|
Name |
Accession |
Description |
Interval |
E-value |
| PLN02717 |
PLN02717 |
uridine nucleosidase |
7-322 |
0e+00 |
|
uridine nucleosidase
Pssm-ID: 178319 [Multi-domain] Cd Length: 316 Bit Score: 595.82 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18390550 7 KKIIIDTDPGIDDAMAIFVALNSPEVDVIGLTTIFGNVYTTLATRNALHLLEVAGRTDIPVAEGTHKTFLNDTKLRIADF 86
Cdd:PLN02717 1 KKLIIDTDPGIDDAMAILMALRSPEVEVIGLTTIFGNVTTKLATRNALHLLEMAGRPDVPVAEGSHEPLKGGTKPRIADF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18390550 87 VHGKDGLGNQNFPPPKGKPIEKSGPEFLVEQAKLCPGEITVVALGPLTNLALAVQLDPEFSKNVGQIVLLGGAFAVNGNV 166
Cdd:PLN02717 81 VHGSDGLGNTNLPPPKGKKIEKSAAEFLVEKVSEYPGEVTVVALGPLTNLALAIKLDPSFAKKVGQIVVLGGAFFVNGNV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18390550 167 NPASEANIFGDPEAADIVFTCGADIIAVGINVTHQVIMTADDKDKLASSKGKLAQYLCKILDVYYDYHLTAYEIKGVYLH 246
Cdd:PLN02717 161 NPAAEANIFGDPEAADIVFTSGADITVVGINVTTQVVLTDADLEELRDSKGKYAQFLCDICKFYRDWHRKSYGIDGIYLH 240
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 18390550 247 DPATILAAFLPSLFTYTEGVARVQTSGITRGLTLLYNNLKRFEEANEWSDKPTVKVAVTVDAPAVVKLIMDRLMES 322
Cdd:PLN02717 241 DPTALLAAVRPSLFTYKEGVVRVETEGICRGLTLFDNGLKRWNGENAWTGRPPVKVAVTVDAPAVVELVKERLMAS 316
|
|
| nuc_hydro_CaPnhB |
cd02650 |
NH_hydro_CaPnhB: A subgroup of nucleoside hydrolases similar to Corynebacterium ammoniagenes ... |
8-316 |
6.54e-157 |
|
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: 440.95 E-value: 6.54e-157
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18390550 8 KIIIDTDPGIDDAMAIFVALNSPEVDVIGLTTIFGNVYTTLATRNALHLLEVAGRTDIPVAEGTHKTFLNDTKlRIADFV 87
Cdd:cd02650 1 KLILDTDPGIDDAMALAYALAHPDVDLIGVTTVYGNVTIETATRNALALLELFGRPDVPVAEGAAKPLTRPPF-RIATFV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18390550 88 HGKDGLGNQNFPPPKGKPIEKSGPEFLVEQAKLCPGEITVVALGPLTNLALAVQLDPEFSKNVGQIVLLGGAFAVNGNVN 167
Cdd:cd02650 80 HGDNGLGDVELPAPPRQPEDESAADFLIELANEYPGELTLVAVGPLTNLALALARDPDFAKLVKQVVVMGGAFTVPGNVT 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18390550 168 PASEANIFGDPEAADIVFTCGADIIAVGINVTHQVIMTADDKDKLASSKGKLAQYLCKILDVYYDYHLTAYEIKGVYLHD 247
Cdd:cd02650 160 PAAEANIHGDPEAADIVFTAGADLTMVGLDVTTQTLLTREDLDELRDSGGKAGQFLADMLDYYIDFYQESPGLRGCALHD 239
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 18390550 248 PATILAAFLPSLFTYTEGVARVQTSGITRGLTLLYNNLKRFeeaNEWSDKPTVKVAVTVDaPAVVKLIM 316
Cdd:cd02650 240 PLAVAAAVDPSLFTTREGVVRVETEGPTRGRTIGDRDGRRF---WDSSPNATVAVDVDVD-ERFLKRLM 304
|
|
| URH1 |
COG1957 |
Inosine-uridine nucleoside N-ribohydrolase [Nucleotide transport and metabolism]; ... |
6-319 |
2.89e-131 |
|
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: 376.03 E-value: 2.89e-131
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18390550 6 RKKIIIDTDPGIDDAMAIFVALNSPEVDVIGLTTIFGNVYTTLATRNALHLLEVAGRTDIPVAEGTHKTFLNDtkLRIAD 85
Cdd:COG1957 2 MRKVIIDTDPGIDDALALLLALASPEIDLLGITTVAGNVPLEQTTRNALKLLELAGRTDVPVAAGAARPLVRP--LVTAE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18390550 86 FVHGKDGLGNQNFPPPKGKPIEKSGPEFLVEQAKLCPGEITVVALGPLTNLALAVQLDPEFSKNVGQIVLLGGAFAVNGN 165
Cdd:COG1957 80 HVHGEDGLGGVDLPEPTRPPEPEHAVDFIIETLRAAPGEVTLVALGPLTNLALALRKDPELAERIKRIVIMGGAFFVPGN 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18390550 166 VNPASEANIFGDPEAADIVFTCGADIIAVGINVTHQVIMTADDKDKLASSKGKLAQYLCKILDVYYDYHLTAYEIKGVYL 245
Cdd:COG1957 160 VTPVAEFNIYVDPEAAKIVFASGIPITMVGLDVTHQALLTPEDLARLAALGTPLGRFLADLLDFYLDFYRERYGLDGCPL 239
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 18390550 246 HDPATILAAFLPSLFTYTEGVARVQTSG-ITRGLTLlynnlkrFEEANEWSDKPTVKVAVTVDAPAVVKLIMDRL 319
Cdd:COG1957 240 HDPLAVAYLLDPELFTTRPAPVDVETDGeLTRGQTV-------VDWRGVTGRPPNARVALDVDAERFLDLLLERL 307
|
|
| IU_nuc_hydro |
pfam01156 |
Inosine-uridine preferring nucleoside hydrolase; |
9-313 |
1.08e-95 |
|
Inosine-uridine preferring nucleoside hydrolase;
Pssm-ID: 460086 [Multi-domain] Cd Length: 253 Bit Score: 283.72 E-value: 1.08e-95
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18390550 9 IIIDTDPGIDDAMAIFVALNSPEVDVIGLTTIFGNVYTTLATRNALHLLEVAGRTDIPVAEGthktflndtklriaDFVH 88
Cdd:pfam01156 1 VIIDTDPGIDDALALLLALASPEIELLGITTVAGNVSLEQTTRNALRLLELGGRDDIPVYAG--------------EAIR 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18390550 89 GkdglgnqnfpppkgkpieksgpeflveqaklcPGEITVVALGPLTNLALAVQLDPEFSKNVGQIVLLGGAFAVNGNVNP 168
Cdd:pfam01156 67 E--------------------------------PGEVTLVATGPLTNLALALRLDPELAKKIKELVIMGGAFGVRGNVTP 114
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18390550 169 ASEANIFGDPEAADIVFTCGADIIAVGINVTHQVIMTADDKDKLASSKGKLAQYLCKILDVYYDYHLTAYEIKGVYLHDP 248
Cdd:pfam01156 115 AAEFNIFVDPEAAKIVFTSGLPITMVPLDVTHQALLTPEDLERLAALGTPLGRFLADLLRFYAEFYRERFGIDGPPLHDP 194
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 18390550 249 ATILAAFLPSLFTYTEGVARVQTSG-ITRGLTLlynnlkrFEEANEWSDKPTVKVAVTVDAPAVVK 313
Cdd:pfam01156 195 LAVAVALDPELFTTRRLNVDVETTGgLTRGQTV-------VDDRGGWGKPPNVRVATDVDVDRFWE 253
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| PLN02717 |
PLN02717 |
uridine nucleosidase |
7-322 |
0e+00 |
|
uridine nucleosidase
Pssm-ID: 178319 [Multi-domain] Cd Length: 316 Bit Score: 595.82 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18390550 7 KKIIIDTDPGIDDAMAIFVALNSPEVDVIGLTTIFGNVYTTLATRNALHLLEVAGRTDIPVAEGTHKTFLNDTKLRIADF 86
Cdd:PLN02717 1 KKLIIDTDPGIDDAMAILMALRSPEVEVIGLTTIFGNVTTKLATRNALHLLEMAGRPDVPVAEGSHEPLKGGTKPRIADF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18390550 87 VHGKDGLGNQNFPPPKGKPIEKSGPEFLVEQAKLCPGEITVVALGPLTNLALAVQLDPEFSKNVGQIVLLGGAFAVNGNV 166
Cdd:PLN02717 81 VHGSDGLGNTNLPPPKGKKIEKSAAEFLVEKVSEYPGEVTVVALGPLTNLALAIKLDPSFAKKVGQIVVLGGAFFVNGNV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18390550 167 NPASEANIFGDPEAADIVFTCGADIIAVGINVTHQVIMTADDKDKLASSKGKLAQYLCKILDVYYDYHLTAYEIKGVYLH 246
Cdd:PLN02717 161 NPAAEANIFGDPEAADIVFTSGADITVVGINVTTQVVLTDADLEELRDSKGKYAQFLCDICKFYRDWHRKSYGIDGIYLH 240
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 18390550 247 DPATILAAFLPSLFTYTEGVARVQTSGITRGLTLLYNNLKRFEEANEWSDKPTVKVAVTVDAPAVVKLIMDRLMES 322
Cdd:PLN02717 241 DPTALLAAVRPSLFTYKEGVVRVETEGICRGLTLFDNGLKRWNGENAWTGRPPVKVAVTVDAPAVVELVKERLMAS 316
|
|
| nuc_hydro_CaPnhB |
cd02650 |
NH_hydro_CaPnhB: A subgroup of nucleoside hydrolases similar to Corynebacterium ammoniagenes ... |
8-316 |
6.54e-157 |
|
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: 440.95 E-value: 6.54e-157
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18390550 8 KIIIDTDPGIDDAMAIFVALNSPEVDVIGLTTIFGNVYTTLATRNALHLLEVAGRTDIPVAEGTHKTFLNDTKlRIADFV 87
Cdd:cd02650 1 KLILDTDPGIDDAMALAYALAHPDVDLIGVTTVYGNVTIETATRNALALLELFGRPDVPVAEGAAKPLTRPPF-RIATFV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18390550 88 HGKDGLGNQNFPPPKGKPIEKSGPEFLVEQAKLCPGEITVVALGPLTNLALAVQLDPEFSKNVGQIVLLGGAFAVNGNVN 167
Cdd:cd02650 80 HGDNGLGDVELPAPPRQPEDESAADFLIELANEYPGELTLVAVGPLTNLALALARDPDFAKLVKQVVVMGGAFTVPGNVT 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18390550 168 PASEANIFGDPEAADIVFTCGADIIAVGINVTHQVIMTADDKDKLASSKGKLAQYLCKILDVYYDYHLTAYEIKGVYLHD 247
Cdd:cd02650 160 PAAEANIHGDPEAADIVFTAGADLTMVGLDVTTQTLLTREDLDELRDSGGKAGQFLADMLDYYIDFYQESPGLRGCALHD 239
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 18390550 248 PATILAAFLPSLFTYTEGVARVQTSGITRGLTLLYNNLKRFeeaNEWSDKPTVKVAVTVDaPAVVKLIM 316
Cdd:cd02650 240 PLAVAAAVDPSLFTTREGVVRVETEGPTRGRTIGDRDGRRF---WDSSPNATVAVDVDVD-ERFLKRLM 304
|
|
| URH1 |
COG1957 |
Inosine-uridine nucleoside N-ribohydrolase [Nucleotide transport and metabolism]; ... |
6-319 |
2.89e-131 |
|
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: 376.03 E-value: 2.89e-131
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18390550 6 RKKIIIDTDPGIDDAMAIFVALNSPEVDVIGLTTIFGNVYTTLATRNALHLLEVAGRTDIPVAEGTHKTFLNDtkLRIAD 85
Cdd:COG1957 2 MRKVIIDTDPGIDDALALLLALASPEIDLLGITTVAGNVPLEQTTRNALKLLELAGRTDVPVAAGAARPLVRP--LVTAE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18390550 86 FVHGKDGLGNQNFPPPKGKPIEKSGPEFLVEQAKLCPGEITVVALGPLTNLALAVQLDPEFSKNVGQIVLLGGAFAVNGN 165
Cdd:COG1957 80 HVHGEDGLGGVDLPEPTRPPEPEHAVDFIIETLRAAPGEVTLVALGPLTNLALALRKDPELAERIKRIVIMGGAFFVPGN 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18390550 166 VNPASEANIFGDPEAADIVFTCGADIIAVGINVTHQVIMTADDKDKLASSKGKLAQYLCKILDVYYDYHLTAYEIKGVYL 245
Cdd:COG1957 160 VTPVAEFNIYVDPEAAKIVFASGIPITMVGLDVTHQALLTPEDLARLAALGTPLGRFLADLLDFYLDFYRERYGLDGCPL 239
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 18390550 246 HDPATILAAFLPSLFTYTEGVARVQTSG-ITRGLTLlynnlkrFEEANEWSDKPTVKVAVTVDAPAVVKLIMDRL 319
Cdd:COG1957 240 HDPLAVAYLLDPELFTTRPAPVDVETDGeLTRGQTV-------VDWRGVTGRPPNARVALDVDAERFLDLLLERL 307
|
|
| IU_nuc_hydro |
pfam01156 |
Inosine-uridine preferring nucleoside hydrolase; |
9-313 |
1.08e-95 |
|
Inosine-uridine preferring nucleoside hydrolase;
Pssm-ID: 460086 [Multi-domain] Cd Length: 253 Bit Score: 283.72 E-value: 1.08e-95
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18390550 9 IIIDTDPGIDDAMAIFVALNSPEVDVIGLTTIFGNVYTTLATRNALHLLEVAGRTDIPVAEGthktflndtklriaDFVH 88
Cdd:pfam01156 1 VIIDTDPGIDDALALLLALASPEIELLGITTVAGNVSLEQTTRNALRLLELGGRDDIPVYAG--------------EAIR 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18390550 89 GkdglgnqnfpppkgkpieksgpeflveqaklcPGEITVVALGPLTNLALAVQLDPEFSKNVGQIVLLGGAFAVNGNVNP 168
Cdd:pfam01156 67 E--------------------------------PGEVTLVATGPLTNLALALRLDPELAKKIKELVIMGGAFGVRGNVTP 114
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18390550 169 ASEANIFGDPEAADIVFTCGADIIAVGINVTHQVIMTADDKDKLASSKGKLAQYLCKILDVYYDYHLTAYEIKGVYLHDP 248
Cdd:pfam01156 115 AAEFNIFVDPEAAKIVFTSGLPITMVPLDVTHQALLTPEDLERLAALGTPLGRFLADLLRFYAEFYRERFGIDGPPLHDP 194
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 18390550 249 ATILAAFLPSLFTYTEGVARVQTSG-ITRGLTLlynnlkrFEEANEWSDKPTVKVAVTVDAPAVVK 313
Cdd:pfam01156 195 LAVAVALDPELFTTRRLNVDVETTGgLTRGQTV-------VDDRGGWGKPPNVRVATDVDVDRFWE 253
|
|
| nuc_hydro_IU_UC_XIUA |
cd02651 |
nuc_hydro_IU_UC_XIUA: inosine-uridine preferring, ... |
8-319 |
1.82e-86 |
|
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: 261.71 E-value: 1.82e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18390550 8 KIIIDTDPGIDDAMAIFVALNSPEVDVIGLTTIFGNVYTTLATRNALHLLEVAGRTDIPVAEGTHKTFLNDtkLRIADFV 87
Cdd:cd02651 1 PIIIDCDPGHDDAVAILLALFHPELDLLGITTVAGNVPLEKTTRNALKLLTLLGRTDVPVAAGAARPLVRP--LITASDI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18390550 88 HGKDGLGNQNFPPPKGKPIEKSGPEFLVEQAKLCPGEITVVALGPLTNLALAVQLDPEFSKNVGQIVLLGGAFAVnGNVN 167
Cdd:cd02651 79 HGESGLDGADLPPPPRRPEDIHAVDAIIDTLRASPEPITLVATGPLTNIALLLRKYPELAERIKEIVLMGGALGR-GNIT 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18390550 168 PASEANIFGDPEAADIVFTCGADIIAVGINVTHQVIMTADDKDKLASSKGKLAQYLCKILDVYYD-YHLTAYEikGVYLH 246
Cdd:cd02651 158 PAAEFNIFVDPEAAKIVFNSGIPITMVPLDVTHKALATPEVIERIRALGNPVGKMLAELLDFFAEtYGSAFTE--GPPLH 235
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 18390550 247 DPATILAAFLPSLFTYTEGVARVQTSG-ITRGLTLLYNNLKRFEEANewsdkptVKVAVTVDAPAVVKLIMDRL 319
Cdd:cd02651 236 DPCAVAYLLDPELFTTKRANVDVETEGeLTRGRTVVDLRGVTGRPAN-------AQVAVDVDVEKFWDLLLEAL 302
|
|
| nuc_hydro |
cd00455 |
nuc_hydro: Nucleoside hydrolases. Nucleoside hydrolases cleave the N-glycosidic bond in ... |
9-315 |
3.03e-78 |
|
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: 240.69 E-value: 3.03e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18390550 9 IIIDTDPGIDDAMAIFVALNSPEVDVIGLTTIFGNVYTTLATRNALHLLEVAGRTDIPVAEGTHKTfLNDTKLRIADFVH 88
Cdd:cd00455 1 VILDTDPGIDDAFALMYALLHPEIELVGIVATYGNVTLEQATQNAAYLLELLGRLDIPVYAGATRP-LTGEIPAAYPEIH 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18390550 89 GKDGLGNqnFPPPKGKPIEKSGPEFLVEQAKLCPGEITVVALGPLTNLALAVQLDPEFSKNVGQIVLLGGAFAVNGNVNP 168
Cdd:cd00455 80 GEGGLGL--PIPPIIEADDPEAVQLLIDLIRKYPDEITIVALGPLTNLAMAFILDPDIKDRVKEIVIMGGAFLVPGNVTP 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18390550 169 ASEANIFGDPEAADIVFTCGADIIAVGINVTHQVIMTADDKDKLASSKGKLAqylcKILDVYYDYHLTAYE---IKGVYL 245
Cdd:cd00455 158 VAEANFYGDPEAANIVFNSAKNLTIVPLDVTNQAVLTPPMVERIFEQGTSIG----LLIKPMIDYYYKAYQkpgIEGSPI 233
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18390550 246 HDPATILAAFLPSLFTYTEGVARVQTSGITRGLTllynnlkrFEEANEWSDKPTVKVAVTVDAPAVVKLI 315
Cdd:cd00455 234 HDPLAVAYLLNPSMFDYSKVPVDVDTDGLTRGQT--------IADFRENPGNGVTRVAVNLDYPDFIELI 295
|
|
| nuc_hydro_3 |
cd02653 |
NH_3: A subgroup of nucleoside hydrolases. This group contains eukaryotic and bacterial ... |
8-321 |
2.23e-71 |
|
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: 223.79 E-value: 2.23e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18390550 8 KIIIDTDPGIDDAMAIFVALNSPEVDVIGLTTIFGNVYTTLATRNALHLLEVAGRTDIPVAEGTHKTFlnDTKLRIADFV 87
Cdd:cd02653 1 KVIIDCDPGIDDALALLYLLASPDLDVVGITTTAGNVPVEQVAANALGVLELLGRTDIPVYLGADKPL--AGPLTTAQDT 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18390550 88 HGKDGLGNQNFPPPKGKPIEKSGPEFLVEQAKLCPgEITVVALGPLTNLALAVQLDPEFSKNVGQIVLLGGAFAVNGNVN 167
Cdd:cd02653 79 HGPDGLGYAELPASTRTLSDESAAQAWVDLARAHP-DLIGLATGPLTNLALALREEPELPRLLRRLVIMGGAFNSRGNTS 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18390550 168 PASEANIFGDPEAADIVF----TCGADIIAVGINVTHQVIMTADDKDKLASSKGKLAQYLCKILDVYYDYHLTAYEIKGV 243
Cdd:cd02653 158 PVAEWNYWVDPEAAKEVLaafgGHPVRPTICGLDVTRAVVLTPNLLERLARAKDSVGAFIEDALRFYFEFHWAYGHGYGA 237
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 18390550 244 YLHDPATILAAFLPSLFTYTEGVARVQTSGITRGLTLLynnlkrfEEANEWSDKPTVKVAVTVDAPAVVKLIMDRLME 321
Cdd:cd02653 238 VIHDPLAAAVALNPNLARGRPAYVDVECTGVLTGQTVV-------DWAGFWGKGANAEILTKVDSQDFMALFIERVLA 308
|
|
| rihA |
PRK10443 |
ribonucleoside hydrolase 1; Provisional |
7-319 |
1.13e-67 |
|
ribonucleoside hydrolase 1; Provisional
Pssm-ID: 182465 [Multi-domain] Cd Length: 311 Bit Score: 214.15 E-value: 1.13e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18390550 7 KKIIIDTDPGIDDAMAIFVALNSPEVDVIGLTTIFGNVYTTLATRNALHLLEVAGRTDIPVAEGTHKTFLNDtkLRIADF 86
Cdd:PRK10443 3 LPIILDCDPGHDDAIALVLALASPELDVKAVTTSAGNQTPEKTLRNALRMLTLLNRTDIPVAGGAVKPLMRE--LIIADN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18390550 87 VHGKDGLGNQNFPPPKGKPIEKSGPEFLVEQAKLCPGEITVVALGPLTNLALAVQLDPEFSKNVGQIVLLGGAFAVnGNV 166
Cdd:PRK10443 81 VHGESGLDGPALPEPTFAPQNCTAVELMAKTLRESAEPVTLVSTGPQTNVALLLASHPELHSKIARIVIMGGAMGL-GNW 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18390550 167 NPASEANIFGDPEAADIVFTCGADIIAVGINVTHQVIMTADDKDKLASSKGKLAQYLCKILDVYYDYHLT-AYEIKGVYL 245
Cdd:PRK10443 160 TPAAEFNIYVDPEAAEIVFQSGIPIVMAGLDVTHKAQIMDEDIERIRAIGNPVATIVAELLDFFMEYHKDeKWGFVGAPL 239
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 18390550 246 HDPATILAAFLPSLFTYTEGVARVQTSG-ITRGLTLlynnLKRFEEANEwsdKPTVKVAVTVDAPAVVKLIMDRL 319
Cdd:PRK10443 240 HDPCTIAWLLKPELFTTVERWVGVETQGeYTQGMTV----VDYYQLTGN---KPNATVLVDVDRQGFVDLLAERL 307
|
|
| PRK10768 |
PRK10768 |
ribonucleoside hydrolase RihC; Provisional |
6-319 |
1.23e-64 |
|
ribonucleoside hydrolase RihC; Provisional
Pssm-ID: 182713 [Multi-domain] Cd Length: 304 Bit Score: 205.91 E-value: 1.23e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18390550 6 RKKIIIDTDPGIDDAMAIFVALNSPEVDVIGLTTIFGNVYTTLATRNALHLLEVAGrTDIPVAEGTHKTFLNDtkLRIAD 85
Cdd:PRK10768 2 RLPIILDTDPGIDDAVAIAAALFAPELDLKLITTVAGNVSVEKTTRNALKLLHFFN-SDVPVAQGAAKPLVRP--LRDAA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18390550 86 FVHGKDGLGNQNFPPPKGKPIEKSGPEFLVEQAKLCPGEITVVALGPLTNLALAVQLDPEFSKNVGQIVLLGGAFAvNGN 165
Cdd:PRK10768 79 SVHGESGMEGYDFPEHTRKPLSIPAVEAMRDALMNAPEPVTLVAIGPLTNIALLLSTYPEVKPYIKRIVLMGGSAG-RGN 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18390550 166 VNPASEANIFGDPEAADIVFTCGADIIAVGINVTHQVIMTADDKDKLAsSKGKLAQYLCKILDVYYDYHLTayeiKGVYL 245
Cdd:PRK10768 158 VTPNAEFNIAVDPEAAAIVFRSGIPIVMCGLDVTNQALLTPDYLATLP-ELNRTGKMLHALFSHYRSGSMQ----TGLRM 232
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 18390550 246 HDPATILAAFLPSLFTYTEGVARVQTSG-ITRGLTLLynNLKrfeeaNEWSDKPTVKVAVTVDAPAVVKLIMDRL 319
Cdd:PRK10768 233 HDVCAIAYLLRPELFTLKPCFVDVETQGeFTAGATVV--DID-----GRLGKPANAQVALDIDVDGFQKWFAEVL 300
|
|
| nuc_hydro_CeIAG |
cd02649 |
nuc_hydro_CeIAG: Nucleoside hydrolases similar to the inosine-adenosine-guanosine-preferring ... |
7-316 |
4.09e-63 |
|
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: 202.10 E-value: 4.09e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18390550 7 KKIIIDTDPGIDDAMAIFVALNSPEVDVIGLTTIFGNVYTTLATRNALHLLEVAGRTDIPVAEGTHKTFLndTKLRIADF 86
Cdd:cd02649 1 RKLIIDTDCGGDDAWALLMALASPNVEVLAITCVHGNTNVEQVVKNALRVLEACGRRDIPVYRGASKPLL--GPGPTAAY 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18390550 87 VHGKDGLGNQNFPPPKG--KPIEKSGPEFLVEQAKLCPGEITVVALGPLTNLALAVQLDPEFSKNVGQIVLLGGAFAVNG 164
Cdd:cd02649 79 FHGKDGFGDVGFPEPKDelELQKEHAVDAIIRLVREYPGEITLVALGPLTNLALAYRLDPSLPQKIKRLYIMGGNREGVG 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18390550 165 NVNPASEANIFGDPEAADIVF---TCGADIIA--VGINVTHqviMTADDKDKLASSKgKLAQYLCKILDVYYDYHLTAYE 239
Cdd:cd02649 159 NTTPAAEFNFHVDPEAAHIVLnsfGCPITIVPweTTLLAFP---LDWEFEDKWANRL-EKALFAESLNRREYAFASEGLG 234
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 18390550 240 IKGVYLHDPATILAAFLPSLFTYT-EGVARVQTSG-ITRGLTLLynnlkrfEEANEWSDKPTVKVAVTVDAPAVVKLIM 316
Cdd:cd02649 235 GDGWVPCDALAVAAALDPSIITRRlTYAVDVELHGeLTRGQMVV-------DWLGTLKKKPNARVITKIDREKFKELLY 306
|
|
| rihB |
PRK09955 |
ribosylpyrimidine nucleosidase; |
5-317 |
3.41e-49 |
|
ribosylpyrimidine nucleosidase;
Pssm-ID: 182166 [Multi-domain] Cd Length: 313 Bit Score: 166.66 E-value: 3.41e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18390550 5 DRKKIIIDTDPGIDDAMAIFVALNSPEVDVIGLTTIFGNVYTTLATRNALHLLEVAgRTDIPVAEGTHKTFLNDTKlrIA 84
Cdd:PRK09955 2 EKRKIILDCDPGHDDAIAMMMAAKHPAIDLLGITIVAGNQTLDKTLINGLNVCQKL-EINVPVYAGMPQPIMRQQI--VA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18390550 85 DFVHGKDGLGNQNFPPPKGKPIEKSGPEFLVEQAKLCPGEITVVALGPLTNLALAVQLDPEFSKNVGQIVLLGGAFAvNG 164
Cdd:PRK09955 79 DNIHGETGLDGPVFEPLTRQAESTHAVKYIIDTLMASDGDITLVPVGPLSNIAVAMRMQPAILPKIREIVLMGGAYG-TG 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18390550 165 NVNPASEANIFGDPEAADIVFTCGADIIAVGINVTHQVIMTADDKDKLASSKGKLAQYLCKILDVYYDYHLTAYEIKGVY 244
Cdd:PRK09955 158 NFTPSAEFNIFADPEAARVVFTSGVPLVMMGLDLTNQTVCTPDVIARMERAGGPAGELFSDIMNFTLKTQFENYGLAGGP 237
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 18390550 245 LHDPATILAAFLPSLFTYTEGVARVQ-TSGITRGLTLLynnlkrfEEANEWSDKPTVKVAVTVDAPAVVKLIMD 317
Cdd:PRK09955 238 VHDATCIGYLINPDGIKTQEMYVEVDvNSGPCYGRTVC-------DELGVLGKPANTKVGITIDTDWFWGLVEE 304
|
|
| nuc_hydro_CjNH |
cd02654 |
nuc_hydro_CjNH. Nucleoside hydrolases similar to Campylobacter jejuni nucleoside hydrolase. ... |
8-264 |
3.92e-40 |
|
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: 143.08 E-value: 3.92e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18390550 8 KIIIDTD----PGIDDAMAIFVALNSPEVDVIGLTTIFGNVYTTLATRNALHLLEVAGRTDIPVAEGTHKTFL--NDTKL 81
Cdd:cd02654 1 KVILDNDiamgRDTDDGLALALLLWSPEVELLGLSAVSGNCWLSAVTYNVLRMLELAGADAIPVYAGANTPLGrtNRAFH 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18390550 82 RIADF--------VHGKDGLgNQNFPPPKGKPIEKSGPEFLVEQAKLCPGEITVVALGPLTNLALAVQLDPEFSKNVGQI 153
Cdd:cd02654 81 AWESLygaylwqgAWSPEYS-DMYTNASIIRNASIPAALFMIEMVRKHPHEVSIVAAGPLTNLALALRIDPDFAPLAKEL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18390550 154 VLLGGAFAVNG---NVNPASEANIFGDPEAADIVFTCGADIIAVGINVTHQVIMTADDKdklaSSKGKLAQYLCKILDVY 230
Cdd:cd02654 160 VIMGGYLDDIGefvNRHYASDFNLIMDPEAASIVLTAPWKSITIPGNVTNRTCLTPEQI----KADDPLRDFIRETLDLP 235
|
250 260 270
....*....|....*....|....*....|....*
gi 18390550 231 YDYHLTAYEIK-GVYLHDPATILAAFLPSLFTYTE 264
Cdd:cd02654 236 IDYAKEFVGTGdGLPMWDELASAVALDPELATSSE 270
|
|
| nuc_hydro_1 |
cd02648 |
NH_1: A subgroup of nucleoside hydrolases. This group contains fungal proteins similar to ... |
8-281 |
1.67e-38 |
|
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: 140.02 E-value: 1.67e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18390550 8 KIIIDTDPGIDDAMAIFVALNSP-EVDVIGLTTIFGNVYTTLATRNAL---HLL--EVAGRTDI-------------PVA 68
Cdd:cd02648 3 PIIIDTDPGVDDVLAILLALSSPeEVDVALISLTFGNTTLDHALRNVLrlfHVLerERAWRATPgvryrafsadaekPIV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18390550 69 EGTHKTFLNDTKLrIADFVHGKDGLGNQNFPPPKGKPIEKSGPEF---LVEQAKLCPGEI------------TVVALGPL 133
Cdd:cd02648 83 ASGSDQPLEGERL-TASYFHGRDGLSGVHWLHPDFTPVETWIPEIvapLTPSDKPAYDVIldilreepdhtvTIAALGPL 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18390550 134 TNLALAVQLDPEFSKNVGQIVLLGGAFAVNGNVNPASEANIFGDPEAADIVFTCGA------------DIIAVGINVTHQ 201
Cdd:cd02648 162 TNLAAAARKDPETFAKVGEVVVMGGAIDVPGNTSPVAEFNCFADPYAAAVVIDEPPstapearrklplQVFPLDITTGHT 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18390550 202 V----IMTADDKDKLASSKGK-LAQYLCKILDVYYDYH---LTAYEIKG-----VYLHDPAT----ILAAFLPSLFTYTE 264
Cdd:cd02648 242 LpyssLFATYVTPRDAPERGSpLARWLEHVFISTFLTHpraFTPEEFLPdrselFEMHDPLAvwyaIFADMPATGSIDGN 321
|
330 340
....*....|....*....|....
gi 18390550 265 GVA------RVQTSG-ITRGLTLL 281
Cdd:cd02648 322 GWKhtprdfRVETSGqWTRGMCVV 345
|
|
| nuc_hydro_TvIAG |
cd02647 |
nuc_hydro_ TvIAG: Nucleoside hydrolases similar to the Inosine-adenosine-guanosine-preferring ... |
7-285 |
1.63e-31 |
|
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: 119.83 E-value: 1.63e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18390550 7 KKIIIDTDPGIDDAMAIFVALNSPEVDVIGLTtIFGNVYTTL------ATRNALHLLEvaGRTDIPVAEGTHKTFLNDTK 80
Cdd:cd02647 1 KNVIFDHDGNVDDLVALLLLLKNEKVDLKGIG-VSGIDADCYvepavsVTRKLIDRLG--QRDAIPVGKGGSRAVNPFPR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18390550 81 --LRIADFvHGKDGLGNQNFPPPKGKPIEKSGPEFLVEQAKLCPGEITVVALGPLTNLALAVQLDPEFSKNVGQIVLLGG 158
Cdd:cd02647 78 swRRDAAF-SVDHLPILNERYTVETPLAEETAQLVLIEKIKASLEPVTLLVTGPLTNLARALDSDPDISSNIEEVYIMGG 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18390550 159 AFAVNGNV-----NPASEANIFGDPEAADIVFTCGADIIAVGINVTHQVIMTADDKDKLASSKGKLAQYLCKILDVYYDY 233
Cdd:cd02647 157 GVDAPGNVftppsNGTAEFNIFWDPLAAKTVFDSGLKITLVPLDATNTVPLTREFLETDRQRFAAQRLPASDLAGQGYAL 236
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 18390550 234 HLTAYEIKGVYLHDP-ATILAAFLPSLFTYTEGVARVQTSGITRGLTLLYNNL 285
Cdd:cd02647 237 VKPLEFNSTYYMWDVlTTLVLGAKEVDNTKESLILEVDTDGLSAGQTVTSPNG 289
|
|
| nuc_hydro_2 |
cd02652 |
NH_2: A subgroup of nucleoside hydrolases. This group contains eukaryotic and bacterial ... |
9-185 |
5.41e-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: 59.44 E-value: 5.41e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18390550 9 IIIDTDPG--IDDAMAIFVALNSPEVDVIGLTTIFGNVYTTLAtRNALHLLevAGRTDIPVaeGTHKTFLNDTKLRIADF 86
Cdd:cd02652 1 LILDTDIGgdPDDALALALAHALQKCDLLAVTITLADASARRA-IDAVNRF--YGRGDIPI--GADYHGWPEDAKDHAKF 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18390550 87 VHGKDGLGnqnfPPPKGKPIEKSGPEFLVEQ-AKLCPGEITVVALGPLTNL-----ALAVQLDPE--FSKNVGQIVLLGG 158
Cdd:cd02652 76 LLEGDRLH----HDLESAEDALDAVKALRRLlASAEDASVTIVSIGPLTNLaalldADADPLTGPelVRQKVKRLVVMGG 151
|
170 180
....*....|....*....|....*..
gi 18390550 159 AFAVNGNVNPASEANIFGDPEAADIVF 185
Cdd:cd02652 152 AFYDPDGNVQHREYNFVTDPKAAQRVA 178
|
|
| PTZ00313 |
PTZ00313 |
inosine-adenosine-guanosine-nucleoside hydrolase; Provisional |
7-223 |
8.10e-10 |
|
inosine-adenosine-guanosine-nucleoside hydrolase; Provisional
Pssm-ID: 140334 [Multi-domain] Cd Length: 326 Bit Score: 59.11 E-value: 8.10e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18390550 7 KKIIIDTDPGIDDAMAIFVALNSPE-VDVIGLT------------TIFGNVYTTLATRNALHLLEVA-----GRTDIPVA 68
Cdd:PTZ00313 3 KPVILDHDGNHDDLVALALLLGNPEkVKVIGCIctdadcfvddafNVTGKLMCMMHAREATPLFPIGkssfkGVNPFPSE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18390550 69 EGTHKTFLNDTK-LRIADFVHGKDGLGNQNfpppkgkpiEK-SGPEFLVEQAKLCPGEITVVALGPLTNLALAV-QLDPE 145
Cdd:PTZ00313 83 WRWSAKNMDDLPcLNIPEHVAIWEKLKPEN---------EAlVGEELLADLVMSSPEKVTICVTGPLSNVAWCIeKYGEE 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18390550 146 FSKNVGQIVLLGGAFAVNGNV-----NPASEANIFGDPEAADIVFTC-GADIIAVGINVTHQVIMTADDKDKL-ASSKGK 218
Cdd:PTZ00313 154 FTKKVEECVIMGGAVDVGGNVflpgtDGSAEWNIYWDPPAAKTVLMCpHIRKVLFSLDSTNSVPVTSEVVKKFgAQNKYL 233
|
....*
gi 18390550 219 LAQYL 223
Cdd:PTZ00313 234 LSQFV 238
|
|
| |
