_gamma-like_repeat2 cd04641
CBS pair domain found in 5'-AMP (adenosine monophosphate)-activated protein kinase; The 5'-AMP ...
 359-492 1.22e-41

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: 144.58  E-value: 1.22e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002253483 359 RPLAMLRPNTSLSAALNLLVQAGVSSIPIVDDNDSLLDTYSRSDITALAKDKVYTHirLDeMTIHQALQLGQDanspfgf 438
Cdd:cd04641     3 ENIATASMDTPVIDALNLFVERRVSALPIVDEDGRVVDIYAKFDVINLAAEKTYNN--LD-LTVGEALQHRSE------- 72

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1002253483 439 fNGQRCQMCLRSDTLLKVMERLANPGVRRVFIVEAgSKRVEGIISLSDIFKFLL 492
Cdd:cd04641    73 -DFEGVHTCTLNDTLETIIDRIVKAEVHRLVVVDE-EDRLEGIVSLSDILKYLV 124
AMPK1_CBM pfam16561
Glycogen recognition site of AMP-activated protein kinase; AMPK1_CBM is a family found in ...
 22-107 1.31e-37

Glycogen recognition site of AMP-activated protein kinase; AMPK1_CBM is a family found in close association with AMPKBI pfam04739. The surface of AMPK1_CBM reveals a carbohydrate-binding pocket.


Pssm-ID: 465176 [Multi-domain]  Cd Length: 85  Bit Score: 132.65  E-value: 1.31e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002253483  22 VPTRFVWPYGGKRVYLTGSFTRWTEHLPMSPvegCPTVFQAICSLSPGIHQYKFCVDGEWRHDERQPTITGDYGVVNTLC 101
Cdd:pfam16561   1 VPTVITWRGGGKKVYVTGSFDNWKKKIPLQK---SGGDFTTILDLPPGTHQYKFIVDGEWRHDPDLPTATDDMGNLNNYI 77


                  ....*.
gi 1002253483 102 LTRDFD 107
Cdd:pfam16561  78 EVKASD 83
E_set_AMPKbeta_like_N cd02859
N-terminal Early set domain, a glycogen binding domain, associated with the catalytic domain ...
 23-98 4.29e-28

N-terminal Early set domain, a glycogen binding domain, associated with the catalytic domain of AMP-activated protein kinase beta subunit; E or "early" set domains are associated with the catalytic domain of AMP-activated protein kinase beta subunit glycogen binding domain at the N-terminal end. AMPK is a metabolic stress sensing protein that senses AMP/ATP and has recently been found to act as a glycogen sensor as well. The protein functions as an alpha-beta-gamma heterotrimer. This N-terminal domain is the glycogen binding domain of the beta subunit. This domain is also a member of the CBM48 (Carbohydrate Binding Module 48) family whose members include pullulanase, maltooligosyl trehalose synthase, starch branching enzyme, glycogen branching enzyme, glycogen debranching enzyme, and isoamylase.


Pssm-ID: 199889 [Multi-domain]  Cd Length: 80  Bit Score: 106.53  E-value: 4.29e-28
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1002253483  23 PTRFVWPY-GGKRVYLTGSFTRWTEHLPMSPVEGcpTVFQAICSLSPGIHQYKFCVDGEWRHDERQPTITGDYGVVN 98
Cdd:cd02859     1 PVTFRWPGpGGKEVYVTGSFDNWQQPIPLEKSGD--GEFSATVELPPGRYEYKFIVDGEWVHDPDLPTVTDEFGNLN 75
CBS COG0517
CBS domain [Signal transduction mechanisms];
352-492 5.92e-11

CBS domain [Signal transduction mechanisms];


Pssm-ID: 440283 [Multi-domain]  Cd Length: 128  Bit Score: 59.88  E-value: 5.92e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002253483 352 KIGDPNGRPLAMLRPNTSLSAALNLLVQAGVSSIPIVDDNDSLLDTYSRSDI--TALAKDKVYTHIRLDE-MTihqalql 428
Cdd:COG0517     2 KVKDIMTTDVVTVSPDATVREALELMSEKRIGGLPVVDEDGKLVGIVTDRDLrrALAAEGKDLLDTPVSEvMT------- 74

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1002253483 429 gqdanspfgffngQRCQMCLRSDTLLKVMERLANPGVRRVFIVEaGSKRVEGIISLSDIFKFLL 492
Cdd:COG0517    75 -------------RPPVTVSPDTSLEEAAELMEEHKIRRLPVVD-DDGRLVGIITIKDLLKALL 124
CBS smart00116
Domain in cystathionine beta-synthase and other proteins; Domain present in all 3 forms of ...
 360-403 3.72e-08

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: 49.43  E-value: 3.72e-08
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....
gi 1002253483  360 PLAMLRPNTSLSAALNLLVQAGVSSIPIVDDNDSLLDTYSRSDI 403
Cdd:smart00116   1 DVVTVSPDTTLEEALELLRENGIRRLPVVDEEGRLVGIVTRRDI 44
CBS pfam00571
CBS domain; CBS domains are small intracellular modules that pair together to form a stable ...
 359-403 2.07e-06

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


Pssm-ID: 425756 [Multi-domain]  Cd Length: 57  Bit Score: 44.90  E-value: 2.07e-06
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 1002253483 359 RPLAMLRPNTSLSAALNLLVQAGVSSIPIVDDNDSLLDTYSRSDI 403
Cdd:pfam00571   7 KDVVTVSPDTTLEEALELMREHGISRLPVVDEDGKLVGIVTLKDL 51
COG2524 COG2524
Predicted transcriptional regulator, contains C-terminal CBS domains [Transcription];
268-403 1.16e-05

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


Pssm-ID: 442013 [Multi-domain]  Cd Length: 206  Bit Score: 46.42  E-value: 1.16e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002253483 268 NHHLVHATPYESLREIAMKILQNGVSTVPIMfssspDGSypQLLHLASLSGILKCIcryfknsQGNLPILSQPVCTIPLg 347
Cdd:COG2524    93 TKDVITVSPDTTLEEALELMLEKGISGLPVV-----DDG--KLVGIITERDLLKAL-------AEGRDLLDAPVSDIMT- 157

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1002253483 348 twvpkigdpngRPLAMLRPNTSLSAALNLLVQAGVSSIPIVDDNDSLLDTYSRSDI 403
Cdd:COG2524   158 -----------RDVVTVSEDDSLEEALRLMLEHGIGRLPVVDDDGKLVGIITRTDI 202
PRK14869 PRK14869
putative manganese-dependent inorganic diphosphatase;
351-404 2.64e-04

putative manganese-dependent inorganic diphosphatase;


Pssm-ID: 237843 [Multi-domain]  Cd Length: 546  Bit Score: 43.67  E-value: 2.64e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1002253483 351 PKIGDPNGRPLAMLRPNTSLSAALNLLVQAGVSSIPIVDDNDSLLDTYSRSDIT 404
Cdd:PRK14869   68 PQVRDLEIDKPVTVSPDTSLKEAWNLMDENNVKTLPVVDEEGKLLGLVSLSDLA 121
 
Name Accession Description Interval E-value
CBS_euAMPK_gamma-like_repeat1 cd04618
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains found in ...
 169-317 5.75e-42

Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains found in AMP-activated protein kinase gamma-like proteins, repeat 1; AMP-activated protein kinase (AMPK) plays multiple roles in the body's overall metabolic balance and response to exercise, nutritional stress, hormonal stimulation, and the glucose-lowering drugs metformin and rosiglitazone. AMPK consists of a catalytic alpha subunit and two non-catalytic subunits, beta and gamma, each with multiple isoforms that form active 1:1:1 heterotrimers. This cd contains 2 tandem repeats of the CBS domains found in the gamma subunits of AMPK. 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: 341388 [Multi-domain]  Cd Length: 138  Bit Score: 146.16  E-value: 5.75e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002253483 169 TGYDLLPDSGKVIALDVNLPVKQSFHILHEQGIPVAPLWDSFRGQFVGLLSPLDFILILRELETHGSnLTEEQLETHTIS 248
Cdd:cd04618     1 TCYDLLPTSSKLVVLDTKLPVKKAFFALVQNGIRSAPLWDSEKQDFVGMLTITDFINILQYYYKSPS-VQMEELEEHTIE 79

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1002253483 249 AWKEAKRQTYARnegswranhHLVHATPYESLREIAMKILQNGVSTVPIMfSSSPDGSYPQLLHLASLS 317
Cdd:cd04618    80 TWREIERQIGVP---------PLVSVHPEDSLYDAALLLLQNKIHRLPVI-DPLTGNVLSVLTHKRILK 138
CBS_euAMPK_gamma-like_repeat2 cd04641
CBS pair domain found in 5'-AMP (adenosine monophosphate)-activated protein kinase; The 5'-AMP ...
 359-492 1.22e-41

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: 144.58  E-value: 1.22e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002253483 359 RPLAMLRPNTSLSAALNLLVQAGVSSIPIVDDNDSLLDTYSRSDITALAKDKVYTHirLDeMTIHQALQLGQDanspfgf 438
Cdd:cd04641     3 ENIATASMDTPVIDALNLFVERRVSALPIVDEDGRVVDIYAKFDVINLAAEKTYNN--LD-LTVGEALQHRSE------- 72

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1002253483 439 fNGQRCQMCLRSDTLLKVMERLANPGVRRVFIVEAgSKRVEGIISLSDIFKFLL 492
Cdd:cd04641    73 -DFEGVHTCTLNDTLETIIDRIVKAEVHRLVVVDE-EDRLEGIVSLSDILKYLV 124
AMPK1_CBM pfam16561
Glycogen recognition site of AMP-activated protein kinase; AMPK1_CBM is a family found in ...
 22-107 1.31e-37

Glycogen recognition site of AMP-activated protein kinase; AMPK1_CBM is a family found in close association with AMPKBI pfam04739. The surface of AMPK1_CBM reveals a carbohydrate-binding pocket.


Pssm-ID: 465176 [Multi-domain]  Cd Length: 85  Bit Score: 132.65  E-value: 1.31e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002253483  22 VPTRFVWPYGGKRVYLTGSFTRWTEHLPMSPvegCPTVFQAICSLSPGIHQYKFCVDGEWRHDERQPTITGDYGVVNTLC 101
Cdd:pfam16561   1 VPTVITWRGGGKKVYVTGSFDNWKKKIPLQK---SGGDFTTILDLPPGTHQYKFIVDGEWRHDPDLPTATDDMGNLNNYI 77


                  ....*.
gi 1002253483 102 LTRDFD 107
Cdd:pfam16561  78 EVKASD 83
E_set_AMPKbeta_like_N cd02859
N-terminal Early set domain, a glycogen binding domain, associated with the catalytic domain ...
 23-98 4.29e-28

N-terminal Early set domain, a glycogen binding domain, associated with the catalytic domain of AMP-activated protein kinase beta subunit; E or "early" set domains are associated with the catalytic domain of AMP-activated protein kinase beta subunit glycogen binding domain at the N-terminal end. AMPK is a metabolic stress sensing protein that senses AMP/ATP and has recently been found to act as a glycogen sensor as well. The protein functions as an alpha-beta-gamma heterotrimer. This N-terminal domain is the glycogen binding domain of the beta subunit. This domain is also a member of the CBM48 (Carbohydrate Binding Module 48) family whose members include pullulanase, maltooligosyl trehalose synthase, starch branching enzyme, glycogen branching enzyme, glycogen debranching enzyme, and isoamylase.


Pssm-ID: 199889 [Multi-domain]  Cd Length: 80  Bit Score: 106.53  E-value: 4.29e-28
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1002253483  23 PTRFVWPY-GGKRVYLTGSFTRWTEHLPMSPVEGcpTVFQAICSLSPGIHQYKFCVDGEWRHDERQPTITGDYGVVN 98
Cdd:cd02859     1 PVTFRWPGpGGKEVYVTGSFDNWQQPIPLEKSGD--GEFSATVELPPGRYEYKFIVDGEWVHDPDLPTVTDEFGNLN 75
CBS_pair_SF cd02205
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains superfamily; The CBS ...
 359-489 3.13e-12

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: 63.03  E-value: 3.13e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002253483 359 RPLAMLRPNTSLSAALNLLVQAGVSSIPIVDDNDSLLDTYSRSDI-TALAKDKVYTHIRLDEMTIHQALQLGQDanspfg 437
Cdd:cd02205     2 RDVVTVDPDTTVREALELMAENGIGALPVVDDDGKLVGIVTERDIlRALVEGGLALDTPVAEVMTPDVITVSPD------ 75

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1002253483 438 ffngqrcqmclrsDTLLKVMERLANPGVRRVFIVEaGSKRVEGIISLSDIFK 489
Cdd:cd02205    76 -------------TDLEEALELMLEHGIRRLPVVD-DDGKLVGIVTRRDILR 113
CBS COG0517
CBS domain [Signal transduction mechanisms];
352-492 5.92e-11

CBS domain [Signal transduction mechanisms];


Pssm-ID: 440283 [Multi-domain]  Cd Length: 128  Bit Score: 59.88  E-value: 5.92e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002253483 352 KIGDPNGRPLAMLRPNTSLSAALNLLVQAGVSSIPIVDDNDSLLDTYSRSDI--TALAKDKVYTHIRLDE-MTihqalql 428
Cdd:COG0517     2 KVKDIMTTDVVTVSPDATVREALELMSEKRIGGLPVVDEDGKLVGIVTDRDLrrALAAEGKDLLDTPVSEvMT------- 74

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1002253483 429 gqdanspfgffngQRCQMCLRSDTLLKVMERLANPGVRRVFIVEaGSKRVEGIISLSDIFKFLL 492
Cdd:COG0517    75 -------------RPPVTVSPDTSLEEAAELMEEHKIRRLPVVD-DDGRLVGIITIKDLLKALL 124
COG2905 COG2905
Signal-transduction protein containing cAMP-binding, CBS, and nucleotidyltransferase domains ...
 359-493 1.36e-10

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


Pssm-ID: 442149 [Multi-domain]  Cd Length: 124  Bit Score: 58.69  E-value: 1.36e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002253483 359 RPLAMLRPNTSLSAALNLLVQAGVSSIPIVDDNDSLLDTYSRSDI--TALAKDKVYTHIRLDE-MTihqalqlgqdansp 435
Cdd:COG2905     7 RDVVTVSPDATVREAARLMTEKGVGSLVVVDDDGRLVGIITDRDLrrRVLAEGLDPLDTPVSEvMT-------------- 72

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1002253483 436 fgffngQRCQMCLRSDTLLKVMERLANPGVRRVFIVEAGskRVEGIISLSDIFKFLLS 493
Cdd:COG2905    73 ------RPPITVSPDDSLAEALELMEEHRIRHLPVVDDG--KLVGIVSITDLLRALSE 122
COG3448 COG3448
CBS-domain-containing membrane protein [Signal transduction mechanisms];
359-492 2.12e-10

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


Pssm-ID: 442671 [Multi-domain]  Cd Length: 136  Bit Score: 58.72  E-value: 2.12e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002253483 359 RPLAMLRPNTSLSAALNLLVQAGVSSIPIVDDNDSLLDTYSRSDITALAKDKVYTHI--RLDEMTIHQALQlgqdanspf 436
Cdd:COG3448    10 RDVVTVSPDTTLREALELMREHGIRGLPVVDEDGRLVGIVTERDLLRALLPDRLDELeeRLLDLPVEDVMT--------- 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1002253483 437 gffngQRCQMCLRSDTLLKVMERLANPGVRRVFIVEaGSKRVEGIISLSDIFKFLL 492
Cdd:COG3448    81 -----RPVVTVTPDTPLEEAAELMLEHGIHRLPVVD-DDGRLVGIVTRTDLLRALA 130
COG2524 COG2524
Predicted transcriptional regulator, contains C-terminal CBS domains [Transcription];
352-491 5.63e-09

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


Pssm-ID: 442013 [Multi-domain]  Cd Length: 206  Bit Score: 56.05  E-value: 5.63e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002253483 352 KIGDPNGRPLAMLRPNTSLSAALNLLVQAGVSSIPIVDDNDsLLDTYSRSDI-TALAKDKVYTHIRLDE-M-----TIHQ 424
Cdd:COG2524    87 KVKDIMTKDVITVSPDTTLEEALELMLEKGISGLPVVDDGK-LVGIITERDLlKALAEGRDLLDAPVSDiMtrdvvTVSE 165

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1002253483 425 alqlgqdanspfgffngqrcqmclrSDTLLKVMERLANPGVRRVFIVEAgSKRVEGIISLSDIFKFL 491
Cdd:COG2524   166 -------------------------DDSLEEALRLMLEHGIGRLPVVDD-DGKLVGIITRTDILRAL 206
CBS smart00116
Domain in cystathionine beta-synthase and other proteins; Domain present in all 3 forms of ...
 360-403 3.72e-08

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: 49.43  E-value: 3.72e-08
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....
gi 1002253483  360 PLAMLRPNTSLSAALNLLVQAGVSSIPIVDDNDSLLDTYSRSDI 403
Cdd:smart00116   1 DVVTVSPDTTLEEALELLRENGIRRLPVVDEEGRLVGIVTRRDI 44
E_set cd02688
Early set domain associated with the catalytic domain of sugar utilizing enzymes at either the ...
 23-97 8.04e-07

Early set domain associated with the catalytic domain of sugar utilizing enzymes at either the N or C terminus; The E or "early" set domains of sugar utilizing enzymes are associated with different types of catalytic domains at either the N-terminal or C-terminal end. These domains may be related to the immunoglobulin and/or fibronectin type III superfamilies. Members of this family include alpha amylase, sialidase, galactose oxidase, cellulase, cellulose, hyaluronate lyase, chitobiase, and chitinase. A subset of these members were recently identified as members of the CBM48 (Carbohydrate Binding Module 48) family. Members of the CBM48 family include pullulanase, maltooligosyl trehalose synthase, starch branching enzyme, glycogen branching enzyme, glycogen debranching enzyme, isoamylase, and the beta subunit of AMP-activated protein kinase.


Pssm-ID: 199878 [Multi-domain]  Cd Length: 82  Bit Score: 46.77  E-value: 8.04e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002253483  23 PTRF-VWPYGGKRVYLTGSFTRWTEHLPMSPVEGCPTVFQAICSLSPGIHQYKFCVDGEWRHDER------QPTITGDYG 95
Cdd:cd02688     1 GVTFrIFAPGAKSVYLIGSFNGWWQAQALPMTKNGGGVWSATIPLPLGTYEYKYVIDGGKNVLPYfdpyyvAGDGNSGAS 80


                  ..
gi 1002253483  96 VV 97
Cdd:cd02688    81 IV 82
CBS pfam00571
CBS domain; CBS domains are small intracellular modules that pair together to form a stable ...
 359-403 2.07e-06

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


Pssm-ID: 425756 [Multi-domain]  Cd Length: 57  Bit Score: 44.90  E-value: 2.07e-06
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 1002253483 359 RPLAMLRPNTSLSAALNLLVQAGVSSIPIVDDNDSLLDTYSRSDI 403
Cdd:pfam00571   7 KDVVTVSPDTTLEEALELMREHGISRLPVVDEDGKLVGIVTLKDL 51
COG2524 COG2524
Predicted transcriptional regulator, contains C-terminal CBS domains [Transcription];
268-403 1.16e-05

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


Pssm-ID: 442013 [Multi-domain]  Cd Length: 206  Bit Score: 46.42  E-value: 1.16e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002253483 268 NHHLVHATPYESLREIAMKILQNGVSTVPIMfssspDGSypQLLHLASLSGILKCIcryfknsQGNLPILSQPVCTIPLg 347
Cdd:COG2524    93 TKDVITVSPDTTLEEALELMLEKGISGLPVV-----DDG--KLVGIITERDLLKAL-------AEGRDLLDAPVSDIMT- 157

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1002253483 348 twvpkigdpngRPLAMLRPNTSLSAALNLLVQAGVSSIPIVDDNDSLLDTYSRSDI 403
Cdd:COG2524   158 -----------RDVVTVSEDDSLEEALRLMLEHGIGRLPVVDDDGKLVGIITRTDI 202
CBS_pair_BON_assoc cd04586
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with the ...
 365-487 3.43e-05

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: 43.57  E-value: 3.43e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002253483 365 RPNTSLSAALNLLVQAGVSSIPIVDDNDSLLDTYSRSDITA-LAKDKVYTHIRLDEMTIHQALQLGQDANSpfgfFNGQR 443
Cdd:cd04586     9 TPDTSVREAARLLLEHRISGLPVVDDDGKLVGIVSEGDLLRrEEPGTEPRRVWWLDALLESPERLAEEYVK----AHGRT 84

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1002253483 444 CQ--M------CLRSDTLLKVMERLANPGVRRVFIVEAGskRVEGIISLSDI 487
Cdd:cd04586    85 VGdvMtrpvvtVSPDTPLEEAARLMERHRIKRLPVVDDG--KLVGIVSRADL 134
CBS pfam00571
CBS domain; CBS domains are small intracellular modules that pair together to form a stable ...
 450-493 3.97e-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: 41.04  E-value: 3.97e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....
gi 1002253483 450 SDTLLKVMERLANPGVRRVFIVEaGSKRVEGIISLSDIFKFLLS 493
Cdd:pfam00571  15 DTTLEEALELMREHGISRLPVVD-EDGKLVGIVTLKDLLRALLG 57
CBS_pair_HRP1_like cd04622
CBS pair domain found in Hypoxic Response Protein 1 (HRP1) -like proteinds; Mycobacterium ...
 359-487 6.70e-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: 42.41  E-value: 6.70e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002253483 359 RPLAMLRPNTSLSAALNLLVQAGVSSIPIVdDNDSLLDTYSRSDIT--ALAKDKvythiRLDEMTIHQALQlgqdanspf 436
Cdd:cd04622     3 RDVVTVSPDTTLREAARLMRDLDIGALPVC-EGDRLVGMVTDRDIVvrAVAEGK-----DPNTTTVREVMT--------- 67

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1002253483 437 gffngQRCQMCLRSDTLLKVMERLANPGVRRVFIVEaGSKRVEGIISLSDI 487
Cdd:cd04622    68 -----GDVVTCSPDDDVEEAARLMAEHQVRRLPVVD-DDGRLVGIVSLGDL 112
CBS_archAMPK_gamma-repeat1 cd17779
signal transduction protein with CBS domains; Archeal gamma-subunit of 5'-AMP-activated ...
 452-491 7.95e-05

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


Pssm-ID: 341415 [Multi-domain]  Cd Length: 136  Bit Score: 42.60  E-value: 7.95e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|
gi 1002253483 452 TLLKVMERLANPGVRRVFIVEAGSKRVEGIISLSDIFKFL 491
Cdd:cd17779    18 TIIGAIKTMTEKGFRRLPVADAGTKRLEGIVTSMDIVDFL 57
YtoI COG4109
Predicted transcriptional regulator containing CBS domains [Transcription];
352-403 9.09e-05

Predicted transcriptional regulator containing CBS domains [Transcription];


Pssm-ID: 443285 [Multi-domain]  Cd Length: 135  Bit Score: 42.21  E-value: 9.09e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1002253483 352 KIGDPNGRPLAMLRPNTSLSAALNLLVQAGVSSIPIVDDNDSLLDTYSRSDI 403
Cdd:COG4109    77 PIEDVMTKNPITVTPDTSLASAAHKMIWEGIELLPVVDDDGRLLGIISRQDV 128
PRK14869 PRK14869
putative manganese-dependent inorganic diphosphatase;
351-404 2.64e-04

putative manganese-dependent inorganic diphosphatase;


Pssm-ID: 237843 [Multi-domain]  Cd Length: 546  Bit Score: 43.67  E-value: 2.64e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1002253483 351 PKIGDPNGRPLAMLRPNTSLSAALNLLVQAGVSSIPIVDDNDSLLDTYSRSDIT 404
Cdd:PRK14869   68 PQVRDLEIDKPVTVSPDTSLKEAWNLMDENNVKTLPVVDEEGKLLGLVSLSDLA 121
E_set_Isoamylase_like_N cd07184
N-terminal Early set domain associated with the catalytic domain of isoamylase-like (also ...
 22-99 5.67e-04

N-terminal Early set domain associated with the catalytic domain of isoamylase-like (also called glycogen 6-glucanohydrolase) proteins; E or "early" set domains are associated with the catalytic domain of isoamylase-like proteins at the N-terminal end. Isoamylase is one of the starch-debranching enzymes that catalyze the hydrolysis of alpha-1,6-glucosidic linkages specific in alpha-glucans such as amylopectin or glycogen. Isoamylase contains a bound calcium ion, but this is not in the same position as the conserved calcium ion that has been reported in other alpha-amylase family enzymes. The N-terminal domain of isoamylase may be related to the immunoglobulin and/or fibronectin type III superfamilies. These domains are associated with different types of catalytic domains at either the N-terminal or C-terminal end and may be involved in homodimeric/tetrameric/dodecameric interactions. Members of this family include members of the alpha amylase family, sialidase, galactose oxidase, cellulase, cellulose, hyaluronate lyase, chitobiase, and chitinase. This domain is also a member of the CBM48 (Carbohydrate Binding Module 48) family whose members include pullulanase, maltooligosyl trehalose synthase, starch branching enzyme, glycogen branching enzyme, glycogen debranching enzyme, and the beta subunit of AMP-activated protein kinase.


Pssm-ID: 199892 [Multi-domain]  Cd Length: 86  Bit Score: 38.76  E-value: 5.67e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002253483  22 VPTRFVWP--YGGKRVYLTGSFTRWTEH-LPMSPVEGcpTVFQAICSLSPG-IHQYKFCVDGE-----WRHDERQPTITG 92
Cdd:cd07184     1 CKVTFELPaeQGADSVSLVGDFNDWDPQaTPMKKLKN--GTFSATLDLPAGrEYQFRYLIDGErwvndPEADAYAPNGFG 78


                  ....*...
gi 1002253483  93 -DYGVVNT 99
Cdd:cd07184    79 eENSVVSV 86
CBS_pair_plant_CBSX cd17789
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains from plant CBSX ...
 365-406 5.85e-04

Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains from plant CBSX proteins; This cd contains two tandem repeats of the cystathionine beta-synthase (CBS pair) domains of plant single cystathionine beta-synthase (CBS) pair proteins (CBSX). CBSX1 and CBSX2 have been identified as redox regulators of the thioredoxin (Trx) system. The CBS domain, named after human CBS, is a small domain originally identified in cystathionine beta-synthase and is subsequently found in a wide range of different proteins. CBS domains usually occur in tandem repeats. They associate to form a so-called Bateman domain or a CBS pair based on crystallographic studies in bacteria. The CBS pair was used as a basis for this cd hierarchy since the human CBS proteins can adopt the typical core structure and form an intramolecular CBS pair. The interface between the two CBS domains forms a cleft that is a potential ligand binding site. The CBS pair coexists with a variety of other functional domains and this has been used to help in its classification here. It has been proposed that the CBS domain may play a regulatory role, although its exact function is unknown. Mutations of conserved residues within this domain are associated with a variety of human hereditary diseases, including congenital myotonia, idiopathic generalized epilepsy, hypercalciuric nephrolithiasis, and classic Bartter syndrome (CLC chloride channel family members), Wolff-Parkinson-White syndrome (gamma 2 subunit of AMP-activated protein kinase), retinitis pigmentosa (IMP dehydrogenase-1), and homocystinuria (cystathionine beta-synthase).


Pssm-ID: 341425 [Multi-domain]  Cd Length: 141  Bit Score: 40.15  E-value: 5.85e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 1002253483 365 RPNTSLSAALNLLVQAGVSSIPIVDDNDSLLDTYSRSDITAL 406
Cdd:cd17789     9 KPNTTVDEALELLVENRITGLPVIDEDWRLVGVVSDYDLLAL 50
CBS_pair_archHTH_assoc cd04588
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains found in archaea and ...
 359-489 8.87e-04

Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains found in archaea and associated with helix turn helix domain; This cd contains two tandem repeats of the cystathionine beta-synthase (CBS pair) domains in the inosine 5' monophosphate dehydrogenase (IMPDH) protein. IMPDH is an essential enzyme that catalyzes the first step unique to GTP synthesis, playing a key role in the regulation of cell proliferation and differentiation. The CBS domain, named after human CBS, is a small domain originally identified in cystathionine beta-synthase and is subsequently found in a wide range of different proteins. CBS domains usually occur in tandem repeats. They associate to form a so-called Bateman domain or a CBS pair based on crystallographic studies in bacteria. The CBS pair was used as a basis for this cd hierarchy since the human CBS proteins can adopt the typical core structure and form an intramolecular CBS pair. The interface between the two CBS domains forms a cleft that is a potential ligand binding site. The CBS pair coexists with a variety of other functional domains and this has been used to help in its classification here. It has been proposed that the CBS domain may play a regulatory role, although its exact function is unknown. Mutations of conserved residues within this domain are associated with a variety of human hereditary diseases, including congenital myotonia, idiopathic generalized epilepsy, hypercalciuric nephrolithiasis, and classic Bartter syndrome (CLC chloride channel family members), Wolff-Parkinson-White syndrome (gamma 2 subunit of AMP-activated protein kinase), retinitis pigmentosa (IMP dehydrogenase-1), and homocystinuria (cystathionine beta-synthase).


Pssm-ID: 341364 [Multi-domain]  Cd Length: 111  Bit Score: 39.05  E-value: 8.87e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002253483 359 RPLAMLRPNTSLSAALNLLVQAGVSSIPIVDDnDSLLDTYSRSDIT-ALAKDKVYTHIRlDEM-----TIHQALQLgQDA 432
Cdd:cd04588     2 KDLITLKPDATIKDAAKLLSENNIHGAPVVDD-GKLVGIVTLTDIAkALAEGKENAKVK-DIMtkdviTIDKDEKI-YDA 78

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1002253483 433 nspfgffngqrcqmclrsdtlLKVMErlaNPGVRRVFIVEAGSKRVeGIISLSDIFK 489
Cdd:cd04588    79 ---------------------IRLMN---KHNIGRLIVVDDNGKPV-GIITRTDILK 110
CBS_pair_arch1_repeat2 cd04632
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains present in archaea, ...
 364-489 1.08e-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: 39.24  E-value: 1.08e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002253483 364 LRPNTSLSAALNLLVQAGVSSIPIVDDNDSLLDTYSRSDITalakDKVythIRldEMTIHQALQLGQDA----------- 432
Cdd:cd04632     7 VNEDDTIGKAINLLREHGISRLPVVDDNGKLVGIVTTYDIV----DFV---VR--PGTKTRGGDRGGEKermldlpvydi 77

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1002253483 433 -NSPFgffngqrcQMCLRSDTLLKVMERLANPGVRRVfIVEAGSKRVEGIISLSDIFK 489
Cdd:cd04632    78 mSSPV--------VTVTRDATVADAVERMLENDISGL-VVTPDDNMVIGILTKTDVLR 126
CBS_pair_bac cd04629
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains present in bacteria; ...
 364-489 1.54e-03

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


Pssm-ID: 341392 [Multi-domain]  Cd Length: 116  Bit Score: 38.19  E-value: 1.54e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002253483 364 LRPNTSLSAALNLLVQAGVSSIPIVDDNDSLLDTYSRSD-ITALAKDKVY--THIRLDE-MTiHQALQLGQDanspfgff 439
Cdd:cd04629     8 LTPDTSILEAVELLLEHKISGAPVVDEQGRLVGFLSEQDcLKALLEASYHcePGGTVADyMS-TEVLTVSPD-------- 78

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 1002253483 440 ngqrcqmclrsDTLLKVMERLANPGVRRVFIVEAGskRVEGIISLSDIFK 489
Cdd:cd04629    79 -----------TSIVDLAQLFLKNKPRRYPVVEDG--KLVGQISRRDVLR 115
CBS_pair_inorgPPase cd04597
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with ...
 364-420 1.84e-03

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


Pssm-ID: 341372 [Multi-domain]  Cd Length: 106  Bit Score: 38.10  E-value: 1.84e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1002253483 364 LRPNTSLSAALNLLVQAGVSSIPIVDDNDSLLDTYSRSDITA-----LAKDKVYTHIRLDEM 420
Cdd:cd04597    10 LSPETSIKDAWNLMDENNLKTLPVTDDNGKLIGLLSISDIARtvdyiMTKDNLIVFKEDDYL 71
COG2524 COG2524
Predicted transcriptional regulator, contains C-terminal CBS domains [Transcription];
450-493 9.61e-03

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


Pssm-ID: 442013 [Multi-domain]  Cd Length: 206  Bit Score: 37.56  E-value: 9.61e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....
gi 1002253483 450 SDTLLKVMERLANPGVRRVFIVEAGskRVEGIISLSDIFKFLLS 493
Cdd:COG2524   102 DTTLEEALELMLEKGISGLPVVDDG--KLVGIITERDLLKALAE 143
 
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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