|
Name |
Accession |
Description |
Interval |
E-value |
| nuc_hydro_TvIAG |
cd02647 |
nuc_hydro_ TvIAG: Nucleoside hydrolases similar to the Inosine-adenosine-guanosine-preferring ... |
4-302 |
4.96e-126 |
|
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: 362.12 E-value: 4.96e-126
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17132380 4 QLVLMDHDGGVDDYLATMLLLTMDNVQLMGVVVT--PADCYVQPAVSATRKIIDLMGF-SHIPVAESTVRGINPFPRLYR 80
Cdd:cd02647 1 KNVIFDHDGNVDDLVALLLLLKNEKVDLKGIGVSgiDADCYVEPAVSVTRKLIDRLGQrDAIPVGKGGSRAVNPFPRSWR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17132380 81 RDS-FIVDHLPILNQTELIHTPLVEETGQDFMVRVLQEALEPVTLMVTGPLTTVAVALDQAPDIEAKIDKIVWMGGALNV 159
Cdd:cd02647 81 RDAaFSVDHLPILNERYTVETPLAEETAQLVLIEKIKASLEPVTLLVTGPLTNLARALDSDPDISSNIEEVYIMGGGVDA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17132380 160 PGNVEKSleaGQDGSAEWNVYWDAVSAARVWQREIKIIMCPLDLTNDVPVTSELVyKMGRQRHY----PVSDLAGQCYAL 235
Cdd:cd02647 161 PGNVFTP---PSNGTAEFNIFWDPLAAKTVFDSGLKITLVPLDATNTVPLTREFL-ETDRQRFAaqrlPASDLAGQGYAL 236
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 17132380 236 VIP----QDYYFWDVLATAYLGHPEfyqLREWE----TEIITSGLSQGRTKVVTGGRKILAMDKVDK----DAFYAYIL 302
Cdd:cd02647 237 VKPlefnSTYYMWDVLTTLVLGAKE---VDNTKesliLEVDTDGLSAGQTVTSPNGRPLTLVTSNNSygsnRFFDDYLE 312
|
|
| URH1 |
COG1957 |
Inosine-uridine nucleoside N-ribohydrolase [Nucleotide transport and metabolism]; ... |
2-307 |
2.64e-79 |
|
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: 243.14 E-value: 2.64e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17132380 2 TKQLVLMDHDGGVDDYLATMLLLTMDNVQLMGVVVTPADCYVQPAVSATRKIIDLMGFSHIPVAESTVRginPFPRLYRR 81
Cdd:COG1957 1 MMRKVIIDTDPGIDDALALLLALASPEIDLLGITTVAGNVPLEQTTRNALKLLELAGRTDVPVAAGAAR---PLVRPLVT 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17132380 82 DSFIvdH---------LPIlnqtelIHTPLVEETGQDFMVRVLQEALEPVTLMVTGPLTTVAVALDQAPDIEAKIDKIVW 152
Cdd:COG1957 78 AEHV--HgedglggvdLPE------PTRPPEPEHAVDFIIETLRAAPGEVTLVALGPLTNLALALRKDPELAERIKRIVI 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17132380 153 MGGALNVPGNVEKsleagqdgSAEWNVYWDAVSAARVWQREIKIIMCPLDLTNDVPVTSELVYKMgRQRHYPVSDLAGQC 232
Cdd:COG1957 150 MGGAFFVPGNVTP--------VAEFNIYVDPEAAKIVFASGIPITMVGLDVTHQALLTPEDLARL-AALGTPLGRFLADL 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17132380 233 YALVIPQD--------YYFWDVLATAYLGHPEFYQLREWETEIITSG-LSQGRTKVVTGGR-----KILAMDKVDKDAFY 298
Cdd:COG1957 221 LDFYLDFYrerygldgCPLHDPLAVAYLLDPELFTTRPAPVDVETDGeLTRGQTVVDWRGVtgrppNARVALDVDAERFL 300
|
....*....
gi 17132380 299 AYILQQWAR 307
Cdd:COG1957 301 DLLLERLAR 309
|
|
| PTZ00313 |
PTZ00313 |
inosine-adenosine-guanosine-nucleoside hydrolase; Provisional |
6-302 |
1.69e-54 |
|
inosine-adenosine-guanosine-nucleoside hydrolase; Provisional
Pssm-ID: 140334 [Multi-domain] Cd Length: 326 Bit Score: 180.06 E-value: 1.69e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17132380 6 VLMDHDGGVDDYLATMLLLTM-DNVQLMGVVVTPADCYVQPAVSATRKIIDLMGFSH----IPVAESTVRGINPFPRLYR 80
Cdd:PTZ00313 5 VILDHDGNHDDLVALALLLGNpEKVKVIGCICTDADCFVDDAFNVTGKLMCMMHAREatplFPIGKSSFKGVNPFPSEWR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17132380 81 RDSFIVDHLPILNQTEliHTPLVEE--------TGQDFMVRVLQEALEPVTLMVTGPLTTVAVALDQ-APDIEAKIDKIV 151
Cdd:PTZ00313 85 WSAKNMDDLPCLNIPE--HVAIWEKlkpenealVGEELLADLVMSSPEKVTICVTGPLSNVAWCIEKyGEEFTKKVEECV 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17132380 152 WMGGALNVPGNVeksLEAGQDGSAEWNVYWDAVSAARVWQ-REIKIIMCPLDLTNDVPVTSELVYKMGRQRHYPVSDLAG 230
Cdd:PTZ00313 163 IMGGAVDVGGNV---FLPGTDGSAEWNIYWDPPAAKTVLMcPHIRKVLFSLDSTNSVPVTSEVVKKFGAQNKYLLSQFVG 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17132380 231 QCYA------LVIPQD-YYFWDVLATAYLGHPEFYQLREWETEI-ITSGLSQGRTKVVTGGRKILAMDK-VDKDAFYAYI 301
Cdd:PTZ00313 240 STWAmcthheLLRPGDgYYAWDVLTAAYVIERNLAELEPVPLEVvVEKAKNEGRTRRAAEGAACTYVAKnTNAELFYDMV 319
|
.
gi 17132380 302 L 302
Cdd:PTZ00313 320 L 320
|
|
| IU_nuc_hydro |
pfam01156 |
Inosine-uridine preferring nucleoside hydrolase; |
6-299 |
4.83e-52 |
|
Inosine-uridine preferring nucleoside hydrolase;
Pssm-ID: 460086 [Multi-domain] Cd Length: 253 Bit Score: 171.62 E-value: 4.83e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17132380 6 VLMDHDGGVDDYLATMLLLTMDNVQLMGVVVTPADCYVQPAVSATRKIIDLMGFSHIPVAestvRGinpfprlyrrdsfi 85
Cdd:pfam01156 1 VIIDTDPGIDDALALLLALASPEIELLGITTVAGNVSLEQTTRNALRLLELGGRDDIPVY----AG-------------- 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17132380 86 vdhlpilnqtELIHTPlveetgqdfmvrvlqealEPVTLMVTGPLTTVAVALDQAPDIEAKIDKIVWMGGALNVPGNVEK 165
Cdd:pfam01156 63 ----------EAIREP------------------GEVTLVATGPLTNLALALRLDPELAKKIKELVIMGGAFGVRGNVTP 114
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17132380 166 sleagqdgSAEWNVYWDAVSAARVWQREIKIIMCPLDLTNDVPVTSELVYKMGRQRHYPVSDLAG------QCYALVIPQ 239
Cdd:pfam01156 115 --------AAEFNIFVDPEAAKIVFTSGLPITMVPLDVTHQALLTPEDLERLAALGTPLGRFLADllrfyaEFYRERFGI 186
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 17132380 240 D-YYFWDVLATAYLGHPEFYQLREWETEIITSG-LSQGRTKVVTGGRK-----ILAMDKVDKDAFYA 299
Cdd:pfam01156 187 DgPPLHDPLAVAVALDPELFTTRRLNVDVETTGgLTRGQTVVDDRGGWgkppnVRVATDVDVDRFWE 253
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| nuc_hydro_TvIAG |
cd02647 |
nuc_hydro_ TvIAG: Nucleoside hydrolases similar to the Inosine-adenosine-guanosine-preferring ... |
4-302 |
4.96e-126 |
|
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: 362.12 E-value: 4.96e-126
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17132380 4 QLVLMDHDGGVDDYLATMLLLTMDNVQLMGVVVT--PADCYVQPAVSATRKIIDLMGF-SHIPVAESTVRGINPFPRLYR 80
Cdd:cd02647 1 KNVIFDHDGNVDDLVALLLLLKNEKVDLKGIGVSgiDADCYVEPAVSVTRKLIDRLGQrDAIPVGKGGSRAVNPFPRSWR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17132380 81 RDS-FIVDHLPILNQTELIHTPLVEETGQDFMVRVLQEALEPVTLMVTGPLTTVAVALDQAPDIEAKIDKIVWMGGALNV 159
Cdd:cd02647 81 RDAaFSVDHLPILNERYTVETPLAEETAQLVLIEKIKASLEPVTLLVTGPLTNLARALDSDPDISSNIEEVYIMGGGVDA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17132380 160 PGNVEKSleaGQDGSAEWNVYWDAVSAARVWQREIKIIMCPLDLTNDVPVTSELVyKMGRQRHY----PVSDLAGQCYAL 235
Cdd:cd02647 161 PGNVFTP---PSNGTAEFNIFWDPLAAKTVFDSGLKITLVPLDATNTVPLTREFL-ETDRQRFAaqrlPASDLAGQGYAL 236
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 17132380 236 VIP----QDYYFWDVLATAYLGHPEfyqLREWE----TEIITSGLSQGRTKVVTGGRKILAMDKVDK----DAFYAYIL 302
Cdd:cd02647 237 VKPlefnSTYYMWDVLTTLVLGAKE---VDNTKesliLEVDTDGLSAGQTVTSPNGRPLTLVTSNNSygsnRFFDDYLE 312
|
|
| URH1 |
COG1957 |
Inosine-uridine nucleoside N-ribohydrolase [Nucleotide transport and metabolism]; ... |
2-307 |
2.64e-79 |
|
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: 243.14 E-value: 2.64e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17132380 2 TKQLVLMDHDGGVDDYLATMLLLTMDNVQLMGVVVTPADCYVQPAVSATRKIIDLMGFSHIPVAESTVRginPFPRLYRR 81
Cdd:COG1957 1 MMRKVIIDTDPGIDDALALLLALASPEIDLLGITTVAGNVPLEQTTRNALKLLELAGRTDVPVAAGAAR---PLVRPLVT 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17132380 82 DSFIvdH---------LPIlnqtelIHTPLVEETGQDFMVRVLQEALEPVTLMVTGPLTTVAVALDQAPDIEAKIDKIVW 152
Cdd:COG1957 78 AEHV--HgedglggvdLPE------PTRPPEPEHAVDFIIETLRAAPGEVTLVALGPLTNLALALRKDPELAERIKRIVI 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17132380 153 MGGALNVPGNVEKsleagqdgSAEWNVYWDAVSAARVWQREIKIIMCPLDLTNDVPVTSELVYKMgRQRHYPVSDLAGQC 232
Cdd:COG1957 150 MGGAFFVPGNVTP--------VAEFNIYVDPEAAKIVFASGIPITMVGLDVTHQALLTPEDLARL-AALGTPLGRFLADL 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17132380 233 YALVIPQD--------YYFWDVLATAYLGHPEFYQLREWETEIITSG-LSQGRTKVVTGGR-----KILAMDKVDKDAFY 298
Cdd:COG1957 221 LDFYLDFYrerygldgCPLHDPLAVAYLLDPELFTTRPAPVDVETDGeLTRGQTVVDWRGVtgrppNARVALDVDAERFL 300
|
....*....
gi 17132380 299 AYILQQWAR 307
Cdd:COG1957 301 DLLLERLAR 309
|
|
| PTZ00313 |
PTZ00313 |
inosine-adenosine-guanosine-nucleoside hydrolase; Provisional |
6-302 |
1.69e-54 |
|
inosine-adenosine-guanosine-nucleoside hydrolase; Provisional
Pssm-ID: 140334 [Multi-domain] Cd Length: 326 Bit Score: 180.06 E-value: 1.69e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17132380 6 VLMDHDGGVDDYLATMLLLTM-DNVQLMGVVVTPADCYVQPAVSATRKIIDLMGFSH----IPVAESTVRGINPFPRLYR 80
Cdd:PTZ00313 5 VILDHDGNHDDLVALALLLGNpEKVKVIGCICTDADCFVDDAFNVTGKLMCMMHAREatplFPIGKSSFKGVNPFPSEWR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17132380 81 RDSFIVDHLPILNQTEliHTPLVEE--------TGQDFMVRVLQEALEPVTLMVTGPLTTVAVALDQ-APDIEAKIDKIV 151
Cdd:PTZ00313 85 WSAKNMDDLPCLNIPE--HVAIWEKlkpenealVGEELLADLVMSSPEKVTICVTGPLSNVAWCIEKyGEEFTKKVEECV 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17132380 152 WMGGALNVPGNVeksLEAGQDGSAEWNVYWDAVSAARVWQ-REIKIIMCPLDLTNDVPVTSELVYKMGRQRHYPVSDLAG 230
Cdd:PTZ00313 163 IMGGAVDVGGNV---FLPGTDGSAEWNIYWDPPAAKTVLMcPHIRKVLFSLDSTNSVPVTSEVVKKFGAQNKYLLSQFVG 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17132380 231 QCYA------LVIPQD-YYFWDVLATAYLGHPEFYQLREWETEI-ITSGLSQGRTKVVTGGRKILAMDK-VDKDAFYAYI 301
Cdd:PTZ00313 240 STWAmcthheLLRPGDgYYAWDVLTAAYVIERNLAELEPVPLEVvVEKAKNEGRTRRAAEGAACTYVAKnTNAELFYDMV 319
|
.
gi 17132380 302 L 302
Cdd:PTZ00313 320 L 320
|
|
| IU_nuc_hydro |
pfam01156 |
Inosine-uridine preferring nucleoside hydrolase; |
6-299 |
4.83e-52 |
|
Inosine-uridine preferring nucleoside hydrolase;
Pssm-ID: 460086 [Multi-domain] Cd Length: 253 Bit Score: 171.62 E-value: 4.83e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17132380 6 VLMDHDGGVDDYLATMLLLTMDNVQLMGVVVTPADCYVQPAVSATRKIIDLMGFSHIPVAestvRGinpfprlyrrdsfi 85
Cdd:pfam01156 1 VIIDTDPGIDDALALLLALASPEIELLGITTVAGNVSLEQTTRNALRLLELGGRDDIPVY----AG-------------- 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17132380 86 vdhlpilnqtELIHTPlveetgqdfmvrvlqealEPVTLMVTGPLTTVAVALDQAPDIEAKIDKIVWMGGALNVPGNVEK 165
Cdd:pfam01156 63 ----------EAIREP------------------GEVTLVATGPLTNLALALRLDPELAKKIKELVIMGGAFGVRGNVTP 114
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17132380 166 sleagqdgSAEWNVYWDAVSAARVWQREIKIIMCPLDLTNDVPVTSELVYKMGRQRHYPVSDLAG------QCYALVIPQ 239
Cdd:pfam01156 115 --------AAEFNIFVDPEAAKIVFTSGLPITMVPLDVTHQALLTPEDLERLAALGTPLGRFLADllrfyaEFYRERFGI 186
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 17132380 240 D-YYFWDVLATAYLGHPEFYQLREWETEIITSG-LSQGRTKVVTGGRK-----ILAMDKVDKDAFYA 299
Cdd:pfam01156 187 DgPPLHDPLAVAVALDPELFTTRRLNVDVETTGgLTRGQTVVDDRGGWgkppnVRVATDVDVDRFWE 253
|
|
| nuc_hydro |
cd00455 |
nuc_hydro: Nucleoside hydrolases. Nucleoside hydrolases cleave the N-glycosidic bond in ... |
6-277 |
5.18e-45 |
|
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: 154.41 E-value: 5.18e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17132380 6 VLMDHDGGVDDYLATMLLLTMDNVQLMGVVVTPADCYVQPAVSATRKIIDLMGFSHIPVAESTVRGINPFPRLYRrdsFI 85
Cdd:cd00455 1 VILDTDPGIDDAFALMYALLHPEIELVGIVATYGNVTLEQATQNAAYLLELLGRLDIPVYAGATRPLTGEIPAAY---PE 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17132380 86 VDHLPILNQTELIHTPLVEETGQDFMVRVLQEALEPVTLMVTGPLTTVAVALDQAPDIEAKIDKIVWMGGALNVPGNVek 165
Cdd:cd00455 78 IHGEGGLGLPIPPIIEADDPEAVQLLIDLIRKYPDEITIVALGPLTNLAMAFILDPDIKDRVKEIVIMGGAFLVPGNV-- 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17132380 166 sleagqDGSAEWNVYWDAVSAARVWQREIKIIMCPLDLTNDVPVTSELVYKMGRQrHYPVSDLAGQ-------CYALVIP 238
Cdd:cd00455 156 ------TPVAEANFYGDPEAANIVFNSAKNLTIVPLDVTNQAVLTPPMVERIFEQ-GTSIGLLIKPmidyyykAYQKPGI 228
|
250 260 270
....*....|....*....|....*....|....*....
gi 17132380 239 QDYYFWDVLATAYLGHPEFYQLREWETEIITSGLSQGRT 277
Cdd:cd00455 229 EGSPIHDPLAVAYLLNPSMFDYSKVPVDVDTDGLTRGQT 267
|
|
| nuc_hydro_IU_UC_XIUA |
cd02651 |
nuc_hydro_IU_UC_XIUA: inosine-uridine preferring, ... |
6-305 |
5.37e-35 |
|
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: 128.43 E-value: 5.37e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17132380 6 VLMDHDGGVDDYLATMLLLTMDNVQLMGVVVtpadCYVQPAVSAT----RKIIDLMGFSHIPVAestvRGiNPFPRLyrR 81
Cdd:cd02651 2 IIIDCDPGHDDAVAILLALFHPELDLLGITT----VAGNVPLEKTtrnaLKLLTLLGRTDVPVA----AG-AARPLV--R 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17132380 82 DSFIVDHlpI-----LNQTELIHTPLVEETGQ--DFMVRVLQEALEPVTLMVTGPLTTVAVALDQAPDIEAKIDKIVWMG 154
Cdd:cd02651 71 PLITASD--IhgesgLDGADLPPPPRRPEDIHavDAIIDTLRASPEPITLVATGPLTNIALLLRKYPELAERIKEIVLMG 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17132380 155 GALNVpGNVEKsleagqdgSAEWNVYWDAVSAARVWQREIKIIMCPLDLTNDVPVTSELV---YKMGRQRHYPVSDLA-- 229
Cdd:cd02651 149 GALGR-GNITP--------AAEFNIFVDPEAAKIVFNSGIPITMVPLDVTHKALATPEVIeriRALGNPVGKMLAELLdf 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17132380 230 -GQCYALVIPQDYYFWDVLATAYLGHPEFYQLREWETEIITSG-LSQGRTKVVTGGRK-----ILAMDKVDKDAFYAYIL 302
Cdd:cd02651 220 fAETYGSAFTEGPPLHDPCAVAYLLDPELFTTKRANVDVETEGeLTRGRTVVDLRGVTgrpanAQVAVDVDVEKFWDLLL 299
|
...
gi 17132380 303 QQW 305
Cdd:cd02651 300 EAL 302
|
|
| nuc_hydro_CaPnhB |
cd02650 |
NH_hydro_CaPnhB: A subgroup of nucleoside hydrolases similar to Corynebacterium ammoniagenes ... |
6-302 |
1.49e-30 |
|
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: 116.61 E-value: 1.49e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17132380 6 VLMDHDGGVDDYLATMLLLTMDNVQLMGVVVTPADCYVQPAVSATRKIIDLMGFSHIPVAESTVRGInpFPRLYRRDSFI 85
Cdd:cd02650 2 LILDTDPGIDDAMALAYALAHPDVDLIGVTTVYGNVTIETATRNALALLELFGRPDVPVAEGAAKPL--TRPPFRIATFV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17132380 86 --VDHLPILNQTELIhTPLVEETGQDFMVRVLQEALEPVTLMVTGPLTTVAVALDQAPDIEAKIDKIVWMGGALNVPGNV 163
Cdd:cd02650 80 hgDNGLGDVELPAPP-RQPEDESAADFLIELANEYPGELTLVAVGPLTNLALALARDPDFAKLVKQVVVMGGAFTVPGNV 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17132380 164 EKSLEAgqdgsaewNVYWDAVSAARVWQREIKIIMCPLDLTNDVPVTSELVYKMgRQRHYPVSDLAGQCYALVIpqDYY- 242
Cdd:cd02650 159 TPAAEA--------NIHGDPEAADIVFTAGADLTMVGLDVTTQTLLTREDLDEL-RDSGGKAGQFLADMLDYYI--DFYq 227
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 17132380 243 ---------FWDVLATAYLGHPEFYQLREWETEIITSGLSQGRTKVVTGGRKI--------LAMDKVDKDAFYAYIL 302
Cdd:cd02650 228 espglrgcaLHDPLAVAAAVDPSLFTTREGVVRVETEGPTRGRTIGDRDGRRFwdsspnatVAVDVDVDERFLKRLM 304
|
|
| PRK10768 |
PRK10768 |
ribonucleoside hydrolase RihC; Provisional |
6-304 |
5.18e-25 |
|
ribonucleoside hydrolase RihC; Provisional
Pssm-ID: 182713 [Multi-domain] Cd Length: 304 Bit Score: 101.91 E-value: 5.18e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17132380 6 VLMDHDGGVDDYLATMLLLTMDN--VQLMGVVvtpadcyvqpA--VS---ATRKIIDLMGF--SHIPVAestvRGIN-PF 75
Cdd:PRK10768 5 IILDTDPGIDDAVAIAAALFAPEldLKLITTV----------AgnVSvekTTRNALKLLHFfnSDVPVA----QGAAkPL 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17132380 76 PRLYRRDSFI-----------VDHlpilnQTELIHTPLVEEtgqdfMVRVLQEALEPVTLMVTGPLTTVAVALDQAPDIE 144
Cdd:PRK10768 71 VRPLRDAASVhgesgmegydfPEH-----TRKPLSIPAVEA-----MRDALMNAPEPVTLVAIGPLTNIALLLSTYPEVK 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17132380 145 AKIDKIVWMGGALNvPGNVEKsleagqdgSAEWNVYWDAVSAARVWQREIKIIMCPLDLTNDVPVTSELVYK---MGRQ- 220
Cdd:PRK10768 141 PYIKRIVLMGGSAG-RGNVTP--------NAEFNIAVDPEAAAIVFRSGIPIVMCGLDVTNQALLTPDYLATlpeLNRTg 211
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17132380 221 -------RHYPVSDLAGQcyalvIPqdyyFWDVLATAYLGHPEFYQLREWETEIITSG-LSQGRTKVVTGGRKI------ 286
Cdd:PRK10768 212 kmlhalfSHYRSGSMQTG-----LR----MHDVCAIAYLLRPELFTLKPCFVDVETQGeFTAGATVVDIDGRLGkpanaq 282
|
330
....*....|....*...
gi 17132380 287 LAMDkVDKDAFYAYILQQ 304
Cdd:PRK10768 283 VALD-IDVDGFQKWFAEV 299
|
|
| nuc_hydro_3 |
cd02653 |
NH_3: A subgroup of nucleoside hydrolases. This group contains eukaryotic and bacterial ... |
6-302 |
1.14e-23 |
|
NH_3: A subgroup of nucleoside hydrolases. This group contains eukaryotic and bacterial proteins similar to nucleoside hydrolases. Nucleoside hydrolases cleave the N-glycosidic bond in nucleosides generating ribose and the respective base. These enzymes vary in their substrate specificity.
Pssm-ID: 239119 [Multi-domain] Cd Length: 320 Bit Score: 98.60 E-value: 1.14e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17132380 6 VLMDHDGGVDDYLATMLLLTMDNVQLMGVVVTPADCYVQPAVSATRKIIDLMGFSHIPVAESTvrginPFPRLYRRDSFI 85
Cdd:cd02653 2 VIIDCDPGIDDALALLYLLASPDLDVVGITTTAGNVPVEQVAANALGVLELLGRTDIPVYLGA-----DKPLAGPLTTAQ 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17132380 86 VDHLPI-LNQTEL--IHTPLVEETGQDFMVRVLQEALEpVTLMVTGPLTTVAVALDQAPDIEAKIDKIVWMGGALNVPGN 162
Cdd:cd02653 77 DTHGPDgLGYAELpaSTRTLSDESAAQAWVDLARAHPD-LIGLATGPLTNLALALREEPELPRLLRRLVIMGGAFNSRGN 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17132380 163 VEKsleagqdgSAEWNVYWDAVSAARV----WQREIKIIMCPLDLTNDVPVTSELvykmgRQRHYPVSDLAGQCYALVIp 238
Cdd:cd02653 156 TSP--------VAEWNYWVDPEAAKEVlaafGGHPVRPTICGLDVTRAVVLTPNL-----LERLARAKDSVGAFIEDAL- 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17132380 239 qDYYF---W-----------DVLATAYLGHPEFYQLREWETEIITSGLSQGRTKVVTGGR-----KILAMDKVDKDAFYA 299
Cdd:cd02653 222 -RFYFefhWayghgygavihDPLAAAVALNPNLARGRPAYVDVECTGVLTGQTVVDWAGFwgkgaNAEILTKVDSQDFMA 300
|
...
gi 17132380 300 YIL 302
Cdd:cd02653 301 LFI 303
|
|
| rihA |
PRK10443 |
ribonucleoside hydrolase 1; Provisional |
1-279 |
1.33e-22 |
|
ribonucleoside hydrolase 1; Provisional
Pssm-ID: 182465 [Multi-domain] Cd Length: 311 Bit Score: 95.50 E-value: 1.33e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17132380 1 MTKQLVLmDHDGGVDDYLATMLLLTMDNVQLMGVVVTPADCYVQPAVSATRKIIDLMGFSHIPVAESTVRginPFPRlyr 80
Cdd:PRK10443 1 MALPIIL-DCDPGHDDAIALVLALASPELDVKAVTTSAGNQTPEKTLRNALRMLTLLNRTDIPVAGGAVK---PLMR--- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17132380 81 rdsfivdhlpilnqtELIHTPLVE-ETGQD------------------FMVRVLQEALEPVTLMVTGPLTTVAVALDQAP 141
Cdd:PRK10443 74 ---------------ELIIADNVHgESGLDgpalpeptfapqnctaveLMAKTLRESAEPVTLVSTGPQTNVALLLASHP 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17132380 142 DIEAKIDKIVWMGGALNVpGNVEKsleagqdgSAEWNVYWDAVSAARVWQREIKIIMCPLDLTNDVPVTSELVYKMgRQR 221
Cdd:PRK10443 139 ELHSKIARIVIMGGAMGL-GNWTP--------AAEFNIYVDPEAAEIVFQSGIPIVMAGLDVTHKAQIMDEDIERI-RAI 208
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 17132380 222 HYPVSdlagQCYALVIpqDYYF-------W--------DVLATAYLGHPEFYQLREWETEIITSG-LSQGRTKV 279
Cdd:PRK10443 209 GNPVA----TIVAELL--DFFMeyhkdekWgfvgaplhDPCTIAWLLKPELFTTVERWVGVETQGeYTQGMTVV 276
|
|
| rihB |
PRK09955 |
ribosylpyrimidine nucleosidase; |
1-277 |
7.18e-17 |
|
ribosylpyrimidine nucleosidase;
Pssm-ID: 182166 [Multi-domain] Cd Length: 313 Bit Score: 79.61 E-value: 7.18e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17132380 1 MTKQLVLMDHDGGVDDYLATMLLLTMDNVQLMGVVVTPADCYVQPAVSATRKIIDLMGFShIPVAEStvrginpFPRLYR 80
Cdd:PRK09955 1 MEKRKIILDCDPGHDDAIAMMMAAKHPAIDLLGITIVAGNQTLDKTLINGLNVCQKLEIN-VPVYAG-------MPQPIM 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17132380 81 RDSFIVDHlpILNQTEL---IHTPLVEET----GQDFMVRVLQEALEPVTLMVTGPLTTVAVALDQAPDIEAKIDKIVWM 153
Cdd:PRK09955 73 RQQIVADN--IHGETGLdgpVFEPLTRQAesthAVKYIIDTLMASDGDITLVPVGPLSNIAVAMRMQPAILPKIREIVLM 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17132380 154 GGALNVpGNVEKsleagqdgSAEWNVYWDAVSAARVWQREIKIIMCPLDLTNDVPVTSELVYKMGRQRHyPVSDLAGQCY 233
Cdd:PRK09955 151 GGAYGT-GNFTP--------SAEFNIFADPEAARVVFTSGVPLVMMGLDLTNQTVCTPDVIARMERAGG-PAGELFSDIM 220
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 17132380 234 ALVIPQDYYFW--------DVLATAYLGHPEFYQLREWETEI-ITSGLSQGRT 277
Cdd:PRK09955 221 NFTLKTQFENYglaggpvhDATCIGYLINPDGIKTQEMYVEVdVNSGPCYGRT 273
|
|
| nuc_hydro_CeIAG |
cd02649 |
nuc_hydro_CeIAG: Nucleoside hydrolases similar to the inosine-adenosine-guanosine-preferring ... |
5-217 |
1.59e-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: 78.45 E-value: 1.59e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17132380 5 LVLMDHDGGVDDYLATMLLLTMDNVQLMGVVVTPADCYVQPAVSATRKIIDLMGFSHIPV----AESTVRginpfPRLYR 80
Cdd:cd02649 2 KLIIDTDCGGDDAWALLMALASPNVEVLAITCVHGNTNVEQVVKNALRVLEACGRRDIPVyrgaSKPLLG-----PGPTA 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17132380 81 RDSFIVDHL-PILNQTELIHTPLVEETGQDFMVRVLQEALEPVTLMVTGPLTTVAVALDQAPDIEAKIDKIVWMGGALNV 159
Cdd:cd02649 77 AYFHGKDGFgDVGFPEPKDELELQKEHAVDAIIRLVREYPGEITLVALGPLTNLALAYRLDPSLPQKIKRLYIMGGNREG 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 17132380 160 PGNVEKsleagqdgSAEWNVYWDAVSAARVWQREIK-IIMCPLDLT-NDVPVTSELVYKM 217
Cdd:cd02649 157 VGNTTP--------AAEFNFHVDPEAAHIVLNSFGCpITIVPWETTlLAFPLDWEFEDKW 208
|
|
| nuc_hydro_1 |
cd02648 |
NH_1: A subgroup of nucleoside hydrolases. This group contains fungal proteins similar to ... |
6-206 |
5.16e-16 |
|
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: 77.62 E-value: 5.16e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17132380 6 VLMDHDGGVDDYLATMLLLTM-DNVQLMGVVVTPADCYVQPAVSATRKIIDLM---------------GFSH------IP 63
Cdd:cd02648 4 IIIDTDPGVDDVLAILLALSSpEEVDVALISLTFGNTTLDHALRNVLRLFHVLererawratpgvryrAFSAdaekpiVA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17132380 64 VAESTVRGINPFPRLY--RRD--SFIVDHLPILNQTEL----IHTPLV--EETGQDFMVRVLQEalEP---VTLMVTGPL 130
Cdd:cd02648 84 SGSDQPLEGERLTASYfhGRDglSGVHWLHPDFTPVETwipeIVAPLTpsDKPAYDVILDILRE--EPdhtVTIAALGPL 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17132380 131 TTVAVALDQAPDIEAKIDKIVWMGGALNVPGNVEKsleagqdgSAEWNVYWDAVSAARVW----------QREIKIIMCP 200
Cdd:cd02648 162 TNLAAAARKDPETFAKVGEVVVMGGAIDVPGNTSP--------VAEFNCFADPYAAAVVIdeppstapeaRRKLPLQVFP 233
|
....*.
gi 17132380 201 LDLTND 206
Cdd:cd02648 234 LDITTG 239
|
|
| PLN02717 |
PLN02717 |
uridine nucleosidase |
4-219 |
1.55e-15 |
|
uridine nucleosidase
Pssm-ID: 178319 [Multi-domain] Cd Length: 316 Bit Score: 75.41 E-value: 1.55e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17132380 4 QLVLMDHDGGVDDYLATMLLLTMDNVQLMGVVVTPADCYVQPAVSATRKIIDLMGFSHIPVAESTVRGINPFPRLYRRDs 83
Cdd:PLN02717 1 KKLIIDTDPGIDDAMAILMALRSPEVEVIGLTTIFGNVTTKLATRNALHLLEMAGRPDVPVAEGSHEPLKGGTKPRIAD- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17132380 84 FI--VDHLPILNQTELIHTPlVEETGQDFMVRVLQEALEPVTLMVTGPLTTVAVALDQAPDIEAKIDKIVWMGGALNVPG 161
Cdd:PLN02717 80 FVhgSDGLGNTNLPPPKGKK-IEKSAAEFLVEKVSEYPGEVTVVALGPLTNLALAIKLDPSFAKKVGQIVVLGGAFFVNG 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 17132380 162 NVEKSLEAgqdgsaewNVYWDAVSAARVWQREIKIIMCPLDLTNDVPVTSELVYKMGR 219
Cdd:PLN02717 159 NVNPAAEA--------NIFGDPEAADIVFTSGADITVVGINVTTQVVLTDADLEELRD 208
|
|
| nuc_hydro_CjNH |
cd02654 |
nuc_hydro_CjNH. Nucleoside hydrolases similar to Campylobacter jejuni nucleoside hydrolase. ... |
6-301 |
3.44e-14 |
|
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: 71.82 E-value: 3.44e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17132380 6 VLMDHDGGV----DDYLATMLLLTMDNVQLMGVVVTPADCYVQPAVSATRKIIDLMGFSHIPVA-----------ESTVR 70
Cdd:cd02654 2 VILDNDIAMgrdtDDGLALALLLWSPEVELLGLSAVSGNCWLSAVTYNVLRMLELAGADAIPVYagantplgrtnRAFHA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17132380 71 GINPFPRLYRRDSFIVDhlPILNQTELIHTPLVEETGQDFMVRVLQEALEPVTLMVTGPLTTVAVALDQAPDIEAKIDKI 150
Cdd:cd02654 82 WESLYGAYLWQGAWSPE--YSDMYTNASIIRNASIPAALFMIEMVRKHPHEVSIVAAGPLTNLALALRIDPDFAPLAKEL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17132380 151 VWMGGALNVPGNVEKSLEAgqdgsAEWNVYWDAVSAARVWQREIKIIMCPLDLTNDVPVTSE------LVYKMGRQRHYP 224
Cdd:cd02654 160 VIMGGYLDDIGEFVNRHYA-----SDFNLIMDPEAASIVLTAPWKSITIPGNVTNRTCLTPEqikaddPLRDFIRETLDL 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17132380 225 VSDLAGQcyaLVIPQD-YYFWDVLATAYLGHPEF------------------YQLREWETEIITSGLSQGRTKVVTGgrk 285
Cdd:cd02654 235 PIDYAKE---FVGTGDgLPMWDELASAVALDPELatssetfyidvqtdsdggGQLIWPEDLLLAKGLRPYHVKVITA--- 308
|
330
....*....|....*.
gi 17132380 286 ilamdkVDKDAFYAYI 301
Cdd:cd02654 309 ------VDVAAFLNLI 318
|
|
| |
