|
Name |
Accession |
Description |
Interval |
E-value |
| URH1 |
COG1957 |
Inosine-uridine nucleoside N-ribohydrolase [Nucleotide transport and metabolism]; ... |
21-332 |
4.47e-134 |
|
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: 383.73 E-value: 4.47e-134
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 763167304 21 APIDLIIDTDPGADDVVALFLAMASPdELNIRAITTVAGNVRLEKTSRNARLAREWAGREDIPVYAGAARPLVRKPIYAA 100
Cdd:COG1957 1 MMRKVIIDTDPGIDDALALLLALASP-EIDLLGITTVAGNVPLEQTTRNALKLLELAGRTDVPVAAGAARPLVRPLVTAE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 763167304 101 DVHGEEGLTGIQVHEPKAPLAQGNAVQYLVDTLgTAKPHSITIAMLGPQTNLALALIQRPDIAKGIKQVVVMGGAHFNGG 180
Cdd:COG1957 80 HVHGEDGLGGVDLPEPTRPPEPEHAVDFIIETL-RAAPGEVTLVALGPLTNLALALRKDPELAERIKRIVIMGGAFFVPG 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 763167304 181 NITPAAEFNLYADPHAAEVVLASGVQLIYLPLDVTHKLLTSDARLKQLAAVNNQASKRVVDILNAYITHDMDLYGMPGGP 260
Cdd:COG1957 159 NVTPVAEFNIYVDPEAAKIVFASGIPITMVGLDVTHQALLTPEDLARLAALGTPLGRFLADLLDFYLDFYRERYGLDGCP 238
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 763167304 261 VHDASVIAYLLKPELFSGRRIHMSIDSREGPSFGQTLADWYGVLKQPANVMWVEEGDAQGLFDLLSARLARL 332
Cdd:COG1957 239 LHDPLAVAYLLDPELFTTRPAPVDVETDGELTRGQTVVDWRGVTGRPPNARVALDVDAERFLDLLLERLARL 310
|
|
| nuc_hydro_IU_UC_XIUA |
cd02651 |
nuc_hydro_IU_UC_XIUA: inosine-uridine preferring, ... |
25-329 |
1.83e-126 |
|
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: 364.18 E-value: 1.83e-126
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 763167304 25 LIIDTDPGADDVVALFLAMASPdELNIRAITTVAGNVRLEKTSRNARLAREWAGREDIPVYAGAARPLVRKPIYAADVHG 104
Cdd:cd02651 2 IIIDCDPGHDDAVAILLALFHP-ELDLLGITTVAGNVPLEKTTRNALKLLTLLGRTDVPVAAGAARPLVRPLITASDIHG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 763167304 105 EEGLTGIQVHEPKAPLAQGNAVQYLVDTLgTAKPHSITIAMLGPQTNLALALIQRPDIAKGIKQVVVMGGAhFNGGNITP 184
Cdd:cd02651 81 ESGLDGADLPPPPRRPEDIHAVDAIIDTL-RASPEPITLVATGPLTNIALLLRKYPELAERIKEIVLMGGA-LGRGNITP 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 763167304 185 AAEFNLYADPHAAEVVLASGVQLIYLPLDVTHKLLTSDARLKQLAAVNNQASKRVVDILNAYITHDMDLYgMPGGPVHDA 264
Cdd:cd02651 159 AAEFNIFVDPEAAKIVFNSGIPITMVPLDVTHKALATPEVIERIRALGNPVGKMLAELLDFFAETYGSAF-TEGPPLHDP 237
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 763167304 265 SVIAYLLKPELFSGRRIHMSIDSREGPSFGQTLADWYGVLKQPANVMWVEEGDAQGLFDLLSARL 329
Cdd:cd02651 238 CAVAYLLDPELFTTKRANVDVETEGELTRGRTVVDLRGVTGRPANAQVAVDVDVEKFWDLLLEAL 302
|
|
| IU_nuc_hydro |
pfam01156 |
Inosine-uridine preferring nucleoside hydrolase; |
25-323 |
2.06e-91 |
|
Inosine-uridine preferring nucleoside hydrolase;
Pssm-ID: 460086 [Multi-domain] Cd Length: 253 Bit Score: 272.93 E-value: 2.06e-91
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 763167304 25 LIIDTDPGADDVVALFLAMASPdELNIRAITTVAGNVRLEKTSRNARLAREWAGREDIPVYAGAArplvrkpiyaadvhg 104
Cdd:pfam01156 1 VIIDTDPGIDDALALLLALASP-EIELLGITTVAGNVSLEQTTRNALRLLELGGRDDIPVYAGEA--------------- 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 763167304 105 eegltgiqvhepkaplaqgnavqylvdtlgTAKPHSITIAMLGPQTNLALALIQRPDIAKGIKQVVVMGGAHFNGGNITP 184
Cdd:pfam01156 65 ------------------------------IREPGEVTLVATGPLTNLALALRLDPELAKKIKELVIMGGAFGVRGNVTP 114
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 763167304 185 AAEFNLYADPHAAEVVLASGVQLIYLPLDVTHKLLTSDARLKQLAAVNNQASKRVVDILNAYITHDMDLYGMPGGPVHDA 264
Cdd:pfam01156 115 AAEFNIFVDPEAAKIVFTSGLPITMVPLDVTHQALLTPEDLERLAALGTPLGRFLADLLRFYAEFYRERFGIDGPPLHDP 194
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 763167304 265 SVIAYLLKPELFSGRRIHMSIDSREGPSFGQTLADWYGVLKQPANVMWVEEGDAQGLFD 323
Cdd:pfam01156 195 LAVAVALDPELFTTRRLNVDVETTGGLTRGQTVVDDRGGWGKPPNVRVATDVDVDRFWE 253
|
|
| rihA |
PRK10443 |
ribonucleoside hydrolase 1; Provisional |
22-331 |
3.83e-80 |
|
ribonucleoside hydrolase 1; Provisional
Pssm-ID: 182465 [Multi-domain] Cd Length: 311 Bit Score: 246.50 E-value: 3.83e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 763167304 22 PIDLIIDTDPGADDVVALFLAMASPdELNIRAITTVAGNVRLEKTSRNARLAREWAGREDIPVYAGAARPLVRKPIYAAD 101
Cdd:PRK10443 2 ALPIILDCDPGHDDAIALVLALASP-ELDVKAVTTSAGNQTPEKTLRNALRMLTLLNRTDIPVAGGAVKPLMRELIIADN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 763167304 102 VHGEEGLTGIQVHEPK-APLAQgNAVQYLVDTLgTAKPHSITIAMLGPQTNLALALIQRPDIAKGIKQVVVMGGAhFNGG 180
Cdd:PRK10443 81 VHGESGLDGPALPEPTfAPQNC-TAVELMAKTL-RESAEPVTLVSTGPQTNVALLLASHPELHSKIARIVIMGGA-MGLG 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 763167304 181 NITPAAEFNLYADPHAAEVVLASGVQLIYLPLDVTHKLLTSDARLKQLAAVNNQASKRVVDILNAY-ITHDMDLYGMPGG 259
Cdd:PRK10443 158 NWTPAAEFNIYVDPEAAEIVFQSGIPIVMAGLDVTHKAQIMDEDIERIRAIGNPVATIVAELLDFFmEYHKDEKWGFVGA 237
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 763167304 260 PVHDASVIAYLLKPELFSGRRIHMSIDSREGPSFGQTLADWYGVLKQPANVMWVEEGDAQGLFDLLSARLAR 331
Cdd:PRK10443 238 PLHDPCTIAWLLKPELFTTVERWVGVETQGEYTQGMTVVDYYQLTGNKPNATVLVDVDRQGFVDLLAERLKF 309
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| URH1 |
COG1957 |
Inosine-uridine nucleoside N-ribohydrolase [Nucleotide transport and metabolism]; ... |
21-332 |
4.47e-134 |
|
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: 383.73 E-value: 4.47e-134
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 763167304 21 APIDLIIDTDPGADDVVALFLAMASPdELNIRAITTVAGNVRLEKTSRNARLAREWAGREDIPVYAGAARPLVRKPIYAA 100
Cdd:COG1957 1 MMRKVIIDTDPGIDDALALLLALASP-EIDLLGITTVAGNVPLEQTTRNALKLLELAGRTDVPVAAGAARPLVRPLVTAE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 763167304 101 DVHGEEGLTGIQVHEPKAPLAQGNAVQYLVDTLgTAKPHSITIAMLGPQTNLALALIQRPDIAKGIKQVVVMGGAHFNGG 180
Cdd:COG1957 80 HVHGEDGLGGVDLPEPTRPPEPEHAVDFIIETL-RAAPGEVTLVALGPLTNLALALRKDPELAERIKRIVIMGGAFFVPG 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 763167304 181 NITPAAEFNLYADPHAAEVVLASGVQLIYLPLDVTHKLLTSDARLKQLAAVNNQASKRVVDILNAYITHDMDLYGMPGGP 260
Cdd:COG1957 159 NVTPVAEFNIYVDPEAAKIVFASGIPITMVGLDVTHQALLTPEDLARLAALGTPLGRFLADLLDFYLDFYRERYGLDGCP 238
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 763167304 261 VHDASVIAYLLKPELFSGRRIHMSIDSREGPSFGQTLADWYGVLKQPANVMWVEEGDAQGLFDLLSARLARL 332
Cdd:COG1957 239 LHDPLAVAYLLDPELFTTRPAPVDVETDGELTRGQTVVDWRGVTGRPPNARVALDVDAERFLDLLLERLARL 310
|
|
| nuc_hydro_IU_UC_XIUA |
cd02651 |
nuc_hydro_IU_UC_XIUA: inosine-uridine preferring, ... |
25-329 |
1.83e-126 |
|
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: 364.18 E-value: 1.83e-126
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 763167304 25 LIIDTDPGADDVVALFLAMASPdELNIRAITTVAGNVRLEKTSRNARLAREWAGREDIPVYAGAARPLVRKPIYAADVHG 104
Cdd:cd02651 2 IIIDCDPGHDDAVAILLALFHP-ELDLLGITTVAGNVPLEKTTRNALKLLTLLGRTDVPVAAGAARPLVRPLITASDIHG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 763167304 105 EEGLTGIQVHEPKAPLAQGNAVQYLVDTLgTAKPHSITIAMLGPQTNLALALIQRPDIAKGIKQVVVMGGAhFNGGNITP 184
Cdd:cd02651 81 ESGLDGADLPPPPRRPEDIHAVDAIIDTL-RASPEPITLVATGPLTNIALLLRKYPELAERIKEIVLMGGA-LGRGNITP 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 763167304 185 AAEFNLYADPHAAEVVLASGVQLIYLPLDVTHKLLTSDARLKQLAAVNNQASKRVVDILNAYITHDMDLYgMPGGPVHDA 264
Cdd:cd02651 159 AAEFNIFVDPEAAKIVFNSGIPITMVPLDVTHKALATPEVIERIRALGNPVGKMLAELLDFFAETYGSAF-TEGPPLHDP 237
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 763167304 265 SVIAYLLKPELFSGRRIHMSIDSREGPSFGQTLADWYGVLKQPANVMWVEEGDAQGLFDLLSARL 329
Cdd:cd02651 238 CAVAYLLDPELFTTKRANVDVETEGELTRGRTVVDLRGVTGRPANAQVAVDVDVEKFWDLLLEAL 302
|
|
| IU_nuc_hydro |
pfam01156 |
Inosine-uridine preferring nucleoside hydrolase; |
25-323 |
2.06e-91 |
|
Inosine-uridine preferring nucleoside hydrolase;
Pssm-ID: 460086 [Multi-domain] Cd Length: 253 Bit Score: 272.93 E-value: 2.06e-91
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 763167304 25 LIIDTDPGADDVVALFLAMASPdELNIRAITTVAGNVRLEKTSRNARLAREWAGREDIPVYAGAArplvrkpiyaadvhg 104
Cdd:pfam01156 1 VIIDTDPGIDDALALLLALASP-EIELLGITTVAGNVSLEQTTRNALRLLELGGRDDIPVYAGEA--------------- 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 763167304 105 eegltgiqvhepkaplaqgnavqylvdtlgTAKPHSITIAMLGPQTNLALALIQRPDIAKGIKQVVVMGGAHFNGGNITP 184
Cdd:pfam01156 65 ------------------------------IREPGEVTLVATGPLTNLALALRLDPELAKKIKELVIMGGAFGVRGNVTP 114
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 763167304 185 AAEFNLYADPHAAEVVLASGVQLIYLPLDVTHKLLTSDARLKQLAAVNNQASKRVVDILNAYITHDMDLYGMPGGPVHDA 264
Cdd:pfam01156 115 AAEFNIFVDPEAAKIVFTSGLPITMVPLDVTHQALLTPEDLERLAALGTPLGRFLADLLRFYAEFYRERFGIDGPPLHDP 194
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 763167304 265 SVIAYLLKPELFSGRRIHMSIDSREGPSFGQTLADWYGVLKQPANVMWVEEGDAQGLFD 323
Cdd:pfam01156 195 LAVAVALDPELFTTRRLNVDVETTGGLTRGQTVVDDRGGWGKPPNVRVATDVDVDRFWE 253
|
|
| rihA |
PRK10443 |
ribonucleoside hydrolase 1; Provisional |
22-331 |
3.83e-80 |
|
ribonucleoside hydrolase 1; Provisional
Pssm-ID: 182465 [Multi-domain] Cd Length: 311 Bit Score: 246.50 E-value: 3.83e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 763167304 22 PIDLIIDTDPGADDVVALFLAMASPdELNIRAITTVAGNVRLEKTSRNARLAREWAGREDIPVYAGAARPLVRKPIYAAD 101
Cdd:PRK10443 2 ALPIILDCDPGHDDAIALVLALASP-ELDVKAVTTSAGNQTPEKTLRNALRMLTLLNRTDIPVAGGAVKPLMRELIIADN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 763167304 102 VHGEEGLTGIQVHEPK-APLAQgNAVQYLVDTLgTAKPHSITIAMLGPQTNLALALIQRPDIAKGIKQVVVMGGAhFNGG 180
Cdd:PRK10443 81 VHGESGLDGPALPEPTfAPQNC-TAVELMAKTL-RESAEPVTLVSTGPQTNVALLLASHPELHSKIARIVIMGGA-MGLG 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 763167304 181 NITPAAEFNLYADPHAAEVVLASGVQLIYLPLDVTHKLLTSDARLKQLAAVNNQASKRVVDILNAY-ITHDMDLYGMPGG 259
Cdd:PRK10443 158 NWTPAAEFNIYVDPEAAEIVFQSGIPIVMAGLDVTHKAQIMDEDIERIRAIGNPVATIVAELLDFFmEYHKDEKWGFVGA 237
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 763167304 260 PVHDASVIAYLLKPELFSGRRIHMSIDSREGPSFGQTLADWYGVLKQPANVMWVEEGDAQGLFDLLSARLAR 331
Cdd:PRK10443 238 PLHDPCTIAWLLKPELFTTVERWVGVETQGEYTQGMTVVDYYQLTGNKPNATVLVDVDRQGFVDLLAERLKF 309
|
|
| nuc_hydro_CaPnhB |
cd02650 |
NH_hydro_CaPnhB: A subgroup of nucleoside hydrolases similar to Corynebacterium ammoniagenes ... |
25-312 |
3.74e-79 |
|
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: 243.72 E-value: 3.74e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 763167304 25 LIIDTDPGADDVVALFLAMASPDeLNIRAITTVAGNVRLEKTSRNARLAREWAGREDIPVYAGAARPLVRKPIYAAD-VH 103
Cdd:cd02650 2 LILDTDPGIDDAMALAYALAHPD-VDLIGVTTVYGNVTIETATRNALALLELFGRPDVPVAEGAAKPLTRPPFRIATfVH 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 763167304 104 GEEGLTGIQVHEPKAPLAQGNAVQYLVDTLGTAkPHSITIAMLGPQTNLALALIQRPDIAKGIKQVVVMGGAHFNGGNIT 183
Cdd:cd02650 81 GDNGLGDVELPAPPRQPEDESAADFLIELANEY-PGELTLVAVGPLTNLALALARDPDFAKLVKQVVVMGGAFTVPGNVT 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 763167304 184 PAAEFNLYADPHAAEVVLASGVQLIYLPLDVTHKLLTSDARLKQLAAVNNQASKRVVDILNAYITHDMDLYGMPGGPVHD 263
Cdd:cd02650 160 PAAEANIHGDPEAADIVFTAGADLTMVGLDVTTQTLLTREDLDELRDSGGKAGQFLADMLDYYIDFYQESPGLRGCALHD 239
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 763167304 264 ASVIAYLLKPELFSGRRIHMSIDSrEGPSFGQTLADWYGVLKQPANVMW 312
Cdd:cd02650 240 PLAVAAAVDPSLFTTREGVVRVET-EGPTRGRTIGDRDGRRFWDSSPNA 287
|
|
| rihB |
PRK09955 |
ribosylpyrimidine nucleosidase; |
25-325 |
2.17e-76 |
|
ribosylpyrimidine nucleosidase;
Pssm-ID: 182166 [Multi-domain] Cd Length: 313 Bit Score: 237.15 E-value: 2.17e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 763167304 25 LIIDTDPGADDVVALFLAMASPdELNIRAITTVAGNVRLEKTSRNArLAREWAGREDIPVYAGAARPLVRKPIYAADVHG 104
Cdd:PRK09955 6 IILDCDPGHDDAIAMMMAAKHP-AIDLLGITIVAGNQTLDKTLING-LNVCQKLEINVPVYAGMPQPIMRQQIVADNIHG 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 763167304 105 EEGLTGIQVHEPKAPLAQGNAVQYLVDTLgTAKPHSITIAMLGPQTNLALALIQRPDIAKGIKQVVVMGGAhFNGGNITP 184
Cdd:PRK09955 84 ETGLDGPVFEPLTRQAESTHAVKYIIDTL-MASDGDITLVPVGPLSNIAVAMRMQPAILPKIREIVLMGGA-YGTGNFTP 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 763167304 185 AAEFNLYADPHAAEVVLASGVQLIYLPLDVTHKLLTSDARLKQLAAVNNQASKRVVDILNAYITHDMDLYGMPGGPVHDA 264
Cdd:PRK09955 162 SAEFNIFADPEAARVVFTSGVPLVMMGLDLTNQTVCTPDVIARMERAGGPAGELFSDIMNFTLKTQFENYGLAGGPVHDA 241
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 763167304 265 SVIAYLLKPELFSGRRIHMSIDSREGPSFGQTLADWYGVLKQPANVMWVEEGDAQGLFDLL 325
Cdd:PRK09955 242 TCIGYLINPDGIKTQEMYVEVDVNSGPCYGRTVCDELGVLGKPANTKVGITIDTDWFWGLV 302
|
|
| PRK10768 |
PRK10768 |
ribonucleoside hydrolase RihC; Provisional |
22-310 |
9.66e-74 |
|
ribonucleoside hydrolase RihC; Provisional
Pssm-ID: 182713 [Multi-domain] Cd Length: 304 Bit Score: 229.80 E-value: 9.66e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 763167304 22 PIdlIIDTDPGADDVVALFLAMASPdELNIRAITTVAGNVRLEKTSRNA-RLAREWagREDIPVYAGAARPLVRKPIYAA 100
Cdd:PRK10768 4 PI--ILDTDPGIDDAVAIAAALFAP-ELDLKLITTVAGNVSVEKTTRNAlKLLHFF--NSDVPVAQGAAKPLVRPLRDAA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 763167304 101 DVHGEEGLTGIQVHEPKAPLAQGNAVQYLVDTLgTAKPHSITIAMLGPQTNLALALIQRPDIAKGIKQVVVMGGAhFNGG 180
Cdd:PRK10768 79 SVHGESGMEGYDFPEHTRKPLSIPAVEAMRDAL-MNAPEPVTLVAIGPLTNIALLLSTYPEVKPYIKRIVLMGGS-AGRG 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 763167304 181 NITPAAEFNLYADPHAAEVVLASGVQLIYLPLDVTHK-LLTSD--ARLKQLaavnNQASKRVVDILNAYITHDMDlygmP 257
Cdd:PRK10768 157 NVTPNAEFNIAVDPEAAAIVFRSGIPIVMCGLDVTNQaLLTPDylATLPEL----NRTGKMLHALFSHYRSGSMQ----T 228
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 763167304 258 GGPVHDASVIAYLLKPELFSGRRIHMSIDSrEGP-SFGQTLADWYGVLKQPANV 310
Cdd:PRK10768 229 GLRMHDVCAIAYLLRPELFTLKPCFVDVET-QGEfTAGATVVDIDGRLGKPANA 281
|
|
| nuc_hydro |
cd00455 |
nuc_hydro: Nucleoside hydrolases. Nucleoside hydrolases cleave the N-glycosidic bond in ... |
25-302 |
7.19e-71 |
|
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: 222.20 E-value: 7.19e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 763167304 25 LIIDTDPGADDVVALFLAMASPdELNIRAITTVAGNVRLEKTSRNARLAREWAGREDIPVYAGAARPLVRKPIYAADVHG 104
Cdd:cd00455 1 VILDTDPGIDDAFALMYALLHP-EIELVGIVATYGNVTLEQATQNAAYLLELLGRLDIPVYAGATRPLTGEIPAAYPEIH 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 763167304 105 EEGLTGIqVHEPKAPLAQGNAVQYLVDTLgTAKPHSITIAMLGPQTNLALALIQRPDIAKGIKQVVVMGGAHFNGGNITP 184
Cdd:cd00455 80 GEGGLGL-PIPPIIEADDPEAVQLLIDLI-RKYPDEITIVALGPLTNLAMAFILDPDIKDRVKEIVIMGGAFLVPGNVTP 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 763167304 185 AAEFNLYADPHAAEVVLASGVQLIYLPLDVTHKLLTSDARLKQLAAVNNQASKRVVDILNAYiTHDMDLYGMPGGPVHDA 264
Cdd:cd00455 158 VAEANFYGDPEAANIVFNSAKNLTIVPLDVTNQAVLTPPMVERIFEQGTSIGLLIKPMIDYY-YKAYQKPGIEGSPIHDP 236
|
250 260 270
....*....|....*....|....*....|....*...
gi 763167304 265 SVIAYLLKPELFSGRRIHMSIDSrEGPSFGQTLADWYG 302
Cdd:cd00455 237 LAVAYLLNPSMFDYSKVPVDVDT-DGLTRGQTIADFRE 273
|
|
| PLN02717 |
PLN02717 |
uridine nucleosidase |
25-329 |
9.46e-71 |
|
uridine nucleosidase
Pssm-ID: 178319 [Multi-domain] Cd Length: 316 Bit Score: 222.56 E-value: 9.46e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 763167304 25 LIIDTDPGADDVVALFLAMASPdELNIRAITTVAGNVRLEKTSRNARLAREWAGREDIPVYAGAARPLVR--KPIYAADV 102
Cdd:PLN02717 3 LIIDTDPGIDDAMAILMALRSP-EVEVIGLTTIFGNVTTKLATRNALHLLEMAGRPDVPVAEGSHEPLKGgtKPRIADFV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 763167304 103 HGEEGLTGIQVHEPKAPLAQGNAVQYLVDTLgTAKPHSITIAMLGPQTNLALALIQRPDIAKGIKQVVVMGGAHFNGGNI 182
Cdd:PLN02717 82 HGSDGLGNTNLPPPKGKKIEKSAAEFLVEKV-SEYPGEVTVVALGPLTNLALAIKLDPSFAKKVGQIVVLGGAFFVNGNV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 763167304 183 TPAAEFNLYADPHAAEVVLASGVQLIYLPLDVTHKLLTSDARLKQLAAVNNQASKRVVDILNAYITHDMDLYGMPGGPVH 262
Cdd:PLN02717 161 NPAAEANIFGDPEAADIVFTSGADITVVGINVTTQVVLTDADLEELRDSKGKYAQFLCDICKFYRDWHRKSYGIDGIYLH 240
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 763167304 263 DASVIAYLLKPELFSGRRIHMSIDSrEGPSFGQTLAD-----------WYGvlKQPANVMWVEegDAQGLFDLLSARL 329
Cdd:PLN02717 241 DPTALLAAVRPSLFTYKEGVVRVET-EGICRGLTLFDnglkrwngenaWTG--RPPVKVAVTV--DAPAVVELVKERL 313
|
|
| nuc_hydro_CeIAG |
cd02649 |
nuc_hydro_CeIAG: Nucleoside hydrolases similar to the inosine-adenosine-guanosine-preferring ... |
25-325 |
5.23e-63 |
|
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: 202.49 E-value: 5.23e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 763167304 25 LIIDTDPGADDVVALFLAMASPDeLNIRAITTVAGNVRLEKTSRNARLAREWAGREDIPVYAGAARPLVRKPIYAADVHG 104
Cdd:cd02649 3 LIIDTDCGGDDAWALLMALASPN-VEVLAITCVHGNTNVEQVVKNALRVLEACGRRDIPVYRGASKPLLGPGPTAAYFHG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 763167304 105 EEGLTGIQVHEPKA--PLAQGNAVQYLVDtLGTAKPHSITIAMLGPQTNLALALIQRPDIAKGIKQVVVMGGAHFNGGNI 182
Cdd:cd02649 82 KDGFGDVGFPEPKDelELQKEHAVDAIIR-LVREYPGEITLVALGPLTNLALAYRLDPSLPQKIKRLYIMGGNREGVGNT 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 763167304 183 TPAAEFNLYADPHAAEVVL-ASGVQLIYLPLDVTHKLLTSDARLKQLAAvNNQASKRVVDILNAYI-THDMDLYGMPGGP 260
Cdd:cd02649 161 TPAAEFNFHVDPEAAHIVLnSFGCPITIVPWETTLLAFPLDWEFEDKWA-NRLEKALFAESLNRREyAFASEGLGGDGWV 239
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 763167304 261 VHDASVIAYLLKPELFSGR-RIHMSIDSREGPSFGQTLADWYGVLKQPANVMWVEEGDAQGLFDLL 325
Cdd:cd02649 240 PCDALAVAAALDPSIITRRlTYAVDVELHGELTRGQMVVDWLGTLKKKPNARVITKIDREKFKELL 305
|
|
| nuc_hydro_3 |
cd02653 |
NH_3: A subgroup of nucleoside hydrolases. This group contains eukaryotic and bacterial ... |
25-329 |
7.41e-61 |
|
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: 197.21 E-value: 7.41e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 763167304 25 LIIDTDPGADDVVALFLAMASPDeLNIRAITTVAGNVRLEKTSRNARLAREWAGREDIPVYAGAARPLVRKPIYAADVHG 104
Cdd:cd02653 2 VIIDCDPGIDDALALLYLLASPD-LDVVGITTTAGNVPVEQVAANALGVLELLGRTDIPVYLGADKPLAGPLTTAQDTHG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 763167304 105 EEGLTGIQVHEPKAPLAQGNAVQYLVDTLgTAKPHSITIAmLGPQTNLALALIQRPDIAKGIKQVVVMGGAHFNGGNITP 184
Cdd:cd02653 81 PDGLGYAELPASTRTLSDESAAQAWVDLA-RAHPDLIGLA-TGPLTNLALALREEPELPRLLRRLVIMGGAFNSRGNTSP 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 763167304 185 AAEFNLYADPHAAEVVLA----SGVQLIYLPLDVTHKLLTSDARLKQLAAVNNQASKRVVDILNAYIT-HDMDLYGMpGG 259
Cdd:cd02653 159 VAEWNYWVDPEAAKEVLAafggHPVRPTICGLDVTRAVVLTPNLLERLARAKDSVGAFIEDALRFYFEfHWAYGHGY-GA 237
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 763167304 260 PVHDASVIAYLLKPELFSGRRIHMSIDSrEGPSFGQTLADWYGVLKQPANVMWVEEGDAQGLFDLLSARL 329
Cdd:cd02653 238 VIHDPLAAAVALNPNLARGRPAYVDVEC-TGVLTGQTVVDWAGFWGKGANAEILTKVDSQDFMALFIERV 306
|
|
| nuc_hydro_1 |
cd02648 |
NH_1: A subgroup of nucleoside hydrolases. This group contains fungal proteins similar to ... |
22-215 |
1.20e-39 |
|
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: 143.10 E-value: 1.20e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 763167304 22 PIDLIIDTDPGADDVVALFLAMASPDELNIRAITTVAGNVRLEKTSRNAR-----LAREWAGREDI-------------P 83
Cdd:cd02648 1 PHPIIIDTDPGVDDVLAILLALSSPEEVDVALISLTFGNTTLDHALRNVLrlfhvLERERAWRATPgvryrafsadaekP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 763167304 84 VYA-GAARPLVRKPIYAADVHGEEGLTGI------------QVHEPKAPLAQGN--AVQYLVDTLGTAKPHSITIAMLGP 148
Cdd:cd02648 81 IVAsGSDQPLEGERLTASYFHGRDGLSGVhwlhpdftpvetWIPEIVAPLTPSDkpAYDVILDILREEPDHTVTIAALGP 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 763167304 149 QTNLALALIQRPDIAKGIKQVVVMGGAHFNGGNITPAAEFNLYADPHAAEVVLASG----------VQLIYLPLDVT 215
Cdd:cd02648 161 LTNLAAAARKDPETFAKVGEVVVMGGAIDVPGNTSPVAEFNCFADPYAAAVVIDEPpstapearrkLPLQVFPLDIT 237
|
|
| nuc_hydro_CjNH |
cd02654 |
nuc_hydro_CjNH. Nucleoside hydrolases similar to Campylobacter jejuni nucleoside hydrolase. ... |
25-275 |
5.34e-31 |
|
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: 118.81 E-value: 5.34e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 763167304 25 LIIDTD----PGADDVVALFLAmASPDELNIRAITTVAGNVRLEKTSRNARLAREWAGREDIPVYAGAARPLVRK----- 95
Cdd:cd02654 2 VILDNDiamgRDTDDGLALALL-LWSPEVELLGLSAVSGNCWLSAVTYNVLRMLELAGADAIPVYAGANTPLGRTnrafh 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 763167304 96 -------PIYAADVHGEEGLTGiQVHEPKAPLAQGNAVQYLVDTLgTAKPHSITIAMLGPQTNLALALIQRPDIAKGIKQ 168
Cdd:cd02654 81 aweslygAYLWQGAWSPEYSDM-YTNASIIRNASIPAALFMIEMV-RKHPHEVSIVAAGPLTNLALALRIDPDFAPLAKE 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 763167304 169 VVVMGGAHFNGG---NITPAAEFNLYADPHAAEVVLASGVQLIYLPLDVTHKLLTSDARLKQLAAVNNqaskRVVDILNA 245
Cdd:cd02654 159 LVIMGGYLDDIGefvNRHYASDFNLIMDPEAASIVLTAPWKSITIPGNVTNRTCLTPEQIKADDPLRD----FIRETLDL 234
|
250 260 270
....*....|....*....|....*....|.
gi 763167304 246 YITHDMDLYGMPGG-PVHDASVIAYLLKPEL 275
Cdd:cd02654 235 PIDYAKEFVGTGDGlPMWDELASAVALDPEL 265
|
|
| nuc_hydro_TvIAG |
cd02647 |
nuc_hydro_ TvIAG: Nucleoside hydrolases similar to the Inosine-adenosine-guanosine-preferring ... |
25-230 |
6.00e-28 |
|
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: 110.59 E-value: 6.00e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 763167304 25 LIIDTDPGADDVVALFLaMASPDELNIRAIT----------TVAGNVRLEKTSRnarlareWAGREDIPVYAG---AARP 91
Cdd:cd02647 3 VIFDHDGNVDDLVALLL-LLKNEKVDLKGIGvsgidadcyvEPAVSVTRKLIDR-------LGQRDAIPVGKGgsrAVNP 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 763167304 92 LVRKPIYAADVHGEEGLTGIQVHEPKAPLAQGNAVQYLVDTLgTAKPHSITIAMLGPQTNLALALIQRPDIAKGIKQVVV 171
Cdd:cd02647 75 FPRSWRRDAAFSVDHLPILNERYTVETPLAEETAQLVLIEKI-KASLEPVTLLVTGPLTNLARALDSDPDISSNIEEVYI 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 763167304 172 MGGAHFNGGNI-----TPAAEFNLYADPHAAEVVLASGVQLIYLPLDVTHKLLTSDARLKQLAA 230
Cdd:cd02647 154 MGGGVDAPGNVftppsNGTAEFNIFWDPLAAKTVFDSGLKITLVPLDATNTVPLTREFLETDRQ 217
|
|
| nuc_hydro_2 |
cd02652 |
NH_2: A subgroup of nucleoside hydrolases. This group contains eukaryotic and bacterial ... |
25-200 |
3.76e-14 |
|
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: 71.76 E-value: 3.76e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 763167304 25 LIIDTDPGAD--DVVALFLAMASPDElNIRAITTVAGNVRlektSRNARLA-REWAGREDIPVyaGAARPLVRKPiyAAD 101
Cdd:cd02652 1 LILDTDIGGDpdDALALALAHALQKC-DLLAVTITLADAS----ARRAIDAvNRFYGRGDIPI--GADYHGWPED--AKD 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 763167304 102 VHGEEGLTGIQVHEPKAPLAQGNAVQYLVDTLGTAKPHSITIAMLGPQTNLALALIQRPDIAKG-------IKQVVVMGG 174
Cdd:cd02652 72 HAKFLLEGDRLHHDLESAEDALDAVKALRRLLASAEDASVTIVSIGPLTNLAALLDADADPLTGpelvrqkVKRLVVMGG 151
|
170 180
....*....|....*....|....*.
gi 763167304 175 AHFNGGNITPAAEFNLYADPHAAEVV 200
Cdd:cd02652 152 AFYDPDGNVQHREYNFVTDPKAAQRV 177
|
|
| PTZ00313 |
PTZ00313 |
inosine-adenosine-guanosine-nucleoside hydrolase; Provisional |
22-296 |
1.10e-09 |
|
inosine-adenosine-guanosine-nucleoside hydrolase; Provisional
Pssm-ID: 140334 [Multi-domain] Cd Length: 326 Bit Score: 58.72 E-value: 1.10e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 763167304 22 PIDLIIDTDPGADDVVALFLAMASPDELN-IRAITTVAGNVRLEKTSRNARLAREWAGREDIPVY------AGAARPLVR 94
Cdd:PTZ00313 2 PKPVILDHDGNHDDLVALALLLGNPEKVKvIGCICTDADCFVDDAFNVTGKLMCMMHAREATPLFpigkssFKGVNPFPS 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 763167304 95 KPIYAADVHGEEGLTGIQVH----EPKAPLAQGNAVQYLVDTLGTAKPHSITIAMLGPQTNLALAlIQR--PDIAKGIKQ 168
Cdd:PTZ00313 82 EWRWSAKNMDDLPCLNIPEHvaiwEKLKPENEALVGEELLADLVMSSPEKVTICVTGPLSNVAWC-IEKygEEFTKKVEE 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 763167304 169 VVVMGGAHFNGGNI-----TPAAEFNLYADPHAAEVVL-ASGVQLIYLPLDVTHKLLTSDARLKQLAAVNNQASKRVVDI 242
Cdd:PTZ00313 161 CVIMGGAVDVGGNVflpgtDGSAEWNIYWDPPAAKTVLmCPHIRKVLFSLDSTNSVPVTSEVVKKFGAQNKYLLSQFVGS 240
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 763167304 243 LNAYITHDMDLYGMPGGPVHDASVIAYLLKPELFSGRRIHMSIDSREGPSFGQT 296
Cdd:PTZ00313 241 TWAMCTHHELLRPGDGYYAWDVLTAAYVIERNLAELEPVPLEVVVEKAKNEGRT 294
|
|
| |
