|
Name |
Accession |
Description |
Interval |
E-value |
| nuc_hydro_TvIAG |
cd02647 |
nuc_hydro_ TvIAG: Nucleoside hydrolases similar to the Inosine-adenosine-guanosine-preferring ... |
3-305 |
3.32e-109 |
|
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: 319.75 E-value: 3.32e-109
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584725277 3 KKVYFNHDGGVDDLVSLFLLLQMENVQL--IGVSTIGADCYLEPSLSASVKIINRFSNED-IQVAPSYERGKNPFPKEWR 79
Cdd:cd02647 1 KNVIFDHDGNVDDLVALLLLLKNEKVDLkgIGVSGIDADCYVEPAVSVTRKLIDRLGQRDaIPVGKGGSRAVNPFPRSWR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584725277 80 MHAFF-MDALPILNEPVKHVASNVSdKEAFEDIIQTLKRQSEKVTLLFTGPLTDLAKALQKDSSIVQYIEKLVWMGGTFL 158
Cdd:cd02647 81 RDAAFsVDHLPILNERYTVETPLAE-ETAQLVLIEKIKASLEPVTLLVTGPLTNLARALDSDPDISSNIEEVYIMGGGVD 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584725277 159 PKGNVEEPEHDGSAEWNAYWDPEAVKIVFDSDIEIDMVALESTNQVPLT----LDVRQRWANERQyTGIDFLGVSYAAVP 234
Cdd:cd02647 160 APGNVFTPPSNGTAEFNIFWDPLAAKTVFDSGLKITLVPLDATNTVPLTreflETDRQRFAAQRL-PASDLAGQGYALVK 238
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 584725277 235 PlthFITNSTYFLWDVLTTAYIGNKDLVHSIEKKVDVISY-GPSQGKTFECKDGRKINV---INHVDNNAFFDYI 305
Cdd:cd02647 239 P---LEFNSTYYMWDVLTTLVLGAKEVDNTKESLILEVDTdGLSAGQTVTSPNGRPLTLvtsNNSYGSNRFFDDY 310
|
|
| URH1 |
COG1957 |
Inosine-uridine nucleoside N-ribohydrolase [Nucleotide transport and metabolism]; ... |
1-308 |
1.98e-78 |
|
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: 241.21 E-value: 1.98e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584725277 1 MTKKVYFNHDGGVDDLVSLFLLLQMENVQLIGVSTIGADCYLEPSLSASVKIINRFSNEDIQVAPSYERgknPFPKEWRM 80
Cdd:COG1957 1 MMRKVIIDTDPGIDDALALLLALASPEIDLLGITTVAGNVPLEQTTRNALKLLELAGRTDVPVAAGAAR---PLVRPLVT 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584725277 81 HAFF--MDALPilNEPVKHVASNVSDKEAFEDIIQTLKRQSEKVTLLFTGPLTDLAKALQKDSSIVQYIEKLVWMGGTFL 158
Cdd:COG1957 78 AEHVhgEDGLG--GVDLPEPTRPPEPEHAVDFIIETLRAAPGEVTLVALGPLTNLALALRKDPELAERIKRIVIMGGAFF 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584725277 159 PKGNVeEPehdgSAEWNAYWDPEAVKIVFDSDIEIDMVALESTNQVPLTLDVRQRWAnERQYTGIDFLGVSYAAVPPLTH 238
Cdd:COG1957 156 VPGNV-TP----VAEFNIYVDPEAAKIVFASGIPITMVGLDVTHQALLTPEDLARLA-ALGTPLGRFLADLLDFYLDFYR 229
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 584725277 239 -FITNSTYFLWDVLTTAYIGNKDLVHSIEKKVDVISYG-PSQGKTFECKDGR-----KINVINHVDNNAFFDYITAL 308
Cdd:COG1957 230 eRYGLDGCPLHDPLAVAYLLDPELFTTRPAPVDVETDGeLTRGQTVVDWRGVtgrppNARVALDVDAERFLDLLLER 306
|
|
| IU_nuc_hydro |
pfam01156 |
Inosine-uridine preferring nucleoside hydrolase; |
5-303 |
1.35e-51 |
|
Inosine-uridine preferring nucleoside hydrolase;
Pssm-ID: 460086 [Multi-domain] Cd Length: 253 Bit Score: 170.47 E-value: 1.35e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584725277 5 VYFNHDGGVDDLVSLFLLLQMENVQLIGVSTIGADCYLEPSLSASVKIINRFSNEDIQVApsyeRGKnpfpkewrmhaff 84
Cdd:pfam01156 1 VIIDTDPGIDDALALLLALASPEIELLGITTVAGNVSLEQTTRNALRLLELGGRDDIPVY----AGE------------- 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584725277 85 mdalpILNEPvkhvasnvsdkeafediiqtlkrqsEKVTLLFTGPLTDLAKALQKDSSIVQYIEKLVWMGGTFLPKGNVE 164
Cdd:pfam01156 64 -----AIREP-------------------------GEVTLVATGPLTNLALALRLDPELAKKIKELVIMGGAFGVRGNVT 113
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584725277 165 EpehdgSAEWNAYWDPEAVKIVFDSDIEIDMVALESTNQVPLTLDVRQRWANERQYTG------IDFLGVSYAAVPPLTH 238
Cdd:pfam01156 114 P-----AAEFNIFVDPEAAKIVFTSGLPITMVPLDVTHQALLTPEDLERLAALGTPLGrfladlLRFYAEFYRERFGIDG 188
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 584725277 239 FItnstyfLWDVLTTAYIGNKDLVHSIEKKVDV-ISYGPSQGKTF-----ECKDGRKINVINHVDNNAFFD 303
Cdd:pfam01156 189 PP------LHDPLAVAVALDPELFTTRRLNVDVeTTGGLTRGQTVvddrgGWGKPPNVRVATDVDVDRFWE 253
|
|
| PTZ00313 |
PTZ00313 |
inosine-adenosine-guanosine-nucleoside hydrolase; Provisional |
1-310 |
1.20e-50 |
|
inosine-adenosine-guanosine-nucleoside hydrolase; Provisional
Pssm-ID: 140334 [Multi-domain] Cd Length: 326 Bit Score: 170.43 E-value: 1.20e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584725277 1 MTKKVYFNHDGGVDDLVSLFLLL-QMENVQLIGVSTIGADCYLEPSLSASVKII----NRFSNEDIQVAPSYERGKNPFP 75
Cdd:PTZ00313 1 MPKPVILDHDGNHDDLVALALLLgNPEKVKVIGCICTDADCFVDDAFNVTGKLMcmmhAREATPLFPIGKSSFKGVNPFP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584725277 76 KEWRMHAFFMDALPILNEPvKHVA-----SNVSDKEAFEDIIQTLKRQS-EKVTLLFTGPLTDLAKALQK-DSSIVQYIE 148
Cdd:PTZ00313 81 SEWRWSAKNMDDLPCLNIP-EHVAiweklKPENEALVGEELLADLVMSSpEKVTICVTGPLSNVAWCIEKyGEEFTKKVE 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584725277 149 KLVWMGGTFLPKGNVEEPEHDGSAEWNAYWDPEAVKIVFD-SDIEIDMVALESTNQVPLTLDVRQRWANERQYTGIDFLG 227
Cdd:PTZ00313 160 ECVIMGGAVDVGGNVFLPGTDGSAEWNIYWDPPAAKTVLMcPHIRKVLFSLDSTNSVPVTSEVVKKFGAQNKYLLSQFVG 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584725277 228 VSYAAVpplTHF---ITNSTYFLWDVLTTAYIGNKDLVHSIEKKVDV-ISYGPSQGKTFECKDGRKIN-VINHVDNNAFF 302
Cdd:PTZ00313 240 STWAMC---THHellRPGDGYYAWDVLTAAYVIERNLAELEPVPLEVvVEKAKNEGRTRRAAEGAACTyVAKNTNAELFY 316
|
....*...
gi 584725277 303 DYITALAK 310
Cdd:PTZ00313 317 DMVLDSAR 324
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| nuc_hydro_TvIAG |
cd02647 |
nuc_hydro_ TvIAG: Nucleoside hydrolases similar to the Inosine-adenosine-guanosine-preferring ... |
3-305 |
3.32e-109 |
|
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: 319.75 E-value: 3.32e-109
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584725277 3 KKVYFNHDGGVDDLVSLFLLLQMENVQL--IGVSTIGADCYLEPSLSASVKIINRFSNED-IQVAPSYERGKNPFPKEWR 79
Cdd:cd02647 1 KNVIFDHDGNVDDLVALLLLLKNEKVDLkgIGVSGIDADCYVEPAVSVTRKLIDRLGQRDaIPVGKGGSRAVNPFPRSWR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584725277 80 MHAFF-MDALPILNEPVKHVASNVSdKEAFEDIIQTLKRQSEKVTLLFTGPLTDLAKALQKDSSIVQYIEKLVWMGGTFL 158
Cdd:cd02647 81 RDAAFsVDHLPILNERYTVETPLAE-ETAQLVLIEKIKASLEPVTLLVTGPLTNLARALDSDPDISSNIEEVYIMGGGVD 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584725277 159 PKGNVEEPEHDGSAEWNAYWDPEAVKIVFDSDIEIDMVALESTNQVPLT----LDVRQRWANERQyTGIDFLGVSYAAVP 234
Cdd:cd02647 160 APGNVFTPPSNGTAEFNIFWDPLAAKTVFDSGLKITLVPLDATNTVPLTreflETDRQRFAAQRL-PASDLAGQGYALVK 238
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 584725277 235 PlthFITNSTYFLWDVLTTAYIGNKDLVHSIEKKVDVISY-GPSQGKTFECKDGRKINV---INHVDNNAFFDYI 305
Cdd:cd02647 239 P---LEFNSTYYMWDVLTTLVLGAKEVDNTKESLILEVDTdGLSAGQTVTSPNGRPLTLvtsNNSYGSNRFFDDY 310
|
|
| URH1 |
COG1957 |
Inosine-uridine nucleoside N-ribohydrolase [Nucleotide transport and metabolism]; ... |
1-308 |
1.98e-78 |
|
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: 241.21 E-value: 1.98e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584725277 1 MTKKVYFNHDGGVDDLVSLFLLLQMENVQLIGVSTIGADCYLEPSLSASVKIINRFSNEDIQVAPSYERgknPFPKEWRM 80
Cdd:COG1957 1 MMRKVIIDTDPGIDDALALLLALASPEIDLLGITTVAGNVPLEQTTRNALKLLELAGRTDVPVAAGAAR---PLVRPLVT 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584725277 81 HAFF--MDALPilNEPVKHVASNVSDKEAFEDIIQTLKRQSEKVTLLFTGPLTDLAKALQKDSSIVQYIEKLVWMGGTFL 158
Cdd:COG1957 78 AEHVhgEDGLG--GVDLPEPTRPPEPEHAVDFIIETLRAAPGEVTLVALGPLTNLALALRKDPELAERIKRIVIMGGAFF 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584725277 159 PKGNVeEPehdgSAEWNAYWDPEAVKIVFDSDIEIDMVALESTNQVPLTLDVRQRWAnERQYTGIDFLGVSYAAVPPLTH 238
Cdd:COG1957 156 VPGNV-TP----VAEFNIYVDPEAAKIVFASGIPITMVGLDVTHQALLTPEDLARLA-ALGTPLGRFLADLLDFYLDFYR 229
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 584725277 239 -FITNSTYFLWDVLTTAYIGNKDLVHSIEKKVDVISYG-PSQGKTFECKDGR-----KINVINHVDNNAFFDYITAL 308
Cdd:COG1957 230 eRYGLDGCPLHDPLAVAYLLDPELFTTRPAPVDVETDGeLTRGQTVVDWRGVtgrppNARVALDVDAERFLDLLLER 306
|
|
| IU_nuc_hydro |
pfam01156 |
Inosine-uridine preferring nucleoside hydrolase; |
5-303 |
1.35e-51 |
|
Inosine-uridine preferring nucleoside hydrolase;
Pssm-ID: 460086 [Multi-domain] Cd Length: 253 Bit Score: 170.47 E-value: 1.35e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584725277 5 VYFNHDGGVDDLVSLFLLLQMENVQLIGVSTIGADCYLEPSLSASVKIINRFSNEDIQVApsyeRGKnpfpkewrmhaff 84
Cdd:pfam01156 1 VIIDTDPGIDDALALLLALASPEIELLGITTVAGNVSLEQTTRNALRLLELGGRDDIPVY----AGE------------- 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584725277 85 mdalpILNEPvkhvasnvsdkeafediiqtlkrqsEKVTLLFTGPLTDLAKALQKDSSIVQYIEKLVWMGGTFLPKGNVE 164
Cdd:pfam01156 64 -----AIREP-------------------------GEVTLVATGPLTNLALALRLDPELAKKIKELVIMGGAFGVRGNVT 113
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584725277 165 EpehdgSAEWNAYWDPEAVKIVFDSDIEIDMVALESTNQVPLTLDVRQRWANERQYTG------IDFLGVSYAAVPPLTH 238
Cdd:pfam01156 114 P-----AAEFNIFVDPEAAKIVFTSGLPITMVPLDVTHQALLTPEDLERLAALGTPLGrfladlLRFYAEFYRERFGIDG 188
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 584725277 239 FItnstyfLWDVLTTAYIGNKDLVHSIEKKVDV-ISYGPSQGKTF-----ECKDGRKINVINHVDNNAFFD 303
Cdd:pfam01156 189 PP------LHDPLAVAVALDPELFTTRRLNVDVeTTGGLTRGQTVvddrgGWGKPPNVRVATDVDVDRFWE 253
|
|
| PTZ00313 |
PTZ00313 |
inosine-adenosine-guanosine-nucleoside hydrolase; Provisional |
1-310 |
1.20e-50 |
|
inosine-adenosine-guanosine-nucleoside hydrolase; Provisional
Pssm-ID: 140334 [Multi-domain] Cd Length: 326 Bit Score: 170.43 E-value: 1.20e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584725277 1 MTKKVYFNHDGGVDDLVSLFLLL-QMENVQLIGVSTIGADCYLEPSLSASVKII----NRFSNEDIQVAPSYERGKNPFP 75
Cdd:PTZ00313 1 MPKPVILDHDGNHDDLVALALLLgNPEKVKVIGCICTDADCFVDDAFNVTGKLMcmmhAREATPLFPIGKSSFKGVNPFP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584725277 76 KEWRMHAFFMDALPILNEPvKHVA-----SNVSDKEAFEDIIQTLKRQS-EKVTLLFTGPLTDLAKALQK-DSSIVQYIE 148
Cdd:PTZ00313 81 SEWRWSAKNMDDLPCLNIP-EHVAiweklKPENEALVGEELLADLVMSSpEKVTICVTGPLSNVAWCIEKyGEEFTKKVE 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584725277 149 KLVWMGGTFLPKGNVEEPEHDGSAEWNAYWDPEAVKIVFD-SDIEIDMVALESTNQVPLTLDVRQRWANERQYTGIDFLG 227
Cdd:PTZ00313 160 ECVIMGGAVDVGGNVFLPGTDGSAEWNIYWDPPAAKTVLMcPHIRKVLFSLDSTNSVPVTSEVVKKFGAQNKYLLSQFVG 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584725277 228 VSYAAVpplTHF---ITNSTYFLWDVLTTAYIGNKDLVHSIEKKVDV-ISYGPSQGKTFECKDGRKIN-VINHVDNNAFF 302
Cdd:PTZ00313 240 STWAMC---THHellRPGDGYYAWDVLTAAYVIERNLAELEPVPLEVvVEKAKNEGRTRRAAEGAACTyVAKNTNAELFY 316
|
....*...
gi 584725277 303 DYITALAK 310
Cdd:PTZ00313 317 DMVLDSAR 324
|
|
| nuc_hydro |
cd00455 |
nuc_hydro: Nucleoside hydrolases. Nucleoside hydrolases cleave the N-glycosidic bond in ... |
5-303 |
1.64e-47 |
|
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: 161.34 E-value: 1.64e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584725277 5 VYFNHDGGVDDLVSLFLLLQMENVQLIGVSTIGADCYLEPSLSASVKIINRFSNEDIQVAPSYERGKNPFPKEWRMHAFF 84
Cdd:cd00455 1 VILDTDPGIDDAFALMYALLHPEIELVGIVATYGNVTLEQATQNAAYLLELLGRLDIPVYAGATRPLTGEIPAAYPEIHG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584725277 85 MDALPILNEPvkhvASNVSDKEAFEDIIQTLKRQSEKVTLLFTGPLTDLAKALQKDSSIVQYIEKLVWMGGTFLPKGNVe 164
Cdd:cd00455 81 EGGLGLPIPP----IIEADDPEAVQLLIDLIRKYPDEITIVALGPLTNLAMAFILDPDIKDRVKEIVIMGGAFLVPGNV- 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584725277 165 epehDGSAEWNAYWDPEAVKIVFDSDIEIDMVALESTNQVPLTLDVRQRWANERQYTG--IDFLGVSYAAVPPLTHfitN 242
Cdd:cd00455 156 ----TPVAEANFYGDPEAANIVFNSAKNLTIVPLDVTNQAVLTPPMVERIFEQGTSIGllIKPMIDYYYKAYQKPG---I 228
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 584725277 243 STYFLWDVLTTAYIGNKDLVHSIEKKVDVISYGPSQGKTFECKDGRKINVINHVDNNAFFD 303
Cdd:cd00455 229 EGSPIHDPLAVAYLLNPSMFDYSKVPVDVDTDGLTRGQTIADFRENPGNGVTRVAVNLDYP 289
|
|
| nuc_hydro_IU_UC_XIUA |
cd02651 |
nuc_hydro_IU_UC_XIUA: inosine-uridine preferring, ... |
4-306 |
1.50e-30 |
|
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: 116.88 E-value: 1.50e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584725277 4 KVYFNHDGGVDDLVSLFLLLQMENVQLIGVSTIGADCYLEPSLSASVKIINRFSNEDIQVAPSYERgknpfpkewrmhaf 83
Cdd:cd02651 1 PIIIDCDPGHDDAVAILLALFHPELDLLGITTVAGNVPLEKTTRNALKLLTLLGRTDVPVAAGAAR-------------- 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584725277 84 fmdalPILNEPVkhVASNV------------------SDKEAFEDIIQTLKRQSEKVTLLFTGPLTDLAKALQKDSSIVQ 145
Cdd:cd02651 67 -----PLVRPLI--TASDIhgesgldgadlpppprrpEDIHAVDAIIDTLRASPEPITLVATGPLTNIALLLRKYPELAE 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584725277 146 YIEKLVWMGGTFlPKGNveepeHDGSAEWNAYWDPEAVKIVFDSDIEIDMVALESTNQVPLTLDVRQRWANERQYTGI-- 223
Cdd:cd02651 140 RIKEIVLMGGAL-GRGN-----ITPAAEFNIFVDPEAAKIVFNSGIPITMVPLDVTHKALATPEVIERIRALGNPVGKml 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584725277 224 ----DFLGVSYAAV----PPLtHfitnstyflwDVLTTAYIGNKDLVHSIEKKVDVISYG-PSQGKT---FECKDGRKIN 291
Cdd:cd02651 214 aellDFFAETYGSAftegPPL-H----------DPCAVAYLLDPELFTTKRANVDVETEGeLTRGRTvvdLRGVTGRPAN 282
|
330
....*....|....*..
gi 584725277 292 --VINHVDNNAFFDYIT 306
Cdd:cd02651 283 aqVAVDVDVEKFWDLLL 299
|
|
| nuc_hydro_CaPnhB |
cd02650 |
NH_hydro_CaPnhB: A subgroup of nucleoside hydrolases similar to Corynebacterium ammoniagenes ... |
4-289 |
6.23e-29 |
|
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: 112.37 E-value: 6.23e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584725277 4 KVYFNHDGGVDDLVSLFLLLQMENVQLIGVSTIGADCYLEPSLSASVKIINRFSNEDIQVAPSYERGKNPFPKEWRMHAF 83
Cdd:cd02650 1 KLILDTDPGIDDAMALAYALAHPDVDLIGVTTVYGNVTIETATRNALALLELFGRPDVPVAEGAAKPLTRPPFRIATFVH 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584725277 84 FMDAL--PILNEPVKhvasNVSDKEAFEDIIQTLKRQSEKVTLLFTGPLTDLAKALQKDSSIVQYIEKLVWMGGTFLPKG 161
Cdd:cd02650 81 GDNGLgdVELPAPPR----QPEDESAADFLIELANEYPGELTLVAVGPLTNLALALARDPDFAKLVKQVVVMGGAFTVPG 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584725277 162 NVeEPehdgSAEWNAYWDPEAVKIVFDSDIEIDMVALESTNQVPLTLDVRQRWAN---ERQYTGIDFLGVSYAAvppLTH 238
Cdd:cd02650 157 NV-TP----AAEANIHGDPEAADIVFTAGADLTMVGLDVTTQTLLTREDLDELRDsggKAGQFLADMLDYYIDF---YQE 228
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 584725277 239 FITNSTYFLWDVLTTAYIGNKDLVHSIEKKVDVISYGPSQGKTFECKDGRK 289
Cdd:cd02650 229 SPGLRGCALHDPLAVAAAVDPSLFTTREGVVRVETEGPTRGRTIGDRDGRR 279
|
|
| PRK10768 |
PRK10768 |
ribonucleoside hydrolase RihC; Provisional |
1-301 |
3.36e-25 |
|
ribonucleoside hydrolase RihC; Provisional
Pssm-ID: 182713 [Multi-domain] Cd Length: 304 Bit Score: 102.30 E-value: 3.36e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584725277 1 MTKKVYFNHDGGVDDLVSLFLLLQMEN--VQLIgvSTIGADCYLEPSLSASVKIInRFSNEDIQVApsyeRG-KNPFPKE 77
Cdd:PRK10768 1 MRLPIILDTDPGIDDAVAIAAALFAPEldLKLI--TTVAGNVSVEKTTRNALKLL-HFFNSDVPVA----QGaAKPLVRP 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584725277 78 wrmhafFMDALPILNEP-------VKHvASNVSDKEAFEDIIQTLKRQSEKVTLLFTGPLTDLAKALQKDSSIVQYIEKL 150
Cdd:PRK10768 74 ------LRDAASVHGESgmegydfPEH-TRKPLSIPAVEAMRDALMNAPEPVTLVAIGPLTNIALLLSTYPEVKPYIKRI 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584725277 151 VWMGGTfLPKGNVEEpehdgSAEWNAYWDPEAVKIVFDSDIEIDMVALESTNQVPLTLDVRQRWANERQyTGIDFLGVsy 230
Cdd:PRK10768 147 VLMGGS-AGRGNVTP-----NAEFNIAVDPEAAAIVFRSGIPIVMCGLDVTNQALLTPDYLATLPELNR-TGKMLHAL-- 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584725277 231 aavppLTHFITNStyF-----LWDVLTTAYIGNKDLVHSIEKKVDVISYGP-SQGKT---FECKDGRKIN--VINHVDNN 299
Cdd:PRK10768 218 -----FSHYRSGS--MqtglrMHDVCAIAYLLRPELFTLKPCFVDVETQGEfTAGATvvdIDGRLGKPANaqVALDIDVD 290
|
..
gi 584725277 300 AF 301
Cdd:PRK10768 291 GF 292
|
|
| nuc_hydro_3 |
cd02653 |
NH_3: A subgroup of nucleoside hydrolases. This group contains eukaryotic and bacterial ... |
4-303 |
6.33e-25 |
|
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: 102.07 E-value: 6.33e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584725277 4 KVYFNHDGGVDDLVSLFLLLQMENVQLIGVSTIGADCYLEPSLSASVKIINRFSNEDIQVAPSYERgknPFPKEWRMHAF 83
Cdd:cd02653 1 KVIIDCDPGIDDALALLYLLASPDLDVVGITTTAGNVPVEQVAANALGVLELLGRTDIPVYLGADK---PLAGPLTTAQD 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584725277 84 F--MDALPILNEPVkhVASNVSDKEAFEDIIQTLkRQSEKVTLLFTGPLTDLAKALQKDSSIVQYIEKLVWMGGTFLPKG 161
Cdd:cd02653 78 ThgPDGLGYAELPA--STRTLSDESAAQAWVDLA-RAHPDLIGLATGPLTNLALALREEPELPRLLRRLVIMGGAFNSRG 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584725277 162 NVEEpehdgSAEWNAYWDPEAVKIVFD----SDIEIDMVALESTNQVPLTLDVRQRWANerqytgidflgvsyaAVPPLT 237
Cdd:cd02653 155 NTSP-----VAEWNYWVDPEAAKEVLAafggHPVRPTICGLDVTRAVVLTPNLLERLAR---------------AKDSVG 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584725277 238 HFITNST--YF-------------LWDVLTTAYIGNKDLVHSIEKKVDVISYGPSQGKTFECKDGR-----KINVINHVD 297
Cdd:cd02653 215 AFIEDALrfYFefhwayghgygavIHDPLAAAVALNPNLARGRPAYVDVECTGVLTGQTVVDWAGFwgkgaNAEILTKVD 294
|
....*.
gi 584725277 298 NNAFFD 303
Cdd:cd02653 295 SQDFMA 300
|
|
| PLN02717 |
PLN02717 |
uridine nucleosidase |
3-216 |
1.76e-24 |
|
uridine nucleosidase
Pssm-ID: 178319 [Multi-domain] Cd Length: 316 Bit Score: 100.84 E-value: 1.76e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584725277 3 KKVYFNHDGGVDDLVSLFLLLQMENVQLIGVSTIGADCYLEPSLSASVKIINRFSNEDIQVApsyERGKNPFPKEWRMH- 81
Cdd:PLN02717 1 KKLIIDTDPGIDDAMAILMALRSPEVEVIGLTTIFGNVTTKLATRNALHLLEMAGRPDVPVA---EGSHEPLKGGTKPRi 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584725277 82 AFFM---DALPILNEPVKhvASNVSDKEAFEDIIQTLKRQSEKVTLLFTGPLTDLAKALQKDSSIVQYIEKLVWMGGTFL 158
Cdd:PLN02717 78 ADFVhgsDGLGNTNLPPP--KGKKIEKSAAEFLVEKVSEYPGEVTVVALGPLTNLALAIKLDPSFAKKVGQIVVLGGAFF 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 584725277 159 PKGNVeepehDGSAEWNAYWDPEAVKIVFDSDIEIDMVALESTNQVPLTLDVRQRWAN 216
Cdd:PLN02717 156 VNGNV-----NPAAEANIFGDPEAADIVFTSGADITVVGINVTTQVVLTDADLEELRD 208
|
|
| nuc_hydro_CeIAG |
cd02649 |
nuc_hydro_CeIAG: Nucleoside hydrolases similar to the inosine-adenosine-guanosine-preferring ... |
3-201 |
1.59e-21 |
|
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: 92.32 E-value: 1.59e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584725277 3 KKVYFNHDGGVDDLVSLFLLLQMENVQLIGVSTIGADCYLEPSLSASVKIINRFSNEDIqvaPSYERGKNP-FPKEWRMH 81
Cdd:cd02649 1 RKLIIDTDCGGDDAWALLMALASPNVEVLAITCVHGNTNVEQVVKNALRVLEACGRRDI---PVYRGASKPlLGPGPTAA 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584725277 82 AFF-MDALPILNEPVKHVASNVSDKEAFEDIIQTLKRQSEKVTLLFTGPLTDLAKALQKDSSIVQYIEKLVWMGGTFLPK 160
Cdd:cd02649 78 YFHgKDGFGDVGFPEPKDELELQKEHAVDAIIRLVREYPGEITLVALGPLTNLALAYRLDPSLPQKIKRLYIMGGNREGV 157
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 584725277 161 GNVeepehDGSAEWNAYWDPEAVKIVFDSDI-EIDMVALEST 201
Cdd:cd02649 158 GNT-----TPAAEFNFHVDPEAAHIVLNSFGcPITIVPWETT 194
|
|
| rihB |
PRK09955 |
ribosylpyrimidine nucleosidase; |
3-305 |
7.60e-20 |
|
ribosylpyrimidine nucleosidase;
Pssm-ID: 182166 [Multi-domain] Cd Length: 313 Bit Score: 88.08 E-value: 7.60e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584725277 3 KKVYFNHDGGVDDLVSLFLLLQMENVQLIGVSTIGADCYLEPSLSASVKIINRFsneDIQVaPSYERGKNPFPKEwRMHA 82
Cdd:PRK09955 4 RKIILDCDPGHDDAIAMMMAAKHPAIDLLGITIVAGNQTLDKTLINGLNVCQKL---EINV-PVYAGMPQPIMRQ-QIVA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584725277 83 FFMDALPILNEPV-KHVASNVSDKEAFEDIIQTLKRQSEKVTLLFTGPLTDLAKALQKDSSIVQYIEKLVWMGGTFlPKG 161
Cdd:PRK09955 79 DNIHGETGLDGPVfEPLTRQAESTHAVKYIIDTLMASDGDITLVPVGPLSNIAVAMRMQPAILPKIREIVLMGGAY-GTG 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584725277 162 NVEEpehdgSAEWNAYWDPEAVKIVFDSDIEIDMVALESTNQVPLTLDVRQRWANERQYTGIDFlgvsyaavPPLTHFIT 241
Cdd:PRK09955 158 NFTP-----SAEFNIFADPEAARVVFTSGVPLVMMGLDLTNQTVCTPDVIARMERAGGPAGELF--------SDIMNFTL 224
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 584725277 242 NSTYF--------LWDVLTTAYIGNKDLVHSIEKKVDV-ISYGPSQGKTFeCKD----GRKIN--VINHVDNNAFFDYI 305
Cdd:PRK09955 225 KTQFEnyglaggpVHDATCIGYLINPDGIKTQEMYVEVdVNSGPCYGRTV-CDElgvlGKPANtkVGITIDTDWFWGLV 302
|
|
| nuc_hydro_CjNH |
cd02654 |
nuc_hydro_CjNH. Nucleoside hydrolases similar to Campylobacter jejuni nucleoside hydrolase. ... |
4-305 |
4.18e-18 |
|
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: 82.99 E-value: 4.18e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584725277 4 KVYFNHDGGV----DDLVSLFLLLQMENVQLIGVSTIGADCYLEPSLSASVKIINRFSNEDIqvaPSYERGKNPF---PK 76
Cdd:cd02654 1 KVILDNDIAMgrdtDDGLALALLLWSPEVELLGLSAVSGNCWLSAVTYNVLRMLELAGADAI---PVYAGANTPLgrtNR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584725277 77 EWRMHAFFMDALP--------ILNEPVKHVASNVSDKEAFEDIIQTLKRQSEKVTLLFTGPLTDLAKALQKDSSIVQYIE 148
Cdd:cd02654 78 AFHAWESLYGAYLwqgawspeYSDMYTNASIIRNASIPAALFMIEMVRKHPHEVSIVAAGPLTNLALALRIDPDFAPLAK 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584725277 149 KLVWMGGTFLPKGNVEEPEHdgSAEWNAYWDPEAVKIVFDSDIEIDMVALESTNQVPLTldvrqrwanERQYTGIDFLG- 227
Cdd:cd02654 158 ELVIMGGYLDDIGEFVNRHY--ASDFNLIMDPEAASIVLTAPWKSITIPGNVTNRTCLT---------PEQIKADDPLRd 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584725277 228 -VSYAAVPPLTH---FITNSTYF-LWDVLTTAYIGNKDLV-HSIEKKVDVIS-----YGPSQGKTFECKDG---RKINVI 293
Cdd:cd02654 227 fIRETLDLPIDYakeFVGTGDGLpMWDELASAVALDPELAtSSETFYIDVQTdsdggGQLIWPEDLLLAKGlrpYHVKVI 306
|
330
....*....|..
gi 584725277 294 NHVDNNAFFDYI 305
Cdd:cd02654 307 TAVDVAAFLNLI 318
|
|
| rihA |
PRK10443 |
ribonucleoside hydrolase 1; Provisional |
1-203 |
9.85e-16 |
|
ribonucleoside hydrolase 1; Provisional
Pssm-ID: 182465 [Multi-domain] Cd Length: 311 Bit Score: 76.24 E-value: 9.85e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584725277 1 MTKKVYFNHDGGVDDLVSLFLLLQMENVQLIGVSTIGADCYLEPSLSASVKIINRFSNEDIQVApsyerGKNPFP--KEW 78
Cdd:PRK10443 1 MALPIILDCDPGHDDAIALVLALASPELDVKAVTTSAGNQTPEKTLRNALRMLTLLNRTDIPVA-----GGAVKPlmREL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584725277 79 ----RMHAFF-MDAlPILNEPvkhvASNVSDKEAFEDIIQTLKRQSEKVTLLFTGPLTDLAKALQKDSSIVQYIEKLVWM 153
Cdd:PRK10443 76 iiadNVHGESgLDG-PALPEP----TFAPQNCTAVELMAKTLRESAEPVTLVSTGPQTNVALLLASHPELHSKIARIVIM 150
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 584725277 154 GGTfLPKGNVEEpehdgSAEWNAYWDPEAVKIVFDSDIEIDMVALESTNQ 203
Cdd:PRK10443 151 GGA-MGLGNWTP-----AAEFNIYVDPEAAEIVFQSGIPIVMAGLDVTHK 194
|
|
| nuc_hydro_1 |
cd02648 |
NH_1: A subgroup of nucleoside hydrolases. This group contains fungal proteins similar to ... |
10-188 |
2.09e-13 |
|
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: 69.91 E-value: 2.09e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584725277 10 DGGVDDLVSLFLLLQM-ENVQLIGVSTIGADCYLEPSLSASVKIINRFSNEDIQVA-PSYERG---------------KN 72
Cdd:cd02648 9 DPGVDDVLAILLALSSpEEVDVALISLTFGNTTLDHALRNVLRLFHVLERERAWRAtPGVRYRafsadaekpivasgsDQ 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584725277 73 PFPKEWRMHAFFM---------DALPILNEPVKHVASNV-----SDKEAFEDIIQTLKRQSEK-VTLLFTGPLTDLAKAL 137
Cdd:cd02648 89 PLEGERLTASYFHgrdglsgvhWLHPDFTPVETWIPEIVapltpSDKPAYDVILDILREEPDHtVTIAALGPLTNLAAAA 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 584725277 138 QKDSSIVQYIEKLVWMGGTFLPKGNVEEpehdgSAEWNAYWDPEAVKIVFD 188
Cdd:cd02648 169 RKDPETFAKVGEVVVMGGAIDVPGNTSP-----VAEFNCFADPYAAAVVID 214
|
|
| nuc_hydro_2 |
cd02652 |
NH_2: A subgroup of nucleoside hydrolases. This group contains eukaryotic and bacterial ... |
11-189 |
2.39e-07 |
|
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: 51.35 E-value: 2.39e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584725277 11 GGVDDLVSLFLLLQMENVQLIGVSTIGADcylePSLSASVKIINRFSNE-DIQVAPSYergkNPFPKEWRMHAFFM---D 86
Cdd:cd02652 9 GDPDDALALALAHALQKCDLLAVTITLAD----ASARRAIDAVNRFYGRgDIPIGADY----HGWPEDAKDHAKFLlegD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584725277 87 ALPILNEPVKHVasnvsdKEAFEDIIQTL-KRQSEKVTLLFTGPLTDLAKALQKDSS-------IVQYIEKLVWMGGTFL 158
Cdd:cd02652 81 RLHHDLESAEDA------LDAVKALRRLLaSAEDASVTIVSIGPLTNLAALLDADADpltgpelVRQKVKRLVVMGGAFY 154
|
170 180 190
....*....|....*....|....*....|..
gi 584725277 159 -PKGNVEEPehdgsaEWNAYWDPEAVKIVFDS 189
Cdd:cd02652 155 dPDGNVQHR------EYNFVTDPKAAQRVAGR 180
|
|
| |
