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Conserved domains on  [gi|19111905|ref|NP_595113|]
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inosine-uridine-preferring nucleoside hydrolase [Schizosaccharomyces pombe]

Protein Classification

nucleoside hydrolase( domain architecture ID 10119107)

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

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
nuc_hydro_CjNH cd02654
nuc_hydro_CjNH. Nucleoside hydrolases similar to Campylobacter jejuni nucleoside hydrolase. ...
 26-351 5.87e-131

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: 378.44  E-value: 5.87e-131
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111905  26 KVIIDNDGL----TDLQVLFALQAKQ---QILGVTAIYGDYTLddslflasdVLSTGNLTY--------CIPSFAGAAQP 90
Cdd:cd02654   1 KVILDNDIAmgrdTDDGLALALLLWSpevELLGLSAVSGNCWL---------SAVTYNVLRmlelagadAIPVYAGANTP 71

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111905  91 LLRTNNTFQIWQELYGSYVWQGYWQPEYETANTNnESYIYNTQISAAQFIIDMVKANPNEITIVAAGPMTNLAIALSIWP 170
Cdd:cd02654  72 LGRTNRAFHAWESLYGAYLWQGAWSPEYSDMYTN-ASIIRNASIPAALFMIEMVRKHPHEVSIVAAGPLTNLALALRIDP 150

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111905 171 DLAKNTKSLVIMGGYVDsqiaqvTGGDFLNDMY-SDFNLFMEPEAAQTAITADWPELIIAGNITSQ--VYPSQ-----SL 242
Cdd:cd02654 151 DFAPLAKELVIMGGYLD------DIGEFVNRHYaSDFNLIMDPEAASIVLTAPWKSITIPGNVTNRtcLTPEQikaddPL 224

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111905 243 YNGIIARaggmanieSDSGLSYAKQFVGNGtlpsGSFPFWDEVASAIAAWPEIVNSSYDAYVSVDTAYDSPFYGSlrmVP 322
Cdd:cd02654 225 RDFIRET--------LDLPIDYAKEFVGTG----DGLPMWDELASAVALDPELATSSETFYIDVQTDSDGGGQLI---WP 289

                       330       340
                ....*....|....*....|....*....
gi 19111905 323 ADLVPKKGVRTAKASMITGINVAMFYQKI 351
Cdd:cd02654 290 EDLLLAKGLRPYHVKVITAVDVAAFLNLI 318
 
Name Accession Description Interval E-value
nuc_hydro_CjNH cd02654
nuc_hydro_CjNH. Nucleoside hydrolases similar to Campylobacter jejuni nucleoside hydrolase. ...
 26-351 5.87e-131

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: 378.44  E-value: 5.87e-131
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111905  26 KVIIDNDGL----TDLQVLFALQAKQ---QILGVTAIYGDYTLddslflasdVLSTGNLTY--------CIPSFAGAAQP 90
Cdd:cd02654   1 KVILDNDIAmgrdTDDGLALALLLWSpevELLGLSAVSGNCWL---------SAVTYNVLRmlelagadAIPVYAGANTP 71

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111905  91 LLRTNNTFQIWQELYGSYVWQGYWQPEYETANTNnESYIYNTQISAAQFIIDMVKANPNEITIVAAGPMTNLAIALSIWP 170
Cdd:cd02654  72 LGRTNRAFHAWESLYGAYLWQGAWSPEYSDMYTN-ASIIRNASIPAALFMIEMVRKHPHEVSIVAAGPLTNLALALRIDP 150

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111905 171 DLAKNTKSLVIMGGYVDsqiaqvTGGDFLNDMY-SDFNLFMEPEAAQTAITADWPELIIAGNITSQ--VYPSQ-----SL 242
Cdd:cd02654 151 DFAPLAKELVIMGGYLD------DIGEFVNRHYaSDFNLIMDPEAASIVLTAPWKSITIPGNVTNRtcLTPEQikaddPL 224

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111905 243 YNGIIARaggmanieSDSGLSYAKQFVGNGtlpsGSFPFWDEVASAIAAWPEIVNSSYDAYVSVDTAYDSPFYGSlrmVP 322
Cdd:cd02654 225 RDFIRET--------LDLPIDYAKEFVGTG----DGLPMWDELASAVALDPELATSSETFYIDVQTDSDGGGQLI---WP 289

                       330       340
                ....*....|....*....|....*....
gi 19111905 323 ADLVPKKGVRTAKASMITGINVAMFYQKI 351
Cdd:cd02654 290 EDLLLAKGLRPYHVKVITAVDVAAFLNLI 318
URH1 COG1957
Inosine-uridine nucleoside N-ribohydrolase [Nucleotide transport and metabolism]; ...
 26-357 6.56e-41

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: 146.45  E-value: 6.56e-41
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111905  26 KVIIDND-GLTDLQ-VLFALQAKQ-QILGVTAIYGDYTLDDSLFLASDVLSTGNLTYcIPSFAGAAQPLLRTNNTfqiWQ 102
Cdd:COG1957   4 KVIIDTDpGIDDALaLLLALASPEiDLLGITTVAGNVPLEQTTRNALKLLELAGRTD-VPVAAGAARPLVRPLVT---AE 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111905 103 ELYGSyvwQGYWQPEYETANTNNESYiyntqiSAAQFIIDMVKANPNEITIVAAGPMTNLAIALSIWPDLAKNTKSLVIM 182
Cdd:COG1957  80 HVHGE---DGLGGVDLPEPTRPPEPE------HAVDFIIETLRAAPGEVTLVALGPLTNLALALRKDPELAERIKRIVIM 150

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111905 183 GGYVDsqiaqVTGgdflND-MYSDFNLFMEPEAAQTAITADWPeLIIAG-NITSQVYPSQSLYNGIIARAGGMANIESDS 260
Cdd:COG1957 151 GGAFF-----VPG----NVtPVAEFNIYVDPEAAKIVFASGIP-ITMVGlDVTHQALLTPEDLARLAALGTPLGRFLADL 220

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111905 261 gLSYAKQFVGNgTLPSGSFPFWDEVASAIAAWPEIVnSSYDAYVSVDTAyDSPFYGslRMVpADLVPKKGvRTAKASMIT 340
Cdd:COG1957 221 -LDFYLDFYRE-RYGLDGCPLHDPLAVAYLLDPELF-TTRPAPVDVETD-GELTRG--QTV-VDWRGVTG-RPPNARVAL 292

                       330
                ....*....|....*..
gi 19111905 341 GINVAMFYQKIYDSLTA 357
Cdd:COG1957 293 DVDAERFLDLLLERLAR 309
IU_nuc_hydro pfam01156
Inosine-uridine preferring nucleoside hydrolase;
27-349 4.27e-32

Inosine-uridine preferring nucleoside hydrolase;


Pssm-ID: 460086 [Multi-domain]  Cd Length: 253  Bit Score: 121.55  E-value: 4.27e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111905    27 VIIDNDGLTD--LQVLFALQAKQ-QILGVTAIYGDYTLDDSLFLASDVLSTGNLTyCIPSFAGaaqpllrtnntfqiwqe 103
Cdd:pfam01156   1 VIIDTDPGIDdaLALLLALASPEiELLGITTVAGNVSLEQTTRNALRLLELGGRD-DIPVYAG----------------- 62

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111905   104 lygsyvwqgywqpeyetantnnesyiyntqisaaqfiiDMVKAnPNEITIVAAGPMTNLAIALSIWPDLAKNTKSLVIMG 183
Cdd:pfam01156  63 --------------------------------------EAIRE-PGEVTLVATGPLTNLALALRLDPELAKKIKELVIMG 103

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111905   184 GYVDSqIAQVTggdflndMYSDFNLFMEPEAAQTAITADWPELIIAGNITSQVYPSQSLYNGIIARAGGMANIESDSGLS 263
Cdd:pfam01156 104 GAFGV-RGNVT-------PAAEFNIFVDPEAAKIVFTSGLPITMVPLDVTHQALLTPEDLERLAALGTPLGRFLADLLRF 175

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111905   264 YAKQFVgnGTLPSGSFPFWDEVASAIAAWPEIVnSSYDAYVSVDTAyDSPFYGslRMVPADLVPKKGVRTAKAsmITGIN 343
Cdd:pfam01156 176 YAEFYR--ERFGIDGPPLHDPLAVAVALDPELF-TTRRLNVDVETT-GGLTRG--QTVVDDRGGWGKPPNVRV--ATDVD 247


                  ....*.
gi 19111905   344 VAMFYQ 349
Cdd:pfam01156 248 VDRFWE 253
rihB PRK09955
ribosylpyrimidine nucleosidase;
23-316 6.18e-20

ribosylpyrimidine nucleosidase;


Pssm-ID: 182166 [Multi-domain]  Cd Length: 313  Bit Score: 89.24  E-value: 6.18e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111905   23 AASKVIIDNDGLTDLQVLFALQAKQ---QILGVTAIYGDYTLDDSLFLASDVLSTGNLTycIPSFAGAAQPLLRTNntfQ 99
Cdd:PRK09955   2 EKRKIILDCDPGHDDAIAMMMAAKHpaiDLLGITIVAGNQTLDKTLINGLNVCQKLEIN--VPVYAGMPQPIMRQQ---I 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111905  100 IWQELYGSYVWQGywqPEYETANTNNESyiyntqISAAQFIIDMVKANPNEITIVAAGPMTNLAIALSIWPDLAKNTKSL 179
Cdd:PRK09955  77 VADNIHGETGLDG---PVFEPLTRQAES------THAVKYIIDTLMASDGDITLVPVGPLSNIAVAMRMQPAILPKIREI 147

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111905  180 VIMGGYVDSqiaqvtgGDFLNDmySDFNLFMEPEAAQTAITADWPELIIAGNITSQVYPSQSlyngIIAR---AGGMA-N 255
Cdd:PRK09955 148 VLMGGAYGT-------GNFTPS--AEFNIFADPEAARVVFTSGVPLVMMGLDLTNQTVCTPD----VIARmerAGGPAgE 214

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 19111905  256 IESD-SGLSYAKQFVGNGtLPSGsfPFWDEVASAIAAWPEIVNSSyDAYVSVDTAyDSPFYG 316
Cdd:PRK09955 215 LFSDiMNFTLKTQFENYG-LAGG--PVHDATCIGYLINPDGIKTQ-EMYVEVDVN-SGPCYG 271
 
Name Accession Description Interval E-value
nuc_hydro_CjNH cd02654
nuc_hydro_CjNH. Nucleoside hydrolases similar to Campylobacter jejuni nucleoside hydrolase. ...
 26-351 5.87e-131

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: 378.44  E-value: 5.87e-131
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111905  26 KVIIDNDGL----TDLQVLFALQAKQ---QILGVTAIYGDYTLddslflasdVLSTGNLTY--------CIPSFAGAAQP 90
Cdd:cd02654   1 KVILDNDIAmgrdTDDGLALALLLWSpevELLGLSAVSGNCWL---------SAVTYNVLRmlelagadAIPVYAGANTP 71

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111905  91 LLRTNNTFQIWQELYGSYVWQGYWQPEYETANTNnESYIYNTQISAAQFIIDMVKANPNEITIVAAGPMTNLAIALSIWP 170
Cdd:cd02654  72 LGRTNRAFHAWESLYGAYLWQGAWSPEYSDMYTN-ASIIRNASIPAALFMIEMVRKHPHEVSIVAAGPLTNLALALRIDP 150

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111905 171 DLAKNTKSLVIMGGYVDsqiaqvTGGDFLNDMY-SDFNLFMEPEAAQTAITADWPELIIAGNITSQ--VYPSQ-----SL 242
Cdd:cd02654 151 DFAPLAKELVIMGGYLD------DIGEFVNRHYaSDFNLIMDPEAASIVLTAPWKSITIPGNVTNRtcLTPEQikaddPL 224

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111905 243 YNGIIARaggmanieSDSGLSYAKQFVGNGtlpsGSFPFWDEVASAIAAWPEIVNSSYDAYVSVDTAYDSPFYGSlrmVP 322
Cdd:cd02654 225 RDFIRET--------LDLPIDYAKEFVGTG----DGLPMWDELASAVALDPELATSSETFYIDVQTDSDGGGQLI---WP 289

                       330       340
                ....*....|....*....|....*....
gi 19111905 323 ADLVPKKGVRTAKASMITGINVAMFYQKI 351
Cdd:cd02654 290 EDLLLAKGLRPYHVKVITAVDVAAFLNLI 318
URH1 COG1957
Inosine-uridine nucleoside N-ribohydrolase [Nucleotide transport and metabolism]; ...
 26-357 6.56e-41

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: 146.45  E-value: 6.56e-41
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111905  26 KVIIDND-GLTDLQ-VLFALQAKQ-QILGVTAIYGDYTLDDSLFLASDVLSTGNLTYcIPSFAGAAQPLLRTNNTfqiWQ 102
Cdd:COG1957   4 KVIIDTDpGIDDALaLLLALASPEiDLLGITTVAGNVPLEQTTRNALKLLELAGRTD-VPVAAGAARPLVRPLVT---AE 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111905 103 ELYGSyvwQGYWQPEYETANTNNESYiyntqiSAAQFIIDMVKANPNEITIVAAGPMTNLAIALSIWPDLAKNTKSLVIM 182
Cdd:COG1957  80 HVHGE---DGLGGVDLPEPTRPPEPE------HAVDFIIETLRAAPGEVTLVALGPLTNLALALRKDPELAERIKRIVIM 150

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111905 183 GGYVDsqiaqVTGgdflND-MYSDFNLFMEPEAAQTAITADWPeLIIAG-NITSQVYPSQSLYNGIIARAGGMANIESDS 260
Cdd:COG1957 151 GGAFF-----VPG----NVtPVAEFNIYVDPEAAKIVFASGIP-ITMVGlDVTHQALLTPEDLARLAALGTPLGRFLADL 220

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111905 261 gLSYAKQFVGNgTLPSGSFPFWDEVASAIAAWPEIVnSSYDAYVSVDTAyDSPFYGslRMVpADLVPKKGvRTAKASMIT 340
Cdd:COG1957 221 -LDFYLDFYRE-RYGLDGCPLHDPLAVAYLLDPELF-TTRPAPVDVETD-GELTRG--QTV-VDWRGVTG-RPPNARVAL 292

                       330
                ....*....|....*..
gi 19111905 341 GINVAMFYQKIYDSLTA 357
Cdd:COG1957 293 DVDAERFLDLLLERLAR 309
IU_nuc_hydro pfam01156
Inosine-uridine preferring nucleoside hydrolase;
27-349 4.27e-32

Inosine-uridine preferring nucleoside hydrolase;


Pssm-ID: 460086 [Multi-domain]  Cd Length: 253  Bit Score: 121.55  E-value: 4.27e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111905    27 VIIDNDGLTD--LQVLFALQAKQ-QILGVTAIYGDYTLDDSLFLASDVLSTGNLTyCIPSFAGaaqpllrtnntfqiwqe 103
Cdd:pfam01156   1 VIIDTDPGIDdaLALLLALASPEiELLGITTVAGNVSLEQTTRNALRLLELGGRD-DIPVYAG----------------- 62

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111905   104 lygsyvwqgywqpeyetantnnesyiyntqisaaqfiiDMVKAnPNEITIVAAGPMTNLAIALSIWPDLAKNTKSLVIMG 183
Cdd:pfam01156  63 --------------------------------------EAIRE-PGEVTLVATGPLTNLALALRLDPELAKKIKELVIMG 103

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111905   184 GYVDSqIAQVTggdflndMYSDFNLFMEPEAAQTAITADWPELIIAGNITSQVYPSQSLYNGIIARAGGMANIESDSGLS 263
Cdd:pfam01156 104 GAFGV-RGNVT-------PAAEFNIFVDPEAAKIVFTSGLPITMVPLDVTHQALLTPEDLERLAALGTPLGRFLADLLRF 175

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111905   264 YAKQFVgnGTLPSGSFPFWDEVASAIAAWPEIVnSSYDAYVSVDTAyDSPFYGslRMVPADLVPKKGVRTAKAsmITGIN 343
Cdd:pfam01156 176 YAEFYR--ERFGIDGPPLHDPLAVAVALDPELF-TTRRLNVDVETT-GGLTRG--QTVVDDRGGWGKPPNVRV--ATDVD 247


                  ....*.
gi 19111905   344 VAMFYQ 349
Cdd:pfam01156 248 VDRFWE 253
nuc_hydro_CeIAG cd02649
nuc_hydro_CeIAG: Nucleoside hydrolases similar to the inosine-adenosine-guanosine-preferring ...
 26-352 4.31e-28

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: 111.97  E-value: 4.31e-28
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111905  26 KVIIDNDGLTD--LQVLFALQAKQ-QILGVTAIYGDYTLDDSLFLASDVLSTGNlTYCIPSFAGAAQPLLRtnntfqiwQ 102
Cdd:cd02649   2 KLIIDTDCGGDdaWALLMALASPNvEVLAITCVHGNTNVEQVVKNALRVLEACG-RRDIPVYRGASKPLLG--------P 72

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111905 103 ELYGSYVW--QGYWQPEYETANTNNESYIYNtqisAAQFIIDMVKANPNEITIVAAGPMTNLAIALSIWPDLAKNTKSLV 180
Cdd:cd02649  73 GPTAAYFHgkDGFGDVGFPEPKDELELQKEH----AVDAIIRLVREYPGEITLVALGPLTNLALAYRLDPSLPQKIKRLY 148

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111905 181 IMGGYVDSqIAQVTggdflndMYSDFNLFMEPEAAQTAITADWPELIIAG-NITSQVYPSQSLYNGIIARAGGMANI-ES 258
Cdd:cd02649 149 IMGGNREG-VGNTT-------PAAEFNFHVDPEAAHIVLNSFGCPITIVPwETTLLAFPLDWEFEDKWANRLEKALFaES 220

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111905 259 DSGLSYAkqFVGNGTLPSGsFPFWDEVASAIAAWPEIVNSSYDAYVSVDTAydspfyGSL-R-MVPADLVPKKGvRTAKA 336
Cdd:cd02649 221 LNRREYA--FASEGLGGDG-WVPCDALAVAAALDPSIITRRLTYAVDVELH------GELtRgQMVVDWLGTLK-KKPNA 290

                       330
                ....*....|....*.
gi 19111905 337 SMITGINVAMFYQKIY 352
Cdd:cd02649 291 RVITKIDREKFKELLY 306
nuc_hydro_CaPnhB cd02650
NH_hydro_CaPnhB: A subgroup of nucleoside hydrolases similar to Corynebacterium ammoniagenes ...
 26-236 5.60e-27

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: 108.90  E-value: 5.60e-27
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111905  26 KVIIDND-GLTD-LQVLFALQAKQ-QILGVTAIYGDYTLDDSLFLASDVLSTGNlTYCIPSFAGAAQPLlrTNNTFQIWQ 102
Cdd:cd02650   1 KLILDTDpGIDDaMALAYALAHPDvDLIGVTTVYGNVTIETATRNALALLELFG-RPDVPVAEGAAKPL--TRPPFRIAT 77

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111905 103 ELYGSyvwQGYWQPEYETANTNNESyiyntqISAAQFIIDMVKANPNEITIVAAGPMTNLAIALSIWPDLAKNTKSLVIM 182
Cdd:cd02650  78 FVHGD---NGLGDVELPAPPRQPED------ESAADFLIELANEYPGELTLVAVGPLTNLALALARDPDFAKLVKQVVVM 148

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....
gi 19111905 183 GGYVDSQiAQVTGgdflndmYSDFNLFMEPEAAQTAITADWPELIIAGNITSQV 236
Cdd:cd02650 149 GGAFTVP-GNVTP-------AAEANIHGDPEAADIVFTAGADLTMVGLDVTTQT 194
nuc_hydro_IU_UC_XIUA cd02651
nuc_hydro_IU_UC_XIUA: inosine-uridine preferring, ...
 26-355 2.30e-26

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: 107.25  E-value: 2.30e-26
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111905  26 KVIIDND-GLTD-LQVLFALQAKQ-QILGVTAIYGDYTLDDSLFLASDVLSTGNLTYcIPSFAGAAQPLLRtnntfqiwQ 102
Cdd:cd02651   1 PIIIDCDpGHDDaVAILLALFHPElDLLGITTVAGNVPLEKTTRNALKLLTLLGRTD-VPVAAGAARPLVR--------P 71

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111905 103 ELYGSYV-----WQGYWQPEyETANTnnesyiynTQISAAQFIIDMVKANPNEITIVAAGPMTNLAIALSIWPDLAKNTK 177
Cdd:cd02651  72 LITASDIhgesgLDGADLPP-PPRRP--------EDIHAVDAIIDTLRASPEPITLVATGPLTNIALLLRKYPELAERIK 142

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111905 178 SLVIMGGyvdsqiaQVTGGDFlnDMYSDFNLFMEPEAAQTAITADWPeLIIAG-NITSQVYPSQSLYNGIIARAGGMANI 256
Cdd:cd02651 143 EIVLMGG-------ALGRGNI--TPAAEFNIFVDPEAAKIVFNSGIP-ITMVPlDVTHKALATPEVIERIRALGNPVGKM 212

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111905 257 ESDSGLSYAKQFvgnGTLPSGSFPFWDEVASAIAAWPEIVNSSyDAYVSVDTAydspfyGSLR--MVPADLVPKKGvRTA 334
Cdd:cd02651 213 LAELLDFFAETY---GSAFTEGPPLHDPCAVAYLLDPELFTTK-RANVDVETE------GELTrgRTVVDLRGVTG-RPA 281

                       330       340
                ....*....|....*....|.
gi 19111905 335 KASMITGINVAMFYQKIYDSL 355
Cdd:cd02651 282 NAQVAVDVDVEKFWDLLLEAL 302
nuc_hydro_TvIAG cd02647
nuc_hydro_ TvIAG: Nucleoside hydrolases similar to the Inosine-adenosine-guanosine-preferring ...
 27-312 1.86e-23

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: 99.41  E-value: 1.86e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111905  27 VIIDNDG----LTDLQVLFALQAKQQIL-GVTAIYGDYTLDDSLFLASDVLSTGNLTYCIPSFAGAAQPLlrtnNTFQI- 100
Cdd:cd02647   3 VIFDHDGnvddLVALLLLLKNEKVDLKGiGVSGIDADCYVEPAVSVTRKLIDRLGQRDAIPVGKGGSRAV----NPFPRs 78

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111905 101 WQELYGSYVWQGYWQPEYETANTNNESYiyntqiSAAQFIIDMVKANPNEITIVAAGPMTNLAIALSIWPDLAKNTKSLV 180
Cdd:cd02647  79 WRRDAAFSVDHLPILNERYTVETPLAEE------TAQLVLIEKIKASLEPVTLLVTGPLTNLARALDSDPDISSNIEEVY 152

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111905 181 IMGGYVDsqiaqVTGGDFL--NDMYSDFNLFMEPEAAQTAITADWPELIIAGNITSQVYPSQSLYNGIIARAGGMANIES 258
Cdd:cd02647 153 IMGGGVD-----APGNVFTppSNGTAEFNIFWDPLAAKTVFDSGLKITLVPLDATNTVPLTREFLETDRQRFAAQRLPAS 227

                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 19111905 259 D---SGLSYAKQFVGNGTlpsgsFPFWDEVASAIAAWPEIVNSSYDAYVSVDTAYDS 312
Cdd:cd02647 228 DlagQGYALVKPLEFNST-----YYMWDVLTTLVLGAKEVDNTKESLILEVDTDGLS 279
nuc_hydro cd00455
nuc_hydro: Nucleoside hydrolases. Nucleoside hydrolases cleave the N-glycosidic bond in ...
 27-308 3.73e-22

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: 95.47  E-value: 3.73e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111905  27 VIIDNDGLTD--LQVLFALQAKQ-QILGVTAIYGDYTLDDSLFLASDVLS-TGNLTycIPSFAGAAQPLLRTNNTFQiwQ 102
Cdd:cd00455   1 VILDTDPGIDdaFALMYALLHPEiELVGIVATYGNVTLEQATQNAAYLLElLGRLD--IPVYAGATRPLTGEIPAAY--P 76

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111905 103 ELYGSYVwQGYWQPEYETANTnnesyiyntqISAAQFIIDMVKANPNEITIVAAGPMTNLAIALSIWPDLAKNTKSLVIM 182
Cdd:cd00455  77 EIHGEGG-LGLPIPPIIEADD----------PEAVQLLIDLIRKYPDEITIVALGPLTNLAMAFILDPDIKDRVKEIVIM 145

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111905 183 GGYVDsqiaqVTGgdflN-DMYSDFNLFMEPEAAQTAITADWPELIIAGNITSQVYPSQSLYNGIIARAGGMANIESDSG 261
Cdd:cd00455 146 GGAFL-----VPG----NvTPVAEANFYGDPEAANIVFNSAKNLTIVPLDVTNQAVLTPPMVERIFEQGTSIGLLIKPMI 216

                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*...
gi 19111905 262 LSYAKqfvgNGTLPSGS-FPFWDEVASAIAAWPEIVNSSYdAYVSVDT 308
Cdd:cd00455 217 DYYYK----AYQKPGIEgSPIHDPLAVAYLLNPSMFDYSK-VPVDVDT 259
rihB PRK09955
ribosylpyrimidine nucleosidase;
23-316 6.18e-20

ribosylpyrimidine nucleosidase;


Pssm-ID: 182166 [Multi-domain]  Cd Length: 313  Bit Score: 89.24  E-value: 6.18e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111905   23 AASKVIIDNDGLTDLQVLFALQAKQ---QILGVTAIYGDYTLDDSLFLASDVLSTGNLTycIPSFAGAAQPLLRTNntfQ 99
Cdd:PRK09955   2 EKRKIILDCDPGHDDAIAMMMAAKHpaiDLLGITIVAGNQTLDKTLINGLNVCQKLEIN--VPVYAGMPQPIMRQQ---I 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111905  100 IWQELYGSYVWQGywqPEYETANTNNESyiyntqISAAQFIIDMVKANPNEITIVAAGPMTNLAIALSIWPDLAKNTKSL 179
Cdd:PRK09955  77 VADNIHGETGLDG---PVFEPLTRQAES------THAVKYIIDTLMASDGDITLVPVGPLSNIAVAMRMQPAILPKIREI 147

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111905  180 VIMGGYVDSqiaqvtgGDFLNDmySDFNLFMEPEAAQTAITADWPELIIAGNITSQVYPSQSlyngIIAR---AGGMA-N 255
Cdd:PRK09955 148 VLMGGAYGT-------GNFTPS--AEFNIFADPEAARVVFTSGVPLVMMGLDLTNQTVCTPD----VIARmerAGGPAgE 214

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 19111905  256 IESD-SGLSYAKQFVGNGtLPSGsfPFWDEVASAIAAWPEIVNSSyDAYVSVDTAyDSPFYG 316
Cdd:PRK09955 215 LFSDiMNFTLKTQFENYG-LAGG--PVHDATCIGYLINPDGIKTQ-EMYVEVDVN-SGPCYG 271
PLN02717 PLN02717
uridine nucleosidase
 26-237 3.39e-18

uridine nucleosidase


Pssm-ID: 178319 [Multi-domain]  Cd Length: 316  Bit Score: 84.27  E-value: 3.39e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111905   26 KVIIDND-GLTD-LQVLFALQAKQ-QILGVTAIYGDYTLDDSlflasdvlsTGN-LTYC-------IPSFAGAAQPLLRT 94
Cdd:PLN02717   2 KLIIDTDpGIDDaMAILMALRSPEvEVIGLTTIFGNVTTKLA---------TRNaLHLLemagrpdVPVAEGSHEPLKGG 72

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111905   95 NNTfQIWQELYGSyvwQGYwqpeyetANTN-NESYIYNTQISAAQFIIDMVKANPNEITIVAAGPMTNLAIALSIWPDLA 173
Cdd:PLN02717  73 TKP-RIADFVHGS---DGL-------GNTNlPPPKGKKIEKSAAEFLVEKVSEYPGEVTVVALGPLTNLALAIKLDPSFA 141

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 19111905  174 KNTKSLVIMGGyvdsqiAQVTGGDfLNDMySDFNLFMEPEAAQTAITADWPELIIAGNITSQVY 237
Cdd:PLN02717 142 KKVGQIVVLGG------AFFVNGN-VNPA-AEANIFGDPEAADIVFTSGADITVVGINVTTQVV 197
nuc_hydro_3 cd02653
NH_3: A subgroup of nucleoside hydrolases. This group contains eukaryotic and bacterial ...
 26-221 2.49e-14

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: 73.18  E-value: 2.49e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111905  26 KVIIDND-GLTD-LQVLFALQAKQ-QILGVTAIYGDYTLDDSLFLASDVLSTGNLTyCIPSFAGAAQPL---LRTNntfq 99
Cdd:cd02653   1 KVIIDCDpGIDDaLALLYLLASPDlDVVGITTTAGNVPVEQVAANALGVLELLGRT-DIPVYLGADKPLagpLTTA---- 75

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111905 100 iwQELYGSyvwQGYWQPEYETANtnnesyIYNTQISAAQFIIDMVKANPnEITIVAAGPMTNLAIALSIWPDLAKNTKSL 179
Cdd:cd02653  76 --QDTHGP---DGLGYAELPAST------RTLSDESAAQAWVDLARAHP-DLIGLATGPLTNLALALREEPELPRLLRRL 143

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....
gi 19111905 180 VIMGGYVDSQ--IAQVtggdflndmySDFNLFMEPEAAQTAITA 221
Cdd:cd02653 144 VIMGGAFNSRgnTSPV----------AEWNYWVDPEAAKEVLAA 177
PRK10768 PRK10768
ribonucleoside hydrolase RihC; Provisional
 81-216 2.56e-11

ribonucleoside hydrolase RihC; Provisional


Pssm-ID: 182713 [Multi-domain]  Cd Length: 304  Bit Score: 63.78  E-value: 2.56e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111905   81 IPSFAGAAQPLLRTnntFQIWQELYGSYVWQGYwqpEYETANTNNESyiyntqISAAQFIIDMVKANPNEITIVAAGPMT 160
Cdd:PRK10768  60 VPVAQGAAKPLVRP---LRDAASVHGESGMEGY---DFPEHTRKPLS------IPAVEAMRDALMNAPEPVTLVAIGPLT 127

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 19111905  161 NLAIALSIWPDLAKNTKSLVIMGGyvdsqiaQVTGGDFlnDMYSDFNLFMEPEAAQ 216
Cdd:PRK10768 128 NIALLLSTYPEVKPYIKRIVLMGG-------SAGRGNV--TPNAEFNIAVDPEAAA 174
rihA PRK10443
ribonucleoside hydrolase 1; Provisional
 24-235 7.36e-11

ribonucleoside hydrolase 1; Provisional


Pssm-ID: 182465 [Multi-domain]  Cd Length: 311  Bit Score: 62.76  E-value: 7.36e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111905   24 ASKVIIDND-GLTD-LQVLFALQAKQ-QILGVTAIYGDYTLDDSLFLASDVLSTGNLTYcIPSFAGAAQPLLRTnntFQI 100
Cdd:PRK10443   2 ALPIILDCDpGHDDaIALVLALASPElDVKAVTTSAGNQTPEKTLRNALRMLTLLNRTD-IPVAGGAVKPLMRE---LII 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111905  101 WQELYGSYVWQGYWQPEYETANTNnesyiyntqISAAQFIIDMVKANPNEITIVAAGPMTNLAIALSIWPDLAKNTKSLV 180
Cdd:PRK10443  78 ADNVHGESGLDGPALPEPTFAPQN---------CTAVELMAKTLRESAEPVTLVSTGPQTNVALLLASHPELHSKIARIV 148

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 19111905  181 IMGGYVDSQIAQVTggdflndmySDFNLFMEPEAAQTAITADWPeLIIAG-NITSQ 235
Cdd:PRK10443 149 IMGGAMGLGNWTPA---------AEFNIYVDPEAAEIVFQSGIP-IVMAGlDVTHK 194
nuc_hydro_1 cd02648
NH_1: A subgroup of nucleoside hydrolases. This group contains fungal proteins similar to ...
 26-219 6.93e-09

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: 56.82  E-value: 6.93e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111905  26 KVIIDND-GLTD-LQVLFALQAKQQ--ILGVTAIYGDYTLDDSL--------FLASDVLSTGNLTYCIPSF-AGAAQPLL 92
Cdd:cd02648   3 PIIIDTDpGVDDvLAILLALSSPEEvdVALISLTFGNTTLDHALrnvlrlfhVLERERAWRATPGVRYRAFsADAEKPIV 82

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111905  93 RTNNTFQIWQELYGSYVWQG-------YWQPEY----ETANTNNESYIYNTQISAAQFIIDMVKANPNE-ITIVAAGPMT 160
Cdd:cd02648  83 ASGSDQPLEGERLTASYFHGrdglsgvHWLHPDftpvETWIPEIVAPLTPSDKPAYDVILDILREEPDHtVTIAALGPLT 162

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 19111905 161 NLAIALSIWPDLAKNTKSLVIMGGYVD--SQIAQVtggdflndmySDFNLFMEPEAAQTAI 219
Cdd:cd02648 163 NLAAAARKDPETFAKVGEVVVMGGAIDvpGNTSPV----------AEFNCFADPYAAAVVI 213
PTZ00313 PTZ00313
inosine-adenosine-guanosine-nucleoside hydrolase; Provisional
 131-220 1.47e-05

inosine-adenosine-guanosine-nucleoside hydrolase; Provisional


Pssm-ID: 140334 [Multi-domain]  Cd Length: 326  Bit Score: 46.39  E-value: 1.47e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111905  131 NTQISAAQFIIDMVKANPNEITIVAAGPMTNLAIALSIW-PDLAKNTKSLVIMGGYVDsqiaqVTGGDFL--NDMYSDFN 207
Cdd:PTZ00313 112 NEALVGEELLADLVMSSPEKVTICVTGPLSNVAWCIEKYgEEFTKKVEECVIMGGAVD-----VGGNVFLpgTDGSAEWN 186

                         90
                 ....*....|...
gi 19111905  208 LFMEPEAAQTAIT 220
Cdd:PTZ00313 187 IYWDPPAAKTVLM 199
 
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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