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Conserved domains on  [gi|1281063122|ref|XP_022974013|]
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probable uridine nucleosidase 2 [Cucurbita maxima]

Protein Classification

nucleoside hydrolase( domain architecture ID 10791442)

nucleoside hydrolase similar to Arabidopsis thaliana uridine nucleosidase 1, which is involved in pyrimidine breakdown rather than in pyrimidine salvage

Graphical summary

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List of domain hits

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
 
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
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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