|
Name |
Accession |
Description |
Interval |
E-value |
| PRK10768 |
PRK10768 |
ribonucleoside hydrolase RihC; Provisional |
1-304 |
0e+00 |
|
ribonucleoside hydrolase RihC; Provisional
Pssm-ID: 182713 [Multi-domain] Cd Length: 304 Bit Score: 581.10 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1248562618 1 MRLPIILDTDPGIDDAAAIAAALFSPELDLQLMTTVAGNVSVEKTTRNALQLLHFWNADIPLAQGAAMPLVRPLRDAASV 80
Cdd:PRK10768 1 MRLPIILDTDPGIDDAVAIAAALFAPELDLKLITTVAGNVSVEKTTRNALKLLHFFNSDVPVAQGAAKPLVRPLRDAASV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1248562618 81 HGESGMAGYDFVEHNRQPLAKPAFQAIRDALMHAPQPVTLVAIGPLTNIALLLTHYPECVFNIRRLVMMGGSAGRGNFTP 160
Cdd:PRK10768 81 HGESGMEGYDFPEHTRKPLSIPAVEAMRDALMNAPEPVTLVAIGPLTNIALLLSTYPEVKPYIKRIVLMGGSAGRGNVTP 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1248562618 161 NAEFNIAVDPEAAAKVFRSGLEIVMCGLDVTNQAMLAPEYLATLPALNQTGKMLHALFSHYRSGSMNTGLRMHDLCAIAW 240
Cdd:PRK10768 161 NAEFNIAVDPEAAAIVFRSGIPIVMCGLDVTNQALLTPDYLATLPELNRTGKMLHALFSHYRSGSMQTGLRMHDVCAIAY 240
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1248562618 241 LVRPDLFTLQPCFVAVETQGEYTSGTTVVDIEGRLGQPANAQVALALDVDGFRQWVAEVLSRAP 304
Cdd:PRK10768 241 LLRPELFTLKPCFVDVETQGEFTAGATVVDIDGRLGKPANAQVALDIDVDGFQKWFAEVLALAN 304
|
|
| nuc_hydro_IU_UC_XIUA |
cd02651 |
nuc_hydro_IU_UC_XIUA: inosine-uridine preferring, ... |
4-300 |
1.35e-145 |
|
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: 411.17 E-value: 1.35e-145
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1248562618 4 PIILDTDPGIDDAAAIAAALFSPELDLQLMTTVAGNVSVEKTTRNALQLLHFWNA-DIPLAQGAAMPLVRPLRDAASVHG 82
Cdd:cd02651 1 PIIIDCDPGHDDAVAILLALFHPELDLLGITTVAGNVPLEKTTRNALKLLTLLGRtDVPVAAGAARPLVRPLITASDIHG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1248562618 83 ESGMAGYDFVEHNRQPLAKPAFQAIRDALMHAPQPVTLVAIGPLTNIALLLTHYPECVFNIRRLVMMGGSAGRGNFTPNA 162
Cdd:cd02651 81 ESGLDGADLPPPPRRPEDIHAVDAIIDTLRASPEPITLVATGPLTNIALLLRKYPELAERIKEIVLMGGALGRGNITPAA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1248562618 163 EFNIAVDPEAAAKVFRSGLEIVMCGLDVTNQAMLAPEYLATLPAL-NQTGKMLHALFSHY--RSGSMNT-GLRMHDLCAI 238
Cdd:cd02651 161 EFNIFVDPEAAKIVFNSGIPITMVPLDVTHKALATPEVIERIRALgNPVGKMLAELLDFFaeTYGSAFTeGPPLHDPCAV 240
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1248562618 239 AWLVRPDLFTLQPCFVAVETQGEYTSGTTVVDIEGRLGQPANAQVALALDVDGFRQWVAEVL 300
Cdd:cd02651 241 AYLLDPELFTTKRANVDVETEGELTRGRTVVDLRGVTGRPANAQVAVDVDVEKFWDLLLEAL 302
|
|
| URH1 |
COG1957 |
Inosine-uridine nucleoside N-ribohydrolase [Nucleotide transport and metabolism]; ... |
1-303 |
4.33e-133 |
|
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: 379.88 E-value: 4.33e-133
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1248562618 1 MRLPIILDTDPGIDDAAAIAAALFSPELDLQLMTTVAGNVSVEKTTRNALQLLHFWNA-DIPLAQGAAMPLVRPLRDAAS 79
Cdd:COG1957 1 MMRKVIIDTDPGIDDALALLLALASPEIDLLGITTVAGNVPLEQTTRNALKLLELAGRtDVPVAAGAARPLVRPLVTAEH 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1248562618 80 VHGESGMAGYDFVEHNRQPLAKPAFQAIRDALMHAPQPVTLVAIGPLTNIALLLTHYPECVFNIRRLVMMGGSA-GRGNF 158
Cdd:COG1957 81 VHGEDGLGGVDLPEPTRPPEPEHAVDFIIETLRAAPGEVTLVALGPLTNLALALRKDPELAERIKRIVIMGGAFfVPGNV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1248562618 159 TPNAEFNIAVDPEAAAKVFRSGLEIVMCGLDVTNQAMLAPEYLATLPAL-NQTGKMLHALFSHYRSGSMNT----GLRMH 233
Cdd:COG1957 161 TPVAEFNIYVDPEAAKIVFASGIPITMVGLDVTHQALLTPEDLARLAALgTPLGRFLADLLDFYLDFYRERygldGCPLH 240
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1248562618 234 DLCAIAWLVRPDLFTLQPCFVAVETQGEYTSGTTVVDIEGRLGQPANAQVALALDVDGFRQWVAEVLSRA 303
Cdd:COG1957 241 DPLAVAYLLDPELFTTRPAPVDVETDGELTRGQTVVDWRGVTGRPPNARVALDVDAERFLDLLLERLARL 310
|
|
| IU_nuc_hydro |
pfam01156 |
Inosine-uridine preferring nucleoside hydrolase; |
5-294 |
3.44e-89 |
|
Inosine-uridine preferring nucleoside hydrolase;
Pssm-ID: 460086 [Multi-domain] Cd Length: 253 Bit Score: 266.38 E-value: 3.44e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1248562618 5 IILDTDPGIDDAAAIAAALFSPELDLQLMTTVAGNVSVEKTTRNALQLLHFWNAD-IPLAQGaamplvrplrdaasvhge 83
Cdd:pfam01156 1 VIIDTDPGIDDALALLLALASPEIELLGITTVAGNVSLEQTTRNALRLLELGGRDdIPVYAG------------------ 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1248562618 84 sgmagyDFVehnrqplakpafqairdalmHAPQPVTLVAIGPLTNIALLLTHYPECVFNIRRLVMMGGSAG-RGNFTPNA 162
Cdd:pfam01156 63 ------EAI--------------------REPGEVTLVATGPLTNLALALRLDPELAKKIKELVIMGGAFGvRGNVTPAA 116
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1248562618 163 EFNIAVDPEAAAKVFRSGLEIVMCGLDVTNQAMLAPEYLATLPAL-NQTGKMLHALFSHYRSGSMNT----GLRMHDLCA 237
Cdd:pfam01156 117 EFNIFVDPEAAKIVFTSGLPITMVPLDVTHQALLTPEDLERLAALgTPLGRFLADLLRFYAEFYRERfgidGPPLHDPLA 196
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 1248562618 238 IAWLVRPDLFTLQPCFVAVETQGEYTSGTTVVDIEGRLGQPANAQVALALDVDGFRQ 294
Cdd:pfam01156 197 VAVALDPELFTTRRLNVDVETTGGLTRGQTVVDDRGGWGKPPNVRVATDVDVDRFWE 253
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| PRK10768 |
PRK10768 |
ribonucleoside hydrolase RihC; Provisional |
1-304 |
0e+00 |
|
ribonucleoside hydrolase RihC; Provisional
Pssm-ID: 182713 [Multi-domain] Cd Length: 304 Bit Score: 581.10 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1248562618 1 MRLPIILDTDPGIDDAAAIAAALFSPELDLQLMTTVAGNVSVEKTTRNALQLLHFWNADIPLAQGAAMPLVRPLRDAASV 80
Cdd:PRK10768 1 MRLPIILDTDPGIDDAVAIAAALFAPELDLKLITTVAGNVSVEKTTRNALKLLHFFNSDVPVAQGAAKPLVRPLRDAASV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1248562618 81 HGESGMAGYDFVEHNRQPLAKPAFQAIRDALMHAPQPVTLVAIGPLTNIALLLTHYPECVFNIRRLVMMGGSAGRGNFTP 160
Cdd:PRK10768 81 HGESGMEGYDFPEHTRKPLSIPAVEAMRDALMNAPEPVTLVAIGPLTNIALLLSTYPEVKPYIKRIVLMGGSAGRGNVTP 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1248562618 161 NAEFNIAVDPEAAAKVFRSGLEIVMCGLDVTNQAMLAPEYLATLPALNQTGKMLHALFSHYRSGSMNTGLRMHDLCAIAW 240
Cdd:PRK10768 161 NAEFNIAVDPEAAAIVFRSGIPIVMCGLDVTNQALLTPDYLATLPELNRTGKMLHALFSHYRSGSMQTGLRMHDVCAIAY 240
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1248562618 241 LVRPDLFTLQPCFVAVETQGEYTSGTTVVDIEGRLGQPANAQVALALDVDGFRQWVAEVLSRAP 304
Cdd:PRK10768 241 LLRPELFTLKPCFVDVETQGEFTAGATVVDIDGRLGKPANAQVALDIDVDGFQKWFAEVLALAN 304
|
|
| nuc_hydro_IU_UC_XIUA |
cd02651 |
nuc_hydro_IU_UC_XIUA: inosine-uridine preferring, ... |
4-300 |
1.35e-145 |
|
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: 411.17 E-value: 1.35e-145
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1248562618 4 PIILDTDPGIDDAAAIAAALFSPELDLQLMTTVAGNVSVEKTTRNALQLLHFWNA-DIPLAQGAAMPLVRPLRDAASVHG 82
Cdd:cd02651 1 PIIIDCDPGHDDAVAILLALFHPELDLLGITTVAGNVPLEKTTRNALKLLTLLGRtDVPVAAGAARPLVRPLITASDIHG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1248562618 83 ESGMAGYDFVEHNRQPLAKPAFQAIRDALMHAPQPVTLVAIGPLTNIALLLTHYPECVFNIRRLVMMGGSAGRGNFTPNA 162
Cdd:cd02651 81 ESGLDGADLPPPPRRPEDIHAVDAIIDTLRASPEPITLVATGPLTNIALLLRKYPELAERIKEIVLMGGALGRGNITPAA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1248562618 163 EFNIAVDPEAAAKVFRSGLEIVMCGLDVTNQAMLAPEYLATLPAL-NQTGKMLHALFSHY--RSGSMNT-GLRMHDLCAI 238
Cdd:cd02651 161 EFNIFVDPEAAKIVFNSGIPITMVPLDVTHKALATPEVIERIRALgNPVGKMLAELLDFFaeTYGSAFTeGPPLHDPCAV 240
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1248562618 239 AWLVRPDLFTLQPCFVAVETQGEYTSGTTVVDIEGRLGQPANAQVALALDVDGFRQWVAEVL 300
Cdd:cd02651 241 AYLLDPELFTTKRANVDVETEGELTRGRTVVDLRGVTGRPANAQVAVDVDVEKFWDLLLEAL 302
|
|
| URH1 |
COG1957 |
Inosine-uridine nucleoside N-ribohydrolase [Nucleotide transport and metabolism]; ... |
1-303 |
4.33e-133 |
|
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: 379.88 E-value: 4.33e-133
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1248562618 1 MRLPIILDTDPGIDDAAAIAAALFSPELDLQLMTTVAGNVSVEKTTRNALQLLHFWNA-DIPLAQGAAMPLVRPLRDAAS 79
Cdd:COG1957 1 MMRKVIIDTDPGIDDALALLLALASPEIDLLGITTVAGNVPLEQTTRNALKLLELAGRtDVPVAAGAARPLVRPLVTAEH 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1248562618 80 VHGESGMAGYDFVEHNRQPLAKPAFQAIRDALMHAPQPVTLVAIGPLTNIALLLTHYPECVFNIRRLVMMGGSA-GRGNF 158
Cdd:COG1957 81 VHGEDGLGGVDLPEPTRPPEPEHAVDFIIETLRAAPGEVTLVALGPLTNLALALRKDPELAERIKRIVIMGGAFfVPGNV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1248562618 159 TPNAEFNIAVDPEAAAKVFRSGLEIVMCGLDVTNQAMLAPEYLATLPAL-NQTGKMLHALFSHYRSGSMNT----GLRMH 233
Cdd:COG1957 161 TPVAEFNIYVDPEAAKIVFASGIPITMVGLDVTHQALLTPEDLARLAALgTPLGRFLADLLDFYLDFYRERygldGCPLH 240
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1248562618 234 DLCAIAWLVRPDLFTLQPCFVAVETQGEYTSGTTVVDIEGRLGQPANAQVALALDVDGFRQWVAEVLSRA 303
Cdd:COG1957 241 DPLAVAYLLDPELFTTRPAPVDVETDGELTRGQTVVDWRGVTGRPPNARVALDVDAERFLDLLLERLARL 310
|
|
| rihA |
PRK10443 |
ribonucleoside hydrolase 1; Provisional |
1-302 |
1.03e-100 |
|
ribonucleoside hydrolase 1; Provisional
Pssm-ID: 182465 [Multi-domain] Cd Length: 311 Bit Score: 297.73 E-value: 1.03e-100
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1248562618 1 MRLPIILDTDPGIDDAAAIAAALFSPELDLQLMTTVAGNVSVEKTTRNALQLLHFWN-ADIPLAQGAAMPLVRPLRDAAS 79
Cdd:PRK10443 1 MALPIILDCDPGHDDAIALVLALASPELDVKAVTTSAGNQTPEKTLRNALRMLTLLNrTDIPVAGGAVKPLMRELIIADN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1248562618 80 VHGESGMAGYDFVEHNRQPLAKPAFQAIRDALMHAPQPVTLVAIGPLTNIALLLTHYPECVFNIRRLVMMGGSAGRGNFT 159
Cdd:PRK10443 81 VHGESGLDGPALPEPTFAPQNCTAVELMAKTLRESAEPVTLVSTGPQTNVALLLASHPELHSKIARIVIMGGAMGLGNWT 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1248562618 160 PNAEFNIAVDPEAAAKVFRSGLEIVMCGLDVTNQAMLAPEYLATLPALNQ-----TGKMLHALFSHYRSGSMN-TGLRMH 233
Cdd:PRK10443 161 PAAEFNIYVDPEAAEIVFQSGIPIVMAGLDVTHKAQIMDEDIERIRAIGNpvatiVAELLDFFMEYHKDEKWGfVGAPLH 240
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1248562618 234 DLCAIAWLVRPDLFTLQPCFVAVETQGEYTSGTTVVDIEGRLGQPANAQVALALDVDGFRQWVAEVLSR 302
Cdd:PRK10443 241 DPCTIAWLLKPELFTTVERWVGVETQGEYTQGMTVVDYYQLTGNKPNATVLVDVDRQGFVDLLAERLKF 309
|
|
| IU_nuc_hydro |
pfam01156 |
Inosine-uridine preferring nucleoside hydrolase; |
5-294 |
3.44e-89 |
|
Inosine-uridine preferring nucleoside hydrolase;
Pssm-ID: 460086 [Multi-domain] Cd Length: 253 Bit Score: 266.38 E-value: 3.44e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1248562618 5 IILDTDPGIDDAAAIAAALFSPELDLQLMTTVAGNVSVEKTTRNALQLLHFWNAD-IPLAQGaamplvrplrdaasvhge 83
Cdd:pfam01156 1 VIIDTDPGIDDALALLLALASPEIELLGITTVAGNVSLEQTTRNALRLLELGGRDdIPVYAG------------------ 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1248562618 84 sgmagyDFVehnrqplakpafqairdalmHAPQPVTLVAIGPLTNIALLLTHYPECVFNIRRLVMMGGSAG-RGNFTPNA 162
Cdd:pfam01156 63 ------EAI--------------------REPGEVTLVATGPLTNLALALRLDPELAKKIKELVIMGGAFGvRGNVTPAA 116
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1248562618 163 EFNIAVDPEAAAKVFRSGLEIVMCGLDVTNQAMLAPEYLATLPAL-NQTGKMLHALFSHYRSGSMNT----GLRMHDLCA 237
Cdd:pfam01156 117 EFNIFVDPEAAKIVFTSGLPITMVPLDVTHQALLTPEDLERLAALgTPLGRFLADLLRFYAEFYRERfgidGPPLHDPLA 196
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 1248562618 238 IAWLVRPDLFTLQPCFVAVETQGEYTSGTTVVDIEGRLGQPANAQVALALDVDGFRQ 294
Cdd:pfam01156 197 VAVALDPELFTTRRLNVDVETTGGLTRGQTVVDDRGGWGKPPNVRVATDVDVDRFWE 253
|
|
| rihB |
PRK09955 |
ribosylpyrimidine nucleosidase; |
2-298 |
1.22e-72 |
|
ribosylpyrimidine nucleosidase;
Pssm-ID: 182166 [Multi-domain] Cd Length: 313 Bit Score: 226.37 E-value: 1.22e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1248562618 2 RLPIILDTDPGIDDAAAIAAALFSPELDLQLMTTVAGNVSVEKTTRNALQLLHFWNADIPLAQGAAMPLVRPLRDAASVH 81
Cdd:PRK09955 3 KRKIILDCDPGHDDAIAMMMAAKHPAIDLLGITIVAGNQTLDKTLINGLNVCQKLEINVPVYAGMPQPIMRQQIVADNIH 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1248562618 82 GESGMAGYDFVEHNRQPLAKPAFQAIRDALMHAPQPVTLVAIGPLTNIALLLTHYPECVFNIRRLVMMGGSAGRGNFTPN 161
Cdd:PRK09955 83 GETGLDGPVFEPLTRQAESTHAVKYIIDTLMASDGDITLVPVGPLSNIAVAMRMQPAILPKIREIVLMGGAYGTGNFTPS 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1248562618 162 AEFNIAVDPEAAAKVFRSGLEIVMCGLDVTNQAMLAPEYLATLPAL-NQTGKMLHALFSH-YRSGSMNTGLR---MHDLC 236
Cdd:PRK09955 163 AEFNIFADPEAARVVFTSGVPLVMMGLDLTNQTVCTPDVIARMERAgGPAGELFSDIMNFtLKTQFENYGLAggpVHDAT 242
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1248562618 237 AIAWLVRPDLFTLQPCFVAVETQGEYTSGTTVVDIEGRLGQPANAQVALALDVDGFRQWVAE 298
Cdd:PRK09955 243 CIGYLINPDGIKTQEMYVEVDVNSGPCYGRTVCDELGVLGKPANTKVGITIDTDWFWGLVEE 304
|
|
| nuc_hydro_CaPnhB |
cd02650 |
NH_hydro_CaPnhB: A subgroup of nucleoside hydrolases similar to Corynebacterium ammoniagenes ... |
5-290 |
2.36e-70 |
|
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: 220.23 E-value: 2.36e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1248562618 5 IILDTDPGIDDAAAIAAALFSPELDLQLMTTVAGNVSVEKTTRNALQLLHFWNA-DIPLAQGAAMPLVRPLRD-AASVHG 82
Cdd:cd02650 2 LILDTDPGIDDAMALAYALAHPDVDLIGVTTVYGNVTIETATRNALALLELFGRpDVPVAEGAAKPLTRPPFRiATFVHG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1248562618 83 ESGMAGYDFVEHNRQPLAKPAFQAIRDALMHAPQPVTLVAIGPLTNIALLLTHYPECVFNIRRLVMMGGSAG-RGNFTPN 161
Cdd:cd02650 82 DNGLGDVELPAPPRQPEDESAADFLIELANEYPGELTLVAVGPLTNLALALARDPDFAKLVKQVVVMGGAFTvPGNVTPA 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1248562618 162 AEFNIAVDPEAAAKVFRSGLEIVMCGLDVTNQAMLAPEYLATLPAL-NQTGKMLHALFSHYR-SGSMNTGLR---MHDLC 236
Cdd:cd02650 162 AEANIHGDPEAADIVFTAGADLTMVGLDVTTQTLLTREDLDELRDSgGKAGQFLADMLDYYIdFYQESPGLRgcaLHDPL 241
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 1248562618 237 AIAWLVRPDLFTLQPCFVAVETQGEYTsGTTVVDIEGRLGQPANAQVALALDVD 290
Cdd:cd02650 242 AVAAAVDPSLFTTREGVVRVETEGPTR-GRTIGDRDGRRFWDSSPNATVAVDVD 294
|
|
| nuc_hydro |
cd00455 |
nuc_hydro: Nucleoside hydrolases. Nucleoside hydrolases cleave the N-glycosidic bond in ... |
5-294 |
5.48e-68 |
|
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: 213.73 E-value: 5.48e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1248562618 5 IILDTDPGIDDAAAIAAALFSPELDLQLMTTVAGNVSVEKTTRNALQLLH-FWNADIPLAQGAAMPLVRPLRDAASVHGE 83
Cdd:cd00455 1 VILDTDPGIDDAFALMYALLHPEIELVGIVATYGNVTLEQATQNAAYLLElLGRLDIPVYAGATRPLTGEIPAAYPEIHG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1248562618 84 SGMAGYDFVEHNRQPlAKPAFQAIRDALMHAPQPVTLVAIGPLTNIALLLTHYPECVFNIRRLVMMGGSAG-RGNFTPNA 162
Cdd:cd00455 81 EGGLGLPIPPIIEAD-DPEAVQLLIDLIRKYPDEITIVALGPLTNLAMAFILDPDIKDRVKEIVIMGGAFLvPGNVTPVA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1248562618 163 EFNIAVDPEAAAKVFRSGLEIVMCGLDVTNQAMLAPEYLATLPALNQTGKMLHALFSHYRSGS----MNTGLRMHDLCAI 238
Cdd:cd00455 160 EANFYGDPEAANIVFNSAKNLTIVPLDVTNQAVLTPPMVERIFEQGTSIGLLIKPMIDYYYKAyqkpGIEGSPIHDPLAV 239
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 1248562618 239 AWLVRPDLFTLQPCFVAVETQGeYTSGTTVVDIEGRLGQPaNAQVALALDVDGFRQ 294
Cdd:cd00455 240 AYLLNPSMFDYSKVPVDVDTDG-LTRGQTIADFRENPGNG-VTRVAVNLDYPDFIE 293
|
|
| nuc_hydro_3 |
cd02653 |
NH_3: A subgroup of nucleoside hydrolases. This group contains eukaryotic and bacterial ... |
4-292 |
1.23e-57 |
|
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: 187.97 E-value: 1.23e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1248562618 4 PIILDTDPGIDDAAAIAAALFSPELDLQLMTTVAGNVSVEKTTRNALQLLHFWNA-DIPLAQGAAMPLVRPLRDAASVHG 82
Cdd:cd02653 1 KVIIDCDPGIDDALALLYLLASPDLDVVGITTTAGNVPVEQVAANALGVLELLGRtDIPVYLGADKPLAGPLTTAQDTHG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1248562618 83 ESGMAGYDFVEHNRQPLAKPAFQAIRDALMHAPQpVTLVAIGPLTNIALLLTHYPECVFNIRRLVMMGGS-AGRGNFTPN 161
Cdd:cd02653 81 PDGLGYAELPASTRTLSDESAAQAWVDLARAHPD-LIGLATGPLTNLALALREEPELPRLLRRLVIMGGAfNSRGNTSPV 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1248562618 162 AEFNIAVDPEAAAKVF----RSGLEIVMCGLDVTNQAMLAPEYLATL-----PALNQTGKMLHALFSHYRSGSMNTGLRM 232
Cdd:cd02653 160 AEWNYWVDPEAAKEVLaafgGHPVRPTICGLDVTRAVVLTPNLLERLarakdSVGAFIEDALRFYFEFHWAYGHGYGAVI 239
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1248562618 233 HDLCAIAWLVRPDLFTLQPCFVAVETQGEYTsGTTVVDIEGRLGQPANAQVALALDVDGF 292
Cdd:cd02653 240 HDPLAAAVALNPNLARGRPAYVDVECTGVLT-GQTVVDWAGFWGKGANAEILTKVDSQDF 298
|
|
| nuc_hydro_CeIAG |
cd02649 |
nuc_hydro_CeIAG: Nucleoside hydrolases similar to the inosine-adenosine-guanosine-preferring ... |
5-294 |
3.90e-56 |
|
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: 183.61 E-value: 3.90e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1248562618 5 IILDTDPGIDDAAAIAAALFSPELDLQLMTTVAGNVSVEKTTRNALQLLHFWN-ADIPLAQGAAMPLVRPLRDAASVHGE 83
Cdd:cd02649 3 LIIDTDCGGDDAWALLMALASPNVEVLAITCVHGNTNVEQVVKNALRVLEACGrRDIPVYRGASKPLLGPGPTAAYFHGK 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1248562618 84 SGM--AGYDFVEHNRQPLAKPAFQAIRDALMHAPQPVTLVAIGPLTNIALLLTHYPECVFNIRRLVMMGGSA-GRGNFTP 160
Cdd:cd02649 83 DGFgdVGFPEPKDELELQKEHAVDAIIRLVREYPGEITLVALGPLTNLALAYRLDPSLPQKIKRLYIMGGNReGVGNTTP 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1248562618 161 NAEFNIAVDPEAAAKVFRS-GLEIVMCGLDVTNQAMLAP-EYLATLPALNQTGKMLHALF-SHYRSGSMNTGLRMHDLC- 236
Cdd:cd02649 163 AAEFNFHVDPEAAHIVLNSfGCPITIVPWETTLLAFPLDwEFEDKWANRLEKALFAESLNrREYAFASEGLGGDGWVPCd 242
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1248562618 237 --AIAWLVRPDLFT-LQPCFVAVETQGEYTSGTTVVDIEGRLGQPANAQVALALDVDGFRQ 294
Cdd:cd02649 243 alAVAAALDPSIITrRLTYAVDVELHGELTRGQMVVDWLGTLKKKPNARVITKIDREKFKE 303
|
|
| PLN02717 |
PLN02717 |
uridine nucleosidase |
5-300 |
2.38e-52 |
|
uridine nucleosidase
Pssm-ID: 178319 [Multi-domain] Cd Length: 316 Bit Score: 174.02 E-value: 2.38e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1248562618 5 IILDTDPGIDDAAAIAAALFSPELDLQLMTTVAGNVSVEKTTRNALQLLH-FWNADIPLAQGAAMPLVR--PLRDAASVH 81
Cdd:PLN02717 3 LIIDTDPGIDDAMAILMALRSPEVEVIGLTTIFGNVTTKLATRNALHLLEmAGRPDVPVAEGSHEPLKGgtKPRIADFVH 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1248562618 82 GESGMAGYDFVEHNRQPLAKPAFQAIRDALMHAPQPVTLVAIGPLTNIALLLTHYPECVFNIRRLVMMGGS-AGRGNFTP 160
Cdd:PLN02717 83 GSDGLGNTNLPPPKGKKIEKSAAEFLVEKVSEYPGEVTVVALGPLTNLALAIKLDPSFAKKVGQIVVLGGAfFVNGNVNP 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1248562618 161 NAEFNIAVDPEAAAKVFRSGLEIVMCGLDVTNQAMLAPEYLATLPALN-QTGKMLHALFSHYRSGSMNT----GLRMHDL 235
Cdd:PLN02717 163 AAEANIFGDPEAADIVFTSGADITVVGINVTTQVVLTDADLEELRDSKgKYAQFLCDICKFYRDWHRKSygidGIYLHDP 242
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1248562618 236 CAIAWLVRPDLFTLQPCFVAVETQGeYTSGTTVVDIEGRLGQPANA-------QVALALDVDGFRQWVAEVL 300
Cdd:PLN02717 243 TALLAAVRPSLFTYKEGVVRVETEG-ICRGLTLFDNGLKRWNGENAwtgrppvKVAVTVDAPAVVELVKERL 313
|
|
| nuc_hydro_CjNH |
cd02654 |
nuc_hydro_CjNH. Nucleoside hydrolases similar to Campylobacter jejuni nucleoside hydrolase. ... |
5-296 |
5.64e-35 |
|
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: 128.83 E-value: 5.64e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1248562618 5 IILDTDPGIDDAA----AIAAALFSPELDLQLMTTVAGNVSVEKTTRNALQLLHFWNAD-IPLAQGAAMPLVRPLR---- 75
Cdd:cd02654 2 VILDNDIAMGRDTddglALALLLWSPEVELLGLSAVSGNCWLSAVTYNVLRMLELAGADaIPVYAGANTPLGRTNRafha 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1248562618 76 -----------DAASVHGESGMAGYDFVEhNRQPlakPAFQAIRDALMHAPQPVTLVAIGPLTNIALLLTHYPECVFNIR 144
Cdd:cd02654 82 weslygaylwqGAWSPEYSDMYTNASIIR-NASI---PAALFMIEMVRKHPHEVSIVAAGPLTNLALALRIDPDFAPLAK 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1248562618 145 RLVMMGGS--AGRGNFTPN--AEFNIAVDPEAAAKVFRSGLEIVMCGLDVTNQAMLAPEYLATLPALNQTGKMLHALFSH 220
Cdd:cd02654 158 ELVIMGGYldDIGEFVNRHyaSDFNLIMDPEAASIVLTAPWKSITIPGNVTNRTCLTPEQIKADDPLRDFIRETLDLPID 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1248562618 221 YRSGSMNT--GLRMHDLCAIAWLVRPDLFTLQPCFvAVETQGEYTSGTTVVDIEGRLGQ----PANAQVALALDVDGFRQ 294
Cdd:cd02654 238 YAKEFVGTgdGLPMWDELASAVALDPELATSSETF-YIDVQTDSDGGGQLIWPEDLLLAkglrPYHVKVITAVDVAAFLN 316
|
..
gi 1248562618 295 WV 296
Cdd:cd02654 317 LI 318
|
|
| nuc_hydro_1 |
cd02648 |
NH_1: A subgroup of nucleoside hydrolases. This group contains fungal proteins similar to ... |
4-270 |
6.22e-32 |
|
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: 121.92 E-value: 6.22e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1248562618 4 PIILDTDPGIDDAAAIAAALFSP-ELDLQLMTTVAGNVSVEKTTRNALQLLHF------WNADIP--------------L 62
Cdd:cd02648 3 PIIIDTDPGVDDVLAILLALSSPeEVDVALISLTFGNTTLDHALRNVLRLFHVlereraWRATPGvryrafsadaekpiV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1248562618 63 AQGAAMPLVRPLRDAASVHGESGMAG---------------YDFVEHnRQPLAKPAFQAIRDAL-MHAPQPVTLVAIGPL 126
Cdd:cd02648 83 ASGSDQPLEGERLTASYFHGRDGLSGvhwlhpdftpvetwiPEIVAP-LTPSDKPAYDVILDILrEEPDHTVTIAALGPL 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1248562618 127 TNIALLLTHYPECVFNIRRLVMMGGSAGR-GNFTPNAEFNIAVDPEAAAKVF----------RSGLEIVMCGLDVT---- 191
Cdd:cd02648 162 TNLAAAARKDPETFAKVGEVVVMGGAIDVpGNTSPVAEFNCFADPYAAAVVIdeppstapeaRRKLPLQVFPLDITtght 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1248562618 192 -NQAMLAPEYLATLPAlNQTGKMLHALFSHYRSGSMNTGLR----------------MHDLCAIAWLVRPDL-------- 246
Cdd:cd02648 242 lPYSSLFATYVTPRDA-PERGSPLARWLEHVFISTFLTHPRaftpeeflpdrselfeMHDPLAVWYAIFADMpatgsidg 320
|
330 340
....*....|....*....|....*.
gi 1248562618 247 --FTLQPCFVAVETQGEYTSGTTVVD 270
Cdd:cd02648 321 ngWKHTPRDFRVETSGQWTRGMCVVD 346
|
|
| nuc_hydro_TvIAG |
cd02647 |
nuc_hydro_ TvIAG: Nucleoside hydrolases similar to the Inosine-adenosine-guanosine-preferring ... |
4-274 |
4.89e-28 |
|
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: 110.20 E-value: 4.89e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1248562618 4 PIILDTDPGIDDAAAIAAALFSPELDLQLMTTVAG--------NVSVektTRNALQLLHFwNADIPLAQGAAMPlVRPL- 74
Cdd:cd02647 2 NVIFDHDGNVDDLVALLLLLKNEKVDLKGIGVSGIdadcyvepAVSV---TRKLIDRLGQ-RDAIPVGKGGSRA-VNPFp 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1248562618 75 ----RDAAsvhgESGMAGYDFVEHN--RQPLAK-PAFQAIRDALMHAPQPVTLVAIGPLTNIALLLTHYPECVFNIRRLV 147
Cdd:cd02647 77 rswrRDAA----FSVDHLPILNERYtvETPLAEeTAQLVLIEKIKASLEPVTLLVTGPLTNLARALDSDPDISSNIEEVY 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1248562618 148 MMGGSAG-RGN-FTP----NAEFNIAVDPEAAAKVFRSGLEIVMCGLDVTNQAMLAPEYLATL-----PALNQTGKMLHA 216
Cdd:cd02647 153 IMGGGVDaPGNvFTPpsngTAEFNIFWDPLAAKTVFDSGLKITLVPLDATNTVPLTREFLETDrqrfaAQRLPASDLAGQ 232
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 1248562618 217 LFSHYRSGSMNTGLRMHDLCAIAWLVRPDL-FTLQPCFVAVETQGEyTSGTTVVDIEGR 274
Cdd:cd02647 233 GYALVKPLEFNSTYYMWDVLTTLVLGAKEVdNTKESLILEVDTDGL-SAGQTVTSPNGR 290
|
|
| nuc_hydro_2 |
cd02652 |
NH_2: A subgroup of nucleoside hydrolases. This group contains eukaryotic and bacterial ... |
5-298 |
1.69e-11 |
|
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: 63.67 E-value: 1.69e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1248562618 5 IILDTDPGIDDAAAIAAALF--SPELDLQLMTTVAGNVS--VEKTTRNALQLlhfwNADIPLAQGAAMPlVRPLRDAASV 80
Cdd:cd02652 1 LILDTDIGGDPDDALALALAhaLQKCDLLAVTITLADASarRAIDAVNRFYG----RGDIPIGADYHGW-PEDAKDHAKF 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1248562618 81 hgesgMAGYDFVEHNRQP--LAKPAFQAIRDALMHA-PQPVTLVAIGPLTNIALLLT------HYPECVFN-IRRLVMMG 150
Cdd:cd02652 76 -----LLEGDRLHHDLESaeDALDAVKALRRLLASAeDASVTIVSIGPLTNLAALLDadadplTGPELVRQkVKRLVVMG 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1248562618 151 GSAGR--GNfTPNAEFNIAVDPEAAAKVFRSG------LEIVMCGLDVTNQAMLAPEYLATLPALNQTGKMLhalfsHYR 222
Cdd:cd02652 151 GAFYDpdGN-VQHREYNFVTDPKAAQRVAGRAqhlgipVRIVWSGYELGEAVSYPHVLVIAHPFNTPVFAAY-----WPR 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1248562618 223 SGSMNTglrmHDLCAIAWLVRP--DLFTLqpcfvaVETQGEYtsGTTVVDIEG--RLGQPANaQVALALDVDGFRQWVAE 298
Cdd:cd02652 225 SHRRPL----WDPLTLLAAVRGggMLFDL------REVQLGP--GRVEVDSSGvtEFHPPES-GRARRLTSSPEKAALRA 291
|
|
| PTZ00313 |
PTZ00313 |
inosine-adenosine-guanosine-nucleoside hydrolase; Provisional |
105-274 |
1.04e-07 |
|
inosine-adenosine-guanosine-nucleoside hydrolase; Provisional
Pssm-ID: 140334 [Multi-domain] Cd Length: 326 Bit Score: 52.56 E-value: 1.04e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1248562618 105 QAIRDALMHAPQPVTLVAIGPLTNIALLLTHYPECVF-NIRRLVMMGGSAG-RGN-FTP----NAEFNIAVDPEAAAKVF 177
Cdd:PTZ00313 119 ELLADLVMSSPEKVTICVTGPLSNVAWCIEKYGEEFTkKVEECVIMGGAVDvGGNvFLPgtdgSAEWNIYWDPPAAKTVL 198
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1248562618 178 R-SGLEIVMCGLDVTNQAMLAPEYLATLPALNQ------TGKMLhALFSHYRSGSMNTGLRMHDLCAIAWLVRPDLFTLQ 250
Cdd:PTZ00313 199 McPHIRKVLFSLDSTNSVPVTSEVVKKFGAQNKyllsqfVGSTW-AMCTHHELLRPGDGYYAWDVLTAAYVIERNLAELE 277
|
170 180
....*....|....*....|....
gi 1248562618 251 PCFVAVETQGEYTSGTTVVDIEGR 274
Cdd:PTZ00313 278 PVPLEVVVEKAKNEGRTRRAAEGA 301
|
|
| |
