GMP synthase, glutamine amidotransferase domain [Nucleotide transport and metabolism]; GMP synthase, glutamine amidotransferase domain is part of the Pathway/BioSystem: Purine biosynthesis

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595728   2 RALVLQHVPFEGS--ARIGDWIGRHCEHEHVCYLYADAHLPA---LDSFDLLVVMGGPMSVHDEAqyPWLVAEKRLIRAA 76
Cdd:COG0518   1 KILILDHDPFGGQypGLIARRLREAGIELDVLRVYAGEILPYdpdLEDPDGLILSGGPMSVYDED--PWLEDEPALIREA 78

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595728  77 LDAGKKVLGICLGAQLLAQALGAAVRPGRQAEIGWWPLHRYSQalgSPLGERLPERLMAFHWHGETFD-LPAGSVPLYGS 155
Cdd:COG0518  79 FELGKPVLGICYGAQLLAHALGGKVEPGPGREIGWAPVELTEA---DPLFAGLPDEFTVWMSHGDTVTeLPEGAEVLASS 155

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15595728 156 AACANQGFIWNEQAIGLQCHLESTAESIEALLDACPQDLQREgavqsaGRIRQGVAHCREVAPVLFLLLDYLAHR 230
Cdd:COG0518 156 DNCPNQAFRYGRRVYGVQFHPEVTHTMMEAWLEERADELAAE------ELLAEASLHDPELREAGRRLLRNFLRE 224

Glutamine amidotransferase class-I;

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595728    45 FDLLVVMGGPMSVHDEAQypwlvaEKRLIRAALDAGKKVLGICLGAQLLAQALGAAVRPGRQAEIGWW--PLHRYSQALG 122
Cdd:pfam00117  41 PDGIILSGGPGSPGAAGG------AIEAIREARELKIPILGICLGHQLLALAFGGKVVKAKKFGHHGKnsPVGDDGCGLF 114

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15595728   123 SPLGERLPERlmafHWHGETFD---LPAGSVPLYGSA-ACANQGFIWNEQAI-GLQCHLEST 179
Cdd:pfam00117 115 YGLPNVFIVR----RYHSYAVDpdtLPDGLEVTATSEnDGTIMGIRHKKLPIfGVQFHPESI 172

GMP synthase, glutamine amidotransferase domain [Nucleotide transport and metabolism]; GMP synthase, glutamine amidotransferase domain is part of the Pathway/BioSystem: Purine biosynthesis

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595728   2 RALVLQHVPFEGS--ARIGDWIGRHCEHEHVCYLYADAHLPA---LDSFDLLVVMGGPMSVHDEAqyPWLVAEKRLIRAA 76
Cdd:COG0518   1 KILILDHDPFGGQypGLIARRLREAGIELDVLRVYAGEILPYdpdLEDPDGLILSGGPMSVYDED--PWLEDEPALIREA 78

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595728  77 LDAGKKVLGICLGAQLLAQALGAAVRPGRQAEIGWWPLHRYSQalgSPLGERLPERLMAFHWHGETFD-LPAGSVPLYGS 155
Cdd:COG0518  79 FELGKPVLGICYGAQLLAHALGGKVEPGPGREIGWAPVELTEA---DPLFAGLPDEFTVWMSHGDTVTeLPEGAEVLASS 155

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15595728 156 AACANQGFIWNEQAIGLQCHLESTAESIEALLDACPQDLQREgavqsaGRIRQGVAHCREVAPVLFLLLDYLAHR 230
Cdd:COG0518 156 DNCPNQAFRYGRRVYGVQFHPEVTHTMMEAWLEERADELAAE------ELLAEASLHDPELREAGRRLLRNFLRE 224

glutamine amidotransferase; Provisional

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595728    1 MRALVLQHVPFEGSARIGDWIGRHCEHEHVCYLYADAHLPA-LDSFDLLVVMGGPMS-VHDEAQYPWL--VAEKRLIRAA 76
Cdd:PRK08250   1 MRVHFIIHESFEAPGAYLKWAENRGYDISYSRVYAGEALPEnADGFDLLIVMGGPQSpRTTREECPYFdsKAEQRLINQA 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595728   77 LDAGKKVLGICLGAQLLAQALGAAVRPGRQAEIGWWPLHRYSQALGSPLGERLPERLMAFHWHGETFDLPAGSVPLYGSA 156
Cdd:PRK08250  81 IKAGKAVIGVCLGAQLIGEALGAKYEHSPEKEIGYFPITLTEAGLKDPLLSHFGSTLTVGHWHNDMPGLTDQAKVLATSE 160

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15595728  157 ACANQGFIWNEQAIGLQCHLESTAESIEALLDACPQDLQREGA---VQSAGRIRqgvAH-CREVAPVLFLLLDYL 227
Cdd:PRK08250 161 GCPRQIVQYSNLVYGFQCHMEFTVEAVELLIAHSQQELSQAQGkrfVQSPEELR---AWdYSEMNQKLFRFLDKL 232

glutamine amidotransferase; Provisional

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595728   18 GDWIGR---HCEHE-HVCYLYADAHLPALDSFDLLVVMGGPMSVHDEAqyPWLVAEKRLIRAALDAGKKVLGICLGAQLL 93
Cdd:PRK09065  24 PHWIRValgLAEQPvVVVRVFAGEPLPAPDDFAGVIITGSWAMVTDRL--DWSERTADWLRQAAAAGMPLLGICYGHQLL 101

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595728   94 AQALGAAV--RP-GRqaEIGWWPLHRYSQALGSPLGERLPERLMAFHWHGET-FDLPAGSVPLYGSAACANQGFIWNEQA 169
Cdd:PRK09065 102 AHALGGEVgyNPaGR--ESGTVTVELHPAAADDPLFAGLPAQFPAHLTHLQSvLRLPPGAVVLARSAQDPHQAFRYGPHA 179

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595728  170 IGLQCHLESTAESIEALLDACPQDLQREGavQSAGRIRQGVAHCREVAPvlfLLLDYLAH 229
Cdd:PRK09065 180 WGVQFHPEFTAHIMRAYLRARADCLRREG--LDARTLLREVSEAPWARK---LLRRFVRL 234

Type 1 glutamine amidotransferase (GATase1) domain found in GMP synthetase; Type 1 glutamine amidotransferase (GATase1) domain found in GMP synthetase. GMP synthetase is a glutamine amidotransferase from the de novo purine biosynthetic pathway. Glutamine amidotransferase (GATase) activity catalyse the transfer of ammonia from the amide side chain of glutamine to an acceptor substrate. GMP synthetase catalyses the amination of the nucleotide precursor xanthosine 5'-monophosphate to form GMP. GMP synthetase belongs to the triad family of amidotransferases having a conserved Cys-His-Glu catalytic triad in the glutaminase active site.

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595728  52 GGPMSVHDEAQYpwlvaekRLIRAALDAGKKVLGICLGAQLLAQALGAAVRPGRQAEIGwwpLHRYSQALGSPLGERLPE 131
Cdd:cd01742  49 GGPSSVYEEDAP-------RVDPEIFELGVPVLGICYGMQLIAKALGGKVERGDKREYG---KAEIEIDDSSPLFEGLPD 118

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|
gi 15595728 132 RLMAFHWHGETFD-LPAGSVPLYGSAACANQGFIWNEQAI-GLQCHLEST 179
Cdd:cd01742 119 EQTVWMSHGDEVVkLPEGFKVIASSDNCPVAAIANEEKKIyGVQFHPEVT 168

amidotransferase; Provisional

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595728   40 PALDSFDLLVVMGgpmSVHDE-AQYPWLVAEKRLIRAALDAGKKVLGICLGAQLLAQALGAAVrpgRQAEIGWWP-LHRY 117
Cdd:PRK05665  53 ADDEKFDAYLVTG---SKADSfGTDPWIQTLKTYLLKLYERGDKLLGVCFGHQLLALLLGGKA---ERASQGWGVgIHRY 126

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15595728  118 SQALGSPLGErlPER----LMAFHwHGETFDLPAGSVPLYGSAACANQGFIWNEQAIGLQCHLESTAESIEALLDA 189
Cdd:PRK05665 127 QLAAHAPWMS--PAVteltLLISH-QDQVTALPEGATVIASSDFCPFAAYHIGDQVLCFQGHPEFVHDYSRALLDL 199

Type 1 glutamine amidotransferase (GATase1)-like domain; Type 1 glutamine amidotransferase (GATase1)-like domain. This group contains proteins similar to Class I glutamine amidotransferases, the intracellular PH1704 from Pyrococcus horikoshii, the C-terminal of the large catalase: Escherichia coli HP-II, Sinorhizobium meliloti Rm1021 ThuA, the A4 beta-galactosidase middle domain and peptidase E. The majority of proteins in this group have a reactive Cys found in the sharp turn between a beta strand and an alpha helix termed the nucleophile elbow. For Class I glutamine amidotransferases proteins which transfer ammonia from the amide side chain of glutamine to an acceptor substrate, this Cys forms a Cys-His-Glu catalytic triad in the active site. Glutamine amidotransferases activity can be found in a range of biosynthetic enzymes included in this cd: glutamine amidotransferase, formylglycinamide ribonucleotide, GMP synthetase, anthranilate synthase component II, glutamine-dependent carbamoyl phosphate synthase (CPSase), cytidine triphosphate synthetase, gamma-glutamyl hydrolase, imidazole glycerol phosphate synthase and, cobyric acid synthase. For Pyrococcus horikoshii PH1704, the Cys of the nucleophile elbow together with a different His and, a Glu from an adjacent monomer form a catalytic triad different from the typical GATase1 triad. Peptidase E is believed to be a serine peptidase having a Ser-His-Glu catalytic triad which differs from the Cys-His-Glu catalytic triad of typical GATase1 domains, by having a Ser in place of the reactive Cys at the nucleophile elbow. The E. coli HP-II C-terminal domain, S. meliloti Rm1021 ThuA and the A4 beta-galactosidase middle domain lack the catalytic triad typical GATaseI domains. GATase1-like domains can occur either as single polypeptides, as in Class I glutamine amidotransferases, or as domains in a much larger multifunctional synthase protein, such as CPSase. Peptidase E has a circular permutation in the common core of a typical GTAse1 domain.

                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*
gi 15595728  39 LPALDSFDLLVVMGGPMSVHDEAqypWLVAEKRLIRAALDAGKKVLGICLGAQLL 93
Cdd:cd03128  41 DVDLDDYDGLILPGGPGTPDDLA---WDEALLALLREAAAAGKPVLGICLGAQLL 92

glutamine amidotransferase; Provisional

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595728   36 DAHLPALDSFDLLVVMGGPMSVHD--EAQYPWLVAEKRLIRAALDAGKK----VLGICLGAQLLAQALGAAVRPGRQAEI 109
Cdd:PRK07567  43 PLPDLDLDDYSGVIVGGSPFNVSDpaESKSPWQRRVEAELSGLLDEVVArdfpFLGACYGVGTLGHHQGGVVDRTYGEPV 122

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595728  110 GWWPLHRYSQALGSPLGERLPERLMAFHWHGE-TFDLPAGSVPLYGSAACANQGFIWNEQAIGLQCHLESTAESIEALLD 188
Cdd:PRK07567 123 GAVTVSLTDAGRADPLLAGLPDTFTAFVGHKEaVSALPPGAVLLATSPTCPVQMFRVGENVYATQFHPELDADGLKTRID 202

                 .
gi 15595728  189 A 189
Cdd:PRK07567 203 F 203

Carbamoylphosphate synthase small subunit [Amino acid transport and metabolism, Nucleotide transport and metabolism]; Carbamoylphosphate synthase small subunit is part of the Pathway/BioSystem: Arginine biosynthesis

                        10        20
                ....*....|....*....|....*...
gi 15595728  72 LIRAALDAGKKVLGICLGAQLLAQALGA 99
Cdd:COG0505 239 TIRELLGKGIPIFGICLGHQLLALALGA 266

Small chain of the glutamine-dependent form of carbamoyl phosphate synthase, CPSase II; This group of sequences represents the small chain of the glutamine-dependent form of carbamoyl phosphate synthase, CPSase II. CPSase II catalyzes the production of carbomyl phosphate (CP) from bicarbonate, glutamine and two molecules of MgATP. The reaction is believed to proceed by a series of four biochemical reactions involving a minimum of three discrete highly reactive intermediates. The synthesis of CP is critical for the initiation of two separate biosynthetic pathways. In one CP is coupled to aspartate, its carbon and nitrogen nuclei ultimately incorporated into the aromatic moieties of pyrimidine nucleotides. In the second pathway CP is condensed with ornithine at the start of the urea cycle and is utilized for the detoxification of ammonia and biosynthesis of arginine. CPSases may be encoded by one or by several genes, depending on the species. The E.coli enzyme is a heterodimer consisting of two polypeptide chains referred to as the small and large subunit. Ammonia an intermediate during the biosynthesis of carbomyl phosphate produced by the hydrolysis of glutamine in the small subunit of the enzyme is delivered via a molecular tunnel between the remotely located carboxyphosphate active site in the large subunit. CPSase IIs belong to the triad family of amidotransferases having a conserved Cys-His-Glu catalytic triad in the glutaminase active site. This group also contains the sequence from the mammalian urea cycle form which has lost the active site Cys, resulting in an ammonia-dependent form, CPSase I.

                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*
gi 15595728  45 FDLLVVMGGPmsvHDEAQYPWLVAEkrlIRAALDAGKKVLGICLGAQLLAQALGA 99
Cdd:cd01744  40 PDGIFLSNGP---GDPALLDEAIKT---VRKLLGKKIPIFGICLGHQLLALALGA 88

Type 1 glutamine amidotransferase (GATase1) domain found in Anthranilate synthase; Type 1 glutamine amidotransferase (GATase1) domain found in Anthranilate synthase (ASase). This group contains proteins similar to para-aminobenzoate (PABA) synthase and ASase. These enzymes catalyze similar reactions and produce similar products, PABA and ortho-aminobenzoate (anthranilate). Each enzyme is composed of non-identical subunits: a glutamine amidotransferase subunit (component II) and a subunit that produces an aminobenzoate products (component I). ASase catalyses the synthesis of anthranilate from chorismate and glutamine and is a tetrameric protein comprising two copies each of components I and II. Component II of ASase belongs to the family of triad GTases which hydrolyze glutamine and transfer nascent ammonia between the active sites. In some bacteria, such as Escherichia coli, component II can be much larger than in other organisms, due to the presence of phosphoribosyl-anthranilate transferase (PRTase) activity. PRTase catalyses the second step in tryptophan biosynthesis and results in the addition of 5-phosphoribosyl-1-pyrophosphate to anthranilate to create N-5'-phosphoribosyl-anthranilate. In E.coli, the first step in the conversion of chorismate to PABA involves two proteins: PabA and PabB which co-operate to transfer the amide nitrogen of glutamine to chorismate forming 4-amino-4 deoxychorismate (ADC). PabA acts as a glutamine amidotransferase, supplying an amino group to PabB, which carries out the amination reaction. A third protein PabC then mediates elimination of pyruvate and aromatization to give PABA. Several organisms have bipartite proteins containing fused domains homologous to PabA and PabB commonly called PABA synthases. These hybrid PABA synthases may produce ADC and not PABA.

                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15595728  39 LPALDSFDLLVVMGGPMSVHDEAQYPWlvaekrlIRAALDAGKKVLGICLGAQLLAQALGAAVRP------GRQAEI 109
Cdd:cd01743  37 ELELLNPDAIVISPGPGHPEDAGISLE-------IIRALAGKVPILGVCLGHQAIAEAFGGKVVRapepmhGKTSEI 106

AraC transcriptional regulators having a Type 1 glutamine amidotransferase (GATase1)-like domain; A subgroup of AraC transcriptional regulators having a Type 1 glutamine amidotransferase (GATase1)-like domain. AraC regulators are defined by a AraC-type helix-turn-helix DNA binding domain at their C-terminal. AraC family transcriptional regulators are widespread among bacteria and are involved in regulating diverse and important biological functions, including carbon metabolism, stress responses and virulence in different microorganisms. The catalytic triad typical of GATase1 domains is not conserved in this GATase1-like domain. However, in common with typical GATase1domains a reactive cys residue is found in the sharp turn between a beta strand and an alpha helix termed the nucleophile elbow.

                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15595728  33 LYADAHLPALDSFDLLVVMGGPMSVHDEAQyPWLVAekrLIRAALDAGKKVLGICLGAQLLAQA 96
Cdd:cd03137  53 LVADAGLDALAAADTVIVPGGPDVDGRPPP-PALLA---ALRRAAARGARVASVCTGAFVLAEA 112

Protein/nucleotide deglycase, PfpI/YajL/DJ-1 family (repair of methylglyoxal-glycated proteins and nucleic acids) [Defense mechanisms];

                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*
gi 15595728  42 LDSFDLLVVMGGPMSVHDEAQYPWLVaekRLIRAALDAGKKVLGICLGAQLLAQA 96
Cdd:COG0693  62 PDDYDALVLPGGHGAPDDLREDPDVV---ALVREFYEAGKPVAAICHGPAVLAAA 113

imidazole glycerol phosphate synthase subunit HisH; Provisional

                         10        20        30        40
                 ....*....|....*....|....*....|....*....|...
gi 15595728   71 RLIRAALDAGKKVLGICLGAQLLAQalgAAVRPGRQAEIGWWP 113
Cdd:PRK13146  68 AVIEAVLAAGRPFLGICVGMQLLFE---RGLEHGDTPGLGLIP 107

Glutamine amidotransferase related to the GATase domain of CobQ [General function prediction only];

                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 15595728  42 LDSFDLLVVMGGPMS----VHDEaqypwLVAEKRLIRAALDAGKKVLGICLGAQLLAQ 95
Cdd:COG3442  48 FDDVDIVFIGGGQDReqeiVADD-----LLRIKDALRAAIEDGVPVLAICGGYQLLGH 100

AraC transcriptional regulators having an N-terminal Type 1 glutamine amidotransferase (GATase1)-like domain; A subgroup of AraC transcriptional regulators having an N-terminal Type 1 glutamine amidotransferase (GATase1)-like domain. This group contains proteins similar to the Pseudomonas aeruginosa ArgR regulator. ArgR functions in the control of expression of certain genes of arginine biosynthesis and catabolism. AraC regulators are defined by a AraC-type helix-turn-helix DNA binding domain at their C-terminal. AraC family transcriptional regulators are widespread among bacteria and are involved in regulating diverse and important biological functions, including carbon metabolism, stress responses and virulence in different microorganisms. The catalytic triad typical of GATase1 domains is not conserved in this GATase1-like domain. However, in common with typical GATase1domains a reactive cys residue is found in some sequences in the sharp turn between a beta strand and an alpha helix termed the nucleophile elbow.

                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15595728  35 ADAHLPALDSFDLLVVMGGPMsvHDEAQYPWLVAekrLIRAALDAGKKVLGICLGAQLLAQA 96
Cdd:cd03136  55 PDAALEDAPPLDYLFVVGGLG--ARRAVTPALLA---WLRRAARRGVALGGIDTGAFLLARA 111

A type 1 glutamine amidotransferase (GATase1)-like domain found in PfpI from Pyrococcus furiosus; A type 1 glutamine amidotransferase (GATase1)-like domain found in PfpI from Pyrococcus furiosus. This group includes proteins similar to PfpI from P. furiosus. and PH1704 from Pyrococcus horikoshii. These enzymes are ATP-independent intracellular proteases and may hydrolyze small peptides to provide a nutritional source. Only Cys of the catalytic triad typical of GATase1 domains is conserved in this group. This Cys residue is found in the sharp turn between a beta strand and an alpha helix termed the nucleophile elbow. For PH1704, it is believed that this Cys together with a different His in one monomer and Glu (from an adjacent monomer) forms a different catalytic triad from the typical GATase1domain. PfpI is homooligomeric. Protease activity is only found for oligomeric forms of PH1704.

                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 15595728  43 DSFDLLVVMGG--P--MSVHDEAQypwlvaekRLIRAALDAGKKVLGICLGAQLLAQA 96
Cdd:cd03134  61 DDYDALVIPGGtnPdkLRRDPDAV--------AFVRAFAEAGKPVAAICHGPWVLISA 110

imidazole glycerol phosphate synthase subunit HisH; Provisional

                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15595728   73 IRAALDAGKKVLGICLGAQLLA--------QALG---AAVR-----PGRQAEIGWWPLHrysQALGSPLGERLPE 131
Cdd:PRK13181  65 LKEHVEKKQPVLGICLGMQLLFesseegnvKGLGlipGDVKrfrsePLKVPQMGWNSVK---PLKESPLFKGIEE 136

Type 1 glutamine amidotransferase (GATase1) domain found in Cobyric Acid Synthase (CobQ); Type 1 glutamine amidotransferase (GATase1) domain found in Cobyric Acid Synthase (CobQ). CobQ plays a role in cobalamin biosythesis. CobQ catalyses amidations at positions B, D, E, and G on adenosylcobyrinic A,C-diamide in the biosynthesis of cobalamin. CobQ belongs to the triad family of amidotransferases. Two of the three residues of the catalytic triad that are involved in glutamine binding, hydrolysis and transfer of the resulting ammonia to the acceptor substrate in other triad aminodotransferases are conserved in CobQ.

                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595728  40 PALDSFDLLVVMGGPMSVHDEAqypWLVAE--KRLIRAALDAGKKVLGICLGAQLLAQAL 97
Cdd:cd01750  33 EGLGDADLIILPGSKDTIQDLA---WLRKRglAEAIKNYARAGGPVLGICGGYQMLGKYI 89