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Conserved domains on  [gi|446679112|ref|WP_000756458|]
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MULTISPECIES: nucleoside hydrolase [Bacillus]

Protein Classification

nucleoside hydrolase( domain architecture ID 10087436)

nucleoside hydrolase cleaves the N-glycosidic bond in nucleosides generating ribose and the corresponding base, similar to inosine-uridine preferring nucleoside hydrolase

CATH:  3.90.245.10
EC:  3.2.2.-
SCOP:  4000751

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
nuc_hydro cd00455
nuc_hydro: Nucleoside hydrolases. Nucleoside hydrolases cleave the N-glycosidic bond in ...
 4-305 9.57e-138

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: 391.31  E-value: 9.57e-138
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446679112   4 VLFLGDPGIDDSLAIMYGLLHPDIDIVGVVTGYGNVTQEKATSNAAYLLQMAGREDIPVINGAKIPLSGDITTYYPEIHG 83
Cdd:cd00455    1 VILDTDPGIDDAFALMYALLHPEIELVGIVATYGNVTLEQATQNAAYLLELLGRLDIPVYAGATRPLTGEIPAAYPEIHG 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446679112  84 TDGLGPIKPPKTFSPNIKPFCTFFDLLEKYKGELIIVDAGRSTTLATAFILEKPMMKYVKEYYIMGGAFLMPGNVTPVAE 163
Cdd:cd00455   81 EGGLGLPIPPIIEADDPEAVQLLIDLIRKYPDEITIVALGPLTNLAMAFILDPDIKDRVKEIVIMGGAFLVPGNVTPVAE 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446679112 164 ANFHGDPIASQLVMQNAKNVTLVPLNVTSEAIITPEMVKYITKHSkTSFNKLIEPIFTYYYKAYRKlnPKIKGSPVHDVV 243
Cdd:cd00455  161 ANFYGDPEAANIVFNSAKNLTIVPLDVTNQAVLTPPMVERIFEQG-TSIGLLIKPMIDYYYKAYQK--PGIEGSPIHDPL 237

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446679112 244 TMMVAANPSLLDYVYRRVDVDTAGIAKGESIADFRPQPDakalKNWVRIGWSLHYKKFLEDF 305
Cdd:cd00455  238 AVAYLLNPSMFDYSKVPVDVDTDGLTRGQTIADFRENPG----NGVTRVAVNLDYPDFIELI 295
 
Name Accession Description Interval E-value
nuc_hydro cd00455
nuc_hydro: Nucleoside hydrolases. Nucleoside hydrolases cleave the N-glycosidic bond in ...
 4-305 9.57e-138

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: 391.31  E-value: 9.57e-138
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446679112   4 VLFLGDPGIDDSLAIMYGLLHPDIDIVGVVTGYGNVTQEKATSNAAYLLQMAGREDIPVINGAKIPLSGDITTYYPEIHG 83
Cdd:cd00455    1 VILDTDPGIDDAFALMYALLHPEIELVGIVATYGNVTLEQATQNAAYLLELLGRLDIPVYAGATRPLTGEIPAAYPEIHG 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446679112  84 TDGLGPIKPPKTFSPNIKPFCTFFDLLEKYKGELIIVDAGRSTTLATAFILEKPMMKYVKEYYIMGGAFLMPGNVTPVAE 163
Cdd:cd00455   81 EGGLGLPIPPIIEADDPEAVQLLIDLIRKYPDEITIVALGPLTNLAMAFILDPDIKDRVKEIVIMGGAFLVPGNVTPVAE 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446679112 164 ANFHGDPIASQLVMQNAKNVTLVPLNVTSEAIITPEMVKYITKHSkTSFNKLIEPIFTYYYKAYRKlnPKIKGSPVHDVV 243
Cdd:cd00455  161 ANFYGDPEAANIVFNSAKNLTIVPLDVTNQAVLTPPMVERIFEQG-TSIGLLIKPMIDYYYKAYQK--PGIEGSPIHDPL 237

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446679112 244 TMMVAANPSLLDYVYRRVDVDTAGIAKGESIADFRPQPDakalKNWVRIGWSLHYKKFLEDF 305
Cdd:cd00455  238 AVAYLLNPSMFDYSKVPVDVDTDGLTRGQTIADFRENPG----NGVTRVAVNLDYPDFIELI 295
URH1 COG1957
Inosine-uridine nucleoside N-ribohydrolase [Nucleotide transport and metabolism]; ...
 1-310 3.83e-102

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: 301.69  E-value: 3.83e-102
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446679112   1 MKKVLFLGDPGIDDSLAIMYGLLHPDIDIVGVVTGYGNVTQEKATSNAAYLLQMAGREDIPVINGAKIPLSGDITTYyPE 80
Cdd:COG1957    2 MRKVIIDTDPGIDDALALLLALASPEIDLLGITTVAGNVPLEQTTRNALKLLELAGRTDVPVAAGAARPLVRPLVTA-EH 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446679112  81 IHGTDGLGPIK-PPKTFSPNIKPFCTFF-DLLEKYKGELIIVDAGRSTTLATAFILEKPMMKYVKEYYIMGGAFLMPGNV 158
Cdd:COG1957   81 VHGEDGLGGVDlPEPTRPPEPEHAVDFIiETLRAAPGEVTLVALGPLTNLALALRKDPELAERIKRIVIMGGAFFVPGNV 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446679112 159 TPVAEANFHGDPIASQLVMQNAKNVTLVPLNVTSEAIITPEMVKYItKHSKTSFNKLIEPIFTYYYKAYRKlNPKIKGSP 238
Cdd:COG1957  161 TPVAEFNIYVDPEAAKIVFASGIPITMVGLDVTHQALLTPEDLARL-AALGTPLGRFLADLLDFYLDFYRE-RYGLDGCP 238

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446679112 239 VHDVVTMMVAANPSLLDYVYRRVDVDTAG-IAKGESIADFRPQPDAKAlkNwVRIGWSLHYKKFLEDFVKFMT 310
Cdd:COG1957  239 LHDPLAVAYLLDPELFTTRPAPVDVETDGeLTRGQTVVDWRGVTGRPP--N-ARVALDVDAERFLDLLLERLA 308
IU_nuc_hydro pfam01156
Inosine-uridine preferring nucleoside hydrolase;
9-303 1.58e-71

Inosine-uridine preferring nucleoside hydrolase;


Pssm-ID: 460086 [Multi-domain]  Cd Length: 253  Bit Score: 221.70  E-value: 1.58e-71
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446679112    9 DPGIDDSLAIMYGLLHPDIDIVGVVTGYGNVTQEKATSNAAYLLQMAGREDIPVINGAKIPLSGDITtyypeihgtdglg 88
Cdd:pfam01156   6 DPGIDDALALLLALASPEIELLGITTVAGNVSLEQTTRNALRLLELGGRDDIPVYAGEAIREPGEVT------------- 72

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446679112   89 pikppktfspnikpfctffdllekykgeliIVDAGRSTTLATAFILEKPMMKYVKEYYIMGGAFLMPGNVTPVAEANFHG 168
Cdd:pfam01156  73 ------------------------------LVATGPLTNLALALRLDPELAKKIKELVIMGGAFGVRGNVTPAAEFNIFV 122

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446679112  169 DPIASQLVMQNAKNVTLVPLNVTSEAIITPEMVKYItKHSKTSFNKLIEPIFTYYYKAYRKLNPkIKGSPVHDVVTMMVA 248
Cdd:pfam01156 123 DPEAAKIVFTSGLPITMVPLDVTHQALLTPEDLERL-AALGTPLGRFLADLLRFYAEFYRERFG-IDGPPLHDPLAVAVA 200

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 446679112  249 ANPSLLDYVYRRVDVDTAG-IAKGESIADFRPQPDAKALknwVRIGWSLHYKKFLE 303
Cdd:pfam01156 201 LDPELFTTRRLNVDVETTGgLTRGQTVVDDRGGWGKPPN---VRVATDVDVDRFWE 253
PLN02717 PLN02717
uridine nucleosidase
 2-295 4.23e-60

uridine nucleosidase


Pssm-ID: 178319 [Multi-domain]  Cd Length: 316  Bit Score: 194.44  E-value: 4.23e-60
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446679112   2 KKVLFLGDPGIDDSLAIMYGLLHPDIDIVGVVTGYGNVTQEKATSNAAYLLQMAGREDIPVINGAKIPLSGDITTYYPE- 80
Cdd:PLN02717   1 KKLIIDTDPGIDDAMAILMALRSPEVEVIGLTTIFGNVTTKLATRNALHLLEMAGRPDVPVAEGSHEPLKGGTKPRIADf 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446679112  81 IHGTDGLGPIKPPKtfsPNIKPF----CTFF-DLLEKYKGELIIVDAGRSTTLATAFILEKPMMKYVKEYYIMGGAFLMP 155
Cdd:PLN02717  81 VHGSDGLGNTNLPP---PKGKKIeksaAEFLvEKVSEYPGEVTVVALGPLTNLALAIKLDPSFAKKVGQIVVLGGAFFVN 157

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446679112 156 GNVTPVAEANFHGDPIASQLVMQNAKNVTLVPLNVTSEAIIT-PEMVKYitKHSKTSFNKLIEPIfTYYYKAYRKLNPKI 234
Cdd:PLN02717 158 GNVNPAAEANIFGDPEAADIVFTSGADITVVGINVTTQVVLTdADLEEL--RDSKGKYAQFLCDI-CKFYRDWHRKSYGI 234

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446679112 235 KGSPVHDVVTMMVAANPSLLDYVYRRVDVDTAGIAKGESIADfrpqpdaKALKNWVRI-GWS 295
Cdd:PLN02717 235 DGIYLHDPTALLAAVRPSLFTYKEGVVRVETEGICRGLTLFD-------NGLKRWNGEnAWT 289
 
Name Accession Description Interval E-value
nuc_hydro cd00455
nuc_hydro: Nucleoside hydrolases. Nucleoside hydrolases cleave the N-glycosidic bond in ...
 4-305 9.57e-138

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: 391.31  E-value: 9.57e-138
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446679112   4 VLFLGDPGIDDSLAIMYGLLHPDIDIVGVVTGYGNVTQEKATSNAAYLLQMAGREDIPVINGAKIPLSGDITTYYPEIHG 83
Cdd:cd00455    1 VILDTDPGIDDAFALMYALLHPEIELVGIVATYGNVTLEQATQNAAYLLELLGRLDIPVYAGATRPLTGEIPAAYPEIHG 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446679112  84 TDGLGPIKPPKTFSPNIKPFCTFFDLLEKYKGELIIVDAGRSTTLATAFILEKPMMKYVKEYYIMGGAFLMPGNVTPVAE 163
Cdd:cd00455   81 EGGLGLPIPPIIEADDPEAVQLLIDLIRKYPDEITIVALGPLTNLAMAFILDPDIKDRVKEIVIMGGAFLVPGNVTPVAE 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446679112 164 ANFHGDPIASQLVMQNAKNVTLVPLNVTSEAIITPEMVKYITKHSkTSFNKLIEPIFTYYYKAYRKlnPKIKGSPVHDVV 243
Cdd:cd00455  161 ANFYGDPEAANIVFNSAKNLTIVPLDVTNQAVLTPPMVERIFEQG-TSIGLLIKPMIDYYYKAYQK--PGIEGSPIHDPL 237

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446679112 244 TMMVAANPSLLDYVYRRVDVDTAGIAKGESIADFRPQPDakalKNWVRIGWSLHYKKFLEDF 305
Cdd:cd00455  238 AVAYLLNPSMFDYSKVPVDVDTDGLTRGQTIADFRENPG----NGVTRVAVNLDYPDFIELI 295
URH1 COG1957
Inosine-uridine nucleoside N-ribohydrolase [Nucleotide transport and metabolism]; ...
 1-310 3.83e-102

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: 301.69  E-value: 3.83e-102
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446679112   1 MKKVLFLGDPGIDDSLAIMYGLLHPDIDIVGVVTGYGNVTQEKATSNAAYLLQMAGREDIPVINGAKIPLSGDITTYyPE 80
Cdd:COG1957    2 MRKVIIDTDPGIDDALALLLALASPEIDLLGITTVAGNVPLEQTTRNALKLLELAGRTDVPVAAGAARPLVRPLVTA-EH 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446679112  81 IHGTDGLGPIK-PPKTFSPNIKPFCTFF-DLLEKYKGELIIVDAGRSTTLATAFILEKPMMKYVKEYYIMGGAFLMPGNV 158
Cdd:COG1957   81 VHGEDGLGGVDlPEPTRPPEPEHAVDFIiETLRAAPGEVTLVALGPLTNLALALRKDPELAERIKRIVIMGGAFFVPGNV 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446679112 159 TPVAEANFHGDPIASQLVMQNAKNVTLVPLNVTSEAIITPEMVKYItKHSKTSFNKLIEPIFTYYYKAYRKlNPKIKGSP 238
Cdd:COG1957  161 TPVAEFNIYVDPEAAKIVFASGIPITMVGLDVTHQALLTPEDLARL-AALGTPLGRFLADLLDFYLDFYRE-RYGLDGCP 238

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446679112 239 VHDVVTMMVAANPSLLDYVYRRVDVDTAG-IAKGESIADFRPQPDAKAlkNwVRIGWSLHYKKFLEDFVKFMT 310
Cdd:COG1957  239 LHDPLAVAYLLDPELFTTRPAPVDVETDGeLTRGQTVVDWRGVTGRPP--N-ARVALDVDAERFLDLLLERLA 308
nuc_hydro_CaPnhB cd02650
NH_hydro_CaPnhB: A subgroup of nucleoside hydrolases similar to Corynebacterium ammoniagenes ...
 3-289 2.01e-76

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: 236.02  E-value: 2.01e-76
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446679112   3 KVLFLGDPGIDDSLAIMYGLLHPDIDIVGVVTGYGNVTQEKATSNAAYLLQMAGREDIPVINGAKIPLSGDITTYYPEIH 82
Cdd:cd02650    1 KLILDTDPGIDDAMALAYALAHPDVDLIGVTTVYGNVTIETATRNALALLELFGRPDVPVAEGAAKPLTRPPFRIATFVH 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446679112  83 GTDGLGPIKPPKTFSPNIKPFCTFF--DLLEKYKGELIIVDAGRSTTLATAFILEKPMMKYVKEYYIMGGAFLMPGNVTP 160
Cdd:cd02650   81 GDNGLGDVELPAPPRQPEDESAADFliELANEYPGELTLVAVGPLTNLALALARDPDFAKLVKQVVVMGGAFTVPGNVTP 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446679112 161 VAEANFHGDPIASQLVMQNAKNVTLVPLNVTSEAIITPEMVKYItKHSKTSFNKLIEPIFTYYYKAYRKlNPKIKGSPVH 240
Cdd:cd02650  161 AAEANIHGDPEAADIVFTAGADLTMVGLDVTTQTLLTREDLDEL-RDSGGKAGQFLADMLDYYIDFYQE-SPGLRGCALH 238

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*....
gi 446679112 241 DVVTMMVAANPSLLDYVYRRVDVDTAGIAKGESIADFRPQPDAKALKNW 289
Cdd:cd02650  239 DPLAVAAAVDPSLFTTREGVVRVETEGPTRGRTIGDRDGRRFWDSSPNA 287
IU_nuc_hydro pfam01156
Inosine-uridine preferring nucleoside hydrolase;
9-303 1.58e-71

Inosine-uridine preferring nucleoside hydrolase;


Pssm-ID: 460086 [Multi-domain]  Cd Length: 253  Bit Score: 221.70  E-value: 1.58e-71
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446679112    9 DPGIDDSLAIMYGLLHPDIDIVGVVTGYGNVTQEKATSNAAYLLQMAGREDIPVINGAKIPLSGDITtyypeihgtdglg 88
Cdd:pfam01156   6 DPGIDDALALLLALASPEIELLGITTVAGNVSLEQTTRNALRLLELGGRDDIPVYAGEAIREPGEVT------------- 72

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446679112   89 pikppktfspnikpfctffdllekykgeliIVDAGRSTTLATAFILEKPMMKYVKEYYIMGGAFLMPGNVTPVAEANFHG 168
Cdd:pfam01156  73 ------------------------------LVATGPLTNLALALRLDPELAKKIKELVIMGGAFGVRGNVTPAAEFNIFV 122

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446679112  169 DPIASQLVMQNAKNVTLVPLNVTSEAIITPEMVKYItKHSKTSFNKLIEPIFTYYYKAYRKLNPkIKGSPVHDVVTMMVA 248
Cdd:pfam01156 123 DPEAAKIVFTSGLPITMVPLDVTHQALLTPEDLERL-AALGTPLGRFLADLLRFYAEFYRERFG-IDGPPLHDPLAVAVA 200

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 446679112  249 ANPSLLDYVYRRVDVDTAG-IAKGESIADFRPQPDAKALknwVRIGWSLHYKKFLE 303
Cdd:pfam01156 201 LDPELFTTRRLNVDVETTGgLTRGQTVVDDRGGWGKPPN---VRVATDVDVDRFWE 253
nuc_hydro_IU_UC_XIUA cd02651
nuc_hydro_IU_UC_XIUA: inosine-uridine preferring, ...
 9-285 1.10e-63

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: 203.16  E-value: 1.10e-63
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446679112   9 DPGIDDSLAIMYGLLHPDIDIVGVVTGYGNVTQEKATSNAAYLLQMAGREDIPVINGAKIPLSGDITTyYPEIHGTDGLG 88
Cdd:cd02651    7 DPGHDDAVAILLALFHPELDLLGITTVAGNVPLEKTTRNALKLLTLLGRTDVPVAAGAARPLVRPLIT-ASDIHGESGLD 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446679112  89 PIK-PPKTFSPNIKPFCTF-FDLLEKYKGELIIVDAGRSTTLATAFILEKPMMKYVKEYYIMGGAFLMpGNVTPVAEANF 166
Cdd:cd02651   86 GADlPPPPRRPEDIHAVDAiIDTLRASPEPITLVATGPLTNIALLLRKYPELAERIKEIVLMGGALGR-GNITPAAEFNI 164

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446679112 167 HGDPIASQLVMQNAKNVTLVPLNVTSEAIITPEMVKYItKHSKTSFNKLIEPIFTYYYKAYRKLnpKIKGSPVHDVVTMM 246
Cdd:cd02651  165 FVDPEAAKIVFNSGIPITMVPLDVTHKALATPEVIERI-RALGNPVGKMLAELLDFFAETYGSA--FTEGPPLHDPCAVA 241

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|
gi 446679112 247 VAANPSLLDYVYRRVDVDTAG-IAKGESIADFRPQPDAKA 285
Cdd:cd02651  242 YLLDPELFTTKRANVDVETEGeLTRGRTVVDLRGVTGRPA 281
PLN02717 PLN02717
uridine nucleosidase
 2-295 4.23e-60

uridine nucleosidase


Pssm-ID: 178319 [Multi-domain]  Cd Length: 316  Bit Score: 194.44  E-value: 4.23e-60
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446679112   2 KKVLFLGDPGIDDSLAIMYGLLHPDIDIVGVVTGYGNVTQEKATSNAAYLLQMAGREDIPVINGAKIPLSGDITTYYPE- 80
Cdd:PLN02717   1 KKLIIDTDPGIDDAMAILMALRSPEVEVIGLTTIFGNVTTKLATRNALHLLEMAGRPDVPVAEGSHEPLKGGTKPRIADf 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446679112  81 IHGTDGLGPIKPPKtfsPNIKPF----CTFF-DLLEKYKGELIIVDAGRSTTLATAFILEKPMMKYVKEYYIMGGAFLMP 155
Cdd:PLN02717  81 VHGSDGLGNTNLPP---PKGKKIeksaAEFLvEKVSEYPGEVTVVALGPLTNLALAIKLDPSFAKKVGQIVVLGGAFFVN 157

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446679112 156 GNVTPVAEANFHGDPIASQLVMQNAKNVTLVPLNVTSEAIIT-PEMVKYitKHSKTSFNKLIEPIfTYYYKAYRKLNPKI 234
Cdd:PLN02717 158 GNVNPAAEANIFGDPEAADIVFTSGADITVVGINVTTQVVLTdADLEEL--RDSKGKYAQFLCDI-CKFYRDWHRKSYGI 234

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446679112 235 KGSPVHDVVTMMVAANPSLLDYVYRRVDVDTAGIAKGESIADfrpqpdaKALKNWVRI-GWS 295
Cdd:PLN02717 235 DGIYLHDPTALLAAVRPSLFTYKEGVVRVETEGICRGLTLFD-------NGLKRWNGEnAWT 289
nuc_hydro_3 cd02653
NH_3: A subgroup of nucleoside hydrolases. This group contains eukaryotic and bacterial ...
 9-276 1.35e-53

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: 177.57  E-value: 1.35e-53
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446679112   9 DPGIDDSLAIMYGLLHPDIDIVGVVTGYGNVTQEKATSNAAYLLQMAGREDIPVINGAKIPLSGDITTyYPEIHGTDGLG 88
Cdd:cd02653    7 DPGIDDALALLYLLASPDLDVVGITTTAGNVPVEQVAANALGVLELLGRTDIPVYLGADKPLAGPLTT-AQDTHGPDGLG 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446679112  89 --PIKPPKTFSPNIKPFCTFFDLLEKYKgELIIVDAGRSTTLATAFILEKPMMKYVKEYYIMGGAFLMPGNVTPVAEANF 166
Cdd:cd02653   86 yaELPASTRTLSDESAAQAWVDLARAHP-DLIGLATGPLTNLALALREEPELPRLLRRLVIMGGAFNSRGNTSPVAEWNY 164

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446679112 167 HGDPIASQLVMQN----AKNVTLVPLNVTSEAIITPEMVKYItKHSKTSFNKLIEPIFTYYYKAYRKLNpKIKGSPVHDV 242
Cdd:cd02653  165 WVDPEAAKEVLAAfgghPVRPTICGLDVTRAVVLTPNLLERL-ARAKDSVGAFIEDALRFYFEFHWAYG-HGYGAVIHDP 242

                        250       260       270
                 ....*....|....*....|....*....|....
gi 446679112 243 VTMMVAANPSLLDYVYRRVDVDTAGIAKGESIAD 276
Cdd:cd02653  243 LAAAVALNPNLARGRPAYVDVECTGVLTGQTVVD 276
nuc_hydro_CeIAG cd02649
nuc_hydro_CeIAG: Nucleoside hydrolases similar to the inosine-adenosine-guanosine-preferring ...
 9-267 1.69e-45

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: 156.27  E-value: 1.69e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446679112   9 DPGIDDSLAIMYGLLHPDIDIVGVVTGYGNVTQEKATSNAAYLLQMAGREDIPVINGAKIPLSGD-ITTYYpeIHGTDGL 87
Cdd:cd02649    8 DCGGDDAWALLMALASPNVEVLAITCVHGNTNVEQVVKNALRVLEACGRRDIPVYRGASKPLLGPgPTAAY--FHGKDGF 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446679112  88 G--PIKPPKTFSPNIKPFCT--FFDLLEKYKGELIIVDAGRSTTLATAFILEKPMMKYVKEYYIMGGAFLMPGNVTPVAE 163
Cdd:cd02649   86 GdvGFPEPKDELELQKEHAVdaIIRLVREYPGEITLVALGPLTNLALAYRLDPSLPQKIKRLYIMGGNREGVGNTTPAAE 165

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446679112 164 ANFHGDPIASQLVMQNAK-NVTLVPLNVTSEAIITP-EMVKYitKHSKTSFNKLIEPIFTYYYKAYRKlNPKIKGSPVHD 241
Cdd:cd02649  166 FNFHVDPEAAHIVLNSFGcPITIVPWETTLLAFPLDwEFEDK--WANRLEKALFAESLNRREYAFASE-GLGGDGWVPCD 242

                        250       260
                 ....*....|....*....|....*..
gi 446679112 242 VVTMMVAANPSLLDYVYR-RVDVDTAG 267
Cdd:cd02649  243 ALAVAAALDPSIITRRLTyAVDVELHG 269
rihA PRK10443
ribonucleoside hydrolase 1; Provisional
 1-277 5.96e-37

ribonucleoside hydrolase 1; Provisional


Pssm-ID: 182465 [Multi-domain]  Cd Length: 311  Bit Score: 134.02  E-value: 5.96e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446679112   1 MKKVLFLGDPGIDDSLAIMYGLLHPDIDIVGVVTGYGNVTQEKATSNAAYLLQMAGREDIPVINGAKIPLSGDITTyYPE 80
Cdd:PRK10443   2 ALPIILDCDPGHDDAIALVLALASPELDVKAVTTSAGNQTPEKTLRNALRMLTLLNRTDIPVAGGAVKPLMRELII-ADN 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446679112  81 IHGTDGL-GPIKPPKTFSPNIkpfCTFFDLLEKYKGE----LIIVDAGRSTTLATaFILEKPMMKY-VKEYYIMGGAFLM 154
Cdd:PRK10443  81 VHGESGLdGPALPEPTFAPQN---CTAVELMAKTLREsaepVTLVSTGPQTNVAL-LLASHPELHSkIARIVIMGGAMGL 156

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446679112 155 pGNVTPVAEANFHGDPIASQLVMQNAKNVTLVPLNVTSEAIITP---EMVKYITKHSKTSFNKLIEpIFTYYYKayrklN 231
Cdd:PRK10443 157 -GNWTPAAEFNIYVDPEAAEIVFQSGIPIVMAGLDVTHKAQIMDediERIRAIGNPVATIVAELLD-FFMEYHK-----D 229

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*....
gi 446679112 232 PK--IKGSPVHDVVTMMVAANPSLLDYVYRRVDVDTAG-IAKGESIADF 277
Cdd:PRK10443 230 EKwgFVGAPLHDPCTIAWLLKPELFTTVERWVGVETQGeYTQGMTVVDY 278
PRK10768 PRK10768
ribonucleoside hydrolase RihC; Provisional
 9-290 1.10e-34

ribonucleoside hydrolase RihC; Provisional


Pssm-ID: 182713 [Multi-domain]  Cd Length: 304  Bit Score: 127.72  E-value: 1.10e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446679112   9 DPGIDDSLAIMYGLLHPDIDIVGVVTGYGNVTQEKATSNAAYLLQMAGrEDIPVINGAKIPLsgdITTYY--PEIHGTDG 86
Cdd:PRK10768  10 DPGIDDAVAIAAALFAPELDLKLITTVAGNVSVEKTTRNALKLLHFFN-SDVPVAQGAAKPL---VRPLRdaASVHGESG 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446679112  87 LG--PIKPPKTFSPNIKPFCTFFDLLEKYKGELIIVDAGRSTTLATAFILEKPMMKYVKEYYIMGGAfLMPGNVTPVAEA 164
Cdd:PRK10768  86 MEgyDFPEHTRKPLSIPAVEAMRDALMNAPEPVTLVAIGPLTNIALLLSTYPEVKPYIKRIVLMGGS-AGRGNVTPNAEF 164

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446679112 165 NFHGDPIASQLVMQNAKNVTLVPLNVTSEAIITPEMVKYITKHSKTSfnKLIEPIFTYYYKAYRKlnpkiKGSPVHDVVT 244
Cdd:PRK10768 165 NIAVDPEAAAIVFRSGIPIVMCGLDVTNQALLTPDYLATLPELNRTG--KMLHALFSHYRSGSMQ-----TGLRMHDVCA 237

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 446679112 245 MMVAANPSLLDYVYRRVDVDTAG-IAKGESIADFRP------------QPDAKALKNWV 290
Cdd:PRK10768 238 IAYLLRPELFTLKPCFVDVETQGeFTAGATVVDIDGrlgkpanaqvalDIDVDGFQKWF 296
rihB PRK09955
ribosylpyrimidine nucleosidase;
2-284 1.82e-29

ribosylpyrimidine nucleosidase;


Pssm-ID: 182166 [Multi-domain]  Cd Length: 313  Bit Score: 114.27  E-value: 1.82e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446679112   2 KKVLFLGDPGIDDSLAIMYGLLHPDIDIVGVVTGYGNVTQEKATSNA---AYLLQMagreDIPVINGAKIPLSGDiTTYY 78
Cdd:PRK09955   4 RKIILDCDPGHDDAIAMMMAAKHPAIDLLGITIVAGNQTLDKTLINGlnvCQKLEI----NVPVYAGMPQPIMRQ-QIVA 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446679112  79 PEIHGTDGL-GPIKPPKTFSPNIKPFCTF-FDLLEKYKGELIIVDAGRSTTLATAFILEKPMMKYVKEYYIMGGAFlMPG 156
Cdd:PRK09955  79 DNIHGETGLdGPVFEPLTRQAESTHAVKYiIDTLMASDGDITLVPVGPLSNIAVAMRMQPAILPKIREIVLMGGAY-GTG 157

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446679112 157 NVTPVAEANFHGDPIASQLVMQNAKNVTLVPLNVTSEAIITPEMVKYITKHSKTSfNKLIEPIFTYYYKAYRKlNPKIKG 236
Cdd:PRK09955 158 NFTPSAEFNIFADPEAARVVFTSGVPLVMMGLDLTNQTVCTPDVIARMERAGGPA-GELFSDIMNFTLKTQFE-NYGLAG 235

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|...
gi 446679112 237 SPVHDVVTMMVAANPSLLDYVYRRVDVD-TAGIAKGESIAD----FRPQPDAK 284
Cdd:PRK09955 236 GPVHDATCIGYLINPDGIKTQEMYVEVDvNSGPCYGRTVCDelgvLGKPANTK 288
nuc_hydro_CjNH cd02654
nuc_hydro_CjNH. Nucleoside hydrolases similar to Campylobacter jejuni nucleoside hydrolase. ...
 6-290 9.10e-25

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: 101.48  E-value: 9.10e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446679112   6 FLGDPGIDDSLAIMYGLLHPDIDIVGVVTGYGNVTQEKATSNAAYLLQMAGREDIPVINGAKIPLSGDITTY------YP 79
Cdd:cd02654    8 IAMGRDTDDGLALALLLWSPEVELLGLSAVSGNCWLSAVTYNVLRMLELAGADAIPVYAGANTPLGRTNRAFhaweslYG 87

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446679112  80 EIHGTDGLGP-IKPPKTFSPNIK----PFCTFF-DLLEKYKGELIIVDAGRSTTLATAFILEKPMMKYVKEYYIMGGAFL 153
Cdd:cd02654   88 AYLWQGAWSPeYSDMYTNASIIRnasiPAALFMiEMVRKHPHEVSIVAAGPLTNLALALRIDPDFAPLAKELVIMGGYLD 167

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446679112 154 MPGN-VTPV--AEANFHGDPIASQLVMQNAKNVTLVPLNVTSEAIITPEMVKYITKHSKTSFNKLIEPIftYYYKAYRKl 230
Cdd:cd02654  168 DIGEfVNRHyaSDFNLIMDPEAASIVLTAPWKSITIPGNVTNRTCLTPEQIKADDPLRDFIRETLDLPI--DYAKEFVG- 244

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446679112 231 npKIKGSPVHDVVTMMVAANPSLLDYVY-RRVDVDTAGIAKGESI--ADFRPQPDAKALKNWV 290
Cdd:cd02654  245 --TGDGLPMWDELASAVALDPELATSSEtFYIDVQTDSDGGGQLIwpEDLLLAKGLRPYHVKV 305
nuc_hydro_1 cd02648
NH_1: A subgroup of nucleoside hydrolases. This group contains fungal proteins similar to ...
 9-193 1.20e-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: 90.71  E-value: 1.20e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446679112   9 DPGIDDSLAIMYGLLHPD-IDIVGVVTGYGNVTQEKATSNA---AYLLQ----------------MAGREDIPVINGAKI 68
Cdd:cd02648    9 DPGVDDVLAILLALSSPEeVDVALISLTFGNTTLDHALRNVlrlFHVLErerawratpgvryrafSADAEKPIVASGSDQ 88

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446679112  69 PLSGD--ITTYYpeiHGTDGLGPI--KPPKTFSPNIKP--FCTFFDLLEKYKGELI-------------IVDAGRSTTLA 129
Cdd:cd02648   89 PLEGErlTASYF---HGRDGLSGVhwLHPDFTPVETWIpeIVAPLTPSDKPAYDVIldilreepdhtvtIAALGPLTNLA 165

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446679112 130 TAFILEKPMMKYVKEYYIMGGAFLMPGNVTPVAEANFHGDPIASQLVMQNA----------KNVTLVPLNVTSE 193
Cdd:cd02648  166 AAARKDPETFAKVGEVVVMGGAIDVPGNTSPVAEFNCFADPYAAAVVIDEPpstapearrkLPLQVFPLDITTG 239
nuc_hydro_TvIAG cd02647
nuc_hydro_ TvIAG: Nucleoside hydrolases similar to the Inosine-adenosine-guanosine-preferring ...
 2-288 1.58e-17

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: 81.31  E-value: 1.58e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446679112   2 KKVLFLGDPGIDDSLAIMYGLLHPDIDIVGVVTGY--GNVTQEKATSNAAYLLQMAGRED-IPVINGAKIPL-------- 70
Cdd:cd02647    1 KNVIFDHDGNVDDLVALLLLLKNEKVDLKGIGVSGidADCYVEPAVSVTRKLIDRLGQRDaIPVGKGGSRAVnpfprswr 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446679112  71 --SGDITTYYPEIHGTDGLGPIKPPKTfspnikpfcTFFDLLEKYKGEL---IIVDAGRSTTLATAFILEKPMMKYVKEY 145
Cdd:cd02647   81 rdAAFSVDHLPILNERYTVETPLAEET---------AQLVLIEKIKASLepvTLLVTGPLTNLARALDSDPDISSNIEEV 151

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446679112 146 YIMGGAFLMPGNV-----TPVAEANFHGDPIASQLVMQNAKNVTLVPLNVTSEAIITPEMVKYITKHsktsFNKLIEPIF 220
Cdd:cd02647  152 YIMGGGVDAPGNVftppsNGTAEFNIFWDPLAAKTVFDSGLKITLVPLDATNTVPLTREFLETDRQR----FAAQRLPAS 227

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446679112 221 TYYYKAYRKLNPKIKGSPVH--DVVTMMVAANPSLLDYVYRRV-DVDTAGIAKGESIADFRPQPDAKALKN 288
Cdd:cd02647  228 DLAGQGYALVKPLEFNSTYYmwDVLTTLVLGAKEVDNTKESLIlEVDTDGLSAGQTVTSPNGRPLTLVTSN 298
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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