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).

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 422948406 198 MTDTAALKNDETIHHFQKLNERTTHGAFPVVTHQNKLVGMITVKDVIGREENELIEKVMTKNPIAGSMKMSVASAGHRMI 277
Cdd:cd04596    1 LEETGYLRETDTVRDYKQLSEETGHSRFPVVDEENRVVGIVTAKDVIGKEDDTPIEKVMTKNPITVKPKTSVASAAHMMI 80

                         90       100
                 ....*....|....*....|....*...
gi 422948406 278 WEGIDLLPIVDDDNILQGVISRQDVLKA 305
Cdd:cd04596   81 WEGIELLPVVDENRKLLGVISRQDVLKA 108

The hotdog fold was initially identified in the E. coli FabA (beta-hydroxydecanoyl-acyl carrier protein (ACP)-dehydratase) structure and subsequently in 4HBT (4-hydroxybenzoyl-CoA thioesterase) from Pseudomonas. A number of other seemingly unrelated proteins also share the hotdog fold. These proteins have related, but distinct, catalytic activities that include metabolic roles such as thioester hydrolysis in fatty acid metabolism, and degradation of phenylacetic acid and the environmental pollutant 4-chlorobenzoate. This superfamily also includes the PaaI-like protein FapR, a non-catalytic bacterial homolog involved in transcriptional regulation of fatty acid biosynthesis.

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 422948406 335 LIVEFKVTPQMTNQYGAISYGAFTTLLAEVGSFALKR--RKRGDAVAENMTIYFIKPVQMESTLTVKPRILDMSRKFVKM 412
Cdd:cd03440    1 FVLRLTVTPEDIDGGGIVHGGLLLALADEAAGAAAARlgGRGLGAVTLSLDVRFLRPVRPGDTLTVEAEVVRVGRSSVTV 80

                 ....*...
gi 422948406 413 DFEVYNQQ 420
Cdd:cd03440   81 EVEVRNED 88

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).

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 422948406 198 MTDTAALKNDETIHHFQKLNERTTHGAFPVVTHQNKLVGMITVKDVIGREENELIEKVMTKNPIAGSMKMSVASAGHRMI 277
Cdd:cd04596    1 LEETGYLRETDTVRDYKQLSEETGHSRFPVVDEENRVVGIVTAKDVIGKEDDTPIEKVMTKNPITVKPKTSVASAAHMMI 80

                         90       100
                 ....*....|....*....|....*...
gi 422948406 278 WEGIDLLPIVDDDNILQGVISRQDVLKA 305
Cdd:cd04596   81 WEGIELLPVVDENRKLLGVISRQDVLKA 108

DRTGG domain; This presumed domain is about 120 amino acids in length. It is found associated with CBS domains pfam00571, as well as the CbiA domain pfam01656. The function of this domain is unknown. It is named the DRTGG domain after some of the most conserved residues. This domain may be very distantly related to a pair of CBS domains. There are no significant sequence similarities, but its length and association with CBS domains supports this idea (Bateman A, pers. obs.).

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 422948406   76 EIVNIVDGQVLGGKSGLHKTLTKFVIGAMQLEDMMRYTDAGSLLIV-GNRIKAHENALRAG-AAVLITGGFDTTEDNKLL 153
Cdd:pfam07085   1 DIARILGAEVLNGGDGLLRRVGKVVVGAMSVENMLKYLRPGDLVITpGDREDIQLAALEAGiAGLILTGGFEPSPEVLKL 80

                          90       100
                  ....*....|....*....|....*
gi 422948406  154 ADSLDLPIISTSYDTFTVATMINRA 178
Cdd:pfam07085  81 AEELGLPVLSTPYDTFTTASRINRA 105

BioD-like N-terminal domain of phosphotransacetylase [General function prediction only];

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 422948406  75 AEIVNIVDGQVLGGKSGLHKTLTKFVIGAMQLEDMMRYTDAGSLLIV-GNR-------IKAHENALRAGAAVLITGGFDT 146
Cdd:COG0857  217 RDLAEALGAEVLNGGELLDRRVESVVVGAMSVPNALERLREGALVITpGDRsdillaaLLAALSGTPSIAGLILTGGLPP 296

                         90       100       110
                 ....*....|....*....|....*....|....
gi 422948406 147 TED-NKLLADSLD-LPIISTSYDTFTVATMINRA 178
Cdd:COG0857  297 DPAvLRLAEGLGQtLPILSVELDTYTTAERLERV 330

inosine-5'-monophosphate dehydrogenase; Provisional

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 422948406 156 SLDLPIISTSYDTFTVATMI--------------NRAIYDQL--IKK----DILFIEDIYVpmtdtaaLKNDETIHHFQK 215
Cdd:PTZ00314  48 RLKIPIVSSPMDTVTEHKMAiamalmggigvihnNCSIEEQVeeVRKvkrfENGFIMDPYV-------LSPNHTVADVLE 120

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 422948406 216 LNERTTHGAFPVVT---HQNKLVGMITVKDVIGREENE-LIEKVMT--KNPIAGSMKMSVASAGHRMIWEGIDLLPIVDD 289
Cdd:PTZ00314 121 IKEKKGFSSILITVdgkVGGKLLGIVTSRDIDFVKDKStPVSEVMTprEKLVVGNTPISLEEANEVLRESRKGKLPIVND 200

                        170
                 ....*....|....*.
gi 422948406 290 DNILQGVISRQDVLKA 305
Cdd:PTZ00314 201 NGELVALVSRSDLKKN 216

Acyl-CoA thioesterase PaaI, contains HGG motif [Secondary metabolites biosynthesis, transport and catabolism];

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 422948406 330 LGDEDLIVEFKVTPQMTNQYGAISYGAFTTLLAEVGSFALKRRKRGD--AVAENMTIYFIKPVQMESTLTVKPRILDMSR 407
Cdd:COG2050   28 VEPGRAVLRLPVRPEHLNPPGTVHGGALAALADSAAGLAANSALPPGrrAVTIELNINFLRPARLGDRLTAEARVVRRGR 107

                         90       100
                 ....*....|....*....|....*....
gi 422948406 408 KFVKMDFEVYNQQ-MLVGKAMMMFQLLER 435
Cdd:COG2050  108 RLAVVEVEVTDEDgKLVATATGTFAVLPK 136

Winged helix-turn-helix (WHTH) DNA-binding domain of the GntR family of transcriptional regulators; This CD represents the winged HTH DNA-binding domain of the GntR (named after the gluconate operon repressor in Bacillus subtilis) family of bacterial transcriptional regulators and their putative homologs found in eukaryota and archaea. The GntR family has over 6000 members distributed among almost all bacterial species, which is comprised of FadR, HutC, MocR, YtrA, AraR, PlmA, and other subfamilies for the regulation of the most varied biological process. The monomeric proteins of the GntR family are characterized by two function domains: a small highly conserved winged helix-turn-helix prokaryotic DNA binding domain in the N-terminus, and a very diverse regulatory ligand-binding domain in the C-terminus for effector-binding/oligomerization, which provides the basis for the subfamily classifications. Binding of the effector to GntR-like transcriptional regulators is presumed to result in a conformational change that regulates the DNA-binding affinity of the repressor. The GntR-like proteins bind as dimers, where each monomer recognizes a half-site of 2-fold symmetric DNA sequences.

                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 422948406   6 EKILQYIES--LPVGDKI-SVRQIAKEMQVSEGTAYRAIKEAENRRLVSSIERVGTI 59
Cdd:cd07377    8 DQLREAILSgeLKPGDRLpSERELAEELGVSRTTVREALRELEAEGLVERRPGRGTF 64

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.

                           10        20
                   ....*....|....*....|....*.
gi 422948406   219 RTTHGAFPVVTHQNKLVGMITVKDVI 244
Cdd:smart00116  20 ENGIRRLPVVDEEGRLVGIVTRRDII 45

CRISPR locus-related DNA-binding protein; Most but not all examples of this family are associated with CRISPR loci, a combination of DNA repeats and characteristic proteins encoded near the repeat cluster. The C-terminal region of this protein is homologous to DNA-binding helix-turn-helix domains with predicted transcriptional regulatory activity. [Regulatory functions, DNA interactions, , ]

                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 422948406    7 KILQYIESLPvgdKISVRQIAKEMQVSEGTAYRAIKEAENRRLVSSIERVGTIRIEKK 64
Cdd:TIGR01884 147 KILEVLKATG---EKSVKNIAKKLGKSLSTISRHLAELEKKGLVEQKGRKGKRYSLTK 201

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).

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 422948406 198 MTDTAALKNDETIHHFQKLNERTTHGAFPVVTHQNKLVGMITVKDVIGREENELIEKVMTKNPIAGSMKMSVASAGHRMI 277
Cdd:cd04596    1 LEETGYLRETDTVRDYKQLSEETGHSRFPVVDEENRVVGIVTAKDVIGKEDDTPIEKVMTKNPITVKPKTSVASAAHMMI 80

                         90       100
                 ....*....|....*....|....*...
gi 422948406 278 WEGIDLLPIVDDDNILQGVISRQDVLKA 305
Cdd:cd04596   81 WEGIELLPVVDENRKLLGVISRQDVLKA 108

DRTGG domain; This presumed domain is about 120 amino acids in length. It is found associated with CBS domains pfam00571, as well as the CbiA domain pfam01656. The function of this domain is unknown. It is named the DRTGG domain after some of the most conserved residues. This domain may be very distantly related to a pair of CBS domains. There are no significant sequence similarities, but its length and association with CBS domains supports this idea (Bateman A, pers. obs.).

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 422948406   76 EIVNIVDGQVLGGKSGLHKTLTKFVIGAMQLEDMMRYTDAGSLLIV-GNRIKAHENALRAG-AAVLITGGFDTTEDNKLL 153
Cdd:pfam07085   1 DIARILGAEVLNGGDGLLRRVGKVVVGAMSVENMLKYLRPGDLVITpGDREDIQLAALEAGiAGLILTGGFEPSPEVLKL 80

                          90       100
                  ....*....|....*....|....*
gi 422948406  154 ADSLDLPIISTSYDTFTVATMINRA 178
Cdd:pfam07085  81 AEELGLPVLSTPYDTFTTASRINRA 105

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).

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 422948406 198 MT-DTAALKNDETIHHFQKLNERTTHGAFPVVtHQNKLVGMITVKDVIGREENELIEKVMTKNPIAGSMKMSVASAGHRM 276
Cdd:cd04610    1 MTrDVITVSPDDTVKDVIKLIKETGHDGFPVV-DDGKVVGYVTAKDLLGKDDDEKVSEIMSRDTVVADPDMDITDAARVI 79

                         90       100
                 ....*....|....*....|....*...
gi 422948406 277 IWEGIDLLPIVDDDNILQGVISRQDVLK 304
Cdd:cd04610   80 FRSGISKLPVVDDEGNLVGIITNMDVIR 107

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

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 422948406 189 LFIEDIyvpMT-DTAALKNDETIHHFQKLNERTTHGAFPVVTHQNKLVGMITVKDVI------------GREENELIEKV 255
Cdd:COG3448    2 MTVRDI---MTrDVVTVSPDTTLREALELMREHGIRGLPVVDEDGRLVGIVTERDLLrallpdrldeleERLLDLPVEDV 78

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|.
gi 422948406 256 MTKNPIAGSMKMSVASAGHRMIWEGIDLLPIVDDDNILQGVISRQDVLKAL 306
Cdd:COG3448   79 MTRPVVTVTPDTPLEEAAELMLEHGIHRLPVVDDDGRLVGIVTRTDLLRAL 129

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

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 422948406 207 DETIHHFQKLNERTTHGAFPVVtHQNKLVGMITVKDVI------GREENELIEKVMTKNPIAGSMKMSVASAGHRMIWEG 280
Cdd:COG2524  102 DTTLEEALELMLEKGISGLPVV-DDGKLVGIITERDLLkalaegRDLLDAPVSDIMTRDVVTVSEDDSLEEALRLMLEHG 180

                         90       100
                 ....*....|....*....|....*.
gi 422948406 281 IDLLPIVDDDNILQGVISRQDVLKAL 306
Cdd:COG2524  181 IGRLPVVDDDGKLVGIITRTDILRAL 206

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).

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 422948406 207 DETIHHFQKLNERTTHGAFPVVTHQNKLVGMITVKDV-IGREENELIEKVMTKNPiagsmKMSVASAG------HRMIWE 279
Cdd:cd04601   10 DATVADVLELKAEYGISGVPVTEDGGKLVGIVTSRDIrFETDLSTPVSEVMTPDE-----RLVTAPEGitleeaKEILHK 84

                         90       100
                 ....*....|....*....|....*.
gi 422948406 280 G-IDLLPIVDDDNILQGVISRQDVLK 304
Cdd:cd04601   85 HkIEKLPIVDDNGELVGLITRKDIEK 110

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).

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 422948406 207 DETIHHFQKLNERTTHGAFPVVTHqNKLVGMITVKDV----IGREENELIEKVMTKNPIAGSMKMSVASAGHRMIWEGID 282
Cdd:cd04595   10 DTTIEEARKIMLRYGHTGLPVVED-GKLVGIISRRDVdkakHHGLGHAPVKGYMSTNVITIDPDTSLEEAQELMVEHDIG 88

                         90       100
                 ....*....|....*....|...
gi 422948406 283 LLPIVDDDNILqGVISRQDVLKA 305
Cdd:cd04595   89 RLPVVEEGKLV-GIVTRSDVLRY 110

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).

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 422948406 197 PMTDTAALKNDETIHHFQKLNERTTHGAFPVVTHQNKLVGMITVKDVIGREENE------LIEKVMTKNPIAGSMKMSVA 270
Cdd:cd04613    1 MPRKVTVLPEGMTFRQFTEFIAGTRQHYFPVVDEQGRLTGILSIQDVRGVLFEEelwdlvVVKDLATTDVITVTPDDDLY 80

                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 422948406 271 SAGHRMIWEGIDLLPIVDDDN--ILQGVISRQDVLKA 305
Cdd:cd04613   81 TALLKFTSTNLDQLPVVDDDDpgKVLGMLSRRDVIAA 117

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).

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 422948406 203 ALKNDETIHHFQK-LNERTTHGAfPVVThQNKLVGMITVKDvIGR-----EENELIEKVMTKNPIAGSMKMSVASAGHRM 276
Cdd:cd04588    6 TLKPDATIKDAAKlLSENNIHGA-PVVD-DGKLVGIVTLTD-IAKalaegKENAKVKDIMTKDVITIDKDEKIYDAIRLM 82

                         90       100
                 ....*....|....*....|....*...
gi 422948406 277 IWEGIDLLPIVDDDNILQGVISRQDVLK 304
Cdd:cd04588   83 NKHNIGRLIVVDDNGKPVGIITRTDILK 110

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).

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 422948406 216 LNERTTHGAFPVVTHQnKLVGMITVKDVIGREENELIEKVMTKNPIAGSMKMSVASAGHRMIWEGIDLLPIVDDDNILqG 295
Cdd:cd04599   20 LMERQRIGGLPVVENG-KLVGIITSRDVRRAHPNRLVADAMSRNVVTISPEASLWEAKELMEEHGIERLVVVEEGRLV-G 97

                 ....*...
gi 422948406 296 VISRQDVL 303
Cdd:cd04599   98 IITKSTLY 105

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).

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 422948406 223 GAFPVVTHQNKLVGMITVKDVIGREENELIEK-----------------------------VMTKNPIAGSMKMSVASAG 273
Cdd:cd04586   27 SGLPVVDDDGKLVGIVSEGDLLRREEPGTEPRrvwwldallesperlaeeyvkahgrtvgdVMTRPVVTVSPDTPLEEAA 106

                         90       100       110
                 ....*....|....*....|....*....|..
gi 422948406 274 HRMIWEGIDLLPIVDDDNiLQGVISRQDVLKA 305
Cdd:cd04586  107 RLMERHRIKRLPVVDDGK-LVGIVSRADLLRA 137

inosine-5'-monophosphate dehydrogenase; Provisional

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 422948406 156 SLDLPIISTSYDTFTVATMI--------------NRAIYDQL--IKK----DILFIEDIYVpmtdtaaLKNDETIHHFQK 215
Cdd:PTZ00314  48 RLKIPIVSSPMDTVTEHKMAiamalmggigvihnNCSIEEQVeeVRKvkrfENGFIMDPYV-------LSPNHTVADVLE 120

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 422948406 216 LNERTTHGAFPVVT---HQNKLVGMITVKDVIGREENE-LIEKVMT--KNPIAGSMKMSVASAGHRMIWEGIDLLPIVDD 289
Cdd:PTZ00314 121 IKEKKGFSSILITVdgkVGGKLLGIVTSRDIDFVKDKStPVSEVMTprEKLVVGNTPISLEEANEVLRESRKGKLPIVND 200

                        170
                 ....*....|....*.
gi 422948406 290 DNILQGVISRQDVLKA 305
Cdd:PTZ00314 201 NGELVALVSRSDLKKN 216

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).

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 422948406 224 AFPVVTHQN-KLVGMITVKDVIGREENELIEKVMTKNPIAGSMKMSVASAGHRMIWEGIDLLPIVDDDNiLQGVISRQDV 302
Cdd:cd04638   28 GVPVVKKETgKLVGIVTRKDLLRNPDEEQIALLMSRDPITISPDDTLSEAAELMLEHNIRRVPVVDDDK-LVGIVTVADL 106

                 ...
gi 422948406 303 LKA 305
Cdd:cd04638  107 VRA 109

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).

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 422948406 223 GAFPVVTHQNKLVGMITVKDVI-----GREENELIEKVMTKNPIAGSMKMSVASAGHRMIWEGIDLLPIVDDDNILQGVI 297
Cdd:cd09836   27 GSVVVVDDDGKPVGIVTERDIVravaeGIDLDTPVEEIMTKNLVTVSPDESIYEAAELMREHNIRHLPVVDGGGKLVGVI 106

                 ....*....
gi 422948406 298 SRQDVLKAL 306
Cdd:cd09836  107 SIRDLAREL 115

The hotdog fold was initially identified in the E. coli FabA (beta-hydroxydecanoyl-acyl carrier protein (ACP)-dehydratase) structure and subsequently in 4HBT (4-hydroxybenzoyl-CoA thioesterase) from Pseudomonas. A number of other seemingly unrelated proteins also share the hotdog fold. These proteins have related, but distinct, catalytic activities that include metabolic roles such as thioester hydrolysis in fatty acid metabolism, and degradation of phenylacetic acid and the environmental pollutant 4-chlorobenzoate. This superfamily also includes the PaaI-like protein FapR, a non-catalytic bacterial homolog involved in transcriptional regulation of fatty acid biosynthesis.

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 422948406 335 LIVEFKVTPQMTNQYGAISYGAFTTLLAEVGSFALKR--RKRGDAVAENMTIYFIKPVQMESTLTVKPRILDMSRKFVKM 412
Cdd:cd03440    1 FVLRLTVTPEDIDGGGIVHGGLLLALADEAAGAAAARlgGRGLGAVTLSLDVRFLRPVRPGDTLTVEAEVVRVGRSSVTV 80

                 ....*...
gi 422948406 413 DFEVYNQQ 420
Cdd:cd03440   81 EVEVRNED 88

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).

                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 422948406 227 VVTHQNKLVGMITVKDV-IGREENELIEKVMTKNPIAGSMKMSVASAGHRMIWEGIDLLPIVDDDNILQGVISR 299
Cdd:cd04583   30 VVDKDNVLLGIVDIEDInRNYRKAKKVGEIMERDVFTVKEDSLLRDTVDRILKRGLKYVPVVDEQGRLVGLVTR 103

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).

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 422948406 227 VVTHQNKLVGMITVKD----VI--GREENELIEKVMTKNPIAGSMKMSVASAGHRMIWEGIDLLPIVDDDNILqGVISRQ 300
Cdd:cd04587   31 LVVDDGRLVGIVTDRDlrnrVVaeGLDPDTPVSEIMTPPPVTIDADALVFEALLLMLERNIHHLPVVDDGRVV-GVVTAT 109

                 ....*
gi 422948406 301 DVLKA 305
Cdd:cd04587  110 DLMRL 114

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.

                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 422948406  252 IEKVMTKNPIAGSMKMSVASAGHRMIWEGIDLLPIVDDDNILQGVISRQDVLKAL 306
Cdd:pfam00571   1 VKDIMTKDVVTVSPDTTLEEALELMREHGISRLPVVDEDGKLVGIVTLKDLLRAL 55

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.

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 422948406 213 FQKLNERTTHGAfpVVTHQNKLVGMITVKDVI----GRE-----------------ENELIEKVMTKNPIAGSMKMSVAS 271
Cdd:cd17777   25 FEKMNRRGIRRL--VVVDENKLEGILSARDLVsylgGGClfkivesrhqgdlysalNREVVETIMTPNPVYVYEDSDLIE 102

                         90       100       110
                 ....*....|....*....|....*....|....*
gi 422948406 272 AGHRMIWEGIDLLPIVDDDNILQGVISRQDVLKAL 306
Cdd:cd17777  103 ALTIMVTRGIGSLPVVDRDGRPVGIVTERDLVLYL 137

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.

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 422948406 226 PVVTHqNKLVGMITVKDVI---GREE--------------NELIEKVMTKNPIAGSMKMSVASAGHRMIWEGIDLLPIVD 288
Cdd:cd04631   35 PVVSD-GKLVGIVTSTDIMrylGSGEafeklktgnihevlNVPISSIMKRDIITTTPDTDLGEAAELMLEKNIGALPVVD 113

                         90
                 ....*....|....*...
gi 422948406 289 DDNILqGVISRQDVLKAL 306
Cdd:cd04631  114 DGKLV-GIITERDILRAI 130