|
Name |
Accession |
Description |
Interval |
E-value |
| nuc_hydro_TvIAG |
cd02647 |
nuc_hydro_ TvIAG: Nucleoside hydrolases similar to the Inosine-adenosine-guanosine-preferring ... |
2-306 |
2.34e-123 |
|
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: 355.57 E-value: 2.34e-123
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489743384 2 KNIYFNHDGNIDDLVSLLLLLQ--APDIKLIGISAIDGDGYIDPAVEACRKMVDKFNlRGDKLEVARSNSRAIHQFPKEW 79
Cdd:cd02647 1 KNVIFDHDGNVDDLVALLLLLKneKVDLKGIGVSGIDADCYVEPAVSVTRKLIDRLG-QRDAIPVGKGGSRAVNPFPRSW 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489743384 80 RMAT-YSFNYFPILNESGEIKTPEAPLPAHLDMIDKIKKADGPVTLIMTGPITDLARALDEDASIQSKIEKVYWMGGSLD 158
Cdd:cd02647 80 RRDAaFSVDHLPILNERYTVETPLAEETAQLVLIEKIKASLEPVTLLVTGPLTNLARALDSDPDISSNIEEVYIMGGGVD 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489743384 159 GHGNVVSVDADETQEWNAFWDPEAVRRVLDSDLDIQMVGLESTEELPLTDEL----RQHWASLRKyPAIDLVGLGYSLII 234
Cdd:cd02647 160 APGNVFTPPSNGTAEFNIFWDPLAAKTVFDSGLKITLVPLDATNTVPLTREFletdRQRFAAQRL-PASDLAGQGYALVK 238
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 489743384 235 SVP-NAELYLWDVLTTMSALYPELVETRQIK-ANVITSGLASGRMFIDPNGKEITEVTKADKDSFFEKIDKILE 306
Cdd:cd02647 239 PLEfNSTYYMWDVLTTLVLGAKEVDNTKESLiLEVDTDGLSAGQTVTSPNGRPLTLVTSNNSYGSNRFFDDYLE 312
|
|
| URH1 |
COG1957 |
Inosine-uridine nucleoside N-ribohydrolase [Nucleotide transport and metabolism]; ... |
1-308 |
4.83e-66 |
|
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: 209.24 E-value: 4.83e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489743384 1 MKNIYFNHDGNIDDLVSLLLLLQAPDIKLIGISAIDGDGYIDPAVEACRKMVDKFNLrgDKLEVARSNSRAIHqfpKEWR 80
Cdd:COG1957 2 MRKVIIDTDPGIDDALALLLALASPEIDLLGITTVAGNVPLEQTTRNALKLLELAGR--TDVPVAAGAARPLV---RPLV 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489743384 81 MATYsfnyfpILNESG-------EIKTPEAPLPAHLDMIDKIKKADGPVTLIMTGPITDLARALDEDASIQSKIEKVYWM 153
Cdd:COG1957 77 TAEH------VHGEDGlggvdlpEPTRPPEPEHAVDFIIETLRAAPGEVTLVALGPLTNLALALRKDPELAERIKRIVIM 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489743384 154 GGSLDGHGNVVSVdadetQEWNAFWDPEAVRRVLDSDLDIQMVGLESTEELPLTDELRQHWASLrKYPAIDLVG--LGYS 231
Cdd:COG1957 151 GGAFFVPGNVTPV-----AEFNIYVDPEAAKIVFASGIPITMVGLDVTHQALLTPEDLARLAAL-GTPLGRFLAdlLDFY 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489743384 232 LIIS---VPNAELYLWDVLTTMSALYPELVETRQIKANVITSG-LASGRMFIDPNGKEITE-----VTKADKDSFFEKID 302
Cdd:COG1957 225 LDFYrerYGLDGCPLHDPLAVAYLLDPELFTTRPAPVDVETDGeLTRGQTVVDWRGVTGRPpnarvALDVDAERFLDLLL 304
|
....*.
gi 489743384 303 KILERQ 308
Cdd:COG1957 305 ERLARL 310
|
|
| IU_nuc_hydro |
pfam01156 |
Inosine-uridine preferring nucleoside hydrolase; |
4-299 |
1.46e-44 |
|
Inosine-uridine preferring nucleoside hydrolase;
Pssm-ID: 460086 [Multi-domain] Cd Length: 253 Bit Score: 151.98 E-value: 1.46e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489743384 4 IYFNHDGNIDDLVSLLLLLQAPDIKLIGISAIDGDGYIDPAVEACRKMVDKFNLrgDKLEVARsnsraihqfpkewrmat 83
Cdd:pfam01156 1 VIIDTDPGIDDALALLLALASPEIELLGITTVAGNVSLEQTTRNALRLLELGGR--DDIPVYA----------------- 61
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489743384 84 ysfnyfpilnesGEIktpeaplpahldmidkIKKAdGPVTLIMTGPITDLARALDEDASIQSKIEKVYWMGGSLDGHGNV 163
Cdd:pfam01156 62 ------------GEA----------------IREP-GEVTLVATGPLTNLALALRLDPELAKKIKELVIMGGAFGVRGNV 112
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489743384 164 VSVdadetQEWNAFWDPEAVRRVLDSDLDIQMVGLESTEELPLTDELRQHWASLRKYPAIDLVGL----GYSLIISVPNA 239
Cdd:pfam01156 113 TPA-----AEFNIFVDPEAAKIVFTSGLPITMVPLDVTHQALLTPEDLERLAALGTPLGRFLADLlrfyAEFYRERFGID 187
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 489743384 240 ELYLWDVLTTMSALYPELVETRQIKANVITSG-LASGRMFIDPNGKEITE-----VTKADKDSFFE 299
Cdd:pfam01156 188 GPPLHDPLAVAVALDPELFTTRRLNVDVETTGgLTRGQTVVDDRGGWGKPpnvrvATDVDVDRFWE 253
|
|
| PTZ00313 |
PTZ00313 |
inosine-adenosine-guanosine-nucleoside hydrolase; Provisional |
2-298 |
2.21e-30 |
|
inosine-adenosine-guanosine-nucleoside hydrolase; Provisional
Pssm-ID: 140334 [Multi-domain] Cd Length: 326 Bit Score: 116.89 E-value: 2.21e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489743384 2 KNIYFNHDGNIDDLVSLLLLLQAPD-IKLIGISAIDGDGYIDPAVEACRKMVDKFNLRGDK--LEVARSNSRAIHQFPKE 78
Cdd:PTZ00313 3 KPVILDHDGNHDDLVALALLLGNPEkVKVIGCICTDADCFVDDAFNVTGKLMCMMHAREATplFPIGKSSFKGVNPFPSE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489743384 79 WRMATYSFNYFPILNESGEIKTPEAPLP---AHLD---MIDKIKKADGPVTLIMTGPITDLARALDE-DASIQSKIEKVY 151
Cdd:PTZ00313 83 WRWSAKNMDDLPCLNIPEHVAIWEKLKPeneALVGeelLADLVMSSPEKVTICVTGPLSNVAWCIEKyGEEFTKKVEECV 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489743384 152 WMGGSLDGHGNVVSVDADETQEWNAFWDPEAVRRVLD-SDLDIQMVGLESTEELPLTDELRQHWASLRKYPAIDLVGLGY 230
Cdd:PTZ00313 163 IMGGAVDVGGNVFLPGTDGSAEWNIYWDPPAAKTVLMcPHIRKVLFSLDSTNSVPVTSEVVKKFGAQNKYLLSQFVGSTW 242
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 489743384 231 SLIISV----PNAELYLWDVLTTMSALYPELVETRQIKANV-ITSGLASGRMFIDPNGKEITEVTKADKDSFF 298
Cdd:PTZ00313 243 AMCTHHellrPGDGYYAWDVLTAAYVIERNLAELEPVPLEVvVEKAKNEGRTRRAAEGAACTYVAKNTNAELF 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 |
2.34e-123 |
|
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: 355.57 E-value: 2.34e-123
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489743384 2 KNIYFNHDGNIDDLVSLLLLLQ--APDIKLIGISAIDGDGYIDPAVEACRKMVDKFNlRGDKLEVARSNSRAIHQFPKEW 79
Cdd:cd02647 1 KNVIFDHDGNVDDLVALLLLLKneKVDLKGIGVSGIDADCYVEPAVSVTRKLIDRLG-QRDAIPVGKGGSRAVNPFPRSW 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489743384 80 RMAT-YSFNYFPILNESGEIKTPEAPLPAHLDMIDKIKKADGPVTLIMTGPITDLARALDEDASIQSKIEKVYWMGGSLD 158
Cdd:cd02647 80 RRDAaFSVDHLPILNERYTVETPLAEETAQLVLIEKIKASLEPVTLLVTGPLTNLARALDSDPDISSNIEEVYIMGGGVD 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489743384 159 GHGNVVSVDADETQEWNAFWDPEAVRRVLDSDLDIQMVGLESTEELPLTDEL----RQHWASLRKyPAIDLVGLGYSLII 234
Cdd:cd02647 160 APGNVFTPPSNGTAEFNIFWDPLAAKTVFDSGLKITLVPLDATNTVPLTREFletdRQRFAAQRL-PASDLAGQGYALVK 238
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 489743384 235 SVP-NAELYLWDVLTTMSALYPELVETRQIK-ANVITSGLASGRMFIDPNGKEITEVTKADKDSFFEKIDKILE 306
Cdd:cd02647 239 PLEfNSTYYMWDVLTTLVLGAKEVDNTKESLiLEVDTDGLSAGQTVTSPNGRPLTLVTSNNSYGSNRFFDDYLE 312
|
|
| URH1 |
COG1957 |
Inosine-uridine nucleoside N-ribohydrolase [Nucleotide transport and metabolism]; ... |
1-308 |
4.83e-66 |
|
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: 209.24 E-value: 4.83e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489743384 1 MKNIYFNHDGNIDDLVSLLLLLQAPDIKLIGISAIDGDGYIDPAVEACRKMVDKFNLrgDKLEVARSNSRAIHqfpKEWR 80
Cdd:COG1957 2 MRKVIIDTDPGIDDALALLLALASPEIDLLGITTVAGNVPLEQTTRNALKLLELAGR--TDVPVAAGAARPLV---RPLV 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489743384 81 MATYsfnyfpILNESG-------EIKTPEAPLPAHLDMIDKIKKADGPVTLIMTGPITDLARALDEDASIQSKIEKVYWM 153
Cdd:COG1957 77 TAEH------VHGEDGlggvdlpEPTRPPEPEHAVDFIIETLRAAPGEVTLVALGPLTNLALALRKDPELAERIKRIVIM 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489743384 154 GGSLDGHGNVVSVdadetQEWNAFWDPEAVRRVLDSDLDIQMVGLESTEELPLTDELRQHWASLrKYPAIDLVG--LGYS 231
Cdd:COG1957 151 GGAFFVPGNVTPV-----AEFNIYVDPEAAKIVFASGIPITMVGLDVTHQALLTPEDLARLAAL-GTPLGRFLAdlLDFY 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489743384 232 LIIS---VPNAELYLWDVLTTMSALYPELVETRQIKANVITSG-LASGRMFIDPNGKEITE-----VTKADKDSFFEKID 302
Cdd:COG1957 225 LDFYrerYGLDGCPLHDPLAVAYLLDPELFTTRPAPVDVETDGeLTRGQTVVDWRGVTGRPpnarvALDVDAERFLDLLL 304
|
....*.
gi 489743384 303 KILERQ 308
Cdd:COG1957 305 ERLARL 310
|
|
| IU_nuc_hydro |
pfam01156 |
Inosine-uridine preferring nucleoside hydrolase; |
4-299 |
1.46e-44 |
|
Inosine-uridine preferring nucleoside hydrolase;
Pssm-ID: 460086 [Multi-domain] Cd Length: 253 Bit Score: 151.98 E-value: 1.46e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489743384 4 IYFNHDGNIDDLVSLLLLLQAPDIKLIGISAIDGDGYIDPAVEACRKMVDKFNLrgDKLEVARsnsraihqfpkewrmat 83
Cdd:pfam01156 1 VIIDTDPGIDDALALLLALASPEIELLGITTVAGNVSLEQTTRNALRLLELGGR--DDIPVYA----------------- 61
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489743384 84 ysfnyfpilnesGEIktpeaplpahldmidkIKKAdGPVTLIMTGPITDLARALDEDASIQSKIEKVYWMGGSLDGHGNV 163
Cdd:pfam01156 62 ------------GEA----------------IREP-GEVTLVATGPLTNLALALRLDPELAKKIKELVIMGGAFGVRGNV 112
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489743384 164 VSVdadetQEWNAFWDPEAVRRVLDSDLDIQMVGLESTEELPLTDELRQHWASLRKYPAIDLVGL----GYSLIISVPNA 239
Cdd:pfam01156 113 TPA-----AEFNIFVDPEAAKIVFTSGLPITMVPLDVTHQALLTPEDLERLAALGTPLGRFLADLlrfyAEFYRERFGID 187
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 489743384 240 ELYLWDVLTTMSALYPELVETRQIKANVITSG-LASGRMFIDPNGKEITE-----VTKADKDSFFE 299
Cdd:pfam01156 188 GPPLHDPLAVAVALDPELFTTRRLNVDVETTGgLTRGQTVVDDRGGWGKPpnvrvATDVDVDRFWE 253
|
|
| nuc_hydro |
cd00455 |
nuc_hydro: Nucleoside hydrolases. Nucleoside hydrolases cleave the N-glycosidic bond in ... |
4-304 |
7.68e-40 |
|
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: 140.93 E-value: 7.68e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489743384 4 IYFNHDGNIDDLVSLLLLLQAPDIKLIGISAIDGDGYIDPAVEACRKMVDKFNLRGdkLEVARSNSRAIHQFPKEWRMAT 83
Cdd:cd00455 1 VILDTDPGIDDAFALMYALLHPEIELVGIVATYGNVTLEQATQNAAYLLELLGRLD--IPVYAGATRPLTGEIPAAYPEI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489743384 84 YSFNYFPILNEsgeIKTPEAPLPAHLDMIDKIKKADGPVTLIMTGPITDLARALDEDASIQSKIEKVYWMGGSLDGHGNV 163
Cdd:cd00455 79 HGEGGLGLPIP---PIIEADDPEAVQLLIDLIRKYPDEITIVALGPLTNLAMAFILDPDIKDRVKEIVIMGGAFLVPGNV 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489743384 164 VSVDadetqEWNAFWDPEAVRRVLDSDLDIQMVGLESTEELPLTDELRQHWASLRKYPA--IDLVGLGYSLIISVP-NAE 240
Cdd:cd00455 156 TPVA-----EANFYGDPEAANIVFNSAKNLTIVPLDVTNQAVLTPPMVERIFEQGTSIGllIKPMIDYYYKAYQKPgIEG 230
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 489743384 241 LYLWDVLTTMSALYPELVETRQIKANVITSGLASGRMFIDPNGKEITEVTKADKDSFFEK-IDKI 304
Cdd:cd00455 231 SPIHDPLAVAYLLNPSMFDYSKVPVDVDTDGLTRGQTIADFRENPGNGVTRVAVNLDYPDfIELI 295
|
|
| PTZ00313 |
PTZ00313 |
inosine-adenosine-guanosine-nucleoside hydrolase; Provisional |
2-298 |
2.21e-30 |
|
inosine-adenosine-guanosine-nucleoside hydrolase; Provisional
Pssm-ID: 140334 [Multi-domain] Cd Length: 326 Bit Score: 116.89 E-value: 2.21e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489743384 2 KNIYFNHDGNIDDLVSLLLLLQAPD-IKLIGISAIDGDGYIDPAVEACRKMVDKFNLRGDK--LEVARSNSRAIHQFPKE 78
Cdd:PTZ00313 3 KPVILDHDGNHDDLVALALLLGNPEkVKVIGCICTDADCFVDDAFNVTGKLMCMMHAREATplFPIGKSSFKGVNPFPSE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489743384 79 WRMATYSFNYFPILNESGEIKTPEAPLP---AHLD---MIDKIKKADGPVTLIMTGPITDLARALDE-DASIQSKIEKVY 151
Cdd:PTZ00313 83 WRWSAKNMDDLPCLNIPEHVAIWEKLKPeneALVGeelLADLVMSSPEKVTICVTGPLSNVAWCIEKyGEEFTKKVEECV 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489743384 152 WMGGSLDGHGNVVSVDADETQEWNAFWDPEAVRRVLD-SDLDIQMVGLESTEELPLTDELRQHWASLRKYPAIDLVGLGY 230
Cdd:PTZ00313 163 IMGGAVDVGGNVFLPGTDGSAEWNIYWDPPAAKTVLMcPHIRKVLFSLDSTNSVPVTSEVVKKFGAQNKYLLSQFVGSTW 242
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 489743384 231 SLIISV----PNAELYLWDVLTTMSALYPELVETRQIKANV-ITSGLASGRMFIDPNGKEITEVTKADKDSFF 298
Cdd:PTZ00313 243 AMCTHHellrPGDGYYAWDVLTAAYVIERNLAELEPVPLEVvVEKAKNEGRTRRAAEGAACTYVAKNTNAELF 315
|
|
| nuc_hydro_CaPnhB |
cd02650 |
NH_hydro_CaPnhB: A subgroup of nucleoside hydrolases similar to Corynebacterium ammoniagenes ... |
4-284 |
5.82e-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: 5.82e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489743384 4 IYFNHDGNIDDLVSLLLLLQAPDIKLIGISAIDGDGYIDPAVEACRKMVDKFNlRGDkLEVARSNSRAIHQFPKEWRMAT 83
Cdd:cd02650 2 LILDTDPGIDDAMALAYALAHPDVDLIGVTTVYGNVTIETATRNALALLELFG-RPD-VPVAEGAAKPLTRPPFRIATFV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489743384 84 YSFNYFPILNESGEIKTPEAPlPAHLDMIDKIKKADGPVTLIMTGPITDLARALDEDASIQSKIEKVYWMGGSLDGHGNV 163
Cdd:cd02650 80 HGDNGLGDVELPAPPRQPEDE-SAADFLIELANEYPGELTLVAVGPLTNLALALARDPDFAKLVKQVVVMGGAFTVPGNV 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489743384 164 VSVdadetQEWNAFWDPEAVRRVLDSDLDIQMVGLESTEELPLTDELRQHWASLrKYPAIDLVG--LGYSLIISVPNAEL 241
Cdd:cd02650 159 TPA-----AEANIHGDPEAADIVFTAGADLTMVGLDVTTQTLLTREDLDELRDS-GGKAGQFLAdmLDYYIDFYQESPGL 232
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 489743384 242 ---YLWDVLTTMSALYPELVETRQIKANVITSGLASGRMFIDPNGK 284
Cdd:cd02650 233 rgcALHDPLAVAAAVDPSLFTTREGVVRVETEGPTRGRTIGDRDGR 278
|
|
| nuc_hydro_IU_UC_XIUA |
cd02651 |
nuc_hydro_IU_UC_XIUA: inosine-uridine preferring, ... |
4-305 |
1.24e-27 |
|
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: 108.79 E-value: 1.24e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489743384 4 IYFNHDGNIDDLVSLLLLLQAPDIKLIGISAIDGDGYIDPAVEACRKMVDKFNlRGDkLEVARSNSRAIHqfpKEWRMAT 83
Cdd:cd02651 2 IIIDCDPGHDDAVAILLALFHPELDLLGITTVAGNVPLEKTTRNALKLLTLLG-RTD-VPVAAGAARPLV---RPLITAS 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489743384 84 YsfnyfpILNESG-------EIKTPEAPLPAHLDMIDKIKKADGPVTLIMTGPITDLARALDEDASIQSKIEKVYWMGGS 156
Cdd:cd02651 77 D------IHGESGldgadlpPPPRRPEDIHAVDAIIDTLRASPEPITLVATGPLTNIALLLRKYPELAERIKEIVLMGGA 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489743384 157 LdGHGNVVSVdadetQEWNAFWDPEAVRRVLDSDLDIQMVGLESTEELPLTDELRQHWASLRKYPAIDLVGL------GY 230
Cdd:cd02651 151 L-GRGNITPA-----AEFNIFVDPEAAKIVFNSGIPITMVPLDVTHKALATPEVIERIRALGNPVGKMLAELldffaeTY 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489743384 231 SliiSVPNAELYLWDVLTTMSALYPELVETRQIKANVITSG-LASGRMFIDPNGKEITE-----VTKADKDSFFEKIDKI 304
Cdd:cd02651 225 G---SAFTEGPPLHDPCAVAYLLDPELFTTKRANVDVETEGeLTRGRTVVDLRGVTGRPanaqvAVDVDVEKFWDLLLEA 301
|
.
gi 489743384 305 L 305
Cdd:cd02651 302 L 302
|
|
| PRK10768 |
PRK10768 |
ribonucleoside hydrolase RihC; Provisional |
1-304 |
1.43e-19 |
|
ribonucleoside hydrolase RihC; Provisional
Pssm-ID: 182713 [Multi-domain] Cd Length: 304 Bit Score: 86.89 E-value: 1.43e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489743384 1 MKNIYFNHDGNIDDLVSLLLLLQAPDIKLIGISAIDGDGYIDPAVEACRKMVDKFNlrgDKLEVAR----------SNSR 70
Cdd:PRK10768 2 RLPIILDTDPGIDDAVAIAAALFAPELDLKLITTVAGNVSVEKTTRNALKLLHFFN---SDVPVAQgaakplvrplRDAA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489743384 71 AIHqfpKEWRMATYSFnyfpilnesGEIKTPEAPLPAHLDMIDKIKKADGPVTLIMTGPITDLARALDEDASIQSKIEKV 150
Cdd:PRK10768 79 SVH---GESGMEGYDF---------PEHTRKPLSIPAVEAMRDALMNAPEPVTLVAIGPLTNIALLLSTYPEVKPYIKRI 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489743384 151 YWMGGSLdGHGNVVSVdadetQEWNAFWDPEAVRRVLDSDLDIQMVGLESTEELPLTDElrqhwaSLRKYPAIDLVG-LG 229
Cdd:PRK10768 147 VLMGGSA-GRGNVTPN-----AEFNIAVDPEAAAIVFRSGIPIVMCGLDVTNQALLTPD------YLATLPELNRTGkML 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489743384 230 YSLII-----SVPNAeLYLWDVLTTMSALYPELVETRQIKANVITSG-LASGRMFID--------PNGKEITEV-TKADK 294
Cdd:PRK10768 215 HALFShyrsgSMQTG-LRMHDVCAIAYLLRPELFTLKPCFVDVETQGeFTAGATVVDidgrlgkpANAQVALDIdVDGFQ 293
|
330
....*....|
gi 489743384 295 DSFFEKIDKI 304
Cdd:PRK10768 294 KWFAEVLALA 303
|
|
| nuc_hydro_CjNH |
cd02654 |
nuc_hydro_CjNH. Nucleoside hydrolases similar to Campylobacter jejuni nucleoside hydrolase. ... |
10-258 |
2.33e-19 |
|
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: 86.45 E-value: 2.33e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489743384 10 GNIDDLVSLLLLLQAPDIKLIGISAIDGDgyiDPAVEACRKMVDKFNLRG-DKLEVARSNSRAIHQFPKEWRM------A 82
Cdd:cd02654 12 RDTDDGLALALLLWSPEVELLGLSAVSGN---CWLSAVTYNVLRMLELAGaDAIPVYAGANTPLGRTNRAFHAweslygA 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489743384 83 TYSFNYF---PILNESGEIKTPEAPLPAHLDMIDKIKKADGPVTLIMTGPITDLARALDEDASIQSKIEKVYWMGGSLDG 159
Cdd:cd02654 89 YLWQGAWspeYSDMYTNASIIRNASIPAALFMIEMVRKHPHEVSIVAAGPLTNLALALRIDPDFAPLAKELVIMGGYLDD 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489743384 160 HGNvvSVDADETQEWNAFWDPEAVRRVLDSDLDIQMVGLESTEELPLTDELRQHWASLRKY-PAIDLVGLGYSLIISVPN 238
Cdd:cd02654 169 IGE--FVNRHYASDFNLIMDPEAASIVLTAPWKSITIPGNVTNRTCLTPEQIKADDPLRDFiRETLDLPIDYAKEFVGTG 246
|
250 260
....*....|....*....|
gi 489743384 239 AELYLWDVLTTMSALYPELV 258
Cdd:cd02654 247 DGLPMWDELASAVALDPELA 266
|
|
| nuc_hydro_CeIAG |
cd02649 |
nuc_hydro_CeIAG: Nucleoside hydrolases similar to the inosine-adenosine-guanosine-preferring ... |
107-302 |
7.97e-19 |
|
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: 84.62 E-value: 7.97e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489743384 107 AHLDMIDKIKKADGPVTLIMTGPITDLARALDEDASIQSKIEKVYWMGGSLDGHGNVVSvdadeTQEWNAFWDPEAVRRV 186
Cdd:cd02649 104 AVDAIIRLVREYPGEITLVALGPLTNLALAYRLDPSLPQKIKRLYIMGGNREGVGNTTP-----AAEFNFHVDPEAAHIV 178
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489743384 187 LDSD-LDIQMVGLESTEEL-PLTDELRQHWASLRKYP--AIDLVGLGYSLIISVPNAELY-LWDVLTTMSALYPELVeTR 261
Cdd:cd02649 179 LNSFgCPITIVPWETTLLAfPLDWEFEDKWANRLEKAlfAESLNRREYAFASEGLGGDGWvPCDALAVAAALDPSII-TR 257
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 489743384 262 QIKANV---ITSGLASGRMFIDPNGK-----EITEVTKADKDSFFEKID 302
Cdd:cd02649 258 RLTYAVdveLHGELTRGQMVVDWLGTlkkkpNARVITKIDREKFKELLY 306
|
|
| nuc_hydro_3 |
cd02653 |
NH_3: A subgroup of nucleoside hydrolases. This group contains eukaryotic and bacterial ... |
9-307 |
8.39e-18 |
|
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: 82.04 E-value: 8.39e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489743384 9 DGNIDDLVSLLLLLQAPDIKLIGISAIDGDGYIDPAVEACRKMVDKFNLRGdkLEVARSNSraihqFPKEWRMATYSFNY 88
Cdd:cd02653 7 DPGIDDALALLYLLASPDLDVVGITTTAGNVPVEQVAANALGVLELLGRTD--IPVYLGAD-----KPLAGPLTTAQDTH 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489743384 89 FPI-LNESgEIKTPEAPLPAH--LDMIDKIKKADGPVTLIMTGPITDLARALDEDASIQSKIEKVYWMGGSLDGHGNvVS 165
Cdd:cd02653 80 GPDgLGYA-ELPASTRTLSDEsaAQAWVDLARAHPDLIGLATGPLTNLALALREEPELPRLLRRLVIMGGAFNSRGN-TS 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489743384 166 VDAdetqEWNAFWDPEAVRRVLD----SDLDIQMVGLESTEELPLTDELRQ-----------------------HWAslr 218
Cdd:cd02653 158 PVA----EWNYWVDPEAAKEVLAafggHPVRPTICGLDVTRAVVLTPNLLErlarakdsvgafiedalrfyfefHWA--- 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489743384 219 kypaidlVGLGYSLIISvpnaelylwDVLTTMSALYPELVETRQIKANVITSGLASGRMFID--------PNGKEITEVT 290
Cdd:cd02653 231 -------YGHGYGAVIH---------DPLAAAVALNPNLARGRPAYVDVECTGVLTGQTVVDwagfwgkgANAEILTKVD 294
|
330
....*....|....*...
gi 489743384 291 KAD-KDSFFEKIDKILER 307
Cdd:cd02653 295 SQDfMALFIERVLAIADT 312
|
|
| PLN02717 |
PLN02717 |
uridine nucleosidase |
9-290 |
1.65e-14 |
|
uridine nucleosidase
Pssm-ID: 178319 [Multi-domain] Cd Length: 316 Bit Score: 72.72 E-value: 1.65e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489743384 9 DGNIDDLVSLLLLLQAPDIKLIGISAIDGDGYIDPAVEACRKMVDKFNlRGDkLEVARSNSRAIHQFPKEwRMATYSFNy 88
Cdd:PLN02717 8 DPGIDDAMAILMALRSPEVEVIGLTTIFGNVTTKLATRNALHLLEMAG-RPD-VPVAEGSHEPLKGGTKP-RIADFVHG- 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489743384 89 fpiLNESGEIKTPEaPLPAHLDM------IDKIKKADGPVTLIMTGPITDLARALDEDASIQSKIEKVYWMGGSLDGHGN 162
Cdd:PLN02717 84 ---SDGLGNTNLPP-PKGKKIEKsaaeflVEKVSEYPGEVTVVALGPLTNLALAIKLDPSFAKKVGQIVVLGGAFFVNGN 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489743384 163 VvsvdaDETQEWNAFWDPEAVRRVLDSDLDIQMVGLESTEELPLTD----ELRQHWASLRKYPAiDLVGLGYSLIISVPN 238
Cdd:PLN02717 160 V-----NPAAEANIFGDPEAADIVFTSGADITVVGINVTTQVVLTDadleELRDSKGKYAQFLC-DICKFYRDWHRKSYG 233
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 489743384 239 AE-LYLWDVLTTMSALYPELVETRQIKANVITSGLASGRMFIDPNGKEITEVT 290
Cdd:PLN02717 234 IDgIYLHDPTALLAAVRPSLFTYKEGVVRVETEGICRGLTLFDNGLKRWNGEN 286
|
|
| rihA |
PRK10443 |
ribonucleoside hydrolase 1; Provisional |
104-209 |
2.81e-13 |
|
ribonucleoside hydrolase 1; Provisional
Pssm-ID: 182465 [Multi-domain] Cd Length: 311 Bit Score: 68.93 E-value: 2.81e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489743384 104 PLPAHLDMIDKIKKADGPVTLIMTGPITDLARALDEDASIQSKIEKVYWMGGSLdGHGNVVSvdadeTQEWNAFWDPEAV 183
Cdd:PRK10443 101 NCTAVELMAKTLRESAEPVTLVSTGPQTNVALLLASHPELHSKIARIVIMGGAM-GLGNWTP-----AAEFNIYVDPEAA 174
|
90 100
....*....|....*....|....*.
gi 489743384 184 RRVLDSDLDIQMVGLESTEELPLTDE 209
Cdd:PRK10443 175 EIVFQSGIPIVMAGLDVTHKAQIMDE 200
|
|
| rihB |
PRK09955 |
ribosylpyrimidine nucleosidase; |
2-283 |
2.95e-13 |
|
ribosylpyrimidine nucleosidase;
Pssm-ID: 182166 [Multi-domain] Cd Length: 313 Bit Score: 68.82 E-value: 2.95e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489743384 2 KNIYFNHDGNIDDLVSLLLLLQAPDIKLIGISAIDGDGYIDpaveacRKMVDKFNLrGDKLEVarsNSRAIHQFPKE-WR 80
Cdd:PRK09955 4 RKIILDCDPGHDDAIAMMMAAKHPAIDLLGITIVAGNQTLD------KTLINGLNV-CQKLEI---NVPVYAGMPQPiMR 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489743384 81 MATYSFNYFPILNESGEIKTPEAPLPAHLD----MIDKIKKADGPVTLIMTGPITDLARALDEDASIQSKIEKVYWMGGS 156
Cdd:PRK09955 74 QQIVADNIHGETGLDGPVFEPLTRQAESTHavkyIIDTLMASDGDITLVPVGPLSNIAVAMRMQPAILPKIREIVLMGGA 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489743384 157 LdGHGNVVSvdadeTQEWNAFWDPEAVRRVLDSDLDIQMVGLESTEELPLTDELRQHWASLRKyPAIDLVG--LGYSLII 234
Cdd:PRK09955 154 Y-GTGNFTP-----SAEFNIFADPEAARVVFTSGVPLVMMGLDLTNQTVCTPDVIARMERAGG-PAGELFSdiMNFTLKT 226
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 489743384 235 SVPNAELY---LWDVLTTMSALYPELVETRQIKANV-ITSGLASGRMFIDPNG 283
Cdd:PRK09955 227 QFENYGLAggpVHDATCIGYLINPDGIKTQEMYVEVdVNSGPCYGRTVCDELG 279
|
|
| nuc_hydro_1 |
cd02648 |
NH_1: A subgroup of nucleoside hydrolases. This group contains fungal proteins similar to ... |
87-188 |
4.52e-12 |
|
NH_1: A subgroup of nucleoside hydrolases. This group contains fungal proteins similar to nucleoside hydrolases. Nucleoside hydrolases cleave the N-glycosidic bond in nucleosides generating ribose and the respective base. These enzymes vary in their substrate specificity.
Pssm-ID: 239114 [Multi-domain] Cd Length: 367 Bit Score: 66.06 E-value: 4.52e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489743384 87 NYFPILNESGEIKTPEAPL--PAHLDMIDKIKKA-DGPVTLIMTGPITDLARALDEDASIQSKIEKVYWMGGSLDGHGNV 163
Cdd:cd02648 115 DFTPVETWIPEIVAPLTPSdkPAYDVILDILREEpDHTVTIAALGPLTNLAAAARKDPETFAKVGEVVVMGGAIDVPGNT 194
|
90 100
....*....|....*....|....*
gi 489743384 164 VSVdadetQEWNAFWDPEAVRRVLD 188
Cdd:cd02648 195 SPV-----AEFNCFADPYAAAVVID 214
|
|
| nuc_hydro_2 |
cd02652 |
NH_2: A subgroup of nucleoside hydrolases. This group contains eukaryotic and bacterial ... |
10-255 |
6.69e-10 |
|
NH_2: A subgroup of nucleoside hydrolases. This group contains eukaryotic and bacterial proteins similar to nucleoside hydrolases. Nucleoside hydrolases cleave the N-glycosidic bond in nucleosides generating ribose and the respective base. These enzymes vary in their substrate specificity.
Pssm-ID: 239118 [Multi-domain] Cd Length: 293 Bit Score: 59.05 E-value: 6.69e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489743384 10 GNIDDLVSLLLLLQAPDIKLIGISAIDGDGYIDPAVEAcrkmVDKFNLRGDKLEVARSNsraihqfpkewrMATYSFNYF 89
Cdd:cd02652 9 GDPDDALALALAHALQKCDLLAVTITLADASARRAIDA----VNRFYGRGDIPIGADYH------------GWPEDAKDH 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489743384 90 PILNESGEIKTPEAPLPAH-LDMIDK-----IKKADGPVTLIMTGPITDLARALDEDAS-------IQSKIEKVYWMGGS 156
Cdd:cd02652 73 AKFLLEGDRLHHDLESAEDaLDAVKAlrrllASAEDASVTIVSIGPLTNLAALLDADADpltgpelVRQKVKRLVVMGGA 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489743384 157 L-DGHGNVvsvdadETQEWNAFWDPEAVRRVLD--SDLDIQMVGLESTEELPLTdeLRQHWASLRKYPAIDLVGLGYSLi 233
Cdd:cd02652 153 FyDPDGNV------QHREYNFVTDPKAAQRVAGraQHLGIPVRIVWSGYELGEA--VSYPHVLVIAHPFNTPVFAAYWP- 223
|
250 260
....*....|....*....|..
gi 489743384 234 isvPNAELYLWDVLTTMSALYP 255
Cdd:cd02652 224 ---RSHRRPLWDPLTLLAAVRG 242
|
|
| |
