|
Name |
Accession |
Description |
Interval |
E-value |
| nuc_hydro_TvIAG |
cd02647 |
nuc_hydro_ TvIAG: Nucleoside hydrolases similar to the Inosine-adenosine-guanosine-preferring ... |
2-306 |
1.61e-103 |
|
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: 305.50 E-value: 1.61e-103
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545090042 2 KQLYFNHDGGVDDLISLFLLLQMENINL--IGVSAIGADSYVEPATSASQKIINRF-STTQIDVAASKERGKNPFPKDWR 78
Cdd:cd02647 1 KNVIFDHDGNVDDLVALLLLLKNEKVDLkgIGVSGIDADCYVEPAVSVTRKLIDRLgQRDAIPVGKGGSRAVNPFPRSWR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545090042 79 MHAFF-MDALPILNEPTASQSTILDTDAYQDIIDKVSQSSEPVTLLFTGPLTDLAKALAVNPTIEHNIARLVWMGGTFLS 157
Cdd:cd02647 81 RDAAFsVDHLPILNERYTVETPLAEETAQLVLIEKIKASLEPVTLLVTGPLTNLARALDSDPDISSNIEEVYIMGGGVDA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545090042 158 KGNVEEPEHDGSAEWNAFWDPEAVAAVFNTTISIDMVALESTNQVPLTPA----IRQQWADERhHIGVDFLGVSYAAVPP 233
Cdd:cd02647 161 PGNVFTPPSNGTAEFNIFWDPLAAKTVFDSGLKITLVPLDATNTVPLTREfletDRQRFAAQR-LPASDLAGQGYALVKP 239
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 545090042 234 lthFQTNSTYFLWDVLTTAYIGKPELVHQYTVK-AAVITDGPSQGKIYQDeTNGREVDVVTHVDHD---DFFLYITD 306
Cdd:cd02647 240 ---LEFNSTYYMWDVLTTLVLGAKEVDNTKESLiLEVDTDGLSAGQTVTS-PNGRPLTLVTSNNSYgsnRFFDDYLE 312
|
|
| URH1 |
COG1957 |
Inosine-uridine nucleoside N-ribohydrolase [Nucleotide transport and metabolism]; ... |
1-307 |
5.88e-73 |
|
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: 227.34 E-value: 5.88e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545090042 1 MKQLYFNHDGGVDDLISLFLLLQMENINLIGVSAIGADSYVEPATSASQKIINRFSTTQIDVAASKERgknPFPKDWRMH 80
Cdd:COG1957 2 MRKVIIDTDPGIDDALALLLALASPEIDLLGITTVAGNVPLEQTTRNALKLLELAGRTDVPVAAGAAR---PLVRPLVTA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545090042 81 AFF--MDALPILNEPTASQStILDTDAYQDIIDKVSQSSEPVTLLFTGPLTDLAKALAVNPTIEHNIARLVWMGGTFLSK 158
Cdd:COG1957 79 EHVhgEDGLGGVDLPEPTRP-PEPEHAVDFIIETLRAAPGEVTLVALGPLTNLALALRKDPELAERIKRIVIMGGAFFVP 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545090042 159 GNVeEPehdgSAEWNAFWDPEAVAAVFNTTISIDMVALESTNQVPLTPAIRQQWADERHHIGvDFLGVSYAAVPPLTH-F 237
Cdd:COG1957 158 GNV-TP----VAEFNIYVDPEAAKIVFASGIPITMVGLDVTHQALLTPEDLARLAALGTPLG-RFLADLLDFYLDFYReR 231
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 545090042 238 QTNSTYFLWDVLTTAYIGKPELVHQYTVKAAVITDG-PSQGKIYQDE----TNGREVDVVTHVDHDDFFLYITDL 307
Cdd:COG1957 232 YGLDGCPLHDPLAVAYLLDPELFTTRPAPVDVETDGeLTRGQTVVDWrgvtGRPPNARVALDVDAERFLDLLLER 306
|
|
| IU_nuc_hydro |
pfam01156 |
Inosine-uridine preferring nucleoside hydrolase; |
4-301 |
6.97e-49 |
|
Inosine-uridine preferring nucleoside hydrolase;
Pssm-ID: 460086 [Multi-domain] Cd Length: 253 Bit Score: 163.53 E-value: 6.97e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545090042 4 LYFNHDGGVDDLISLFLLLQMENINLIGVSAIGADSYVEPATSASQKIINRFSTTQIDVAaskeRGKnpfpkdwrmhaff 83
Cdd:pfam01156 1 VIIDTDPGIDDALALLLALASPEIELLGITTVAGNVSLEQTTRNALRLLELGGRDDIPVY----AGE------------- 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545090042 84 mdalpILNEPtasqstildtdayqdiidkvsqssEPVTLLFTGPLTDLAKALAVNPTIEHNIARLVWMGGTFLSKGNVEE 163
Cdd:pfam01156 64 -----AIREP------------------------GEVTLVATGPLTNLALALRLDPELAKKIKELVIMGGAFGVRGNVTP 114
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545090042 164 pehdgSAEWNAFWDPEAVAAVFNTTISIDMVALESTNQVPLTPAIRQQWADERHHIG------VDFLGVSYAAVPPLTHF 237
Cdd:pfam01156 115 -----AAEFNIFVDPEAAKIVFTSGLPITMVPLDVTHQALLTPEDLERLAALGTPLGrfladlLRFYAEFYRERFGIDGP 189
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 545090042 238 QtnstyfLWDVLTTAYIGKPELVHQYTVKAAVITDG-PSQGKIYQDETNGRE----VDVVTHVDHDDFF 301
Cdd:pfam01156 190 P------LHDPLAVAVALDPELFTTRRLNVDVETTGgLTRGQTVVDDRGGWGkppnVRVATDVDVDRFW 252
|
|
| PTZ00313 |
PTZ00313 |
inosine-adenosine-guanosine-nucleoside hydrolase; Provisional |
2-301 |
1.34e-41 |
|
inosine-adenosine-guanosine-nucleoside hydrolase; Provisional
Pssm-ID: 140334 [Multi-domain] Cd Length: 326 Bit Score: 146.93 E-value: 1.34e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545090042 2 KQLYFNHDGGVDDLISLFLLL-QMENINLIGVSAIGADSYVEPATSASQKII----NRFSTTQIDVAASKERGKNPFPKD 76
Cdd:PTZ00313 3 KPVILDHDGNHDDLVALALLLgNPEKVKVIGCICTDADCFVDDAFNVTGKLMcmmhAREATPLFPIGKSSFKGVNPFPSE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545090042 77 WRMHAFFMDALPILNEP--TASQSTILD-TDAY---QDIIDKVSQSSEPVTLLFTGPLTDLAKAL-AVNPTIEHNIARLV 149
Cdd:PTZ00313 83 WRWSAKNMDDLPCLNIPehVAIWEKLKPeNEALvgeELLADLVMSSPEKVTICVTGPLSNVAWCIeKYGEEFTKKVEECV 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545090042 150 WMGGTFLSKGNVEEPEHDGSAEWNAFWDPEAVAAVFNTT-ISIDMVALESTNQVPLTPAIRQQWADERHHIGVDFLGVSY 228
Cdd:PTZ00313 163 IMGGAVDVGGNVFLPGTDGSAEWNIYWDPPAAKTVLMCPhIRKVLFSLDSTNSVPVTSEVVKKFGAQNKYLLSQFVGSTW 242
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 545090042 229 AAVpplTHFQ---TNSTYFLWDVLTTAYIGKPELVHQYTVKAAV-ITDGPSQGKIYQdETNGREVDVVTHVDHDDFF 301
Cdd:PTZ00313 243 AMC---THHEllrPGDGYYAWDVLTAAYVIERNLAELEPVPLEVvVEKAKNEGRTRR-AAEGAACTYVAKNTNAELF 315
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| nuc_hydro_TvIAG |
cd02647 |
nuc_hydro_ TvIAG: Nucleoside hydrolases similar to the Inosine-adenosine-guanosine-preferring ... |
2-306 |
1.61e-103 |
|
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: 305.50 E-value: 1.61e-103
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545090042 2 KQLYFNHDGGVDDLISLFLLLQMENINL--IGVSAIGADSYVEPATSASQKIINRF-STTQIDVAASKERGKNPFPKDWR 78
Cdd:cd02647 1 KNVIFDHDGNVDDLVALLLLLKNEKVDLkgIGVSGIDADCYVEPAVSVTRKLIDRLgQRDAIPVGKGGSRAVNPFPRSWR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545090042 79 MHAFF-MDALPILNEPTASQSTILDTDAYQDIIDKVSQSSEPVTLLFTGPLTDLAKALAVNPTIEHNIARLVWMGGTFLS 157
Cdd:cd02647 81 RDAAFsVDHLPILNERYTVETPLAEETAQLVLIEKIKASLEPVTLLVTGPLTNLARALDSDPDISSNIEEVYIMGGGVDA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545090042 158 KGNVEEPEHDGSAEWNAFWDPEAVAAVFNTTISIDMVALESTNQVPLTPA----IRQQWADERhHIGVDFLGVSYAAVPP 233
Cdd:cd02647 161 PGNVFTPPSNGTAEFNIFWDPLAAKTVFDSGLKITLVPLDATNTVPLTREfletDRQRFAAQR-LPASDLAGQGYALVKP 239
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 545090042 234 lthFQTNSTYFLWDVLTTAYIGKPELVHQYTVK-AAVITDGPSQGKIYQDeTNGREVDVVTHVDHD---DFFLYITD 306
Cdd:cd02647 240 ---LEFNSTYYMWDVLTTLVLGAKEVDNTKESLiLEVDTDGLSAGQTVTS-PNGRPLTLVTSNNSYgsnRFFDDYLE 312
|
|
| URH1 |
COG1957 |
Inosine-uridine nucleoside N-ribohydrolase [Nucleotide transport and metabolism]; ... |
1-307 |
5.88e-73 |
|
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: 227.34 E-value: 5.88e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545090042 1 MKQLYFNHDGGVDDLISLFLLLQMENINLIGVSAIGADSYVEPATSASQKIINRFSTTQIDVAASKERgknPFPKDWRMH 80
Cdd:COG1957 2 MRKVIIDTDPGIDDALALLLALASPEIDLLGITTVAGNVPLEQTTRNALKLLELAGRTDVPVAAGAAR---PLVRPLVTA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545090042 81 AFF--MDALPILNEPTASQStILDTDAYQDIIDKVSQSSEPVTLLFTGPLTDLAKALAVNPTIEHNIARLVWMGGTFLSK 158
Cdd:COG1957 79 EHVhgEDGLGGVDLPEPTRP-PEPEHAVDFIIETLRAAPGEVTLVALGPLTNLALALRKDPELAERIKRIVIMGGAFFVP 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545090042 159 GNVeEPehdgSAEWNAFWDPEAVAAVFNTTISIDMVALESTNQVPLTPAIRQQWADERHHIGvDFLGVSYAAVPPLTH-F 237
Cdd:COG1957 158 GNV-TP----VAEFNIYVDPEAAKIVFASGIPITMVGLDVTHQALLTPEDLARLAALGTPLG-RFLADLLDFYLDFYReR 231
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 545090042 238 QTNSTYFLWDVLTTAYIGKPELVHQYTVKAAVITDG-PSQGKIYQDE----TNGREVDVVTHVDHDDFFLYITDL 307
Cdd:COG1957 232 YGLDGCPLHDPLAVAYLLDPELFTTRPAPVDVETDGeLTRGQTVVDWrgvtGRPPNARVALDVDAERFLDLLLER 306
|
|
| IU_nuc_hydro |
pfam01156 |
Inosine-uridine preferring nucleoside hydrolase; |
4-301 |
6.97e-49 |
|
Inosine-uridine preferring nucleoside hydrolase;
Pssm-ID: 460086 [Multi-domain] Cd Length: 253 Bit Score: 163.53 E-value: 6.97e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545090042 4 LYFNHDGGVDDLISLFLLLQMENINLIGVSAIGADSYVEPATSASQKIINRFSTTQIDVAaskeRGKnpfpkdwrmhaff 83
Cdd:pfam01156 1 VIIDTDPGIDDALALLLALASPEIELLGITTVAGNVSLEQTTRNALRLLELGGRDDIPVY----AGE------------- 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545090042 84 mdalpILNEPtasqstildtdayqdiidkvsqssEPVTLLFTGPLTDLAKALAVNPTIEHNIARLVWMGGTFLSKGNVEE 163
Cdd:pfam01156 64 -----AIREP------------------------GEVTLVATGPLTNLALALRLDPELAKKIKELVIMGGAFGVRGNVTP 114
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545090042 164 pehdgSAEWNAFWDPEAVAAVFNTTISIDMVALESTNQVPLTPAIRQQWADERHHIG------VDFLGVSYAAVPPLTHF 237
Cdd:pfam01156 115 -----AAEFNIFVDPEAAKIVFTSGLPITMVPLDVTHQALLTPEDLERLAALGTPLGrfladlLRFYAEFYRERFGIDGP 189
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 545090042 238 QtnstyfLWDVLTTAYIGKPELVHQYTVKAAVITDG-PSQGKIYQDETNGRE----VDVVTHVDHDDFF 301
Cdd:pfam01156 190 P------LHDPLAVAVALDPELFTTRRLNVDVETTGgLTRGQTVVDDRGGWGkppnVRVATDVDVDRFW 252
|
|
| PTZ00313 |
PTZ00313 |
inosine-adenosine-guanosine-nucleoside hydrolase; Provisional |
2-301 |
1.34e-41 |
|
inosine-adenosine-guanosine-nucleoside hydrolase; Provisional
Pssm-ID: 140334 [Multi-domain] Cd Length: 326 Bit Score: 146.93 E-value: 1.34e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545090042 2 KQLYFNHDGGVDDLISLFLLL-QMENINLIGVSAIGADSYVEPATSASQKII----NRFSTTQIDVAASKERGKNPFPKD 76
Cdd:PTZ00313 3 KPVILDHDGNHDDLVALALLLgNPEKVKVIGCICTDADCFVDDAFNVTGKLMcmmhAREATPLFPIGKSSFKGVNPFPSE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545090042 77 WRMHAFFMDALPILNEP--TASQSTILD-TDAY---QDIIDKVSQSSEPVTLLFTGPLTDLAKAL-AVNPTIEHNIARLV 149
Cdd:PTZ00313 83 WRWSAKNMDDLPCLNIPehVAIWEKLKPeNEALvgeELLADLVMSSPEKVTICVTGPLSNVAWCIeKYGEEFTKKVEECV 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545090042 150 WMGGTFLSKGNVEEPEHDGSAEWNAFWDPEAVAAVFNTT-ISIDMVALESTNQVPLTPAIRQQWADERHHIGVDFLGVSY 228
Cdd:PTZ00313 163 IMGGAVDVGGNVFLPGTDGSAEWNIYWDPPAAKTVLMCPhIRKVLFSLDSTNSVPVTSEVVKKFGAQNKYLLSQFVGSTW 242
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 545090042 229 AAVpplTHFQ---TNSTYFLWDVLTTAYIGKPELVHQYTVKAAV-ITDGPSQGKIYQdETNGREVDVVTHVDHDDFF 301
Cdd:PTZ00313 243 AMC---THHEllrPGDGYYAWDVLTAAYVIERNLAELEPVPLEVvVEKAKNEGRTRR-AAEGAACTYVAKNTNAELF 315
|
|
| nuc_hydro |
cd00455 |
nuc_hydro: Nucleoside hydrolases. Nucleoside hydrolases cleave the N-glycosidic bond in ... |
6-277 |
4.28e-39 |
|
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: 139.39 E-value: 4.28e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545090042 6 FNHDGGVDDLISLFLLLQMENINLIGVSAIGADSYVEPATSASQKIINRFSTTQIDVAASKERGKNPFPKDWRMHAFFMD 85
Cdd:cd00455 3 LDTDPGIDDAFALMYALLHPEIELVGIVATYGNVTLEQATQNAAYLLELLGRLDIPVYAGATRPLTGEIPAAYPEIHGEG 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545090042 86 ALPILNEPTASQSTIldtDAYQDIIDKVSQSSEPVTLLFTGPLTDLAKALAVNPTIEHNIARLVWMGGTFLSKGNVeepe 165
Cdd:cd00455 83 GLGLPIPPIIEADDP---EAVQLLIDLIRKYPDEITIVALGPLTNLAMAFILDPDIKDRVKEIVIMGGAFLVPGNV---- 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545090042 166 hDGSAEWNAFWDPEAVAAVFNTTISIDMVALESTNQVPLTPAIRQQWADERHHIGVdflgvsyaAVPPLTHFQTNS---- 241
Cdd:cd00455 156 -TPVAEANFYGDPEAANIVFNSAKNLTIVPLDVTNQAVLTPPMVERIFEQGTSIGL--------LIKPMIDYYYKAyqkp 226
|
250 260 270
....*....|....*....|....*....|....*....
gi 545090042 242 ---TYFLWDVLTTAYIGKPELVHQYTVKAAVITDGPSQG 277
Cdd:cd00455 227 gieGSPIHDPLAVAYLLNPSMFDYSKVPVDVDTDGLTRG 265
|
|
| nuc_hydro_IU_UC_XIUA |
cd02651 |
nuc_hydro_IU_UC_XIUA: inosine-uridine preferring, ... |
8-306 |
1.05e-31 |
|
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: 119.96 E-value: 1.05e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545090042 8 HDGGVDDLISLFLLLQMENINLIGVSAIGADSYVEPATSASQKIINRFSTTQIDVAASKER---GKNPFPKDwrMH-AFF 83
Cdd:cd02651 6 CDPGHDDAVAILLALFHPELDLLGITTVAGNVPLEKTTRNALKLLTLLGRTDVPVAAGAARplvRPLITASD--IHgESG 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545090042 84 MDAlPILNEPTASQstiLDTDAYQDIIDKVSQSSEPVTLLFTGPLTDLAKALAVNPTIEHNIARLVWMGGTFlSKGNvee 163
Cdd:cd02651 84 LDG-ADLPPPPRRP---EDIHAVDAIIDTLRASPEPITLVATGPLTNIALLLRKYPELAERIKEIVLMGGAL-GRGN--- 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545090042 164 peHDGSAEWNAFWDPEAVAAVFNTTISIDMVALESTNQVPLTPAIRQQWADERHHIGV------DFLGVSYAAV----PP 233
Cdd:cd02651 156 --ITPAAEFNIFVDPEAAKIVFNSGIPITMVPLDVTHKALATPEVIERIRALGNPVGKmlaellDFFAETYGSAftegPP 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545090042 234 LtHfqtnstyflwDVLTTAYIGKPELVHQYTVKAAVITDG-PSQGKI------YQDETNGreVDVVTHVDHDDFFLYITD 306
Cdd:cd02651 234 L-H----------DPCAVAYLLDPELFTTKRANVDVETEGeLTRGRTvvdlrgVTGRPAN--AQVAVDVDVEKFWDLLLE 300
|
|
| nuc_hydro_CaPnhB |
cd02650 |
NH_hydro_CaPnhB: A subgroup of nucleoside hydrolases similar to Corynebacterium ammoniagenes ... |
9-302 |
5.02e-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: 112.76 E-value: 5.02e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545090042 9 DGGVDDLISLFLLLQMENINLIGVSAIGADSYVEPATSASQKIINRFSTTQIDVA--ASKERGKNPFPKDWRMHAffMDA 86
Cdd:cd02650 7 DPGIDDAMALAYALAHPDVDLIGVTTVYGNVTIETATRNALALLELFGRPDVPVAegAAKPLTRPPFRIATFVHG--DNG 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545090042 87 LPILnEPTASQSTILDTDAYQDIIDKVSQSSEPVTLLFTGPLTDLAKALAVNPTIEHNIARLVWMGGTFLSKGNVEEpeh 166
Cdd:cd02650 85 LGDV-ELPAPPRQPEDESAADFLIELANEYPGELTLVAVGPLTNLALALARDPDFAKLVKQVVVMGGAFTVPGNVTP--- 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545090042 167 dgSAEWNAFWDPEAVAAVFNTTISIDMVALESTNQVPLTPAIRQQWAD---ERHHIGVDFLGVSYAAvpplthFQTNSTY 243
Cdd:cd02650 161 --AAEANIHGDPEAADIVFTAGADLTMVGLDVTTQTLLTREDLDELRDsggKAGQFLADMLDYYIDF------YQESPGL 232
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 545090042 244 ---FLWDVLTTAYIGKPELVHQYTVKAAVITDGPSQGKIYQDET------NGREVDVVTHVDHDDFFL 302
Cdd:cd02650 233 rgcALHDPLAVAAAVDPSLFTTREGVVRVETEGPTRGRTIGDRDgrrfwdSSPNATVAVDVDVDERFL 300
|
|
| PRK10768 |
PRK10768 |
ribonucleoside hydrolase RihC; Provisional |
9-300 |
3.26e-25 |
|
ribonucleoside hydrolase RihC; Provisional
Pssm-ID: 182713 [Multi-domain] Cd Length: 304 Bit Score: 102.68 E-value: 3.26e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545090042 9 DGGVDDLISLFLLLQMENINLIGVSAIGADSYVEPATSASQKIInRFSTTQIDVAaskeRG-KNPFPKDwrmhafFMDAL 87
Cdd:PRK10768 10 DPGIDDAVAIAAALFAPELDLKLITTVAGNVSVEKTTRNALKLL-HFFNSDVPVA----QGaAKPLVRP------LRDAA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545090042 88 PILNEP-------TASQSTILDTDAYQDIIDKVSQSSEPVTLLFTGPLTDLAKALAVNPTIEHNIARLVWMGGTfLSKGN 160
Cdd:PRK10768 79 SVHGESgmegydfPEHTRKPLSIPAVEAMRDALMNAPEPVTLVAIGPLTNIALLLSTYPEVKPYIKRIVLMGGS-AGRGN 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545090042 161 VEEpehdgSAEWNAFWDPEAVAAVFNTTISIDMVALESTNQVPLTPAIRQQWADeRHHIGVDFLGVsyaavppLTHFQTN 240
Cdd:PRK10768 158 VTP-----NAEFNIAVDPEAAAIVFRSGIPIVMCGLDVTNQALLTPDYLATLPE-LNRTGKMLHAL-------FSHYRSG 224
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 545090042 241 StyF-----LWDVLTTAYIGKPELvhqYTVKAA---VITDGPS---------QGKiYQDETNgreVDVVTHVDHDDF 300
Cdd:PRK10768 225 S--MqtglrMHDVCAIAYLLRPEL---FTLKPCfvdVETQGEFtagatvvdiDGR-LGKPAN---AQVALDIDVDGF 292
|
|
| nuc_hydro_3 |
cd02653 |
NH_3: A subgroup of nucleoside hydrolases. This group contains eukaryotic and bacterial ... |
9-307 |
1.20e-24 |
|
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: 101.30 E-value: 1.20e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545090042 9 DGGVDDLISLFLLLQMENINLIGVSAIGADSYVEPATSASQKIINRFSTTQIDVAaskeRGKNpFPKDWRM------HAf 82
Cdd:cd02653 7 DPGIDDALALLYLLASPDLDVVGITTTAGNVPVEQVAANALGVLELLGRTDIPVY----LGAD-KPLAGPLttaqdtHG- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545090042 83 fMDALPiLNEPTASQSTILDTDAYQDIIDKVSQSSEpVTLLFTGPLTDLAKALAVNPTIEHNIARLVWMGGTFLSKGNVE 162
Cdd:cd02653 81 -PDGLG-YAELPASTRTLSDESAAQAWVDLARAHPD-LIGLATGPLTNLALALREEPELPRLLRRLVIMGGAFNSRGNTS 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545090042 163 EpehdgSAEWNAFWDPEAVAAVFN----TTISIDMVALESTNQVPLTPAIRQQWADERHHIG----------VDF---LG 225
Cdd:cd02653 158 P-----VAEWNYWVDPEAAKEVLAafggHPVRPTICGLDVTRAVVLTPNLLERLARAKDSVGafiedalrfyFEFhwaYG 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545090042 226 VSYAAVpplthfqtnstyfLWDVLTTAYIGKPELVHQYTVKAAVITDGPSQGKIYQDET----NGREVDVVTHVDHDDFF 301
Cdd:cd02653 233 HGYGAV-------------IHDPLAAAVALNPNLARGRPAYVDVECTGVLTGQTVVDWAgfwgKGANAEILTKVDSQDFM 299
|
....*..
gi 545090042 302 -LYITDL 307
Cdd:cd02653 300 aLFIERV 306
|
|
| nuc_hydro_CjNH |
cd02654 |
nuc_hydro_CjNH. Nucleoside hydrolases similar to Campylobacter jejuni nucleoside hydrolase. ... |
10-300 |
6.64e-20 |
|
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: 87.99 E-value: 6.64e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545090042 10 GGVDDLISLFLLLQMENINLIGVSAIGADSYVEPATSASQKIINRFSTTQIDVAA---------SKER-------GKNPF 73
Cdd:cd02654 12 RDTDDGLALALLLWSPEVELLGLSAVSGNCWLSAVTYNVLRMLELAGADAIPVYAgantplgrtNRAFhaweslyGAYLW 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545090042 74 PKDWRMHAFFMDAlpilNEPTASQSTIldtDAYQDIIDKVSQSSEPVTLLFTGPLTDLAKALAVNPTIEHNIARLVWMGG 153
Cdd:cd02654 92 QGAWSPEYSDMYT----NASIIRNASI---PAALFMIEMVRKHPHEVSIVAAGPLTNLALALRIDPDFAPLAKELVIMGG 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545090042 154 TFLSKGNVEEPEHdgSAEWNAFWDPEAVAAVFNTTISIDMVALESTNQVPLTPairqqwadERHHIGVDFLG-VSYAAVP 232
Cdd:cd02654 165 YLDDIGEFVNRHY--ASDFNLIMDPEAASIVLTAPWKSITIPGNVTNRTCLTP--------EQIKADDPLRDfIRETLDL 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545090042 233 PLTH---FQTNSTYF-LWDVLTTAYIGKPELV-HQYTVKAAVITDGPSQGKIYQDETNG-------REVDVVTHVDHDDF 300
Cdd:cd02654 235 PIDYakeFVGTGDGLpMWDELASAVALDPELAtSSETFYIDVQTDSDGGGQLIWPEDLLlakglrpYHVKVITAVDVAAF 314
|
|
| PLN02717 |
PLN02717 |
uridine nucleosidase |
9-214 |
1.47e-19 |
|
uridine nucleosidase
Pssm-ID: 178319 [Multi-domain] Cd Length: 316 Bit Score: 86.97 E-value: 1.47e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545090042 9 DGGVDDLISLFLLLQMENINLIGVSAIGADSYVEPATSASQKIINRFSTTQIDVAASKERgknPFPKDWRMH-AFFM--- 84
Cdd:PLN02717 8 DPGIDDAMAILMALRSPEVEVIGLTTIFGNVTTKLATRNALHLLEMAGRPDVPVAEGSHE---PLKGGTKPRiADFVhgs 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545090042 85 DALPILNEPTASQSTIlDTDAYQDIIDKVSQSSEPVTLLFTGPLTDLAKALAVNPTIEHNIARLVWMGGTFLSKGNVeep 164
Cdd:PLN02717 85 DGLGNTNLPPPKGKKI-EKSAAEFLVEKVSEYPGEVTVVALGPLTNLALAIKLDPSFAKKVGQIVVLGGAFFVNGNV--- 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 545090042 165 ehDGSAEWNAFWDPEAVAAVFNTTISIDMVALESTNQVPLTPAIRQQWAD 214
Cdd:PLN02717 161 --NPAAEANIFGDPEAADIVFTSGADITVVGINVTTQVVLTDADLEELRD 208
|
|
| rihB |
PRK09955 |
ribosylpyrimidine nucleosidase; |
2-310 |
1.05e-16 |
|
ribosylpyrimidine nucleosidase;
Pssm-ID: 182166 [Multi-domain] Cd Length: 313 Bit Score: 79.22 E-value: 1.05e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545090042 2 KQLYFNHDGGVDDLISLFLLLQMENINLIGVSAIGADSyvepatSASQKIINRFSTTQ---IDVAASKERGKnPFPKDW- 77
Cdd:PRK09955 4 RKIILDCDPGHDDAIAMMMAAKHPAIDLLGITIVAGNQ------TLDKTLINGLNVCQkleINVPVYAGMPQ-PIMRQQi 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545090042 78 ---RMHAFFMDALPILNEPTASQSTildTDAYQDIIDKVSQSSEPVTLLFTGPLTDLAKALAVNPTIEHNIARLVWMGGT 154
Cdd:PRK09955 77 vadNIHGETGLDGPVFEPLTRQAES---THAVKYIIDTLMASDGDITLVPVGPLSNIAVAMRMQPAILPKIREIVLMGGA 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545090042 155 FlSKGNVEEpehdgSAEWNAFWDPEAVAAVFNTTISIDMVALESTNQVPLTPAIrqqwADERHHIGvdflGVSYAAVPPL 234
Cdd:PRK09955 154 Y-GTGNFTP-----SAEFNIFADPEAARVVFTSGVPLVMMGLDLTNQTVCTPDV----IARMERAG----GPAGELFSDI 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545090042 235 THFQTNSTYF--------LWDVLTTAYIGKPELVHQYTVKAAV-ITDGPSQGKIYQDETN--GREVD--VVTHVDHDDFF 301
Cdd:PRK09955 220 MNFTLKTQFEnyglaggpVHDATCIGYLINPDGIKTQEMYVEVdVNSGPCYGRTVCDELGvlGKPANtkVGITIDTDWFW 299
|
....*....
gi 545090042 302 LYITDLAKK 310
Cdd:PRK09955 300 GLVEECVRG 308
|
|
| rihA |
PRK10443 |
ribonucleoside hydrolase 1; Provisional |
88-210 |
5.85e-16 |
|
ribonucleoside hydrolase 1; Provisional
Pssm-ID: 182465 [Multi-domain] Cd Length: 311 Bit Score: 77.02 E-value: 5.85e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545090042 88 PILNEPTASQSTIldtDAYQDIIDKVSQSSEPVTLLFTGPLTDLAKALAVNPTIEHNIARLVWMGGTfLSKGNVEEpehd 167
Cdd:PRK10443 90 PALPEPTFAPQNC---TAVELMAKTLRESAEPVTLVSTGPQTNVALLLASHPELHSKIARIVIMGGA-MGLGNWTP---- 161
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 545090042 168 gSAEWNAFWDPEAVAAVFNTTISIDMVALESTNQVPLTPA----IRQ 210
Cdd:PRK10443 162 -AAEFNIYVDPEAAEIVFQSGIPIVMAGLDVTHKAQIMDEdierIRA 207
|
|
| nuc_hydro_CeIAG |
cd02649 |
nuc_hydro_CeIAG: Nucleoside hydrolases similar to the inosine-adenosine-guanosine-preferring ... |
9-199 |
9.30e-16 |
|
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: 76.14 E-value: 9.30e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545090042 9 DGGVDDLISLFLLLQMENINLIGVSAIGADSYVEPATSASQKIINRFSTTQIDV-AASKERGKNPFPKDWRMHAF--FMD 85
Cdd:cd02649 8 DCGGDDAWALLMALASPNVEVLAITCVHGNTNVEQVVKNALRVLEACGRRDIPVyRGASKPLLGPGPTAAYFHGKdgFGD 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545090042 86 ALpilNEPTASQSTILDTDAYQDIIDKVSQSSEPVTLLFTGPLTDLAKALAVNPTIEHNIARLVWMGGTFLSKGNVeepe 165
Cdd:cd02649 88 VG---FPEPKDELELQKEHAVDAIIRLVREYPGEITLVALGPLTNLALAYRLDPSLPQKIKRLYIMGGNREGVGNT---- 160
|
170 180 190
....*....|....*....|....*....|....*
gi 545090042 166 hDGSAEWNAFWDPEAVAAVFN-TTISIDMVALEST 199
Cdd:cd02649 161 -TPAAEFNFHVDPEAAHIVLNsFGCPITIVPWETT 194
|
|
| nuc_hydro_1 |
cd02648 |
NH_1: A subgroup of nucleoside hydrolases. This group contains fungal proteins similar to ... |
102-185 |
4.43e-10 |
|
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: 59.90 E-value: 4.43e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545090042 102 DTDAYQDIIDKVSQS-SEPVTLLFTGPLTDLAKALAVNPTIEHNIARLVWMGGTFLSKGNVEEpehdgSAEWNAFWDPEA 180
Cdd:cd02648 134 DKPAYDVILDILREEpDHTVTIAALGPLTNLAAAARKDPETFAKVGEVVVMGGAIDVPGNTSP-----VAEFNCFADPYA 208
|
....*
gi 545090042 181 VAAVF 185
Cdd:cd02648 209 AAVVI 213
|
|
| nuc_hydro_2 |
cd02652 |
NH_2: A subgroup of nucleoside hydrolases. This group contains eukaryotic and bacterial ... |
10-253 |
3.16e-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: 54.04 E-value: 3.16e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545090042 10 GGVDDLISLFLLLQMENINLIGVSAIGADSYVEPATSAsqkiINRFSTtqiDVAASKERGKNPFPKDWRMHAFFMDALPI 89
Cdd:cd02652 9 GDPDDALALALAHALQKCDLLAVTITLADASARRAIDA----VNRFYG---RGDIPIGADYHGWPEDAKDHAKFLLEGDR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545090042 90 LNEPTASQSTILDT-DAYQDIIDkvSQSSEPVTLLFTGPLTDLAKAL-AVNPTIEH------NIARLVWMGGTFlskgnV 161
Cdd:cd02652 82 LHHDLESAEDALDAvKALRRLLA--SAEDASVTIVSIGPLTNLAALLdADADPLTGpelvrqKVKRLVVMGGAF-----Y 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545090042 162 EEPEHDGSAEWNAFWDPEAVAAVFN--TTISIDMVALESTNQVplTPAIRQQWADERHHigvDFLGVSYAAVPPLTHFQT 239
Cdd:cd02652 155 DPDGNVQHREYNFVTDPKAAQRVAGraQHLGIPVRIVWSGYEL--GEAVSYPHVLVIAH---PFNTPVFAAYWPRSHRRP 229
|
250
....*....|....
gi 545090042 240 nstyfLWDVLTTAY 253
Cdd:cd02652 230 -----LWDPLTLLA 238
|
|
| |
