|
Name |
Accession |
Description |
Interval |
E-value |
| nuc_hydro_CeIAG |
cd02649 |
nuc_hydro_CeIAG: Nucleoside hydrolases similar to the inosine-adenosine-guanosine-preferring ... |
6-319 |
1.93e-122 |
|
nuc_hydro_CeIAG: Nucleoside hydrolases similar to the inosine-adenosine-guanosine-preferring nucleoside hydrolase from Caenorhabditis elegans. Nucleoside hydrolases cleave the N-glycosidic bond in nucleosides generating ribose and the respective base. These enzymes vary in their substrate specificity. This group contains eukaryotic, bacterial and archeal proteins similar to the purine-preferring nucleoside hydrolase (IAG-NH) from C. elegans and the salivary purine nucleosidase from Aedes aegypti. C. elegans IAG-NH exhibits a high affinity for the substrate analogue p-nitrophenylriboside (p-NPR).
Pssm-ID: 239115 [Multi-domain] Cd Length: 306 Bit Score: 354.26 E-value: 1.93e-122
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17565698 6 VKLVIDSDGVSDDVRAISLALQHPKAEILAFTAVHGCVTVDQACANIKRTIRANDRSNIPVYKGAAKSILSLPKddTVSD 85
Cdd:cd02649 1 RKLIIDTDCGGDDAWALLMALASPNVEVLAITCVHGNTNVEQVVKNALRVLEACGRRDIPVYRGASKPLLGPGP--TAAY 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17565698 86 FFGIDGIGDKPEEFPKVErsdFEGEGKHASLALIDILREN-RDATLVTIGPLTNVAIALQLCEEFSTYPSRLVIMGGNYY 164
Cdd:cd02649 79 FHGKDGFGDVGFPEPKDE---LELQKEHAVDAIIRLVREYpGEITLVALGPLTNLALAYRLDPSLPQKIKRLYIMGGNRE 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17565698 165 AVGNVDggSSAEYNFHGDPEAASIVLRRMKCPITIVPWEAFYFESKT-----------HDASVDFSAHLKYGTPLANYLS 233
Cdd:cd02649 156 GVGNTT--PAAEFNFHVDPEAAHIVLNSFGCPITIVPWETTLLAFPLdwefedkwanrLEKALFAESLNRREYAFASEGL 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17565698 234 latsigrvkceaNGRQYSYCDEIAVATAIDEDkIAKKSQYLYVDVELNGTKTRGQVVVDWTEQLWSNEEAPNQHTHRRVK 313
Cdd:cd02649 234 ------------GGDGWVPCDALAVAAALDPS-IITRRLTYAVDVELHGELTRGQMVVDWLGTLKKKPNARVITKIDREK 300
|
....*.
gi 17565698 314 FVTSYD 319
Cdd:cd02649 301 FKELLY 306
|
|
| URH1 |
COG1957 |
Inosine-uridine nucleoside N-ribohydrolase [Nucleotide transport and metabolism]; ... |
5-330 |
3.09e-70 |
|
Inosine-uridine nucleoside N-ribohydrolase [Nucleotide transport and metabolism]; Inosine-uridine nucleoside N-ribohydrolase is part of the Pathway/BioSystem: Pyrimidine salvage
Pssm-ID: 441560 [Multi-domain] Cd Length: 310 Bit Score: 221.18 E-value: 3.09e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17565698 5 KVKLVIDSDGVSDDVRAISLALQHPKAEILAFTAVHGCVTVDQACANIKRTIRANDRSNIPVYKGAAKSILSLPkdDTVS 84
Cdd:COG1957 2 MRKVIIDTDPGIDDALALLLALASPEIDLLGITTVAGNVPLEQTTRNALKLLELAGRTDVPVAAGAARPLVRPL--VTAE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17565698 85 DFFGIDGIGDkpEEFPKVERsdfEGEGKHASLALIDILREN-RDATLVTIGPLTNVAIALQLCEEFSTYPSRLVIMGGNY 163
Cdd:COG1957 80 HVHGEDGLGG--VDLPEPTR---PPEPEHAVDFIIETLRAApGEVTLVALGPLTNLALALRKDPELAERIKRIVIMGGAF 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17565698 164 YAVGNVdgGSSAEYNFHGDPEAASIVLRRmKCPITIVPWEAfyfeskTHDASVDFsAHLKY----GTPLANYLS--LATS 237
Cdd:COG1957 155 FVPGNV--TPVAEFNIYVDPEAAKIVFAS-GIPITMVGLDV------THQALLTP-EDLARlaalGTPLGRFLAdlLDFY 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17565698 238 IGRVKcEANGRQYSYC-DEIAVATAIDEDKIakKSQYLYVDVELNGTKTRGQVVVDWTEQLwsnEEAPNqhthrrVKFVT 316
Cdd:COG1957 225 LDFYR-ERYGLDGCPLhDPLAVAYLLDPELF--TTRPAPVDVETDGELTRGQTVVDWRGVT---GRPPN------ARVAL 292
|
330
....*....|....
gi 17565698 317 SYDVHTVDKWLHAA 330
Cdd:COG1957 293 DVDAERFLDLLLER 306
|
|
| IU_nuc_hydro |
pfam01156 |
Inosine-uridine preferring nucleoside hydrolase; |
8-320 |
8.94e-60 |
|
Inosine-uridine preferring nucleoside hydrolase;
Pssm-ID: 460086 [Multi-domain] Cd Length: 253 Bit Score: 192.42 E-value: 8.94e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17565698 8 LVIDSDGVSDDVRAISLALQHPKAEILAFTAVHGCVTVDQACANIKRTIRANDRSNIPVYKGaaksilslpkddtvsdff 87
Cdd:pfam01156 1 VIIDTDPGIDDALALLLALASPEIELLGITTVAGNVSLEQTTRNALRLLELGGRDDIPVYAG------------------ 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17565698 88 gidgigdkpeefpkversdfegegkhaslaliDILRENRDATLVTIGPLTNVAIALQLCEEFSTYPSRLVIMGGNYYAVG 167
Cdd:pfam01156 63 --------------------------------EAIREPGEVTLVATGPLTNLALALRLDPELAKKIKELVIMGGAFGVRG 110
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17565698 168 NVdgGSSAEYNFHGDPEAASIVLRRmKCPITIVPWEAfyfeskTHDASV---DFSAHLKYGTPLANYLSLATS--IGRVK 242
Cdd:pfam01156 111 NV--TPAAEFNIFVDPEAAKIVFTS-GLPITMVPLDV------THQALLtpeDLERLAALGTPLGRFLADLLRfyAEFYR 181
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 17565698 243 CEANGRQYSYCDEIAVATAIDEDKIAKKSqyLYVDVELNGTKTRGQVVVDWTEQLwsnEEAPNqhthrrVKFVTSYDV 320
Cdd:pfam01156 182 ERFGIDGPPLHDPLAVAVALDPELFTTRR--LNVDVETTGGLTRGQTVVDDRGGW---GKPPN------VRVATDVDV 248
|
|
| PLN02717 |
PLN02717 |
uridine nucleosidase |
7-190 |
4.20e-32 |
|
uridine nucleosidase
Pssm-ID: 178319 [Multi-domain] Cd Length: 316 Bit Score: 122.02 E-value: 4.20e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17565698 7 KLVIDSDGVSDDVRAISLALQHPKAEILAFTAVHGCVTVDQACANIKRTIRANDRSNIPVYKGAAKSILSLPKDdTVSDF 86
Cdd:PLN02717 2 KLIIDTDPGIDDAMAILMALRSPEVEVIGLTTIFGNVTTKLATRNALHLLEMAGRPDVPVAEGSHEPLKGGTKP-RIADF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17565698 87 F-GIDGIGDKPEEFPKVERSDfegegKHASLALIDILREN-RDATLVTIGPLTNVAIALQLCEEFSTYPSRLVIMGGNYY 164
Cdd:PLN02717 81 VhGSDGLGNTNLPPPKGKKIE-----KSAAEFLVEKVSEYpGEVTVVALGPLTNLALAIKLDPSFAKKVGQIVVLGGAFF 155
|
170 180
....*....|....*....|....*.
gi 17565698 165 AVGNVDggSSAEYNFHGDPEAASIVL 190
Cdd:PLN02717 156 VNGNVN--PAAEANIFGDPEAADIVF 179
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| nuc_hydro_CeIAG |
cd02649 |
nuc_hydro_CeIAG: Nucleoside hydrolases similar to the inosine-adenosine-guanosine-preferring ... |
6-319 |
1.93e-122 |
|
nuc_hydro_CeIAG: Nucleoside hydrolases similar to the inosine-adenosine-guanosine-preferring nucleoside hydrolase from Caenorhabditis elegans. Nucleoside hydrolases cleave the N-glycosidic bond in nucleosides generating ribose and the respective base. These enzymes vary in their substrate specificity. This group contains eukaryotic, bacterial and archeal proteins similar to the purine-preferring nucleoside hydrolase (IAG-NH) from C. elegans and the salivary purine nucleosidase from Aedes aegypti. C. elegans IAG-NH exhibits a high affinity for the substrate analogue p-nitrophenylriboside (p-NPR).
Pssm-ID: 239115 [Multi-domain] Cd Length: 306 Bit Score: 354.26 E-value: 1.93e-122
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17565698 6 VKLVIDSDGVSDDVRAISLALQHPKAEILAFTAVHGCVTVDQACANIKRTIRANDRSNIPVYKGAAKSILSLPKddTVSD 85
Cdd:cd02649 1 RKLIIDTDCGGDDAWALLMALASPNVEVLAITCVHGNTNVEQVVKNALRVLEACGRRDIPVYRGASKPLLGPGP--TAAY 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17565698 86 FFGIDGIGDKPEEFPKVErsdFEGEGKHASLALIDILREN-RDATLVTIGPLTNVAIALQLCEEFSTYPSRLVIMGGNYY 164
Cdd:cd02649 79 FHGKDGFGDVGFPEPKDE---LELQKEHAVDAIIRLVREYpGEITLVALGPLTNLALAYRLDPSLPQKIKRLYIMGGNRE 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17565698 165 AVGNVDggSSAEYNFHGDPEAASIVLRRMKCPITIVPWEAFYFESKT-----------HDASVDFSAHLKYGTPLANYLS 233
Cdd:cd02649 156 GVGNTT--PAAEFNFHVDPEAAHIVLNSFGCPITIVPWETTLLAFPLdwefedkwanrLEKALFAESLNRREYAFASEGL 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17565698 234 latsigrvkceaNGRQYSYCDEIAVATAIDEDkIAKKSQYLYVDVELNGTKTRGQVVVDWTEQLWSNEEAPNQHTHRRVK 313
Cdd:cd02649 234 ------------GGDGWVPCDALAVAAALDPS-IITRRLTYAVDVELHGELTRGQMVVDWLGTLKKKPNARVITKIDREK 300
|
....*.
gi 17565698 314 FVTSYD 319
Cdd:cd02649 301 FKELLY 306
|
|
| URH1 |
COG1957 |
Inosine-uridine nucleoside N-ribohydrolase [Nucleotide transport and metabolism]; ... |
5-330 |
3.09e-70 |
|
Inosine-uridine nucleoside N-ribohydrolase [Nucleotide transport and metabolism]; Inosine-uridine nucleoside N-ribohydrolase is part of the Pathway/BioSystem: Pyrimidine salvage
Pssm-ID: 441560 [Multi-domain] Cd Length: 310 Bit Score: 221.18 E-value: 3.09e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17565698 5 KVKLVIDSDGVSDDVRAISLALQHPKAEILAFTAVHGCVTVDQACANIKRTIRANDRSNIPVYKGAAKSILSLPkdDTVS 84
Cdd:COG1957 2 MRKVIIDTDPGIDDALALLLALASPEIDLLGITTVAGNVPLEQTTRNALKLLELAGRTDVPVAAGAARPLVRPL--VTAE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17565698 85 DFFGIDGIGDkpEEFPKVERsdfEGEGKHASLALIDILREN-RDATLVTIGPLTNVAIALQLCEEFSTYPSRLVIMGGNY 163
Cdd:COG1957 80 HVHGEDGLGG--VDLPEPTR---PPEPEHAVDFIIETLRAApGEVTLVALGPLTNLALALRKDPELAERIKRIVIMGGAF 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17565698 164 YAVGNVdgGSSAEYNFHGDPEAASIVLRRmKCPITIVPWEAfyfeskTHDASVDFsAHLKY----GTPLANYLS--LATS 237
Cdd:COG1957 155 FVPGNV--TPVAEFNIYVDPEAAKIVFAS-GIPITMVGLDV------THQALLTP-EDLARlaalGTPLGRFLAdlLDFY 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17565698 238 IGRVKcEANGRQYSYC-DEIAVATAIDEDKIakKSQYLYVDVELNGTKTRGQVVVDWTEQLwsnEEAPNqhthrrVKFVT 316
Cdd:COG1957 225 LDFYR-ERYGLDGCPLhDPLAVAYLLDPELF--TTRPAPVDVETDGELTRGQTVVDWRGVT---GRPPN------ARVAL 292
|
330
....*....|....
gi 17565698 317 SYDVHTVDKWLHAA 330
Cdd:COG1957 293 DVDAERFLDLLLER 306
|
|
| IU_nuc_hydro |
pfam01156 |
Inosine-uridine preferring nucleoside hydrolase; |
8-320 |
8.94e-60 |
|
Inosine-uridine preferring nucleoside hydrolase;
Pssm-ID: 460086 [Multi-domain] Cd Length: 253 Bit Score: 192.42 E-value: 8.94e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17565698 8 LVIDSDGVSDDVRAISLALQHPKAEILAFTAVHGCVTVDQACANIKRTIRANDRSNIPVYKGaaksilslpkddtvsdff 87
Cdd:pfam01156 1 VIIDTDPGIDDALALLLALASPEIELLGITTVAGNVSLEQTTRNALRLLELGGRDDIPVYAG------------------ 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17565698 88 gidgigdkpeefpkversdfegegkhaslaliDILRENRDATLVTIGPLTNVAIALQLCEEFSTYPSRLVIMGGNYYAVG 167
Cdd:pfam01156 63 --------------------------------EAIREPGEVTLVATGPLTNLALALRLDPELAKKIKELVIMGGAFGVRG 110
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17565698 168 NVdgGSSAEYNFHGDPEAASIVLRRmKCPITIVPWEAfyfeskTHDASV---DFSAHLKYGTPLANYLSLATS--IGRVK 242
Cdd:pfam01156 111 NV--TPAAEFNIFVDPEAAKIVFTS-GLPITMVPLDV------THQALLtpeDLERLAALGTPLGRFLADLLRfyAEFYR 181
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 17565698 243 CEANGRQYSYCDEIAVATAIDEDKIAKKSqyLYVDVELNGTKTRGQVVVDWTEQLwsnEEAPNqhthrrVKFVTSYDV 320
Cdd:pfam01156 182 ERFGIDGPPLHDPLAVAVALDPELFTTRR--LNVDVETTGGLTRGQTVVDDRGGW---GKPPN------VRVATDVDV 248
|
|
| nuc_hydro_IU_UC_XIUA |
cd02651 |
nuc_hydro_IU_UC_XIUA: inosine-uridine preferring, ... |
7-293 |
1.07e-45 |
|
nuc_hydro_IU_UC_XIUA: inosine-uridine preferring, xanthosine-inosine-uridine-adenosine-preferring and, uridine-cytidine preferring nucleoside hydrolases. Nucleoside hydrolases cleave the N-glycosidic bond in nucleosides generating ribose and the respective base. These enzymes vary in their substrate specificity. This group contains proteins similar to nucleoside hydrolases which hydrolyze both pyrimidine and purine ribonucleosides: the inosine-uridine preferring nucleoside hydrolase from Crithidia fasciculata, the inosine-uridine-xanthosine preferring nucleoside hydrolase RihC from Escherichia coli and the xanthosine-inosine-uridine-adenosine-preferring nucleoside hydrolase RihC from Salmonella enterica serovar Typhimurium. This group also contains proteins similar to the pyrimidine-specific uridine-cytidine preferring nucleoside hydrolases URH1 from Saccharomyces cerevisiae, E. coli RihA and E. coli RihB. E. coli RihA is equally efficient with uridine and cytidine, E. coli RihB prefers cytidine over uridine. S. cerevisiae URH1 prefers uridine over cytidine.
Pssm-ID: 239117 [Multi-domain] Cd Length: 302 Bit Score: 157.32 E-value: 1.07e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17565698 7 KLVIDSDGVSDDVRAISLALQHPKAEILAFTAVHGCVTVDQACANIKRTIRANDRSNIPVYKGAAKSILSLPKddTVSDF 86
Cdd:cd02651 1 PIIIDCDPGHDDAVAILLALFHPELDLLGITTVAGNVPLEKTTRNALKLLTLLGRTDVPVAAGAARPLVRPLI--TASDI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17565698 87 FGIDGIGDKpeEFPKVersDFEGEGKHASLALIDILREN-RDATLVTIGPLTNVAIALQLCEEFSTYPSRLVIMGGNyYA 165
Cdd:cd02651 79 HGESGLDGA--DLPPP---PRRPEDIHAVDAIIDTLRASpEPITLVATGPLTNIALLLRKYPELAERIKEIVLMGGA-LG 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17565698 166 VGNVdgGSSAEYNFHGDPEAASIVLRRmKCPITIVPWEAfyfeskTHDA--SVDFSAHLKY-GTPLANYLS-----LATS 237
Cdd:cd02651 153 RGNI--TPAAEFNIFVDPEAAKIVFNS-GIPITMVPLDV------THKAlaTPEVIERIRAlGNPVGKMLAelldfFAET 223
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 17565698 238 IGRVKcEANGRQYsycDEIAVATAIDEDKIakKSQYLYVDVELNGTKTRGQVVVDW 293
Cdd:cd02651 224 YGSAF-TEGPPLH---DPCAVAYLLDPELF--TTKRANVDVETEGELTRGRTVVDL 273
|
|
| nuc_hydro |
cd00455 |
nuc_hydro: Nucleoside hydrolases. Nucleoside hydrolases cleave the N-glycosidic bond in ... |
8-301 |
1.74e-42 |
|
nuc_hydro: Nucleoside hydrolases. Nucleoside hydrolases cleave the N-glycosidic bond in nucleosides generating ribose and the respective base. These enzymes vary in their substrate specificity. This group contains eukaryotic, bacterial and archeal proteins similar to the inosine-uridine preferring nucleoside hydrolase from Crithidia fasciculata, the xanthosine-inosine-uridine-adenosine-preferring nucleoside hydrolase RihC from Salmonella enterica serovar Typhimurium, the purine-specific inosine-adenosine-guanosine-preferring nucleoside hydrolase from Trypanosoma vivax and, pyrimidine-specific uridine-cytidine preferring nucleoside hydrolases such as URH1 from Saccharomyces cerevisiae, RihA and RihB from Escherichia coli. Nucleoside hydrolases are of interest as a target for antiprotozoan drugs as, no nucleoside hydrolase activity or genes encoding these enzymes have been detected in humans and, parasitic protozoans lack de novo purine synthesis relying on nucleoside hydrolase to scavenge purine and/or pyrimidines from the environment.
Pssm-ID: 238257 [Multi-domain] Cd Length: 295 Bit Score: 149.02 E-value: 1.74e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17565698 8 LVIDSDGVSDDVRAISLALQHPKAEILAFTAVHGCVTVDQACANIKRTIRANDRSNIPVYKGAAKsilslPKDDTVSDFF 87
Cdd:cd00455 1 VILDTDPGIDDAFALMYALLHPEIELVGIVATYGNVTLEQATQNAAYLLELLGRLDIPVYAGATR-----PLTGEIPAAY 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17565698 88 -GIDGIGDKPEEFPKVERSDfegeGKHASLALIDILREN-RDATLVTIGPLTNVAIALQLCEEFSTYPSRLVIMGGNYYA 165
Cdd:cd00455 76 pEIHGEGGLGLPIPPIIEAD----DPEAVQLLIDLIRKYpDEITIVALGPLTNLAMAFILDPDIKDRVKEIVIMGGAFLV 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17565698 166 VGNVDggSSAEYNFHGDPEAASIVLRRMKcPITIVPWEAfyfeskTHDAsVDFSAHLKYGTPlanylsLATSIGRVKCEA 245
Cdd:cd00455 152 PGNVT--PVAEANFYGDPEAANIVFNSAK-NLTIVPLDV------TNQA-VLTPPMVERIFE------QGTSIGLLIKPM 215
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 17565698 246 NGRQYSY-----------CDEIAVATAIDEDkIAKKSqYLYVDVELNGtKTRGQVVVDWTEQLWSNE 301
Cdd:cd00455 216 IDYYYKAyqkpgiegspiHDPLAVAYLLNPS-MFDYS-KVPVDVDTDG-LTRGQTIADFRENPGNGV 279
|
|
| nuc_hydro_CaPnhB |
cd02650 |
NH_hydro_CaPnhB: A subgroup of nucleoside hydrolases similar to Corynebacterium ammoniagenes ... |
7-305 |
2.44e-38 |
|
NH_hydro_CaPnhB: A subgroup of nucleoside hydrolases similar to Corynebacterium ammoniagenes Purine/pyrimidine nucleoside hydrolase (pnhB). Nucleoside hydrolases cleave the N-glycosidic bond in nucleosides generating ribose and the respective base. These enzymes vary in their substrate specificity.
Pssm-ID: 239116 [Multi-domain] Cd Length: 304 Bit Score: 138.18 E-value: 2.44e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17565698 7 KLVIDSD-GVsDDVRAISLALQHPKAEILAFTAVHGCVTVDQACANIKRTIRANDRSNIPVYKGAAKSILSLPKDdtVSD 85
Cdd:cd02650 1 KLILDTDpGI-DDAMALAYALAHPDVDLIGVTTVYGNVTIETATRNALALLELFGRPDVPVAEGAAKPLTRPPFR--IAT 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17565698 86 FF-GIDGIGDKPEEFPKVERSDfegegKHASLALIDILRENRDA-TLVTIGPLTNVAIALQLCEEFSTYPSRLVIMGGNY 163
Cdd:cd02650 78 FVhGDNGLGDVELPAPPRQPED-----ESAADFLIELANEYPGElTLVAVGPLTNLALALARDPDFAKLVKQVVVMGGAF 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17565698 164 YAVGNVDggSSAEYNFHGDPEAASIVlrrMKCP--ITIVPWEAfyfeskTHDASVDfSAHLK----YGTPLANYLS---- 233
Cdd:cd02650 153 TVPGNVT--PAAEANIHGDPEAADIV---FTAGadLTMVGLDV------TTQTLLT-REDLDelrdSGGKAGQFLAdmld 220
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 17565698 234 -----LATSIGRVKCEANgrqysycDEIAVATAIDEDKIAKKSqyLYVDVELNGtKTRGQVVVDWT-EQLWSNEEAPN 305
Cdd:cd02650 221 yyidfYQESPGLRGCALH-------DPLAVAAAVDPSLFTTRE--GVVRVETEG-PTRGRTIGDRDgRRFWDSSPNAT 288
|
|
| nuc_hydro_3 |
cd02653 |
NH_3: A subgroup of nucleoside hydrolases. This group contains eukaryotic and bacterial ... |
7-293 |
9.74e-36 |
|
NH_3: A subgroup of nucleoside hydrolases. This group contains eukaryotic and bacterial proteins similar to nucleoside hydrolases. Nucleoside hydrolases cleave the N-glycosidic bond in nucleosides generating ribose and the respective base. These enzymes vary in their substrate specificity.
Pssm-ID: 239119 [Multi-domain] Cd Length: 320 Bit Score: 131.73 E-value: 9.74e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17565698 7 KLVIDSDGVSDDVRAISLALQHPKAEILAFTAVHGCVTVDQACANIKRTIRANDRSNIPVYKGAAKSiLSLPKDDTvSDF 86
Cdd:cd02653 1 KVIIDCDPGIDDALALLYLLASPDLDVVGITTTAGNVPVEQVAANALGVLELLGRTDIPVYLGADKP-LAGPLTTA-QDT 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17565698 87 FGIDGIGDKPEEFPKVERSDFEGEGkhaslALIDILRENRDATLVTIGPLTNVAIALQLCEEFSTYPSRLVIMGGNYYAV 166
Cdd:cd02653 79 HGPDGLGYAELPASTRTLSDESAAQ-----AWVDLARAHPDLIGLATGPLTNLALALREEPELPRLLRRLVIMGGAFNSR 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17565698 167 GNVdgGSSAEYNFHGDPEAASIVLRRMKCP---ITIVPweafyfeskthdasVDFSAHLKYGTPLANYL-SLATSIGRVK 242
Cdd:cd02653 154 GNT--SPVAEWNYWVDPEAAKEVLAAFGGHpvrPTICG--------------LDVTRAVVLTPNLLERLaRAKDSVGAFI 217
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 17565698 243 CEA--------NGRQYSYC----DEIAVATAIDEDKIAKKSqyLYVDVELNGTkTRGQVVVDW 293
Cdd:cd02653 218 EDAlrfyfefhWAYGHGYGavihDPLAAAVALNPNLARGRP--AYVDVECTGV-LTGQTVVDW 277
|
|
| PLN02717 |
PLN02717 |
uridine nucleosidase |
7-190 |
4.20e-32 |
|
uridine nucleosidase
Pssm-ID: 178319 [Multi-domain] Cd Length: 316 Bit Score: 122.02 E-value: 4.20e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17565698 7 KLVIDSDGVSDDVRAISLALQHPKAEILAFTAVHGCVTVDQACANIKRTIRANDRSNIPVYKGAAKSILSLPKDdTVSDF 86
Cdd:PLN02717 2 KLIIDTDPGIDDAMAILMALRSPEVEVIGLTTIFGNVTTKLATRNALHLLEMAGRPDVPVAEGSHEPLKGGTKP-RIADF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17565698 87 F-GIDGIGDKPEEFPKVERSDfegegKHASLALIDILREN-RDATLVTIGPLTNVAIALQLCEEFSTYPSRLVIMGGNYY 164
Cdd:PLN02717 81 VhGSDGLGNTNLPPPKGKKIE-----KSAAEFLVEKVSEYpGEVTVVALGPLTNLALAIKLDPSFAKKVGQIVVLGGAFF 155
|
170 180
....*....|....*....|....*.
gi 17565698 165 AVGNVDggSSAEYNFHGDPEAASIVL 190
Cdd:PLN02717 156 VNGNVN--PAAEANIFGDPEAADIVF 179
|
|
| nuc_hydro_CjNH |
cd02654 |
nuc_hydro_CjNH. Nucleoside hydrolases similar to Campylobacter jejuni nucleoside hydrolase. ... |
7-327 |
1.77e-30 |
|
nuc_hydro_CjNH. Nucleoside hydrolases similar to Campylobacter jejuni nucleoside hydrolase. This group contains eukaryotic and bacterial proteins similar to C. jejuni nucleoside hydrolase. Nucleoside hydrolases cleave the N-glycosidic bond in nucleosides generating ribose and the respective base. These enzymes vary in their substrate specificity. C. jejuni nucleoside hydrolase is inactive against natural nucleosides or against common nucleoside analogues.
Pssm-ID: 239120 [Multi-domain] Cd Length: 318 Bit Score: 117.66 E-value: 1.77e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17565698 7 KLVIDSDGV----SDDVRAISLALQHPKAEILAFTAVHGCVTVDQACANIKRTIRANDRSNIPVYKGAAKSILSlPKDDT 82
Cdd:cd02654 1 KVILDNDIAmgrdTDDGLALALLLWSPEVELLGLSAVSGNCWLSAVTYNVLRMLELAGADAIPVYAGANTPLGR-TNRAF 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17565698 83 --VSDFFGI---DGIGDKPEEFPKVERSDFEGEGKHASLALIDILREN-RDATLVTIGPLTNVAIALQLCEEFSTYPSRL 156
Cdd:cd02654 80 haWESLYGAylwQGAWSPEYSDMYTNASIIRNASIPAALFMIEMVRKHpHEVSIVAAGPLTNLALALRIDPDFAPLAKEL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17565698 157 VIMGGNYYAVGNVDGGSSA-EYNFHGDPEAASIVLrRMKCPITIVPWEAFYFESKTHDasvdfsaHLKYGTPLANYLS-- 233
Cdd:cd02654 160 VIMGGYLDDIGEFVNRHYAsDFNLIMDPEAASIVL-TAPWKSITIPGNVTNRTCLTPE-------QIKADDPLRDFIRet 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17565698 234 LATSIGRVK-CEANGRQYSYCDEIAVATAIDeDKIAKKSQYLYVDVElNGTKTRGQVVVDWTEQLwsneeAPNQHThRRV 312
Cdd:cd02654 232 LDLPIDYAKeFVGTGDGLPMWDELASAVALD-PELATSSETFYIDVQ-TDSDGGGQLIWPEDLLL-----AKGLRP-YHV 303
|
330
....*....|....*
gi 17565698 313 KFVTSYDVHTVDKWL 327
Cdd:cd02654 304 KVITAVDVAAFLNLI 318
|
|
| PRK10768 |
PRK10768 |
ribonucleoside hydrolase RihC; Provisional |
5-327 |
4.38e-30 |
|
ribonucleoside hydrolase RihC; Provisional
Pssm-ID: 182713 [Multi-domain] Cd Length: 304 Bit Score: 116.16 E-value: 4.38e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17565698 5 KVKLVIDSDGVSDDVRAISLALQHPKAEILAFTAVHGCVTVDQACANIKRTIRANDrSNIPVYKGAAKSILSLPKDDT-V 83
Cdd:PRK10768 2 RLPIILDTDPGIDDAVAIAAALFAPELDLKLITTVAGNVSVEKTTRNALKLLHFFN-SDVPVAQGAAKPLVRPLRDAAsV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17565698 84 SDFFGIDGIgdkpeEFPKVERSDFEgegKHASLALIDILRENRDA-TLVTIGPLTNVAIALQLCEEFSTYPSRLVIMGGN 162
Cdd:PRK10768 81 HGESGMEGY-----DFPEHTRKPLS---IPAVEAMRDALMNAPEPvTLVAIGPLTNIALLLSTYPEVKPYIKRIVLMGGS 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17565698 163 yYAVGNVdgGSSAEYNFHGDPEAASIVLRRmKCPITI----VPWEAFYfeskTHDASVDFSAHLKYGTPLANYL------ 232
Cdd:PRK10768 153 -AGRGNV--TPNAEFNIAVDPEAAAIVFRS-GIPIVMcgldVTNQALL----TPDYLATLPELNRTGKMLHALFshyrsg 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17565698 233 SLATSIgrvkceangRQYSYCdeiAVATAIDEDKIakKSQYLYVDVELNGTKTRGQVVVDwTEQLWSNEeaPNqhthrrV 312
Cdd:PRK10768 225 SMQTGL---------RMHDVC---AIAYLLRPELF--TLKPCFVDVETQGEFTAGATVVD-IDGRLGKP--AN------A 281
|
330
....*....|....*
gi 17565698 313 KFVTSYDVHTVDKWL 327
Cdd:PRK10768 282 QVALDIDVDGFQKWF 296
|
|
| nuc_hydro_1 |
cd02648 |
NH_1: A subgroup of nucleoside hydrolases. This group contains fungal proteins similar to ... |
5-292 |
6.34e-23 |
|
NH_1: A subgroup of nucleoside hydrolases. This group contains fungal proteins similar to nucleoside hydrolases. Nucleoside hydrolases cleave the N-glycosidic bond in nucleosides generating ribose and the respective base. These enzymes vary in their substrate specificity.
Pssm-ID: 239114 [Multi-domain] Cd Length: 367 Bit Score: 98.03 E-value: 6.34e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17565698 5 KVKLVIDSDGVSDDVRAISLALQHP-KAEILAFTAVHGCVTVDQACANI---------KRTIRANDRSNIPVY-KGAAKS 73
Cdd:cd02648 1 PHPIIIDTDPGVDDVLAILLALSSPeEVDVALISLTFGNTTLDHALRNVlrlfhvlerERAWRATPGVRYRAFsADAEKP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17565698 74 ILSLPKDD-------TVSDFFGIDGIG---DKPEEFPKVERSD------FEGEGKHASLALIDILRENRD--ATLVTIGP 135
Cdd:cd02648 81 IVASGSDQplegerlTASYFHGRDGLSgvhWLHPDFTPVETWIpeivapLTPSDKPAYDVILDILREEPDhtVTIAALGP 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17565698 136 LTNVAIALQLCEEFSTYPSRLVIMGGNYYAVGNVDggSSAEYNFHGDPEAASIV---------LRRMKCPITIVPWE--- 203
Cdd:cd02648 161 LTNLAAAARKDPETFAKVGEVVVMGGAIDVPGNTS--PVAEFNCFADPYAAAVVideppstapEARRKLPLQVFPLDitt 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17565698 204 --AFYFESKTHDASVDFSAHLKyGTPLANYLS-------------LATSIGRVKCEANGRQYsycDEIAVATAIDEDKIA 268
Cdd:cd02648 239 ghTLPYSSLFATYVTPRDAPER-GSPLARWLEhvfistflthpraFTPEEFLPDRSELFEMH---DPLAVWYAIFADMPA 314
|
330 340 350
....*....|....*....|....*....|..
gi 17565698 269 K--------KSQYLYVDVELNGTKTRGQVVVD 292
Cdd:cd02648 315 TgsidgngwKHTPRDFRVETSGQWTRGMCVVD 346
|
|
| rihA |
PRK10443 |
ribonucleoside hydrolase 1; Provisional |
7-216 |
1.16e-22 |
|
ribonucleoside hydrolase 1; Provisional
Pssm-ID: 182465 [Multi-domain] Cd Length: 311 Bit Score: 96.28 E-value: 1.16e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17565698 7 KLVIDSDGVSDDVRAISLALQHPKAEILAFTAVHGCVTVDQACANIKRTIRANDRSNIPVYKGAAKSIL-SLPKDDTVSD 85
Cdd:PRK10443 4 PIILDCDPGHDDAIALVLALASPELDVKAVTTSAGNQTPEKTLRNALRMLTLLNRTDIPVAGGAVKPLMrELIIADNVHG 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17565698 86 FFGIDGigdkpeefPKVERSDFEGEGKHASLALIDILRENRDA-TLVTIGPLTNVAIALQLCEEFSTYPSRLVIMGGnyy 164
Cdd:PRK10443 84 ESGLDG--------PALPEPTFAPQNCTAVELMAKTLRESAEPvTLVSTGPQTNVALLLASHPELHSKIARIVIMGG--- 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 17565698 165 AVGNVDGGSSAEYNFHGDPEAASIVLRRmKCPITIVPWEAfyfeskTHDASV 216
Cdd:PRK10443 153 AMGLGNWTPAAEFNIYVDPEAAEIVFQS-GIPIVMAGLDV------THKAQI 197
|
|
| rihB |
PRK09955 |
ribosylpyrimidine nucleosidase; |
3-191 |
1.86e-21 |
|
ribosylpyrimidine nucleosidase;
Pssm-ID: 182166 [Multi-domain] Cd Length: 313 Bit Score: 93.09 E-value: 1.86e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17565698 3 VDKVKLVIDSDGVSDDVRAISLALQHPKAEILAFTAVHGCVTVDQACANiKRTIRANDRSNIPVYKGAAKSILslpKDDT 82
Cdd:PRK09955 1 MEKRKIILDCDPGHDDAIAMMMAAKHPAIDLLGITIVAGNQTLDKTLIN-GLNVCQKLEINVPVYAGMPQPIM---RQQI 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17565698 83 VSDFF----GIDGigdkpeefPKVERSDFEGEGKHASLALID-ILRENRDATLVTIGPLTNVAIALQLCEEFSTYPSRLV 157
Cdd:PRK09955 77 VADNIhgetGLDG--------PVFEPLTRQAESTHAVKYIIDtLMASDGDITLVPVGPLSNIAVAMRMQPAILPKIREIV 148
|
170 180 190
....*....|....*....|....*....|....
gi 17565698 158 IMGGNyYAVGNVDggSSAEYNFHGDPEAASIVLR 191
Cdd:PRK09955 149 LMGGA-YGTGNFT--PSAEFNIFADPEAARVVFT 179
|
|
| nuc_hydro_TvIAG |
cd02647 |
nuc_hydro_ TvIAG: Nucleoside hydrolases similar to the Inosine-adenosine-guanosine-preferring ... |
8-204 |
1.62e-16 |
|
nuc_hydro_ TvIAG: Nucleoside hydrolases similar to the Inosine-adenosine-guanosine-preferring nucleoside hydrolase from Trypanosoma vivax. Nucleoside hydrolases cleave the N-glycosidic bond in nucleosides generating ribose and the respective base. Nucleoside hydrolases vary in their substrate specificity. This group contains eukaryotic and bacterial proteins similar to the purine specific inosine-adenosine-guanosine-preferring nucleoside hydrolase (IAG-NH) from T. vivax. T. vivax IAG-NH is of the order of a thousand to ten thousand fold more specific towards the naturally occurring purine nucleosides, than towards the pyrimidine nucleosides.
Pssm-ID: 239113 [Multi-domain] Cd Length: 312 Bit Score: 79.00 E-value: 1.62e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17565698 8 LVIDSDGVSDDVRAISLALQHPKAEILAFT---AVHGCVTVDQACANIKRTIRANDRSNIPVYKGAAKSILSLPKDDTVS 84
Cdd:cd02647 3 VIFDHDGNVDDLVALLLLLKNEKVDLKGIGvsgIDADCYVEPAVSVTRKLIDRLGQRDAIPVGKGGSRAVNPFPRSWRRD 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17565698 85 DFFGIDgigDKPEEFPKVErSDFEGEGKHASLALID-ILRENRDATLVTIGPLTNVAIALQLCEEFSTYPSRLVIMGGNY 163
Cdd:cd02647 83 AAFSVD---HLPILNERYT-VETPLAEETAQLVLIEkIKASLEPVTLLVTGPLTNLARALDSDPDISSNIEEVYIMGGGV 158
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 17565698 164 YAVGNV-----DGgsSAEYNFHGDPEAASIVLRRmKCPITIVPWEA 204
Cdd:cd02647 159 DAPGNVftppsNG--TAEFNIFWDPLAAKTVFDS-GLKITLVPLDA 201
|
|
| nuc_hydro_2 |
cd02652 |
NH_2: A subgroup of nucleoside hydrolases. This group contains eukaryotic and bacterial ... |
8-208 |
3.37e-11 |
|
NH_2: A subgroup of nucleoside hydrolases. This group contains eukaryotic and bacterial proteins similar to nucleoside hydrolases. Nucleoside hydrolases cleave the N-glycosidic bond in nucleosides generating ribose and the respective base. These enzymes vary in their substrate specificity.
Pssm-ID: 239118 [Multi-domain] Cd Length: 293 Bit Score: 62.90 E-value: 3.37e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17565698 8 LVIDSD--GVSDDVRAISLALQHPKAEILAFTAVHGCVTVDQACANIKRtirANDRSNIPVykGAAKSILslPKDDTVSD 85
Cdd:cd02652 1 LILDTDigGDPDDALALALAHALQKCDLLAVTITLADASARRAIDAVNR---FYGRGDIPI--GADYHGW--PEDAKDHA 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17565698 86 FFGIDGIGDKPeefpKVERSDfegEGKHASLALIDILRENRDA--TLVTIGPLTNVAIALQLCEEFSTYP-------SRL 156
Cdd:cd02652 74 KFLLEGDRLHH----DLESAE---DALDAVKALRRLLASAEDAsvTIVSIGPLTNLAALLDADADPLTGPelvrqkvKRL 146
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 17565698 157 VIMGG-NYYAVGNVdggSSAEYNFHGDPEAASIVLRRMKCPITIVPWEAFYFE 208
Cdd:cd02652 147 VVMGGaFYDPDGNV---QHREYNFVTDPKAAQRVAGRAQHLGIPVRIVWSGYE 196
|
|
| PTZ00313 |
PTZ00313 |
inosine-adenosine-guanosine-nucleoside hydrolase; Provisional |
8-196 |
1.49e-07 |
|
inosine-adenosine-guanosine-nucleoside hydrolase; Provisional
Pssm-ID: 140334 [Multi-domain] Cd Length: 326 Bit Score: 52.17 E-value: 1.49e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17565698 8 LVIDSDGVSDDVRAISLALQHPKAeilafTAVHGCVTVDQACA-----NIKRTIRA--NDRSN---IPVYKGAAKSILSL 77
Cdd:PTZ00313 5 VILDHDGNHDDLVALALLLGNPEK-----VKVIGCICTDADCFvddafNVTGKLMCmmHAREAtplFPIGKSSFKGVNPF 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17565698 78 PKDDTVS----DFFGIDGIGDKPEEFPKV--ERSDFEGEGKHASLalidILRENRDATLVTIGPLTNVAIAL-QLCEEFS 150
Cdd:PTZ00313 80 PSEWRWSaknmDDLPCLNIPEHVAIWEKLkpENEALVGEELLADL----VMSSPEKVTICVTGPLSNVAWCIeKYGEEFT 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 17565698 151 TYPSRLVIMGGNYYAVGNV-----DGgsSAEYNFHGDPEAASIVLrrmKCP 196
Cdd:PTZ00313 156 KKVEECVIMGGAVDVGGNVflpgtDG--SAEWNIYWDPPAAKTVL---MCP 201
|
|
| |
