|
Name |
Accession |
Description |
Interval |
E-value |
| PLN02717 |
PLN02717 |
uridine nucleosidase |
6-321 |
0e+00 |
|
uridine nucleosidase
Pssm-ID: 178319 [Multi-domain] Cd Length: 316 Bit Score: 588.50 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1281063122 6 KKTIIDTDPGIDDAMAIFLALQSPELDVLGLTTIFGNVYTTLSTRNALHLLEIAGRADIPVAEGSHVTITKGTKLRVADF 85
Cdd:PLN02717 1 KKLIIDTDPGIDDAMAILMALRSPEVEVIGLTTIFGNVTTKLATRNALHLLEMAGRPDVPVAEGSHEPLKGGTKPRIADF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1281063122 86 VHGADGLGNQNFPPPNGKPIDQSAAAFLVEQANLYPGEVTVVALGPLTNIALALQLDPGFPKKIGKIIILGGAFFVNGNV 165
Cdd:PLN02717 81 VHGSDGLGNTNLPPPKGKKIEKSAAEFLVEKVSEYPGEVTVVALGPLTNLALAIKLDPSFAKKVGQIVVLGGAFFVNGNV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1281063122 166 NPAAEANIFGDPEAADMVFTSGADVLVVGLNVTHQVVMTEADRDKLGRSDGKFAKYLCKILDIYFSYHRYAYETKGVYLH 245
Cdd:PLN02717 161 NPAAEANIFGDPEAADIVFTSGADITVVGINVTTQVVLTDADLEELRDSKGKYAQFLCDICKFYRDWHRKSYGIDGIYLH 240
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1281063122 246 DPATVLAAVDPSLFTYTEGVVRVQTTGITRGLTILYNNKKRFGEVSEWCDKPTVKVAVTVDAPAVAKLVMDRLIDS 321
Cdd:PLN02717 241 DPTALLAAVRPSLFTYKEGVVRVETEGICRGLTLFDNGLKRWNGENAWTGRPPVKVAVTVDAPAVVELVKERLMAS 316
|
|
| nuc_hydro_CaPnhB |
cd02650 |
NH_hydro_CaPnhB: A subgroup of nucleoside hydrolases similar to Corynebacterium ammoniagenes ... |
7-314 |
7.88e-150 |
|
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: 422.84 E-value: 7.88e-150
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1281063122 7 KTIIDTDPGIDDAMAIFLALQSPELDVLGLTTIFGNVYTTLSTRNALHLLEIAGRADIPVAEGSHVTITKGTKlRVADFV 86
Cdd:cd02650 1 KLILDTDPGIDDAMALAYALAHPDVDLIGVTTVYGNVTIETATRNALALLELFGRPDVPVAEGAAKPLTRPPF-RIATFV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1281063122 87 HGADGLGNQNFPPPNGKPIDQSAAAFLVEQANLYPGEVTVVALGPLTNIALALQLDPGFPKKIGKIIILGGAFFVNGNVN 166
Cdd:cd02650 80 HGDNGLGDVELPAPPRQPEDESAADFLIELANEYPGELTLVAVGPLTNLALALARDPDFAKLVKQVVVMGGAFTVPGNVT 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1281063122 167 PAAEANIFGDPEAADMVFTSGADVLVVGLNVTHQVVMTEADRDKLGRSDGKFAKYLCKILDIYFSYHRYAYETKGVYLHD 246
Cdd:cd02650 160 PAAEANIHGDPEAADIVFTAGADLTMVGLDVTTQTLLTREDLDELRDSGGKAGQFLADMLDYYIDFYQESPGLRGCALHD 239
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1281063122 247 PATVLAAVDPSLFTYTEGVVRVQTTGITRGLTILYNNKKRFgevSEWCDKPTVKVAVTVDAPAVAKLV 314
Cdd:cd02650 240 PLAVAAAVDPSLFTTREGVVRVETEGPTRGRTIGDRDGRRF---WDSSPNATVAVDVDVDERFLKRLM 304
|
|
| URH1 |
COG1957 |
Inosine-uridine nucleoside N-ribohydrolase [Nucleotide transport and metabolism]; ... |
4-318 |
3.38e-137 |
|
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: 391.05 E-value: 3.38e-137
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1281063122 4 SRKKTIIDTDPGIDDAMAIFLALQSPELDVLGLTTIFGNVYTTLSTRNALHLLEIAGRADIPVAEGSHVTITKgtKLRVA 83
Cdd:COG1957 1 MMRKVIIDTDPGIDDALALLLALASPEIDLLGITTVAGNVPLEQTTRNALKLLELAGRTDVPVAAGAARPLVR--PLVTA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1281063122 84 DFVHGADGLGNQNFPPPNGKPIDQSAAAFLVEQANLYPGEVTVVALGPLTNIALALQLDPGFPKKIGKIIILGGAFFVNG 163
Cdd:COG1957 79 EHVHGEDGLGGVDLPEPTRPPEPEHAVDFIIETLRAAPGEVTLVALGPLTNLALALRKDPELAERIKRIVIMGGAFFVPG 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1281063122 164 NVNPAAEANIFGDPEAADMVFTSGADVLVVGLNVTHQVVMTEADRDKLGRSDGKFAKYLCKILDIYFSYHRYAYETKGVY 243
Cdd:COG1957 159 NVTPVAEFNIYVDPEAAKIVFASGIPITMVGLDVTHQALLTPEDLARLAALGTPLGRFLADLLDFYLDFYRERYGLDGCP 238
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1281063122 244 LHDPATVLAAVDPSLFTYTEGVVRVQTTG-ITRGLTIlynnkkrFGEVSEWCDKPTVKVAVTVDAPAVAKLVMDRL 318
Cdd:COG1957 239 LHDPLAVAYLLDPELFTTRPAPVDVETDGeLTRGQTV-------VDWRGVTGRPPNARVALDVDAERFLDLLLERL 307
|
|
| IU_nuc_hydro |
pfam01156 |
Inosine-uridine preferring nucleoside hydrolase; |
9-310 |
1.07e-101 |
|
Inosine-uridine preferring nucleoside hydrolase;
Pssm-ID: 460086 [Multi-domain] Cd Length: 253 Bit Score: 298.74 E-value: 1.07e-101
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1281063122 9 IIDTDPGIDDAMAIFLALQSPELDVLGLTTIFGNVYTTLSTRNALHLLEIAGRADIPVAEGshvtitkgtklrvaDFVHG 88
Cdd:pfam01156 2 IIDTDPGIDDALALLLALASPEIELLGITTVAGNVSLEQTTRNALRLLELGGRDDIPVYAG--------------EAIRE 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1281063122 89 adglgnqnfpppngkpidqsaaaflveqanlyPGEVTVVALGPLTNIALALQLDPGFPKKIGKIIILGGAFFVNGNVNPA 168
Cdd:pfam01156 68 --------------------------------PGEVTLVATGPLTNLALALRLDPELAKKIKELVIMGGAFGVRGNVTPA 115
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1281063122 169 AEANIFGDPEAADMVFTSGADVLVVGLNVTHQVVMTEADRDKLGRSDGKFAKYLCKILDIYFSYHRYAYETKGVYLHDPA 248
Cdd:pfam01156 116 AEFNIFVDPEAAKIVFTSGLPITMVPLDVTHQALLTPEDLERLAALGTPLGRFLADLLRFYAEFYRERFGIDGPPLHDPL 195
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1281063122 249 TVLAAVDPSLFTYTEGVVRVQTTG-ITRGLTILYNNKKrfgevseWCDKPTVKVAVTVDAPAV 310
Cdd:pfam01156 196 AVAVALDPELFTTRRLNVDVETTGgLTRGQTVVDDRGG-------WGKPPNVRVATDVDVDRF 251
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| PLN02717 |
PLN02717 |
uridine nucleosidase |
6-321 |
0e+00 |
|
uridine nucleosidase
Pssm-ID: 178319 [Multi-domain] Cd Length: 316 Bit Score: 588.50 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1281063122 6 KKTIIDTDPGIDDAMAIFLALQSPELDVLGLTTIFGNVYTTLSTRNALHLLEIAGRADIPVAEGSHVTITKGTKLRVADF 85
Cdd:PLN02717 1 KKLIIDTDPGIDDAMAILMALRSPEVEVIGLTTIFGNVTTKLATRNALHLLEMAGRPDVPVAEGSHEPLKGGTKPRIADF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1281063122 86 VHGADGLGNQNFPPPNGKPIDQSAAAFLVEQANLYPGEVTVVALGPLTNIALALQLDPGFPKKIGKIIILGGAFFVNGNV 165
Cdd:PLN02717 81 VHGSDGLGNTNLPPPKGKKIEKSAAEFLVEKVSEYPGEVTVVALGPLTNLALAIKLDPSFAKKVGQIVVLGGAFFVNGNV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1281063122 166 NPAAEANIFGDPEAADMVFTSGADVLVVGLNVTHQVVMTEADRDKLGRSDGKFAKYLCKILDIYFSYHRYAYETKGVYLH 245
Cdd:PLN02717 161 NPAAEANIFGDPEAADIVFTSGADITVVGINVTTQVVLTDADLEELRDSKGKYAQFLCDICKFYRDWHRKSYGIDGIYLH 240
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1281063122 246 DPATVLAAVDPSLFTYTEGVVRVQTTGITRGLTILYNNKKRFGEVSEWCDKPTVKVAVTVDAPAVAKLVMDRLIDS 321
Cdd:PLN02717 241 DPTALLAAVRPSLFTYKEGVVRVETEGICRGLTLFDNGLKRWNGENAWTGRPPVKVAVTVDAPAVVELVKERLMAS 316
|
|
| nuc_hydro_CaPnhB |
cd02650 |
NH_hydro_CaPnhB: A subgroup of nucleoside hydrolases similar to Corynebacterium ammoniagenes ... |
7-314 |
7.88e-150 |
|
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: 422.84 E-value: 7.88e-150
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1281063122 7 KTIIDTDPGIDDAMAIFLALQSPELDVLGLTTIFGNVYTTLSTRNALHLLEIAGRADIPVAEGSHVTITKGTKlRVADFV 86
Cdd:cd02650 1 KLILDTDPGIDDAMALAYALAHPDVDLIGVTTVYGNVTIETATRNALALLELFGRPDVPVAEGAAKPLTRPPF-RIATFV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1281063122 87 HGADGLGNQNFPPPNGKPIDQSAAAFLVEQANLYPGEVTVVALGPLTNIALALQLDPGFPKKIGKIIILGGAFFVNGNVN 166
Cdd:cd02650 80 HGDNGLGDVELPAPPRQPEDESAADFLIELANEYPGELTLVAVGPLTNLALALARDPDFAKLVKQVVVMGGAFTVPGNVT 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1281063122 167 PAAEANIFGDPEAADMVFTSGADVLVVGLNVTHQVVMTEADRDKLGRSDGKFAKYLCKILDIYFSYHRYAYETKGVYLHD 246
Cdd:cd02650 160 PAAEANIHGDPEAADIVFTAGADLTMVGLDVTTQTLLTREDLDELRDSGGKAGQFLADMLDYYIDFYQESPGLRGCALHD 239
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1281063122 247 PATVLAAVDPSLFTYTEGVVRVQTTGITRGLTILYNNKKRFgevSEWCDKPTVKVAVTVDAPAVAKLV 314
Cdd:cd02650 240 PLAVAAAVDPSLFTTREGVVRVETEGPTRGRTIGDRDGRRF---WDSSPNATVAVDVDVDERFLKRLM 304
|
|
| URH1 |
COG1957 |
Inosine-uridine nucleoside N-ribohydrolase [Nucleotide transport and metabolism]; ... |
4-318 |
3.38e-137 |
|
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: 391.05 E-value: 3.38e-137
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1281063122 4 SRKKTIIDTDPGIDDAMAIFLALQSPELDVLGLTTIFGNVYTTLSTRNALHLLEIAGRADIPVAEGSHVTITKgtKLRVA 83
Cdd:COG1957 1 MMRKVIIDTDPGIDDALALLLALASPEIDLLGITTVAGNVPLEQTTRNALKLLELAGRTDVPVAAGAARPLVR--PLVTA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1281063122 84 DFVHGADGLGNQNFPPPNGKPIDQSAAAFLVEQANLYPGEVTVVALGPLTNIALALQLDPGFPKKIGKIIILGGAFFVNG 163
Cdd:COG1957 79 EHVHGEDGLGGVDLPEPTRPPEPEHAVDFIIETLRAAPGEVTLVALGPLTNLALALRKDPELAERIKRIVIMGGAFFVPG 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1281063122 164 NVNPAAEANIFGDPEAADMVFTSGADVLVVGLNVTHQVVMTEADRDKLGRSDGKFAKYLCKILDIYFSYHRYAYETKGVY 243
Cdd:COG1957 159 NVTPVAEFNIYVDPEAAKIVFASGIPITMVGLDVTHQALLTPEDLARLAALGTPLGRFLADLLDFYLDFYRERYGLDGCP 238
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1281063122 244 LHDPATVLAAVDPSLFTYTEGVVRVQTTG-ITRGLTIlynnkkrFGEVSEWCDKPTVKVAVTVDAPAVAKLVMDRL 318
Cdd:COG1957 239 LHDPLAVAYLLDPELFTTRPAPVDVETDGeLTRGQTV-------VDWRGVTGRPPNARVALDVDAERFLDLLLERL 307
|
|
| IU_nuc_hydro |
pfam01156 |
Inosine-uridine preferring nucleoside hydrolase; |
9-310 |
1.07e-101 |
|
Inosine-uridine preferring nucleoside hydrolase;
Pssm-ID: 460086 [Multi-domain] Cd Length: 253 Bit Score: 298.74 E-value: 1.07e-101
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1281063122 9 IIDTDPGIDDAMAIFLALQSPELDVLGLTTIFGNVYTTLSTRNALHLLEIAGRADIPVAEGshvtitkgtklrvaDFVHG 88
Cdd:pfam01156 2 IIDTDPGIDDALALLLALASPEIELLGITTVAGNVSLEQTTRNALRLLELGGRDDIPVYAG--------------EAIRE 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1281063122 89 adglgnqnfpppngkpidqsaaaflveqanlyPGEVTVVALGPLTNIALALQLDPGFPKKIGKIIILGGAFFVNGNVNPA 168
Cdd:pfam01156 68 --------------------------------PGEVTLVATGPLTNLALALRLDPELAKKIKELVIMGGAFGVRGNVTPA 115
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1281063122 169 AEANIFGDPEAADMVFTSGADVLVVGLNVTHQVVMTEADRDKLGRSDGKFAKYLCKILDIYFSYHRYAYETKGVYLHDPA 248
Cdd:pfam01156 116 AEFNIFVDPEAAKIVFTSGLPITMVPLDVTHQALLTPEDLERLAALGTPLGRFLADLLRFYAEFYRERFGIDGPPLHDPL 195
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1281063122 249 TVLAAVDPSLFTYTEGVVRVQTTG-ITRGLTILYNNKKrfgevseWCDKPTVKVAVTVDAPAV 310
Cdd:pfam01156 196 AVAVALDPELFTTRRLNVDVETTGgLTRGQTVVDDRGG-------WGKPPNVRVATDVDVDRF 251
|
|
| nuc_hydro_IU_UC_XIUA |
cd02651 |
nuc_hydro_IU_UC_XIUA: inosine-uridine preferring, ... |
7-318 |
2.59e-92 |
|
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: 276.73 E-value: 2.59e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1281063122 7 KTIIDTDPGIDDAMAIFLALQSPELDVLGLTTIFGNVYTTLSTRNALHLLEIAGRADIPVAEGSHVTITKgtKLRVADFV 86
Cdd:cd02651 1 PIIIDCDPGHDDAVAILLALFHPELDLLGITTVAGNVPLEKTTRNALKLLTLLGRTDVPVAAGAARPLVR--PLITASDI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1281063122 87 HGADGLGNQNFPPPNGKPIDQSAAAFLVEQANLYPGEVTVVALGPLTNIALALQLDPGFPKKIGKIIILGGAFFVnGNVN 166
Cdd:cd02651 79 HGESGLDGADLPPPPRRPEDIHAVDAIIDTLRASPEPITLVATGPLTNIALLLRKYPELAERIKEIVLMGGALGR-GNIT 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1281063122 167 PAAEANIFGDPEAADMVFTSGADVLVVGLNVTHQVVMTEADRDKLGRSDGKFAKYLCKILDIYF-SYHryAYETKGVYLH 245
Cdd:cd02651 158 PAAEFNIFVDPEAAKIVFNSGIPITMVPLDVTHKALATPEVIERIRALGNPVGKMLAELLDFFAeTYG--SAFTEGPPLH 235
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1281063122 246 DPATVLAAVDPSLFTYTEGVVRVQTTG-ITRGLTI--LYNNKKRfgevsewcdKPTVKVAVTVDAPAVAKLVMDRL 318
Cdd:cd02651 236 DPCAVAYLLDPELFTTKRANVDVETEGeLTRGRTVvdLRGVTGR---------PANAQVAVDVDVEKFWDLLLEAL 302
|
|
| nuc_hydro |
cd00455 |
nuc_hydro: Nucleoside hydrolases. Nucleoside hydrolases cleave the N-glycosidic bond in ... |
9-309 |
2.27e-84 |
|
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: 256.10 E-value: 2.27e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1281063122 9 IIDTDPGIDDAMAIFLALQSPELDVLGLTTIFGNVYTTLSTRNALHLLEIAGRADIPVAEGSHVTITkGTKLRVADFVHG 88
Cdd:cd00455 2 ILDTDPGIDDAFALMYALLHPEIELVGIVATYGNVTLEQATQNAAYLLELLGRLDIPVYAGATRPLT-GEIPAAYPEIHG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1281063122 89 ADGLGNqnFPPPNGKPIDQSAAAFLVEQANLYPGEVTVVALGPLTNIALALQLDPGFPKKIGKIIILGGAFFVNGNVNPA 168
Cdd:cd00455 81 EGGLGL--PIPPIIEADDPEAVQLLIDLIRKYPDEITIVALGPLTNLAMAFILDPDIKDRVKEIVIMGGAFLVPGNVTPV 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1281063122 169 AEANIFGDPEAADMVFTSGADVLVVGLNVTHQVVMTEADRDKLGRSDGKFAKYLCKILDIYFSYHrYAYETKGVYLHDPA 248
Cdd:cd00455 159 AEANFYGDPEAANIVFNSAKNLTIVPLDVTNQAVLTPPMVERIFEQGTSIGLLIKPMIDYYYKAY-QKPGIEGSPIHDPL 237
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1281063122 249 TVLAAVDPSLFTYTEGVVRVQTTGITRGLTIlynnkKRFGEVSewcDKPTVKVAVTVDAPA 309
Cdd:cd00455 238 AVAYLLNPSMFDYSKVPVDVDTDGLTRGQTI-----ADFRENP---GNGVTRVAVNLDYPD 290
|
|
| nuc_hydro_3 |
cd02653 |
NH_3: A subgroup of nucleoside hydrolases. This group contains eukaryotic and bacterial ... |
7-318 |
2.39e-78 |
|
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: 241.90 E-value: 2.39e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1281063122 7 KTIIDTDPGIDDAMAIFLALQSPELDVLGLTTIFGNVYTTLSTRNALHLLEIAGRADIPVAEGSHVTITKgtKLRVADFV 86
Cdd:cd02653 1 KVIIDCDPGIDDALALLYLLASPDLDVVGITTTAGNVPVEQVAANALGVLELLGRTDIPVYLGADKPLAG--PLTTAQDT 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1281063122 87 HGADGLGNQNFPPPNGKPIDQSAAAFLVEQANLYPgEVTVVALGPLTNIALALQLDPGFPKKIGKIIILGGAFFVNGNVN 166
Cdd:cd02653 79 HGPDGLGYAELPASTRTLSDESAAQAWVDLARAHP-DLIGLATGPLTNLALALREEPELPRLLRRLVIMGGAFNSRGNTS 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1281063122 167 PAAEANIFGDPEAADMVFT--SGADVL--VVGLNVTHQVVMTEADRDKLGRSDGKFAKYLCKILDIYFSYHrYAYE-TKG 241
Cdd:cd02653 158 PVAEWNYWVDPEAAKEVLAafGGHPVRptICGLDVTRAVVLTPNLLERLARAKDSVGAFIEDALRFYFEFH-WAYGhGYG 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1281063122 242 VYLHDPATVLAAVDPSLFTYTEGVVRVQTTGITRGLTilynnkkrfgeVSEWCDK----PTVKVAVTVDAPAVAKLVMDR 317
Cdd:cd02653 237 AVIHDPLAAAVALNPNLARGRPAYVDVECTGVLTGQT-----------VVDWAGFwgkgANAEILTKVDSQDFMALFIER 305
|
.
gi 1281063122 318 L 318
Cdd:cd02653 306 V 306
|
|
| rihA |
PRK10443 |
ribonucleoside hydrolase 1; Provisional |
6-318 |
4.40e-71 |
|
ribonucleoside hydrolase 1; Provisional
Pssm-ID: 182465 [Multi-domain] Cd Length: 311 Bit Score: 223.01 E-value: 4.40e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1281063122 6 KKTIIDTDPGIDDAMAIFLALQSPELDVLGLTTIFGNVYTTLSTRNALHLLEIAGRADIPVAEGSHVTITKgtKLRVADF 85
Cdd:PRK10443 3 LPIILDCDPGHDDAIALVLALASPELDVKAVTTSAGNQTPEKTLRNALRMLTLLNRTDIPVAGGAVKPLMR--ELIIADN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1281063122 86 VHGADGLGNQNFPPPNGKPIDQSAAAFLVEQANLYPGEVTVVALGPLTNIALALQLDPGFPKKIGKIIILGGAFFVnGNV 165
Cdd:PRK10443 81 VHGESGLDGPALPEPTFAPQNCTAVELMAKTLRESAEPVTLVSTGPQTNVALLLASHPELHSKIARIVIMGGAMGL-GNW 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1281063122 166 NPAAEANIFGDPEAADMVFTSGADVLVVGLNVTHQVVMTEADRDKLGRSDGKFAKYLCKILDIYFSYHR-YAYETKGVYL 244
Cdd:PRK10443 160 TPAAEFNIYVDPEAAEIVFQSGIPIVMAGLDVTHKAQIMDEDIERIRAIGNPVATIVAELLDFFMEYHKdEKWGFVGAPL 239
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1281063122 245 HDPATVLAAVDPSLFTYTEGVVRVQTTG-ITRGLTILynnkKRFGEVSEwcdKPTVKVAVTVDAPAVAKLVMDRL 318
Cdd:PRK10443 240 HDPCTIAWLLKPELFTTVERWVGVETQGeYTQGMTVV----DYYQLTGN---KPNATVLVDVDRQGFVDLLAERL 307
|
|
| PRK10768 |
PRK10768 |
ribonucleoside hydrolase RihC; Provisional |
5-318 |
6.13e-68 |
|
ribonucleoside hydrolase RihC; Provisional
Pssm-ID: 182713 [Multi-domain] Cd Length: 304 Bit Score: 214.39 E-value: 6.13e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1281063122 5 RKKTIIDTDPGIDDAMAIFLALQSPELDVLGLTTIFGNVYTTLSTRNALHLLEIAGrADIPVAEGSHVTITKgtKLRVAD 84
Cdd:PRK10768 2 RLPIILDTDPGIDDAVAIAAALFAPELDLKLITTVAGNVSVEKTTRNALKLLHFFN-SDVPVAQGAAKPLVR--PLRDAA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1281063122 85 FVHGADGLGNQNFPPPNGKPIDQSAAAFLVEQANLYPGEVTVVALGPLTNIALALQLDPGFPKKIGKIIILGGAfFVNGN 164
Cdd:PRK10768 79 SVHGESGMEGYDFPEHTRKPLSIPAVEAMRDALMNAPEPVTLVAIGPLTNIALLLSTYPEVKPYIKRIVLMGGS-AGRGN 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1281063122 165 VNPAAEANIFGDPEAADMVFTSGADVLVVGLNVTHQVVMTEADRDKLgRSDGKFAKYLCKIldiyFSYHRYAYETKGVYL 244
Cdd:PRK10768 158 VTPNAEFNIAVDPEAAAIVFRSGIPIVMCGLDVTNQALLTPDYLATL-PELNRTGKMLHAL----FSHYRSGSMQTGLRM 232
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1281063122 245 HDPATVLAAVDPSLFTYTEGVVRVQTTG-ITRGLTIL-YNNKkrfgevseWCDKPTVKVAVTVDAPAVAKLVMDRL 318
Cdd:PRK10768 233 HDVCAIAYLLRPELFTLKPCFVDVETQGeFTAGATVVdIDGR--------LGKPANAQVALDIDVDGFQKWFAEVL 300
|
|
| nuc_hydro_CeIAG |
cd02649 |
nuc_hydro_CeIAG: Nucleoside hydrolases similar to the inosine-adenosine-guanosine-preferring ... |
6-280 |
5.37e-65 |
|
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: 207.11 E-value: 5.37e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1281063122 6 KKTIIDTDPGIDDAMAIFLALQSPELDVLGLTTIFGNVYTTLSTRNALHLLEIAGRADIPVAEGSHVTITkgTKLRVADF 85
Cdd:cd02649 1 RKLIIDTDCGGDDAWALLMALASPNVEVLAITCVHGNTNVEQVVKNALRVLEACGRRDIPVYRGASKPLL--GPGPTAAY 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1281063122 86 VHGADGLGNQNFPPPNGKPIDQS--AAAFLVEQANLYPGEVTVVALGPLTNIALALQLDPGFPKKIGKIIILGGAFFVNG 163
Cdd:cd02649 79 FHGKDGFGDVGFPEPKDELELQKehAVDAIIRLVREYPGEITLVALGPLTNLALAYRLDPSLPQKIKRLYIMGGNREGVG 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1281063122 164 NVNPAAEANIFGDPEAADMVFTS-GADVLVVGLNVTHQVV-MTEADRDKLGRSDGKFAKYLCKILDIYFSYhRYAYETKG 241
Cdd:cd02649 159 NTTPAAEFNFHVDPEAAHIVLNSfGCPITIVPWETTLLAFpLDWEFEDKWANRLEKALFAESLNRREYAFA-SEGLGGDG 237
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 1281063122 242 VYLHDPATVLAAVDPSLFTYT-EGVVRVQTTG-ITRGLTIL 280
Cdd:cd02649 238 WVPCDALAVAAALDPSIITRRlTYAVDVELHGeLTRGQMVV 278
|
|
| rihB |
PRK09955 |
ribosylpyrimidine nucleosidase; |
4-316 |
6.83e-50 |
|
ribosylpyrimidine nucleosidase;
Pssm-ID: 182166 [Multi-domain] Cd Length: 313 Bit Score: 168.20 E-value: 6.83e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1281063122 4 SRKKTIIDTDPGIDDAMAIFLALQSPELDVLGLTTIFGNVYTTLSTRNALH---LLEIagraDIPVAEGSHVTITKgtKL 80
Cdd:PRK09955 2 EKRKIILDCDPGHDDAIAMMMAAKHPAIDLLGITIVAGNQTLDKTLINGLNvcqKLEI----NVPVYAGMPQPIMR--QQ 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1281063122 81 RVADFVHGADGLGNQNFPPPNGKPIDQSAAAFLVEQANLYPGEVTVVALGPLTNIALALQLDPGFPKKIGKIIILGGAFF 160
Cdd:PRK09955 76 IVADNIHGETGLDGPVFEPLTRQAESTHAVKYIIDTLMASDGDITLVPVGPLSNIAVAMRMQPAILPKIREIVLMGGAYG 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1281063122 161 vNGNVNPAAEANIFGDPEAADMVFTSGADVLVVGLNVTHQVVMTEADRDKLGRSDGKFAKYLCKILDIYFSYHRYAYETK 240
Cdd:PRK09955 156 -TGNFTPSAEFNIFADPEAARVVFTSGVPLVMMGLDLTNQTVCTPDVIARMERAGGPAGELFSDIMNFTLKTQFENYGLA 234
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1281063122 241 GVYLHDPATVLAAVDPSLFTYTEGVVRVQ-TTGITRGLTILynnkkrfGEVSEWCDKPTVKVAVTVDAPAVAKLVMD 316
Cdd:PRK09955 235 GGPVHDATCIGYLINPDGIKTQEMYVEVDvNSGPCYGRTVC-------DELGVLGKPANTKVGITIDTDWFWGLVEE 304
|
|
| nuc_hydro_CjNH |
cd02654 |
nuc_hydro_CjNH. Nucleoside hydrolases similar to Campylobacter jejuni nucleoside hydrolase. ... |
7-263 |
4.39e-39 |
|
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: 140.00 E-value: 4.39e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1281063122 7 KTIIDTD----PGIDDAMAIFLALQSPELDVLGLTTIFGNVYTTLSTRNALHLLEIAGRADIPVAEGSHVTI--TKGTKL 80
Cdd:cd02654 1 KVILDNDiamgRDTDDGLALALLLWSPEVELLGLSAVSGNCWLSAVTYNVLRMLELAGADAIPVYAGANTPLgrTNRAFH 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1281063122 81 RVADFV-----------HGADGLGNqnfpPPNGKPIDQSAAAFLVEQANLYPGEVTVVALGPLTNIALALQLDPGFPKKI 149
Cdd:cd02654 81 AWESLYgaylwqgawspEYSDMYTN----ASIIRNASIPAALFMIEMVRKHPHEVSIVAAGPLTNLALALRIDPDFAPLA 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1281063122 150 GKIIILGGAF-----FVNGNVnpAAEANIFGDPEAADMVFTSGADVLVVGLNVTHQVVMTEadrdklgrSDGKFAKYLC- 223
Cdd:cd02654 157 KELVIMGGYLddigeFVNRHY--ASDFNLIMDPEAASIVLTAPWKSITIPGNVTNRTCLTP--------EQIKADDPLRd 226
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 1281063122 224 ---KILDIYFSYHRYAYETK-GVYLHDPATVLAAVDPSLFTYTE 263
Cdd:cd02654 227 firETLDLPIDYAKEFVGTGdGLPMWDELASAVALDPELATSSE 270
|
|
| nuc_hydro_1 |
cd02648 |
NH_1: A subgroup of nucleoside hydrolases. This group contains fungal proteins similar to ... |
7-280 |
2.05e-37 |
|
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: 136.94 E-value: 2.05e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1281063122 7 KTIIDTDPGIDDAMAIFLALQSP-ELDVLGLTTIFGNVYTTLSTRNAL---HLL--EIAGRADIP--------------V 66
Cdd:cd02648 3 PIIIDTDPGVDDVLAILLALSSPeEVDVALISLTFGNTTLDHALRNVLrlfHVLerERAWRATPGvryrafsadaekpiV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1281063122 67 AEGSHVTItKGTKLrVADFVHGADGLGNQN------FPPPNGK--------PIDQSAAAFLVEQANLYPGE-VTVVALGP 131
Cdd:cd02648 83 ASGSDQPL-EGERL-TASYFHGRDGLSGVHwlhpdfTPVETWIpeivapltPSDKPAYDVILDILREEPDHtVTIAALGP 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1281063122 132 LTNIALALQLDPGFPKKIGKIIILGGAFFVNGNVNPAAEANIFGDPEAADMVFTSGA----------DVLVVGLNVT--H 199
Cdd:cd02648 161 LTNLAAAARKDPETFAKVGEVVVMGGAIDVPGNTSPVAEFNCFADPYAAAVVIDEPPstapearrklPLQVFPLDITtgH 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1281063122 200 QV----VMTEADRDKLGRSDGK-FAKYLCKILDIYFSYHRYAYETKGVY--------LHDPATV----------LAAVDP 256
Cdd:cd02648 241 TLpyssLFATYVTPRDAPERGSpLARWLEHVFISTFLTHPRAFTPEEFLpdrselfeMHDPLAVwyaifadmpaTGSIDG 320
|
330 340
....*....|....*....|....*
gi 1281063122 257 SLFTYTEGVVRVQTTG-ITRGLTIL 280
Cdd:cd02648 321 NGWKHTPRDFRVETSGqWTRGMCVV 345
|
|
| nuc_hydro_TvIAG |
cd02647 |
nuc_hydro_ TvIAG: Nucleoside hydrolases similar to the Inosine-adenosine-guanosine-preferring ... |
6-283 |
7.53e-27 |
|
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: 107.50 E-value: 7.53e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1281063122 6 KKTIIDTDPGIDDAMAIFLALQSPELDV--LGLTTIFGNVYTTLSTRNALHLLEIAGRAD-IPVAEGSHVTITKGTKLRV 82
Cdd:cd02647 1 KNVIFDHDGNVDDLVALLLLLKNEKVDLkgIGVSGIDADCYVEPAVSVTRKLIDRLGQRDaIPVGKGGSRAVNPFPRSWR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1281063122 83 ADFVHGADGLGNQNFPPPNGKPIDQSAAAF-LVEQANLYPGEVTVVALGPLTNIALALQLDPGFPKKIGKIIILGGAFFV 161
Cdd:cd02647 81 RDAAFSVDHLPILNERYTVETPLAEETAQLvLIEKIKASLEPVTLLVTGPLTNLARALDSDPDISSNIEEVYIMGGGVDA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1281063122 162 NGNV-----NPAAEANIFGDPEAADMVFTSGADVLVVGLNVTHQVVMTEADRDKLGRSDGKFAKYLCKILDIYFSYHRYA 236
Cdd:cd02647 161 PGNVftppsNGTAEFNIFWDPLAAKTVFDSGLKITLVPLDATNTVPLTREFLETDRQRFAAQRLPASDLAGQGYALVKPL 240
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 1281063122 237 YETKGVYLHDPATVLAAVDPSL-FTYTEGVVRVQTTGITRGLTILYNN 283
Cdd:cd02647 241 EFNSTYYMWDVLTTLVLGAKEVdNTKESLILEVDTDGLSAGQTVTSPN 288
|
|
| nuc_hydro_2 |
cd02652 |
NH_2: A subgroup of nucleoside hydrolases. This group contains eukaryotic and bacterial ... |
8-274 |
1.43e-15 |
|
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: 75.61 E-value: 1.43e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1281063122 8 TIIDTDPG--IDDAMAIFLALQSPELDVLGLTTIFGNVYTTLStRNALHLLeiAGRADIPVAEGSHvtitkGTKLRVADF 85
Cdd:cd02652 1 LILDTDIGgdPDDALALALAHALQKCDLLAVTITLADASARRA-IDAVNRF--YGRGDIPIGADYH-----GWPEDAKDH 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1281063122 86 VHGADGLGNQNFPPPNGKPIDQSAAAFLVEQANLYPGEVTVVALGPLTNIA--LALQLDPGFP-----KKIGKIIILGGA 158
Cdd:cd02652 73 AKFLLEGDRLHHDLESAEDALDAVKALRRLLASAEDASVTIVSIGPLTNLAalLDADADPLTGpelvrQKVKRLVVMGGA 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1281063122 159 F-FVNGNVNpAAEANIFGDPEAADMVFTSGADVLVVGLNVTH-----QVVMTEADRDKLGrsdgkfakylckildiYFSY 232
Cdd:cd02652 153 FyDPDGNVQ-HREYNFVTDPKAAQRVAGRAQHLGIPVRIVWSgyelgEAVSYPHVLVIAH----------------PFNT 215
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 1281063122 233 H---RYAYETKGVYLHDPATVLAAVDPS--LFTYTE-----GVVRVQTTGIT 274
Cdd:cd02652 216 PvfaAYWPRSHRRPLWDPLTLLAAVRGGgmLFDLREvqlgpGRVEVDSSGVT 267
|
|
| PTZ00313 |
PTZ00313 |
inosine-adenosine-guanosine-nucleoside hydrolase; Provisional |
6-222 |
1.16e-08 |
|
inosine-adenosine-guanosine-nucleoside hydrolase; Provisional
Pssm-ID: 140334 [Multi-domain] Cd Length: 326 Bit Score: 55.64 E-value: 1.16e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1281063122 6 KKTIIDTDPGIDDAMAIFLALQSPE-LDVLGLT------------TIFGNVYTTLSTRNALHLLeiagradiPVAEGShv 72
Cdd:PTZ00313 3 KPVILDHDGNHDDLVALALLLGNPEkVKVIGCIctdadcfvddafNVTGKLMCMMHAREATPLF--------PIGKSS-- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1281063122 73 tiTKGTKLRVADFVHGA---DGLGNQNFP----------PPNGKPIDQSAAAFLVEQAnlyPGEVTVVALGPLTNIALAL 139
Cdd:PTZ00313 73 --FKGVNPFPSEWRWSAknmDDLPCLNIPehvaiweklkPENEALVGEELLADLVMSS---PEKVTICVTGPLSNVAWCI 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1281063122 140 -QLDPGFPKKIGKIIILGGAFFVNGNV-----NPAAEANIFGDPEAADMVFT-SGADVLVVGLNVTHQVVMTEADRDKLG 212
Cdd:PTZ00313 148 eKYGEEFTKKVEECVIMGGAVDVGGNVflpgtDGSAEWNIYWDPPAAKTVLMcPHIRKVLFSLDSTNSVPVTSEVVKKFG 227
|
250
....*....|
gi 1281063122 213 RSDgkfaKYL 222
Cdd:PTZ00313 228 AQN----KYL 233
|
|
| |
