NCBI Conserved Domain Search

Conserved domains on [gi|515637361|ref|WP_017069961|]

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MULTISPECIES: DUF294 nucleotidyltransferase-like domain-containing protein [Vibrio]

Protein Classification

DUF294 nucleotidyltransferase-like/CBS domain-containing protein( domain architecture ID 1000477)

uncharacterized DUF294 nucleotidyltransferase-like/CBS (cystathione beta synthase) domain-containing protein

Gene Ontology: GO:0008773

Graphical summary

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List of domain hits

Name

Accession

Description

Interval

E-value

DUF294

pfam03445

Putative nucleotidyltransferase DUF294; This domain is found associated with pfam00571. This ...

301-437

1.35e-49

Putative nucleotidyltransferase DUF294; This domain is found associated with pfam00571. This region is uncharacterized, however it seems to be similar to pfam01909, conserving the DXD motif. This strongly suggests that members of this family are also nucleotidyltransferases (Bateman A pers. obs.).

Pssm-ID: 460919 Cd Length: 138 Bit Score: 168.56 E-value: 1.35e-49

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515637361  301 ERQAIFEALVEGKVAPETVGKVMTMIMDAYTRRLIQIAIDKLGPPPCDFSWIVAGSHARNEVHMLSDQDSAIVLADDATD 380
Cdd:pfam03445   2 RIPRLVRALLARGVRAEEIARLVSELNDALTRRLIELAEAELGPPPVPFAWLVMGSEGRGEQTLKTDQDNALVLADEEGD 81

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 515637361  381 SDRIYFKHLAMMVTNGLASCHYPLCPGKFMAATPKWCQPLSVWKHYYKKWVANPEYE 437
Cdd:pfam03445  82 AHREYFAAFAERVNAALDACGYPPCPGGIMASNPEWCGSLSEWRQRFRRWIRTPTPE 138

DUF294_C

pfam10335

Putative nucleotidyltransferase substrate binding domain; This domain is found associated with ...

475-617

1.80e-42

Putative nucleotidyltransferase substrate binding domain; This domain is found associated with presumed nucleotidyltransferase domains and seems to be distantly related to other helical substrate binding domains.

Pssm-ID: 463050 Cd Length: 144 Bit Score: 149.66 E-value: 1.80e-42

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515637361  475 FLSTLVKDAVNTNPPLGIFNSLVLEKSGENKKTLNVKKYAINLIIDLARIYGLAVECDLSATDERFAAANEKGMLSDDAF 554
Cdd:pfam10335   2 FLARLARNALRFRPPLGLFGRLVTERSGEHRGELDLKKGGIFPIVDGARLLALEHGIPATNTLERLRALAEAGVLSAELA 81

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 515637361  555 KNILGAYQFILSFRFGHQLEALKNGDVPDNNINPDSFGSFERKHLKDAFRIIADLQEAAKIRF 617
Cdd:pfam10335  82 EDLLEAYEFLLRLRLRHQLEAIKAGRPPDNYVDPSELSRLERDLLKDAFRVVKRLQEALARRF 144

CBS_pair_SF super family

cl15354

Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains superfamily; The CBS ...

161-272

3.22e-30

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 cd04587:

Pssm-ID: 449531 [Multi-domain] Cd Length: 114 Bit Score: 114.45 E-value: 3.22e-30

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515637361 161 VASGQVAIVKSEQTIQSVAVEMLHQRSPCAVIYEGETIVGLITDRDMTKRVIAHGVSTDSLISEVMTHSPLTVKPDDLVL 240
Cdd:cd04587    1 LMSRPPVTVPPDATIQEAAQLMSEERVSSLLVVDDGRLVGIVTDRDLRNRVVAEGLDPDTPVSEIMTPPPVTIDADALVF 80

                         90       100       110
                 ....*....|....*....|....*....|..
gi 515637361 241 HAASIMMQFNIRNLPVVKENKVVGLLTTSHLV 272
Cdd:cd04587   81 EALLLMLERNIHHLPVVDDGRVVGVVTATDLM 112

Crp

COG0664

cAMP-binding domain of CRP or a regulatory subunit of cAMP-dependent protein kinases [Signal ...

19-148

9.77e-10

cAMP-binding domain of CRP or a regulatory subunit of cAMP-dependent protein kinases [Signal transduction mechanisms];

Pssm-ID: 440428 [Multi-domain] Cd Length: 207 Bit Score: 58.84 E-value: 9.77e-10

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515637361  19 FDKIPKQALRELASNVQITYLGKGDVvdLCESGKE-KSLYIIRTG--SMEQRKSDG--VLRARLGSEDLFG-FTFLDSEV 92
Cdd:COG0664    1 FAGLSDEELEALLAHLELRTLKKGEV--LFREGDPaDHLYFVLSGlvKLYRISEDGreQILGFLGPGDFFGeLSLLGGEP 78

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 515637361  93 NDekgYRAVAIENTLLYVIPHSALQTLFKAFPSCAEHFASQAQVRLKSALDVVWSN 148
Cdd:COG0664   79 SP---ATAEALEDSELLRIPREDLEELLERNPELARALLRLLARRLRQLQERLVSL 131

Name

Accession

Description

Interval

E-value

DUF294

pfam03445

Putative nucleotidyltransferase DUF294; This domain is found associated with pfam00571. This ...

301-437

1.35e-49

Pssm-ID: 460919 Cd Length: 138 Bit Score: 168.56 E-value: 1.35e-49

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515637361  301 ERQAIFEALVEGKVAPETVGKVMTMIMDAYTRRLIQIAIDKLGPPPCDFSWIVAGSHARNEVHMLSDQDSAIVLADDATD 380
Cdd:pfam03445   2 RIPRLVRALLARGVRAEEIARLVSELNDALTRRLIELAEAELGPPPVPFAWLVMGSEGRGEQTLKTDQDNALVLADEEGD 81

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 515637361  381 SDRIYFKHLAMMVTNGLASCHYPLCPGKFMAATPKWCQPLSVWKHYYKKWVANPEYE 437
Cdd:pfam03445  82 AHREYFAAFAERVNAALDACGYPPCPGGIMASNPEWCGSLSEWRQRFRRWIRTPTPE 138

DUF294_C

pfam10335

Putative nucleotidyltransferase substrate binding domain; This domain is found associated with ...

475-617

1.80e-42

Pssm-ID: 463050 Cd Length: 144 Bit Score: 149.66 E-value: 1.80e-42

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515637361  475 FLSTLVKDAVNTNPPLGIFNSLVLEKSGENKKTLNVKKYAINLIIDLARIYGLAVECDLSATDERFAAANEKGMLSDDAF 554
Cdd:pfam10335   2 FLARLARNALRFRPPLGLFGRLVTERSGEHRGELDLKKGGIFPIVDGARLLALEHGIPATNTLERLRALAEAGVLSAELA 81

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 515637361  555 KNILGAYQFILSFRFGHQLEALKNGDVPDNNINPDSFGSFERKHLKDAFRIIADLQEAAKIRF 617
Cdd:pfam10335  82 EDLLEAYEFLLRLRLRHQLEAIKAGRPPDNYVDPSELSRLERDLLKDAFRVVKRLQEALARRF 144

NT_GlnE_GlnD_like

cd05401

Nucleotidyltransferase (NT) domain of Escherichia coli adenylyltransferase (GlnE), Escherichia ...

305-470

6.39e-36

Nucleotidyltransferase (NT) domain of Escherichia coli adenylyltransferase (GlnE), Escherichia coli uridylyl transferase (GlnD), and similar proteins; Escherichia coli GlnD and -E participate in the Glutamine synthetase (GS)/Glutamate synthase (GOGAT) pathway for the assimilation of ammonium nitrogen. In nitrogen sufficiency, GlnE adenylates GS, reducing GS activity; when nitrogen is limiting, GlnE deadenylates GS-AMP, restoring GS activity. When nitrogen is limiting, GlnD uridylylates the nitrogen regulatory protein PII to PII-UTP, and in nitrogen sufficiency, it removes the modifying groups. The activity of Escherichia coli GlnE is modulated by PII-proteins. PII-UMP promotes GlnE deadenylation activity, and PII promotes GlnE adenylation activity. Escherichia coli GlnE has two separate NT domains. The N-terminal NT domain catalyzes the deadenylylation of GS, and the C-terminal NT domain the adenylylation reaction. The majority of proteins in this family contain a C-terminal NT domain which is associated with a cystathionine beta-synthase (CBS) domain pair and a CAP_ED (cAMP receptor protein effector ) domain. This family belongs to the Pol beta-like NT superfamily. In the majority of enzymes in this superfamily, two carboxylates, Dx[D/E], together with a third more distal carboxylate, coordinate two divalent metal cations involved in a two-metal ion mechanism of nucleotide addition. For the majority of proteins in this family, these carboxylate residues are conserved.

Pssm-ID: 143391 [Multi-domain] Cd Length: 172 Bit Score: 132.85 E-value: 6.39e-36

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515637361 305 IFEALVEGKVAPETVGKVMTMIMDAYTRRLIQIAIDKLG--PPPCDFSWIVAGSHARNEVHMLSDQDSAIVLADDATDSD 382
Cdd:cd05401   10 ILRRDLLGGASIRAISRALSDLADALLRRALELALAELGkgPPPVPFALLALGSYGRGELNPSSDQDLLLLYDDDGDEVA 89

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515637361 383 RiYFKHLAMMVTNGLASCHYPLCPGKFMAATPKWCQPLSVWKHYYKKWVANPeyERLLNISVFLEIRTIYGNSEfegiLR 462
Cdd:cd05401   90 A-YFEELAERLIKILSEAGGPYCLGDVMLRPPGWRRSLAEWLDAARDWLTEP--GRLWERTALLDARPVAGDRA----LA 162


                 ....*...
gi 515637361 463 DELHSNIR 470
Cdd:cd05401  163 EELRRRIR 170

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 ...

161-272

3.22e-30

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: 114.45 E-value: 3.22e-30

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515637361 161 VASGQVAIVKSEQTIQSVAVEMLHQRSPCAVIYEGETIVGLITDRDMTKRVIAHGVSTDSLISEVMTHSPLTVKPDDLVL 240
Cdd:cd04587    1 LMSRPPVTVPPDATIQEAAQLMSEERVSSLLVVDDGRLVGIVTDRDLRNRVVAEGLDPDTPVSEIMTPPPVTIDADALVF 80

                         90       100       110
                 ....*....|....*....|....*....|..
gi 515637361 241 HAASIMMQFNIRNLPVVKENKVVGLLTTSHLV 272
Cdd:cd04587   81 EALLLMLERNIHHLPVVDDGRVVGVVTATDLM 112

COG2905

Signal-transduction protein containing cAMP-binding, CBS, and nucleotidyltransferase domains ...

158-273

5.66e-30

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

Pssm-ID: 442149 [Multi-domain] Cd Length: 124 Bit Score: 114.16 E-value: 5.66e-30

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515637361 158 VEEVASGQVAIVKSEQTIQSVAVEMLHQRSPCAVIYEGE-TIVGLITDRDMTKRVIAHGVSTDSL-ISEVMTHSPLTVKP 235
Cdd:COG2905    1 VKDIMSRDVVTVSPDATVREAARLMTEKGVGSLVVVDDDgRLVGIITDRDLRRRVLAEGLDPLDTpVSEVMTRPPITVSP 80

                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 515637361 236 DDLVLHAASIMMQFNIRNLPVVKENKVVGLLTTSHLVQ 273
Cdd:COG2905   81 DDSLAEALELMEEHRIRHLPVVDDGKLVGIVSITDLLR 118

CBS

pfam00571

CBS domain; CBS domains are small intracellular modules that pair together to form a stable ...

222-272

5.25e-10

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: 55.30 E-value: 5.25e-10

                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 515637361  222 ISEVMTHSPLTVKPDDLVLHAASIMMQFNIRNLPVVKEN-KVVGLLTTSHLV 272
Cdd:pfam00571   1 VKDIMTKDVVTVSPDTTLEEALELMREHGISRLPVVDEDgKLVGIVTLKDLL 52

Crp

COG0664

cAMP-binding domain of CRP or a regulatory subunit of cAMP-dependent protein kinases [Signal ...

19-148

9.77e-10

cAMP-binding domain of CRP or a regulatory subunit of cAMP-dependent protein kinases [Signal transduction mechanisms];

Pssm-ID: 440428 [Multi-domain] Cd Length: 207 Bit Score: 58.84 E-value: 9.77e-10

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515637361  19 FDKIPKQALRELASNVQITYLGKGDVvdLCESGKE-KSLYIIRTG--SMEQRKSDG--VLRARLGSEDLFG-FTFLDSEV 92
Cdd:COG0664    1 FAGLSDEELEALLAHLELRTLKKGEV--LFREGDPaDHLYFVLSGlvKLYRISEDGreQILGFLGPGDFFGeLSLLGGEP 78

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 515637361  93 NDekgYRAVAIENTLLYVIPHSALQTLFKAFPSCAEHFASQAQVRLKSALDVVWSN 148
Cdd:COG0664   79 SP---ATAEALEDSELLRIPREDLEELLERNPELARALLRLLARRLRQLQERLVSL 131

CAP_ED

cd00038

effector domain of the CAP family of transcription factors; members include CAP (or cAMP ...

18-125

6.57e-08

effector domain of the CAP family of transcription factors; members include CAP (or cAMP receptor protein (CRP)), which binds cAMP, FNR (fumarate and nitrate reduction), 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. Cyclic nucleotide-binding domain similar to CAP are also present in cAMP- and cGMP-dependent protein kinases (cAPK and cGPK) and vertebrate cyclic nucleotide-gated ion-channels. Cyclic nucleotide-monophosphate binding domain; proteins that bind cyclic nucleotides (cAMP or cGMP) share a structural domain of about 120 residues; the best studied is the prokaryotic catabolite gene activator, CAP, where such a domain is known to be composed of three alpha-helices and a distinctive eight-stranded, antiparallel beta-barrel structure; three conserved glycine residues are thought to be essential for maintenance of the structural integrity of the beta-barrel; CooA is a homodimeric transcription factor that belongs to CAP family; cAMP- and cGMP-dependent protein kinases (cAPK and cGPK) contain two tandem copies of the cyclic nucleotide-binding domain; cAPK's are composed of two different subunits, a catalytic chain and a regulatory chain, which contains both copies of the domain; cGPK's are single chain enzymes that include the two copies of the domain in their N-terminal section; also found in vertebrate cyclic nucleotide-gated ion-channels

Pssm-ID: 237999 [Multi-domain] Cd Length: 115 Bit Score: 51.17 E-value: 6.57e-08

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515637361  18 PFDKIPKQALRELASNVQITYLGKGDVVdLCESGKEKSLYIIRTGSME--QRKSDG--VLRARLGSEDLFGFTFLDSevN 93
Cdd:cd00038    1 LFSGLDDEELEELADALEERRFPAGEVI-IRQGDPADSLYIVLSGSVEvyKLDEDGreQIVGFLGPGDLFGELALLG--N 77

                         90       100       110
                 ....*....|....*....|....*....|..
gi 515637361  94 DEKGYRAVAIENTLLYVIPHSALQTLFKAFPS 125
Cdd:cd00038   78 GPRSATVRALTDSELLVLPRSDFRRLLQEYPE 109

CBS

smart00116

Domain in cystathionine beta-synthase and other proteins; Domain present in all 3 forms of ...

230-274

9.45e-06

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: 42.89 E-value: 9.45e-06

                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*.
gi 515637361   230 PLTVKPDDLVLHAASIMMQFNIRNLPVVKE-NKVVGLLTTSHLVQN 274
Cdd:smart00116   2 VVTVSPDTTLEEALELLRENGIRRLPVVDEeGRLVGIVTRRDIIKA 47

PRK14869

putative manganese-dependent inorganic diphosphatase;

222-271

1.18e-05

putative manganese-dependent inorganic diphosphatase;

Pssm-ID: 237843 [Multi-domain] Cd Length: 546 Bit Score: 48.29 E-value: 1.18e-05

                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|.
gi 515637361 222 ISEVMTHSPLTVKPDDLVLHAASIMMQFNIRNLPVV-KENKVVGLLTTSHL 271
Cdd:PRK14869  70 VRDLEIDKPVTVSPDTSLKEAWNLMDENNVKTLPVVdEEGKLLGLVSLSDL 120

cNMP_binding

pfam00027

Cyclic nucleotide-binding domain; This domain sensor domain can bind cAMP, cGMP, c-di-GMP, ...

38-121

4.89e-05

Cyclic nucleotide-binding domain; This domain sensor domain can bind cAMP, cGMP, c-di-GMP, oxygen and 2-oxoglutarate (Matilla et. al., FEMS Microbiology Reviews, fuab043, 45, 2021, 1. https://doi.org/10.1093/femsre/fuab043).

Pssm-ID: 459637 [Multi-domain] Cd Length: 89 Bit Score: 42.21 E-value: 4.89e-05

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515637361   38 YLGKGDVvdLCESGKE-KSLYIIRTGSME--QRKSDG--VLRARLGSEDLFGF-TFLDSEVNDekgYRAVAIENTLLYVI 111
Cdd:pfam00027   3 SYKAGEV--IFREGDPaDSLYIVLSGKVKvyRTLEDGreQILAVLGPGDFFGElALLGGEPRS---ATVVALTDSELLVI 77

                          90
                  ....*....|
gi 515637361  112 PHSALQTLFK 121
Cdd:pfam00027  78 PREDFLELLE 87

cNMP

smart00100

Cyclic nucleotide-monophosphate binding domain; Catabolite gene activator protein (CAP) is a ...

18-131

1.74e-04

Cyclic nucleotide-monophosphate binding domain; Catabolite gene activator protein (CAP) is a prokaryotic homologue of eukaryotic cNMP-binding domains, present in ion channels, and cNMP-dependent kinases.

Pssm-ID: 197516 [Multi-domain] Cd Length: 120 Bit Score: 41.62 E-value: 1.74e-04

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515637361    18 PFDKIPKQALRELASNVQITYLGKGDVVdlCESGKE-KSLYIIRTGSMEQRKSD----GVLRARLGSEDLFGFTFLdseV 92
Cdd:smart00100   1 LFKNLDAEELRELADALEPVRYPAGEVI--IRQGDVgDSFYIIVSGEVEVYKVLedgeEQIVGTLGPGDFFGELAL---L 75

                           90       100       110
                   ....*....|....*....|....*....|....*....
gi 515637361    93 NDEKGYRAVAIENTLLYVIPHSALQTLFKAFPSCAEHFA 131
Cdd:smart00100  76 TNSRRAASAAAVALELATLLRIDFRDFLQLLPELPQLLL 114

Name

Accession

Description

Interval

E-value

DUF294

pfam03445

Putative nucleotidyltransferase DUF294; This domain is found associated with pfam00571. This ...

301-437

1.35e-49

Pssm-ID: 460919 Cd Length: 138 Bit Score: 168.56 E-value: 1.35e-49

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515637361  301 ERQAIFEALVEGKVAPETVGKVMTMIMDAYTRRLIQIAIDKLGPPPCDFSWIVAGSHARNEVHMLSDQDSAIVLADDATD 380
Cdd:pfam03445   2 RIPRLVRALLARGVRAEEIARLVSELNDALTRRLIELAEAELGPPPVPFAWLVMGSEGRGEQTLKTDQDNALVLADEEGD 81

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 515637361  381 SDRIYFKHLAMMVTNGLASCHYPLCPGKFMAATPKWCQPLSVWKHYYKKWVANPEYE 437
Cdd:pfam03445  82 AHREYFAAFAERVNAALDACGYPPCPGGIMASNPEWCGSLSEWRQRFRRWIRTPTPE 138

DUF294_C

pfam10335

Putative nucleotidyltransferase substrate binding domain; This domain is found associated with ...

475-617

1.80e-42

Pssm-ID: 463050 Cd Length: 144 Bit Score: 149.66 E-value: 1.80e-42

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515637361  475 FLSTLVKDAVNTNPPLGIFNSLVLEKSGENKKTLNVKKYAINLIIDLARIYGLAVECDLSATDERFAAANEKGMLSDDAF 554
Cdd:pfam10335   2 FLARLARNALRFRPPLGLFGRLVTERSGEHRGELDLKKGGIFPIVDGARLLALEHGIPATNTLERLRALAEAGVLSAELA 81

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 515637361  555 KNILGAYQFILSFRFGHQLEALKNGDVPDNNINPDSFGSFERKHLKDAFRIIADLQEAAKIRF 617
Cdd:pfam10335  82 EDLLEAYEFLLRLRLRHQLEAIKAGRPPDNYVDPSELSRLERDLLKDAFRVVKRLQEALARRF 144

NT_GlnE_GlnD_like

cd05401

Nucleotidyltransferase (NT) domain of Escherichia coli adenylyltransferase (GlnE), Escherichia ...

305-470

6.39e-36

Pssm-ID: 143391 [Multi-domain] Cd Length: 172 Bit Score: 132.85 E-value: 6.39e-36

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515637361 305 IFEALVEGKVAPETVGKVMTMIMDAYTRRLIQIAIDKLG--PPPCDFSWIVAGSHARNEVHMLSDQDSAIVLADDATDSD 382
Cdd:cd05401   10 ILRRDLLGGASIRAISRALSDLADALLRRALELALAELGkgPPPVPFALLALGSYGRGELNPSSDQDLLLLYDDDGDEVA 89

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515637361 383 RiYFKHLAMMVTNGLASCHYPLCPGKFMAATPKWCQPLSVWKHYYKKWVANPeyERLLNISVFLEIRTIYGNSEfegiLR 462
Cdd:cd05401   90 A-YFEELAERLIKILSEAGGPYCLGDVMLRPPGWRRSLAEWLDAARDWLTEP--GRLWERTALLDARPVAGDRA----LA 162


                 ....*...
gi 515637361 463 DELHSNIR 470
Cdd:cd05401  163 EELRRRIR 170

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 ...

161-272

3.22e-30

Pssm-ID: 341363 [Multi-domain] Cd Length: 114 Bit Score: 114.45 E-value: 3.22e-30

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515637361 161 VASGQVAIVKSEQTIQSVAVEMLHQRSPCAVIYEGETIVGLITDRDMTKRVIAHGVSTDSLISEVMTHSPLTVKPDDLVL 240
Cdd:cd04587    1 LMSRPPVTVPPDATIQEAAQLMSEERVSSLLVVDDGRLVGIVTDRDLRNRVVAEGLDPDTPVSEIMTPPPVTIDADALVF 80

                         90       100       110
                 ....*....|....*....|....*....|..
gi 515637361 241 HAASIMMQFNIRNLPVVKENKVVGLLTTSHLV 272
Cdd:cd04587   81 EALLLMLERNIHHLPVVDDGRVVGVVTATDLM 112

COG2905

Signal-transduction protein containing cAMP-binding, CBS, and nucleotidyltransferase domains ...

158-273

5.66e-30

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

Pssm-ID: 442149 [Multi-domain] Cd Length: 124 Bit Score: 114.16 E-value: 5.66e-30

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515637361 158 VEEVASGQVAIVKSEQTIQSVAVEMLHQRSPCAVIYEGE-TIVGLITDRDMTKRVIAHGVSTDSL-ISEVMTHSPLTVKP 235
Cdd:COG2905    1 VKDIMSRDVVTVSPDATVREAARLMTEKGVGSLVVVDDDgRLVGIITDRDLRRRVLAEGLDPLDTpVSEVMTRPPITVSP 80

                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 515637361 236 DDLVLHAASIMMQFNIRNLPVVKENKVVGLLTTSHLVQ 273
Cdd:COG2905   81 DDSLAEALELMEEHRIRHLPVVDDGKLVGIVSITDLLR 118

CBS

COG0517

CBS domain [Signal transduction mechanisms];

157-273

1.19e-26

CBS domain [Signal transduction mechanisms];

Pssm-ID: 440283 [Multi-domain] Cd Length: 128 Bit Score: 104.95 E-value: 1.19e-26

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515637361 157 KVEEVASGQVAIVKSEQTIQSVAVEMLHQRSPCA-VIYEGETIVGLITDRDMTKRVIAHGVSTDSL-ISEVMTHSPLTVK 234
Cdd:COG0517    2 KVKDIMTTDVVTVSPDATVREALELMSEKRIGGLpVVDEDGKLVGIVTDRDLRRALAAEGKDLLDTpVSEVMTRPPVTVS 81

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 515637361 235 PDDLVLHAASIMMQFNIRNLPVV-KENKVVGLLTTSHLVQ 273
Cdd:COG0517   82 PDTSLEEAAELMEEHKIRRLPVVdDDGRLVGIITIKDLLK 121

COG2524

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

157-272

4.36e-22

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

Pssm-ID: 442013 [Multi-domain] Cd Length: 206 Bit Score: 94.57 E-value: 4.36e-22

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515637361 157 KVEEVASGQVAIVKSEQTIQSVAVEMLHQRSPCAVIYEGETIVGLITDRDMTKRVIAHGVSTDSLISEVMTHSPLTVKPD 236
Cdd:COG2524   87 KVKDIMTKDVITVSPDTTLEEALELMLEKGISGLPVVDDGKLVGIITERDLLKALAEGRDLLDAPVSDIMTRDVVTVSED 166

                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 515637361 237 DLVLHAASIMMQFNIRNLPVV-KENKVVGLLTTSHLV 272
Cdd:COG2524  167 DSLEEALRLMLEHGIGRLPVVdDDGKLVGIITRTDIL 203

CBS_pair_SF

cd02205

Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains superfamily; The CBS ...

165-273

7.11e-21

Pssm-ID: 341358 [Multi-domain] Cd Length: 113 Bit Score: 88.07 E-value: 7.11e-21

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515637361 165 QVAIVKSEQTIQSVAVEMLHQRSPCA-VIYEGETIVGLITDRDMTKRVIAHGVSTDSLISEVMTHSPLTVKPDDLVLHAA 243
Cdd:cd02205    3 DVVTVDPDTTVREALELMAENGIGALpVVDDDGKLVGIVTERDILRALVEGGLALDTPVAEVMTPDVITVSPDTDLEEAL 82

                         90       100       110
                 ....*....|....*....|....*....|.
gi 515637361 244 SIMMQFNIRNLPVVKEN-KVVGLLTTSHLVQ 273
Cdd:cd02205   83 ELMLEHGIRRLPVVDDDgKLVGIVTRRDILR 113

CBS_pair_arch

cd09836

Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains; The CBS domain, ...

166-272

2.18e-20

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: 86.81 E-value: 2.18e-20

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515637361 166 VAIVKSEQTIQSVAVEMLHQR-SPCAVIYEGETIVGLITDRDMTkRVIAHGVSTDSLISEVMTHSPLTVKPDDLVLHAAS 244
Cdd:cd09836    5 VVTVPPETTIREAAKLMAENNiGSVVVVDDDGKPVGIVTERDIV-RAVAEGIDLDTPVEEIMTKNLVTVSPDESIYEAAE 83

                         90       100
                 ....*....|....*....|....*....
gi 515637361 245 IMMQFNIRNLPVV-KENKVVGLLTTSHLV 272
Cdd:cd09836   84 LMREHNIRHLPVVdGGGKLVGVISIRDLA 112

CBS_pair_HRP1_like

cd04622

CBS pair domain found in Hypoxic Response Protein 1 (HRP1) -like proteinds; Mycobacterium ...

166-267

3.63e-19

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: 83.24 E-value: 3.63e-19

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515637361 166 VAIVKSEQTIQSVAVEMLHQRSPCAVIYEGETIVGLITDRDMTKRVIAHGVSTDSL-ISEVMTHSPLTVKPDDLVLHAAS 244
Cdd:cd04622    5 VVTVSPDTTLREAARLMRDLDIGALPVCEGDRLVGMVTDRDIVVRAVAEGKDPNTTtVREVMTGDVVTCSPDDDVEEAAR 84

                         90       100
                 ....*....|....*....|....
gi 515637361 245 IMMQFNIRNLPVVKENK-VVGLLT 267
Cdd:cd04622   85 LMAEHQVRRLPVVDDDGrLVGIVS 108

CBS_pair_bact_arch

cd17775

Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains present in bacteria ...

165-272

6.69e-19

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

Pssm-ID: 341411 [Multi-domain] Cd Length: 117 Bit Score: 82.59 E-value: 6.69e-19

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515637361 165 QVAIVKSEQTIQSVAVEMLHQRSPCAVIYEGETI-VGLITDRDMTKRVIAHGVSTDSL-ISEVMTHSPLTVKPDDLVLHA 242
Cdd:cd17775    4 EVVTASPDTSVLEAARLMRDHHVGSVVVVEEDGKpVGIVTDRDIVVEVVAKGLDPKDVtVGDIMSADLITAREDDGLFEA 83

                         90       100       110
                 ....*....|....*....|....*....|.
gi 515637361 243 ASIMMQFNIRNLPVV-KENKVVGLLTTSHLV 272
Cdd:cd17775   84 LERMREKGVRRLPVVdDDGELVGIVTLDDIL 114

CBS_pair_bac_euk

cd04623

Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains present in bacteria ...

163-266

7.21e-19

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: 82.46 E-value: 7.21e-19

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515637361 163 SGQVAIVKSEQTIQSVAVEMLHQRSPCAVIYEG-ETIVGLITDRDMTKRVIAHGVST-DSLISEVMTHSPLTVKPDDLVL 240
Cdd:cd04623    1 GRDVVTVSPDATVAEALRLLAEKNIGALVVVDDgGRLVGILSERDYVRKLALRGASSlDTPVSEIMTRDVVTCTPDDTVE 80

                         90       100
                 ....*....|....*....|....*.
gi 515637361 241 HAASIMMQFNIRNLPVVKENKVVGLL 266
Cdd:cd04623   81 ECMALMTERRIRHLPVVEDGKLVGIV 106

COG3448

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

157-273

6.12e-17

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

Pssm-ID: 442671 [Multi-domain] Cd Length: 136 Bit Score: 77.60 E-value: 6.12e-17

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515637361 157 KVEEVASGQVAIVKSEQTIQSVAVEMLHQRSPCA-VIYEGETIVGLITDRDMTKRVIAHGVS------TDSLISEVMTHS 229
Cdd:COG3448    3 TVRDIMTRDVVTVSPDTTLREALELMREHGIRGLpVVDEDGRLVGIVTERDLLRALLPDRLDeleerlLDLPVEDVMTRP 82

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 515637361 230 PLTVKPDDLVLHAASIMMQFNIRNLPVV-KENKVVGLLTTSHLVQ 273
Cdd:COG3448   83 VVTVTPDTPLEEAAELMLEHGIHRLPVVdDDGRLVGIVTRTDLLR 127

CBS_pair_MUG70_1

cd17781

Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains similar to MUG70 ...

168-266

1.00e-16

Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains similar to MUG70 repeat1; Two tandem repeats of the cystathionine beta-synthase (CBS pair) domain, present in MUG70. The MUG70 protein, encoded by the Meiotically Up-regulated Gene 70, plays a role in meiosis and contains, beside the two CBS pairs, a PB1 domain. The CBS domain, named after human CBS, is a small domain originally identified in cystathionine beta-synthase and is subsequently found in a wide range of different proteins. CBS domains usually occur in tandem repeats. They associate to form a so-called Bateman domain or a CBS pair based on crystallographic studies in bacteria. The CBS pair was used as a basis for this cd hierarchy since the human CBS proteins can adopt the typical core structure and form an intramolecular CBS pair. The interface between the two CBS domains forms a cleft that is a potential ligand binding site. The CBS pair coexists with a variety of other functional domains and this has been used to help in its classification here. It has been proposed that the CBS domain may play a regulatory role, although its exact function is unknown. Mutations of conserved residues within this domain are associated with a variety of human hereditary diseases, including congenital myotonia, idiopathic generalized epilepsy, hypercalciuric nephrolithiasis, and classic Bartter syndrome (CLC chloride channel family members), Wolff-Parkinson-White syndrome (gamma 2 subunit of AMP-activated protein kinase), retinitis pigmentosa (IMP dehydrogenase-1), and homocystinuria (cystathionine beta-synthase).

Pssm-ID: 341417 [Multi-domain] Cd Length: 118 Bit Score: 76.47 E-value: 1.00e-16

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515637361 168 IVKSEQTIQSVAVEMLHQRSPCA-VIYEGETIVGLITDRDMTKRVIAHGVSTDS-LISEVMTHSPLTVKPDDLVLHAASI 245
Cdd:cd17781    6 TVPETTTVAEAAQLMAAKRTDAVlVVDDDGGLSGIFTDKDLARRVVASGLDPRStLVSSVMTPNPLCVTMDTSATDALDL 85

                         90       100
                 ....*....|....*....|..
gi 515637361 246 MMQFNIRNLPVVKEN-KVVGLL 266
Cdd:cd17781   86 MVEGKFRHLPVVDDDgDVVGVL 107

CBS_two-component_sensor_histidine_kinase_repeat1

cd04620

2 tandem repeats of the CBS domain in the two-component sensor histidine kinase and ...

169-273

6.40e-16

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

Pssm-ID: 341389 [Multi-domain] Cd Length: 136 Bit Score: 74.88 E-value: 6.40e-16

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515637361 169 VKSEQTIQSVAVEMLHQRSPCAVIYEGETIVGLITDRDMTkRVIAHGVSTDSL-ISEVMTHSPLTVKPDDL--VLHAASI 245
Cdd:cd04620   28 TRSSCCLLSEDSIITEARSSCVLVVENQQLVGIFTERDVV-RLTASGIDLSGVtIAEVMTQPVITLKESEFqdIFTVLSL 106

                         90       100
                 ....*....|....*....|....*....
gi 515637361 246 MMQFNIRNLPVVKE-NKVVGLLTTSHLVQ 273
Cdd:cd04620  107 LRQHQIRHLPIVDDqGQLVGLITPESLRQ 135

CBS_pair_AcuB_like

cd04584

Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with the ...

157-269

6.61e-16

Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with the ACT domain; The putative Acetoin Utilization Protein (Acub) from Vibrio Cholerae contains a CBS pair domain. The acetoin utilization protein plays a role in growth and sporulation on acetoin or butanediol for use as a carbon source. Acetoin is an important physiological metabolite excreted by many microorganisms. It is used as an external energy store by a number of fermentive bacteria. Acetoin is produced by the decarboxylation of alpha-acetolactate. Once superior carbon sources are exhausted, and the culture enters stationary phase, acetoin can be utilised in order to maintain the culture density. The conversion of acetoin into acetyl-CoA or 2,3-butanediol is catalysed by the acetoin dehydrogenase complex and acetoin reductase/2,3-butanediol dehydrogenase, respectively. Acetoin utilization proteins, acetylpolyamine amidohydrolases, and histone deacetylases are members of an ancient protein superfamily.This cd contains two tandem repeats of the cystathionine beta-synthase (CBS pair) domains in the acetoin utilization proteins in bacteria. Acetoin is a product of fermentative metabolism in many prokaryotic and eukaryotic microorganisms. They produce acetoin as an external carbon storage compound and then later reuse it as a carbon and energy source during their stationary phase and sporulation. In addition these CBS domains are associated with a downstream ACT (aspartate kinase/chorismate mutase/TyrA) domain, which is linked to a wide range of metabolic enzymes that are regulated by amino acid concentration. Pairs of ACT domains bind specifically to a particular amino acid leading to regulation of the linked enzyme. The CBS domain, named after human CBS, is a small domain originally identified in cystathionine beta-synthase and is subsequently found in a wide range of different proteins. CBS domains usually occur in tandem repeats. They associate to form a so-called Bateman domain or a CBS pair based on crystallographic studies in bacteria. The CBS pair was used as a basis for this cd hierarchy since the human CBS proteins can adopt the typical core structure and form an intramolecular CBS pair. The interface between the two CBS domains forms a cleft that is a potential ligand binding site. The CBS pair coexists with a variety of other functional domains and this has been used to help in its classification here. It has been proposed that the CBS domain may play a regulatory role, although its exact function is unknown. Mutations of conserved residues within this domain are associated with a variety of human hereditary diseases, including congenital myotonia, idiopathic generalized epilepsy, hypercalciuric nephrolithiasis, and classic Bartter syndrome (CLC chloride channel family members), Wolff-Parkinson-White syndrome (gamma 2 subunit of AMP-activated protein kinase), retinitis pigmentosa (IMP dehydrogenase-1), and homocystinuria (cystathionine beta-synthase).

Pssm-ID: 341361 [Multi-domain] Cd Length: 130 Bit Score: 74.38 E-value: 6.61e-16

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515637361 157 KVEEVASGQVAIVKSEQTIqSVAVEMLHQRS----PcaVIyEGETIVGLITDRDMtKRVIAHGVSTDSL----------- 221
Cdd:cd04584    1 LVKDIMTKNVVTVTPDTSL-AEARELMKEHKirhlP--VV-DDGKLVGIVTDRDL-LRASPSKATSLSIyelnyllskip 75

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 515637361 222 ISEVMTHSPLTVKPDDLVLHAASIMMQFNIRNLPVVKENKVVGLLTTS 269
Cdd:cd04584   76 VKDIMTKDVITVSPDDTVEEAALLMLENKIGCLPVVDGGKLVGIITET 123

CBS_pair_SIS_assoc

cd04604

Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with the ...

156-266

5.40e-15

Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with the with the SIS (Sugar ISomerase) domain; This cd contains two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with the SIS (Sugar ISomerase) domain in the API [A5P (D-arabinose 5-phosphate) isomerase] protein KpsF/GutQ. These APIs catalyze the conversion of the pentose pathway intermediate D-ribulose 5-phosphate into A5P, a precursor of 3-deoxy-D-manno-octulosonate, which is an integral carbohydrate component of various glycolipids coating the surface of the outer membrane of Gram-negative bacteria, including lipopolysaccharide and many group 2 K-antigen capsules. 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: 341378 [Multi-domain] Cd Length: 124 Bit Score: 71.64 E-value: 5.40e-15

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515637361 156 RKVEEV--ASGQVAIVKSEQTIQSVAVEMLHQRSPCAVIYEGE-TIVGLITDRDMtKRVIAHGVSTDSL-ISEVMTHSPL 231
Cdd:cd04604    3 LRVSDLmhTGDELPLVSPDTSLKEALLEMTRKGLGCTAVVDEDgRLVGIITDGDL-RRALEKGLDILNLpAKDVMTRNPK 81

                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 515637361 232 TVKPDDLVLHAASIMMQFNIRNLPVV-KENKVVGLL 266
Cdd:cd04604   82 TISPDALAAEALELMEEHKITVLPVVdEDGKPVGIL 117

CBS_pair_arch_MET2_assoc

cd04605

Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with the ...

158-271

1.35e-14

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

Pssm-ID: 341379 [Multi-domain] Cd Length: 116 Bit Score: 70.35 E-value: 1.35e-14

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515637361 158 VEEVASGQVAIVKSEQTIQSVAVEML-HQRSPCAVIYEGETIVGLITDRDMTKRViAHGVSTdslISEVMTHSPLTVKPD 236
Cdd:cd04605    2 VEDIMSKDVATIREDISIEEAAKIMIdKNVTHLPVVSEDGKLIGIVTSWDISKAV-ALKKDS---LEEIMTRNVITARPD 77

                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 515637361 237 DLVLHAASIMMQFNIRNLPVV-KENKVVGLLTTSHL 271
Cdd:cd04605   78 EPIELAARKMEKHNISALPVVdDDRRVIGIITSDDI 113

CBS_pair_bac

cd04629

Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains present in bacteria; ...

169-273

1.31e-13

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: 67.46 E-value: 1.31e-13

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515637361 169 VKSEQTIQSVAVEMLHQRSPCA-VIYEGETIVGLITDRDMTKRVIA---HGvSTDSLISEVMTHSPLTVKPDDLVLHAAS 244
Cdd:cd04629    8 LTPDTSILEAVELLLEHKISGApVVDEQGRLVGFLSEQDCLKALLEasyHC-EPGGTVADYMSTEVLTVSPDTSIVDLAQ 86

                         90       100
                 ....*....|....*....|....*....
gi 515637361 245 IMMQFNIRNLPVVKENKVVGLLTTSHLVQ 273
Cdd:cd04629   87 LFLKNKPRRYPVVEDGKLVGQISRRDVLR 115

YtoI

COG4109

Predicted transcriptional regulator containing CBS domains [Transcription];

157-267

1.84e-12

Predicted transcriptional regulator containing CBS domains [Transcription];

Pssm-ID: 443285 [Multi-domain] Cd Length: 135 Bit Score: 64.93 E-value: 1.84e-12

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515637361 157 KVEEV-ASGQVAIVKSEQTIQSvAVEML----HQRSPcaVIYEGETIVGLITDRDMTkrviahGVSTDSLISEVMTHSPL 231
Cdd:COG4109   17 LVEDImTLEDVATLSEDDTVED-ALELLektgHSRFP--VVDENGRLVGIVTSKDIL------GKDDDTPIEDVMTKNPI 87

                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 515637361 232 TVKPDDLVLHAASIMMQFNIRNLPVVKEN-KVVGLLT 267
Cdd:COG4109   88 TVTPDTSLASAAHKMIWEGIELLPVVDDDgRLLGIIS 124

CBS_pair_DHH_polyA_Pol_assoc

cd04595

Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with the ...

166-269

5.89e-12

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

Pssm-ID: 341370 [Multi-domain] Cd Length: 110 Bit Score: 62.51 E-value: 5.89e-12

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515637361 166 VAIVKSEQTIQSVAVEML---HQRSPcaVIyEGETIVGLITDRDMTKrVIAHGVStDSLISEVMTHSPLTVKPDDLVLHA 242
Cdd:cd04595    4 VKTVSPDTTIEEARKIMLrygHTGLP--VV-EDGKLVGIISRRDVDK-AKHHGLG-HAPVKGYMSTNVITIDPDTSLEEA 78

                         90       100
                 ....*....|....*....|....*..
gi 515637361 243 ASIMMQFNIRNLPVVKENKVVGLLTTS 269
Cdd:cd04595   79 QELMVEHDIGRLPVVEEGKLVGIVTRS 105

CBS_pair_arch2_repeat1

cd04638

Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains present in archaea, ...

194-274

6.48e-12

Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains present in archaea, repeat 1; 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: 341396 [Multi-domain] Cd Length: 109 Bit Score: 62.36 E-value: 6.48e-12

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515637361 194 EGETIVGLITDRDMTKRviahgvSTDSLISEVMTHSPLTVKPDDLVLHAASIMMQFNIRNLPVVKENKVVGLLTTSHLVQ 273
Cdd:cd04638   35 ETGKLVGIVTRKDLLRN------PDEEQIALLMSRDPITISPDDTLSEAAELMLEHNIRRVPVVDDDKLVGIVTVADLVR 108


                 .
gi 515637361 274 N 274
Cdd:cd04638  109 A 109

CBS_pair_GGDEF_PAS_repeat2

cd04611

Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains found in diguanylate ...

153-267

1.40e-11

Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains found in diguanylate cyclase/phosphodiesterase proteins with PAS sensors, repeat 2; 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: 341384 [Multi-domain] Cd Length: 131 Bit Score: 61.97 E-value: 1.40e-11

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515637361 153 LFIRKVEEVASGQVAIVKSEQTIQSVAVEMLHQRSPCAVIYEGETIVGLITDRDMTKRVIAHgvSTDSLISEVMTHSPLT 232
Cdd:cd04611    2 LRLREVGSAMNRSPLVLPGDASLAEAARRMRSHRADAAVIECPDGGLGILTERDLVRFIARH--PGNTPVGELASRPLLT 79

                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 515637361 233 VKPDDLVLHAASIMMQFNIRNLPVVKE-NKVVGLLT 267
Cdd:cd04611   80 VGAEDSLIHARDLLIDHRIRHLAVVDEdGQVTGLLG 115

CBS_pair_MUG70_2

cd17782

Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains similar to MUG70 ...

166-271

2.01e-11

Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains similar to MUG70 repeat2; Two tandem repeats of the cystathionine beta-synthase (CBS pair) domain, present in MUG70. The MUG70 protein, encoded by the Meiotically Up-regulated Gene 70, plays a role in meiosis and contains, beside the two CBS pairs, a PB1 domain. The CBS domain, named after human CBS, is a small domain originally identified in cystathionine beta-synthase and is subsequently found in a wide range of different proteins. CBS domains usually occur in tandem repeats. They associate to form a so-called Bateman domain or a CBS pair based on crystallographic studies in bacteria. The CBS pair was used as a basis for this cd hierarchy since the human CBS proteins can adopt the typical core structure and form an intramolecular CBS pair. The interface between the two CBS domains forms a cleft that is a potential ligand binding site. The CBS pair coexists with a variety of other functional domains and this has been used to help in its classification here. It has been proposed that the CBS domain may play a regulatory role, although its exact function is unknown. Mutations of conserved residues within this domain are associated with a variety of human hereditary diseases, including congenital myotonia, idiopathic generalized epilepsy, hypercalciuric nephrolithiasis, and classic Bartter syndrome (CLC chloride channel family members), Wolff-Parkinson-White syndrome (gamma 2 subunit of AMP-activated protein kinase), retinitis pigmentosa (IMP dehydrogenase-1), and homocystinuria (cystathionine beta-synthase).

Pssm-ID: 341418 [Multi-domain] Cd Length: 118 Bit Score: 61.11 E-value: 2.01e-11

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515637361 166 VAIVKSEQTIQSVAVEMLHQRSPCAVIYEGE-TIVGLITDRDMTKRVIAHGVSTD-SLISEVMTHSPLTVKPDDLVLHAA 243
Cdd:cd17782    4 PPLVSPKTTVREAARLMKENRTTAVLVMDNSgKVIGIFTSKDVVLRVLAAGLDPAtTSVVRVMTPNPETAPPSTTILDAL 83

                         90       100
                 ....*....|....*....|....*....
gi 515637361 244 SIMMQFNIRNLPVV-KENKVVGLLTTSHL 271
Cdd:cd17782   84 HKMHEGKFLNLPVVdDEGEIVGLVDVLQL 112

CBS_pair_bac

cd04630

Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains present in bacteria; ...

158-274

6.22e-11

Pssm-ID: 341393 [Multi-domain] Cd Length: 120 Bit Score: 59.92 E-value: 6.22e-11

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515637361 158 VEEVASGQVAIVKSEQTIQSvAVEMLHQRSPCAVIYE---GETIVGLITDRDMTKRVIAHGVSTDSL-ISEVMTHSPLTV 233
Cdd:cd04630    1 VRDVMKTNVVTIDGLATVRE-ALQLMKEHNVKSLIVEkrhEHDAYGIVTYTDILKKVIAEDRDPDLVnVYEIMTKPAISV 79

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 515637361 234 KPDDLVLHAASIMMQFNIRNLPVVKENKVVGLLTTSHLVQN 274
Cdd:cd04630   80 SPDLDIKYAARLMARFNLKRAPVIENNELIGIVSMTDLVLD 120

CBS_pair_arch

cd17776

Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains present in archaea; ...

166-275

6.82e-11

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

Pssm-ID: 341412 [Multi-domain] Cd Length: 115 Bit Score: 59.73 E-value: 6.82e-11

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515637361 166 VAIVKSEQTIQSVAVEMLHQRSPCAVIYEGETIVGLITDRDmtkrVIAHGVSTDSLISE-----VMTHSPLTVKPDDLVL 240
Cdd:cd17776    5 VVTVDADASLEDAAERMLRNRVGSVVVTDDGTPAGILTETD----ALHAGYATDDPFSEipvraVASRPLVTISPTATLR 80

                         90       100       110
                 ....*....|....*....|....*....|....*
gi 515637361 241 HAASIMMQFNIRNLPVVKENKVVGLLTTSHLVQNH 275
Cdd:cd17776   81 EAAERMVDEGVKKLPVVDGLDLVGILTATDIIRAY 115

CBS_pair_BON_assoc

cd04586

Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with the ...

166-273

9.26e-11

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: 59.75 E-value: 9.26e-11

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515637361 166 VAIVKSEQTIQSVAVEML-HQRS--PcaVIYEGETIVGLITDRDMTKRVIAHGVSTDSLI-------------------- 222
Cdd:cd04586    5 VVTVTPDTSVREAARLLLeHRISglP--VVDDDGKLVGIVSEGDLLRREEPGTEPRRVWWldallesperlaeeyvkahg 82

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....
gi 515637361 223 ---SEVMTHSPLTVKPDDLVLHAASIMMQFNIRNLPVVKENKVVGLLTTSHLVQ 273
Cdd:cd04586   83 rtvGDVMTRPVVTVSPDTPLEEAARLMERHRIKRLPVVDDGKLVGIVSRADLLR 136

CBS_pair_CcpN

cd04617

Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains of CcpN repressor; ...

168-273

2.65e-10

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

Pssm-ID: 341387 [Multi-domain] Cd Length: 125 Bit Score: 58.27 E-value: 2.65e-10

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515637361 168 IVKSEQTIQSVAVEM-LHQRSPCAVIYEGETIVGLITDRDMTKRVIAHGVSTDSLISEVMTHSP--LTVKPDDLVLHAAS 244
Cdd:cd04617    8 VVDETTSVYDAIVTLfLEDVGSLFVVDEEGYLVGVVSRKDLLKATLGGQDLEKTPVSMIMTRMPniVTVTPDDSVLEAAR 87

                         90       100       110
                 ....*....|....*....|....*....|...
gi 515637361 245 IMMQFNIRNLPVVKEN----KVVGLLTTSHLVQ 273
Cdd:cd04617   88 KLIEHEIDSLPVVEKEdgklKVVGRITKTNITR 120

CBS_pair_ABC_OpuCA_assoc

cd04583

Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains found associated with ...

169-272

3.00e-10

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

Pssm-ID: 341360 [Multi-domain] Cd Length: 110 Bit Score: 57.53 E-value: 3.00e-10

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515637361 169 VKSEQTIQSvAVEMLHQRS--PCAVIYEGETIVGLITDRDmtkrvIAHGVSTDSLISEVMTHSPLTVKPDDLVLHAASIM 246
Cdd:cd04583    7 ITPERTLAQ-AIEIMREKRvdSLLVVDKDNVLLGIVDIED-----INRNYRKAKKVGEIMERDVFTVKEDSLLRDTVDRI 80

                         90       100
                 ....*....|....*....|....*..
gi 515637361 247 MQFNIRNLPVV-KENKVVGLLTTSHLV 272
Cdd:cd04583   81 LKRGLKYVPVVdEQGRLVGLVTRASLV 107

CBS_pair_CAP-ED_NT_Pol-beta-like_DUF294_assoc

cd04589

Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with the ...

168-271

3.37e-10

Pssm-ID: 341365 [Multi-domain] Cd Length: 113 Bit Score: 57.58 E-value: 3.37e-10

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515637361 168 IVKSEQTIQSVAVEMLHQRSPCAVIYEGETIVGLITDRDMTKRVIAHGVSTDSLISEVMTHSPLTVKPDDLVLHAASIMM 247
Cdd:cd04589    7 FVDAETSIREATRLMKENGADSLLVRDGDGRVGIVTRTDLRDAVVLDGQPVDTPVGEIATFPLISVEPDDFLFNALLLMT 86

                         90       100
                 ....*....|....*....|....
gi 515637361 248 QFNIRNLPVVKENKVVGLLTTSHL 271
Cdd:cd04589   87 RHRVKRVVVREGEEIVGVLEQTDL 110

CBS

pfam00571

CBS domain; CBS domains are small intracellular modules that pair together to form a stable ...

222-272

5.25e-10

Pssm-ID: 425756 [Multi-domain] Cd Length: 57 Bit Score: 55.30 E-value: 5.25e-10

                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 515637361  222 ISEVMTHSPLTVKPDDLVLHAASIMMQFNIRNLPVVKEN-KVVGLLTTSHLV 272
Cdd:pfam00571   1 VKDIMTKDVVTVSPDTTLEEALELMREHGISRLPVVDEDgKLVGIVTLKDLL 52

CBS_archAMPK_gamma-repeat2

cd04631

CBS pair domains found in archeal 5'-AMP-activated protein kinase gamma subunit-like proteins; ...

157-272

6.79e-10

CBS pair domains found in archeal 5'-AMP-activated protein kinase gamma subunit-like proteins; 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: 341394 [Multi-domain] Cd Length: 130 Bit Score: 57.24 E-value: 6.79e-10

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515637361 157 KVEEVASGQVAIVKSEQTIQSVAVEMLH---QRSPcavIYEGETIVGLITDRDM-----TKRVIAHGVS------TDSLI 222
Cdd:cd04631    1 VVEDYMTKNVITATPGTPIEDVAKIMVRngfRRLP---VVSDGKLVGIVTSTDImrylgSGEAFEKLKTgnihevLNVPI 77

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|
gi 515637361 223 SEVMTHSPLTVKPDDLVLHAASIMMQFNIRNLPVVKENKVVGLLTTSHLV 272
Cdd:cd04631   78 SSIMKRDIITTTPDTDLGEAAELMLEKNIGALPVVDDGKLVGIITERDIL 127

CBS_pair_DRTGG_assoc

cd04596

Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with the ...

184-267

9.49e-10

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

Pssm-ID: 341371 [Multi-domain] Cd Length: 108 Bit Score: 56.32 E-value: 9.49e-10

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515637361 184 HQRSPcaVIYEGETIVGLITDRDMTkrviahGVSTDSLISEVMTHSPLTVKPDDLVLHAASIMMQFNIRNLPVVKEN-KV 262
Cdd:cd04596   25 HSRFP--VVDEENRVVGIVTAKDVI------GKEDDTPIEKVMTKNPITVKPKTSVASAAHMMIWEGIELLPVVDENrKL 96


                 ....*
gi 515637361 263 VGLLT 267
Cdd:cd04596   97 LGVIS 101

Crp

COG0664

cAMP-binding domain of CRP or a regulatory subunit of cAMP-dependent protein kinases [Signal ...

19-148

9.77e-10

cAMP-binding domain of CRP or a regulatory subunit of cAMP-dependent protein kinases [Signal transduction mechanisms];

Pssm-ID: 440428 [Multi-domain] Cd Length: 207 Bit Score: 58.84 E-value: 9.77e-10

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515637361  19 FDKIPKQALRELASNVQITYLGKGDVvdLCESGKE-KSLYIIRTG--SMEQRKSDG--VLRARLGSEDLFG-FTFLDSEV 92
Cdd:COG0664    1 FAGLSDEELEALLAHLELRTLKKGEV--LFREGDPaDHLYFVLSGlvKLYRISEDGreQILGFLGPGDFFGeLSLLGGEP 78

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 515637361  93 NDekgYRAVAIENTLLYVIPHSALQTLFKAFPSCAEHFASQAQVRLKSALDVVWSN 148
Cdd:COG0664   79 SP---ATAEALEDSELLRIPREDLEELLERNPELARALLRLLARRLRQLQERLVSL 131

CBS_pair_GGDEF_assoc

cd04599

Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with the ...

163-271

2.47e-09

Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with the GGDEF (DiGuanylate-Cyclase (DGC)) domain; This cd contains two tandem repeats of the cystathionine beta-synthase (CBS pair) domains in association with the GGDEF (DiGuanylate-Cyclase (DGC)) domain. 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: 341374 [Multi-domain] Cd Length: 107 Bit Score: 55.04 E-value: 2.47e-09

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515637361 163 SGQVAIVKSEQTIQSVAVEMLHQRSPCAVIYEGETIVGLITDRDMTKrviAHgvsTDSLISEVMTHSPLTVKPDDLVLHA 242
Cdd:cd04599    2 TRNPITISPLDSVARAAALMERQRIGGLPVVENGKLVGIITSRDVRR---AH---PNRLVADAMSRNVVTISPEASLWEA 75

                         90       100
                 ....*....|....*....|....*....
gi 515637361 243 ASIMMQFNIRNLPVVKENKVVGLLTTSHL 271
Cdd:cd04599   76 KELMEEHGIERLVVVEEGRLVGIITKSTL 104

CBS_pair_NTP_transferase_assoc

cd04607

Two tandem repeats of the cystathionine beta-synthase (CBS pair) domain associated with the ...

199-273

8.28e-09

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

Pssm-ID: 341381 [Multi-domain] Cd Length: 112 Bit Score: 53.60 E-value: 8.28e-09

                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 515637361 199 VGLITDRDMtKRVIAHGVSTDSLISEVMTHSPLTVKPDDLVLHAASIMMQFNIRNLPVVKE-NKVVGLLTTSHLVQ 273
Cdd:cd04607   38 LGTVTDGDI-RRGLLKGLSLDAPVEEVMNKNPITASPSTSREELLALMRAKKILQLPIVDEqGRVVGLETLDDLLA 112

CBS_pair_peptidase_M50

cd04801

Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains found in the ...

194-272

1.33e-08

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

Pssm-ID: 341401 [Multi-domain] Cd Length: 113 Bit Score: 52.96 E-value: 1.33e-08

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515637361 194 EGETIVGLITDRDmtkrviAHGVSTD----SLISEVMTHSPLTVKPDDLVLHAASIMMQFNIRNLPVVKENKVVGLLTTS 269
Cdd:cd04801   35 ENGRLVGIVTLED------IRKVPEVereaTRVRDVMTKDVITVSPDADAMEALKLMSQNNIGRLPVVEDGELVGIISRT 108


                 ...
gi 515637361 270 HLV 272
Cdd:cd04801  109 DLM 111

CBS_pair_CAP-ED_NT_Pol-beta-like_DUF294_assoc

cd17771

CBS domain protein; This cd contains two tandem repeats of the cystathionine beta-synthase ...

179-266

2.14e-08

CBS domain protein; This cd contains two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with the bacterial CAP_ED (cAMP receptor protein effector domain) family of transcription factors, the NT_Pol-beta-like domain, and the DUF294 domain. Members of CAP_ED, include CAP which binds cAMP, FNR (fumarate and nitrate reductase) which uses an iron-sulfur cluster to sense oxygen, and CooA a heme containing CO sensor. In all cases binding of the effector leads to conformational changes and the ability to activate transcription. The NT_Pol-beta-like domain includes the Nucleotidyltransferase (NT) domains of DNA polymerase beta and other family X DNA polymerases, as well as the NT domains of class I and class II CCA-adding enzymes, RelA- and SpoT-like ppGpp synthetases and hydrolases, 2'5'-oligoadenylate (2-5A)synthetases, Escherichia coli adenylyltransferase (GlnE), Escherichia coli uridylyl transferase (GlnD), poly (A) polymerases, terminal uridylyl transferases, Staphylococcus aureus kanamycin nucleotidyltransferase, and similar proteins. DUF294 is a putative nucleotidyltransferase with a conserved DxD motif. CBS is a small domain originally identified in cystathionine beta-synthase and subsequently found in a wide range of different proteins. The CBS domain, named after human CBS, is a small domain originally identified in cystathionine beta-synthase and is subsequently found in a wide range of different proteins. CBS domains usually occur in tandem repeats. They associate to form a so-called Bateman domain or a CBS pair based on crystallographic studies in bacteria. The CBS pair was used as a basis for this cd hierarchy since the human CBS proteins can adopt the typical core structure and form an intramolecular CBS pair. The interface between the two CBS domains forms a cleft that is a potential ligand binding site. The CBS pair coexists with a variety of other functional domains and this has been used to help in its classification here. It has been proposed that the CBS domain may play a regulatory role, although its exact function is unknown. Mutations of conserved residues within this domain are associated with a variety of human hereditary diseases, including congenital myotonia, idiopathic generalized epilepsy, hypercalciuric nephrolithiasis, and classic Bartter syndrome (CLC chloride channel family members), Wolff-Parkinson-White syndrome (gamma 2 subunit of AMP-activated protein kinase), retinitis pigmentosa (IMP dehydrogenase-1), and homocystinuria (cystathionine beta-synthase).

Pssm-ID: 341407 [Multi-domain] Cd Length: 115 Bit Score: 52.71 E-value: 2.14e-08

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515637361 179 AVEMLHQRS-PCAVIYEGET-IVGLITDRDMTKRVIAHGVSTDSLISEVMTHSPLTVKPDDLVLHAASIMMQFNIRNLPV 256
Cdd:cd17771   18 ALETMHERRvGSMVVVDANRrPVGIFTLRDLLSRVALPQIDLDAPISEVMTPDPVRLPPSASAFEAALLMAEHGFRHVCV 97

                         90
                 ....*....|
gi 515637361 257 VKENKVVGLL 266
Cdd:cd17771   98 VDNGRLVGVV 107

CBS_pair_ParBc_assoc

cd04610

Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with a ...

198-272

2.57e-08

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

Pssm-ID: 341383 [Multi-domain] Cd Length: 108 Bit Score: 52.32 E-value: 2.57e-08

                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 515637361 198 IVGLITDRDMtkrVIAHgvsTDSLISEVMTHSPLTVKPDDLVLHAASIMMQFNIRNLPVV-KENKVVGLLTTSHLV 272
Cdd:cd04610   37 VVGYVTAKDL---LGKD---DDEKVSEIMSRDTVVADPDMDITDAARVIFRSGISKLPVVdDEGNLVGIITNMDVI 106

CBS_arch_repeat2

cd17778

CBS pair domains found in archeal proteins, repeat 2; CBS pair domains found in archeal ...

157-267

3.34e-08

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

Pssm-ID: 341414 [Multi-domain] Cd Length: 131 Bit Score: 52.33 E-value: 3.34e-08

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515637361 157 KVEEVASGQVAIVKSEQTIQSVAVEMLHQ---RSPcavIYEGETIVGLITDRDMTKRVIAHGVSTDSL-----------I 222
Cdd:cd17778    1 KVKEFMTTPVVTIYPDDTLKEAMELMVTRgfrRLP---VVSGGKLVGIVTAMDIVKYFGSHEAKKRLTtgdideaystpV 77

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 515637361 223 SEVMTHSPLTVKPDDLVLHAASIMMQFNIRNLPVV-KENKVVGLLT 267
Cdd:cd17778   78 EEIMSKEVVTIEPDADIAEAARLMIKKNVGSLLVVdDEGELKGIIT 123

CBS_arch_repeat2

cd17778

CBS pair domains found in archeal proteins, repeat 2; CBS pair domains found in archeal ...

222-293

4.42e-08

Pssm-ID: 341414 [Multi-domain] Cd Length: 131 Bit Score: 51.95 E-value: 4.42e-08

                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 515637361 222 ISEVMTHSPLTVKPDDLVLHAASIMMQFNIRNLPVVKENKVVGLLTTSHLVQN---HRVQAIFLIEKIKYAGSVK 293
Cdd:cd17778    2 VKEFMTTPVVTIYPDDTLKEAMELMVTRGFRRLPVVSGGKLVGIVTAMDIVKYfgsHEAKKRLTTGDIDEAYSTP 76

CBS_pair_DHH_polyA_Pol_assoc

cd17772

Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with the ...

198-267

5.85e-08

Pssm-ID: 341408 [Multi-domain] Cd Length: 112 Bit Score: 51.03 E-value: 5.85e-08

                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515637361 198 IVGLITDRDMTKrVIAHGVStDSLISEVMTHSPLTVKPDDLVLHAASIMMQFNIRNLPVVKENKVVGLLT 267
Cdd:cd17772   38 LVGIITRQVAEK-AIYHGLG-DLPVSEYMTTEFATVTPDAPLSEIQEIIVEQRQRLVPVVEDGRLVGVIT 105

CAP_ED

cd00038

effector domain of the CAP family of transcription factors; members include CAP (or cAMP ...

18-125

6.57e-08

Pssm-ID: 237999 [Multi-domain] Cd Length: 115 Bit Score: 51.17 E-value: 6.57e-08

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515637361  18 PFDKIPKQALRELASNVQITYLGKGDVVdLCESGKEKSLYIIRTGSME--QRKSDG--VLRARLGSEDLFGFTFLDSevN 93
Cdd:cd00038    1 LFSGLDDEELEELADALEERRFPAGEVI-IRQGDPADSLYIVLSGSVEvyKLDEDGreQIVGFLGPGDLFGELALLG--N 77

                         90       100       110
                 ....*....|....*....|....*....|..
gi 515637361  94 DEKGYRAVAIENTLLYVIPHSALQTLFKAFPS 125
Cdd:cd00038   78 GPRSATVRALTDSELLVLPRSDFRRLLQEYPE 109

CBS_pair_voltage-gated_CLC_euk_bac

cd04592

Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with the ...

163-267

1.53e-07

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

Pssm-ID: 341368 [Multi-domain] Cd Length: 128 Bit Score: 50.44 E-value: 1.53e-07

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515637361 163 SGQVAIVKSEQTIQSVAVEMLHQRSPCAVIY-EGETIVGLITDRDMtKRVIAHGVST-----DSLISEVMTHS------P 230
Cdd:cd04592    2 STRYITVLMSTTLKEAVLLMLEEKQSCALIVdSDDFLIGILTLGDI-QRFLKRAKADnedpkTILVSSICTRNggycrgL 80

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 515637361 231 LTVKPDDLVLHAASIMMQFNIRNLPVVKEN------KVVGLLT 267
Cdd:cd04592   81 WTCTPDMDLLTAKMLMEARGINQLPVVKRGgeerrrRVVGLLD 123

CBS_pair_BON_assoc

cd04586

Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with the ...

226-324

3.47e-07

Pssm-ID: 341362 [Multi-domain] Cd Length: 137 Bit Score: 49.74 E-value: 3.47e-07

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515637361 226 MTHSPLTVKPDDLVLHAASIMMQFNIRNLPVV-KENKVVGLLTTSHLVqnHRvqaifliEKIKYAGSVKTMSSFTSERQA 304
Cdd:cd04586    1 MTTDVVTVTPDTSVREAARLLLEHRISGLPVVdDDGKLVGIVSEGDLL--RR-------EEPGTEPRRVWWLDALLESPE 71

                         90       100
                 ....*....|....*....|
gi 515637361 305 IFEALVEgKVAPETVGKVMT 324
Cdd:cd04586   72 RLAEEYV-KAHGRTVGDVMT 90

CBS_pair_GGDEF_assoc

cd04599

Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with the ...

226-275

3.87e-07

Pssm-ID: 341374 [Multi-domain] Cd Length: 107 Bit Score: 48.88 E-value: 3.87e-07

                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|
gi 515637361 226 MTHSPLTVKPDDLVLHAASIMMQFNIRNLPVVKENKVVGLLTTSHLVQNH 275
Cdd:cd04599    1 MTRNPITISPLDSVARAAALMERQRIGGLPVVENGKLVGIITSRDVRRAH 50

CBS_pair_HRP1_like

cd04622

CBS pair domain found in Hypoxic Response Protein 1 (HRP1) -like proteinds; Mycobacterium ...

226-267

1.05e-06

Pssm-ID: 341390 [Multi-domain] Cd Length: 115 Bit Score: 47.80 E-value: 1.05e-06

                         10        20        30        40
                 ....*....|....*....|....*....|....*....|..
gi 515637361 226 MTHSPLTVKPDDLVLHAASIMMQFNIRNLPVVKENKVVGLLT 267
Cdd:cd04622    1 MTRDVVTVSPDTTLREAARLMRDLDIGALPVCEGDRLVGMVT 42

IMPDH

pfam00478

IMP dehydrogenase / GMP reductase domain; This family is involved in biosynthesis of guanosine ...

155-267

1.07e-06

IMP dehydrogenase / GMP reductase domain; This family is involved in biosynthesis of guanosine nucleotide. Members of this family contain a TIM barrel structure. In the inosine monophosphate dehydrogenases 2 CBS domains pfam00571 are inserted in the TIM barrel. This family is a member of the common phosphate binding site TIM barrel family.

Pssm-ID: 459826 [Multi-domain] Cd Length: 463 Bit Score: 51.62 E-value: 1.07e-06

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515637361  155 IRKVEEVASGQVA---IVKSEQTIQSVAVEMLHQRSPCAVIYEGETIVGLITDRDMtkRVIAHgvsTDSLISEVMTHSPL 231
Cdd:pfam00478  76 VRKVKRSESGMITdpvTLSPDATVADALALMERYGISGVPVVDDGKLVGIVTNRDL--RFETD---LSQPVSEVMTKENL 150

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 515637361  232 TVKPDDLVL-HAASIMMQFNIRNLPVV-KENKVVGLLT 267
Cdd:pfam00478 151 VTAPEGTTLeEAKEILHKHKIEKLPVVdDNGRLVGLIT 188

CBS_two-component_sensor_histidine_kinase_repeat2

cd17774

2 tandem repeats of the CBS domain in the two-component sensor histidine kinase and ...

160-273

1.46e-06

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

Pssm-ID: 341410 [Multi-domain] Cd Length: 137 Bit Score: 47.92 E-value: 1.46e-06

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515637361 160 EVASGQVAIVKSEQTIQSVAVEMLHQRSPCAVIYEGETI--------VGLITDRDMTKrVIAHGVSTDSLI-SEVMTHSP 230
Cdd:cd17774    1 EVMTTRVIHAPPTASVLELAQLMAEHRVSCVVIVEEDEQqeknklipVGIVTERDIVQ-FQALGLDLSQTQaQTVMSSPL 79

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 515637361 231 LTVKPDDLVLHAASIMMQFNIRNLPVVKE-NKVVGLLTTSHLVQ 273
Cdd:cd17774   80 FSLRPDDSLWTAHQLMQQRRIRRLVVVGEqGELLGIVTQTSLLQ 123

CBS_pair_GGDEF_PAS_repeat1

cd09833

Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains found in diguanylate ...

172-274

1.66e-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: 47.22 E-value: 1.66e-06

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515637361 172 EQTIQSVAVEMLHQRSPCAVIYEGETIVGLITDRDMTKRVIAHGVSTDSLISEVMTHSPLTVKPDDLVLHAASIMMQFNI 251
Cdd:cd09833   13 DTPLADAAARMAERRCSSILIVENGEIVGIWTERDALKLDFSDPDAFRRPISEVMSSPVLTIPQDTTLGEAAVRFRQEGV 92

                         90       100
                 ....*....|....*....|....
gi 515637361 252 RNLPVVKE-NKVVGLLTTSHLVQN 274
Cdd:cd09833   93 RHLLVVDDdGRPVGIVSQTDVVLN 116

CBS_pair_CBS

cd04608

Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with the ...

219-278

2.62e-06

Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with the pyridoxal-phosphate (PALP) dependent enzyme domain; This cd contains two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with the pyridoxal-phosphate (PALP) dependent enzyme domain upstream. Cystathionine beta-synthase (CBS ) contains, besides the C-terminal regulatory CBS-pair, an N-terminal heme-binding module, followed by a pyridoxal phosphate (PLP) domain, which houses the active site. It is the first enzyme in the transsulfuration pathway, catalyzing the conversion of serine and homocysteine to cystathionine and water. In general, 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: 341382 [Multi-domain] Cd Length: 120 Bit Score: 46.76 E-value: 2.62e-06

                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 515637361 219 DSLISEVMTHSPLTVKPDDLVLHAASIMMQFNIRNLPVVKE-NKVVGLLTTSHL---VQNHRVQ 278
Cdd:cd04608    1 DLIVRRLDLGAPVTVLPDDTLGEAIEIMREYGVDQLPVVDEdGRVVGMVTEGNLlssLLAGRAQ 64

CBS_pair_inorgPPase

cd04597

Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with ...

190-272

3.53e-06

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: 45.80 E-value: 3.53e-06

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515637361 190 AVIYEGETIVGLITDRDmtkrvIAHGVSTdsliseVMTHS-PLTVKPDDLVLHAASIMMQFNIRNLPVVKE-NKVVGLLT 267
Cdd:cd04597   32 PVTDDNGKLIGLLSISD-----IARTVDY------IMTKDnLIVFKEDDYLDEVKEIMLNTNFRNYPVVDEnNKFLGTIS 100


                 ....*
gi 515637361 268 TSHLV 272
Cdd:cd04597  101 RKHLI 105

CBS_pair_plant_CBSX

cd17789

Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains from plant CBSX ...

163-273

5.00e-06

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: 46.31 E-value: 5.00e-06

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515637361 163 SGQVAIVKSEQTIQSvAVEMLHQR--SPCAVIYEGETIVGLITDRDMTKRVIAHGVSTDS-------------------- 220
Cdd:cd17789    2 KGKLHVVKPNTTVDE-ALELLVENriTGLPVIDEDWRLVGVVSDYDLLALDSISGRSQTDnnfppadstwktfnevqkll 80

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 515637361 221 ------LISEVMTHSPLTVKPDDLVLHAASIMMQFNIRNLPVVKEN-KVVGLLTTSHLVQ 273
Cdd:cd17789   81 sktngkVVGDVMTPSPLVVREKTNLEDAARILLETKFRRLPVVDSDgKLVGIITRGNVVR 140

CBS_pair_IMPDH

cd04601

Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains in the inosine 5' ...

169-267

5.74e-06

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

Pssm-ID: 341376 [Multi-domain] Cd Length: 110 Bit Score: 45.48 E-value: 5.74e-06

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515637361 169 VKSEQTIQSVAVEMLHQRSPC-AVIYEGETIVGLITDRDMtkRVIAhgvSTDSLISEVMT-HSPLTVKPDDLVL-HAASI 245
Cdd:cd04601    7 LSPDATVADVLELKAEYGISGvPVTEDGGKLVGIVTSRDI--RFET---DLSTPVSEVMTpDERLVTAPEGITLeEAKEI 81

                         90       100
                 ....*....|....*....|...
gi 515637361 246 MMQFNIRNLPVV-KENKVVGLLT 267
Cdd:cd04601   82 LHKHKIEKLPIVdDNGELVGLIT 104

CBS_pair_SF

cd02205

Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains superfamily; The CBS ...

227-273

7.94e-06

Pssm-ID: 341358 [Multi-domain] Cd Length: 113 Bit Score: 45.31 E-value: 7.94e-06

                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*...
gi 515637361 227 THSPLTVKPDDLVLHAASIMMQFNIRNLPVVKEN-KVVGLLTTSHLVQ 273
Cdd:cd02205    1 TRDVVTVDPDTTVREALELMAENGIGALPVVDDDgKLVGIVTERDILR 48

CBS

smart00116

Domain in cystathionine beta-synthase and other proteins; Domain present in all 3 forms of ...

230-274

9.45e-06

Pssm-ID: 214522 [Multi-domain] Cd Length: 49 Bit Score: 42.89 E-value: 9.45e-06

                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*.
gi 515637361   230 PLTVKPDDLVLHAASIMMQFNIRNLPVVKE-NKVVGLLTTSHLVQN 274
Cdd:smart00116   2 VVTVSPDTTLEEALELLRENGIRRLPVVDEeGRLVGIVTRRDIIKA 47

PRK14869

putative manganese-dependent inorganic diphosphatase;

222-271

1.18e-05

putative manganese-dependent inorganic diphosphatase;

Pssm-ID: 237843 [Multi-domain] Cd Length: 546 Bit Score: 48.29 E-value: 1.18e-05

                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|.
gi 515637361 222 ISEVMTHSPLTVKPDDLVLHAASIMMQFNIRNLPVV-KENKVVGLLTTSHL 271
Cdd:PRK14869  70 VRDLEIDKPVTVSPDTSLKEAWNLMDENNVKTLPVVdEEGKLLGLVSLSDL 120

CBS_arch_repeat1

cd17777

CBS pair domains found in archeal proteins, repeat 1; CBS pair domains found in archeal ...

159-272

1.40e-05

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

Pssm-ID: 341413 [Multi-domain] Cd Length: 137 Bit Score: 45.03 E-value: 1.40e-05

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515637361 159 EEVASGQVAIVKSEQTIQSVAVEMLHQRSPCAVIYEGETIVGLITDRDM---------TKRVIA-HGVSTDSL-----IS 223
Cdd:cd17777    5 MIIASPPVLSISPSAPILSAFEKMNRRGIRRLVVVDENKLEGILSARDLvsylgggclFKIVESrHQGDLYSAlnrevVE 84

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|
gi 515637361 224 EVMTHSPLTVKPDDLVLHAASIMMQFNIRNLPVV-KENKVVGLLTTSHLV 272
Cdd:cd17777   85 TIMTPNPVYVYEDSDLIEALTIMVTRGIGSLPVVdRDGRPVGIVTERDLV 134

CBS_pair_Mg_transporter

cd04606

Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains in the magnesium ...

169-267

1.42e-05

Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains in the magnesium transporter, MgtE; This cd contains two tandem repeats of the cystathionine beta-synthase (CBS pair) domain in the magnesium transporter, MgtE. MgtE and its homologs are found in eubacteria, archaebacteria, and eukaryota. Members of this family transport Mg2+ or other divalent cations into the cell via two highly conserved aspartates. The CBS domain, named after human CBS, is a small domain originally identified in cystathionine beta-synthase and is subsequently found in a wide range of different proteins. CBS domains usually occur in tandem repeats. They associate to form a so-called Bateman domain or a CBS pair based on crystallographic studies in bacteria. The CBS pair was used as a basis for this cd hierarchy since the human CBS proteins can adopt the typical core structure and form an intramolecular CBS pair. The interface between the two CBS domains forms a cleft that is a potential ligand binding site. The CBS pair coexists with a variety of other functional domains and this has been used to help in its classification here. It has been proposed that the CBS domain may play a regulatory role, although its exact function is unknown. Mutations of conserved residues within this domain are associated with a variety of human hereditary diseases, including congenital myotonia, idiopathic generalized epilepsy, hypercalciuric nephrolithiasis, and classic Bartter syndrome (CLC chloride channel family members), Wolff-Parkinson-White syndrome (gamma 2 subunit of AMP-activated protein kinase), retinitis pigmentosa (IMP dehydrogenase-1), and homocystinuria (cystathionine beta-synthase).

Pssm-ID: 341380 [Multi-domain] Cd Length: 121 Bit Score: 44.63 E-value: 1.42e-05

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515637361 169 VKSEQTIQsVAVEMLHQRSP-------CAVIYEGETIVGLITDRDMtkrVIAhgvSTDSLISEVMTHSPLTVKPDDLVLH 241
Cdd:cd04606   14 VRPDWTVE-EALEYLRRLAPdpetiyyIYVVDEDRRLLGVVSLRDL---LLA---DPDTKVSDIMDTDVISVSADDDQEE 86

                         90       100
                 ....*....|....*....|....*..
gi 515637361 242 AASIMMQFNIRNLPVV-KENKVVGLLT 267
Cdd:cd04606   87 VARLFAKYDLLALPVVdEEGRLVGIIT 113

PRK14869

putative manganese-dependent inorganic diphosphatase;

159-280

1.66e-05

putative manganese-dependent inorganic diphosphatase;

Pssm-ID: 237843 [Multi-domain] Cd Length: 546 Bit Score: 47.90 E-value: 1.66e-05

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515637361 159 EEVASGQVAIVKSEQTIQSVAVEMlhqRSPCAVIYEGETIvglitDRDMTKRVIAHGVS----------TDSLI------ 222
Cdd:PRK14869 177 ERIEEGDIVIVGDREDIQLAAIEA---GVRLLIITGGAPV-----SEDVLELAKENGVTvistpydtftTARLInqsipv 248

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 515637361 223 SEVMTHS-PLTVKPDDLVLHAASIMMQFNIRNLPVV-KENKVVGLLTTSHLVQNHRVQAI 280
Cdd:PRK14869 249 SYIMTTEdLVTFSKDDYLEDVKEVMLKSRYRSYPVVdEDGKVVGVISRYHLLSPVRKKVI 308

CBS_pair_Euryarchaeota

cd17784

Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains present in ...

181-267

1.86e-05

Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains present in Euryarchaeota; 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: 341420 [Multi-domain] Cd Length: 120 Bit Score: 44.33 E-value: 1.86e-05

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515637361 181 EMLHQR-SPCAVIYEGETIVGLITDRDMTKRVIAHGVSTDSLISEVMTHSPLTVKPDDLVLHAASIMMQF----NIRN-L 254
Cdd:cd17784   19 KMLKHKiSALPVVDDEGKLIGIVTATDLGHNLILDKYELGTTVEEVMVKDVATVHPDETLLEAIKKMDSNapdeEIINqL 98

                         90
                 ....*....|...
gi 515637361 255 PVVKENKVVGLLT 267
Cdd:cd17784   99 PVVDDGKLVGIIS 111

CBS_pair_HPP_assoc

cd04600

Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with the ...

226-324

4.28e-05

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: 43.70 E-value: 4.28e-05

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515637361 226 MTHSPLTVKPDDLVLHAASIMMQFNIRNLPVVKEN-KVVGLLTTSHLVQNHRVQAifliekikyagsvktmssFTSERQA 304
Cdd:cd04600    1 MSRDVVTVTPDTSLEEAWRLLRRHRIKALPVVDRArRLVGIVTLADLLKHADLDP------------------PRGLRGR 62

                         90       100
                 ....*....|....*....|
gi 515637361 305 IFEALVEGKVAPETVGKVMT 324
Cdd:cd04600   63 LRRTLGLRRDRPETVGDIMT 82

CBS_pair_arch2_repeat2

cd04614

Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains present in archaea, ...

172-272

4.42e-05

Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains present in archaea, repeat 2; This cd contains two tandem repeats of the cystathionine beta-synthase (CBS pair) domains found in Inosine monophosphate (IMP) dehydrogenases and related proteins including IMP dehydrogenase IX from Methanothermobacter. IMP dehydrogenase is an essential enzyme in the de novo biosynthesis of Guanosine monophosphate (GMP), catalyzing the NAD-dependent oxidation of IMP to xanthosine monophosphate (XMP). 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: 341386 [Multi-domain] Cd Length: 150 Bit Score: 43.81 E-value: 4.42e-05

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515637361 172 EQTIQSVAVE-MLHQRSPCAVIYEGE-TIVGLITDRDM-TKRVIAHGVS------------------------------- 217
Cdd:cd04614   11 DETPLPVALRaMRLANVPAAPVLDSEgKLVGIVTERDLiDVSRIVESEEesgmsiaddedewswegirdvmslyyptsnv 90

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 515637361 218 --TDSLISEVMTHSPLTVKPDDLVLHAASIMMQFNIRNLPVVK-ENKVVGLLTTSHLV 272
Cdd:cd04614   91 elPDKPVKDVMTKDVVTAFPSSTVSEAAKKMIRNDIEQLPVVSgEGDLAGMLRDVDLL 148

cNMP_binding

pfam00027

Cyclic nucleotide-binding domain; This domain sensor domain can bind cAMP, cGMP, c-di-GMP, ...

38-121

4.89e-05

Pssm-ID: 459637 [Multi-domain] Cd Length: 89 Bit Score: 42.21 E-value: 4.89e-05

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515637361   38 YLGKGDVvdLCESGKE-KSLYIIRTGSME--QRKSDG--VLRARLGSEDLFGF-TFLDSEVNDekgYRAVAIENTLLYVI 111
Cdd:pfam00027   3 SYKAGEV--IFREGDPaDSLYIVLSGKVKvyRTLEDGreQILAVLGPGDFFGElALLGGEPRS---ATVVALTDSELLVI 77

                          90
                  ....*....|
gi 515637361  112 PHSALQTLFK 121
Cdd:pfam00027  78 PREDFLELLE 87

CBS_pair_bac

cd04629

Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains present in bacteria; ...

226-267

9.43e-05

Pssm-ID: 341392 [Multi-domain] Cd Length: 116 Bit Score: 42.04 E-value: 9.43e-05

                         10        20        30        40
                 ....*....|....*....|....*....|....*....|...
gi 515637361 226 MTHSPLTVKPDDLVLHAASIMMQFNIRNLPVV-KENKVVGLLT 267
Cdd:cd04629    1 MTRNPVTLTPDTSILEAVELLLEHKISGAPVVdEQGRLVGFLS 43

cNMP

smart00100

Cyclic nucleotide-monophosphate binding domain; Catabolite gene activator protein (CAP) is a ...

18-131

1.74e-04

Pssm-ID: 197516 [Multi-domain] Cd Length: 120 Bit Score: 41.62 E-value: 1.74e-04

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515637361    18 PFDKIPKQALRELASNVQITYLGKGDVVdlCESGKE-KSLYIIRTGSMEQRKSD----GVLRARLGSEDLFGFTFLdseV 92
Cdd:smart00100   1 LFKNLDAEELRELADALEPVRYPAGEVI--IRQGDVgDSFYIIVSGEVEVYKVLedgeEQIVGTLGPGDFFGELAL---L 75

                           90       100       110
                   ....*....|....*....|....*....|....*....
gi 515637361    93 NDEKGYRAVAIENTLLYVIPHSALQTLFKAFPSCAEHFA 131
Cdd:smart00100  76 TNSRRAASAAAVALELATLLRIDFRDFLQLLPELPQLLL 114

CBS_pair_archHTH_assoc

cd04588

Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains found in archaea and ...

227-269

2.12e-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: 40.98 E-value: 2.12e-04

                         10        20        30        40
                 ....*....|....*....|....*....|....*....|...
gi 515637361 227 THSPLTVKPDDLVLHAASIMMQFNIRNLPVVKENKVVGLLTTS 269
Cdd:cd04588    1 SKDLITLKPDATIKDAAKLLSENNIHGAPVVDDGKLVGIVTLT 43

CBS_pair_Euryarchaeota

cd17784

Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains present in ...

227-274

4.26e-04

Pssm-ID: 341420 [Multi-domain] Cd Length: 120 Bit Score: 40.48 E-value: 4.26e-04

                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*....
gi 515637361 227 THSPLTVKPDDLVLHAASIMMQFNIRNLPVV-KENKVVGLLTTSHLVQN 274
Cdd:cd17784    1 TKNVITAKPNEGVVEAFEKMLKHKISALPVVdDEGKLIGIVTATDLGHN 49

CBS_pair_bac_arch

cd17785

Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains present in bacteria ...

167-266

4.36e-04

Pssm-ID: 341421 [Multi-domain] Cd Length: 136 Bit Score: 40.72 E-value: 4.36e-04

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515637361 167 AIVKSEQTIQSVAVEMLhqRSPCA----VIYEGETIVGLITDRDMTKRVIAHG---------------VSTDSLISEVMT 227
Cdd:cd17785   13 SVVHENTSIRDVIDKMI--EDPKTrsvyVVDDDEKLLGIITLMELLKYIGYRFgvtiykgvsfglllrISLKEKAKDIML 90

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 515637361 228 HsPLTVKPDDLVLHAASIMMQFNIRNLPVVKEN-KVVGLL 266
Cdd:cd17785   91 S-PIYVKKEDTLEEALELMVKNRLQELPVVDENgKVIGDL 129

CBS_archAMPK_gamma-repeat1

cd17779

signal transduction protein with CBS domains; Archeal gamma-subunit of 5'-AMP-activated ...

222-267

5.18e-04

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: 40.68 E-value: 5.18e-04

                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*..
gi 515637361 222 ISEVMTHSPLTVKPDDLVLHAASIMMQFNIRNLPVV-KENKVVGLLT 267
Cdd:cd17779   82 VREIMTRDVISVKENASIDDAIELMLEKNVGGLPIVdKDGKVIGIVT 128

PRK10892

arabinose-5-phosphate isomerase KdsD;

169-266

5.83e-04

arabinose-5-phosphate isomerase KdsD;

Pssm-ID: 182814 [Multi-domain] Cd Length: 326 Bit Score: 42.40 E-value: 5.83e-04

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515637361 169 VKSEQTIQSVAVEMLHQRSPCAVIYEGET-IVGLITDRDMtKRVIAHGVSTDSL-ISEVMTHSPLTVKPDDLVLHAASIM 246
Cdd:PRK10892 217 VSKTASLRDALLEITRKNLGMTVICDDNMkIEGIFTDGDL-RRVFDMGIDLRQAsIADVMTPGGIRVRPGILAVDALNLM 295

                         90       100
                 ....*....|....*....|
gi 515637361 247 MQFNIRNLPVVKENKVVGLL 266
Cdd:PRK10892 296 QSRHITSVLVADGDHLLGVL 315

CBS_pair_voltage-gated_CLC_bac

cd04613

Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with the ...

191-273

6.94e-04

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

Pssm-ID: 341385 [Multi-domain] Cd Length: 119 Bit Score: 39.87 E-value: 6.94e-04

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515637361 191 VIYEGETIVGLITDRDMTKRVIAHGVSTDSLISEVMTHSPLTVKPDDlVLHAAsiMMQFNIRN---LPVVKE---NKVVG 264
Cdd:cd04613   31 VVDEQGRLTGILSIQDVRGVLFEEELWDLVVVKDLATTDVITVTPDD-DLYTA--LLKFTSTNldqLPVVDDddpGKVLG 107


                 ....*....
gi 515637361 265 LLTTSHLVQ 273
Cdd:cd04613  108 MLSRRDVIA 116

MgtE

COG2239

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

169-267

7.31e-04

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

Pssm-ID: 441840 [Multi-domain] Cd Length: 443 Bit Score: 42.36 E-value: 7.31e-04

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515637361 169 VKSEQTIQsVAVEMLHQRSPcaviyEGETIVGL-ITDRDMT-------KRVIAHgvSTDSLISEVMTHSPLTVKPDDLVL 240
Cdd:COG2239  142 VREDWTVG-EALRYLRRQAE-----DPETIYYIyVVDDDGRlvgvvslRDLLLA--DPDTKVSDIMDTDVISVPADDDQE 213

                         90       100
                 ....*....|....*....|....*...
gi 515637361 241 HAASIMMQFNIRNLPVV-KENKVVGLLT 267
Cdd:COG2239  214 EVARLFERYDLLALPVVdEEGRLVGIIT 241

CBS_pair_bac

cd17783

Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains present in bacteria; ...

232-271

8.44e-04

Pssm-ID: 341419 [Multi-domain] Cd Length: 108 Bit Score: 39.09 E-value: 8.44e-04

                         10        20        30        40
                 ....*....|....*....|....*....|....*....|
gi 515637361 232 TVKPDDLVLHAASIMMQFNIRNLPVVKENKVVGLLTTSHL 271
Cdd:cd17783    6 PLKPTDSVEKALDWMEEFRVSQLPVVDNGQYLGLISEDDL 45

CBS_pair_arch

cd09836

Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains; The CBS domain, ...

226-272

1.02e-03

Pssm-ID: 341405 [Multi-domain] Cd Length: 116 Bit Score: 39.04 E-value: 1.02e-03

                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*...
gi 515637361 226 MTHSPLTVKPDDLVLHAASIMMQFNIRNLPVV-KENKVVGLLTTSHLV 272
Cdd:cd09836    1 MSKPVVTVPPETTIREAAKLMAENNIGSVVVVdDDGKPVGIVTERDIV 48

CBS_pair_DHH_polyA_Pol_assoc

cd17772

Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with the ...

227-267

1.32e-03

Pssm-ID: 341408 [Multi-domain] Cd Length: 112 Bit Score: 38.70 E-value: 1.32e-03

                         10        20        30        40
                 ....*....|....*....|....*....|....*....|...
gi 515637361 227 THSPLTVKPDDLVLHAASIMMQFNIRNLPVVKEN--KVVGLLT 267
Cdd:cd17772    1 SSPVISVEPDTTIAEAAELMTRYNINALPVVDGGtgRLVGIIT 43

CBS_pair_voltage-gated_CLC_euk_bac

cd04591

Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with the ...

158-267

1.75e-03

Pssm-ID: 341367 [Multi-domain] Cd Length: 114 Bit Score: 38.65 E-value: 1.75e-03

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515637361 158 VEEVASGQVAIVKSEQTIQSVaVEMLHQRS----PCAVIYEGETIVGLITDRDMtkrVIAHGVStdslISEVMTHSPLTV 233
Cdd:cd04591    2 AEDVMRPPLTVLARDETVGDI-VSVLKTTDhngfPVVDSTESQTLVGFILRSQL---ILLLEAD----LRPIMDPSPFTV 73

                         90       100       110
                 ....*....|....*....|....*....|....
gi 515637361 234 KPDDLVLHAASIMMQFNIRNLPVVKENKVVGLLT 267
Cdd:cd04591   74 TEETSLEKVHDLFRLLGLRHLLVTNNGRLVGIVT 107

CBS_pair_IMPDH

cd04601

Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains in the inosine 5' ...

229-268

1.81e-03

Pssm-ID: 341376 [Multi-domain] Cd Length: 110 Bit Score: 38.16 E-value: 1.81e-03

                         10        20        30        40
                 ....*....|....*....|....*....|....*....|.
gi 515637361 229 SPLTVKPDDLVLHAASIMMQFNIRNLPVVKE-NKVVGLLTT 268
Cdd:cd04601    3 DPVTLSPDATVADVLELKAEYGISGVPVTEDgGKLVGIVTS 43

CBS_pair_arch_MET2_assoc

cd04605

Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with the ...

221-267

2.65e-03

Pssm-ID: 341379 [Multi-domain] Cd Length: 116 Bit Score: 37.99 E-value: 2.65e-03

                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*...
gi 515637361 221 LISEVMTHSPLTVKPDDLVLHAASIMMQFNIRNLPVV-KENKVVGLLT 267
Cdd:cd04605    1 LVEDIMSKDVATIREDISIEEAAKIMIDKNVTHLPVVsEDGKLIGIVT 48

CBS_pair_inorgPPase

cd04597

Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with ...

230-271

2.77e-03

Pssm-ID: 341372 [Multi-domain] Cd Length: 106 Bit Score: 37.71 E-value: 2.77e-03

                         10        20        30        40
                 ....*....|....*....|....*....|....*....|...
gi 515637361 230 PLTVKPDDLVLHAASIMMQFNIRNLPVV-KENKVVGLLTTSHL 271
Cdd:cd04597    7 VEPLSPETSIKDAWNLMDENNLKTLPVTdDNGKLIGLLSISDI 49

gutQ

PRK11543

arabinose-5-phosphate isomerase GutQ;

190-274

3.27e-03

arabinose-5-phosphate isomerase GutQ;

Pssm-ID: 183186 [Multi-domain] Cd Length: 321 Bit Score: 40.14 E-value: 3.27e-03

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515637361 190 AVIYEGETIVGLITDRDMtKRVIAHGVSTDSLISEVMTHSPLTVKPDDLVLHAASIMMQFNIRNLPVVKEN-KVVGLLTT 268
Cdd:PRK11543 234 AVCDAQQQVQGVFTDGDL-RRWLVGGGALTTPVNEAMTRGGTTLQAQSRAIDAKEILMKRKITAAPVVDENgKLTGAINL 312


                 ....*.
gi 515637361 269 SHLVQN 274
Cdd:PRK11543 313 QDFYQA 318

CBS_pair_arch1_repeat2

cd04632

Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains present in archaea, ...

191-267

4.86e-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: 37.70 E-value: 4.86e-03

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515637361 191 VIYEGETIVGLITDRDMTKRVIAHGVST-------------DSLISEVMTHSPLTVKPDDLVLHAASIMMQFNIRNLPVV 257
Cdd:cd04632   30 VVDDNGKLVGIVTTYDIVDFVVRPGTKTrggdrggekermlDLPVYDIMSSPVVTVTRDATVADAVERMLENDISGLVVT 109

                         90
                 ....*....|.
gi 515637361 258 KE-NKVVGLLT 267
Cdd:cd04632  110 PDdNMVIGILT 120

CBS_pair_arch1_repeat1

cd17780

Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains present in archaea, ...

191-271

5.96e-03

Pssm-ID: 341416 [Multi-domain] Cd Length: 106 Bit Score: 36.94 E-value: 5.96e-03

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515637361 191 VIYEGETIVGLITDRDMTKrviAHgVSTDSLISEVMTHSPlTVKPDDLVLHAASIMMQFNIRNLPVVKENKVVGLLTTSH 270
Cdd:cd17780   29 VVTDDGEYEGVVTERQLLQ---SH-VEDDAKVGALVRAAP-KVDRTEDVREVARLLVEGGTKVAPVFEGGSLWGVVTADA 103


                 .
gi 515637361 271 L 271
Cdd:cd17780  104 I 104

CBS_pair_CBS

cd04608

Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with the ...

157-237

7.03e-03

Pssm-ID: 341382 [Multi-domain] Cd Length: 120 Bit Score: 36.74 E-value: 7.03e-03

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515637361 157 KVEEVASGQVAIVKSEQTIQSvAVEMLHQRS----PcaVIYEGETIVGLITDRDMTKRVIAHGVSTDSLISEVMTHSPLT 232
Cdd:cd04608    3 IVRRLDLGAPVTVLPDDTLGE-AIEIMREYGvdqlP--VVDEDGRVVGMVTEGNLLSSLLAGRAQPSDPVSKAMYKQFKQ 79


                 ....*
gi 515637361 233 VKPDD 237
Cdd:cd04608   80 VDLDT 84

CBS_pair_Thermoplasmatales

cd17786

Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains present in ...

199-271

8.27e-03

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

Pssm-ID: 341422 [Multi-domain] Cd Length: 114 Bit Score: 36.74 E-value: 8.27e-03

                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 515637361 199 VGLITDRDMTKRVIAHGVSTDSL-ISEVMTHSPLTVKPDDLVLHAASIMMQFNIRNLPVV-KENKVVGLLTTSHL 271
Cdd:cd17786   38 VGLISERSIIKRFIPRNVKPDEVpVKLVMRKPIPKVKSDYDVKDVAAFLSENGLERCAVVdDNGRVVGIVTITDL 112

CBS_pair_voltage-gated_CLC_archaea

cd04594

Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with the ...

191-267

8.91e-03

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

Pssm-ID: 341369 [Multi-domain] Cd Length: 107 Bit Score: 36.17 E-value: 8.91e-03

                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 515637361 191 VIYEGETIVGLITDRDMTKRviahgvSTDSLISEVMTHSPlTVKPDDLVLHAASIMMQFNIRNLPVVKENKVVGLLT 267
Cdd:cd04594   30 VVDNDSNFLGAVYLRDIENK------SPGKVGKYVVRGSP-YVTPTSSLEEAWEIMMRNKSRWVAVVEKGKFLGIIT 99

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