|
Name |
Accession |
Description |
Interval |
E-value |
| nuc_hydro |
cd00455 |
nuc_hydro: Nucleoside hydrolases. Nucleoside hydrolases cleave the N-glycosidic bond in ... |
5-307 |
2.82e-114 |
|
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: 331.99 E-value: 2.82e-114
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926918551 5 VLLFTDLGIDDAFAILYTFFREDIQLVGIVADYGNVSREKAIWNINYLKYIAGRQEIPVFLGASIPLTGIAVEAFPEIHG 84
Cdd:cd00455 1 VILDTDPGIDDAFALMYALLHPEIELVGIVATYGNVTLEQATQNAAYLLELLGRLDIPVYAGATRPLTGEIPAAYPEIHG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926918551 85 EAGLGPIIPPQINL-PVYPIHDIYQVIDLHSDNLTVINLGRLSSLATAFVLNlPKMRE-VKDYICMGGAFFYPGNVTAVA 162
Cdd:cd00455 81 EGGLGLPIPPIIEAdDPEAVQLLIDLIRKYPDEITIVALGPLTNLAMAFILD-PDIKDrVKEIVIMGGAFLVPGNVTPVA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926918551 163 EANFFSDPYAANLIVKHAKNLTIIPLNVTQSAIVTPEMVQQIDAFHqhtkDPAGLLIKPMLDYYYNFYSKsnPGIQGSPM 242
Cdd:cd00455 160 EANFYGDPEAANIVFNSAKNLTIVPLDVTNQAVLTPPMVERIFEQG----TSIGLLIKPMIDYYYKAYQK--PGIEGSPI 233
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1926918551 243 HDFVTIWYLLNRDAVHLSKVPIKIIPDqGEGFGQSIADFRFttNSSYSIHNVAFQFNYERFKQDI 307
Cdd:cd00455 234 HDPLAVAYLLNPSMFDYSKVPVDVDTD-GLTRGQTIADFRE--NPGNGVTRVAVNLDYPDFIELI 295
|
|
| URH1 |
COG1957 |
Inosine-uridine nucleoside N-ribohydrolase [Nucleotide transport and metabolism]; ... |
1-313 |
1.47e-84 |
|
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: 257.00 E-value: 1.47e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926918551 1 MQKKVLLFTDLGIDDAFAILYTFFREDIQLVGIVADYGNVSREKAIWNINYLKYIAGRQEIPVFLGASIPLTGIAVEAfP 80
Cdd:COG1957 1 MMRKVIIDTDPGIDDALALLLALASPEIDLLGITTVAGNVPLEQTTRNALKLLELAGRTDVPVAAGAARPLVRPLVTA-E 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926918551 81 EIHGEAGLGPIIPPQINLPVYPIHDIYQVIDL---HSDNLTVINLGRLSSLATAFVLNlPKMRE-VKDYICMGGAFFYPG 156
Cdd:COG1957 80 HVHGEDGLGGVDLPEPTRPPEPEHAVDFIIETlraAPGEVTLVALGPLTNLALALRKD-PELAErIKRIVIMGGAFFVPG 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926918551 157 NVTAVAEANFFSDPYAANLIVKHAKNLTIIPLNVTQSAIVTPEMVQQIDAfhqhTKDPAGLLIKPMLDYYYNFYsKSNPG 236
Cdd:COG1957 159 NVTPVAEFNIYVDPEAAKIVFASGIPITMVGLDVTHQALLTPEDLARLAA----LGTPLGRFLADLLDFYLDFY-RERYG 233
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1926918551 237 IQGSPMHDFVTIWYLLNRDAVHLSKVPIKIIPDQGEGFGQSIADFRFTTNSSYSIHnVAFQFNYERFKQDILDTFLK 313
Cdd:COG1957 234 LDGCPLHDPLAVAYLLDPELFTTRPAPVDVETDGELTRGQTVVDWRGVTGRPPNAR-VALDVDAERFLDLLLERLAR 309
|
|
| IU_nuc_hydro |
pfam01156 |
Inosine-uridine preferring nucleoside hydrolase; |
5-305 |
3.12e-59 |
|
Inosine-uridine preferring nucleoside hydrolase;
Pssm-ID: 460086 [Multi-domain] Cd Length: 253 Bit Score: 190.11 E-value: 3.12e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926918551 5 VLLFTDLGIDDAFAILYTFFREDIQLVGIVADYGNVSREKAIWNINYLKYIAGRQEIPVFLGAsipltgiAVEAFPEIhg 84
Cdd:pfam01156 1 VIIDTDPGIDDALALLLALASPEIELLGITTVAGNVSLEQTTRNALRLLELGGRDDIPVYAGE-------AIREPGEV-- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926918551 85 eaglgpiippqinlpvypihdiyqvidlhsdnlTVINLGRLSSLATAFVL--NLPKMreVKDYICMGGAFFYPGNVTAVA 162
Cdd:pfam01156 72 ---------------------------------TLVATGPLTNLALALRLdpELAKK--IKELVIMGGAFGVRGNVTPAA 116
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926918551 163 EANFFSDPYAANLIVKHAKNLTIIPLNVTQSAIVTPEMVQQIDAFHqhtkDPAGLLIKPMLDYYYNFYSKSNpGIQGSPM 242
Cdd:pfam01156 117 EFNIFVDPEAAKIVFTSGLPITMVPLDVTHQALLTPEDLERLAALG----TPLGRFLADLLRFYAEFYRERF-GIDGPPL 191
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1926918551 243 HDFVTIWYLLNRDAVHLSKVPIKIIPDQGEGFGQSIADFRFTTNSSYSIHnVAFQFNYERFKQ 305
Cdd:pfam01156 192 HDPLAVAVALDPELFTTRRLNVDVETTGGLTRGQTVVDDRGGWGKPPNVR-VATDVDVDRFWE 253
|
|
| PLN02717 |
PLN02717 |
uridine nucleosidase |
3-255 |
1.11e-38 |
|
uridine nucleosidase
Pssm-ID: 178319 [Multi-domain] Cd Length: 316 Bit Score: 138.97 E-value: 1.11e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926918551 3 KKVLLFTDLGIDDAFAILYTFFREDIQLVGIVADYGNVSREKAIWNINYLKYIAGRQEIPVFLGASIPLTGIAVEAFPE- 81
Cdd:PLN02717 1 KKLIIDTDPGIDDAMAILMALRSPEVEVIGLTTIFGNVTTKLATRNALHLLEMAGRPDVPVAEGSHEPLKGGTKPRIADf 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926918551 82 IHGEAGLGPIIPPQinlPVYPIHD------IYQVIDLHSDNLTVINLGRLSSLATAFVLNLPKMREVKDYICMGGAFFYP 155
Cdd:PLN02717 81 VHGSDGLGNTNLPP---PKGKKIEksaaefLVEKVSEYPGEVTVVALGPLTNLALAIKLDPSFAKKVGQIVVLGGAFFVN 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926918551 156 GNVTAVAEANFFSDPYAANLIVKHAKNLTIIPLNVTQSAIVTPEMVQQIdafhQHTKDPAGLLIKPMLDYYYNFYSKSNp 235
Cdd:PLN02717 158 GNVNPAAEANIFGDPEAADIVFTSGADITVVGINVTTQVVLTDADLEEL----RDSKGKYAQFLCDICKFYRDWHRKSY- 232
|
250 260
....*....|....*....|
gi 1926918551 236 GIQGSPMHDFVTIWYLLNRD 255
Cdd:PLN02717 233 GIDGIYLHDPTALLAAVRPS 252
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| nuc_hydro |
cd00455 |
nuc_hydro: Nucleoside hydrolases. Nucleoside hydrolases cleave the N-glycosidic bond in ... |
5-307 |
2.82e-114 |
|
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: 331.99 E-value: 2.82e-114
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926918551 5 VLLFTDLGIDDAFAILYTFFREDIQLVGIVADYGNVSREKAIWNINYLKYIAGRQEIPVFLGASIPLTGIAVEAFPEIHG 84
Cdd:cd00455 1 VILDTDPGIDDAFALMYALLHPEIELVGIVATYGNVTLEQATQNAAYLLELLGRLDIPVYAGATRPLTGEIPAAYPEIHG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926918551 85 EAGLGPIIPPQINL-PVYPIHDIYQVIDLHSDNLTVINLGRLSSLATAFVLNlPKMRE-VKDYICMGGAFFYPGNVTAVA 162
Cdd:cd00455 81 EGGLGLPIPPIIEAdDPEAVQLLIDLIRKYPDEITIVALGPLTNLAMAFILD-PDIKDrVKEIVIMGGAFLVPGNVTPVA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926918551 163 EANFFSDPYAANLIVKHAKNLTIIPLNVTQSAIVTPEMVQQIDAFHqhtkDPAGLLIKPMLDYYYNFYSKsnPGIQGSPM 242
Cdd:cd00455 160 EANFYGDPEAANIVFNSAKNLTIVPLDVTNQAVLTPPMVERIFEQG----TSIGLLIKPMIDYYYKAYQK--PGIEGSPI 233
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1926918551 243 HDFVTIWYLLNRDAVHLSKVPIKIIPDqGEGFGQSIADFRFttNSSYSIHNVAFQFNYERFKQDI 307
Cdd:cd00455 234 HDPLAVAYLLNPSMFDYSKVPVDVDTD-GLTRGQTIADFRE--NPGNGVTRVAVNLDYPDFIELI 295
|
|
| URH1 |
COG1957 |
Inosine-uridine nucleoside N-ribohydrolase [Nucleotide transport and metabolism]; ... |
1-313 |
1.47e-84 |
|
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: 257.00 E-value: 1.47e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926918551 1 MQKKVLLFTDLGIDDAFAILYTFFREDIQLVGIVADYGNVSREKAIWNINYLKYIAGRQEIPVFLGASIPLTGIAVEAfP 80
Cdd:COG1957 1 MMRKVIIDTDPGIDDALALLLALASPEIDLLGITTVAGNVPLEQTTRNALKLLELAGRTDVPVAAGAARPLVRPLVTA-E 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926918551 81 EIHGEAGLGPIIPPQINLPVYPIHDIYQVIDL---HSDNLTVINLGRLSSLATAFVLNlPKMRE-VKDYICMGGAFFYPG 156
Cdd:COG1957 80 HVHGEDGLGGVDLPEPTRPPEPEHAVDFIIETlraAPGEVTLVALGPLTNLALALRKD-PELAErIKRIVIMGGAFFVPG 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926918551 157 NVTAVAEANFFSDPYAANLIVKHAKNLTIIPLNVTQSAIVTPEMVQQIDAfhqhTKDPAGLLIKPMLDYYYNFYsKSNPG 236
Cdd:COG1957 159 NVTPVAEFNIYVDPEAAKIVFASGIPITMVGLDVTHQALLTPEDLARLAA----LGTPLGRFLADLLDFYLDFY-RERYG 233
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1926918551 237 IQGSPMHDFVTIWYLLNRDAVHLSKVPIKIIPDQGEGFGQSIADFRFTTNSSYSIHnVAFQFNYERFKQDILDTFLK 313
Cdd:COG1957 234 LDGCPLHDPLAVAYLLDPELFTTRPAPVDVETDGELTRGQTVVDWRGVTGRPPNAR-VALDVDAERFLDLLLERLAR 309
|
|
| nuc_hydro_CaPnhB |
cd02650 |
NH_hydro_CaPnhB: A subgroup of nucleoside hydrolases similar to Corynebacterium ammoniagenes ... |
4-282 |
2.15e-62 |
|
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: 200.20 E-value: 2.15e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926918551 4 KVLLFTDLGIDDAFAILYTFFREDIQLVGIVADYGNVSREKAIWNINYLKYIAGRQEIPVFLGASIPLTGIAVEAFPEIH 83
Cdd:cd02650 1 KLILDTDPGIDDAMALAYALAHPDVDLIGVTTVYGNVTIETATRNALALLELFGRPDVPVAEGAAKPLTRPPFRIATFVH 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926918551 84 GEAGLGPIIPPQINLPVYPIHDIYQVIDL---HSDNLTVINLGRLSSLATAFVLN--LPKMreVKDYICMGGAFFYPGNV 158
Cdd:cd02650 81 GDNGLGDVELPAPPRQPEDESAADFLIELaneYPGELTLVAVGPLTNLALALARDpdFAKL--VKQVVVMGGAFTVPGNV 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926918551 159 TAVAEANFFSDPYAANLIVKHAKNLTIIPLNVTQSAIVTPEmvqQIDAFHQhTKDPAGLLIKPMLDYYYNFYSKsNPGIQ 238
Cdd:cd02650 159 TPAAEANIHGDPEAADIVFTAGADLTMVGLDVTTQTLLTRE---DLDELRD-SGGKAGQFLADMLDYYIDFYQE-SPGLR 233
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 1926918551 239 GSPMHDFVTIWYLLNRDAVHLSKVPIKIIPDqGEGFGQSIADFR 282
Cdd:cd02650 234 GCALHDPLAVAAAVDPSLFTTREGVVRVETE-GPTRGRTIGDRD 276
|
|
| IU_nuc_hydro |
pfam01156 |
Inosine-uridine preferring nucleoside hydrolase; |
5-305 |
3.12e-59 |
|
Inosine-uridine preferring nucleoside hydrolase;
Pssm-ID: 460086 [Multi-domain] Cd Length: 253 Bit Score: 190.11 E-value: 3.12e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926918551 5 VLLFTDLGIDDAFAILYTFFREDIQLVGIVADYGNVSREKAIWNINYLKYIAGRQEIPVFLGAsipltgiAVEAFPEIhg 84
Cdd:pfam01156 1 VIIDTDPGIDDALALLLALASPEIELLGITTVAGNVSLEQTTRNALRLLELGGRDDIPVYAGE-------AIREPGEV-- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926918551 85 eaglgpiippqinlpvypihdiyqvidlhsdnlTVINLGRLSSLATAFVL--NLPKMreVKDYICMGGAFFYPGNVTAVA 162
Cdd:pfam01156 72 ---------------------------------TLVATGPLTNLALALRLdpELAKK--IKELVIMGGAFGVRGNVTPAA 116
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926918551 163 EANFFSDPYAANLIVKHAKNLTIIPLNVTQSAIVTPEMVQQIDAFHqhtkDPAGLLIKPMLDYYYNFYSKSNpGIQGSPM 242
Cdd:pfam01156 117 EFNIFVDPEAAKIVFTSGLPITMVPLDVTHQALLTPEDLERLAALG----TPLGRFLADLLRFYAEFYRERF-GIDGPPL 191
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1926918551 243 HDFVTIWYLLNRDAVHLSKVPIKIIPDQGEGFGQSIADFRFTTNSSYSIHnVAFQFNYERFKQ 305
Cdd:pfam01156 192 HDPLAVAVALDPELFTTRRLNVDVETTGGLTRGQTVVDDRGGWGKPPNVR-VATDVDVDRFWE 253
|
|
| nuc_hydro_IU_UC_XIUA |
cd02651 |
nuc_hydro_IU_UC_XIUA: inosine-uridine preferring, ... |
4-309 |
3.32e-50 |
|
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: 168.49 E-value: 3.32e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926918551 4 KVLLFTDLGIDDAFAILYTFFREDIQLVGIVADYGNVSREKAIWNINYLKYIAGRQEIPVFLGASIPLTGIAVEAfPEIH 83
Cdd:cd02651 1 PIIIDCDPGHDDAVAILLALFHPELDLLGITTVAGNVPLEKTTRNALKLLTLLGRTDVPVAAGAARPLVRPLITA-SDIH 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926918551 84 GEAGLGPIIPPQINLPVYPIHD---IYQVIDLHSDNLTVINLGRLSSLATAFVLNlPKMRE-VKDYICMGGAFFYpGNVT 159
Cdd:cd02651 80 GESGLDGADLPPPPRRPEDIHAvdaIIDTLRASPEPITLVATGPLTNIALLLRKY-PELAErIKEIVLMGGALGR-GNIT 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926918551 160 AVAEANFFSDPYAANLIVKHAKNLTIIPLNVTQSAIVTPEMVQQIDAfhqhTKDPAGLLIKPMLDYYYNFYSKSnpGIQG 239
Cdd:cd02651 158 PAAEFNIFVDPEAAKIVFNSGIPITMVPLDVTHKALATPEVIERIRA----LGNPVGKMLAELLDFFAETYGSA--FTEG 231
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926918551 240 SPMHDFVTIWYLLNRDAVHLSKVPIKIIPDQGEGFGQSIADFRFTTNSSYSIHnVAFQFNYERFKQDILD 309
Cdd:cd02651 232 PPLHDPCAVAYLLDPELFTTKRANVDVETEGELTRGRTVVDLRGVTGRPANAQ-VAVDVDVEKFWDLLLE 300
|
|
| nuc_hydro_3 |
cd02653 |
NH_3: A subgroup of nucleoside hydrolases. This group contains eukaryotic and bacterial ... |
4-280 |
3.62e-42 |
|
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: 148.29 E-value: 3.62e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926918551 4 KVLLFTDLGIDDAFAILYTFFREDIQLVGIVADYGNVSREKAIWNINYLKYIAGRQEIPVFLGASIPLTGIAVEAfPEIH 83
Cdd:cd02653 1 KVIIDCDPGIDDALALLYLLASPDLDVVGITTTAGNVPVEQVAANALGVLELLGRTDIPVYLGADKPLAGPLTTA-QDTH 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926918551 84 GEAGLG--PIIPPQINLPVYPIHDIYqvIDL--HSDNLTVINLGRLSSLATAFVLNlPKM-REVKDYICMGGAFFYPGNV 158
Cdd:cd02653 80 GPDGLGyaELPASTRTLSDESAAQAW--VDLarAHPDLIGLATGPLTNLALALREE-PELpRLLRRLVIMGGAFNSRGNT 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926918551 159 TAVAEANFFSDPYAA----NLIVKHAKNLTIIPLNVTQSAIVTPEMVQQIDAFhqhtKDPAGLLIKPMLDYYYNFYSKSN 234
Cdd:cd02653 157 SPVAEWNYWVDPEAAkevlAAFGGHPVRPTICGLDVTRAVVLTPNLLERLARA----KDSVGAFIEDALRFYFEFHWAYG 232
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 1926918551 235 PGIqGSPMHDFVTIWYLLNRDAVHLSKVPIKIIpDQGEGFGQSIAD 280
Cdd:cd02653 233 HGY-GAVIHDPLAAAVALNPNLARGRPAYVDVE-CTGVLTGQTVVD 276
|
|
| PLN02717 |
PLN02717 |
uridine nucleosidase |
3-255 |
1.11e-38 |
|
uridine nucleosidase
Pssm-ID: 178319 [Multi-domain] Cd Length: 316 Bit Score: 138.97 E-value: 1.11e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926918551 3 KKVLLFTDLGIDDAFAILYTFFREDIQLVGIVADYGNVSREKAIWNINYLKYIAGRQEIPVFLGASIPLTGIAVEAFPE- 81
Cdd:PLN02717 1 KKLIIDTDPGIDDAMAILMALRSPEVEVIGLTTIFGNVTTKLATRNALHLLEMAGRPDVPVAEGSHEPLKGGTKPRIADf 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926918551 82 IHGEAGLGPIIPPQinlPVYPIHD------IYQVIDLHSDNLTVINLGRLSSLATAFVLNLPKMREVKDYICMGGAFFYP 155
Cdd:PLN02717 81 VHGSDGLGNTNLPP---PKGKKIEksaaefLVEKVSEYPGEVTVVALGPLTNLALAIKLDPSFAKKVGQIVVLGGAFFVN 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926918551 156 GNVTAVAEANFFSDPYAANLIVKHAKNLTIIPLNVTQSAIVTPEMVQQIdafhQHTKDPAGLLIKPMLDYYYNFYSKSNp 235
Cdd:PLN02717 158 GNVNPAAEANIFGDPEAADIVFTSGADITVVGINVTTQVVLTDADLEEL----RDSKGKYAQFLCDICKFYRDWHRKSY- 232
|
250 260
....*....|....*....|
gi 1926918551 236 GIQGSPMHDFVTIWYLLNRD 255
Cdd:PLN02717 233 GIDGIYLHDPTALLAAVRPS 252
|
|
| rihB |
PRK09955 |
ribosylpyrimidine nucleosidase; |
2-280 |
1.93e-33 |
|
ribosylpyrimidine nucleosidase;
Pssm-ID: 182166 [Multi-domain] Cd Length: 313 Bit Score: 125.06 E-value: 1.93e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926918551 2 QKKVLLFTDLGIDDAFAILYTFFREDIQLVGIVADYGNVSREKAIWN-INYLKYIagRQEIPVFLGASIPLTGIAVEAfP 80
Cdd:PRK09955 3 KRKIILDCDPGHDDAIAMMMAAKHPAIDLLGITIVAGNQTLDKTLINgLNVCQKL--EINVPVYAGMPQPIMRQQIVA-D 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926918551 81 EIHGEAGL-GPIIPPqINLPVYPIHDIYQVID--LHSD-NLTVINLGRLSSLATAFVLN---LPKMREVkdyICMGGAFf 153
Cdd:PRK09955 80 NIHGETGLdGPVFEP-LTRQAESTHAVKYIIDtlMASDgDITLVPVGPLSNIAVAMRMQpaiLPKIREI---VLMGGAY- 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926918551 154 YPGNVTAVAEANFFSDPYAANLIVKHAKNLTIIPLNVTQSAIVTPEMVQQIDAfhqhTKDPAGLLIKPMLdyyyNFYSKS 233
Cdd:PRK09955 155 GTGNFTPSAEFNIFADPEAARVVFTSGVPLVMMGLDLTNQTVCTPDVIARMER----AGGPAGELFSDIM----NFTLKT 226
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 1926918551 234 ---NPGIQGSPMHDFVTIWYLLNRDAVHLSKVPIKIIPDQGEGFGQSIAD 280
Cdd:PRK09955 227 qfeNYGLAGGPVHDATCIGYLINPDGIKTQEMYVEVDVNSGPCYGRTVCD 276
|
|
| PRK10768 |
PRK10768 |
ribonucleoside hydrolase RihC; Provisional |
1-311 |
4.32e-31 |
|
ribonucleoside hydrolase RihC; Provisional
Pssm-ID: 182713 [Multi-domain] Cd Length: 304 Bit Score: 118.47 E-value: 4.32e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926918551 1 MQKKVLLFTDLGIDDAFAILYTFFRE--DIQLVGIVAdyGNVSREKAiwNINYLKYIA-GRQEIPVFLGASIPLTGIAVE 77
Cdd:PRK10768 1 MRLPIILDTDPGIDDAVAIAAALFAPelDLKLITTVA--GNVSVEKT--TRNALKLLHfFNSDVPVAQGAAKPLVRPLRD 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926918551 78 AfPEIHGEAGLGPIIPPQIN---LPVYPIHDIYQVIDLHSDNLTVINLGRLSSLAtafvLNLPKMREVKDYI----CMGG 150
Cdd:PRK10768 77 A-ASVHGESGMEGYDFPEHTrkpLSIPAVEAMRDALMNAPEPVTLVAIGPLTNIA----LLLSTYPEVKPYIkrivLMGG 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926918551 151 AFfYPGNVTAVAEANFFSDPYAANLIVKHAKNLTIIPLNVTQSAIVTPEMVQQIDAFHQhtkdpAGLLIKPMLDYYynfY 230
Cdd:PRK10768 152 SA-GRGNVTPNAEFNIAVDPEAAAIVFRSGIPIVMCGLDVTNQALLTPDYLATLPELNR-----TGKMLHALFSHY---R 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926918551 231 SKSNPGiqGSPMHDFVTIWYLLNRDAVHLSKVPIKIIPDQGEGFGQSIADFRFTTNSSYSIHnVAFQFNYERFKQDILDT 310
Cdd:PRK10768 223 SGSMQT--GLRMHDVCAIAYLLRPELFTLKPCFVDVETQGEFTAGATVVDIDGRLGKPANAQ-VALDIDVDGFQKWFAEV 299
|
.
gi 1926918551 311 F 311
Cdd:PRK10768 300 L 300
|
|
| nuc_hydro_CeIAG |
cd02649 |
nuc_hydro_CeIAG: Nucleoside hydrolases similar to the inosine-adenosine-guanosine-preferring ... |
3-194 |
5.03e-30 |
|
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: 115.43 E-value: 5.03e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926918551 3 KKVLLFTDLGIDDAFAILYTFFREDIQLVGIVADYGNVSREKAIWNINYLKYIAGRQEIPVFLGASIPLTGIAVEAFpEI 82
Cdd:cd02649 1 RKLIIDTDCGGDDAWALLMALASPNVEVLAITCVHGNTNVEQVVKNALRVLEACGRRDIPVYRGASKPLLGPGPTAA-YF 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926918551 83 HGEAGLG--PIIPPQINLPVYPIHDIYQVIDL---HSDNLTVINLGRLSSLATAFVL--NLPKMreVKDYICMGGAFFYP 155
Cdd:cd02649 80 HGKDGFGdvGFPEPKDELELQKEHAVDAIIRLvreYPGEITLVALGPLTNLALAYRLdpSLPQK--IKRLYIMGGNREGV 157
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1926918551 156 GNVTAVAEANFFSDPYAANlIVKHA--KNLTIIPLNVTQSA 194
Cdd:cd02649 158 GNTTPAAEFNFHVDPEAAH-IVLNSfgCPITIVPWETTLLA 197
|
|
| rihA |
PRK10443 |
ribonucleoside hydrolase 1; Provisional |
1-253 |
1.10e-26 |
|
ribonucleoside hydrolase 1; Provisional
Pssm-ID: 182465 [Multi-domain] Cd Length: 311 Bit Score: 106.68 E-value: 1.10e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926918551 1 MQKKVLLFTDLGIDDAFAILYTFFREDIQLVGIVADYGNVSREKAIWNINYLKYIAGRQEIPVFLGASIPLTGIAVEAfP 80
Cdd:PRK10443 1 MALPIILDCDPGHDDAIALVLALASPELDVKAVTTSAGNQTPEKTLRNALRMLTLLNRTDIPVAGGAVKPLMRELIIA-D 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926918551 81 EIHGEAGL-GPIIP-----PQinlPVYPIHDIYQVIDLHSDNLTVINLGRLSSLATaFVLNLPKMREVKDYIC-MGGAFF 153
Cdd:PRK10443 80 NVHGESGLdGPALPeptfaPQ---NCTAVELMAKTLRESAEPVTLVSTGPQTNVAL-LLASHPELHSKIARIViMGGAMG 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926918551 154 YpGNVTAVAEANFFSDPYAANLIVKHAKNLTIIPLNVTQSAIVTPEMVQQIDAfhqhTKDPAGLLIKPMLDYYYNFYSKS 233
Cdd:PRK10443 156 L-GNWTPAAEFNIYVDPEAAEIVFQSGIPIVMAGLDVTHKAQIMDEDIERIRA----IGNPVATIVAELLDFFMEYHKDE 230
|
250 260
....*....|....*....|
gi 1926918551 234 NPGIQGSPMHDFVTIWYLLN 253
Cdd:PRK10443 231 KWGFVGAPLHDPCTIAWLLK 250
|
|
| nuc_hydro_1 |
cd02648 |
NH_1: A subgroup of nucleoside hydrolases. This group contains fungal proteins similar to ... |
4-290 |
3.72e-20 |
|
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: 89.56 E-value: 3.72e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926918551 4 KVLLFTDLGIDDAFAILYTFFR-EDIQLVGIVADYGNVSREKAIWNINYLKYI-------------------AGRQEIPV 63
Cdd:cd02648 3 PIIIDTDPGVDDVLAILLALSSpEEVDVALISLTFGNTTLDHALRNVLRLFHVlererawratpgvryrafsADAEKPIV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926918551 64 FLGASIPLTGIAVEAfPEIHGEAGLG------------PIIPPQINLPVYPIHDI-YQVI-DL---HSDN-LTVINLGRL 125
Cdd:cd02648 83 ASGSDQPLEGERLTA-SYFHGRDGLSgvhwlhpdftpvETWIPEIVAPLTPSDKPaYDVIlDIlreEPDHtVTIAALGPL 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926918551 126 SSLATAFVLNLPKMREVKDYICMGGAFFYPGNVTAVAEANFFSDPYAANLIV----KHAK------NLTIIPLNVTqsai 195
Cdd:cd02648 162 TNLAAAARKDPETFAKVGEVVVMGGAIDVPGNTSPVAEFNCFADPYAAAVVIdeppSTAPearrklPLQVFPLDIT---- 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926918551 196 vTPEMVQQIDAFHQH-----TKDPAGLLIKPMLDYYYNFYSKSNPGIQGSP----------MHDFVTIWYLLNRDAVHLS 260
Cdd:cd02648 238 -TGHTLPYSSLFATYvtprdAPERGSPLARWLEHVFISTFLTHPRAFTPEEflpdrselfeMHDPLAVWYAIFADMPATG 316
|
330 340 350
....*....|....*....|....*....|
gi 1926918551 261 KVPikiipdqGEGFGQSIADFRFTTNSSYS 290
Cdd:cd02648 317 SID-------GNGWKHTPRDFRVETSGQWT 339
|
|
| nuc_hydro_CjNH |
cd02654 |
nuc_hydro_CjNH. Nucleoside hydrolases similar to Campylobacter jejuni nucleoside hydrolase. ... |
4-248 |
1.12e-13 |
|
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: 70.28 E-value: 1.12e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926918551 4 KVLLFTDLGI----DDAFAILYTFFREDIQLVGIVADYGNVSREKAIWNINYLKYIAGRQEIPVFLGASIPLTGI----- 74
Cdd:cd02654 1 KVILDNDIAMgrdtDDGLALALLLWSPEVELLGLSAVSGNCWLSAVTYNVLRMLELAGADAIPVYAGANTPLGRTnrafh 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926918551 75 AVEAF-----------PEIHGEAGLGPIIpPQINLPVypIHDIYQVIDLHSDNLTVINLGRLSSLATAFVLNLPKMREVK 143
Cdd:cd02654 81 AWESLygaylwqgawsPEYSDMYTNASII-RNASIPA--ALFMIEMVRKHPHEVSIVAAGPLTNLALALRIDPDFAPLAK 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926918551 144 DYICMGGAF-FYPGNVTAV--AEANFFSDPYAANLIVKHAKNLTIIPLNVTQSAIVTPEmvqqidafHQHTKDPAGLLIK 220
Cdd:cd02654 158 ELVIMGGYLdDIGEFVNRHyaSDFNLIMDPEAASIVLTAPWKSITIPGNVTNRTCLTPE--------QIKADDPLRDFIR 229
|
250 260
....*....|....*....|....*...
gi 1926918551 221 PMLDYYYNFYSKSNPGIQGSPMHDFVTI 248
Cdd:cd02654 230 ETLDLPIDYAKEFVGTGDGLPMWDELAS 257
|
|
| nuc_hydro_TvIAG |
cd02647 |
nuc_hydro_ TvIAG: Nucleoside hydrolases similar to the Inosine-adenosine-guanosine-preferring ... |
3-280 |
3.63e-12 |
|
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: 65.90 E-value: 3.63e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926918551 3 KKVLLFTDLGIDDAFAILYTFFREDIQLVGI-----VAD-YGNVSREKAIWNINYLKyiaGRQEIPVFLGASIPltgiaV 76
Cdd:cd02647 1 KNVIFDHDGNVDDLVALLLLLKNEKVDLKGIgvsgiDADcYVEPAVSVTRKLIDRLG---QRDAIPVGKGGSRA-----V 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926918551 77 EAFP-EIHGEAGLGPIIPPQIN--------LPVYPIH-DIYQVIDLHSDNLTVINLGRLSSLATAFVLNlpkmREVKDYI 146
Cdd:cd02647 73 NPFPrSWRRDAAFSVDHLPILNerytvetpLAEETAQlVLIEKIKASLEPVTLLVTGPLTNLARALDSD----PDISSNI 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926918551 147 ----CMGGAFFYPGNVTAV-----AEANFFSDPYAANLIVKHAKNLTIIPLNVTQSAIVTPEMVQQIDAFHQHTKDPAGL 217
Cdd:cd02647 149 eevyIMGGGVDAPGNVFTPpsngtAEFNIFWDPLAAKTVFDSGLKITLVPLDATNTVPLTREFLETDRQRFAAQRLPASD 228
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1926918551 218 LIKPMLDYYynfysKSNPGIQGSPMHDFVTIWYLLNRDAVHLSKVPIKIIPDQGEGFGQSIAD 280
Cdd:cd02647 229 LAGQGYALV-----KPLEFNSTYYMWDVLTTLVLGAKEVDNTKESLILEVDTDGLSAGQTVTS 286
|
|
| nuc_hydro_2 |
cd02652 |
NH_2: A subgroup of nucleoside hydrolases. This group contains eukaryotic and bacterial ... |
5-218 |
9.46e-05 |
|
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: 43.26 E-value: 9.46e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926918551 5 VLLFTDLG--IDDAFAILYTFFREDIQLVGIVADYGNVSREKAIWNINYLkyiAGRQEIPVFLGASIPLTGiAVEAFPEI 82
Cdd:cd02652 1 LILDTDIGgdPDDALALALAHALQKCDLLAVTITLADASARRAIDAVNRF---YGRGDIPIGADYHGWPED-AKDHAKFL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926918551 83 HGEAGLGPIIPPQINLPvypihDIYQV-----IDLHSDNLTVINLGRLSSL-----ATAFVLNLPKM--REVKDYICMGG 150
Cdd:cd02652 77 LEGDRLHHDLESAEDAL-----DAVKAlrrllASAEDASVTIVSIGPLTNLaalldADADPLTGPELvrQKVKRLVVMGG 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926918551 151 AFFYPGNVTAVAEANFFSDPYAANLIVKHAKNLTiIPLNVTQS------AIVTPeMVQQI---------DAFHQH----- 210
Cdd:cd02652 152 AFYDPDGNVQHREYNFVTDPKAAQRVAGRAQHLG-IPVRIVWSgyelgeAVSYP-HVLVIahpfntpvfAAYWPRshrrp 229
|
....*...
gi 1926918551 211 TKDPAGLL 218
Cdd:cd02652 230 LWDPLTLL 237
|
|
| PTZ00313 |
PTZ00313 |
inosine-adenosine-guanosine-nucleoside hydrolase; Provisional |
140-277 |
7.84e-04 |
|
inosine-adenosine-guanosine-nucleoside hydrolase; Provisional
Pssm-ID: 140334 [Multi-domain] Cd Length: 326 Bit Score: 40.62 E-value: 7.84e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926918551 140 REVKDYICMGGAFFYPGNV-----TAVAEANFFSDPYAAN--LIVKHAKNLtIIPLNVTQSAIVTPEMVQQIDAFHQHtk 212
Cdd:PTZ00313 156 KKVEECVIMGGAVDVGGNVflpgtDGSAEWNIYWDPPAAKtvLMCPHIRKV-LFSLDSTNSVPVTSEVVKKFGAQNKY-- 232
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1926918551 213 dpaglLIKPMLDYYY---NFYSKSNPGiQGSPMHDFVTIWYLLNRDAVHLSKVPIKIIPDQGEGFGQS 277
Cdd:PTZ00313 233 -----LLSQFVGSTWamcTHHELLRPG-DGYYAWDVLTAAYVIERNLAELEPVPLEVVVEKAKNEGRT 294
|
|
| |
