|
Name |
Accession |
Description |
Interval |
E-value |
| rihA |
PRK10443 |
ribonucleoside hydrolase 1; Provisional |
1-311 |
0e+00 |
|
ribonucleoside hydrolase 1; Provisional
Pssm-ID: 182465 [Multi-domain] Cd Length: 311 Bit Score: 669.84 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128634 1 MALPILLDCDPGHDDAIAIVLALASPELDVKAITSSAGNQTPEKTLRNVLRMLTLLNRTDIPVAGGAVKPLMRELIIADN 80
Cdd:PRK10443 1 MALPIILDCDPGHDDAIALVLALASPELDVKAVTTSAGNQTPEKTLRNALRMLTLLNRTDIPVAGGAVKPLMRELIIADN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128634 81 VHGESGLDGPALPEPTFAPQNCTAVELMAKTLRESAEPVTIVSTGPQTNVALLLNSHPELHSKIARIVIMGGAMGLGNWT 160
Cdd:PRK10443 81 VHGESGLDGPALPEPTFAPQNCTAVELMAKTLRESAEPVTLVSTGPQTNVALLLASHPELHSKIARIVIMGGAMGLGNWT 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128634 161 PAAEFNIYVDPEAAEIVFQSGIPVVMAGLDVTHKAQIHVEDTERFRAIGNPVSTIVAELLDFFLEYHKDEKWGFVGAPLH 240
Cdd:PRK10443 161 PAAEFNIYVDPEAAEIVFQSGIPIVMAGLDVTHKAQIMDEDIERIRAIGNPVATIVAELLDFFMEYHKDEKWGFVGAPLH 240
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 16128634 241 DPCTIAWLLKPELFTSVERWVGVETQGKYTQGMTVVDYYYLTGNKPNATVMVDVDRQGFVDLLADRLKFYA 311
Cdd:PRK10443 241 DPCTIAWLLKPELFTTVERWVGVETQGEYTQGMTVVDYYQLTGNKPNATVLVDVDRQGFVDLLAERLKFYA 311
|
|
| nuc_hydro_IU_UC_XIUA |
cd02651 |
nuc_hydro_IU_UC_XIUA: inosine-uridine preferring, ... |
4-307 |
3.74e-177 |
|
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: 491.29 E-value: 3.74e-177
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128634 4 PILLDCDPGHDDAIAIVLALASPELDVKAITSSAGNQTPEKTLRNVLRMLTLLNRTDIPVAGGAVKPLMRELIIADNVHG 83
Cdd:cd02651 1 PIIIDCDPGHDDAVAILLALFHPELDLLGITTVAGNVPLEKTTRNALKLLTLLGRTDVPVAAGAARPLVRPLITASDIHG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128634 84 ESGLDGPALPEPTFAPQNCTAVELMAKTLRESAEPVTIVSTGPQTNVALLLNSHPELHSKIARIVIMGGAMGLGNWTPAA 163
Cdd:cd02651 81 ESGLDGADLPPPPRRPEDIHAVDAIIDTLRASPEPITLVATGPLTNIALLLRKYPELAERIKEIVLMGGALGRGNITPAA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128634 164 EFNIYVDPEAAEIVFQSGIPVVMAGLDVTHKAQIHVEDTERFRAIGNPVSTIVAELLDFFLEYHKDEKwgFVGAPLHDPC 243
Cdd:cd02651 161 EFNIFVDPEAAKIVFNSGIPITMVPLDVTHKALATPEVIERIRALGNPVGKMLAELLDFFAETYGSAF--TEGPPLHDPC 238
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 16128634 244 TIAWLLKPELFTSVERWVGVETQGKYTQGMTVVDYYYLTGNKPNATVMVDVDRQGFVDLLADRL 307
Cdd:cd02651 239 AVAYLLDPELFTTKRANVDVETEGELTRGRTVVDLRGVTGRPANAQVAVDVDVEKFWDLLLEAL 302
|
|
| URH1 |
COG1957 |
Inosine-uridine nucleoside N-ribohydrolase [Nucleotide transport and metabolism]; ... |
1-308 |
3.71e-160 |
|
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: 448.83 E-value: 3.71e-160
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128634 1 MALPILLDCDPGHDDAIAIVLALASPELDVKAITSSAGNQTPEKTLRNVLRMLTLLNRTDIPVAGGAVKPLMRELIIADN 80
Cdd:COG1957 1 MMRKVIIDTDPGIDDALALLLALASPEIDLLGITTVAGNVPLEQTTRNALKLLELAGRTDVPVAAGAARPLVRPLVTAEH 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128634 81 VHGESGLDGPALPEPTFAPQNCTAVELMAKTLRESAEPVTIVSTGPQTNVALLLNSHPELHSKIARIVIMGGAM-GLGNW 159
Cdd:COG1957 81 VHGEDGLGGVDLPEPTRPPEPEHAVDFIIETLRAAPGEVTLVALGPLTNLALALRKDPELAERIKRIVIMGGAFfVPGNV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128634 160 TPAAEFNIYVDPEAAEIVFQSGIPVVMAGLDVTHKAQIHVEDTERFRAIGNPVSTIVAELLDFFLEYHKdEKWGFVGAPL 239
Cdd:COG1957 161 TPVAEFNIYVDPEAAKIVFASGIPITMVGLDVTHQALLTPEDLARLAALGTPLGRFLADLLDFYLDFYR-ERYGLDGCPL 239
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 16128634 240 HDPCTIAWLLKPELFTSVERWVGVETQGKYTQGMTVVDYYYLTGNKPNATVMVDVDRQGFVDLLADRLK 308
Cdd:COG1957 240 HDPLAVAYLLDPELFTTRPAPVDVETDGELTRGQTVVDWRGVTGRPPNARVALDVDAERFLDLLLERLA 308
|
|
| IU_nuc_hydro |
pfam01156 |
Inosine-uridine preferring nucleoside hydrolase; |
5-301 |
2.71e-113 |
|
Inosine-uridine preferring nucleoside hydrolase;
Pssm-ID: 460086 [Multi-domain] Cd Length: 253 Bit Score: 328.01 E-value: 2.71e-113
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128634 5 ILLDCDPGHDDAIAIVLALASPELDVKAITSSAGNQTPEKTLRNVLRMLTLLNRTDIPVAGGavkplmreliiadnvhge 84
Cdd:pfam01156 1 VIIDTDPGIDDALALLLALASPEIELLGITTVAGNVSLEQTTRNALRLLELGGRDDIPVYAG------------------ 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128634 85 sgldgpalpeptfapqnctavelmaKTLRESAEpVTIVSTGPQTNVALLLNSHPELHSKIARIVIMGGAMGL-GNWTPAA 163
Cdd:pfam01156 63 -------------------------EAIREPGE-VTLVATGPLTNLALALRLDPELAKKIKELVIMGGAFGVrGNVTPAA 116
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128634 164 EFNIYVDPEAAEIVFQSGIPVVMAGLDVTHKAQIHVEDTERFRAIGNPVSTIVAELLDFFLEYHKdEKWGFVGAPLHDPC 243
Cdd:pfam01156 117 EFNIFVDPEAAKIVFTSGLPITMVPLDVTHQALLTPEDLERLAALGTPLGRFLADLLRFYAEFYR-ERFGIDGPPLHDPL 195
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 16128634 244 TIAWLLKPELFTSVERWVGVETQGKYTQGMTVVDYYYLTGNKPNATVMVDVDRQGFVD 301
Cdd:pfam01156 196 AVAVALDPELFTTRRLNVDVETTGGLTRGQTVVDDRGGWGKPPNVRVATDVDVDRFWE 253
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| rihA |
PRK10443 |
ribonucleoside hydrolase 1; Provisional |
1-311 |
0e+00 |
|
ribonucleoside hydrolase 1; Provisional
Pssm-ID: 182465 [Multi-domain] Cd Length: 311 Bit Score: 669.84 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128634 1 MALPILLDCDPGHDDAIAIVLALASPELDVKAITSSAGNQTPEKTLRNVLRMLTLLNRTDIPVAGGAVKPLMRELIIADN 80
Cdd:PRK10443 1 MALPIILDCDPGHDDAIALVLALASPELDVKAVTTSAGNQTPEKTLRNALRMLTLLNRTDIPVAGGAVKPLMRELIIADN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128634 81 VHGESGLDGPALPEPTFAPQNCTAVELMAKTLRESAEPVTIVSTGPQTNVALLLNSHPELHSKIARIVIMGGAMGLGNWT 160
Cdd:PRK10443 81 VHGESGLDGPALPEPTFAPQNCTAVELMAKTLRESAEPVTLVSTGPQTNVALLLASHPELHSKIARIVIMGGAMGLGNWT 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128634 161 PAAEFNIYVDPEAAEIVFQSGIPVVMAGLDVTHKAQIHVEDTERFRAIGNPVSTIVAELLDFFLEYHKDEKWGFVGAPLH 240
Cdd:PRK10443 161 PAAEFNIYVDPEAAEIVFQSGIPIVMAGLDVTHKAQIMDEDIERIRAIGNPVATIVAELLDFFMEYHKDEKWGFVGAPLH 240
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 16128634 241 DPCTIAWLLKPELFTSVERWVGVETQGKYTQGMTVVDYYYLTGNKPNATVMVDVDRQGFVDLLADRLKFYA 311
Cdd:PRK10443 241 DPCTIAWLLKPELFTTVERWVGVETQGEYTQGMTVVDYYQLTGNKPNATVLVDVDRQGFVDLLAERLKFYA 311
|
|
| nuc_hydro_IU_UC_XIUA |
cd02651 |
nuc_hydro_IU_UC_XIUA: inosine-uridine preferring, ... |
4-307 |
3.74e-177 |
|
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: 491.29 E-value: 3.74e-177
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128634 4 PILLDCDPGHDDAIAIVLALASPELDVKAITSSAGNQTPEKTLRNVLRMLTLLNRTDIPVAGGAVKPLMRELIIADNVHG 83
Cdd:cd02651 1 PIIIDCDPGHDDAVAILLALFHPELDLLGITTVAGNVPLEKTTRNALKLLTLLGRTDVPVAAGAARPLVRPLITASDIHG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128634 84 ESGLDGPALPEPTFAPQNCTAVELMAKTLRESAEPVTIVSTGPQTNVALLLNSHPELHSKIARIVIMGGAMGLGNWTPAA 163
Cdd:cd02651 81 ESGLDGADLPPPPRRPEDIHAVDAIIDTLRASPEPITLVATGPLTNIALLLRKYPELAERIKEIVLMGGALGRGNITPAA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128634 164 EFNIYVDPEAAEIVFQSGIPVVMAGLDVTHKAQIHVEDTERFRAIGNPVSTIVAELLDFFLEYHKDEKwgFVGAPLHDPC 243
Cdd:cd02651 161 EFNIFVDPEAAKIVFNSGIPITMVPLDVTHKALATPEVIERIRALGNPVGKMLAELLDFFAETYGSAF--TEGPPLHDPC 238
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 16128634 244 TIAWLLKPELFTSVERWVGVETQGKYTQGMTVVDYYYLTGNKPNATVMVDVDRQGFVDLLADRL 307
Cdd:cd02651 239 AVAYLLDPELFTTKRANVDVETEGELTRGRTVVDLRGVTGRPANAQVAVDVDVEKFWDLLLEAL 302
|
|
| URH1 |
COG1957 |
Inosine-uridine nucleoside N-ribohydrolase [Nucleotide transport and metabolism]; ... |
1-308 |
3.71e-160 |
|
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: 448.83 E-value: 3.71e-160
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128634 1 MALPILLDCDPGHDDAIAIVLALASPELDVKAITSSAGNQTPEKTLRNVLRMLTLLNRTDIPVAGGAVKPLMRELIIADN 80
Cdd:COG1957 1 MMRKVIIDTDPGIDDALALLLALASPEIDLLGITTVAGNVPLEQTTRNALKLLELAGRTDVPVAAGAARPLVRPLVTAEH 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128634 81 VHGESGLDGPALPEPTFAPQNCTAVELMAKTLRESAEPVTIVSTGPQTNVALLLNSHPELHSKIARIVIMGGAM-GLGNW 159
Cdd:COG1957 81 VHGEDGLGGVDLPEPTRPPEPEHAVDFIIETLRAAPGEVTLVALGPLTNLALALRKDPELAERIKRIVIMGGAFfVPGNV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128634 160 TPAAEFNIYVDPEAAEIVFQSGIPVVMAGLDVTHKAQIHVEDTERFRAIGNPVSTIVAELLDFFLEYHKdEKWGFVGAPL 239
Cdd:COG1957 161 TPVAEFNIYVDPEAAKIVFASGIPITMVGLDVTHQALLTPEDLARLAALGTPLGRFLADLLDFYLDFYR-ERYGLDGCPL 239
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 16128634 240 HDPCTIAWLLKPELFTSVERWVGVETQGKYTQGMTVVDYYYLTGNKPNATVMVDVDRQGFVDLLADRLK 308
Cdd:COG1957 240 HDPLAVAYLLDPELFTTRPAPVDVETDGELTRGQTVVDWRGVTGRPPNARVALDVDAERFLDLLLERLA 308
|
|
| PRK10768 |
PRK10768 |
ribonucleoside hydrolase RihC; Provisional |
1-308 |
1.12e-125 |
|
ribonucleoside hydrolase RihC; Provisional
Pssm-ID: 182713 [Multi-domain] Cd Length: 304 Bit Score: 361.15 E-value: 1.12e-125
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128634 1 MALPILLDCDPGHDDAIAIVLALASPELDVKAITSSAGNQTPEKTLRNVLRMLTLLNrTDIPVAGGAVKPLMRELIIADN 80
Cdd:PRK10768 1 MRLPIILDTDPGIDDAVAIAAALFAPELDLKLITTVAGNVSVEKTTRNALKLLHFFN-SDVPVAQGAAKPLVRPLRDAAS 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128634 81 VHGESGLDGPALPEPTFAPQNCTAVELMAKTLRESAEPVTIVSTGPQTNVALLLNSHPELHSKIARIVIMGGAMGLGNWT 160
Cdd:PRK10768 80 VHGESGMEGYDFPEHTRKPLSIPAVEAMRDALMNAPEPVTLVAIGPLTNIALLLSTYPEVKPYIKRIVLMGGSAGRGNVT 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128634 161 PAAEFNIYVDPEAAEIVFQSGIPVVMAGLDVTHKAQIHVEDTERFRAIGNpvstiVAELL-DFFLEYHKDEKWGfvGAPL 239
Cdd:PRK10768 160 PNAEFNIAVDPEAAAIVFRSGIPIVMCGLDVTNQALLTPDYLATLPELNR-----TGKMLhALFSHYRSGSMQT--GLRM 232
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 16128634 240 HDPCTIAWLLKPELFTSVERWVGVETQGKYTQGMTVVDYYYLTGNKPNATVMVDVDRQGFVDLLADRLK 308
Cdd:PRK10768 233 HDVCAIAYLLRPELFTLKPCFVDVETQGEFTAGATVVDIDGRLGKPANAQVALDIDVDGFQKWFAEVLA 301
|
|
| IU_nuc_hydro |
pfam01156 |
Inosine-uridine preferring nucleoside hydrolase; |
5-301 |
2.71e-113 |
|
Inosine-uridine preferring nucleoside hydrolase;
Pssm-ID: 460086 [Multi-domain] Cd Length: 253 Bit Score: 328.01 E-value: 2.71e-113
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128634 5 ILLDCDPGHDDAIAIVLALASPELDVKAITSSAGNQTPEKTLRNVLRMLTLLNRTDIPVAGGavkplmreliiadnvhge 84
Cdd:pfam01156 1 VIIDTDPGIDDALALLLALASPEIELLGITTVAGNVSLEQTTRNALRLLELGGRDDIPVYAG------------------ 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128634 85 sgldgpalpeptfapqnctavelmaKTLRESAEpVTIVSTGPQTNVALLLNSHPELHSKIARIVIMGGAMGL-GNWTPAA 163
Cdd:pfam01156 63 -------------------------EAIREPGE-VTLVATGPLTNLALALRLDPELAKKIKELVIMGGAFGVrGNVTPAA 116
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128634 164 EFNIYVDPEAAEIVFQSGIPVVMAGLDVTHKAQIHVEDTERFRAIGNPVSTIVAELLDFFLEYHKdEKWGFVGAPLHDPC 243
Cdd:pfam01156 117 EFNIFVDPEAAKIVFTSGLPITMVPLDVTHQALLTPEDLERLAALGTPLGRFLADLLRFYAEFYR-ERFGIDGPPLHDPL 195
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 16128634 244 TIAWLLKPELFTSVERWVGVETQGKYTQGMTVVDYYYLTGNKPNATVMVDVDRQGFVD 301
Cdd:pfam01156 196 AVAVALDPELFTTRRLNVDVETTGGLTRGQTVVDDRGGWGKPPNVRVATDVDVDRFWE 253
|
|
| rihB |
PRK09955 |
ribosylpyrimidine nucleosidase; |
5-310 |
2.87e-93 |
|
ribosylpyrimidine nucleosidase;
Pssm-ID: 182166 [Multi-domain] Cd Length: 313 Bit Score: 279.14 E-value: 2.87e-93
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128634 5 ILLDCDPGHDDAIAIVLALASPELDVKAITSSAGNQTPEKTLRNVLRMLTLLNrTDIPVAGGAVKPLMRELIIADNVHGE 84
Cdd:PRK09955 6 IILDCDPGHDDAIAMMMAAKHPAIDLLGITIVAGNQTLDKTLINGLNVCQKLE-INVPVYAGMPQPIMRQQIVADNIHGE 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128634 85 SGLDGPALPEPTFAPQNCTAVELMAKTLRESAEPVTIVSTGPQTNVALLLNSHPELHSKIARIVIMGGAMGLGNWTPAAE 164
Cdd:PRK09955 85 TGLDGPVFEPLTRQAESTHAVKYIIDTLMASDGDITLVPVGPLSNIAVAMRMQPAILPKIREIVLMGGAYGTGNFTPSAE 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128634 165 FNIYVDPEAAEIVFQSGIPVVMAGLDVTHKAQIHVEDTERFRAIGNPVSTIVAELLDFFLEYhKDEKWGFVGAPLHDPCT 244
Cdd:PRK09955 165 FNIFADPEAARVVFTSGVPLVMMGLDLTNQTVCTPDVIARMERAGGPAGELFSDIMNFTLKT-QFENYGLAGGPVHDATC 243
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 16128634 245 IAWLLKPELFTSVERWVGVETQGKYTQGMTVVDYYYLTGNKPNATVMVDVDRQGFVDLLADRLKFY 310
Cdd:PRK09955 244 IGYLINPDGIKTQEMYVEVDVNSGPCYGRTVCDELGVLGKPANTKVGITIDTDWFWGLVEECVRGY 309
|
|
| nuc_hydro |
cd00455 |
nuc_hydro: Nucleoside hydrolases. Nucleoside hydrolases cleave the N-glycosidic bond in ... |
5-303 |
5.32e-89 |
|
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: 267.66 E-value: 5.32e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128634 5 ILLDCDPGHDDAIAIVLALASPELDVKAITSSAGNQTPEKTLRNVLRMLTLLNRTDIPVAGGAVKPLMRELIIADNVHGE 84
Cdd:cd00455 1 VILDTDPGIDDAFALMYALLHPEIELVGIVATYGNVTLEQATQNAAYLLELLGRLDIPVYAGATRPLTGEIPAAYPEIHG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128634 85 SGLDGPALPEPTFAPqNCTAVELMAKTLRESAEPVTIVSTGPQTNVALLLNSHPELHSKIARIVIMGGAMG-LGNWTPAA 163
Cdd:cd00455 81 EGGLGLPIPPIIEAD-DPEAVQLLIDLIRKYPDEITIVALGPLTNLAMAFILDPDIKDRVKEIVIMGGAFLvPGNVTPVA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128634 164 EFNIYVDPEAAEIVFQSGIPVVMAGLDVTHKAQIHVEDTERFRAIGNPVSTIVAELLDFFLEYHKdeKWGFVGAPLHDPC 243
Cdd:cd00455 160 EANFYGDPEAANIVFNSAKNLTIVPLDVTNQAVLTPPMVERIFEQGTSIGLLIKPMIDYYYKAYQ--KPGIEGSPIHDPL 237
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128634 244 TIAWLLKPELFTSVERWVGVETQGkYTQGMTVVDYYYLTGNkPNATVMVDVDRQGFVDLL 303
Cdd:cd00455 238 AVAYLLNPSMFDYSKVPVDVDTDG-LTRGQTIADFRENPGN-GVTRVAVNLDYPDFIELI 295
|
|
| nuc_hydro_CaPnhB |
cd02650 |
NH_hydro_CaPnhB: A subgroup of nucleoside hydrolases similar to Corynebacterium ammoniagenes ... |
5-303 |
1.63e-87 |
|
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: 264.14 E-value: 1.63e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128634 5 ILLDCDPGHDDAIAIVLALASPELDVKAITSSAGNQTPEKTLRNVLRMLTLLNRTDIPVAGGAVKPLMRELI-IADNVHG 83
Cdd:cd02650 2 LILDTDPGIDDAMALAYALAHPDVDLIGVTTVYGNVTIETATRNALALLELFGRPDVPVAEGAAKPLTRPPFrIATFVHG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128634 84 ESGLDGPALPEPTFAPQNCTAVELMAKTLRESAEPVTIVSTGPQTNVALLLNSHPELHSKIARIVIMGGAMG-LGNWTPA 162
Cdd:cd02650 82 DNGLGDVELPAPPRQPEDESAADFLIELANEYPGELTLVAVGPLTNLALALARDPDFAKLVKQVVVMGGAFTvPGNVTPA 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128634 163 AEFNIYVDPEAAEIVFQSGIPVVMAGLDVTHKAQIHVEDTERFRAIGNPVSTIVAELLDFFLEYHKdEKWGFVGAPLHDP 242
Cdd:cd02650 162 AEANIHGDPEAADIVFTAGADLTMVGLDVTTQTLLTREDLDELRDSGGKAGQFLADMLDYYIDFYQ-ESPGLRGCALHDP 240
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 16128634 243 CTIAWLLKPELFTSVERWVGVETQGKyTQGMTVVDYYYLT--GNKPNATVMVDVDRQG-FVDLL 303
Cdd:cd02650 241 LAVAAAVDPSLFTTREGVVRVETEGP-TRGRTIGDRDGRRfwDSSPNATVAVDVDVDErFLKRL 303
|
|
| PLN02717 |
PLN02717 |
uridine nucleosidase |
5-307 |
7.01e-78 |
|
uridine nucleosidase
Pssm-ID: 178319 [Multi-domain] Cd Length: 316 Bit Score: 239.89 E-value: 7.01e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128634 5 ILLDCDPGHDDAIAIVLALASPELDVKAITSSAGNQTPEKTLRNVLRMLTLLNRTDIPVAGGAVKPLMRELI--IADNVH 82
Cdd:PLN02717 3 LIIDTDPGIDDAMAILMALRSPEVEVIGLTTIFGNVTTKLATRNALHLLEMAGRPDVPVAEGSHEPLKGGTKprIADFVH 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128634 83 GESGLDGPALPEPTFAPQNCTAVELMAKTLRESAEPVTIVSTGPQTNVALLLNSHPELHSKIARIVIMGGAM-GLGNWTP 161
Cdd:PLN02717 83 GSDGLGNTNLPPPKGKKIEKSAAEFLVEKVSEYPGEVTVVALGPLTNLALAIKLDPSFAKKVGQIVVLGGAFfVNGNVNP 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128634 162 AAEFNIYVDPEAAEIVFQSGIPVVMAGLDVTHKAQIHVEDTERFRAIGNPVSTIVAELLDFFLEYHKDeKWGFVGAPLHD 241
Cdd:PLN02717 163 AAEANIFGDPEAADIVFTSGADITVVGINVTTQVVLTDADLEELRDSKGKYAQFLCDICKFYRDWHRK-SYGIDGIYLHD 241
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 16128634 242 PCTIAWLLKPELFTSVERWVGVETQGkYTQGMTVVD-----YYYLTG--NKPNATVMVDVDRQGFVDLLADRL 307
Cdd:PLN02717 242 PTALLAAVRPSLFTYKEGVVRVETEG-ICRGLTLFDnglkrWNGENAwtGRPPVKVAVTVDAPAVVELVKERL 313
|
|
| nuc_hydro_CeIAG |
cd02649 |
nuc_hydro_CeIAG: Nucleoside hydrolases similar to the inosine-adenosine-guanosine-preferring ... |
5-303 |
3.68e-76 |
|
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: 235.23 E-value: 3.68e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128634 5 ILLDCDPGHDDAIAIVLALASPELDVKAITSSAGNQTPEKTLRNVLRMLTLLNRTDIPVAGGAVKPLMRELIIADNVHGE 84
Cdd:cd02649 3 LIIDTDCGGDDAWALLMALASPNVEVLAITCVHGNTNVEQVVKNALRVLEACGRRDIPVYRGASKPLLGPGPTAAYFHGK 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128634 85 SGLDGPALPEP--TFAPQNCTAVELMAKTLRESAEPVTIVSTGPQTNVALLLNSHPELHSKIARIVIMGGAM-GLGNWTP 161
Cdd:cd02649 83 DGFGDVGFPEPkdELELQKEHAVDAIIRLVREYPGEITLVALGPLTNLALAYRLDPSLPQKIKRLYIMGGNReGVGNTTP 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128634 162 AAEFNIYVDPEAAEIVFQS-GIPVVMAGLDVT---HKAQIHVEDTERFRAIGNPVSTIVAELLDFFLEyhkdEKWGFVGA 237
Cdd:cd02649 163 AAEFNFHVDPEAAHIVLNSfGCPITIVPWETTllaFPLDWEFEDKWANRLEKALFAESLNRREYAFAS----EGLGGDGW 238
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 16128634 238 PLHDPCTIAWLLKPELFTSVERW-VGVETQGKYTQGMTVVDYYYLTGNKPNATVMVDVDRQGFVDLL 303
Cdd:cd02649 239 VPCDALAVAAALDPSIITRRLTYaVDVELHGELTRGQMVVDWLGTLKKKPNARVITKIDREKFKELL 305
|
|
| nuc_hydro_3 |
cd02653 |
NH_3: A subgroup of nucleoside hydrolases. This group contains eukaryotic and bacterial ... |
4-307 |
5.35e-74 |
|
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: 230.34 E-value: 5.35e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128634 4 PILLDCDPGHDDAIAIVLALASPELDVKAITSSAGNQTPEKTLRNVLRMLTLLNRTDIPVAGGAVKPLMRELIIADNVHG 83
Cdd:cd02653 1 KVIIDCDPGIDDALALLYLLASPDLDVVGITTTAGNVPVEQVAANALGVLELLGRTDIPVYLGADKPLAGPLTTAQDTHG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128634 84 ESGLDGPALPEPTFAPQNCTAVELMAKTLRESAEpVTIVSTGPQTNVALLLNSHPELHSKIARIVIMGGAMGL-GNWTPA 162
Cdd:cd02653 81 PDGLGYAELPASTRTLSDESAAQAWVDLARAHPD-LIGLATGPLTNLALALREEPELPRLLRRLVIMGGAFNSrGNTSPV 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128634 163 AEFNIYVDPEAAEIVFQ----SGIPVVMAGLDVTHKAQIHVEDTERFRAIGNPVSTIVAELLDFFLEYHKDEKWGFvGAP 238
Cdd:cd02653 160 AEWNYWVDPEAAKEVLAafggHPVRPTICGLDVTRAVVLTPNLLERLARAKDSVGAFIEDALRFYFEFHWAYGHGY-GAV 238
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 16128634 239 LHDPCTIAWLLKPELFTSVERWVGVETQGKYTqGMTVVDYYYLTGNKPNATVMVDVDRQGFVDLLADRL 307
Cdd:cd02653 239 IHDPLAAAVALNPNLARGRPAYVDVECTGVLT-GQTVVDWAGFWGKGANAEILTKVDSQDFMALFIERV 306
|
|
| nuc_hydro_1 |
cd02648 |
NH_1: A subgroup of nucleoside hydrolases. This group contains fungal proteins similar to ... |
4-277 |
1.55e-40 |
|
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: 145.03 E-value: 1.55e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128634 4 PILLDCDPGHDDAIAIVLALASP-ELDVKAITSSAGNQTPEKTLRNVLRMLTLLNR-------------------TDIPV 63
Cdd:cd02648 3 PIIIDTDPGVDDVLAILLALSSPeEVDVALISLTFGNTTLDHALRNVLRLFHVLERerawratpgvryrafsadaEKPIV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128634 64 AGGAVKPLMRELIIADNVHGESGLDG--PALPEPT------------FAPQNCTAVELMAKTLRESA-EPVTIVSTGPQT 128
Cdd:cd02648 83 ASGSDQPLEGERLTASYFHGRDGLSGvhWLHPDFTpvetwipeivapLTPSDKPAYDVILDILREEPdHTVTIAALGPLT 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128634 129 NVALLLNSHPELHSKIARIVIMGGAMGL-GNWTPAAEFNIYVDPEAAEIVFQSG----------IPVVMAGLDVTHKAQI 197
Cdd:cd02648 163 NLAAAARKDPETFAKVGEVVVMGGAIDVpGNTSPVAEFNCFADPYAAAVVIDEPpstapearrkLPLQVFPLDITTGHTL 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128634 198 HVED--TERFRAI-----GNPVSTIVAELLDFFLEYHKDEKWGFVGAP-------LHDPCTIAWLL----KPELFTSVER 259
Cdd:cd02648 243 PYSSlfATYVTPRdaperGSPLARWLEHVFISTFLTHPRAFTPEEFLPdrselfeMHDPLAVWYAIfadmPATGSIDGNG 322
|
330 340
....*....|....*....|....
gi 16128634 260 W------VGVETQGKYTQGMTVVD 277
Cdd:cd02648 323 WkhtprdFRVETSGQWTRGMCVVD 346
|
|
| nuc_hydro_TvIAG |
cd02647 |
nuc_hydro_ TvIAG: Nucleoside hydrolases similar to the Inosine-adenosine-guanosine-preferring ... |
4-307 |
5.33e-39 |
|
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: 139.48 E-value: 5.33e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128634 4 PILLDCDPGHDDAIAIVLALASPELDVKAITSSA--GNQTPEKTLRNVLRMLTLLNRTD-IPVAGG---AVKPLMRE-LI 76
Cdd:cd02647 2 NVIFDHDGNVDDLVALLLLLKNEKVDLKGIGVSGidADCYVEPAVSVTRKLIDRLGQRDaIPVGKGgsrAVNPFPRSwRR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128634 77 IADNvhgeSGLDGPAL---PEPTFAPQNCTAVELMAKTLRESAEPVTIVSTGPQTNVALLLNSHPELHSKIARIVIMGGA 153
Cdd:cd02647 82 DAAF----SVDHLPILnerYTVETPLAEETAQLVLIEKIKASLEPVTLLVTGPLTNLARALDSDPDISSNIEEVYIMGGG 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128634 154 MGL-GNW-----TPAAEFNIYVDPEAAEIVFQSGIPVVMAGLDVTHKAQI----HVEDTERFRAIGNPVSTIVAELLDFF 223
Cdd:cd02647 158 VDApGNVftppsNGTAEFNIFWDPLAAKTVFDSGLKITLVPLDATNTVPLtrefLETDRQRFAAQRLPASDLAGQGYALV 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128634 224 LEYHKDEKWgfvgaPLHDPCTIAWLLKPELFTSVERWVG-VETQGKyTQGMTVVDyyyltGNKPNATVMVDVDRQGFVDL 302
Cdd:cd02647 238 KPLEFNSTY-----YMWDVLTTLVLGAKEVDNTKESLILeVDTDGL-SAGQTVTS-----PNGRPLTLVTSNNSYGSNRF 306
|
....*
gi 16128634 303 LADRL 307
Cdd:cd02647 307 FDDYL 311
|
|
| nuc_hydro_CjNH |
cd02654 |
nuc_hydro_CjNH. Nucleoside hydrolases similar to Campylobacter jejuni nucleoside hydrolase. ... |
5-303 |
1.38e-32 |
|
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: 122.66 E-value: 1.38e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128634 5 ILLDCD----PGHDDAIAIVLALASPELDVKAITSSAGNQTPEKTLRNVLRMLTLLNRTDIPVAGGAVKPLMRE---LII 77
Cdd:cd02654 2 VILDNDiamgRDTDDGLALALLLWSPEVELLGLSAVSGNCWLSAVTYNVLRMLELAGADAIPVYAGANTPLGRTnraFHA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128634 78 ADNVHGESGLDGPALPEPTFAPQNCTAVE--------LMAKTLRESAEPVTIVSTGPQTNVALLLNSHPELHSKIARIVI 149
Cdd:cd02654 82 WESLYGAYLWQGAWSPEYSDMYTNASIIRnasipaalFMIEMVRKHPHEVSIVAAGPLTNLALALRIDPDFAPLAKELVI 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128634 150 MGGAMGLG----NWTPAAEFNIYVDPEAAEIVFQSGIPVVMAGLDVThkAQIHVedTERFRAIGNPVSTIVAELLDFFLE 225
Cdd:cd02654 162 MGGYLDDIgefvNRHYASDFNLIMDPEAASIVLTAPWKSITIPGNVT--NRTCL--TPEQIKADDPLRDFIRETLDLPID 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128634 226 YHKDEKWGFVGAPLHDPCTIAWLLKPELFTSVE-RWVGVET-QGKYTQGMTVVDYYYLTGNKP-NATVMVDVDRQGFVDL 302
Cdd:cd02654 238 YAKEFVGTGDGLPMWDELASAVALDPELATSSEtFYIDVQTdSDGGGQLIWPEDLLLAKGLRPyHVKVITAVDVAAFLNL 317
|
.
gi 16128634 303 L 303
Cdd:cd02654 318 I 318
|
|
| nuc_hydro_2 |
cd02652 |
NH_2: A subgroup of nucleoside hydrolases. This group contains eukaryotic and bacterial ... |
5-262 |
3.64e-17 |
|
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: 79.85 E-value: 3.64e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128634 5 ILLDCDPGHD--DAIAIVLALASPELDVKAITSSAGNqtpEKTLRNVLRMLTLLNRTDIPVagGAVKPLMRELiiaDNVH 82
Cdd:cd02652 1 LILDTDIGGDpdDALALALAHALQKCDLLAVTITLAD---ASARRAIDAVNRFYGRGDIPI--GADYHGWPED---AKDH 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128634 83 GESGLDGPALPEPTFAPQNC-TAVELMAKTLRESAE-PVTIVSTGPQTNVALLLNS------HPEL-HSKIARIVIMGGA 153
Cdd:cd02652 73 AKFLLEGDRLHHDLESAEDAlDAVKALRRLLASAEDaSVTIVSIGPLTNLAALLDAdadpltGPELvRQKVKRLVVMGGA 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128634 154 MG--LGNwTPAAEFNIYVDPEAAEIVF----QSGIPVVMagldVTHkaqihvedterFRAIGNPVSTIVAELLDFFLEYH 227
Cdd:cd02652 153 FYdpDGN-VQHREYNFVTDPKAAQRVAgraqHLGIPVRI----VWS-----------GYELGEAVSYPHVLVIAHPFNTP 216
|
250 260 270
....*....|....*....|....*....|....*....
gi 16128634 228 -KDEKWGFVGA-PLHDPCTIAWLLKP--ELFTSVERWVG 262
Cdd:cd02652 217 vFAAYWPRSHRrPLWDPLTLLAAVRGggMLFDLREVQLG 255
|
|
| PTZ00313 |
PTZ00313 |
inosine-adenosine-guanosine-nucleoside hydrolase; Provisional |
1-207 |
1.10e-12 |
|
inosine-adenosine-guanosine-nucleoside hydrolase; Provisional
Pssm-ID: 140334 [Multi-domain] Cd Length: 326 Bit Score: 67.58 E-value: 1.10e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128634 1 MALPILLDCDPGHDDAIAIVLALASPE---------LDVKAITSSAGNQTPektlrnvlRMLTLLNRTD----IPVAGG- 66
Cdd:PTZ00313 1 MPKPVILDHDGNHDDLVALALLLGNPEkvkvigcicTDADCFVDDAFNVTG--------KLMCMMHAREatplFPIGKSs 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128634 67 --AVKPLMREL-IIADNVHgesglDGPAL--PEPT-----FAPQNCTAV--ELMAKTLRESAEPVTIVSTGPQTNVALLL 134
Cdd:PTZ00313 73 fkGVNPFPSEWrWSAKNMD-----DLPCLniPEHVaiwekLKPENEALVgeELLADLVMSSPEKVTICVTGPLSNVAWCI 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128634 135 NSHPE-LHSKIARIVIMGGAMGLGN--WTP----AAEFNIYVDPEAAEIVFQ-SGIPVVMAGLDVTHKAQIHVEDTERFR 206
Cdd:PTZ00313 148 EKYGEeFTKKVEECVIMGGAVDVGGnvFLPgtdgSAEWNIYWDPPAAKTVLMcPHIRKVLFSLDSTNSVPVTSEVVKKFG 227
|
.
gi 16128634 207 A 207
Cdd:PTZ00313 228 A 228
|
|
| |
