|
Name |
Accession |
Description |
Interval |
E-value |
| rihB |
PRK09955 |
ribosylpyrimidine nucleosidase; |
1-313 |
0e+00 |
|
ribosylpyrimidine nucleosidase;
Pssm-ID: 182166 [Multi-domain] Cd Length: 313 Bit Score: 670.12 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446337600 1 MEKRKIILDCDPGHDDAIAMMMAAKHPAIDLLGITIVAGNQTLDKTLINGLNVCQKLEINVPVYAGMPQPIMRQQIVADN 80
Cdd:PRK09955 1 MEKRKIILDCDPGHDDAIAMMMAAKHPAIDLLGITIVAGNQTLDKTLINGLNVCQKLEINVPVYAGMPQPIMRQQIVADN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446337600 81 IHGETGLDGPVFEPLTRQAESTHAVKYIIDTLMASDGDITLVPVGPLSNIAVAMRMQPAILPKIREIVLMGGAYGTGNFT 160
Cdd:PRK09955 81 IHGETGLDGPVFEPLTRQAESTHAVKYIIDTLMASDGDITLVPVGPLSNIAVAMRMQPAILPKIREIVLMGGAYGTGNFT 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446337600 161 PSAEFNIFADPEAARVVFTSGVPLVMMGLDLTNQTVCTPDVIARMERAGGPAGELFSDIMNFTLKTQFENYGLAGGPVHD 240
Cdd:PRK09955 161 PSAEFNIFADPEAARVVFTSGVPLVMMGLDLTNQTVCTPDVIARMERAGGPAGELFSDIMNFTLKTQFENYGLAGGPVHD 240
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446337600 241 ATCIGYLINPDGIKTQEMYVEVDVNSGPCYGRTVCDELGVLGKPANTKVGITIDTDWFWGLVEECVRGYIKTH 313
Cdd:PRK09955 241 ATCIGYLINPDGIKTQEMYVEVDVNSGPCYGRTVCDELGVLGKPANTKVGITIDTDWFWGLVEECVRGYIKTH 313
|
|
| nuc_hydro_IU_UC_XIUA |
cd02651 |
nuc_hydro_IU_UC_XIUA: inosine-uridine preferring, ... |
5-306 |
5.14e-157 |
|
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: 440.44 E-value: 5.14e-157
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446337600 5 KIILDCDPGHDDAIAMMMAAKHPAIDLLGITIVAGNQTLDKTLINGLNVCQKLEI-NVPVYAGMPQPIMRQQIVADNIHG 83
Cdd:cd02651 1 PIIIDCDPGHDDAVAILLALFHPELDLLGITTVAGNVPLEKTTRNALKLLTLLGRtDVPVAAGAARPLVRPLITASDIHG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446337600 84 ETGLDGPVFEPLTRQAESTHAVKYIIDTLMASDGDITLVPVGPLSNIAVAMRMQPAILPKIREIVLMGGAYGTGNFTPSA 163
Cdd:cd02651 81 ESGLDGADLPPPPRRPEDIHAVDAIIDTLRASPEPITLVATGPLTNIALLLRKYPELAERIKEIVLMGGALGRGNITPAA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446337600 164 EFNIFADPEAARVVFTSGVPLVMMGLDLTNQTVCTPDVIARMERAGGPAGELFSDIMNFTLKTqFENYGLAGGPVHDATC 243
Cdd:cd02651 161 EFNIFVDPEAAKIVFNSGIPITMVPLDVTHKALATPEVIERIRALGNPVGKMLAELLDFFAET-YGSAFTEGPPLHDPCA 239
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446337600 244 IGYLINPDGIKTQEMYVEVDVNSGPCYGRTVCDELGVLGKPANTKVGITIDTDWFWGLVEECV 306
Cdd:cd02651 240 VAYLLDPELFTTKRANVDVETEGELTRGRTVVDLRGVTGRPANAQVAVDVDVEKFWDLLLEAL 302
|
|
| URH1 |
COG1957 |
Inosine-uridine nucleoside N-ribohydrolase [Nucleotide transport and metabolism]; ... |
2-309 |
4.48e-144 |
|
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: 408.00 E-value: 4.48e-144
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446337600 2 EKRKIILDCDPGHDDAIAMMMAAKHPAIDLLGITIVAGNQTLDKTLINGLNVCQKLEI-NVPVYAGMPQPIMRQQIVADN 80
Cdd:COG1957 1 MMRKVIIDTDPGIDDALALLLALASPEIDLLGITTVAGNVPLEQTTRNALKLLELAGRtDVPVAAGAARPLVRPLVTAEH 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446337600 81 IHGETGLDGPVFEPLTRQAESTHAVKYIIDTLMASDGDITLVPVGPLSNIAVAMRMQPAILPKIREIVLMGGAY-GTGNF 159
Cdd:COG1957 81 VHGEDGLGGVDLPEPTRPPEPEHAVDFIIETLRAAPGEVTLVALGPLTNLALALRKDPELAERIKRIVIMGGAFfVPGNV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446337600 160 TPSAEFNIFADPEAARVVFTSGVPLVMMGLDLTNQTVCTPDVIARMERAGGPAGELFSDIMNFTLKTQFENYGLAGGPVH 239
Cdd:COG1957 161 TPVAEFNIYVDPEAAKIVFASGIPITMVGLDVTHQALLTPEDLARLAALGTPLGRFLADLLDFYLDFYRERYGLDGCPLH 240
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446337600 240 DATCIGYLINPDGIKTQEMYVEVDVNSGPCYGRTVCDELGVLGKPANTKVGITIDTDWFWGLVEECVRGY 309
Cdd:COG1957 241 DPLAVAYLLDPELFTTRPAPVDVETDGELTRGQTVVDWRGVTGRPPNARVALDVDAERFLDLLLERLARL 310
|
|
| IU_nuc_hydro |
pfam01156 |
Inosine-uridine preferring nucleoside hydrolase; |
6-299 |
2.26e-103 |
|
Inosine-uridine preferring nucleoside hydrolase;
Pssm-ID: 460086 [Multi-domain] Cd Length: 253 Bit Score: 302.59 E-value: 2.26e-103
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446337600 6 IILDCDPGHDDAIAMMMAAKHPAIDLLGITIVAGNQTLDKTLINGLNVCQKLEIN-VPVYAGmpqpimrqqivadnihge 84
Cdd:pfam01156 1 VIIDTDPGIDDALALLLALASPEIELLGITTVAGNVSLEQTTRNALRLLELGGRDdIPVYAG------------------ 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446337600 85 tgldgpvfepltrqaesthavkyiiDTLMASdGDITLVPVGPLSNIAVAMRMQPAILPKIREIVLMGGAYGT-GNFTPSA 163
Cdd:pfam01156 63 -------------------------EAIREP-GEVTLVATGPLTNLALALRLDPELAKKIKELVIMGGAFGVrGNVTPAA 116
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446337600 164 EFNIFADPEAARVVFTSGVPLVMMGLDLTNQTVCTPDVIARMERAGGPAGELFSDIMNFTLKTQFENYGLAGGPVHDATC 243
Cdd:pfam01156 117 EFNIFVDPEAAKIVFTSGLPITMVPLDVTHQALLTPEDLERLAALGTPLGRFLADLLRFYAEFYRERFGIDGPPLHDPLA 196
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 446337600 244 IGYLINPDGIKTQEMYVEVDVNSGPCYGRTVCDELGVLGKPANTKVGITIDTDWFW 299
Cdd:pfam01156 197 VAVALDPELFTTRRLNVDVETTGGLTRGQTVVDDRGGWGKPPNVRVATDVDVDRFW 252
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| rihB |
PRK09955 |
ribosylpyrimidine nucleosidase; |
1-313 |
0e+00 |
|
ribosylpyrimidine nucleosidase;
Pssm-ID: 182166 [Multi-domain] Cd Length: 313 Bit Score: 670.12 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446337600 1 MEKRKIILDCDPGHDDAIAMMMAAKHPAIDLLGITIVAGNQTLDKTLINGLNVCQKLEINVPVYAGMPQPIMRQQIVADN 80
Cdd:PRK09955 1 MEKRKIILDCDPGHDDAIAMMMAAKHPAIDLLGITIVAGNQTLDKTLINGLNVCQKLEINVPVYAGMPQPIMRQQIVADN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446337600 81 IHGETGLDGPVFEPLTRQAESTHAVKYIIDTLMASDGDITLVPVGPLSNIAVAMRMQPAILPKIREIVLMGGAYGTGNFT 160
Cdd:PRK09955 81 IHGETGLDGPVFEPLTRQAESTHAVKYIIDTLMASDGDITLVPVGPLSNIAVAMRMQPAILPKIREIVLMGGAYGTGNFT 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446337600 161 PSAEFNIFADPEAARVVFTSGVPLVMMGLDLTNQTVCTPDVIARMERAGGPAGELFSDIMNFTLKTQFENYGLAGGPVHD 240
Cdd:PRK09955 161 PSAEFNIFADPEAARVVFTSGVPLVMMGLDLTNQTVCTPDVIARMERAGGPAGELFSDIMNFTLKTQFENYGLAGGPVHD 240
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446337600 241 ATCIGYLINPDGIKTQEMYVEVDVNSGPCYGRTVCDELGVLGKPANTKVGITIDTDWFWGLVEECVRGYIKTH 313
Cdd:PRK09955 241 ATCIGYLINPDGIKTQEMYVEVDVNSGPCYGRTVCDELGVLGKPANTKVGITIDTDWFWGLVEECVRGYIKTH 313
|
|
| nuc_hydro_IU_UC_XIUA |
cd02651 |
nuc_hydro_IU_UC_XIUA: inosine-uridine preferring, ... |
5-306 |
5.14e-157 |
|
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: 440.44 E-value: 5.14e-157
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446337600 5 KIILDCDPGHDDAIAMMMAAKHPAIDLLGITIVAGNQTLDKTLINGLNVCQKLEI-NVPVYAGMPQPIMRQQIVADNIHG 83
Cdd:cd02651 1 PIIIDCDPGHDDAVAILLALFHPELDLLGITTVAGNVPLEKTTRNALKLLTLLGRtDVPVAAGAARPLVRPLITASDIHG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446337600 84 ETGLDGPVFEPLTRQAESTHAVKYIIDTLMASDGDITLVPVGPLSNIAVAMRMQPAILPKIREIVLMGGAYGTGNFTPSA 163
Cdd:cd02651 81 ESGLDGADLPPPPRRPEDIHAVDAIIDTLRASPEPITLVATGPLTNIALLLRKYPELAERIKEIVLMGGALGRGNITPAA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446337600 164 EFNIFADPEAARVVFTSGVPLVMMGLDLTNQTVCTPDVIARMERAGGPAGELFSDIMNFTLKTqFENYGLAGGPVHDATC 243
Cdd:cd02651 161 EFNIFVDPEAAKIVFNSGIPITMVPLDVTHKALATPEVIERIRALGNPVGKMLAELLDFFAET-YGSAFTEGPPLHDPCA 239
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446337600 244 IGYLINPDGIKTQEMYVEVDVNSGPCYGRTVCDELGVLGKPANTKVGITIDTDWFWGLVEECV 306
Cdd:cd02651 240 VAYLLDPELFTTKRANVDVETEGELTRGRTVVDLRGVTGRPANAQVAVDVDVEKFWDLLLEAL 302
|
|
| URH1 |
COG1957 |
Inosine-uridine nucleoside N-ribohydrolase [Nucleotide transport and metabolism]; ... |
2-309 |
4.48e-144 |
|
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: 408.00 E-value: 4.48e-144
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446337600 2 EKRKIILDCDPGHDDAIAMMMAAKHPAIDLLGITIVAGNQTLDKTLINGLNVCQKLEI-NVPVYAGMPQPIMRQQIVADN 80
Cdd:COG1957 1 MMRKVIIDTDPGIDDALALLLALASPEIDLLGITTVAGNVPLEQTTRNALKLLELAGRtDVPVAAGAARPLVRPLVTAEH 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446337600 81 IHGETGLDGPVFEPLTRQAESTHAVKYIIDTLMASDGDITLVPVGPLSNIAVAMRMQPAILPKIREIVLMGGAY-GTGNF 159
Cdd:COG1957 81 VHGEDGLGGVDLPEPTRPPEPEHAVDFIIETLRAAPGEVTLVALGPLTNLALALRKDPELAERIKRIVIMGGAFfVPGNV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446337600 160 TPSAEFNIFADPEAARVVFTSGVPLVMMGLDLTNQTVCTPDVIARMERAGGPAGELFSDIMNFTLKTQFENYGLAGGPVH 239
Cdd:COG1957 161 TPVAEFNIYVDPEAAKIVFASGIPITMVGLDVTHQALLTPEDLARLAALGTPLGRFLADLLDFYLDFYRERYGLDGCPLH 240
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446337600 240 DATCIGYLINPDGIKTQEMYVEVDVNSGPCYGRTVCDELGVLGKPANTKVGITIDTDWFWGLVEECVRGY 309
Cdd:COG1957 241 DPLAVAYLLDPELFTTRPAPVDVETDGELTRGQTVVDWRGVTGRPPNARVALDVDAERFLDLLLERLARL 310
|
|
| IU_nuc_hydro |
pfam01156 |
Inosine-uridine preferring nucleoside hydrolase; |
6-299 |
2.26e-103 |
|
Inosine-uridine preferring nucleoside hydrolase;
Pssm-ID: 460086 [Multi-domain] Cd Length: 253 Bit Score: 302.59 E-value: 2.26e-103
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446337600 6 IILDCDPGHDDAIAMMMAAKHPAIDLLGITIVAGNQTLDKTLINGLNVCQKLEIN-VPVYAGmpqpimrqqivadnihge 84
Cdd:pfam01156 1 VIIDTDPGIDDALALLLALASPEIELLGITTVAGNVSLEQTTRNALRLLELGGRDdIPVYAG------------------ 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446337600 85 tgldgpvfepltrqaesthavkyiiDTLMASdGDITLVPVGPLSNIAVAMRMQPAILPKIREIVLMGGAYGT-GNFTPSA 163
Cdd:pfam01156 63 -------------------------EAIREP-GEVTLVATGPLTNLALALRLDPELAKKIKELVIMGGAFGVrGNVTPAA 116
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446337600 164 EFNIFADPEAARVVFTSGVPLVMMGLDLTNQTVCTPDVIARMERAGGPAGELFSDIMNFTLKTQFENYGLAGGPVHDATC 243
Cdd:pfam01156 117 EFNIFVDPEAAKIVFTSGLPITMVPLDVTHQALLTPEDLERLAALGTPLGRFLADLLRFYAEFYRERFGIDGPPLHDPLA 196
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 446337600 244 IGYLINPDGIKTQEMYVEVDVNSGPCYGRTVCDELGVLGKPANTKVGITIDTDWFW 299
Cdd:pfam01156 197 VAVALDPELFTTRRLNVDVETTGGLTRGQTVVDDRGGWGKPPNVRVATDVDVDRFW 252
|
|
| rihA |
PRK10443 |
ribonucleoside hydrolase 1; Provisional |
4-309 |
4.94e-100 |
|
ribonucleoside hydrolase 1; Provisional
Pssm-ID: 182465 [Multi-domain] Cd Length: 311 Bit Score: 296.58 E-value: 4.94e-100
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446337600 4 RKIILDCDPGHDDAIAMMMAAKHPAIDLLGITIVAGNQTLDKTLINGLNVCQKLE-INVPVYAGMPQPIMRQQIVADNIH 82
Cdd:PRK10443 3 LPIILDCDPGHDDAIALVLALASPELDVKAVTTSAGNQTPEKTLRNALRMLTLLNrTDIPVAGGAVKPLMRELIIADNVH 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446337600 83 GETGLDGPVFEPLTRQAESTHAVKYIIDTLMASDGDITLVPVGPLSNIAVAMRMQPAILPKIREIVLMGGAYGTGNFTPS 162
Cdd:PRK10443 83 GESGLDGPALPEPTFAPQNCTAVELMAKTLRESAEPVTLVSTGPQTNVALLLASHPELHSKIARIVIMGGAMGLGNWTPA 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446337600 163 AEFNIFADPEAARVVFTSGVPLVMMGLDLTNQTVCTPDVIARMERAGGPAGELFSDIMNFTLKT-QFENYGLAGGPVHDA 241
Cdd:PRK10443 163 AEFNIYVDPEAAEIVFQSGIPIVMAGLDVTHKAQIMDEDIERIRAIGNPVATIVAELLDFFMEYhKDEKWGFVGAPLHDP 242
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446337600 242 TCIGYLINPDGIKTQEMYVEVDVNSGPCYGRTVCDELGVLGKPANTKVGITIDTDWFWGLVEECVRGY 309
Cdd:PRK10443 243 CTIAWLLKPELFTTVERWVGVETQGEYTQGMTVVDYYQLTGNKPNATVLVDVDRQGFVDLLAERLKFY 310
|
|
| PRK10768 |
PRK10768 |
ribonucleoside hydrolase RihC; Provisional |
3-298 |
2.48e-97 |
|
ribonucleoside hydrolase RihC; Provisional
Pssm-ID: 182713 [Multi-domain] Cd Length: 304 Bit Score: 289.12 E-value: 2.48e-97
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446337600 3 KRKIILDCDPGHDDAIAMMMAAKHPAIDLLGITIVAGNQTLDKTLINGLNVCQKLEINVPVYAGMPQPIMRQQIVADNIH 82
Cdd:PRK10768 2 RLPIILDTDPGIDDAVAIAAALFAPELDLKLITTVAGNVSVEKTTRNALKLLHFFNSDVPVAQGAAKPLVRPLRDAASVH 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446337600 83 GETGLDGPVFEPLTRQAESTHAVKYIIDTLMASDGDITLVPVGPLSNIAVAMRMQPAILPKIREIVLMGGAYGTGNFTPS 162
Cdd:PRK10768 82 GESGMEGYDFPEHTRKPLSIPAVEAMRDALMNAPEPVTLVAIGPLTNIALLLSTYPEVKPYIKRIVLMGGSAGRGNVTPN 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446337600 163 AEFNIFADPEAARVVFTSGVPLVMMGLDLTNQTVCTPDVIARMeRAGGPAGELFSDIMNFTLKTQFENyglaGGPVHDAT 242
Cdd:PRK10768 162 AEFNIAVDPEAAAIVFRSGIPIVMCGLDVTNQALLTPDYLATL-PELNRTGKMLHALFSHYRSGSMQT----GLRMHDVC 236
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 446337600 243 CIGYLINPDGIKTQEMYVEVDVNSGPCYGRTVCDELGVLGKPANTKVGITIDTDWF 298
Cdd:PRK10768 237 AIAYLLRPELFTLKPCFVDVETQGEFTAGATVVDIDGRLGKPANAQVALDIDVDGF 292
|
|
| nuc_hydro_CaPnhB |
cd02650 |
NH_hydro_CaPnhB: A subgroup of nucleoside hydrolases similar to Corynebacterium ammoniagenes ... |
5-294 |
5.49e-91 |
|
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: 273.00 E-value: 5.49e-91
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446337600 5 KIILDCDPGHDDAIAMMMAAKHPAIDLLGITIVAGNQTLDKTLINGLNVCQKL-EINVPVYAGMPQPIMRQQI-VADNIH 82
Cdd:cd02650 1 KLILDTDPGIDDAMALAYALAHPDVDLIGVTTVYGNVTIETATRNALALLELFgRPDVPVAEGAAKPLTRPPFrIATFVH 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446337600 83 GETGLDGPVFEPLTRQAESTHAVKYIIDTLMASDGDITLVPVGPLSNIAVAMRMQPAILPKIREIVLMGGAYGT-GNFTP 161
Cdd:cd02650 81 GDNGLGDVELPAPPRQPEDESAADFLIELANEYPGELTLVAVGPLTNLALALARDPDFAKLVKQVVVMGGAFTVpGNVTP 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446337600 162 SAEFNIFADPEAARVVFTSGVPLVMMGLDLTNQTVCTPDVIARMERAGGPAGELFSDIMNFTLKTQFENYGLAGGPVHDA 241
Cdd:cd02650 161 AAEANIHGDPEAADIVFTAGADLTMVGLDVTTQTLLTREDLDELRDSGGKAGQFLADMLDYYIDFYQESPGLRGCALHDP 240
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 446337600 242 TCIGYLINPDGIKTQEMYVEVDVnSGPCYGRTVCDELGV----LGKPANTKVGITID 294
Cdd:cd02650 241 LAVAAAVDPSLFTTREGVVRVET-EGPTRGRTIGDRDGRrfwdSSPNATVAVDVDVD 296
|
|
| nuc_hydro |
cd00455 |
nuc_hydro: Nucleoside hydrolases. Nucleoside hydrolases cleave the N-glycosidic bond in ... |
6-302 |
1.78e-75 |
|
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: 233.38 E-value: 1.78e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446337600 6 IILDCDPGHDDAIAMMMAAKHPAIDLLGITIVAGNQTLDKTLIN-GLNVCQKLEINVPVYAGMPQPIMRQQIVADNIHGE 84
Cdd:cd00455 1 VILDTDPGIDDAFALMYALLHPEIELVGIVATYGNVTLEQATQNaAYLLELLGRLDIPVYAGATRPLTGEIPAAYPEIHG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446337600 85 TGLDGPVFEPLTRQAEStHAVKYIIDTLMASDGDITLVPVGPLSNIAVAMRMQPAILPKIREIVLMGGAYGT-GNFTPSA 163
Cdd:cd00455 81 EGGLGLPIPPIIEADDP-EAVQLLIDLIRKYPDEITIVALGPLTNLAMAFILDPDIKDRVKEIVIMGGAFLVpGNVTPVA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446337600 164 EFNIFADPEAARVVFTSGVPLVMMGLDLTNQTVCTPDVIARMERAGGPAGELFSDIMNFtlktQFENY---GLAGGPVHD 240
Cdd:cd00455 160 EANFYGDPEAANIVFNSAKNLTIVPLDVTNQAVLTPPMVERIFEQGTSIGLLIKPMIDY----YYKAYqkpGIEGSPIHD 235
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446337600 241 ATCIGYLINPDGIKTQEMYVEVDVNsGPCYGRTVCDELGVLGKPaNTKVGITIDTDWFWGLV 302
Cdd:cd00455 236 PLAVAYLLNPSMFDYSKVPVDVDTD-GLTRGQTIADFRENPGNG-VTRVAVNLDYPDFIELI 295
|
|
| nuc_hydro_CeIAG |
cd02649 |
nuc_hydro_CeIAG: Nucleoside hydrolases similar to the inosine-adenosine-guanosine-preferring ... |
4-303 |
1.12e-69 |
|
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: 218.67 E-value: 1.12e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446337600 4 RKIILDCDPGHDDAIAMMMAAKHPAIDLLGITIVAGNQTLDKTLINGLNVCQKL-EINVPVYAGMPQPIMRQQIVADNIH 82
Cdd:cd02649 1 RKLIIDTDCGGDDAWALLMALASPNVEVLAITCVHGNTNVEQVVKNALRVLEACgRRDIPVYRGASKPLLGPGPTAAYFH 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446337600 83 GETGL--DGPVFEPLTRQAESTHAVKYIIDTLMASDGDITLVPVGPLSNIAVAMRMQPAILPKIREIVLMGGAY-GTGNF 159
Cdd:cd02649 81 GKDGFgdVGFPEPKDELELQKEHAVDAIIRLVREYPGEITLVALGPLTNLALAYRLDPSLPQKIKRLYIMGGNReGVGNT 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446337600 160 TPSAEFNIFADPEAARVVFTS-GVPLVMMGLDLTNQTVctpDVIARMERAGGPAGELFSDIMNFTLKTQFENYGLAGGPV 238
Cdd:cd02649 161 TPAAEFNFHVDPEAAHIVLNSfGCPITIVPWETTLLAF---PLDWEFEDKWANRLEKALFAESLNRREYAFASEGLGGDG 237
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446337600 239 H---DATCIGYLINPDGIKTQEMY-VEVDVNSGPCYGRTVCDELGVLGKPANTKVGITIDTDWFWGLVE 303
Cdd:cd02649 238 WvpcDALAVAAALDPSIITRRLTYaVDVELHGELTRGQMVVDWLGTLKKKPNARVITKIDREKFKELLY 306
|
|
| nuc_hydro_3 |
cd02653 |
NH_3: A subgroup of nucleoside hydrolases. This group contains eukaryotic and bacterial ... |
5-313 |
1.71e-66 |
|
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: 211.08 E-value: 1.71e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446337600 5 KIILDCDPGHDDAIAMMMAAKHPAIDLLGITIVAGNQTLDKTLINGLNVCQKL-EINVPVYAGMPQPIMRQQIVADNIHG 83
Cdd:cd02653 1 KVIIDCDPGIDDALALLYLLASPDLDVVGITTTAGNVPVEQVAANALGVLELLgRTDIPVYLGADKPLAGPLTTAQDTHG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446337600 84 ETGLDGPVFEPLTRQAESTHAVKYIIDTLMASDGDITLVpVGPLSNIAVAMRMQPAILPKIREIVLMGGAYGT-GNFTPS 162
Cdd:cd02653 81 PDGLGYAELPASTRTLSDESAAQAWVDLARAHPDLIGLA-TGPLTNLALALREEPELPRLLRRLVIMGGAFNSrGNTSPV 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446337600 163 AEFNIFADPEAARVVF----TSGVPLVMMGLDLTNQTVCTPDVIARMERAGGPAGELFSDIMNFTLKTQfENYGLAGGPV 238
Cdd:cd02653 160 AEWNYWVDPEAAKEVLaafgGHPVRPTICGLDVTRAVVLTPNLLERLARAKDSVGAFIEDALRFYFEFH-WAYGHGYGAV 238
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 446337600 239 -HDATCIGYLINPDGIKTQEMYVEVdVNSGPCYGRTVCDELGVLGKPANTKVGITIDTDWFWGLVEECVRGYIKTH 313
Cdd:cd02653 239 iHDPLAAAVALNPNLARGRPAYVDV-ECTGVLTGQTVVDWAGFWGKGANAEILTKVDSQDFMALFIERVLAIADTI 313
|
|
| PLN02717 |
PLN02717 |
uridine nucleosidase |
4-296 |
1.25e-60 |
|
uridine nucleosidase
Pssm-ID: 178319 [Multi-domain] Cd Length: 316 Bit Score: 195.98 E-value: 1.25e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446337600 4 RKIILDCDPGHDDAIAMMMAAKHPAIDLLGITIVAGNQTLDKTLINGLNVCQKL-EINVPVYAGMPQPIMR--QQIVADN 80
Cdd:PLN02717 1 KKLIIDTDPGIDDAMAILMALRSPEVEVIGLTTIFGNVTTKLATRNALHLLEMAgRPDVPVAEGSHEPLKGgtKPRIADF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446337600 81 IHGETGLDGPVFEPLTRQAESTHAVKYIIDTLMASDGDITLVPVGPLSNIAVAMRMQPAILPKIREIVLMGGAYGT-GNF 159
Cdd:PLN02717 81 VHGSDGLGNTNLPPPKGKKIEKSAAEFLVEKVSEYPGEVTVVALGPLTNLALAIKLDPSFAKKVGQIVVLGGAFFVnGNV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446337600 160 TPSAEFNIFADPEAARVVFTSGVPLVMMGLDLTNQTVCTPDVIARMERAGGPAGELFSDIMNFTLKTQFENYGLAGGPVH 239
Cdd:PLN02717 161 NPAAEANIFGDPEAADIVFTSGADITVVGINVTTQVVLTDADLEELRDSKGKYAQFLCDICKFYRDWHRKSYGIDGIYLH 240
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 446337600 240 DATCIGYLINPDGIKTQEMYVEVDVnSGPCYGRTVCD--------ELGVLGKPAnTKVGITIDTD 296
Cdd:PLN02717 241 DPTALLAAVRPSLFTYKEGVVRVET-EGICRGLTLFDnglkrwngENAWTGRPP-VKVAVTVDAP 303
|
|
| nuc_hydro_1 |
cd02648 |
NH_1: A subgroup of nucleoside hydrolases. This group contains fungal proteins similar to ... |
3-192 |
4.48e-35 |
|
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: 130.39 E-value: 4.48e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446337600 3 KRKIILDCDPGHDDAIAMMMA-AKHPAIDLLGITIVAGNQTLDKTLINGLNVCQKLEINV-------------------P 62
Cdd:cd02648 1 PHPIIIDTDPGVDDVLAILLAlSSPEEVDVALISLTFGNTTLDHALRNVLRLFHVLERERawratpgvryrafsadaekP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446337600 63 VYA-GMPQPIMRQQIVADNIHGETGLDG-----PVFEPLTRQAESTH---------AVKYIIDTLMAS-DGDITLVPVGP 126
Cdd:cd02648 81 IVAsGSDQPLEGERLTASYFHGRDGLSGvhwlhPDFTPVETWIPEIVapltpsdkpAYDVILDILREEpDHTVTIAALGP 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 446337600 127 LSNIAVAMRMQPAILPKIREIVLMGGAYGT-GNFTPSAEFNIFADPEAARVVFTSG----------VPLVMMGLDLT 192
Cdd:cd02648 161 LTNLAAAARKDPETFAKVGEVVVMGGAIDVpGNTSPVAEFNCFADPYAAAVVIDEPpstapearrkLPLQVFPLDIT 237
|
|
| nuc_hydro_CjNH |
cd02654 |
nuc_hydro_CjNH. Nucleoside hydrolases similar to Campylobacter jejuni nucleoside hydrolase. ... |
5-298 |
5.51e-33 |
|
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: 123.82 E-value: 5.51e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446337600 5 KIILDCD----PGHDDAIAMMMAAKHPAIDLLGITIVAGNQTLDKTLingLNVCQKLEI----NVPVYAGMPQPIMRQ-- 74
Cdd:cd02654 1 KVILDNDiamgRDTDDGLALALLLWSPEVELLGLSAVSGNCWLSAVT---YNVLRMLELagadAIPVYAGANTPLGRTnr 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446337600 75 ----------QIVADNIHGETGLDGPVFEPLTRQAESThAVKYIIDTLMASDGDITLVPVGPLSNIAVAMRMQPAILPKI 144
Cdd:cd02654 78 afhaweslygAYLWQGAWSPEYSDMYTNASIIRNASIP-AALFMIEMVRKHPHEVSIVAAGPLTNLALALRIDPDFAPLA 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446337600 145 REIVLMGGA------YGTGNFTpsAEFNIFADPEAARVVFTSGVPLVMMGLDLTNQTVCTPDVIARMERAGGPAGELFSD 218
Cdd:cd02654 157 KELVIMGGYlddigeFVNRHYA--SDFNLIMDPEAASIVLTAPWKSITIPGNVTNRTCLTPEQIKADDPLRDFIRETLDL 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446337600 219 IMNFTLKTQfenYGLAGGPVHDATCIGYLINPDgIKTQEMYVEVDVN---SGPCYGRTVCDELGVLG-KPANTKVGITID 294
Cdd:cd02654 235 PIDYAKEFV---GTGDGLPMWDELASAVALDPE-LATSSETFYIDVQtdsDGGGQLIWPEDLLLAKGlRPYHVKVITAVD 310
|
....
gi 446337600 295 TDWF 298
Cdd:cd02654 311 VAAF 314
|
|
| nuc_hydro_TvIAG |
cd02647 |
nuc_hydro_ TvIAG: Nucleoside hydrolases similar to the Inosine-adenosine-guanosine-preferring ... |
6-194 |
1.20e-29 |
|
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: 114.82 E-value: 1.20e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446337600 6 IILDCDPGHDDAIAMMMAAKHPAIDLLGITIVAGNQtlDKTLINGLNVCQKL------EINVPVYAG-------MPQPIM 72
Cdd:cd02647 3 VIFDHDGNVDDLVALLLLLKNEKVDLKGIGVSGIDA--DCYVEPAVSVTRKLidrlgqRDAIPVGKGgsravnpFPRSWR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446337600 73 RQqivADNIHGETGLDGPVFEPLTRQAESThAVKYIIDTLMASDGDITLVPVGPLSNIAVAMRMQPAILPKIREIVLMGG 152
Cdd:cd02647 81 RD---AAFSVDHLPILNERYTVETPLAEET-AQLVLIEKIKASLEPVTLLVTGPLTNLARALDSDPDISSNIEEVYIMGG 156
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 446337600 153 AYGT-GN-FTPS----AEFNIFADPEAARVVFTSGVPLVMMGLDLTNQ 194
Cdd:cd02647 157 GVDApGNvFTPPsngtAEFNIFWDPLAAKTVFDSGLKITLVPLDATNT 204
|
|
| nuc_hydro_2 |
cd02652 |
NH_2: A subgroup of nucleoside hydrolases. This group contains eukaryotic and bacterial ... |
6-280 |
1.94e-14 |
|
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: 72.15 E-value: 1.94e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446337600 6 IILDCDPGHD--DAIAMMMAAKHPAIDLLGITIVAGNQTLD--KTLINGLNvcqkLEINVPV---YAGMPQPIMRqqiva 78
Cdd:cd02652 1 LILDTDIGGDpdDALALALAHALQKCDLLAVTITLADASARraIDAVNRFY----GRGDIPIgadYHGWPEDAKD----- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446337600 79 dniHGETGLDGPVFEP-LTRQAESTHAVKYIIDTLM-ASDGDITLVPVGPLSNIA------VAMRMQPAIL-PKIREIVL 149
Cdd:cd02652 72 ---HAKFLLEGDRLHHdLESAEDALDAVKALRRLLAsAEDASVTIVSIGPLTNLAalldadADPLTGPELVrQKVKRLVV 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446337600 150 MGGAYG-TGNFTPSAEFNIFADPEAARVVFTSGvplvmmgldltnQTVCTPDVIAR-----MERAGGPAGElfsDIMNFT 223
Cdd:cd02652 149 MGGAFYdPDGNVQHREYNFVTDPKAAQRVAGRA------------QHLGIPVRIVWsgyelGEAVSYPHVL---VIAHPF 213
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 446337600 224 LKTQFENYGLAGG--PVHDATCIGYLINPDGiktqeMYVEVdVNSGPCYGRTVCDELGV 280
Cdd:cd02652 214 NTPVFAAYWPRSHrrPLWDPLTLLAAVRGGG-----MLFDL-REVQLGPGRVEVDSSGV 266
|
|
| PTZ00313 |
PTZ00313 |
inosine-adenosine-guanosine-nucleoside hydrolase; Provisional |
4-273 |
3.96e-12 |
|
inosine-adenosine-guanosine-nucleoside hydrolase; Provisional
Pssm-ID: 140334 [Multi-domain] Cd Length: 326 Bit Score: 66.04 E-value: 3.96e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446337600 4 RKIILDCDPGHDDAIAMMMAAKHP-AIDLLGITIVAGNQTLDktliNGLNVCQKL------EINVPVY--------AGMP 68
Cdd:PTZ00313 3 KPVILDHDGNHDDLVALALLLGNPeKVKVIGCICTDADCFVD----DAFNVTGKLmcmmhaREATPLFpigkssfkGVNP 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446337600 69 QPiMRQQIVADNIHGETGLDGP----VFEPLTRQAESTHAVKYIIDTLMASDGDITLVPVGPLSNIAVAM-RMQPAILPK 143
Cdd:PTZ00313 79 FP-SEWRWSAKNMDDLPCLNIPehvaIWEKLKPENEALVGEELLADLVMSSPEKVTICVTGPLSNVAWCIeKYGEEFTKK 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446337600 144 IREIVLMGGAYGTGN--FTP----SAEFNIFADPEAARVVFT-SGVPLVMMGLDLTNQTVCTPDVIARMeraGGPAGELF 216
Cdd:PTZ00313 158 VEECVIMGGAVDVGGnvFLPgtdgSAEWNIYWDPPAAKTVLMcPHIRKVLFSLDSTNSVPVTSEVVKKF---GAQNKYLL 234
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 446337600 217 SDIMNFT--LKTQFENYGLAGG-PVHDATCIGYLINPDGIKTQEMYVEVDVNSGPCYGRT 273
Cdd:PTZ00313 235 SQFVGSTwaMCTHHELLRPGDGyYAWDVLTAAYVIERNLAELEPVPLEVVVEKAKNEGRT 294
|
|
| |
