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Conserved domains on  [gi|488943555|ref|WP_002854630|]
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MULTISPECIES: nucleoside hydrolase [Campylobacter]

Protein Classification

nucleoside hydrolase( domain architecture ID 2730)

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.-
Gene Ontology:  GO:0016799
SCOP:  4000751

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
nuc_hydro super family cl00226
nuc_hydro: Nucleoside hydrolases. Nucleoside hydrolases cleave the N-glycosidic bond in ...
 2-317 2.33e-127

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.


The actual alignment was detected with superfamily member cd02654:

Pssm-ID: 469670 [Multi-domain]  Cd Length: 318  Bit Score: 366.88  E-value: 2.33e-127
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488943555   2 RLILDTDIGNaiaGANTDDGLALALILASKEIKLEMLSTICGNVP-SLVAYSVAKDLFKRLNLNIPVYLGANEALKEPSK 80
Cdd:cd02654    1 KVILDNDIAM---GRDTDDGLALALLLWSPEVELLGLSAVSGNCWlSAVTYNVLRMLELAGADAIPVYAGANTPLGRTNR 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488943555  81 AWRqrldeSVKNFKLEYLWENIKSPEIL---------ENINPDAIFKMGELVGKNPKEISICAIGPLTNIAMAMKIFKDF 151
Cdd:cd02654   78 AFH-----AWESLYGAYLWQGAWSPEYSdmytnasiiRNASIPAALFMIEMVRKHPHEVSIVAAGPLTNLALALRIDPDF 152

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488943555 152 DINLKELFIMGG------SFDMPYYTKDTNFGFDPEAASIVLNSRAKITLVPYNVTMQTLLTHEDLKelqAKNILCDFIV 225
Cdd:cd02654  153 APLAKELVIMGGylddigEFVNRHYASDFNLIMDPEAASIVLTAPWKSITIPGNVTNRTCLTPEQIK---ADDPLRDFIR 229

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488943555 226 ETLGVWIDYASKTRGTK-GTWIHDALTIAYALDSSIADFDEC-YADVICDSSLARGMSWRCFKEPKMSMGmdlstKNCVK 303
Cdd:cd02654  230 ETLDLPIDYAKEFVGTGdGLPMWDELASAVALDPELATSSETfYIDVQTDSDGGGQLIWPEDLLLAKGLR-----PYHVK 304

                        330
                 ....*....|....
gi 488943555 304 ILKNVDNAKLLKLI 317
Cdd:cd02654  305 VITAVDVAAFLNLI 318
 
Name Accession Description Interval E-value
nuc_hydro_CjNH cd02654
nuc_hydro_CjNH. Nucleoside hydrolases similar to Campylobacter jejuni nucleoside hydrolase. ...
 2-317 2.33e-127

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: 366.88  E-value: 2.33e-127
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488943555   2 RLILDTDIGNaiaGANTDDGLALALILASKEIKLEMLSTICGNVP-SLVAYSVAKDLFKRLNLNIPVYLGANEALKEPSK 80
Cdd:cd02654    1 KVILDNDIAM---GRDTDDGLALALLLWSPEVELLGLSAVSGNCWlSAVTYNVLRMLELAGADAIPVYAGANTPLGRTNR 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488943555  81 AWRqrldeSVKNFKLEYLWENIKSPEIL---------ENINPDAIFKMGELVGKNPKEISICAIGPLTNIAMAMKIFKDF 151
Cdd:cd02654   78 AFH-----AWESLYGAYLWQGAWSPEYSdmytnasiiRNASIPAALFMIEMVRKHPHEVSIVAAGPLTNLALALRIDPDF 152

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488943555 152 DINLKELFIMGG------SFDMPYYTKDTNFGFDPEAASIVLNSRAKITLVPYNVTMQTLLTHEDLKelqAKNILCDFIV 225
Cdd:cd02654  153 APLAKELVIMGGylddigEFVNRHYASDFNLIMDPEAASIVLTAPWKSITIPGNVTNRTCLTPEQIK---ADDPLRDFIR 229

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488943555 226 ETLGVWIDYASKTRGTK-GTWIHDALTIAYALDSSIADFDEC-YADVICDSSLARGMSWRCFKEPKMSMGmdlstKNCVK 303
Cdd:cd02654  230 ETLDLPIDYAKEFVGTGdGLPMWDELASAVALDPELATSSETfYIDVQTDSDGGGQLIWPEDLLLAKGLR-----PYHVK 304

                        330
                 ....*....|....
gi 488943555 304 ILKNVDNAKLLKLI 317
Cdd:cd02654  305 VITAVDVAAFLNLI 318
URH1 COG1957
Inosine-uridine nucleoside N-ribohydrolase [Nucleotide transport and metabolism]; ...
 1-323 1.70e-81

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: 250.07  E-value: 1.70e-81
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488943555   1 MRLILDTDIGnaiaganTDDGLALALILASKEIKLEMLSTICGNVPSLVAYSVAKDLFKRLNL-NIPVYLGANEALKEPS 79
Cdd:COG1957    3 RKVIIDTDPG-------IDDALALLLALASPEIDLLGITTVAGNVPLEQTTRNALKLLELAGRtDVPVAAGAARPLVRPL 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488943555  80 KAWRQRLDESvknfkleyLWENIKSPEILENINP-DAIFKMGELVGKNPKEISICAIGPLTNIAMAMKIFKDFDINLKEL 158
Cdd:COG1957   76 VTAEHVHGED--------GLGGVDLPEPTRPPEPeHAVDFIIETLRAAPGEVTLVALGPLTNLALALRKDPELAERIKRI 147

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488943555 159 FIMGGSFDMPYYT---KDTNFGFDPEAASIVLNSRAKITLVPYNVTMQTLLTHEDLKELQA-KNILCDFIVETLGVWIDY 234
Cdd:COG1957  148 VIMGGAFFVPGNVtpvAEFNIYVDPEAAKIVFASGIPITMVGLDVTHQALLTPEDLARLAAlGTPLGRFLADLLDFYLDF 227

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488943555 235 ASKTRGTKGTWIHDALTIAYALDSSIADFDECYADVICDSSLARGMS---WRcfkepkmsmGMDLSTKNcVKILKNVDNA 311
Cdd:COG1957  228 YRERYGLDGCPLHDPLAVAYLLDPELFTTRPAPVDVETDGELTRGQTvvdWR---------GVTGRPPN-ARVALDVDAE 297

                        330
                 ....*....|..
gi 488943555 312 KLLKLIKERLLK 323
Cdd:COG1957  298 RFLDLLLERLAR 309
IU_nuc_hydro pfam01156
Inosine-uridine preferring nucleoside hydrolase;
3-315 1.18e-61

Inosine-uridine preferring nucleoside hydrolase;


Pssm-ID: 460086 [Multi-domain]  Cd Length: 253  Bit Score: 197.05  E-value: 1.18e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488943555    3 LILDTDIGnaiaganTDDGLALALILASKEIKLEMLSTICGNVPSLVAYSVAKDLFKRLNLN-IPVYLGanEALKEPska 81
Cdd:pfam01156   1 VIIDTDPG-------IDDALALLLALASPEIELLGITTVAGNVSLEQTTRNALRLLELGGRDdIPVYAG--EAIREP--- 68

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488943555   82 wrqrldesvknfkleylwenikspeileninpdaifkmgelvgknpKEISICAIGPLTNIAMAMKIFKDFDINLKELFIM 161
Cdd:pfam01156  69 ----------------------------------------------GEVTLVATGPLTNLALALRLDPELAKKIKELVIM 102

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488943555  162 GGSFDMPYYTK---DTNFGFDPEAASIVLNSRAKITLVPYNVTMQTLLTHEDLKELQA-KNILCDFIVETLGVWIDYASK 237
Cdd:pfam01156 103 GGAFGVRGNVTpaaEFNIFVDPEAAKIVFTSGLPITMVPLDVTHQALLTPEDLERLAAlGTPLGRFLADLLRFYAEFYRE 182

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 488943555  238 TRGTKGTWIHDALTIAYALDSSIADFDECYADVICDSSLARGMSWrcfkepkMSMGMDLSTKNCVKILKNVDNAKLLK 315
Cdd:pfam01156 183 RFGIDGPPLHDPLAVAVALDPELFTTRRLNVDVETTGGLTRGQTV-------VDDRGGWGKPPNVRVATDVDVDRFWE 253
PRK10768 PRK10768
ribonucleoside hydrolase RihC; Provisional
 3-279 1.07e-32

ribonucleoside hydrolase RihC; Provisional


Pssm-ID: 182713 [Multi-domain]  Cd Length: 304  Bit Score: 123.10  E-value: 1.07e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488943555   3 LILDTDIGnaiaganTDDGLALALILASKEIKLEMLSTICGNVpslvaySVAK------DLFKRLNLNIPVYLGANEALK 76
Cdd:PRK10768   5 IILDTDPG-------IDDAVAIAAALFAPELDLKLITTVAGNV------SVEKttrnalKLLHFFNSDVPVAQGAAKPLV 71

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488943555  77 EPSKAWRQRLDESVK---NFkleylweniksPEILENINP-DAIFKMGELVGKNPKEISICAIGPLTNIAMAMKIFKDFD 152
Cdd:PRK10768  72 RPLRDAASVHGESGMegyDF-----------PEHTRKPLSiPAVEAMRDALMNAPEPVTLVAIGPLTNIALLLSTYPEVK 140

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488943555 153 INLKELFIMGGSFDMPYYT--KDTNFGFDPEAASIVLNSRAKITLVPYNVTMQTLLTHEDLKELQAKNilcdfivETLGV 230
Cdd:PRK10768 141 PYIKRIVLMGGSAGRGNVTpnAEFNIAVDPEAAAIVFRSGIPIVMCGLDVTNQALLTPDYLATLPELN-------RTGKM 213

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|..
gi 488943555 231 WIDYASKTRG---TKGTWIHDALTIAYALDSSIADFDECYADVICDSSLARG 279
Cdd:PRK10768 214 LHALFSHYRSgsmQTGLRMHDVCAIAYLLRPELFTLKPCFVDVETQGEFTAG 265
 
Name Accession Description Interval E-value
nuc_hydro_CjNH cd02654
nuc_hydro_CjNH. Nucleoside hydrolases similar to Campylobacter jejuni nucleoside hydrolase. ...
 2-317 2.33e-127

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: 366.88  E-value: 2.33e-127
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488943555   2 RLILDTDIGNaiaGANTDDGLALALILASKEIKLEMLSTICGNVP-SLVAYSVAKDLFKRLNLNIPVYLGANEALKEPSK 80
Cdd:cd02654    1 KVILDNDIAM---GRDTDDGLALALLLWSPEVELLGLSAVSGNCWlSAVTYNVLRMLELAGADAIPVYAGANTPLGRTNR 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488943555  81 AWRqrldeSVKNFKLEYLWENIKSPEIL---------ENINPDAIFKMGELVGKNPKEISICAIGPLTNIAMAMKIFKDF 151
Cdd:cd02654   78 AFH-----AWESLYGAYLWQGAWSPEYSdmytnasiiRNASIPAALFMIEMVRKHPHEVSIVAAGPLTNLALALRIDPDF 152

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488943555 152 DINLKELFIMGG------SFDMPYYTKDTNFGFDPEAASIVLNSRAKITLVPYNVTMQTLLTHEDLKelqAKNILCDFIV 225
Cdd:cd02654  153 APLAKELVIMGGylddigEFVNRHYASDFNLIMDPEAASIVLTAPWKSITIPGNVTNRTCLTPEQIK---ADDPLRDFIR 229

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488943555 226 ETLGVWIDYASKTRGTK-GTWIHDALTIAYALDSSIADFDEC-YADVICDSSLARGMSWRCFKEPKMSMGmdlstKNCVK 303
Cdd:cd02654  230 ETLDLPIDYAKEFVGTGdGLPMWDELASAVALDPELATSSETfYIDVQTDSDGGGQLIWPEDLLLAKGLR-----PYHVK 304

                        330
                 ....*....|....
gi 488943555 304 ILKNVDNAKLLKLI 317
Cdd:cd02654  305 VITAVDVAAFLNLI 318
nuc_hydro cd00455
nuc_hydro: Nucleoside hydrolases. Nucleoside hydrolases cleave the N-glycosidic bond in ...
 3-317 1.13e-90

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: 272.67  E-value: 1.13e-90
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488943555   3 LILDTDIGnaiaganTDDGLALALILASKEIKLEMLSTICGNVP-SLVAYSVAKDLFKRLNLNIPVYLGANEALKEPSKA 81
Cdd:cd00455    1 VILDTDPG-------IDDAFALMYALLHPEIELVGIVATYGNVTlEQATQNAAYLLELLGRLDIPVYAGATRPLTGEIPA 73

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488943555  82 WRQRLDESVKNfkleylweNIKSPEILENINPDAIFKMGELVGKNPKEISICAIGPLTNIAMAMKIFKDFDINLKELFIM 161
Cdd:cd00455   74 AYPEIHGEGGL--------GLPIPPIIEADDPEAVQLLIDLIRKYPDEITIVALGPLTNLAMAFILDPDIKDRVKEIVIM 145

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488943555 162 GGSFDMP---YYTKDTNFGFDPEAASIVLNSRAKITLVPYNVTMQTLLTHEdlkelqakniLCDFIVET---LGVWIDYA 235
Cdd:cd00455  146 GGAFLVPgnvTPVAEANFYGDPEAANIVFNSAKNLTIVPLDVTNQAVLTPP----------MVERIFEQgtsIGLLIKPM 215

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488943555 236 SKTRGT-------KGTWIHDALTIAYALDSSIADFDECYADVICDsSLARGMSWRCFKEPkmsmgmdlSTKNCVKILKNV 308
Cdd:cd00455  216 IDYYYKayqkpgiEGSPIHDPLAVAYLLNPSMFDYSKVPVDVDTD-GLTRGQTIADFREN--------PGNGVTRVAVNL 286


                 ....*....
gi 488943555 309 DNAKLLKLI 317
Cdd:cd00455  287 DYPDFIELI 295
URH1 COG1957
Inosine-uridine nucleoside N-ribohydrolase [Nucleotide transport and metabolism]; ...
 1-323 1.70e-81

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: 250.07  E-value: 1.70e-81
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488943555   1 MRLILDTDIGnaiaganTDDGLALALILASKEIKLEMLSTICGNVPSLVAYSVAKDLFKRLNL-NIPVYLGANEALKEPS 79
Cdd:COG1957    3 RKVIIDTDPG-------IDDALALLLALASPEIDLLGITTVAGNVPLEQTTRNALKLLELAGRtDVPVAAGAARPLVRPL 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488943555  80 KAWRQRLDESvknfkleyLWENIKSPEILENINP-DAIFKMGELVGKNPKEISICAIGPLTNIAMAMKIFKDFDINLKEL 158
Cdd:COG1957   76 VTAEHVHGED--------GLGGVDLPEPTRPPEPeHAVDFIIETLRAAPGEVTLVALGPLTNLALALRKDPELAERIKRI 147

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488943555 159 FIMGGSFDMPYYT---KDTNFGFDPEAASIVLNSRAKITLVPYNVTMQTLLTHEDLKELQA-KNILCDFIVETLGVWIDY 234
Cdd:COG1957  148 VIMGGAFFVPGNVtpvAEFNIYVDPEAAKIVFASGIPITMVGLDVTHQALLTPEDLARLAAlGTPLGRFLADLLDFYLDF 227

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488943555 235 ASKTRGTKGTWIHDALTIAYALDSSIADFDECYADVICDSSLARGMS---WRcfkepkmsmGMDLSTKNcVKILKNVDNA 311
Cdd:COG1957  228 YRERYGLDGCPLHDPLAVAYLLDPELFTTRPAPVDVETDGELTRGQTvvdWR---------GVTGRPPN-ARVALDVDAE 297

                        330
                 ....*....|..
gi 488943555 312 KLLKLIKERLLK 323
Cdd:COG1957  298 RFLDLLLERLAR 309
IU_nuc_hydro pfam01156
Inosine-uridine preferring nucleoside hydrolase;
3-315 1.18e-61

Inosine-uridine preferring nucleoside hydrolase;


Pssm-ID: 460086 [Multi-domain]  Cd Length: 253  Bit Score: 197.05  E-value: 1.18e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488943555    3 LILDTDIGnaiaganTDDGLALALILASKEIKLEMLSTICGNVPSLVAYSVAKDLFKRLNLN-IPVYLGanEALKEPska 81
Cdd:pfam01156   1 VIIDTDPG-------IDDALALLLALASPEIELLGITTVAGNVSLEQTTRNALRLLELGGRDdIPVYAG--EAIREP--- 68

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488943555   82 wrqrldesvknfkleylwenikspeileninpdaifkmgelvgknpKEISICAIGPLTNIAMAMKIFKDFDINLKELFIM 161
Cdd:pfam01156  69 ----------------------------------------------GEVTLVATGPLTNLALALRLDPELAKKIKELVIM 102

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488943555  162 GGSFDMPYYTK---DTNFGFDPEAASIVLNSRAKITLVPYNVTMQTLLTHEDLKELQA-KNILCDFIVETLGVWIDYASK 237
Cdd:pfam01156 103 GGAFGVRGNVTpaaEFNIFVDPEAAKIVFTSGLPITMVPLDVTHQALLTPEDLERLAAlGTPLGRFLADLLRFYAEFYRE 182

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 488943555  238 TRGTKGTWIHDALTIAYALDSSIADFDECYADVICDSSLARGMSWrcfkepkMSMGMDLSTKNCVKILKNVDNAKLLK 315
Cdd:pfam01156 183 RFGIDGPPLHDPLAVAVALDPELFTTRRLNVDVETTGGLTRGQTV-------VDDRGGWGKPPNVRVATDVDVDRFWE 253
nuc_hydro_IU_UC_XIUA cd02651
nuc_hydro_IU_UC_XIUA: inosine-uridine preferring, ...
 2-321 1.15e-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: 170.42  E-value: 1.15e-50
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488943555   2 RLILDTDIGNaiagantDDGLALALILASKEIKLEMLSTICGNVP-SLVAYSVAK--DLFKRLNlnIPVYLGANEALKEP 78
Cdd:cd02651    1 PIIIDCDPGH-------DDAVAILLALFHPELDLLGITTVAGNVPlEKTTRNALKllTLLGRTD--VPVAAGAARPLVRP 71

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488943555  79 SKAWRQRLDES-VKNFKLEylweniKSPEILENInpDAIFKMGELVGKNPKEISICAIGPLTNIAMAMKIFKDFDINLKE 157
Cdd:cd02651   72 LITASDIHGESgLDGADLP------PPPRRPEDI--HAVDAIIDTLRASPEPITLVATGPLTNIALLLRKYPELAERIKE 143

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488943555 158 LFIMGGSFDMPYYTK--DTNFGFDPEAASIVLNSRAKITLVPYNVTMQTLLTHEDLKEL-QAKNILCDFIVETLGVWIDy 234
Cdd:cd02651  144 IVLMGGALGRGNITPaaEFNIFVDPEAAKIVFNSGIPITMVPLDVTHKALATPEVIERIrALGNPVGKMLAELLDFFAE- 222

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488943555 235 ASKTRGTKGTWIHDALTIAYALDSSIADFDECYADVICDSSLARGMS---WRcfkepkmsmgMDLSTKNCVKILKNVDNA 311
Cdd:cd02651  223 TYGSAFTEGPPLHDPCAVAYLLDPELFTTKRANVDVETEGELTRGRTvvdLR----------GVTGRPANAQVAVDVDVE 292

                        330
                 ....*....|
gi 488943555 312 KLLKLIKERL 321
Cdd:cd02651  293 KFWDLLLEAL 302
nuc_hydro_CeIAG cd02649
nuc_hydro_CeIAG: Nucleoside hydrolases similar to the inosine-adenosine-guanosine-preferring ...
 1-317 1.99e-47

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: 162.04  E-value: 1.99e-47
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488943555   1 MRLILDTDIGnaiaganTDDGLALALILASKEIKLEMLSTICGNVP-SLVAYSVAKDLFKRLNLNIPVYLGANEALKEPS 79
Cdd:cd02649    1 RKLIIDTDCG-------GDDAWALLMALASPNVEVLAITCVHGNTNvEQVVKNALRVLEACGRRDIPVYRGASKPLLGPG 73

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488943555  80 KAWrqrldesvknfklEYLW----------ENIKSPEILENINpdAIFKMGELVGKNPKEISICAIGPLTNIAMAMKIFK 149
Cdd:cd02649   74 PTA-------------AYFHgkdgfgdvgfPEPKDELELQKEH--AVDAIIRLVREYPGEITLVALGPLTNLALAYRLDP 138

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488943555 150 DFDINLKELFIMGGSfdmpYYTK-------DTNFGFDPEAASIVLNSRAK-ITLVPYNVTMQ-TLLTHEDLKELQAKNIL 220
Cdd:cd02649  139 SLPQKIKRLYIMGGN----REGVgnttpaaEFNFHVDPEAAHIVLNSFGCpITIVPWETTLLaFPLDWEFEDKWANRLEK 214

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488943555 221 CDFIVETLGVWIDYASKTRGTKGtWIH-DALTIAYALDSSIAD-FDECYADVICDSSLARGMswrcfkepkmsMGMD--- 295
Cdd:cd02649  215 ALFAESLNRREYAFASEGLGGDG-WVPcDALAVAAALDPSIITrRLTYAVDVELHGELTRGQ-----------MVVDwlg 282

                        330       340
                 ....*....|....*....|...
gi 488943555 296 -LSTKNCVKILKNVDNAKLLKLI 317
Cdd:cd02649  283 tLKKKPNARVITKIDREKFKELL 305
nuc_hydro_CaPnhB cd02650
NH_hydro_CaPnhB: A subgroup of nucleoside hydrolases similar to Corynebacterium ammoniagenes ...
 2-280 2.72e-45

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: 156.28  E-value: 2.72e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488943555   2 RLILDTDIGnaiaganTDDGLALALILASKEIKLEMLSTICGNVPSLVAYSVAKDLFKRLN-LNIPVYLGANEALKEPSK 80
Cdd:cd02650    1 KLILDTDPG-------IDDAMALAYALAHPDVDLIGVTTVYGNVTIETATRNALALLELFGrPDVPVAEGAAKPLTRPPF 73

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488943555  81 AWRQRL--DESVKNFKLEylwENIKSPEilENINPDAIFkmgELVGKNPKEISICAIGPLTNIAMAMKIFKDFDINLKEL 158
Cdd:cd02650   74 RIATFVhgDNGLGDVELP---APPRQPE--DESAADFLI---ELANEYPGELTLVAVGPLTNLALALARDPDFAKLVKQV 145

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488943555 159 FIMGGSFDM-----PYytKDTNFGFDPEAASIVLNSRAKITLVPYNVTMQTLLTHEDLKEL-QAKNILCDFIVETLGVWI 232
Cdd:cd02650  146 VVMGGAFTVpgnvtPA--AEANIHGDPEAADIVFTAGADLTMVGLDVTTQTLLTREDLDELrDSGGKAGQFLADMLDYYI 223

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*...
gi 488943555 233 DYASKTRGTKGTWIHDALTIAYALDSSIADFDECYADVICDsSLARGM 280
Cdd:cd02650  224 DFYQESPGLRGCALHDPLAVAAAVDPSLFTTREGVVRVETE-GPTRGR 270
PRK10768 PRK10768
ribonucleoside hydrolase RihC; Provisional
 3-279 1.07e-32

ribonucleoside hydrolase RihC; Provisional


Pssm-ID: 182713 [Multi-domain]  Cd Length: 304  Bit Score: 123.10  E-value: 1.07e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488943555   3 LILDTDIGnaiaganTDDGLALALILASKEIKLEMLSTICGNVpslvaySVAK------DLFKRLNLNIPVYLGANEALK 76
Cdd:PRK10768   5 IILDTDPG-------IDDAVAIAAALFAPELDLKLITTVAGNV------SVEKttrnalKLLHFFNSDVPVAQGAAKPLV 71

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488943555  77 EPSKAWRQRLDESVK---NFkleylweniksPEILENINP-DAIFKMGELVGKNPKEISICAIGPLTNIAMAMKIFKDFD 152
Cdd:PRK10768  72 RPLRDAASVHGESGMegyDF-----------PEHTRKPLSiPAVEAMRDALMNAPEPVTLVAIGPLTNIALLLSTYPEVK 140

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488943555 153 INLKELFIMGGSFDMPYYT--KDTNFGFDPEAASIVLNSRAKITLVPYNVTMQTLLTHEDLKELQAKNilcdfivETLGV 230
Cdd:PRK10768 141 PYIKRIVLMGGSAGRGNVTpnAEFNIAVDPEAAAIVFRSGIPIVMCGLDVTNQALLTPDYLATLPELN-------RTGKM 213

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|..
gi 488943555 231 WIDYASKTRG---TKGTWIHDALTIAYALDSSIADFDECYADVICDSSLARG 279
Cdd:PRK10768 214 LHALFSHYRSgsmQTGLRMHDVCAIAYLLRPELFTLKPCFVDVETQGEFTAG 265
nuc_hydro_3 cd02653
NH_3: A subgroup of nucleoside hydrolases. This group contains eukaryotic and bacterial ...
 3-324 8.33e-32

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: 121.33  E-value: 8.33e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488943555   3 LILDTDIGnaiaganTDDGLALALILASKEIKLEMLSTICGNVPSLVaysVAKDLFKRLNL----NIPVYLGANEALKEP 78
Cdd:cd02653    2 VIIDCDPG-------IDDALALLYLLASPDLDVVGITTTAGNVPVEQ---VAANALGVLELlgrtDIPVYLGADKPLAGP 71

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488943555  79 ------------------SKAWRQRLDESVKNFKLEYLwenikspeileninpdaifkmgelvgKNPKEISICAIGPLTN 140
Cdd:cd02653   72 lttaqdthgpdglgyaelPASTRTLSDESAAQAWVDLA--------------------------RAHPDLIGLATGPLTN 125

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488943555 141 IAMAMKIFKDFDINLKELFIMGGSFDMPYYTKDT---NFGFDPEAASIVLN----SRAKITLVPYNVTMQTLLThEDLKE 213
Cdd:cd02653  126 LALALREEPELPRLLRRLVIMGGAFNSRGNTSPVaewNYWVDPEAAKEVLAafggHPVRPTICGLDVTRAVVLT-PNLLE 204

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488943555 214 L--QAKNILCDFIVETLGVWIDYASKTRGTKGTWIHDALTIAYALDSSIADFDECYADVICDsSLARGMS---WRCFKEP 288
Cdd:cd02653  205 RlaRAKDSVGAFIEDALRFYFEFHWAYGHGYGAVIHDPLAAAVALNPNLARGRPAYVDVECT-GVLTGQTvvdWAGFWGK 283

                        330       340       350
                 ....*....|....*....|....*....|....*.
gi 488943555 289 kmsmgmdlsTKNcVKILKNVDNAKLLKLIKERLLKG 324
Cdd:cd02653  284 ---------GAN-AEILTKVDSQDFMALFIERVLAI 309
PLN02717 PLN02717
uridine nucleosidase
 1-324 2.05e-30

uridine nucleosidase


Pssm-ID: 178319 [Multi-domain]  Cd Length: 316  Bit Score: 117.40  E-value: 2.05e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488943555   1 MRLILDTDIGnaiaganTDDGLALALILASKEIKLEMLSTICGNVPSLVAYSVAKDLFKRL-NLNIPVYLGANEALKEPS 79
Cdd:PLN02717   1 KKLIIDTDPG-------IDDAMAILMALRSPEVEVIGLTTIFGNVTTKLATRNALHLLEMAgRPDVPVAEGSHEPLKGGT 73

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488943555  80 KawrqrldESVKNFkleylwenIKSPEILENIN--PDAIFKMG--------ELVGKNPKEISICAIGPLTNIAMAMKIFK 149
Cdd:PLN02717  74 K-------PRIADF--------VHGSDGLGNTNlpPPKGKKIEksaaeflvEKVSEYPGEVTVVALGPLTNLALAIKLDP 138

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488943555 150 DFDINLKELFIMGGSFdmpYYTKDTN-------FGfDPEAASIVLNSRAKITLVPYNVTMQTLLTHEDLKEL-QAKNILC 221
Cdd:PLN02717 139 SFAKKVGQIVVLGGAF---FVNGNVNpaaeaniFG-DPEAADIVFTSGADITVVGINVTTQVVLTDADLEELrDSKGKYA 214

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488943555 222 DFIVETLGVWIDYASKTRGTKGTWIHDALTIAYALDSSIADFDECYADVICDsSLARG-----MSWRCFKEPKmsmgmDL 296
Cdd:PLN02717 215 QFLCDICKFYRDWHRKSYGIDGIYLHDPTALLAAVRPSLFTYKEGVVRVETE-GICRGltlfdNGLKRWNGEN-----AW 288

                        330       340
                 ....*....|....*....|....*...
gi 488943555 297 STKNCVKILKNVDNAKLLKLIKERLLKG 324
Cdd:PLN02717 289 TGRPPVKVAVTVDAPAVVELVKERLMAS 316
rihA PRK10443
ribonucleoside hydrolase 1; Provisional
 3-281 6.76e-23

ribonucleoside hydrolase 1; Provisional


Pssm-ID: 182465 [Multi-domain]  Cd Length: 311  Bit Score: 96.66  E-value: 6.76e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488943555   3 LILDTDIGNaiagantDDGLALALILASKEIKLEMLSTICGN-VPSLVAYSVAK--DLFKRLNlnIPVYLGANEALKEPS 79
Cdd:PRK10443   5 IILDCDPGH-------DDAIALVLALASPELDVKAVTTSAGNqTPEKTLRNALRmlTLLNRTD--IPVAGGAVKPLMREL 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488943555  80 kawrqrldESVKNFKLEYLWENIKSPEileninPD-------AIFKMGELVGKNPKEISICAIGPLTNIAMAMKIFKDFD 152
Cdd:PRK10443  76 --------IIADNVHGESGLDGPALPE------PTfapqnctAVELMAKTLRESAEPVTLVSTGPQTNVALLLASHPELH 141

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488943555 153 INLKELFIMGGSFDMPYYTKDTNFGF--DPEAASIVLNSRAKITLVPYNVTMQTLLTHEDLKELQA-KNILCDFIVETLG 229
Cdd:PRK10443 142 SKIARIVIMGGAMGLGNWTPAAEFNIyvDPEAAEIVFQSGIPIVMAGLDVTHKAQIMDEDIERIRAiGNPVATIVAELLD 221

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|...
gi 488943555 230 VWIDY-ASKTRGTKGTWIHDALTIAYALDSSIADFDECYADVICDSSLARGMS 281
Cdd:PRK10443 222 FFMEYhKDEKWGFVGAPLHDPCTIAWLLKPELFTTVERWVGVETQGEYTQGMT 274
nuc_hydro_TvIAG cd02647
nuc_hydro_ TvIAG: Nucleoside hydrolases similar to the Inosine-adenosine-guanosine-preferring ...
 2-280 8.47e-20

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: 88.24  E-value: 8.47e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488943555   2 RLILDTDignaiagANTDDGLALALILASKEIKLE--MLSTICGNVPSLVAYSVAKDLFKRLNLN--IPVYLGANEALKE 77
Cdd:cd02647    2 NVIFDHD-------GNVDDLVALLLLLKNEKVDLKgiGVSGIDADCYVEPAVSVTRKLIDRLGQRdaIPVGKGGSRAVNP 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488943555  78 PSKAWRQRLDESVKNFKLEylweNIKSPEILENINPDAIFKMGELVGKNPKEISICAIGPLTNIAMAMKIFKDFDINLKE 157
Cdd:cd02647   75 FPRSWRRDAAFSVDHLPIL----NERYTVETPLAEETAQLVLIEKIKASLEPVTLLVTGPLTNLARALDSDPDISSNIEE 150

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488943555 158 LFIMGGSFDMP----YYTKDTNFGF----DPEAASIVLNSRAKITLVPYNVTMQTLLTHEDLKEL-QAKNILCDFIVETL 228
Cdd:cd02647  151 VYIMGGGVDAPgnvfTPPSNGTAEFnifwDPLAAKTVFDSGLKITLVPLDATNTVPLTREFLETDrQRFAAQRLPASDLA 230

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|..
gi 488943555 229 GVWIDYASKTRGTKGTWIHDALTIAYALDSSIADFDECYADVICDSSLARGM 280
Cdd:cd02647  231 GQGYALVKPLEFNSTYYMWDVLTTLVLGAKEVDNTKESLILEVDTDGLSAGQ 282
rihB PRK09955
ribosylpyrimidine nucleosidase;
2-273 3.51e-16

ribosylpyrimidine nucleosidase;


Pssm-ID: 182166 [Multi-domain]  Cd Length: 313  Bit Score: 78.06  E-value: 3.51e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488943555   2 RLILDTDIGNaiagantDDGLALALILASKEIKLEMLSTICGNVPSLVAYSVAKDLFKRLNLNIPVYLGAnealkePSKA 81
Cdd:PRK09955   5 KIILDCDPGH-------DDAIAMMMAAKHPAIDLLGITIVAGNQTLDKTLINGLNVCQKLEINVPVYAGM------PQPI 71

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488943555  82 WRQRLdeSVKNFKLEylwENIKSPeILENINPDAIFKMG-----ELVGKNPKEISICAIGPLTNIAMAMKIFKDFDINLK 156
Cdd:PRK09955  72 MRQQI--VADNIHGE---TGLDGP-VFEPLTRQAESTHAvkyiiDTLMASDGDITLVPVGPLSNIAVAMRMQPAILPKIR 145

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488943555 157 ELFIMGGSFDMPYYTKDTNFGF--DPEAASIVLNSRAKITLVPYNVTMQTLLTHEDLKELQ-----AKNILCDFIVETLg 229
Cdd:PRK09955 146 EIVLMGGAYGTGNFTPSAEFNIfaDPEAARVVFTSGVPLVMMGLDLTNQTVCTPDVIARMEraggpAGELFSDIMNFTL- 224

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 488943555 230 vwidyasKTR----GTKGTWIHDALTIAYALDSSIADFDE-----------CYADVICD 273
Cdd:PRK09955 225 -------KTQfenyGLAGGPVHDATCIGYLINPDGIKTQEmyvevdvnsgpCYGRTVCD 276
PTZ00313 PTZ00313
inosine-adenosine-guanosine-nucleoside hydrolase; Provisional
 3-286 8.93e-14

inosine-adenosine-guanosine-nucleoside hydrolase; Provisional


Pssm-ID: 140334 [Multi-domain]  Cd Length: 326  Bit Score: 71.05  E-value: 8.93e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488943555   3 LILDTDignaiagANTDDGLALALILASKEiKLEMLSTICGNVPSLV--AYSVAKDLFKRLN--LNIPVYLGANEALKE- 77
Cdd:PTZ00313   5 VILDHD-------GNHDDLVALALLLGNPE-KVKVIGCICTDADCFVddAFNVTGKLMCMMHarEATPLFPIGKSSFKGv 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488943555  78 ---PSKaWR---QRLDE--SVKNFKLEYLWENIKsPEILENINPDAifkMGELVGKNPKEISICAIGPLTNIAMAM-KIF 148
Cdd:PTZ00313  77 npfPSE-WRwsaKNMDDlpCLNIPEHVAIWEKLK-PENEALVGEEL---LADLVMSSPEKVTICVTGPLSNVAWCIeKYG 151

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488943555 149 KDFDINLKELFIMGGSFDMPYY--------TKDTNFGFDPEAASIVLN-SRAKITLVPYNVTMQTLLTHEDLKELQAKN- 218
Cdd:PTZ00313 152 EEFTKKVEECVIMGGAVDVGGNvflpgtdgSAEWNIYWDPPAAKTVLMcPHIRKVLFSLDSTNSVPVTSEVVKKFGAQNk 231

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 488943555 219 -ILCDFIVETlgvwidYASKT-----RGTKGTWIHDALTIAYALDSSIADFDECYADVICDSSLARGMSWRCFK 286
Cdd:PTZ00313 232 yLLSQFVGST------WAMCThhellRPGDGYYAWDVLTAAYVIERNLAELEPVPLEVVVEKAKNEGRTRRAAE 299
nuc_hydro_1 cd02648
NH_1: A subgroup of nucleoside hydrolases. This group contains fungal proteins similar to ...
 2-256 1.08e-12

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: 67.99  E-value: 1.08e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488943555   2 RLILDTDIGnaiaganTDDGLALALILAS-KEIKLEMLSTICGNVPSLVAYSVAKDLFkrlnlnipvylganeALKEPSK 80
Cdd:cd02648    3 PIIIDTDPG-------VDDVLAILLALSSpEEVDVALISLTFGNTTLDHALRNVLRLF---------------HVLERER 60

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488943555  81 AWRQRLD-----ESVKNFKL-------------EYLWENIKSPEILENIN---------PDAIFKMGE------------ 121
Cdd:cd02648   61 AWRATPGvryraFSADAEKPivasgsdqplegeRLTASYFHGRDGLSGVHwlhpdftpvETWIPEIVApltpsdkpaydv 140

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488943555 122 ----LVGKNPKEISICAIGPLTNIAMAMKIFKDFDINLKELFIMGGSFDMPYYTK---DTNFGFDPEAASIVLNSRA--- 191
Cdd:cd02648  141 ildiLREEPDHTVTIAALGPLTNLAAAARKDPETFAKVGEVVVMGGAIDVPGNTSpvaEFNCFADPYAAAVVIDEPPsta 220

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488943555 192 -------KITLVPYNVTMQTLLTHEDLKELQAKNILCDFIVETLGVWIDYA------SKTRGTKGTWI----------HD 248
Cdd:cd02648  221 pearrklPLQVFPLDITTGHTLPYSSLFATYVTPRDAPERGSPLARWLEHVfistflTHPRAFTPEEFlpdrselfemHD 300


                 ....*...
gi 488943555 249 ALTIAYAL 256
Cdd:cd02648  301 PLAVWYAI 308
nuc_hydro_2 cd02652
NH_2: A subgroup of nucleoside hydrolases. This group contains eukaryotic and bacterial ...
 3-186 9.53e-10

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: 58.67  E-value: 9.53e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488943555   3 LILDTDIGNAIagantDDGLALALILASKEIKLEMLSTICGNVPSLVAysvaKDLFKRLNLNIPVYLGANEALK-EPSKA 81
Cdd:cd02652    1 LILDTDIGGDP-----DDALALALAHALQKCDLLAVTITLADASARRA----IDAVNRFYGRGDIPIGADYHGWpEDAKD 71

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488943555  82 WRQRLDESvknFKLEYLWEnikspeiLENINPDAIFKMGELVGK-NPKEISICAIGPLTNIAMAMKIFKDFDINL----- 155
Cdd:cd02652   72 HAKFLLEG---DRLHHDLE-------SAEDALDAVKALRRLLASaEDASVTIVSIGPLTNLAALLDADADPLTGPelvrq 141

                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 488943555 156 --KELFIMGGSFDMPY---YTKDTNFGFDPEAASIV 186
Cdd:cd02652  142 kvKRLVVMGGAFYDPDgnvQHREYNFVTDPKAAQRV 177
 
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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