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Conserved domains on  [gi|489709865|ref|WP_003614002|]
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MULTISPECIES: nucleoside hydrolase [Lactobacillus]

Protein Classification

nucleoside hydrolase( domain architecture ID 10119093)

nucleoside hydrolase cleaves the N-glycosidic bond in nucleosides to generate ribose and the respective base, similar to Bacillus anthracis inosine-uridine preferring nucleoside hydrolase

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
nuc_hydro_TvIAG cd02647
nuc_hydro_ TvIAG: Nucleoside hydrolases similar to the Inosine-adenosine-guanosine-preferring ...
 2-307 3.22e-145

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: 411.04  E-value: 3.22e-145
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489709865   2 KNFYLNHDSNMDDFTSLLLMLL--APDIKLIGVGVTDADGYVEPGVSASRKLIDRFNQRgDKLEVAKSDSRAVHQFPEAW 79
Cdd:cd02647    1 KNVIFDHDGNVDDLVALLLLLKneKVDLKGIGVSGIDADCYVEPAVSVTRKLIDRLGQR-DAIPVGKGGSRAVNPFPRSW 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489709865  80 RVSA-FSVDHFPILNEKGTVETPVAAKPAHLDMIDKIHAADGPVTLVFTGPLTDLARALEIDPSIQDKIEELYWMGGSLN 158
Cdd:cd02647   80 RRDAaFSVDHLPILNERYTVETPLAEETAQLVLIEKIKASLEPVTLLVTGPLTNLARALDSDPDISSNIEEVYIMGGGVD 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489709865 159 AHGNVYAPCADGTQEWNAWWDPEACKTVWDSKIKIQQVGLESTEELPLTDEM----RQHFASNRKyPAFEFLGYVYALVN 234
Cdd:cd02647  160 APGNVFTPPSNGTAEFNIFWDPLAAKTVFDSGLKITLVPLDATNTVPLTREFletdRQRFAAQRL-PASDLAGQGYALVK 238

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 489709865 235 SFEVDSTYYLWDVLTTMSALYPEIATTRNTK-SDVYTDGDRAARFFETENGRPMTLVTSANYDKFWERFDDLCE 307
Cdd:cd02647  239 PLEFNSTYYMWDVLTTLVLGAKEVDNTKESLiLEVDTDGLSAGQTVTSPNGRPLTLVTSNNSYGSNRFFDDYLE 312
 
Name Accession Description Interval E-value
nuc_hydro_TvIAG cd02647
nuc_hydro_ TvIAG: Nucleoside hydrolases similar to the Inosine-adenosine-guanosine-preferring ...
 2-307 3.22e-145

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: 411.04  E-value: 3.22e-145
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489709865   2 KNFYLNHDSNMDDFTSLLLMLL--APDIKLIGVGVTDADGYVEPGVSASRKLIDRFNQRgDKLEVAKSDSRAVHQFPEAW 79
Cdd:cd02647    1 KNVIFDHDGNVDDLVALLLLLKneKVDLKGIGVSGIDADCYVEPAVSVTRKLIDRLGQR-DAIPVGKGGSRAVNPFPRSW 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489709865  80 RVSA-FSVDHFPILNEKGTVETPVAAKPAHLDMIDKIHAADGPVTLVFTGPLTDLARALEIDPSIQDKIEELYWMGGSLN 158
Cdd:cd02647   80 RRDAaFSVDHLPILNERYTVETPLAEETAQLVLIEKIKASLEPVTLLVTGPLTNLARALDSDPDISSNIEEVYIMGGGVD 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489709865 159 AHGNVYAPCADGTQEWNAWWDPEACKTVWDSKIKIQQVGLESTEELPLTDEM----RQHFASNRKyPAFEFLGYVYALVN 234
Cdd:cd02647  160 APGNVFTPPSNGTAEFNIFWDPLAAKTVFDSGLKITLVPLDATNTVPLTREFletdRQRFAAQRL-PASDLAGQGYALVK 238

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 489709865 235 SFEVDSTYYLWDVLTTMSALYPEIATTRNTK-SDVYTDGDRAARFFETENGRPMTLVTSANYDKFWERFDDLCE 307
Cdd:cd02647  239 PLEFNSTYYMWDVLTTLVLGAKEVDNTKESLiLEVDTDGLSAGQTVTSPNGRPLTLVTSNNSYGSNRFFDDYLE 312
URH1 COG1957
Inosine-uridine nucleoside N-ribohydrolase [Nucleotide transport and metabolism]; ...
 1-305 4.18e-69

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: 217.33  E-value: 4.18e-69
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489709865   1 MKNFYLNHDSNMDDFTSLLLMLLAPDIKLIGVGVTDADGYVEPGVSASRKLIDRFNQrgDKLEVAKSDSRA-VHQFPEAW 79
Cdd:COG1957    2 MRKVIIDTDPGIDDALALLLALASPEIDLLGITTVAGNVPLEQTTRNALKLLELAGR--TDVPVAAGAARPlVRPLVTAE 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489709865  80 RV---SAFSVDHFPIlnekgtVETPVAAKPAHLDMIDKIHAADGPVTLVFTGPLTDLARALEIDPSIQDKIEELYWMGGS 156
Cdd:COG1957   80 HVhgeDGLGGVDLPE------PTRPPEPEHAVDFIIETLRAAPGEVTLVALGPLTNLALALRKDPELAERIKRIVIMGGA 153

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489709865 157 LNAHGNVyAPCAdgtqEWNAWWDPEACKTVWDSKIKIQQVGLESTEELPLTDEMRQHFASnRKYPAFEFLGYVYALVNSF 236
Cdd:COG1957  154 FFVPGNV-TPVA----EFNIYVDPEAAKIVFASGIPITMVGLDVTHQALLTPEDLARLAA-LGTPLGRFLADLLDFYLDF 227

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489709865 237 EVDS----TYYLWDVLTTMSALYPEIATTRNTKSDVYTDG---------DRAARFFETENgrpMTLVTSANYDKFWERFD 303
Cdd:COG1957  228 YRERygldGCPLHDPLAVAYLLDPELFTTRPAPVDVETDGeltrgqtvvDWRGVTGRPPN---ARVALDVDAERFLDLLL 304


                 ..
gi 489709865 304 DL 305
Cdd:COG1957  305 ER 306
IU_nuc_hydro pfam01156
Inosine-uridine preferring nucleoside hydrolase;
5-300 3.07e-47

Inosine-uridine preferring nucleoside hydrolase;


Pssm-ID: 460086 [Multi-domain]  Cd Length: 253  Bit Score: 159.30  E-value: 3.07e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489709865    5 YLNHDSNMDDFTSLLLMLLAPDIKLIGVGVTDADGYVEPGVSASRKLidrfnqrgdkLEVAKSDsravhqfpeawrvsaf 84
Cdd:pfam01156   2 IIDTDPGIDDALALLLALASPEIELLGITTVAGNVSLEQTTRNALRL----------LELGGRD---------------- 55

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489709865   85 svdhfpilnekgtvETPVAAKpahldmiDKIHAAdGPVTLVFTGPLTDLARALEIDPSIQDKIEELYWMGGSLNAHGNVy 164
Cdd:pfam01156  56 --------------DIPVYAG-------EAIREP-GEVTLVATGPLTNLALALRLDPELAKKIKELVIMGGAFGVRGNV- 112

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489709865  165 APCAdgtqEWNAWWDPEACKTVWDSKIKIQQVGLESTEELPLTDEMRQHFASNRKYPA------FEFLGYVYALVNSFEv 238
Cdd:pfam01156 113 TPAA----EFNIFVDPEAAKIVFTSGLPITMVPLDVTHQALLTPEDLERLAALGTPLGrfladlLRFYAEFYRERFGID- 187

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 489709865  239 dsTYYLWDVLTTMSALYPEIATTRNTKSDVYTDGD------RAARFFETENGRPMTLVTSANYDKFWE 300
Cdd:pfam01156 188 --GPPLHDPLAVAVALDPELFTTRRLNVDVETTGGltrgqtVVDDRGGWGKPPNVRVATDVDVDRFWE 253
PTZ00313 PTZ00313
inosine-adenosine-guanosine-nucleoside hydrolase; Provisional
 2-300 6.75e-45

inosine-adenosine-guanosine-nucleoside hydrolase; Provisional


Pssm-ID: 140334 [Multi-domain]  Cd Length: 326  Bit Score: 155.41  E-value: 6.75e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489709865   2 KNFYLNHDSNMDDFTSLLLMLLAPD-IKLIGVGVTDADGYVEPGVSASRKLIDRFNQRGDK--LEVAKSDSRAVHQFPEA 78
Cdd:PTZ00313   3 KPVILDHDGNHDDLVALALLLGNPEkVKVIGCICTDADCFVDDAFNVTGKLMCMMHAREATplFPIGKSSFKGVNPFPSE 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489709865  79 WRVSAFSVDHFPILNEKGTVETPVAAKP---AHLD---MIDKIHAADGPVTLVFTGPLTDLARALE-IDPSIQDKIEELY 151
Cdd:PTZ00313  83 WRWSAKNMDDLPCLNIPEHVAIWEKLKPeneALVGeelLADLVMSSPEKVTICVTGPLSNVAWCIEkYGEEFTKKVEECV 162

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489709865 152 WMGGSLNAHGNVYAPCADGTQEWNAWWDPEACKTVWD-SKIKIQQVGLESTEELPLTDEMRQHFASNRKYPAFEFLGYVY 230
Cdd:PTZ00313 163 IMGGAVDVGGNVFLPGTDGSAEWNIYWDPPAAKTVLMcPHIRKVLFSLDSTNSVPVTSEVVKKFGAQNKYLLSQFVGSTW 242

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 489709865 231 ALVNSFEV---DSTYYLWDVLTTMSALYPEIATTRNTKSDV-YTDGDRAARFFETENGRPMTLVT-SANYDKFWE 300
Cdd:PTZ00313 243 AMCTHHELlrpGDGYYAWDVLTAAYVIERNLAELEPVPLEVvVEKAKNEGRTRRAAEGAACTYVAkNTNAELFYD 317
 
Name Accession Description Interval E-value
nuc_hydro_TvIAG cd02647
nuc_hydro_ TvIAG: Nucleoside hydrolases similar to the Inosine-adenosine-guanosine-preferring ...
 2-307 3.22e-145

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: 411.04  E-value: 3.22e-145
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489709865   2 KNFYLNHDSNMDDFTSLLLMLL--APDIKLIGVGVTDADGYVEPGVSASRKLIDRFNQRgDKLEVAKSDSRAVHQFPEAW 79
Cdd:cd02647    1 KNVIFDHDGNVDDLVALLLLLKneKVDLKGIGVSGIDADCYVEPAVSVTRKLIDRLGQR-DAIPVGKGGSRAVNPFPRSW 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489709865  80 RVSA-FSVDHFPILNEKGTVETPVAAKPAHLDMIDKIHAADGPVTLVFTGPLTDLARALEIDPSIQDKIEELYWMGGSLN 158
Cdd:cd02647   80 RRDAaFSVDHLPILNERYTVETPLAEETAQLVLIEKIKASLEPVTLLVTGPLTNLARALDSDPDISSNIEEVYIMGGGVD 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489709865 159 AHGNVYAPCADGTQEWNAWWDPEACKTVWDSKIKIQQVGLESTEELPLTDEM----RQHFASNRKyPAFEFLGYVYALVN 234
Cdd:cd02647  160 APGNVFTPPSNGTAEFNIFWDPLAAKTVFDSGLKITLVPLDATNTVPLTREFletdRQRFAAQRL-PASDLAGQGYALVK 238

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 489709865 235 SFEVDSTYYLWDVLTTMSALYPEIATTRNTK-SDVYTDGDRAARFFETENGRPMTLVTSANYDKFWERFDDLCE 307
Cdd:cd02647  239 PLEFNSTYYMWDVLTTLVLGAKEVDNTKESLiLEVDTDGLSAGQTVTSPNGRPLTLVTSNNSYGSNRFFDDYLE 312
URH1 COG1957
Inosine-uridine nucleoside N-ribohydrolase [Nucleotide transport and metabolism]; ...
 1-305 4.18e-69

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: 217.33  E-value: 4.18e-69
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489709865   1 MKNFYLNHDSNMDDFTSLLLMLLAPDIKLIGVGVTDADGYVEPGVSASRKLIDRFNQrgDKLEVAKSDSRA-VHQFPEAW 79
Cdd:COG1957    2 MRKVIIDTDPGIDDALALLLALASPEIDLLGITTVAGNVPLEQTTRNALKLLELAGR--TDVPVAAGAARPlVRPLVTAE 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489709865  80 RV---SAFSVDHFPIlnekgtVETPVAAKPAHLDMIDKIHAADGPVTLVFTGPLTDLARALEIDPSIQDKIEELYWMGGS 156
Cdd:COG1957   80 HVhgeDGLGGVDLPE------PTRPPEPEHAVDFIIETLRAAPGEVTLVALGPLTNLALALRKDPELAERIKRIVIMGGA 153

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489709865 157 LNAHGNVyAPCAdgtqEWNAWWDPEACKTVWDSKIKIQQVGLESTEELPLTDEMRQHFASnRKYPAFEFLGYVYALVNSF 236
Cdd:COG1957  154 FFVPGNV-TPVA----EFNIYVDPEAAKIVFASGIPITMVGLDVTHQALLTPEDLARLAA-LGTPLGRFLADLLDFYLDF 227

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489709865 237 EVDS----TYYLWDVLTTMSALYPEIATTRNTKSDVYTDG---------DRAARFFETENgrpMTLVTSANYDKFWERFD 303
Cdd:COG1957  228 YRERygldGCPLHDPLAVAYLLDPELFTTRPAPVDVETDGeltrgqtvvDWRGVTGRPPN---ARVALDVDAERFLDLLL 304


                 ..
gi 489709865 304 DL 305
Cdd:COG1957  305 ER 306
IU_nuc_hydro pfam01156
Inosine-uridine preferring nucleoside hydrolase;
5-300 3.07e-47

Inosine-uridine preferring nucleoside hydrolase;


Pssm-ID: 460086 [Multi-domain]  Cd Length: 253  Bit Score: 159.30  E-value: 3.07e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489709865    5 YLNHDSNMDDFTSLLLMLLAPDIKLIGVGVTDADGYVEPGVSASRKLidrfnqrgdkLEVAKSDsravhqfpeawrvsaf 84
Cdd:pfam01156   2 IIDTDPGIDDALALLLALASPEIELLGITTVAGNVSLEQTTRNALRL----------LELGGRD---------------- 55

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489709865   85 svdhfpilnekgtvETPVAAKpahldmiDKIHAAdGPVTLVFTGPLTDLARALEIDPSIQDKIEELYWMGGSLNAHGNVy 164
Cdd:pfam01156  56 --------------DIPVYAG-------EAIREP-GEVTLVATGPLTNLALALRLDPELAKKIKELVIMGGAFGVRGNV- 112

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489709865  165 APCAdgtqEWNAWWDPEACKTVWDSKIKIQQVGLESTEELPLTDEMRQHFASNRKYPA------FEFLGYVYALVNSFEv 238
Cdd:pfam01156 113 TPAA----EFNIFVDPEAAKIVFTSGLPITMVPLDVTHQALLTPEDLERLAALGTPLGrfladlLRFYAEFYRERFGID- 187

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 489709865  239 dsTYYLWDVLTTMSALYPEIATTRNTKSDVYTDGD------RAARFFETENGRPMTLVTSANYDKFWE 300
Cdd:pfam01156 188 --GPPLHDPLAVAVALDPELFTTRRLNVDVETTGGltrgqtVVDDRGGWGKPPNVRVATDVDVDRFWE 253
PTZ00313 PTZ00313
inosine-adenosine-guanosine-nucleoside hydrolase; Provisional
 2-300 6.75e-45

inosine-adenosine-guanosine-nucleoside hydrolase; Provisional


Pssm-ID: 140334 [Multi-domain]  Cd Length: 326  Bit Score: 155.41  E-value: 6.75e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489709865   2 KNFYLNHDSNMDDFTSLLLMLLAPD-IKLIGVGVTDADGYVEPGVSASRKLIDRFNQRGDK--LEVAKSDSRAVHQFPEA 78
Cdd:PTZ00313   3 KPVILDHDGNHDDLVALALLLGNPEkVKVIGCICTDADCFVDDAFNVTGKLMCMMHAREATplFPIGKSSFKGVNPFPSE 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489709865  79 WRVSAFSVDHFPILNEKGTVETPVAAKP---AHLD---MIDKIHAADGPVTLVFTGPLTDLARALE-IDPSIQDKIEELY 151
Cdd:PTZ00313  83 WRWSAKNMDDLPCLNIPEHVAIWEKLKPeneALVGeelLADLVMSSPEKVTICVTGPLSNVAWCIEkYGEEFTKKVEECV 162

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489709865 152 WMGGSLNAHGNVYAPCADGTQEWNAWWDPEACKTVWD-SKIKIQQVGLESTEELPLTDEMRQHFASNRKYPAFEFLGYVY 230
Cdd:PTZ00313 163 IMGGAVDVGGNVFLPGTDGSAEWNIYWDPPAAKTVLMcPHIRKVLFSLDSTNSVPVTSEVVKKFGAQNKYLLSQFVGSTW 242

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 489709865 231 ALVNSFEV---DSTYYLWDVLTTMSALYPEIATTRNTKSDV-YTDGDRAARFFETENGRPMTLVT-SANYDKFWE 300
Cdd:PTZ00313 243 AMCTHHELlrpGDGYYAWDVLTAAYVIERNLAELEPVPLEVvVEKAKNEGRTRRAAEGAACTYVAkNTNAELFYD 317
nuc_hydro cd00455
nuc_hydro: Nucleoside hydrolases. Nucleoside hydrolases cleave the N-glycosidic bond in ...
 6-302 5.46e-43

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: 149.40  E-value: 5.46e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489709865   6 LNHDSNMDDFTSLLLMLLAPDIKLIGVGVTDADGYVEPGVSASRKLIDRFNQRGdkLEVAKSDSRAVHQFPEAWRVSA-F 84
Cdd:cd00455    3 LDTDPGIDDAFALMYALLHPEIELVGIVATYGNVTLEQATQNAAYLLELLGRLD--IPVYAGATRPLTGEIPAAYPEIhG 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489709865  85 SVDHFPILNEKGTVETPvaakPAHLDMIDKIHAADGPVTLVFTGPLTDLARALEIDPSIQDKIEELYWMGGSLNAHGNVY 164
Cdd:cd00455   81 EGGLGLPIPPIIEADDP----EAVQLLIDLIRKYPDEITIVALGPLTNLAMAFILDPDIKDRVKEIVIMGGAFLVPGNVT 156

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489709865 165 ApcadgTQEWNAWWDPEACKTVWDSKIKIQQVGLESTEELPLTDEMRQHFASNRKYPAF---EFLGYvYALVNSFEVDST 241
Cdd:cd00455  157 P-----VAEANFYGDPEAANIVFNSAKNLTIVPLDVTNQAVLTPPMVERIFEQGTSIGLlikPMIDY-YYKAYQKPGIEG 230

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 489709865 242 YYLWDVLTTMSALYPEIATTRNTKSDVYTDGD------RAARFFETENGrpMTLVTSANYDKFWERF 302
Cdd:cd00455  231 SPIHDPLAVAYLLNPSMFDYSKVPVDVDTDGLtrgqtiADFRENPGNGV--TRVAVNLDYPDFIELI 295
nuc_hydro_CeIAG cd02649
nuc_hydro_CeIAG: Nucleoside hydrolases similar to the inosine-adenosine-guanosine-preferring ...
 13-290 1.62e-27

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: 108.89  E-value: 1.62e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489709865  13 DDFTSLLLMLLAPDIKLIGVGVTDADGYVEPGVSASRKLIDRfnqrGDKLEV---AKSDSRAVHQFPEAWRVsaFSVDHF 89
Cdd:cd02649   12 DDAWALLMALASPNVEVLAITCVHGNTNVEQVVKNALRVLEA----CGRRDIpvyRGASKPLLGPGPTAAYF--HGKDGF 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489709865  90 pilNEKGTVETPVAAKP----AHLDMIDKIHAADGPVTLVFTGPLTDLARALEIDPSIQDKIEELYWMGGSLNAHGNVyA 165
Cdd:cd02649   86 ---GDVGFPEPKDELELqkehAVDAIIRLVREYPGEITLVALGPLTNLALAYRLDPSLPQKIKRLYIMGGNREGVGNT-T 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489709865 166 PCAdgtqEWNAWWDPEACKTVWDSKIK-IQQVGLEST---EELPLTDEMRQHFASNRKYPAFEFLGYVYALVNSFEVDST 241
Cdd:cd02649  162 PAA----EFNFHVDPEAAHIVLNSFGCpITIVPWETTllaFPLDWEFEDKWANRLEKALFAESLNRREYAFASEGLGGDG 237

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|
gi 489709865 242 YYLWDVLTTMSALYPEIATTRNT-KSDVYTDGdraarffetENGRPMTLV 290
Cdd:cd02649  238 WVPCDALAVAAALDPSIITRRLTyAVDVELHG---------ELTRGQMVV 278
nuc_hydro_CaPnhB cd02650
NH_hydro_CaPnhB: A subgroup of nucleoside hydrolases similar to Corynebacterium ammoniagenes ...
 9-272 1.14e-25

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: 103.90  E-value: 1.14e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489709865   9 DSNMDDFTSLLLMLLAPDIKLIGVGVTDADGYVEPGVSASRKLIDRFNqRGDkLEVAKSDSRAVHQFPEawRVSAFSvdH 88
Cdd:cd02650    7 DPGIDDAMALAYALAHPDVDLIGVTTVYGNVTIETATRNALALLELFG-RPD-VPVAEGAAKPLTRPPF--RIATFV--H 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489709865  89 FPilNEKGTVE-----TPVAAKPAHLDMIDKIHAADGPVTLVFTGPLTDLARALEIDPSIQDKIEELYWMGGSLNAHGNV 163
Cdd:cd02650   81 GD--NGLGDVElpappRQPEDESAADFLIELANEYPGELTLVAVGPLTNLALALARDPDFAKLVKQVVVMGGAFTVPGNV 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489709865 164 yAPCAdgtqEWNAWWDPEACKTVWDSKIKIQQVGLESTEELPLTDEMRQHFAsNRKYPAFEFLG-----YVYALVNSFEV 238
Cdd:cd02650  159 -TPAA----EANIHGDPEAADIVFTAGADLTMVGLDVTTQTLLTREDLDELR-DSGGKAGQFLAdmldyYIDFYQESPGL 232

                        250       260       270
                 ....*....|....*....|....*....|....
gi 489709865 239 DSTyYLWDVLTTMSALYPEIATTRNTKSDVYTDG 272
Cdd:cd02650  233 RGC-ALHDPLAVAAAVDPSLFTTREGVVRVETEG 265
nuc_hydro_IU_UC_XIUA cd02651
nuc_hydro_IU_UC_XIUA: inosine-uridine preferring, ...
 111-272 4.64e-25

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: 101.85  E-value: 4.64e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489709865 111 MIDKIHAADGPVTLVFTGPLTDLARALEIDPSIQDKIEELYWMGGSLNaHGNVyAPCAdgtqEWNAWWDPEACKTVWDSK 190
Cdd:cd02651  105 IIDTLRASPEPITLVATGPLTNIALLLRKYPELAERIKEIVLMGGALG-RGNI-TPAA----EFNIFVDPEAAKIVFNSG 178

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489709865 191 IKIQQVGLESTEELPLTDEMRQHF--ASNRKYPAFEFLGYVYALVNSFEVDSTYYLWDVLTTMSALYPEIATTRNTKSDV 268
Cdd:cd02651  179 IPITMVPLDVTHKALATPEVIERIraLGNPVGKMLAELLDFFAETYGSAFTEGPPLHDPCAVAYLLDPELFTTKRANVDV 258


                 ....
gi 489709865 269 YTDG 272
Cdd:cd02651  259 ETEG 262
nuc_hydro_3 cd02653
NH_3: A subgroup of nucleoside hydrolases. This group contains eukaryotic and bacterial ...
 9-310 6.65e-23

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: 96.29  E-value: 6.65e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489709865   9 DSNMDDFTSLLLMLLAPDIKLIGVGVTDADGYVEPGVSASRKLIDRFNqRGDkLEVAKSDSravhqFPEAWRVSAFSVDH 88
Cdd:cd02653    7 DPGIDDALALLYLLASPDLDVVGITTTAGNVPVEQVAANALGVLELLG-RTD-IPVYLGAD-----KPLAGPLTTAQDTH 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489709865  89 FPilNEKGTVETPVAAKP-----AHLDMIDKIHAADgPVTLVFTGPLTDLARALEIDPSIQDKIEELYWMGGSLNAHGNV 163
Cdd:cd02653   80 GP--DGLGYAELPASTRTlsdesAAQAWVDLARAHP-DLIGLATGPLTNLALALREEPELPRLLRRLVIMGGAFNSRGNT 156

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489709865 164 YApcadgTQEWNAWWDPEACKTVWD----SKIKIQQVGLESTEELPLTDEMRQHFASN------------RKYpaFEF-- 225
Cdd:cd02653  157 SP-----VAEWNYWVDPEAAKEVLAafggHPVRPTICGLDVTRAVVLTPNLLERLARAkdsvgafiedalRFY--FEFhw 229

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489709865 226 -LGYVYALvnsfevdstyYLWDVLTTMSALYPEIATTRNTKSDVYTDG--------DRAARFFETENGRPMTLVTSANyd 296
Cdd:cd02653  230 aYGHGYGA----------VIHDPLAAAVALNPNLARGRPAYVDVECTGvltgqtvvDWAGFWGKGANAEILTKVDSQD-- 297

                        330
                 ....*....|....
gi 489709865 297 kFWERFDDLCEKAK 310
Cdd:cd02653  298 -FMALFIERVLAIA 310
PRK10768 PRK10768
ribonucleoside hydrolase RihC; Provisional
 96-276 2.78e-18

ribonucleoside hydrolase RihC; Provisional


Pssm-ID: 182713 [Multi-domain]  Cd Length: 304  Bit Score: 83.42  E-value: 2.78e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489709865  96 GTVETPVAAKPAHLDMIDKIHAADGPVTLVFTGPLTDLARALEIDPSIQDKIEELYWMGGSLnAHGNVyAPCAdgtqEWN 175
Cdd:PRK10768  92 PEHTRKPLSIPAVEAMRDALMNAPEPVTLVAIGPLTNIALLLSTYPEVKPYIKRIVLMGGSA-GRGNV-TPNA----EFN 165

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489709865 176 AWWDPEACKTVWDSKIKIQQVGLESTEELPLTDEMRQHFAS-NRkypAFEFLgyvYALVNSFEVDST---YYLWDVLTTM 251
Cdd:PRK10768 166 IAVDPEAAAIVFRSGIPIVMCGLDVTNQALLTPDYLATLPElNR---TGKML---HALFSHYRSGSMqtgLRMHDVCAIA 239

                        170       180
                 ....*....|....*....|....*
gi 489709865 252 SALYPEIATTRNTKSDVYTDGDRAA 276
Cdd:PRK10768 240 YLLRPELFTLKPCFVDVETQGEFTA 264
PLN02717 PLN02717
uridine nucleosidase
 111-273 5.24e-17

uridine nucleosidase


Pssm-ID: 178319 [Multi-domain]  Cd Length: 316  Bit Score: 80.04  E-value: 5.24e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489709865 111 MIDKIHAADGPVTLVFTGPLTDLARALEIDPSIQDKIEELYWMGGSLNAHGNVyAPCAdgtqEWNAWWDPEACKTVWDSK 190
Cdd:PLN02717 108 LVEKVSEYPGEVTVVALGPLTNLALAIKLDPSFAKKVGQIVVLGGAFFVNGNV-NPAA----EANIFGDPEAADIVFTSG 182

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489709865 191 IKIQQVGLESTEELPLTD----EMRQhfaSNRKYPAF-----EFlgYVYALVNSFEVDSTyYLWDVLTTMSALYPEIATT 261
Cdd:PLN02717 183 ADITVVGINVTTQVVLTDadleELRD---SKGKYAQFlcdicKF--YRDWHRKSYGIDGI-YLHDPTALLAAVRPSLFTY 256

                        170
                 ....*....|..
gi 489709865 262 RNTKSDVYTDGD 273
Cdd:PLN02717 257 KEGVVRVETEGI 268
nuc_hydro_CjNH cd02654
nuc_hydro_CjNH. Nucleoside hydrolases similar to Campylobacter jejuni nucleoside hydrolase. ...
 106-273 2.14e-16

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: 78.36  E-value: 2.14e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489709865 106 PAHLDMIDKIHAADGPVTLVFTGPLTDLARALEIDPSIQDKIEELYWMGGSLNAHGN-VYAPCAdgtQEWNAWWDPEACK 184
Cdd:cd02654  115 PAALFMIEMVRKHPHEVSIVAAGPLTNLALALRIDPDFAPLAKELVIMGGYLDDIGEfVNRHYA---SDFNLIMDPEAAS 191

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489709865 185 TVWDSKIKIQQVGLESTEELPLTDEMRQHFASNRKYpAFEFLGYVYALVNSF-EVDSTYYLWDVLTTMSALYPEIATTRN 263
Cdd:cd02654  192 IVLTAPWKSITIPGNVTNRTCLTPEQIKADDPLRDF-IRETLDLPIDYAKEFvGTGDGLPMWDELASAVALDPELATSSE 270

                        170
                 ....*....|.
gi 489709865 264 TKS-DVYTDGD 273
Cdd:cd02654  271 TFYiDVQTDSD 281
rihA PRK10443
ribonucleoside hydrolase 1; Provisional
 111-209 4.51e-14

ribonucleoside hydrolase 1; Provisional


Pssm-ID: 182465 [Multi-domain]  Cd Length: 311  Bit Score: 71.24  E-value: 4.51e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489709865 111 MIDKIHAADGPVTLVFTGPLTDLARALEIDPSIQDKIEELYWMGGSLNAhGNvYAPCAdgtqEWNAWWDPEACKTVWDSK 190
Cdd:PRK10443 108 MAKTLRESAEPVTLVSTGPQTNVALLLASHPELHSKIARIVIMGGAMGL-GN-WTPAA----EFNIYVDPEAAEIVFQSG 181

                         90
                 ....*....|....*....
gi 489709865 191 IKIQQVGLESTEELPLTDE 209
Cdd:PRK10443 182 IPIVMAGLDVTHKAQIMDE 200
rihB PRK09955
ribosylpyrimidine nucleosidase;
111-203 1.33e-13

ribosylpyrimidine nucleosidase;


Pssm-ID: 182166 [Multi-domain]  Cd Length: 313  Bit Score: 69.98  E-value: 1.33e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489709865 111 MIDKIHAADGPVTLVFTGPLTDLARALEIDPSIQDKIEELYWMGGSLNAhGNvYAPCAdgtqEWNAWWDPEACKTVWDSK 190
Cdd:PRK09955 108 IIDTLMASDGDITLVPVGPLSNIAVAMRMQPAILPKIREIVLMGGAYGT-GN-FTPSA----EFNIFADPEAARVVFTSG 181

                         90
                 ....*....|...
gi 489709865 191 IKIQQVGLESTEE 203
Cdd:PRK09955 182 VPLVMMGLDLTNQ 194
nuc_hydro_1 cd02648
NH_1: A subgroup of nucleoside hydrolases. This group contains fungal proteins similar to ...
 87-188 6.35e-11

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: 62.59  E-value: 6.35e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489709865  87 DHFPILNEKGTVETPVAA--KPAHLDMIDKIHAA-DGPVTLVFTGPLTDLARALEIDPSIQDKIEELYWMGGSLNAHGNV 163
Cdd:cd02648  115 DFTPVETWIPEIVAPLTPsdKPAYDVILDILREEpDHTVTIAALGPLTNLAAAARKDPETFAKVGEVVVMGGAIDVPGNT 194

                         90       100
                 ....*....|....*....|....*
gi 489709865 164 yAPCAdgtqEWNAWWDPEACKTVWD 188
Cdd:cd02648  195 -SPVA----EFNCFADPYAAAVVID 214
nuc_hydro_2 cd02652
NH_2: A subgroup of nucleoside hydrolases. This group contains eukaryotic and bacterial ...
 13-256 6.77e-08

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: 52.89  E-value: 6.77e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489709865  13 DDFTSLLLMLLAPDIKLIGVGVTDADGYVEPGVSAsrklIDRFNQRGDKLEVAKSDSRAVHQFpeawrvsafsvDHFPIL 92
Cdd:cd02652   12 DDALALALAHALQKCDLLAVTITLADASARRAIDA----VNRFYGRGDIPIGADYHGWPEDAK-----------DHAKFL 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489709865  93 NEKGTVETPVAAKPAHLDMIDKIH-----AADGPVTLVFTGPLTDLARALEIDPS-------IQDKIEELYWMGGSLN-A 159
Cdd:cd02652   77 LEGDRLHHDLESAEDALDAVKALRrllasAEDASVTIVSIGPLTNLAALLDADADpltgpelVRQKVKRLVVMGGAFYdP 156

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489709865 160 HGNVYAPcadgtqEWNAWWDPEACKTVWDSK------IKIQQVGLESTEELPL-TDEMRQHFASnrkYPAFEflgyvyal 232
Cdd:cd02652  157 DGNVQHR------EYNFVTDPKAAQRVAGRAqhlgipVRIVWSGYELGEAVSYpHVLVIAHPFN---TPVFA-------- 219

                        250       260
                 ....*....|....*....|....*
gi 489709865 233 vnSFEVDSTYY-LWDVLTTMSALYP 256
Cdd:cd02652  220 --AYWPRSHRRpLWDPLTLLAAVRG 242
 
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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