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Conserved domains on  [gi|1174556942|ref|WP_081491430|]
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nucleoside hydrolase [Schaalia georgiae]

Protein Classification

URH1 superfamily protein( domain architecture ID 1903929)

URH1 superfamily protein

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
URH1 COG1957
Inosine-uridine nucleoside N-ribohydrolase [Nucleotide transport and metabolism]; ...
2-333 9.14e-53

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: 176.11  E-value: 9.14e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1174556942   2 APRRIIVDCDPGngvpganVDDALALAYALRSPLVDVGAVWTVFGNTPPDLGYRCASEVIRVVGGEGSragggpsasPVL 81
Cdd:COG1957     1 MMRKVIIDTDPG-------IDDALALLLALASPEIDLLGITTVAGNVPLEQTTRNALKLLELAGRTDV---------PVA 64
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1174556942  82 RcgpfqptsGDPqRWLRQRREFASSPAGLAAWGRRLERAPVREEADRDvtgevppArLDDLVDDLR-SPERSTVVGIGPL 160
Cdd:COG1957    65 A--------GAA-RPLVRPLVTAEHVHGEDGLGGVDLPEPTRPPEPEH-------A-VDFIIETLRaAPGEVTLVALGPL 127
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1174556942 161 TNIARVLTEWDGASGRIDRIVVMGGALAFG---TMV-DTNFAVDPRAARVVVRFGIPITIVPLDTTRTTCLTRDRWRAIv 236
Cdd:COG1957   128 TNLALALRKDPELAERIKRIVIMGGAFFVPgnvTPVaEFNIYVDPEAAKIVFASGIPITMVGLDVTHQALLTPEDLARL- 206
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1174556942 237 rrAAMKGPTAIATASAFDAwvspWLSYSEATRPVDGMWVHDLVALVALAHPELVDSSQHRVDVRDDGKL-----VECPDG 311
Cdd:COG1957   207 --AALGTPLGRFLADLLDF----YLDFYRERYGLDGCPLHDPLAVAYLLDPELFTTRPAPVDVETDGELtrgqtVVDWRG 280
                         330       340
                  ....*....|....*....|....*..
gi 1174556942 312 VP-----VDIVEAVDNEAMISLWERTV 333
Cdd:COG1957   281 VTgrppnARVALDVDAERFLDLLLERL 307
 
Name Accession Description Interval E-value
URH1 COG1957
Inosine-uridine nucleoside N-ribohydrolase [Nucleotide transport and metabolism]; ...
2-333 9.14e-53

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: 176.11  E-value: 9.14e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1174556942   2 APRRIIVDCDPGngvpganVDDALALAYALRSPLVDVGAVWTVFGNTPPDLGYRCASEVIRVVGGEGSragggpsasPVL 81
Cdd:COG1957     1 MMRKVIIDTDPG-------IDDALALLLALASPEIDLLGITTVAGNVPLEQTTRNALKLLELAGRTDV---------PVA 64
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1174556942  82 RcgpfqptsGDPqRWLRQRREFASSPAGLAAWGRRLERAPVREEADRDvtgevppArLDDLVDDLR-SPERSTVVGIGPL 160
Cdd:COG1957    65 A--------GAA-RPLVRPLVTAEHVHGEDGLGGVDLPEPTRPPEPEH-------A-VDFIIETLRaAPGEVTLVALGPL 127
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1174556942 161 TNIARVLTEWDGASGRIDRIVVMGGALAFG---TMV-DTNFAVDPRAARVVVRFGIPITIVPLDTTRTTCLTRDRWRAIv 236
Cdd:COG1957   128 TNLALALRKDPELAERIKRIVIMGGAFFVPgnvTPVaEFNIYVDPEAAKIVFASGIPITMVGLDVTHQALLTPEDLARL- 206
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1174556942 237 rrAAMKGPTAIATASAFDAwvspWLSYSEATRPVDGMWVHDLVALVALAHPELVDSSQHRVDVRDDGKL-----VECPDG 311
Cdd:COG1957   207 --AALGTPLGRFLADLLDF----YLDFYRERYGLDGCPLHDPLAVAYLLDPELFTTRPAPVDVETDGELtrgqtVVDWRG 280
                         330       340
                  ....*....|....*....|....*..
gi 1174556942 312 VP-----VDIVEAVDNEAMISLWERTV 333
Cdd:COG1957   281 VTgrppnARVALDVDAERFLDLLLERL 307
IU_nuc_hydro pfam01156
Inosine-uridine preferring nucleoside hydrolase;
6-324 2.41e-37

Inosine-uridine preferring nucleoside hydrolase;


Pssm-ID: 460086 [Multi-domain]  Cd Length: 253  Bit Score: 134.26  E-value: 2.41e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1174556942   6 IIVDCDPGngvpganVDDALALAYALRSPLVDVGAVWTVFGNTPPDLGYRCASEVirvvggegsragggpsaspvlrcgp 85
Cdd:pfam01156   1 VIIDTDPG-------IDDALALLLALASPEIELLGITTVAGNVSLEQTTRNALRL------------------------- 48
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1174556942  86 fqptsgdpqrwlrqrrefasspagLAAWGRrlERAPVreeadrdVTGEVpparlddlvddLRSPERSTVVGIGPLTNIAR 165
Cdd:pfam01156  49 ------------------------LELGGR--DDIPV-------YAGEA-----------IREPGEVTLVATGPLTNLAL 84
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1174556942 166 VLTEWDGASGRIDRIVVMGGALAFG---TMV-DTNFAVDPRAARVVVRFGIPITIVPLDTTRTTCLTRDRWRAIvrrAAM 241
Cdd:pfam01156  85 ALRLDPELAKKIKELVIMGGAFGVRgnvTPAaEFNIFVDPEAAKIVFTSGLPITMVPLDVTHQALLTPEDLERL---AAL 161
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1174556942 242 KGPTAIATASAFDAwvspWLSYSEATRPVDGMWVHDLVALVALAHPELVDSSQHRVDVRDDGKL----------VECPDG 311
Cdd:pfam01156 162 GTPLGRFLADLLRF----YAEFYRERFGIDGPPLHDPLAVAVALDPELFTTRRLNVDVETTGGLtrgqtvvddrGGWGKP 237
                         330
                  ....*....|...
gi 1174556942 312 VPVDIVEAVDNEA 324
Cdd:pfam01156 238 PNVRVATDVDVDR 250
nuc_hydro_IU_UC_XIUA cd02651
nuc_hydro_IU_UC_XIUA: inosine-uridine preferring, ...
5-305 1.56e-36

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: 133.44  E-value: 1.56e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1174556942   5 RIIVDCDPGNgvpganvDDALALAYALRSPLVDVGAVWTVFGNTPPDLGYRCASEVIRVVGGEGSragggpsasPVLRcg 84
Cdd:cd02651     1 PIIIDCDPGH-------DDAVAILLALFHPELDLLGITTVAGNVPLEKTTRNALKLLTLLGRTDV---------PVAA-- 62
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1174556942  85 pfqptsGDPQRWLRQRrEFASS---PAGLAawGRRLERAPVREEAdrdvtgevPPArLDDLVDDLR-SPERSTVVGIGPL 160
Cdd:cd02651    63 ------GAARPLVRPL-ITASDihgESGLD--GADLPPPPRRPED--------IHA-VDAIIDTLRaSPEPITLVATGPL 124
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1174556942 161 TNIARVLTEWDGASGRIDRIVVMGGALAFGTMVDT---NFAVDPRAARVVVRFGIPITIVPLDTTRTTCLTRDRWRAIvr 237
Cdd:cd02651   125 TNIALLLRKYPELAERIKEIVLMGGALGRGNITPAaefNIFVDPEAAKIVFNSGIPITMVPLDVTHKALATPEVIERI-- 202
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1174556942 238 rAAMKGPTAIATASAFDAWVSPWlsyseATRPVDGMWVHDLVALVALAHPELVDSSQHRVDVRDDGKL 305
Cdd:cd02651   203 -RALGNPVGKMLAELLDFFAETY-----GSAFTEGPPLHDPCAVAYLLDPELFTTKRANVDVETEGEL 264
PRK10768 PRK10768
ribonucleoside hydrolase RihC; Provisional
4-305 1.92e-25

ribonucleoside hydrolase RihC; Provisional


Pssm-ID: 182713 [Multi-domain]  Cd Length: 304  Bit Score: 103.84  E-value: 1.92e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1174556942   4 RRIIVDCDPGngvpganVDDALALAYALRSPLVDVGAVWTVFGNTPPDLGYRCA--------SEVirvvggegsragggp 75
Cdd:PRK10768    3 LPIILDTDPG-------IDDAVAIAAALFAPELDLKLITTVAGNVSVEKTTRNAlkllhffnSDV--------------- 60
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1174556942  76 sasPVLRcGPFQPTsgdpqrwLRQRREFAS--SPAGLAAW------GRRLERAPVreEADRDVTgevpparlddlvddLR 147
Cdd:PRK10768   61 ---PVAQ-GAAKPL-------VRPLRDAASvhGESGMEGYdfpehtRKPLSIPAV--EAMRDAL--------------MN 113
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1174556942 148 SPERSTVVGIGPLTNIARVLTEWDGASGRIDRIVVMGGALA---FGTMVDTNFAVDPRAARVVVRFGIPITIVPLDTTRT 224
Cdd:PRK10768  114 APEPVTLVAIGPLTNIALLLSTYPEVKPYIKRIVLMGGSAGrgnVTPNAEFNIAVDPEAAAIVFRSGIPIVMCGLDVTNQ 193
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1174556942 225 TCLTRDRWRAIvrraamkgPTAIATASAFDAWVSPWLSYSEATrpvdGMWVHDLVALVALAHPELVDSSQHRVDVRDDGK 304
Cdd:PRK10768  194 ALLTPDYLATL--------PELNRTGKMLHALFSHYRSGSMQT----GLRMHDVCAIAYLLRPELFTLKPCFVDVETQGE 261

                  .
gi 1174556942 305 L 305
Cdd:PRK10768  262 F 262
 
Name Accession Description Interval E-value
URH1 COG1957
Inosine-uridine nucleoside N-ribohydrolase [Nucleotide transport and metabolism]; ...
2-333 9.14e-53

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: 176.11  E-value: 9.14e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1174556942   2 APRRIIVDCDPGngvpganVDDALALAYALRSPLVDVGAVWTVFGNTPPDLGYRCASEVIRVVGGEGSragggpsasPVL 81
Cdd:COG1957     1 MMRKVIIDTDPG-------IDDALALLLALASPEIDLLGITTVAGNVPLEQTTRNALKLLELAGRTDV---------PVA 64
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1174556942  82 RcgpfqptsGDPqRWLRQRREFASSPAGLAAWGRRLERAPVREEADRDvtgevppArLDDLVDDLR-SPERSTVVGIGPL 160
Cdd:COG1957    65 A--------GAA-RPLVRPLVTAEHVHGEDGLGGVDLPEPTRPPEPEH-------A-VDFIIETLRaAPGEVTLVALGPL 127
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1174556942 161 TNIARVLTEWDGASGRIDRIVVMGGALAFG---TMV-DTNFAVDPRAARVVVRFGIPITIVPLDTTRTTCLTRDRWRAIv 236
Cdd:COG1957   128 TNLALALRKDPELAERIKRIVIMGGAFFVPgnvTPVaEFNIYVDPEAAKIVFASGIPITMVGLDVTHQALLTPEDLARL- 206
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1174556942 237 rrAAMKGPTAIATASAFDAwvspWLSYSEATRPVDGMWVHDLVALVALAHPELVDSSQHRVDVRDDGKL-----VECPDG 311
Cdd:COG1957   207 --AALGTPLGRFLADLLDF----YLDFYRERYGLDGCPLHDPLAVAYLLDPELFTTRPAPVDVETDGELtrgqtVVDWRG 280
                         330       340
                  ....*....|....*....|....*..
gi 1174556942 312 VP-----VDIVEAVDNEAMISLWERTV 333
Cdd:COG1957   281 VTgrppnARVALDVDAERFLDLLLERL 307
IU_nuc_hydro pfam01156
Inosine-uridine preferring nucleoside hydrolase;
6-324 2.41e-37

Inosine-uridine preferring nucleoside hydrolase;


Pssm-ID: 460086 [Multi-domain]  Cd Length: 253  Bit Score: 134.26  E-value: 2.41e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1174556942   6 IIVDCDPGngvpganVDDALALAYALRSPLVDVGAVWTVFGNTPPDLGYRCASEVirvvggegsragggpsaspvlrcgp 85
Cdd:pfam01156   1 VIIDTDPG-------IDDALALLLALASPEIELLGITTVAGNVSLEQTTRNALRL------------------------- 48
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1174556942  86 fqptsgdpqrwlrqrrefasspagLAAWGRrlERAPVreeadrdVTGEVpparlddlvddLRSPERSTVVGIGPLTNIAR 165
Cdd:pfam01156  49 ------------------------LELGGR--DDIPV-------YAGEA-----------IREPGEVTLVATGPLTNLAL 84
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1174556942 166 VLTEWDGASGRIDRIVVMGGALAFG---TMV-DTNFAVDPRAARVVVRFGIPITIVPLDTTRTTCLTRDRWRAIvrrAAM 241
Cdd:pfam01156  85 ALRLDPELAKKIKELVIMGGAFGVRgnvTPAaEFNIFVDPEAAKIVFTSGLPITMVPLDVTHQALLTPEDLERL---AAL 161
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1174556942 242 KGPTAIATASAFDAwvspWLSYSEATRPVDGMWVHDLVALVALAHPELVDSSQHRVDVRDDGKL----------VECPDG 311
Cdd:pfam01156 162 GTPLGRFLADLLRF----YAEFYRERFGIDGPPLHDPLAVAVALDPELFTTRRLNVDVETTGGLtrgqtvvddrGGWGKP 237
                         330
                  ....*....|...
gi 1174556942 312 VPVDIVEAVDNEA 324
Cdd:pfam01156 238 PNVRVATDVDVDR 250
nuc_hydro_IU_UC_XIUA cd02651
nuc_hydro_IU_UC_XIUA: inosine-uridine preferring, ...
5-305 1.56e-36

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: 133.44  E-value: 1.56e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1174556942   5 RIIVDCDPGNgvpganvDDALALAYALRSPLVDVGAVWTVFGNTPPDLGYRCASEVIRVVGGEGSragggpsasPVLRcg 84
Cdd:cd02651     1 PIIIDCDPGH-------DDAVAILLALFHPELDLLGITTVAGNVPLEKTTRNALKLLTLLGRTDV---------PVAA-- 62
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1174556942  85 pfqptsGDPQRWLRQRrEFASS---PAGLAawGRRLERAPVREEAdrdvtgevPPArLDDLVDDLR-SPERSTVVGIGPL 160
Cdd:cd02651    63 ------GAARPLVRPL-ITASDihgESGLD--GADLPPPPRRPED--------IHA-VDAIIDTLRaSPEPITLVATGPL 124
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1174556942 161 TNIARVLTEWDGASGRIDRIVVMGGALAFGTMVDT---NFAVDPRAARVVVRFGIPITIVPLDTTRTTCLTRDRWRAIvr 237
Cdd:cd02651   125 TNIALLLRKYPELAERIKEIVLMGGALGRGNITPAaefNIFVDPEAAKIVFNSGIPITMVPLDVTHKALATPEVIERI-- 202
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1174556942 238 rAAMKGPTAIATASAFDAWVSPWlsyseATRPVDGMWVHDLVALVALAHPELVDSSQHRVDVRDDGKL 305
Cdd:cd02651   203 -RALGNPVGKMLAELLDFFAETY-----GSAFTEGPPLHDPCAVAYLLDPELFTTKRANVDVETEGEL 264
nuc_hydro_CaPnhB cd02650
NH_hydro_CaPnhB: A subgroup of nucleoside hydrolases similar to Corynebacterium ammoniagenes ...
5-304 3.46e-28

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: 111.21  E-value: 3.46e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1174556942   5 RIIVDCDPGngvpganVDDALALAYALRSPLVDVGAVWTVFGNTPPDLGYRCASEVIRVVGGEGSragggpsasPVLRcG 84
Cdd:cd02650     1 KLILDTDPG-------IDDAMALAYALAHPDVDLIGVTTVYGNVTIETATRNALALLELFGRPDV---------PVAE-G 63
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1174556942  85 PFQPTSGDPQRWLrqrrEFASSPAGLAawgrrlerapvreeadrDVTGEVPPARLDD------LVDDLRS-PERSTVVGI 157
Cdd:cd02650    64 AAKPLTRPPFRIA----TFVHGDNGLG-----------------DVELPAPPRQPEDesaadfLIELANEyPGELTLVAV 122
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1174556942 158 GPLTNIARVLTEWDGASGRIDRIVVMGGALAFG----TMVDTNFAVDPRAARVVVRFGIPITIVPLDTTRTTCLTRDrWR 233
Cdd:cd02650   123 GPLTNLALALARDPDFAKLVKQVVVMGGAFTVPgnvtPAAEANIHGDPEAADIVFTAGADLTMVGLDVTTQTLLTRE-DL 201
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1174556942 234 AIVRRAAMKGPTAIATASAF--DAWVSPWLsyseatrpVDGMWVHDLVALVALAHPELVDSSQHRVDVRDDGK 304
Cdd:cd02650   202 DELRDSGGKAGQFLADMLDYyiDFYQESPG--------LRGCALHDPLAVAAAVDPSLFTTREGVVRVETEGP 266
nuc_hydro cd00455
nuc_hydro: Nucleoside hydrolases. Nucleoside hydrolases cleave the N-glycosidic bond in ...
6-303 1.37e-25

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: 103.95  E-value: 1.37e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1174556942   6 IIVDCDPGngvpganVDDALALAYALRSPLVDVGAVWTVFGNTPPDLGYRCASEVIRVVGGEGSragggpsasPVLRcGP 85
Cdd:cd00455     1 VILDTDPG-------IDDAFALMYALLHPEIELVGIVATYGNVTLEQATQNAAYLLELLGRLDI---------PVYA-GA 63
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1174556942  86 FQPTSGDPQRWLRQRREfasspaglaaWGRRLERAPVREEADrdvtgevPPARLDDLVDDLRS-PERSTVVGIGPLTNIA 164
Cdd:cd00455    64 TRPLTGEIPAAYPEIHG----------EGGLGLPIPPIIEAD-------DPEAVQLLIDLIRKyPDEITIVALGPLTNLA 126
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1174556942 165 RVL-TEWDGASgRIDRIVVMGGALAFGTMV----DTNFAVDPRAARVVVRFGIPITIVPLDTTRTTCLTRDRWRAIVRRA 239
Cdd:cd00455   127 MAFiLDPDIKD-RVKEIVIMGGAFLVPGNVtpvaEANFYGDPEAANIVFNSAKNLTIVPLDVTNQAVLTPPMVERIFEQG 205
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1174556942 240 AMKGPTaIATASAFdawvspwlsYSEA--TRPVDGMWVHDLVALVALAHPELVDSSQHRVDVRDDG 303
Cdd:cd00455   206 TSIGLL-IKPMIDY---------YYKAyqKPGIEGSPIHDPLAVAYLLNPSMFDYSKVPVDVDTDG 261
PRK10768 PRK10768
ribonucleoside hydrolase RihC; Provisional
4-305 1.92e-25

ribonucleoside hydrolase RihC; Provisional


Pssm-ID: 182713 [Multi-domain]  Cd Length: 304  Bit Score: 103.84  E-value: 1.92e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1174556942   4 RRIIVDCDPGngvpganVDDALALAYALRSPLVDVGAVWTVFGNTPPDLGYRCA--------SEVirvvggegsragggp 75
Cdd:PRK10768    3 LPIILDTDPG-------IDDAVAIAAALFAPELDLKLITTVAGNVSVEKTTRNAlkllhffnSDV--------------- 60
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1174556942  76 sasPVLRcGPFQPTsgdpqrwLRQRREFAS--SPAGLAAW------GRRLERAPVreEADRDVTgevpparlddlvddLR 147
Cdd:PRK10768   61 ---PVAQ-GAAKPL-------VRPLRDAASvhGESGMEGYdfpehtRKPLSIPAV--EAMRDAL--------------MN 113
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1174556942 148 SPERSTVVGIGPLTNIARVLTEWDGASGRIDRIVVMGGALA---FGTMVDTNFAVDPRAARVVVRFGIPITIVPLDTTRT 224
Cdd:PRK10768  114 APEPVTLVAIGPLTNIALLLSTYPEVKPYIKRIVLMGGSAGrgnVTPNAEFNIAVDPEAAAIVFRSGIPIVMCGLDVTNQ 193
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1174556942 225 TCLTRDRWRAIvrraamkgPTAIATASAFDAWVSPWLSYSEATrpvdGMWVHDLVALVALAHPELVDSSQHRVDVRDDGK 304
Cdd:PRK10768  194 ALLTPDYLATL--------PELNRTGKMLHALFSHYRSGSMQT----GLRMHDVCAIAYLLRPELFTLKPCFVDVETQGE 261

                  .
gi 1174556942 305 L 305
Cdd:PRK10768  262 F 262
rihA PRK10443
ribonucleoside hydrolase 1; Provisional
3-305 2.05e-22

ribonucleoside hydrolase 1; Provisional


Pssm-ID: 182465 [Multi-domain]  Cd Length: 311  Bit Score: 95.50  E-value: 2.05e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1174556942   3 PRRIIVDCDPGNgvpganvDDALALAYALRSPLVDVGAVWTVFGNTPPDLGYRCASEVIRVVGGEGSragggpsaspvlr 82
Cdd:PRK10443    2 ALPIILDCDPGH-------DDAIALVLALASPELDVKAVTTSAGNQTPEKTLRNALRMLTLLNRTDI------------- 61
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1174556942  83 cgpfqPTSGDPQRWLRQRREFASSPAGLAAWGrrlerAPVREEADRDVtgeVPPARLDDLVDDLR-SPERSTVVGIGPLT 161
Cdd:PRK10443   62 -----PVAGGAVKPLMRELIIADNVHGESGLD-----GPALPEPTFAP---QNCTAVELMAKTLReSAEPVTLVSTGPQT 128
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1174556942 162 NIARVLTEWDGASGRIDRIVVMGGALAFGT---MVDTNFAVDPRAARVVVRFGIPITIVPLDTT-RTTCLTRDrwraIVR 237
Cdd:PRK10443  129 NVALLLASHPELHSKIARIVIMGGAMGLGNwtpAAEFNIYVDPEAAEIVFQSGIPIVMAGLDVThKAQIMDED----IER 204
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1174556942 238 RAAMKGPTAIATASAFDAWVspwLSYSEATRPVDGMWVHDLVALVALAHPELVDSSQHRVDVRDDGKL 305
Cdd:PRK10443  205 IRAIGNPVATIVAELLDFFM---EYHKDEKWGFVGAPLHDPCTIAWLLKPELFTTVERWVGVETQGEY 269
nuc_hydro_CjNH cd02654
nuc_hydro_CjNH. Nucleoside hydrolases similar to Campylobacter jejuni nucleoside hydrolase. ...
5-293 1.26e-20

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: 90.69  E-value: 1.26e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1174556942   5 RIIVDCDPGNGvpgANVDDALALAYALRSPLVDVGAVWTVFGNTPPDLGyrcASEVIRVVGGEGSRagggpsaspvlrCG 84
Cdd:cd02654     1 KVILDNDIAMG---RDTDDGLALALLLWSPEVELLGLSAVSGNCWLSAV---TYNVLRMLELAGAD------------AI 62
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1174556942  85 PFQPTSGDP---QRWLRQRREfasSPAGLAAWGRRLERAPVREEADRDVTGEVPPARLDDLVDDLRS-PERSTVVGIGPL 160
Cdd:cd02654    63 PVYAGANTPlgrTNRAFHAWE---SLYGAYLWQGAWSPEYSDMYTNASIIRNASIPAALFMIEMVRKhPHEVSIVAAGPL 139
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1174556942 161 TNIARVLTEWDGASGRIDRIVVMGGALAFGTMV-------DTNFAVDPRAARVVVRFGIPITIVPLDTTRTTCLTRDRWR 233
Cdd:cd02654   140 TNLALALRIDPDFAPLAKELVIMGGYLDDIGEFvnrhyasDFNLIMDPEAASIVLTAPWKSITIPGNVTNRTCLTPEQIK 219
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1174556942 234 AIVRRAAMkgptaiatasaFDAWVSPWLSY-SEATRPVDGMWVHDLVALVALAHPELVDSS 293
Cdd:cd02654   220 ADDPLRDF-----------IRETLDLPIDYaKEFVGTGDGLPMWDELASAVALDPELATSS 269
nuc_hydro_CeIAG cd02649
nuc_hydro_CeIAG: Nucleoside hydrolases similar to the inosine-adenosine-guanosine-preferring ...
4-305 6.21e-20

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: 88.47  E-value: 6.21e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1174556942   4 RRIIVDCDPGngvpganVDDALALAYALRSPLVDVGAVWTVFGNTPPDLGYRCASEVIRVVGGEGSragggpsasPVLRc 83
Cdd:cd02649     1 RKLIIDTDCG-------GDDAWALLMALASPNVEVLAITCVHGNTNVEQVVKNALRVLEACGRRDI---------PVYR- 63
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1174556942  84 gpfqptsGDPQRWLRQRRE----FASSpaGLAAWGrrLERAPVREEADRdvTGEVpparlDDLVDDLRSPERS-TVVGIG 158
Cdd:cd02649    64 -------GASKPLLGPGPTaayfHGKD--GFGDVG--FPEPKDELELQK--EHAV-----DAIIRLVREYPGEiTLVALG 125
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1174556942 159 PLTNIARVLTEWDGASGRIDRIVVMGGAlAFG----TMV-DTNFAVDPRAARVVV-RFGIPITIVPLDTTRTTCLTRDRW 232
Cdd:cd02649   126 PLTNLALAYRLDPSLPQKIKRLYIMGGN-REGvgntTPAaEFNFHVDPEAAHIVLnSFGCPITIVPWETTLLAFPLDWEF 204
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1174556942 233 raivrraAMKGPTAIATASAFDAwVSPwLSYSEA-TRPVDGMWVH-DLVALVALAHPELVDSSQ-HRVDVRDDGKL 305
Cdd:cd02649   205 -------EDKWANRLEKALFAES-LNR-REYAFAsEGLGGDGWVPcDALAVAAALDPSIITRRLtYAVDVELHGEL 271
nuc_hydro_3 cd02653
NH_3: A subgroup of nucleoside hydrolases. This group contains eukaryotic and bacterial ...
6-306 7.98e-20

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: 88.59  E-value: 7.98e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1174556942   6 IIVDCDPGngvpganVDDALALAYALRSPLVDVGAVWTVFGNTPPDLGYRCASEVIRVVGGegsragggpSASPVLRcGP 85
Cdd:cd02653     2 VIIDCDPG-------IDDALALLYLLASPDLDVVGITTTAGNVPVEQVAANALGVLELLGR---------TDIPVYL-GA 64
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1174556942  86 FQPTsgdpQRWLRQRREFaSSPAGLaawGRRLERAPVREEADRDVTGEvpparlddLVDDLRSPERSTVVGIGPLTNIAR 165
Cdd:cd02653    65 DKPL----AGPLTTAQDT-HGPDGL---GYAELPASTRTLSDESAAQA--------WVDLARAHPDLIGLATGPLTNLAL 128
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1174556942 166 VLTEwDGASGR-IDRIVVMGGALAF--GTMVDT--NFAVDPRAARVVV----RFGIPITIVPLDTTRTTCLTRDrWRAIV 236
Cdd:cd02653   129 ALRE-EPELPRlLRRLVIMGGAFNSrgNTSPVAewNYWVDPEAAKEVLaafgGHPVRPTICGLDVTRAVVLTPN-LLERL 206
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1174556942 237 RRAAMKGPTAIATASAFdawvspWLSYSEATRPVDGMWVHDLVALVALAHPELVDSSQHRVDVRDDGKLV 306
Cdd:cd02653   207 ARAKDSVGAFIEDALRF------YFEFHWAYGHGYGAVIHDPLAAAVALNPNLARGRPAYVDVECTGVLT 270
nuc_hydro_TvIAG cd02647
nuc_hydro_ TvIAG: Nucleoside hydrolases similar to the Inosine-adenosine-guanosine-preferring ...
4-322 4.37e-19

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: 86.32  E-value: 4.37e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1174556942   4 RRIIVDCDpgngvpgANVDDALALAYALRSPLVDVGAVwtVFGNTPPDLGYRCASEVIRvvggEGSRAGGGPSASPVLRC 83
Cdd:cd02647     1 KNVIFDHD-------GNVDDLVALLLLLKNEKVDLKGI--GVSGIDADCYVEPAVSVTR----KLIDRLGQRDAIPVGKG 67
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1174556942  84 GpfqptsgdpqrwLRQRREFASSPAGLAAWgrRLERAPVREEADRDVTGEVPPARLDDLVD-DLRSPERSTVVGIGPLTN 162
Cdd:cd02647    68 G------------SRAVNPFPRSWRRDAAF--SVDHLPILNERYTVETPLAEETAQLVLIEkIKASLEPVTLLVTGPLTN 133
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1174556942 163 IARVLTEWDGASGRIDRIVVMGGAL-----AFGTMVDT----NFAVDPRAARVVVRFGIPITIVPLDTTRTTCLTRDRWR 233
Cdd:cd02647   134 LARALDSDPDISSNIEEVYIMGGGVdapgnVFTPPSNGtaefNIFWDPLAAKTVFDSGLKITLVPLDATNTVPLTREFLE 213
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1174556942 234 AIVRRAAMKGPTAIATASAFDAWVSPWLSYSEATrpvdgMWvhDLVALVALAHPELVDSSQHR-----VDVRDDGKLVEC 308
Cdd:cd02647   214 TDRQRFAAQRLPASDLAGQGYALVKPLEFNSTYY-----MW--DVLTTLVLGAKEVDNTKESLilevdTDGLSAGQTVTS 286
                         330
                  ....*....|....
gi 1174556942 309 PDGVPVDIVEAVDN 322
Cdd:cd02647   287 PNGRPLTLVTSNNS 300
PLN02717 PLN02717
uridine nucleosidase
4-303 7.58e-19

uridine nucleosidase


Pssm-ID: 178319 [Multi-domain]  Cd Length: 316  Bit Score: 85.81  E-value: 7.58e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1174556942   4 RRIIVDCDPGngvpganVDDALALAYALRSPLVDVGAVWTVFGNTPPDLGYRCASEVIRVVGGEGSragggpsasPVLRc 83
Cdd:PLN02717    1 KKLIIDTDPG-------IDDAMAILMALRSPEVEVIGLTTIFGNVTTKLATRNALHLLEMAGRPDV---------PVAE- 63
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1174556942  84 GPFQPTSGDPQRWLRqrrEFASSPAGLaawGRRLERAPVREEADRDVTgevpparlDDLVDDLR-SPERSTVVGIGPLTN 162
Cdd:PLN02717   64 GSHEPLKGGTKPRIA---DFVHGSDGL---GNTNLPPPKGKKIEKSAA--------EFLVEKVSeYPGEVTVVALGPLTN 129
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1174556942 163 IARVLTEWDGASGRIDRIVVMGGALAFGTMV----DTNFAVDPRAARVVVRFGIPITIVPLDTTRTTCLTrDRWRAIVRR 238
Cdd:PLN02717  130 LALAIKLDPSFAKKVGQIVVLGGAFFVNGNVnpaaEANIFGDPEAADIVFTSGADITVVGINVTTQVVLT-DADLEELRD 208
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1174556942 239 AAMKGPTAIATASAFdawvspWLSYSEATRPVDGMWVHDLVALVALAHPELVDSSQHRVDVRDDG 303
Cdd:PLN02717  209 SKGKYAQFLCDICKF------YRDWHRKSYGIDGIYLHDPTALLAAVRPSLFTYKEGVVRVETEG 267
rihB PRK09955
ribosylpyrimidine nucleosidase;
1-299 1.98e-17

ribosylpyrimidine nucleosidase;


Pssm-ID: 182166 [Multi-domain]  Cd Length: 313  Bit Score: 81.53  E-value: 1.98e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1174556942   1 MAPRRIIVDCDPGNgvpganvDDALALAYALRSPLVDVGAVWTVFGNTPPDLGYRCASEVIRVVGGEGsragggpsasPV 80
Cdd:PRK09955    1 MEKRKIILDCDPGH-------DDAIAMMMAAKHPAIDLLGITIVAGNQTLDKTLINGLNVCQKLEINV----------PV 63
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1174556942  81 LrcgpfqptSGDPQRWLRQR--REFASSPAGLaawgrrleRAPVREEADRDVTGEVPPARLDDLVddLRSPERSTVVGIG 158
Cdd:PRK09955   64 Y--------AGMPQPIMRQQivADNIHGETGL--------DGPVFEPLTRQAESTHAVKYIIDTL--MASDGDITLVPVG 125
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1174556942 159 PLTNIARVLTEWDGASGRIDRIVVMGGALAFGTMVDT---NFAVDPRAARVVVRFGIPITIVPLDTTRTTCLTRDrwrAI 235
Cdd:PRK09955  126 PLSNIAVAMRMQPAILPKIREIVLMGGAYGTGNFTPSaefNIFADPEAARVVFTSGVPLVMMGLDLTNQTVCTPD---VI 202
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1174556942 236 VRRAAMKGPtaiaTASAFDAWVSPWLSYSEATRPVDGMWVHDLVALVALAHPELVDSSQHRVDV 299
Cdd:PRK09955  203 ARMERAGGP----AGELFSDIMNFTLKTQFENYGLAGGPVHDATCIGYLINPDGIKTQEMYVEV 262
nuc_hydro_1 cd02648
NH_1: A subgroup of nucleoside hydrolases. This group contains fungal proteins similar to ...
3-286 3.70e-15

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: 75.69  E-value: 3.70e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1174556942   3 PRRIIVDCDPGngvpganVDDALALAYALRSP-LVDVGAVWTVFGNTPPDLGYRCASEVIRV----VGGEGSRAGGGPSA 77
Cdd:cd02648     1 PHPIIIDTDPG-------VDDVLAILLALSSPeEVDVALISLTFGNTTLDHALRNVLRLFHVlereRAWRATPGVRYRAF 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1174556942  78 S-----PVLRCGPFQPTSGDpqrwlRQRREFASSPAGLAAWGRRL-ERAPVREEADRDVTGEVPPARL--DDLVDDLR-S 148
Cdd:cd02648    74 SadaekPIVASGSDQPLEGE-----RLTASYFHGRDGLSGVHWLHpDFTPVETWIPEIVAPLTPSDKPayDVILDILReE 148
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1174556942 149 PERS-TVVGIGPLTNIARVLTEWDGASGRIDRIVVMGGALAF----GTMVDTNFAVDPRAARVVVRFG----------IP 213
Cdd:cd02648   149 PDHTvTIAALGPLTNLAAAARKDPETFAKVGEVVVMGGAIDVpgntSPVAEFNCFADPYAAAVVIDEPpstapearrkLP 228
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1174556942 214 ITIVPLDTTRTTCLTRDRWR--AIVRRAAMKgptaiaTASAFDAWVSPWLSYSEATRP---------VDGMWVHDLVALV 282
Cdd:cd02648   229 LQVFPLDITTGHTLPYSSLFatYVTPRDAPE------RGSPLARWLEHVFISTFLTHPraftpeeflPDRSELFEMHDPL 302

                  ....
gi 1174556942 283 ALAH 286
Cdd:cd02648   303 AVWY 306
nuc_hydro_2 cd02652
NH_2: A subgroup of nucleoside hydrolases. This group contains eukaryotic and bacterial ...
153-218 1.28e-04

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: 43.26  E-value: 1.28e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1174556942 153 TVVGIGPLTNIARVL-TEWDGASG------RIDRIVVMGGALAF----GTMVDTNFAVDPRAARVVVR----FGIPITIV 217
Cdd:cd02652   112 TIVSIGPLTNLAALLdADADPLTGpelvrqKVKRLVVMGGAFYDpdgnVQHREYNFVTDPKAAQRVAGraqhLGIPVRIV 191

                  .
gi 1174556942 218 P 218
Cdd:cd02652   192 W 192
 
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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