|
Name |
Accession |
Description |
Interval |
E-value |
| URH1 |
COG1957 |
Inosine-uridine nucleoside N-ribohydrolase [Nucleotide transport and metabolism]; ... |
38-349 |
8.20e-149 |
|
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: 421.48 E-value: 8.20e-149
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119167454 38 SPRTLIIDTDPGADDVIALLFAMASPkELKIQALTTVAGNVPLEKTARNARLAREWGKRPDIPVYAGAPRPLLRTPIYAA 117
Cdd:COG1957 1 MMRKVIIDTDPGIDDALALLLALASP-EIDLLGITTVAGNVPLEQTTRNALKLLELAGRTDVPVAAGAARPLVRPLVTAE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119167454 118 DVHGSEGISGVEVHEPKQPLAEGNAVDYLIRTLRAAPEKsVTLAMLGPETNLALALTQAPDIVKGVREIVIMGGAHFNGG 197
Cdd:COG1957 80 HVHGEDGLGGVDLPEPTRPPEPEHAVDFIIETLRAAPGE-VTLVALGPLTNLALALRKDPELAERIKRIVIMGGAFFVPG 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119167454 198 NITPAAEFNIFADPHAAEIVLKSGAPITMLPLDVTHKILTSPERIAKLRNLGNQAGKTVADILDAYVQYDIKYYGLKGGP 277
Cdd:COG1957 159 NVTPVAEFNIYVDPEAAKIVFASGIPITMVGLDVTHQALLTPEDLARLAALGTPLGRFLADLLDFYLDFYRERYGLDGCP 238
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 119167454 278 VHDATVVAYLLKPSLFKGKRINVQVDSREGITFGQTVADWYGGLKQPANVEWINEGDAQGFFDLLTERIARL 349
Cdd:COG1957 239 LHDPLAVAYLLDPELFTTRPAPVDVETDGELTRGQTVVDWRGVTGRPPNARVALDVDAERFLDLLLERLARL 310
|
|
| nuc_hydro_IU_UC_XIUA |
cd02651 |
nuc_hydro_IU_UC_XIUA: inosine-uridine preferring, ... |
42-346 |
1.45e-147 |
|
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: 418.10 E-value: 1.45e-147
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119167454 42 LIIDTDPGADDVIALLFAMASPkELKIQALTTVAGNVPLEKTARNARLAREWGKRPDIPVYAGAPRPLLRTPIYAADVHG 121
Cdd:cd02651 2 IIIDCDPGHDDAVAILLALFHP-ELDLLGITTVAGNVPLEKTTRNALKLLTLLGRTDVPVAAGAARPLVRPLITASDIHG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119167454 122 SEGISGVEVHEPKQPLAEGNAVDYLIRTLRAAPEKsVTLAMLGPETNLALALTQAPDIVKGVREIVIMGGAhFNGGNITP 201
Cdd:cd02651 81 ESGLDGADLPPPPRRPEDIHAVDAIIDTLRASPEP-ITLVATGPLTNIALLLRKYPELAERIKEIVLMGGA-LGRGNITP 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119167454 202 AAEFNIFADPHAAEIVLKSGAPITMLPLDVTHKILTSPERIAKLRNLGNQAGKTVADILDAYVqydiKYYGLK---GGPV 278
Cdd:cd02651 159 AAEFNIFVDPEAAKIVFNSGIPITMVPLDVTHKALATPEVIERIRALGNPVGKMLAELLDFFA----ETYGSAfteGPPL 234
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 119167454 279 HDATVVAYLLKPSLFKGKRINVQVDSREGITFGQTVADWYGGLKQPANVEWINEGDAQGFFDLLTERI 346
Cdd:cd02651 235 HDPCAVAYLLDPELFTTKRANVDVETEGELTRGRTVVDLRGVTGRPANAQVAVDVDVEKFWDLLLEAL 302
|
|
| IU_nuc_hydro |
pfam01156 |
Inosine-uridine preferring nucleoside hydrolase; |
42-340 |
4.12e-106 |
|
Inosine-uridine preferring nucleoside hydrolase;
Pssm-ID: 460086 [Multi-domain] Cd Length: 253 Bit Score: 311.06 E-value: 4.12e-106
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119167454 42 LIIDTDPGADDVIALLFAMASPkELKIQALTTVAGNVPLEKTARNARLAREWGKRPDIPVYAGaprpllrtpiyaadvhg 121
Cdd:pfam01156 1 VIIDTDPGIDDALALLLALASP-EIELLGITTVAGNVSLEQTTRNALRLLELGGRDDIPVYAG----------------- 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119167454 122 segisgvevhepkqplaegnavdyliRTLRAAPEksVTLAMLGPETNLALALTQAPDIVKGVREIVIMGGAHFNGGNITP 201
Cdd:pfam01156 63 --------------------------EAIREPGE--VTLVATGPLTNLALALRLDPELAKKIKELVIMGGAFGVRGNVTP 114
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119167454 202 AAEFNIFADPHAAEIVLKSGAPITMLPLDVTHKILTSPERIAKLRNLGNQAGKTVADILDAYVQYDIKYYGLKGGPVHDA 281
Cdd:pfam01156 115 AAEFNIFVDPEAAKIVFTSGLPITMVPLDVTHQALLTPEDLERLAALGTPLGRFLADLLRFYAEFYRERFGIDGPPLHDP 194
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 119167454 282 TVVAYLLKPSLFKGKRINVQVDSREGITFGQTVADWYGGLKQPANVEWINEGDAQGFFD 340
Cdd:pfam01156 195 LAVAVALDPELFTTRRLNVDVETTGGLTRGQTVVDDRGGWGKPPNVRVATDVDVDRFWE 253
|
|
| rihA |
PRK10443 |
ribonucleoside hydrolase 1; Provisional |
39-348 |
2.11e-94 |
|
ribonucleoside hydrolase 1; Provisional
Pssm-ID: 182465 [Multi-domain] Cd Length: 311 Bit Score: 283.48 E-value: 2.11e-94
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119167454 39 PRTLIIDTDPGADDVIALLFAMASPkELKIQALTTVAGNVPLEKTARNARLAREWGKRPDIPVYAGAPRPLLRTPIYAAD 118
Cdd:PRK10443 2 ALPIILDCDPGHDDAIALVLALASP-ELDVKAVTTSAGNQTPEKTLRNALRMLTLLNRTDIPVAGGAVKPLMRELIIADN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119167454 119 VHGSEGISGVEVHEPKQPLAEGNAVDYLIRTLRAAPEKsVTLAMLGPETNLALALTQAPDIVKGVREIVIMGGAhFNGGN 198
Cdd:PRK10443 81 VHGESGLDGPALPEPTFAPQNCTAVELMAKTLRESAEP-VTLVSTGPQTNVALLLASHPELHSKIARIVIMGGA-MGLGN 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119167454 199 ITPAAEFNIFADPHAAEIVLKSGAPITMLPLDVTHKILTSPERIAKLRNLGNQAGKTVADILDAYVQY--DIKyYGLKGG 276
Cdd:PRK10443 159 WTPAAEFNIYVDPEAAEIVFQSGIPIVMAGLDVTHKAQIMDEDIERIRAIGNPVATIVAELLDFFMEYhkDEK-WGFVGA 237
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 119167454 277 PVHDATVVAYLLKPSLFKGKRINVQVDSREGITFGQTVADWYGGLKQPANVEWINEGDAQGFFDLLTERIAR 348
Cdd:PRK10443 238 PLHDPCTIAWLLKPELFTTVERWVGVETQGEYTQGMTVVDYYQLTGNKPNATVLVDVDRQGFVDLLAERLKF 309
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| URH1 |
COG1957 |
Inosine-uridine nucleoside N-ribohydrolase [Nucleotide transport and metabolism]; ... |
38-349 |
8.20e-149 |
|
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: 421.48 E-value: 8.20e-149
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119167454 38 SPRTLIIDTDPGADDVIALLFAMASPkELKIQALTTVAGNVPLEKTARNARLAREWGKRPDIPVYAGAPRPLLRTPIYAA 117
Cdd:COG1957 1 MMRKVIIDTDPGIDDALALLLALASP-EIDLLGITTVAGNVPLEQTTRNALKLLELAGRTDVPVAAGAARPLVRPLVTAE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119167454 118 DVHGSEGISGVEVHEPKQPLAEGNAVDYLIRTLRAAPEKsVTLAMLGPETNLALALTQAPDIVKGVREIVIMGGAHFNGG 197
Cdd:COG1957 80 HVHGEDGLGGVDLPEPTRPPEPEHAVDFIIETLRAAPGE-VTLVALGPLTNLALALRKDPELAERIKRIVIMGGAFFVPG 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119167454 198 NITPAAEFNIFADPHAAEIVLKSGAPITMLPLDVTHKILTSPERIAKLRNLGNQAGKTVADILDAYVQYDIKYYGLKGGP 277
Cdd:COG1957 159 NVTPVAEFNIYVDPEAAKIVFASGIPITMVGLDVTHQALLTPEDLARLAALGTPLGRFLADLLDFYLDFYRERYGLDGCP 238
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 119167454 278 VHDATVVAYLLKPSLFKGKRINVQVDSREGITFGQTVADWYGGLKQPANVEWINEGDAQGFFDLLTERIARL 349
Cdd:COG1957 239 LHDPLAVAYLLDPELFTTRPAPVDVETDGELTRGQTVVDWRGVTGRPPNARVALDVDAERFLDLLLERLARL 310
|
|
| nuc_hydro_IU_UC_XIUA |
cd02651 |
nuc_hydro_IU_UC_XIUA: inosine-uridine preferring, ... |
42-346 |
1.45e-147 |
|
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: 418.10 E-value: 1.45e-147
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119167454 42 LIIDTDPGADDVIALLFAMASPkELKIQALTTVAGNVPLEKTARNARLAREWGKRPDIPVYAGAPRPLLRTPIYAADVHG 121
Cdd:cd02651 2 IIIDCDPGHDDAVAILLALFHP-ELDLLGITTVAGNVPLEKTTRNALKLLTLLGRTDVPVAAGAARPLVRPLITASDIHG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119167454 122 SEGISGVEVHEPKQPLAEGNAVDYLIRTLRAAPEKsVTLAMLGPETNLALALTQAPDIVKGVREIVIMGGAhFNGGNITP 201
Cdd:cd02651 81 ESGLDGADLPPPPRRPEDIHAVDAIIDTLRASPEP-ITLVATGPLTNIALLLRKYPELAERIKEIVLMGGA-LGRGNITP 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119167454 202 AAEFNIFADPHAAEIVLKSGAPITMLPLDVTHKILTSPERIAKLRNLGNQAGKTVADILDAYVqydiKYYGLK---GGPV 278
Cdd:cd02651 159 AAEFNIFVDPEAAKIVFNSGIPITMVPLDVTHKALATPEVIERIRALGNPVGKMLAELLDFFA----ETYGSAfteGPPL 234
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 119167454 279 HDATVVAYLLKPSLFKGKRINVQVDSREGITFGQTVADWYGGLKQPANVEWINEGDAQGFFDLLTERI 346
Cdd:cd02651 235 HDPCAVAYLLDPELFTTKRANVDVETEGELTRGRTVVDLRGVTGRPANAQVAVDVDVEKFWDLLLEAL 302
|
|
| IU_nuc_hydro |
pfam01156 |
Inosine-uridine preferring nucleoside hydrolase; |
42-340 |
4.12e-106 |
|
Inosine-uridine preferring nucleoside hydrolase;
Pssm-ID: 460086 [Multi-domain] Cd Length: 253 Bit Score: 311.06 E-value: 4.12e-106
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119167454 42 LIIDTDPGADDVIALLFAMASPkELKIQALTTVAGNVPLEKTARNARLAREWGKRPDIPVYAGaprpllrtpiyaadvhg 121
Cdd:pfam01156 1 VIIDTDPGIDDALALLLALASP-EIELLGITTVAGNVSLEQTTRNALRLLELGGRDDIPVYAG----------------- 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119167454 122 segisgvevhepkqplaegnavdyliRTLRAAPEksVTLAMLGPETNLALALTQAPDIVKGVREIVIMGGAHFNGGNITP 201
Cdd:pfam01156 63 --------------------------EAIREPGE--VTLVATGPLTNLALALRLDPELAKKIKELVIMGGAFGVRGNVTP 114
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119167454 202 AAEFNIFADPHAAEIVLKSGAPITMLPLDVTHKILTSPERIAKLRNLGNQAGKTVADILDAYVQYDIKYYGLKGGPVHDA 281
Cdd:pfam01156 115 AAEFNIFVDPEAAKIVFTSGLPITMVPLDVTHQALLTPEDLERLAALGTPLGRFLADLLRFYAEFYRERFGIDGPPLHDP 194
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 119167454 282 TVVAYLLKPSLFKGKRINVQVDSREGITFGQTVADWYGGLKQPANVEWINEGDAQGFFD 340
Cdd:pfam01156 195 LAVAVALDPELFTTRRLNVDVETTGGLTRGQTVVDDRGGWGKPPNVRVATDVDVDRFWE 253
|
|
| nuc_hydro_CaPnhB |
cd02650 |
NH_hydro_CaPnhB: A subgroup of nucleoside hydrolases similar to Corynebacterium ammoniagenes ... |
42-329 |
1.75e-96 |
|
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: 288.41 E-value: 1.75e-96
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119167454 42 LIIDTDPGADDVIALLFAMASPkELKIQALTTVAGNVPLEKTARNA-RLAREWGkRPDIPVYAGAPRPLLR-TPIYAADV 119
Cdd:cd02650 2 LILDTDPGIDDAMALAYALAHP-DVDLIGVTTVYGNVTIETATRNAlALLELFG-RPDVPVAEGAAKPLTRpPFRIATFV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119167454 120 HGSEGISGVEVHEPKQPLAEGNAVDYLIRTLRAAPeKSVTLAMLGPETNLALALTQAPDIVKGVREIVIMGGAHFNGGNI 199
Cdd:cd02650 80 HGDNGLGDVELPAPPRQPEDESAADFLIELANEYP-GELTLVAVGPLTNLALALARDPDFAKLVKQVVVMGGAFTVPGNV 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119167454 200 TPAAEFNIFADPHAAEIVLKSGAPITMLPLDVTHKILTSPERIAKLRNLGNQAGKTVADILDAYVQYDIKYYGLKGGPVH 279
Cdd:cd02650 159 TPAAEANIHGDPEAADIVFTAGADLTMVGLDVTTQTLLTREDLDELRDSGGKAGQFLADMLDYYIDFYQESPGLRGCALH 238
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 119167454 280 DATVVAYLLKPSLFKGKRINVQVDSrEGITFGQTVADWYGGLKQPANVEW 329
Cdd:cd02650 239 DPLAVAAAVDPSLFTTREGVVRVET-EGPTRGRTIGDRDGRRFWDSSPNA 287
|
|
| rihA |
PRK10443 |
ribonucleoside hydrolase 1; Provisional |
39-348 |
2.11e-94 |
|
ribonucleoside hydrolase 1; Provisional
Pssm-ID: 182465 [Multi-domain] Cd Length: 311 Bit Score: 283.48 E-value: 2.11e-94
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119167454 39 PRTLIIDTDPGADDVIALLFAMASPkELKIQALTTVAGNVPLEKTARNARLAREWGKRPDIPVYAGAPRPLLRTPIYAAD 118
Cdd:PRK10443 2 ALPIILDCDPGHDDAIALVLALASP-ELDVKAVTTSAGNQTPEKTLRNALRMLTLLNRTDIPVAGGAVKPLMRELIIADN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119167454 119 VHGSEGISGVEVHEPKQPLAEGNAVDYLIRTLRAAPEKsVTLAMLGPETNLALALTQAPDIVKGVREIVIMGGAhFNGGN 198
Cdd:PRK10443 81 VHGESGLDGPALPEPTFAPQNCTAVELMAKTLRESAEP-VTLVSTGPQTNVALLLASHPELHSKIARIVIMGGA-MGLGN 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119167454 199 ITPAAEFNIFADPHAAEIVLKSGAPITMLPLDVTHKILTSPERIAKLRNLGNQAGKTVADILDAYVQY--DIKyYGLKGG 276
Cdd:PRK10443 159 WTPAAEFNIYVDPEAAEIVFQSGIPIVMAGLDVTHKAQIMDEDIERIRAIGNPVATIVAELLDFFMEYhkDEK-WGFVGA 237
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 119167454 277 PVHDATVVAYLLKPSLFKGKRINVQVDSREGITFGQTVADWYGGLKQPANVEWINEGDAQGFFDLLTERIAR 348
Cdd:PRK10443 238 PLHDPCTIAWLLKPELFTTVERWVGVETQGEYTQGMTVVDYYQLTGNKPNATVLVDVDRQGFVDLLAERLKF 309
|
|
| PRK10768 |
PRK10768 |
ribonucleoside hydrolase RihC; Provisional |
42-350 |
1.12e-87 |
|
ribonucleoside hydrolase RihC; Provisional
Pssm-ID: 182713 [Multi-domain] Cd Length: 304 Bit Score: 266.00 E-value: 1.12e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119167454 42 LIIDTDPGADDVIALLFAMASPkELKIQALTTVAGNVPLEKTARNA-RLAREWGKrpDIPVYAGAPRPLLRTPIYAADVH 120
Cdd:PRK10768 5 IILDTDPGIDDAVAIAAALFAP-ELDLKLITTVAGNVSVEKTTRNAlKLLHFFNS--DVPVAQGAAKPLVRPLRDAASVH 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119167454 121 GSEGISGVEVHEPKQPLAEGNAVDYLIRTLRAAPEKsVTLAMLGPETNLALALTQAPDIVKGVREIVIMGGAhFNGGNIT 200
Cdd:PRK10768 82 GESGMEGYDFPEHTRKPLSIPAVEAMRDALMNAPEP-VTLVAIGPLTNIALLLSTYPEVKPYIKRIVLMGGS-AGRGNVT 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119167454 201 PAAEFNIFADPHAAEIVLKSGAPITMLPLDVTHKILTSPERIAKLRNLgNQAGKTVADILDAYVQYDIKyyglKGGPVHD 280
Cdd:PRK10768 160 PNAEFNIAVDPEAAAIVFRSGIPIVMCGLDVTNQALLTPDYLATLPEL-NRTGKMLHALFSHYRSGSMQ----TGLRMHD 234
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119167454 281 ATVVAYLLKPSLFKGKRINVQVDSREGITFGQTVADWYGGLKQPANVEWINEGDAQGFFDLLTERIARLP 350
Cdd:PRK10768 235 VCAIAYLLRPELFTLKPCFVDVETQGEFTAGATVVDIDGRLGKPANAQVALDIDVDGFQKWFAEVLALAN 304
|
|
| rihB |
PRK09955 |
ribosylpyrimidine nucleosidase; |
40-344 |
1.13e-85 |
|
ribosylpyrimidine nucleosidase;
Pssm-ID: 182166 [Multi-domain] Cd Length: 313 Bit Score: 261.42 E-value: 1.13e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119167454 40 RTLIIDTDPGADDVIALLFAMASPKeLKIQALTTVAGNVPLEKTARNArLAREWGKRPDIPVYAGAPRPLLRTPIYAADV 119
Cdd:PRK09955 4 RKIILDCDPGHDDAIAMMMAAKHPA-IDLLGITIVAGNQTLDKTLING-LNVCQKLEINVPVYAGMPQPIMRQQIVADNI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119167454 120 HGSEGISGvEVHEP--KQPlAEGNAVDYLIRTLRAApEKSVTLAMLGPETNLALALTQAPDIVKGVREIVIMGGAhFNGG 197
Cdd:PRK09955 82 HGETGLDG-PVFEPltRQA-ESTHAVKYIIDTLMAS-DGDITLVPVGPLSNIAVAMRMQPAILPKIREIVLMGGA-YGTG 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119167454 198 NITPAAEFNIFADPHAAEIVLKSGAPITMLPLDVTHKILTSPERIAKLRNLGNQAGKTVADILDAYVQYDIKYYGLKGGP 277
Cdd:PRK09955 158 NFTPSAEFNIFADPEAARVVFTSGVPLVMMGLDLTNQTVCTPDVIARMERAGGPAGELFSDIMNFTLKTQFENYGLAGGP 237
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 119167454 278 VHDATVVAYLLKPSLFKGKRINVQVDSREGITFGQTVADWYGGLKQPANVEWINEGDAQGFFDLLTE 344
Cdd:PRK09955 238 VHDATCIGYLINPDGIKTQEMYVEVDVNSGPCYGRTVCDELGVLGKPANTKVGITIDTDWFWGLVEE 304
|
|
| nuc_hydro |
cd00455 |
nuc_hydro: Nucleoside hydrolases. Nucleoside hydrolases cleave the N-glycosidic bond in ... |
42-342 |
1.31e-80 |
|
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: 247.63 E-value: 1.31e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119167454 42 LIIDTDPGADDVIALLFAMASPkELKIQALTTVAGNVPLEKTARNARLAREWGKRPDIPVYAGAPRPLlRTPIYAADVHG 121
Cdd:cd00455 1 VILDTDPGIDDAFALMYALLHP-EIELVGIVATYGNVTLEQATQNAAYLLELLGRLDIPVYAGATRPL-TGEIPAAYPEI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119167454 122 SEGISGVEVHEPKQPLAEGNAVDYLIRTLRAAPeKSVTLAMLGPETNLALALTQAPDIVKGVREIVIMGGAHFNGGNITP 201
Cdd:cd00455 79 HGEGGLGLPIPPIIEADDPEAVQLLIDLIRKYP-DEITIVALGPLTNLAMAFILDPDIKDRVKEIVIMGGAFLVPGNVTP 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119167454 202 AAEFNIFADPHAAEIVLKSGAPITMLPLDVTHKILTSPERIAKLRNLGNQAGKTVADILDAYvQYDIKYYGLKGGPVHDA 281
Cdd:cd00455 158 VAEANFYGDPEAANIVFNSAKNLTIVPLDVTNQAVLTPPMVERIFEQGTSIGLLIKPMIDYY-YKAYQKPGIEGSPIHDP 236
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 119167454 282 TVVAYLLKPSLFKGKRINVQVDSrEGITFGQTVADWYGGlkQPANVEWINEG-DAQGFFDLL 342
Cdd:cd00455 237 LAVAYLLNPSMFDYSKVPVDVDT-DGLTRGQTIADFREN--PGNGVTRVAVNlDYPDFIELI 295
|
|
| nuc_hydro_CeIAG |
cd02649 |
nuc_hydro_CeIAG: Nucleoside hydrolases similar to the inosine-adenosine-guanosine-preferring ... |
40-342 |
7.62e-79 |
|
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: 243.71 E-value: 7.62e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119167454 40 RTLIIDTDPGADDVIALLFAMASPKeLKIQALTTVAGNVPLEKTARNARLAREWGKRPDIPVYAGAPRPLLRTPIYAADV 119
Cdd:cd02649 1 RKLIIDTDCGGDDAWALLMALASPN-VEVLAITCVHGNTNVEQVVKNALRVLEACGRRDIPVYRGASKPLLGPGPTAAYF 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119167454 120 HGSEGISGVEVHEPK--QPLAEGNAVDYLIRTLRAAPeKSVTLAMLGPETNLALALTQAPDIVKGVREIVIMGGAHFNGG 197
Cdd:cd02649 80 HGKDGFGDVGFPEPKdeLELQKEHAVDAIIRLVREYP-GEITLVALGPLTNLALAYRLDPSLPQKIKRLYIMGGNREGVG 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119167454 198 NITPAAEFNIFADPHAAEIVLKS-GAPITMLPLDVT-HKILTSPERIAKLRNLGNQAGKTVADILDAYVQYDIKyYGLKG 275
Cdd:cd02649 159 NTTPAAEFNFHVDPEAAHIVLNSfGCPITIVPWETTlLAFPLDWEFEDKWANRLEKALFAESLNRREYAFASEG-LGGDG 237
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 119167454 276 GPVHDATVVAYLLKPSLF-KGKRINVQVDSREGITFGQTVADWYGGLKQPANVEWINEGDAQGFFDLL 342
Cdd:cd02649 238 WVPCDALAVAAALDPSIItRRLTYAVDVELHGELTRGQMVVDWLGTLKKKPNARVITKIDREKFKELL 305
|
|
| PLN02717 |
PLN02717 |
uridine nucleosidase |
40-316 |
2.43e-77 |
|
uridine nucleosidase
Pssm-ID: 178319 [Multi-domain] Cd Length: 316 Bit Score: 239.89 E-value: 2.43e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119167454 40 RTLIIDTDPGADDVIALLFAMASPkELKIQALTTVAGNVPLEKTARNARLAREWGKRPDIPVYAGAPRPLLR-TPIYAAD 118
Cdd:PLN02717 1 KKLIIDTDPGIDDAMAILMALRSP-EVEVIGLTTIFGNVTTKLATRNALHLLEMAGRPDVPVAEGSHEPLKGgTKPRIAD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119167454 119 -VHGSEGISGVEVHEPKQPLAEGNAVDYLIRTLRAAPEKsVTLAMLGPETNLALALTQAPDIVKGVREIVIMGGAHFNGG 197
Cdd:PLN02717 80 fVHGSDGLGNTNLPPPKGKKIEKSAAEFLVEKVSEYPGE-VTVVALGPLTNLALAIKLDPSFAKKVGQIVVLGGAFFVNG 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119167454 198 NITPAAEFNIFADPHAAEIVLKSGAPITMLPLDVTHKILTSPERIAKLRNLGNQAGKTVADILDAYVQYDIKYYGLKGGP 277
Cdd:PLN02717 159 NVNPAAEANIFGDPEAADIVFTSGADITVVGINVTTQVVLTDADLEELRDSKGKYAQFLCDICKFYRDWHRKSYGIDGIY 238
|
250 260 270
....*....|....*....|....*....|....*....
gi 119167454 278 VHDATVVAYLLKPSLFKGKRINVQVDSrEGITFGQTVAD 316
Cdd:PLN02717 239 LHDPTALLAAVRPSLFTYKEGVVRVET-EGICRGLTLFD 276
|
|
| nuc_hydro_3 |
cd02653 |
NH_3: A subgroup of nucleoside hydrolases. This group contains eukaryotic and bacterial ... |
42-346 |
5.62e-67 |
|
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: 213.78 E-value: 5.62e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119167454 42 LIIDTDPGADDVIALLFAMASPkELKIQALTTVAGNVPLEKTARNARLAREWGKRPDIPVYAGAPRPLLRTPIYAADVHG 121
Cdd:cd02653 2 VIIDCDPGIDDALALLYLLASP-DLDVVGITTTAGNVPVEQVAANALGVLELLGRTDIPVYLGADKPLAGPLTTAQDTHG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119167454 122 SEGISGVEVHEPKQPLAEGNAVDYLIRTLRAAPEksVTLAMLGPETNLALALTQAPDIVKGVREIVIMGGAHFNGGNITP 201
Cdd:cd02653 81 PDGLGYAELPASTRTLSDESAAQAWVDLARAHPD--LIGLATGPLTNLALALREEPELPRLLRRLVIMGGAFNSRGNTSP 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119167454 202 AAEFNIFADPHAAEIVLK----SGAPITMLPLDVTHKILTSPERIAKLRNLGNQAGKTVADILDAYVQYDIKYYGLKGGP 277
Cdd:cd02653 159 VAEWNYWVDPEAAKEVLAafggHPVRPTICGLDVTRAVVLTPNLLERLARAKDSVGAFIEDALRFYFEFHWAYGHGYGAV 238
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 119167454 278 VHDATVVAYLLKPSLFKGKRINVQVDSrEGITFGQTVADWYGGLKQPANVEWINEGDAQGFFDLLTERI 346
Cdd:cd02653 239 IHDPLAAAVALNPNLARGRPAYVDVEC-TGVLTGQTVVDWAGFWGKGANAEILTKVDSQDFMALFIERV 306
|
|
| nuc_hydro_1 |
cd02648 |
NH_1: A subgroup of nucleoside hydrolases. This group contains fungal proteins similar to ... |
39-232 |
1.73e-43 |
|
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: 153.89 E-value: 1.73e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119167454 39 PRTLIIDTDPGADDVIALLFAMASPKELKIQALTTVAGNVPLEKTARNAR-----LARE--WGKRPDIPVYA-------- 103
Cdd:cd02648 1 PHPIIIDTDPGVDDVLAILLALSSPEEVDVALISLTFGNTTLDHALRNVLrlfhvLEREraWRATPGVRYRAfsadaekp 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119167454 104 ----GAPRPLLRTPIYAADVHGSEGISGV---------------EVHEPKQPlAEGNAVDYLIRTLRAAPEKSVTLAMLG 164
Cdd:cd02648 81 ivasGSDQPLEGERLTASYFHGRDGLSGVhwlhpdftpvetwipEIVAPLTP-SDKPAYDVILDILREEPDHTVTIAALG 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 119167454 165 PETNLALALTQAPDIVKGVREIVIMGGAHFNGGNITPAAEFNIFADPHAAEIVLKSGA----------PITMLPLDVT 232
Cdd:cd02648 160 PLTNLAAAARKDPETFAKVGEVVVMGGAIDVPGNTSPVAEFNCFADPYAAAVVIDEPPstapearrklPLQVFPLDIT 237
|
|
| nuc_hydro_CjNH |
cd02654 |
nuc_hydro_CjNH. Nucleoside hydrolases similar to Campylobacter jejuni nucleoside hydrolase. ... |
42-342 |
3.43e-39 |
|
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: 141.15 E-value: 3.43e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119167454 42 LIIDTD----PGADDVIALLFAmASPKELKIQALTTVAGNVPLEKTARNARLAREWGKRPDIPVYAGAPRPLLRT---PI 114
Cdd:cd02654 2 VILDNDiamgRDTDDGLALALL-LWSPEVELLGLSAVSGNCWLSAVTYNVLRMLELAGADAIPVYAGANTPLGRTnraFH 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119167454 115 YAADVHGS---EGISGVE-----VHEPKQPLAEGNAVDYLIRTLRAAPeKSVTLAMLGPETNLALALTQAPDIVKGVREI 186
Cdd:cd02654 81 AWESLYGAylwQGAWSPEysdmyTNASIIRNASIPAALFMIEMVRKHP-HEVSIVAAGPLTNLALALRIDPDFAPLAKEL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119167454 187 VIMGGAHFNGG---NITPAAEFNIFADPHAAEIVLKSGAPITMLPLDVTHKILTSPERIAKLRNLGNQAGKTvadiLDAY 263
Cdd:cd02654 160 VIMGGYLDDIGefvNRHYASDFNLIMDPEAASIVLTAPWKSITIPGNVTNRTCLTPEQIKADDPLRDFIRET----LDLP 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119167454 264 VQYDIKYYGLKGG-PVHDATVVAYLLKPSLFKGKR---INVQVDSREGitfGQTVADWYGGLK---QPANVEWINEGDAQ 336
Cdd:cd02654 236 IDYAKEFVGTGDGlPMWDELASAVALDPELATSSEtfyIDVQTDSDGG---GQLIWPEDLLLAkglRPYHVKVITAVDVA 312
|
....*.
gi 119167454 337 GFFDLL 342
Cdd:cd02654 313 AFLNLI 318
|
|
| nuc_hydro_TvIAG |
cd02647 |
nuc_hydro_ TvIAG: Nucleoside hydrolases similar to the Inosine-adenosine-guanosine-preferring ... |
42-235 |
2.63e-34 |
|
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: 127.92 E-value: 2.63e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119167454 42 LIIDTDPGADDVIALLFaMASPKELKIQALTtVAGNVP--LEKTARNARLAR--EWGKRPDIPVYAGAPRPLLRTPI--- 114
Cdd:cd02647 3 VIFDHDGNVDDLVALLL-LLKNEKVDLKGIG-VSGIDAdcYVEPAVSVTRKLidRLGQRDAIPVGKGGSRAVNPFPRswr 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119167454 115 -YAADV--HGSEGisgVEVHEPKQPLAEGNAVDYLIRTLRAAPEKsVTLAMLGPETNLALALTQAPDIVKGVREIVIMGG 191
Cdd:cd02647 81 rDAAFSvdHLPIL---NERYTVETPLAEETAQLVLIEKIKASLEP-VTLLVTGPLTNLARALDSDPDISSNIEEVYIMGG 156
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 119167454 192 AHFNGGNI-----TPAAEFNIFADPHAAEIVLKSGAPITMLPLDVTHKI 235
Cdd:cd02647 157 GVDAPGNVftppsNGTAEFNIFWDPLAAKTVFDSGLKITLVPLDATNTV 205
|
|
| nuc_hydro_2 |
cd02652 |
NH_2: A subgroup of nucleoside hydrolases. This group contains eukaryotic and bacterial ... |
42-229 |
1.23e-15 |
|
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: 76.38 E-value: 1.23e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119167454 42 LIIDTDPGAD--DVIALLFAMASPKElKIQALTTVAGNVplekTARNARLA--REWGkRPDIPV---YAGAPRPLLRTPI 114
Cdd:cd02652 1 LILDTDIGGDpdDALALALAHALQKC-DLLAVTITLADA----SARRAIDAvnRFYG-RGDIPIgadYHGWPEDAKDHAK 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119167454 115 YAADVhgsegisgvEVHEPKQPLAEG--NAVDYLIRTLRAAPEKSVTLAMLGPETNLALALTQAPDIVKG-------VRE 185
Cdd:cd02652 75 FLLEG---------DRLHHDLESAEDalDAVKALRRLLASAEDASVTIVSIGPLTNLAALLDADADPLTGpelvrqkVKR 145
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 119167454 186 IVIMGGAHFNGGNITPAAEFNIFADPHAAEIVLKSgAPITMLPL 229
Cdd:cd02652 146 LVVMGGAFYDPDGNVQHREYNFVTDPKAAQRVAGR-AQHLGIPV 188
|
|
| PTZ00313 |
PTZ00313 |
inosine-adenosine-guanosine-nucleoside hydrolase; Provisional |
38-218 |
2.64e-08 |
|
inosine-adenosine-guanosine-nucleoside hydrolase; Provisional
Pssm-ID: 140334 [Multi-domain] Cd Length: 326 Bit Score: 54.87 E-value: 2.64e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119167454 38 SPRTLIIDTDPGADDVIALLFAMASPKELK-IQALTTVAGNVPLEKTARNARLAREWGKRPDIPVYagaprPLLRTPIYA 116
Cdd:PTZ00313 1 MPKPVILDHDGNHDDLVALALLLGNPEKVKvIGCICTDADCFVDDAFNVTGKLMCMMHAREATPLF-----PIGKSSFKG 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119167454 117 ADVHGSEG---------------ISGVEVHEPKQPLAEG-NAVDYLIRTLRAAPEKsVTLAMLGPETNLALALTQ-APDI 179
Cdd:PTZ00313 76 VNPFPSEWrwsaknmddlpclniPEHVAIWEKLKPENEAlVGEELLADLVMSSPEK-VTICVTGPLSNVAWCIEKyGEEF 154
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 119167454 180 VKGVREIVIMGGAHFNGGNI-----TPAAEFNIFADPHAAEIVL 218
Cdd:PTZ00313 155 TKKVEECVIMGGAVDVGGNVflpgtDGSAEWNIYWDPPAAKTVL 198
|
|
| |
