|
Name |
Accession |
Description |
Interval |
E-value |
| nuc_hydro_TvIAG |
cd02647 |
nuc_hydro_ TvIAG: Nucleoside hydrolases similar to the Inosine-adenosine-guanosine-preferring ... |
46-396 |
4.16e-82 |
|
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: 266.98 E-value: 4.16e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239586 46 FAILYLLKLnkSEFDLVGITLSAnAWTNAGH--AVNQVYDLLHMMD-RDDIPVGVGGEGGIsddgtihsdvgGYFPIIEQ 122
Cdd:cd02647 15 VALLLLLKN--EKVDLKGIGVSG-IDADCYVepAVSVTRKLIDRLGqRDAIPVGKGGSRAV-----------NPFPRSWR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239586 123 GMTTtgecryrqaipkglgglldidsnygFRKQFLPQGNRRY---TPLQQPTAQKVIVDKISEG--PTTVILLGSHTNFA 197
Cdd:cd02647 81 RDAA-------------------------FSVDHLPILNERYtveTPLAEETAQLVLIEKIKASlePVTLLVTGPLTNLA 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239586 198 LFLMSNPHLKHNIQHIYIMGGGVrsqnptgccpanstvaecqprqcGNRGNLFTdYTSNPYSEFNIFADPFAAYQVFHSG 277
Cdd:cd02647 136 RALDSDPDISSNIEEVYIMGGGV-----------------------DAPGNVFT-PPSNGTAEFNIFWDPLAAKTVFDSG 191
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239586 278 VPVTLVPLDATNTIPINQKFFETFENNYQ-----RTYEAQYVFLSLKIArdtwfddEFYKSYFMWDSFTAGVAVSiMRNS 352
Cdd:cd02647 192 LKITLVPLDATNTVPLTREFLETDRQRFAaqrlpASDLAGQGYALVKPL-------EFNSTYYMWDVLTTLVLGA-KEVD 263
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|...
gi 15239586 353 ANKNNKNGENDFAEM-EYMNI--------TVVTSNKPYgrsdGSNPFFDNRRT 396
Cdd:cd02647 264 NTKESLILEVDTDGLsAGQTVtspngrplTLVTSNNSY----GSNRFFDDYLE 312
|
|
| nuc_hydro_TvIAG |
cd02647 |
nuc_hydro_ TvIAG: Nucleoside hydrolases similar to the Inosine-adenosine-guanosine-preferring ... |
509-867 |
4.96e-79 |
|
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: 258.50 E-value: 4.96e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239586 509 KPVVFDMDMSAGDFLSLFYLLKVPvdKIDLKAIIVSPtgwanaatidVVYDLLHmmgRDDIPVGLGDMLALNQSDpifpp 588
Cdd:cd02647 1 KNVIFDHDGNVDDLVALLLLLKNE--KVDLKGIGVSG----------IDADCYV---EPAVSVTRKLIDRLGQRD----- 60
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239586 589 vggckyvkAIPRGCGGFLDSdtlyglaRDLPRSPRRYTAeNSVTHGaPRDTDRPELRQPLAIEVWQNL--TKSGNGVSKI 666
Cdd:cd02647 61 --------AIPVGKGGSRAV-------NPFPRSWRRDAA-FSVDHL-PILNERYTVETPLAEETAQLVliEKIKASLEPV 123
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239586 667 TVLTNGPLTNLAKIISSDKKSSSLIKEVYIVGGHINreksDKGNIFTIPSNAYAEFNMFLDPLAAKTVLESALNITLVPL 746
Cdd:cd02647 124 TLLVTGPLTNLARALDSDPDISSNIEEVYIMGGGVD----APGNVFTPPSNGTAEFNIFWDPLAAKTVFDSGLKITLVPL 199
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239586 747 ATQHKLSSFQTMLdrlysstKTPEARFVKRLLVRLQALHQKHRR---------YTHIDMFLGEVLGAvllggddaslkpk 817
Cdd:cd02647 200 DATNTVPLTREFL-------ETDRQRFAAQRLPASDLAGQGYALvkplefnstYYMWDVLTTLVLGA------------- 259
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*....
gi 15239586 818 mraehiKVIAEGDESRDGKILIDKL-RGKQIKI-----LERVDLISISES---FASRLD 867
Cdd:cd02647 260 ------KEVDNTKESLILEVDTDGLsAGQTVTSpngrpLTLVTSNNSYGSnrfFDDYLE 312
|
|
| URH1 |
COG1957 |
Inosine-uridine nucleoside N-ribohydrolase [Nucleotide transport and metabolism]; ... |
46-384 |
1.82e-34 |
|
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: 134.13 E-value: 1.82e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239586 46 FAILYLLKLnkSEFDLVGITLSA-NawTNAGHAVNQVYDLLHMMDRDDIPVGVGGEGgisddgtihsdvggyfPIIEQGM 124
Cdd:COG1957 17 LALLLALAS--PEIDLLGITTVAgN--VPLEQTTRNALKLLELAGRTDVPVAAGAAR----------------PLVRPLV 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239586 125 TTT---GECryrqaipkGLGGLldidsnygfrkqFLPQGNRrytPLQQPTAQKVIVDKI--SEGPTTVILLGSHTNFALF 199
Cdd:COG1957 77 TAEhvhGED--------GLGGV------------DLPEPTR---PPEPEHAVDFIIETLraAPGEVTLVALGPLTNLALA 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239586 200 LMSNPHLKHNIQHIYIMGGGVRSqnptgccpanstvaecqprqcgnRGNLftdytsNPYSEFNIFADPFAAYQVFHSGVP 279
Cdd:COG1957 134 LRKDPELAERIKRIVIMGGAFFV-----------------------PGNV------TPVAEFNIYVDPEAAKIVFASGIP 184
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239586 280 VTLVPLDATNTIPINQKFFETFENnyQRTYEAQYVFLSLKIARDTWFDDEFYKSYFMWDSFTAGVAVsimrnsanknnkn 359
Cdd:COG1957 185 ITMVGLDVTHQALLTPEDLARLAA--LGTPLGRFLADLLDFYLDFYRERYGLDGCPLHDPLAVAYLL------------- 249
|
330 340
....*....|....*....|....*.
gi 15239586 360 gENDFAEMEYMNITVVTSNKP-YGRS 384
Cdd:COG1957 250 -DPELFTTRPAPVDVETDGELtRGQT 274
|
|
| IU_nuc_hydro |
pfam01156 |
Inosine-uridine preferring nucleoside hydrolase; |
46-384 |
1.24e-29 |
|
Inosine-uridine preferring nucleoside hydrolase;
Pssm-ID: 460086 [Multi-domain] Cd Length: 253 Bit Score: 118.46 E-value: 1.24e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239586 46 FAILYLLKLNksEFDLVGITLSAnAWTNAGHAVNQVYDLLHMMDRDDIPVGVGgeggisddgtihsdvggyfpiieqgmt 125
Cdd:pfam01156 13 LALLLALASP--EIELLGITTVA-GNVSLEQTTRNALRLLELGGRDDIPVYAG--------------------------- 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239586 126 ttgecryrqaipkglgglldidsnygfrkqflpqgnrrytplqqptaqkvivDKISEGPT-TVILLGSHTNFALFLMSNP 204
Cdd:pfam01156 63 ----------------------------------------------------EAIREPGEvTLVATGPLTNLALALRLDP 90
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239586 205 HLKHNIQHIYIMGGGVrsqnptgccpanstvaecqprqcGNRGNlftdytSNPYSEFNIFADPFAAYQVFHSGVPVTLVP 284
Cdd:pfam01156 91 ELAKKIKELVIMGGAF-----------------------GVRGN------VTPAAEFNIFVDPEAAKIVFTSGLPITMVP 141
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239586 285 LDATNTIPINQKFFEtfennyqrTYEAQYVFLSLKIARDTWFDDEFYKSYF------MWDSFTAGVAVsimrnsanknnk 358
Cdd:pfam01156 142 LDVTHQALLTPEDLE--------RLAALGTPLGRFLADLLRFYAEFYRERFgidgppLHDPLAVAVAL------------ 201
|
330 340
....*....|....*....|....*..
gi 15239586 359 ngENDFAEMEYMNITVVTSNKP-YGRS 384
Cdd:pfam01156 202 --DPELFTTRRLNVDVETTGGLtRGQT 226
|
|
| IU_nuc_hydro |
pfam01156 |
Inosine-uridine preferring nucleoside hydrolase; |
511-854 |
2.58e-24 |
|
Inosine-uridine preferring nucleoside hydrolase;
Pssm-ID: 460086 [Multi-domain] Cd Length: 253 Bit Score: 103.06 E-value: 2.58e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239586 511 VVFDMDMSAGDFLSLFYLLKVPvdKIDLKAIIVSPtGWANAA-TIDVVYDLLHMMGRDDIPVGLGDMLalnqsdpifppv 589
Cdd:pfam01156 1 VIIDTDPGIDDALALLLALASP--EIELLGITTVA-GNVSLEqTTRNALRLLELGGRDDIPVYAGEAI------------ 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239586 590 ggckyvkaiprgcggfldsdtlyglardlprsprrytaensvthgaprdtdrpelRQPlaievwqnltksgngvSKITVL 669
Cdd:pfam01156 66 -------------------------------------------------------REP----------------GEVTLV 74
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239586 670 TNGPLTNLAKIISSDKKSSSLIKEVYIVGGHINReksdKGNIftipsNAYAEFNMFLDPLAAKTVLESALNITLVPLATQ 749
Cdd:pfam01156 75 ATGPLTNLALALRLDPELAKKIKELVIMGGAFGV----RGNV-----TPAAEFNIFVDPEAAKIVFTSGLPITMVPLDVT 145
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239586 750 HKLSSFQTMLDRlYSSTKTPEARFVKRLLVRLQALHQKHRRYTHidMFLGEVLG-AVLLggdDASLKPKMRAeHIKVIAE 828
Cdd:pfam01156 146 HQALLTPEDLER-LAALGTPLGRFLADLLRFYAEFYRERFGIDG--PPLHDPLAvAVAL---DPELFTTRRL-NVDVETT 218
|
330 340 350
....*....|....*....|....*....|
gi 15239586 829 GDESRdGKILID----KLRGKQIKILERVD 854
Cdd:pfam01156 219 GGLTR-GQTVVDdrggWGKPPNVRVATDVD 247
|
|
| URH1 |
COG1957 |
Inosine-uridine nucleoside N-ribohydrolase [Nucleotide transport and metabolism]; ... |
509-854 |
5.06e-23 |
|
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: 100.61 E-value: 5.06e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239586 509 KPVVFDMDMSAGDFLSLFYLLKVPvdKIDLKAIIVSP------TGWANAATIdvvydlLHMMGRDDIPVGLGDmlalnqS 582
Cdd:COG1957 3 RKVIIDTDPGIDDALALLLALASP--EIDLLGITTVAgnvpleQTTRNALKL------LELAGRTDVPVAAGA------A 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239586 583 DPIFPPVGGCKYVkaipRGCGGFLDSDtlyglardLPRSPRRYTAENsvthgaprdtdrpelrqplAIEVWQNLTKSGNG 662
Cdd:COG1957 69 RPLVRPLVTAEHV----HGEDGLGGVD--------LPEPTRPPEPEH-------------------AVDFIIETLRAAPG 117
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239586 663 vsKITVLTNGPLTNLAKIISSDKKSSSLIKEVYIVGGHINReksdKGNIftipsNAYAEFNMFLDPLAAKTVLESALNIT 742
Cdd:COG1957 118 --EVTLVALGPLTNLALALRKDPELAERIKRIVIMGGAFFV----PGNV-----TPVAEFNIYVDPEAAKIVFASGIPIT 186
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239586 743 LVPL-AT-QHKLSsfQTMLDRLySSTKTPEARFVKRLLVRLQALHqkHRRYTHIDMFLGEVLGAVLLggddasLKP---K 817
Cdd:COG1957 187 MVGLdVThQALLT--PEDLARL-AALGTPLGRFLADLLDFYLDFY--RERYGLDGCPLHDPLAVAYL------LDPelfT 255
|
330 340 350 360
....*....|....*....|....*....|....*....|.
gi 15239586 818 MRAEHIKVIAEGDESRdGKILIDKL----RGKQIKILERVD 854
Cdd:COG1957 256 TRPAPVDVETDGELTR-GQTVVDWRgvtgRPPNARVALDVD 295
|
|
| PRK10768 |
PRK10768 |
ribonucleoside hydrolase RihC; Provisional |
181-303 |
5.26e-19 |
|
ribonucleoside hydrolase RihC; Provisional
Pssm-ID: 182713 [Multi-domain] Cd Length: 304 Bit Score: 88.81 E-value: 5.26e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239586 181 SEGPTTVILLGSHTNFALFLMSNPHLKHNIQHIYIMGGGVrsqnptgccpanstvaecqprqcgNRGNLftdytsNPYSE 260
Cdd:PRK10768 114 APEPVTLVAIGPLTNIALLLSTYPEVKPYIKRIVLMGGSA------------------------GRGNV------TPNAE 163
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 15239586 261 FNIFADPFAAYQVFHSGVPVTLVPLDATNTIPINQKFFETFEN 303
Cdd:PRK10768 164 FNIAVDPEAAAIVFRSGIPIVMCGLDVTNQALLTPDYLATLPE 206
|
|
| rihA |
PRK10443 |
ribonucleoside hydrolase 1; Provisional |
509-751 |
5.20e-09 |
|
ribonucleoside hydrolase 1; Provisional
Pssm-ID: 182465 [Multi-domain] Cd Length: 311 Bit Score: 58.53 E-value: 5.20e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239586 509 KPVVFDMDMSAGDFLSLFYLLKVPvdKIDLKAIIVSPTGWANAATIDVVYDLLHMMGRDDIPVGLGdmlalnqsdpifpp 588
Cdd:PRK10443 3 LPIILDCDPGHDDAIALVLALASP--ELDVKAVTTSAGNQTPEKTLRNALRMLTLLNRTDIPVAGG-------------- 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239586 589 vggckyvKAIPrgcggfldsdtlygLARDLprsprrYTAENsvTHGAPrDTDRPELRQP-------LAIEVW-QNLTKSG 660
Cdd:PRK10443 67 -------AVKP--------------LMREL------IIADN--VHGES-GLDGPALPEPtfapqncTAVELMaKTLRESA 116
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239586 661 ngvSKITVLTNGPLTNLAKIISSDKKSSSLIKEVYIVGGHINreksdKGNifTIPSnayAEFNMFLDPLAAKTVLESALN 740
Cdd:PRK10443 117 ---EPVTLVSTGPQTNVALLLASHPELHSKIARIVIMGGAMG-----LGN--WTPA---AEFNIYVDPEAAEIVFQSGIP 183
|
250
....*....|.
gi 15239586 741 ITLVPLATQHK 751
Cdd:PRK10443 184 IVMAGLDVTHK 194
|
|
|
|
Name |
Accession |
Description |
Interval |
E-value |
| nuc_hydro_TvIAG |
cd02647 |
nuc_hydro_ TvIAG: Nucleoside hydrolases similar to the Inosine-adenosine-guanosine-preferring ... |
46-396 |
4.16e-82 |
|
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: 266.98 E-value: 4.16e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239586 46 FAILYLLKLnkSEFDLVGITLSAnAWTNAGH--AVNQVYDLLHMMD-RDDIPVGVGGEGGIsddgtihsdvgGYFPIIEQ 122
Cdd:cd02647 15 VALLLLLKN--EKVDLKGIGVSG-IDADCYVepAVSVTRKLIDRLGqRDAIPVGKGGSRAV-----------NPFPRSWR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239586 123 GMTTtgecryrqaipkglgglldidsnygFRKQFLPQGNRRY---TPLQQPTAQKVIVDKISEG--PTTVILLGSHTNFA 197
Cdd:cd02647 81 RDAA-------------------------FSVDHLPILNERYtveTPLAEETAQLVLIEKIKASlePVTLLVTGPLTNLA 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239586 198 LFLMSNPHLKHNIQHIYIMGGGVrsqnptgccpanstvaecqprqcGNRGNLFTdYTSNPYSEFNIFADPFAAYQVFHSG 277
Cdd:cd02647 136 RALDSDPDISSNIEEVYIMGGGV-----------------------DAPGNVFT-PPSNGTAEFNIFWDPLAAKTVFDSG 191
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239586 278 VPVTLVPLDATNTIPINQKFFETFENNYQ-----RTYEAQYVFLSLKIArdtwfddEFYKSYFMWDSFTAGVAVSiMRNS 352
Cdd:cd02647 192 LKITLVPLDATNTVPLTREFLETDRQRFAaqrlpASDLAGQGYALVKPL-------EFNSTYYMWDVLTTLVLGA-KEVD 263
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|...
gi 15239586 353 ANKNNKNGENDFAEM-EYMNI--------TVVTSNKPYgrsdGSNPFFDNRRT 396
Cdd:cd02647 264 NTKESLILEVDTDGLsAGQTVtspngrplTLVTSNNSY----GSNRFFDDYLE 312
|
|
| nuc_hydro_TvIAG |
cd02647 |
nuc_hydro_ TvIAG: Nucleoside hydrolases similar to the Inosine-adenosine-guanosine-preferring ... |
509-867 |
4.96e-79 |
|
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: 258.50 E-value: 4.96e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239586 509 KPVVFDMDMSAGDFLSLFYLLKVPvdKIDLKAIIVSPtgwanaatidVVYDLLHmmgRDDIPVGLGDMLALNQSDpifpp 588
Cdd:cd02647 1 KNVIFDHDGNVDDLVALLLLLKNE--KVDLKGIGVSG----------IDADCYV---EPAVSVTRKLIDRLGQRD----- 60
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239586 589 vggckyvkAIPRGCGGFLDSdtlyglaRDLPRSPRRYTAeNSVTHGaPRDTDRPELRQPLAIEVWQNL--TKSGNGVSKI 666
Cdd:cd02647 61 --------AIPVGKGGSRAV-------NPFPRSWRRDAA-FSVDHL-PILNERYTVETPLAEETAQLVliEKIKASLEPV 123
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239586 667 TVLTNGPLTNLAKIISSDKKSSSLIKEVYIVGGHINreksDKGNIFTIPSNAYAEFNMFLDPLAAKTVLESALNITLVPL 746
Cdd:cd02647 124 TLLVTGPLTNLARALDSDPDISSNIEEVYIMGGGVD----APGNVFTPPSNGTAEFNIFWDPLAAKTVFDSGLKITLVPL 199
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239586 747 ATQHKLSSFQTMLdrlysstKTPEARFVKRLLVRLQALHQKHRR---------YTHIDMFLGEVLGAvllggddaslkpk 817
Cdd:cd02647 200 DATNTVPLTREFL-------ETDRQRFAAQRLPASDLAGQGYALvkplefnstYYMWDVLTTLVLGA------------- 259
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*....
gi 15239586 818 mraehiKVIAEGDESRDGKILIDKL-RGKQIKI-----LERVDLISISES---FASRLD 867
Cdd:cd02647 260 ------KEVDNTKESLILEVDTDGLsAGQTVTSpngrpLTLVTSNNSYGSnrfFDDYLE 312
|
|
| URH1 |
COG1957 |
Inosine-uridine nucleoside N-ribohydrolase [Nucleotide transport and metabolism]; ... |
46-384 |
1.82e-34 |
|
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: 134.13 E-value: 1.82e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239586 46 FAILYLLKLnkSEFDLVGITLSA-NawTNAGHAVNQVYDLLHMMDRDDIPVGVGGEGgisddgtihsdvggyfPIIEQGM 124
Cdd:COG1957 17 LALLLALAS--PEIDLLGITTVAgN--VPLEQTTRNALKLLELAGRTDVPVAAGAAR----------------PLVRPLV 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239586 125 TTT---GECryrqaipkGLGGLldidsnygfrkqFLPQGNRrytPLQQPTAQKVIVDKI--SEGPTTVILLGSHTNFALF 199
Cdd:COG1957 77 TAEhvhGED--------GLGGV------------DLPEPTR---PPEPEHAVDFIIETLraAPGEVTLVALGPLTNLALA 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239586 200 LMSNPHLKHNIQHIYIMGGGVRSqnptgccpanstvaecqprqcgnRGNLftdytsNPYSEFNIFADPFAAYQVFHSGVP 279
Cdd:COG1957 134 LRKDPELAERIKRIVIMGGAFFV-----------------------PGNV------TPVAEFNIYVDPEAAKIVFASGIP 184
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239586 280 VTLVPLDATNTIPINQKFFETFENnyQRTYEAQYVFLSLKIARDTWFDDEFYKSYFMWDSFTAGVAVsimrnsanknnkn 359
Cdd:COG1957 185 ITMVGLDVTHQALLTPEDLARLAA--LGTPLGRFLADLLDFYLDFYRERYGLDGCPLHDPLAVAYLL------------- 249
|
330 340
....*....|....*....|....*.
gi 15239586 360 gENDFAEMEYMNITVVTSNKP-YGRS 384
Cdd:COG1957 250 -DPELFTTRPAPVDVETDGELtRGQT 274
|
|
| IU_nuc_hydro |
pfam01156 |
Inosine-uridine preferring nucleoside hydrolase; |
46-384 |
1.24e-29 |
|
Inosine-uridine preferring nucleoside hydrolase;
Pssm-ID: 460086 [Multi-domain] Cd Length: 253 Bit Score: 118.46 E-value: 1.24e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239586 46 FAILYLLKLNksEFDLVGITLSAnAWTNAGHAVNQVYDLLHMMDRDDIPVGVGgeggisddgtihsdvggyfpiieqgmt 125
Cdd:pfam01156 13 LALLLALASP--EIELLGITTVA-GNVSLEQTTRNALRLLELGGRDDIPVYAG--------------------------- 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239586 126 ttgecryrqaipkglgglldidsnygfrkqflpqgnrrytplqqptaqkvivDKISEGPT-TVILLGSHTNFALFLMSNP 204
Cdd:pfam01156 63 ----------------------------------------------------EAIREPGEvTLVATGPLTNLALALRLDP 90
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239586 205 HLKHNIQHIYIMGGGVrsqnptgccpanstvaecqprqcGNRGNlftdytSNPYSEFNIFADPFAAYQVFHSGVPVTLVP 284
Cdd:pfam01156 91 ELAKKIKELVIMGGAF-----------------------GVRGN------VTPAAEFNIFVDPEAAKIVFTSGLPITMVP 141
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239586 285 LDATNTIPINQKFFEtfennyqrTYEAQYVFLSLKIARDTWFDDEFYKSYF------MWDSFTAGVAVsimrnsanknnk 358
Cdd:pfam01156 142 LDVTHQALLTPEDLE--------RLAALGTPLGRFLADLLRFYAEFYRERFgidgppLHDPLAVAVAL------------ 201
|
330 340
....*....|....*....|....*..
gi 15239586 359 ngENDFAEMEYMNITVVTSNKP-YGRS 384
Cdd:pfam01156 202 --DPELFTTRRLNVDVETTGGLtRGQT 226
|
|
| nuc_hydro_IU_UC_XIUA |
cd02651 |
nuc_hydro_IU_UC_XIUA: inosine-uridine preferring, ... |
46-303 |
2.34e-25 |
|
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: 107.25 E-value: 2.34e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239586 46 FAILylLKLNKSEFDLVGITLSANawtNAGHA--VNQVYDLLHMMDRDDIPVGVGGEggisddgtihsdvggyFPIIEQG 123
Cdd:cd02651 14 VAIL--LALFHPELDLLGITTVAG---NVPLEktTRNALKLLTLLGRTDVPVAAGAA----------------RPLVRPL 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239586 124 MTTT---GEcryrqaipKGLGGlldIDsnygfrkqfLPQGNRRytpLQQPTAQKVIVDKI--SEGPTTVILLGSHTNFAL 198
Cdd:cd02651 73 ITASdihGE--------SGLDG---AD---------LPPPPRR---PEDIHAVDAIIDTLraSPEPITLVATGPLTNIAL 129
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239586 199 FLMSNPHLKHNIQHIYIMGGGVrsqnptgccpanstvaecqprqcgNRGNLftdytsNPYSEFNIFADPFAAYQVFHSGV 278
Cdd:cd02651 130 LLRKYPELAERIKEIVLMGGAL------------------------GRGNI------TPAAEFNIFVDPEAAKIVFNSGI 179
|
250 260
....*....|....*....|....*
gi 15239586 279 PVTLVPLDATNTIPINQKFFETFEN 303
Cdd:cd02651 180 PITMVPLDVTHKALATPEVIERIRA 204
|
|
| IU_nuc_hydro |
pfam01156 |
Inosine-uridine preferring nucleoside hydrolase; |
511-854 |
2.58e-24 |
|
Inosine-uridine preferring nucleoside hydrolase;
Pssm-ID: 460086 [Multi-domain] Cd Length: 253 Bit Score: 103.06 E-value: 2.58e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239586 511 VVFDMDMSAGDFLSLFYLLKVPvdKIDLKAIIVSPtGWANAA-TIDVVYDLLHMMGRDDIPVGLGDMLalnqsdpifppv 589
Cdd:pfam01156 1 VIIDTDPGIDDALALLLALASP--EIELLGITTVA-GNVSLEqTTRNALRLLELGGRDDIPVYAGEAI------------ 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239586 590 ggckyvkaiprgcggfldsdtlyglardlprsprrytaensvthgaprdtdrpelRQPlaievwqnltksgngvSKITVL 669
Cdd:pfam01156 66 -------------------------------------------------------REP----------------GEVTLV 74
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239586 670 TNGPLTNLAKIISSDKKSSSLIKEVYIVGGHINReksdKGNIftipsNAYAEFNMFLDPLAAKTVLESALNITLVPLATQ 749
Cdd:pfam01156 75 ATGPLTNLALALRLDPELAKKIKELVIMGGAFGV----RGNV-----TPAAEFNIFVDPEAAKIVFTSGLPITMVPLDVT 145
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239586 750 HKLSSFQTMLDRlYSSTKTPEARFVKRLLVRLQALHQKHRRYTHidMFLGEVLG-AVLLggdDASLKPKMRAeHIKVIAE 828
Cdd:pfam01156 146 HQALLTPEDLER-LAALGTPLGRFLADLLRFYAEFYRERFGIDG--PPLHDPLAvAVAL---DPELFTTRRL-NVDVETT 218
|
330 340 350
....*....|....*....|....*....|
gi 15239586 829 GDESRdGKILID----KLRGKQIKILERVD 854
Cdd:pfam01156 219 GGLTR-GQTVVDdrggWGKPPNVRVATDVD 247
|
|
| URH1 |
COG1957 |
Inosine-uridine nucleoside N-ribohydrolase [Nucleotide transport and metabolism]; ... |
509-854 |
5.06e-23 |
|
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: 100.61 E-value: 5.06e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239586 509 KPVVFDMDMSAGDFLSLFYLLKVPvdKIDLKAIIVSP------TGWANAATIdvvydlLHMMGRDDIPVGLGDmlalnqS 582
Cdd:COG1957 3 RKVIIDTDPGIDDALALLLALASP--EIDLLGITTVAgnvpleQTTRNALKL------LELAGRTDVPVAAGA------A 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239586 583 DPIFPPVGGCKYVkaipRGCGGFLDSDtlyglardLPRSPRRYTAENsvthgaprdtdrpelrqplAIEVWQNLTKSGNG 662
Cdd:COG1957 69 RPLVRPLVTAEHV----HGEDGLGGVD--------LPEPTRPPEPEH-------------------AVDFIIETLRAAPG 117
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239586 663 vsKITVLTNGPLTNLAKIISSDKKSSSLIKEVYIVGGHINReksdKGNIftipsNAYAEFNMFLDPLAAKTVLESALNIT 742
Cdd:COG1957 118 --EVTLVALGPLTNLALALRKDPELAERIKRIVIMGGAFFV----PGNV-----TPVAEFNIYVDPEAAKIVFASGIPIT 186
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239586 743 LVPL-AT-QHKLSsfQTMLDRLySSTKTPEARFVKRLLVRLQALHqkHRRYTHIDMFLGEVLGAVLLggddasLKP---K 817
Cdd:COG1957 187 MVGLdVThQALLT--PEDLARL-AALGTPLGRFLADLLDFYLDFY--RERYGLDGCPLHDPLAVAYL------LDPelfT 255
|
330 340 350 360
....*....|....*....|....*....|....*....|.
gi 15239586 818 MRAEHIKVIAEGDESRdGKILIDKL----RGKQIKILERVD 854
Cdd:COG1957 256 TRPAPVDVETDGELTR-GQTVVDWRgvtgRPPNARVALDVD 295
|
|
| nuc_hydro |
cd00455 |
nuc_hydro: Nucleoside hydrolases. Nucleoside hydrolases cleave the N-glycosidic bond in ... |
46-398 |
1.01e-21 |
|
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: 96.63 E-value: 1.01e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239586 46 FAILYLLKLNksEFDLVGITLSA-NawTNAGHAVNQVYDLLHMMDRDDIPVGVGGEggisddgtihsdvggyFPIIEqgm 124
Cdd:cd00455 13 FALMYALLHP--EIELVGIVATYgN--VTLEQATQNAAYLLELLGRLDIPVYAGAT----------------RPLTG--- 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239586 125 tttGECRYRQAIPKGLGGLLDIDSNYGFRKqflpqgnrrytplqqPTAQKVIVDKISEGP--TTVILLGSHTNFALFLMS 202
Cdd:cd00455 70 ---EIPAAYPEIHGEGGLGLPIPPIIEADD---------------PEAVQLLIDLIRKYPdeITIVALGPLTNLAMAFIL 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239586 203 NPHLKHNIQHIYIMGGGVrsqnptgccpanstvaecqprqcGNRGNLFtdytsnPYSEFNIFADPFAAYQVFHSGVPVTL 282
Cdd:cd00455 132 DPDIKDRVKEIVIMGGAF-----------------------LVPGNVT------PVAEANFYGDPEAANIVFNSAKNLTI 182
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239586 283 VPLDATNTIPInqkffetfENNYQRTYEAQYVFLSLKIARdtwFDDEFYKSYF--------MWDSFTAGVAVsimrnsan 354
Cdd:cd00455 183 VPLDVTNQAVL--------TPPMVERIFEQGTSIGLLIKP---MIDYYYKAYQkpgiegspIHDPLAVAYLL-------- 243
|
330 340 350 360
....*....|....*....|....*....|....*....|....
gi 15239586 355 knnkngENDFAEMEYMNITVVTSNKPYGRSdgsnpFFDNRRTPK 398
Cdd:cd00455 244 ------NPSMFDYSKVPVDVDTDGLTRGQT-----IADFRENPG 276
|
|
| PRK10768 |
PRK10768 |
ribonucleoside hydrolase RihC; Provisional |
181-303 |
5.26e-19 |
|
ribonucleoside hydrolase RihC; Provisional
Pssm-ID: 182713 [Multi-domain] Cd Length: 304 Bit Score: 88.81 E-value: 5.26e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239586 181 SEGPTTVILLGSHTNFALFLMSNPHLKHNIQHIYIMGGGVrsqnptgccpanstvaecqprqcgNRGNLftdytsNPYSE 260
Cdd:PRK10768 114 APEPVTLVAIGPLTNIALLLSTYPEVKPYIKRIVLMGGSA------------------------GRGNV------TPNAE 163
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 15239586 261 FNIFADPFAAYQVFHSGVPVTLVPLDATNTIPINQKFFETFEN 303
Cdd:PRK10768 164 FNIAVDPEAAAIVFRSGIPIVMCGLDVTNQALLTPDYLATLPE 206
|
|
| rihA |
PRK10443 |
ribonucleoside hydrolase 1; Provisional |
47-288 |
1.52e-18 |
|
ribonucleoside hydrolase 1; Provisional
Pssm-ID: 182465 [Multi-domain] Cd Length: 311 Bit Score: 87.42 E-value: 1.52e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239586 47 AILYLLKLNKSEFDLVGITLSANAWTnAGHAVNQVYDLLHMMDRDDIPVGVGGEGGISDDGTIHSDVGGyfpiiEQGMTT 126
Cdd:PRK10443 16 AIALVLALASPELDVKAVTTSAGNQT-PEKTLRNALRMLTLLNRTDIPVAGGAVKPLMRELIIADNVHG-----ESGLDG 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239586 127 TgecryrqAIPKglgglldidsnygfrKQFLPQGNrrytplqqpTAQKVIVDKISEGPTTVILL--GSHTNFALFLMSNP 204
Cdd:PRK10443 90 P-------ALPE---------------PTFAPQNC---------TAVELMAKTLRESAEPVTLVstGPQTNVALLLASHP 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239586 205 HLKHNIQHIYIMGGGVRSQNPTgccpanstvaecqprqcgnrgnlftdytsnPYSEFNIFADPFAAYQVFHSGVPVTLVP 284
Cdd:PRK10443 139 ELHSKIARIVIMGGAMGLGNWT------------------------------PAAEFNIYVDPEAAEIVFQSGIPIVMAG 188
|
....
gi 15239586 285 LDAT 288
Cdd:PRK10443 189 LDVT 192
|
|
| nuc_hydro |
cd00455 |
nuc_hydro: Nucleoside hydrolases. Nucleoside hydrolases cleave the N-glycosidic bond in ... |
511-750 |
9.83e-17 |
|
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: 81.61 E-value: 9.83e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239586 511 VVFDMDMSAGDFLSLFYLLKVPvdKIDLKAIIvspTGWANA----ATIDVVYdLLHMMGRDDIPVGLGDMLALNQSDPIF 586
Cdd:cd00455 1 VILDTDPGIDDAFALMYALLHP--EIELVGIV---ATYGNVtleqATQNAAY-LLELLGRLDIPVYAGATRPLTGEIPAA 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239586 587 PPVGGCKYVKAIPrgcggfldsdtlyglardlprSPRRYTAENsvthgaprdtdrpelrqPLAIEVWQNLTKSGNGvsKI 666
Cdd:cd00455 75 YPEIHGEGGLGLP---------------------IPPIIEADD-----------------PEAVQLLIDLIRKYPD--EI 114
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239586 667 TVLTNGPLTNLAKIISSDKKSSSLIKEVYIVGGHinreksdkgniFTIPSNAY--AEFNMFLDPLAAKTVLESALNITLV 744
Cdd:cd00455 115 TIVALGPLTNLAMAFILDPDIKDRVKEIVIMGGA-----------FLVPGNVTpvAEANFYGDPEAANIVFNSAKNLTIV 183
|
....*..
gi 15239586 745 PL-ATQH 750
Cdd:cd00455 184 PLdVTNQ 190
|
|
| nuc_hydro_CeIAG |
cd02649 |
nuc_hydro_CeIAG: Nucleoside hydrolases similar to the inosine-adenosine-guanosine-preferring ... |
509-745 |
1.49e-13 |
|
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: 72.29 E-value: 1.49e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239586 509 KPVVFDMDMSAGDFLSLFYLLKVPvdKIDLKAI-IVsptgWANAATIDVVYD---LLHMMGRDDIPVGLGdmlalnQSDP 584
Cdd:cd02649 1 RKLIIDTDCGGDDAWALLMALASP--NVEVLAItCV----HGNTNVEQVVKNalrVLEACGRRDIPVYRG------ASKP 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239586 585 IFPPVGGCKYVkaipRGCGGFLDSDtlyglardLPRSPRRYTAENsvTHGAprdtdrpelrqpLAIevwQNLTKSGNGVs 664
Cdd:cd02649 69 LLGPGPTAAYF----HGKDGFGDVG--------FPEPKDELELQK--EHAV------------DAI---IRLVREYPGE- 118
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239586 665 kITVLTNGPLTNLAKIISSDKKSSSLIKEVYIVGGhiNREKsdKGNIftipsNAYAEFNMFLDPLAAKTVLESA-LNITL 743
Cdd:cd02649 119 -ITLVALGPLTNLALAYRLDPSLPQKIKRLYIMGG--NREG--VGNT-----TPAAEFNFHVDPEAAHIVLNSFgCPITI 188
|
..
gi 15239586 744 VP 745
Cdd:cd02649 189 VP 190
|
|
| nuc_hydro_CeIAG |
cd02649 |
nuc_hydro_CeIAG: Nucleoside hydrolases similar to the inosine-adenosine-guanosine-preferring ... |
46-325 |
2.59e-13 |
|
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: 71.52 E-value: 2.59e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239586 46 FAILYLLKLNKseFDLVGITLSA-NawTNAGHAVNQVYDLLHMMDRDDIPVGVGGEGgisddgtihsdvggyfPIIEQGM 124
Cdd:cd02649 15 WALLMALASPN--VEVLAITCVHgN--TNVEQVVKNALRVLEACGRRDIPVYRGASK----------------PLLGPGP 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239586 125 TTT---GEcryrqaipKGLGglldiDSNYGFRKQFLPqgnrrytpLQQPTAQKVIVDKISEGP--TTVILLGSHTNFALF 199
Cdd:cd02649 75 TAAyfhGK--------DGFG-----DVGFPEPKDELE--------LQKEHAVDAIIRLVREYPgeITLVALGPLTNLALA 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239586 200 LMSNPHLKHNIQHIYIMGGgvrsqNPTGccpanstvaecqprqcgnRGNlftdytSNPYSEFNIFADPFAAYQVFHS-GV 278
Cdd:cd02649 134 YRLDPSLPQKIKRLYIMGG-----NREG------------------VGN------TTPAAEFNFHVDPEAAHIVLNSfGC 184
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 15239586 279 PVTLVPLDAT-NTIPINQKFFE--TFENNYQRTYEA----QYVFLSLKIARDTW 325
Cdd:cd02649 185 PITIVPWETTlLAFPLDWEFEDkwANRLEKALFAESlnrrEYAFASEGLGGDGW 238
|
|
| nuc_hydro_CaPnhB |
cd02650 |
NH_hydro_CaPnhB: A subgroup of nucleoside hydrolases similar to Corynebacterium ammoniagenes ... |
46-289 |
1.75e-12 |
|
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: 69.23 E-value: 1.75e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239586 46 FAILYLLKlnKSEFDLVGITLS-ANAWTNAGhAVNQVYdLLHMMDRDDIPVGVGGEGGISDDGT-----IHSDvggyfpi 119
Cdd:cd02650 14 MALAYALA--HPDVDLIGVTTVyGNVTIETA-TRNALA-LLELFGRPDVPVAEGAAKPLTRPPFriatfVHGD------- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239586 120 ieqgmtttgecryrqaipKGLGGLldidsnygfrkqFLPQGNRRytPLQQPTAQkVIVDKISEGP--TTVILLGSHTNFA 197
Cdd:cd02650 83 ------------------NGLGDV------------ELPAPPRQ--PEDESAAD-FLIELANEYPgeLTLVAVGPLTNLA 129
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239586 198 LFLMSNPHLKHNIQHIYIMGGGVRSqnptgccpanstvaecqprqcgnRGNLftdytsNPYSEFNIFADPFAAYQVFHSG 277
Cdd:cd02650 130 LALARDPDFAKLVKQVVVMGGAFTV-----------------------PGNV------TPAAEANIHGDPEAADIVFTAG 180
|
250
....*....|..
gi 15239586 278 VPVTLVPLDATN 289
Cdd:cd02650 181 ADLTMVGLDVTT 192
|
|
| nuc_hydro_IU_UC_XIUA |
cd02651 |
nuc_hydro_IU_UC_XIUA: inosine-uridine preferring, ... |
638-778 |
4.72e-12 |
|
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: 67.96 E-value: 4.72e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239586 638 DTDRPELRQPlAIEVWQNLTKSGNGvsKITVLTNGPLTNLAKIISSDKKSSSLIKEVYIVGGHINReksdkGNIftipsN 717
Cdd:cd02651 91 PPPRRPEDIH-AVDAIIDTLRASPE--PITLVATGPLTNIALLLRKYPELAERIKEIVLMGGALGR-----GNI-----T 157
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15239586 718 AYAEFNMFLDPLAAKTVLESALNITLVPLATQHKLSSFQTMLDRLYSSTKtPEARFVKRLL 778
Cdd:cd02651 158 PAAEFNIFVDPEAAKIVFNSGIPITMVPLDVTHKALATPEVIERIRALGN-PVGKMLAELL 217
|
|
| PLN02717 |
PLN02717 |
uridine nucleosidase |
46-288 |
1.98e-11 |
|
uridine nucleosidase
Pssm-ID: 178319 [Multi-domain] Cd Length: 316 Bit Score: 66.17 E-value: 1.98e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239586 46 FAILylLKLNKSEFDLVGIT-LSANAWT-----NAGHavnqvydLLHMMDRDDIPVGvggeggisdDGTIHSDVGGYFPI 119
Cdd:PLN02717 15 MAIL--MALRSPEVEVIGLTtIFGNVTTklatrNALH-------LLEMAGRPDVPVA---------EGSHEPLKGGTKPR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239586 120 IeqgmtttgecryrQAIPKGLGGLLDIdsnygfrkqFLPQgnrrytPLQQP---TAQKVIVDKISEGP--TTVILLGSHT 194
Cdd:PLN02717 77 I-------------ADFVHGSDGLGNT---------NLPP------PKGKKiekSAAEFLVEKVSEYPgeVTVVALGPLT 128
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239586 195 NFALFLMSNPHLKHNIQHIYIMGGGVRSQnptgccpanstvaecqprqcgnrGNLftdytsNPYSEFNIFADPFAAYQVF 274
Cdd:PLN02717 129 NLALAIKLDPSFAKKVGQIVVLGGAFFVN-----------------------GNV------NPAAEANIFGDPEAADIVF 179
|
250
....*....|....
gi 15239586 275 HSGVPVTLVPLDAT 288
Cdd:PLN02717 180 TSGADITVVGINVT 193
|
|
| nuc_hydro_1 |
cd02648 |
NH_1: A subgroup of nucleoside hydrolases. This group contains fungal proteins similar to ... |
51-299 |
7.81e-11 |
|
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: 64.91 E-value: 7.81e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239586 51 LLKLNKS-EFDLVGITLS-ANawTNAGHAVNQVYDLLHMMDRDDI-PVGVGGEGGisddGTIHSDVGgyfPIIEQGMTTT 127
Cdd:cd02648 19 LLALSSPeEVDVALISLTfGN--TTLDHALRNVLRLFHVLERERAwRATPGVRYR----AFSADAEK---PIVASGSDQP 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239586 128 -GECRYRQAI---PKGLGGLLDIDSNYGFRKQFLPQGNRRYTPLQQPTAQkVIVDKISEGP---TTVILLGSHTNFALFL 200
Cdd:cd02648 90 lEGERLTASYfhgRDGLSGVHWLHPDFTPVETWIPEIVAPLTPSDKPAYD-VILDILREEPdhtVTIAALGPLTNLAAAA 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239586 201 MSNPHLKHNIQHIYIMGGGVRsqnptgcCPANSTvaecqprqcgnrgnlftdytsnPYSEFNIFADPFAAYQVF------ 274
Cdd:cd02648 169 RKDPETFAKVGEVVVMGGAID-------VPGNTS----------------------PVAEFNCFADPYAAAVVIdeppst 219
|
250 260 270
....*....|....*....|....*....|.
gi 15239586 275 ----HSGVPVTLVPLDAT--NTIPINQKFFE 299
Cdd:cd02648 220 apeaRRKLPLQVFPLDITtgHTLPYSSLFAT 250
|
|
| rihB |
PRK09955 |
ribosylpyrimidine nucleosidase; |
172-289 |
1.14e-09 |
|
ribosylpyrimidine nucleosidase;
Pssm-ID: 182166 [Multi-domain] Cd Length: 313 Bit Score: 60.73 E-value: 1.14e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239586 172 AQKVIVDKI--SEGPTTVILLGSHTNFALFLMSNPHLKHNIQHIYIMGGGVRSQNptgccpanstvaecqprqcgnrgnl 249
Cdd:PRK09955 104 AVKYIIDTLmaSDGDITLVPVGPLSNIAVAMRMQPAILPKIREIVLMGGAYGTGN------------------------- 158
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 15239586 250 FTdytsnPYSEFNIFADPFAAYQVFHSGVPVTLVPLDATN 289
Cdd:PRK09955 159 FT-----PSAEFNIFADPEAARVVFTSGVPLVMMGLDLTN 193
|
|
| rihA |
PRK10443 |
ribonucleoside hydrolase 1; Provisional |
509-751 |
5.20e-09 |
|
ribonucleoside hydrolase 1; Provisional
Pssm-ID: 182465 [Multi-domain] Cd Length: 311 Bit Score: 58.53 E-value: 5.20e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239586 509 KPVVFDMDMSAGDFLSLFYLLKVPvdKIDLKAIIVSPTGWANAATIDVVYDLLHMMGRDDIPVGLGdmlalnqsdpifpp 588
Cdd:PRK10443 3 LPIILDCDPGHDDAIALVLALASP--ELDVKAVTTSAGNQTPEKTLRNALRMLTLLNRTDIPVAGG-------------- 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239586 589 vggckyvKAIPrgcggfldsdtlygLARDLprsprrYTAENsvTHGAPrDTDRPELRQP-------LAIEVW-QNLTKSG 660
Cdd:PRK10443 67 -------AVKP--------------LMREL------IIADN--VHGES-GLDGPALPEPtfapqncTAVELMaKTLRESA 116
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239586 661 ngvSKITVLTNGPLTNLAKIISSDKKSSSLIKEVYIVGGHINreksdKGNifTIPSnayAEFNMFLDPLAAKTVLESALN 740
Cdd:PRK10443 117 ---EPVTLVSTGPQTNVALLLASHPELHSKIARIVIMGGAMG-----LGN--WTPA---AEFNIYVDPEAAEIVFQSGIP 183
|
250
....*....|.
gi 15239586 741 ITLVPLATQHK 751
Cdd:PRK10443 184 IVMAGLDVTHK 194
|
|
| nuc_hydro_3 |
cd02653 |
NH_3: A subgroup of nucleoside hydrolases. This group contains eukaryotic and bacterial ... |
510-750 |
1.55e-08 |
|
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: 57.39 E-value: 1.55e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239586 510 PVVFDMDMSAGDFLSLFYLLKVPvdKIDLKAIIVSPtgwANAATIDVVYD---LLHMMGRDDIPVGLGDMLALNQSDPIF 586
Cdd:cd02653 1 KVIIDCDPGIDDALALLYLLASP--DLDVVGITTTA---GNVPVEQVAANalgVLELLGRTDIPVYLGADKPLAGPLTTA 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239586 587 PPVGGckyvkaiPRGCGgfldsdtlYGlarDLPRSPRRYTAENSVThgaprdtdrpelrqplaieVWQNLTKSGNgvsKI 666
Cdd:cd02653 76 QDTHG-------PDGLG--------YA---ELPASTRTLSDESAAQ-------------------AWVDLARAHP---DL 115
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239586 667 TVLTNGPLTNLAKIISSDKKSSSLIKEVYIVGGHINREksdkGNifTIPSnayAEFNMFLDPLAAKTVLE----SALNIT 742
Cdd:cd02653 116 IGLATGPLTNLALALREEPELPRLLRRLVIMGGAFNSR----GN--TSPV---AEWNYWVDPEAAKEVLAafggHPVRPT 186
|
....*....
gi 15239586 743 LVPL-ATQH 750
Cdd:cd02653 187 ICGLdVTRA 195
|
|
| nuc_hydro_CaPnhB |
cd02650 |
NH_hydro_CaPnhB: A subgroup of nucleoside hydrolases similar to Corynebacterium ammoniagenes ... |
511-778 |
3.93e-08 |
|
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: 55.75 E-value: 3.93e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239586 511 VVFDMDMSAGDFLSLFYLLKVPvdKIDLKAIIvspTGWANA----ATIDVVYdLLHMMGRDDIPVGLGdmlalnqsdpif 586
Cdd:cd02650 2 LILDTDPGIDDAMALAYALAHP--DVDLIGVT---TVYGNVtietATRNALA-LLELFGRPDVPVAEG------------ 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239586 587 ppvggckyvKAIPrgcggfldsdtlygLARDLPRSPRRYTAENSVTH-GAPRDTDRPELRQplAIEVWQNLTKSGNGvsK 665
Cdd:cd02650 64 ---------AAKP--------------LTRPPFRIATFVHGDNGLGDvELPAPPRQPEDES--AADFLIELANEYPG--E 116
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239586 666 ITVLTNGPLTNLAKIISSDKKSSSLIKEVYIVGGhinreksdkgnIFTIPSNA--YAEFNMFLDPLAAKTVLESALNITL 743
Cdd:cd02650 117 LTLVAVGPLTNLALALARDPDFAKLVKQVVVMGG-----------AFTVPGNVtpAAEANIHGDPEAADIVFTAGADLTM 185
|
250 260 270
....*....|....*....|....*....|....*....
gi 15239586 744 VPLATQHklssfQTMLDRLY----SSTKTPEARFVKRLL 778
Cdd:cd02650 186 VGLDVTT-----QTLLTREDldelRDSGGKAGQFLADML 219
|
|
| PRK10768 |
PRK10768 |
ribonucleoside hydrolase RihC; Provisional |
645-746 |
1.14e-07 |
|
ribonucleoside hydrolase RihC; Provisional
Pssm-ID: 182713 [Multi-domain] Cd Length: 304 Bit Score: 54.53 E-value: 1.14e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239586 645 RQPL---AIEVWQN-LTKSgngVSKITVLTNGPLTNLAKIISSDKKSSSLIKEVYIVGGHINReksdkGNIftipsNAYA 720
Cdd:PRK10768 96 RKPLsipAVEAMRDaLMNA---PEPVTLVAIGPLTNIALLLSTYPEVKPYIKRIVLMGGSAGR-----GNV-----TPNA 162
|
90 100
....*....|....*....|....*.
gi 15239586 721 EFNMFLDPLAAKTVLESALNITLVPL 746
Cdd:PRK10768 163 EFNIAVDPEAAAIVFRSGIPIVMCGL 188
|
|
| PTZ00313 |
PTZ00313 |
inosine-adenosine-guanosine-nucleoside hydrolase; Provisional |
507-736 |
9.10e-07 |
|
inosine-adenosine-guanosine-nucleoside hydrolase; Provisional
Pssm-ID: 140334 [Multi-domain] Cd Length: 326 Bit Score: 51.79 E-value: 9.10e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239586 507 PGKPVVFDMDMSAGDFLSLFYLLKVPvDKIDLKAIIVSPTGWANAATIDVVYDLLHMMGRddipvglgdmlalNQSDPIF 586
Cdd:PTZ00313 1 MPKPVILDHDGNHDDLVALALLLGNP-EKVKVIGCICTDADCFVDDAFNVTGKLMCMMHA-------------REATPLF 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239586 587 P-PVGGCKYVKAIP---RGCGGFLDsdtlyglarDLPrsprrytAENSVTHGAPRDTDRPELRQPLAIEVWQNLTKSGNg 662
Cdd:PTZ00313 67 PiGKSSFKGVNPFPsewRWSAKNMD---------DLP-------CLNIPEHVAIWEKLKPENEALVGEELLADLVMSSP- 129
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15239586 663 vSKITVLTNGPLTNLA-KIISSDKKSSSLIKEVYIVGGHINReksdKGNIFTIPSNAYAEFNMFLDPLAAKTVLE 736
Cdd:PTZ00313 130 -EKVTICVTGPLSNVAwCIEKYGEEFTKKVEECVIMGGAVDV----GGNVFLPGTDGSAEWNIYWDPPAAKTVLM 199
|
|
| PLN02717 |
PLN02717 |
uridine nucleosidase |
665-798 |
6.85e-06 |
|
uridine nucleosidase
Pssm-ID: 178319 [Multi-domain] Cd Length: 316 Bit Score: 48.84 E-value: 6.85e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239586 665 KITVLTNGPLTNLAKIISSDKKSSSLIKEVYIVGGHINReksdKGNIftipsNAYAEFNMFLDPLAAKTVLESALNITLV 744
Cdd:PLN02717 118 EVTVVALGPLTNLALAIKLDPSFAKKVGQIVVLGGAFFV----NGNV-----NPAAEANIFGDPEAADIVFTSGADITVV 188
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 15239586 745 PL--ATQHKLSSFQtmLDRLYSStKTPEARFVKRLlvrLQALHQKHRRYTHID-MFL 798
Cdd:PLN02717 189 GInvTTQVVLTDAD--LEELRDS-KGKYAQFLCDI---CKFYRDWHRKSYGIDgIYL 239
|
|
| nuc_hydro_1 |
cd02648 |
NH_1: A subgroup of nucleoside hydrolases. This group contains fungal proteins similar to ... |
510-800 |
1.45e-05 |
|
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: 48.34 E-value: 1.45e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239586 510 PVVFDMDMSAGDFLSLFYLLKVPvDKIDLKAIIVS------PTGWANAATIdvvYDLL--HMMGRDDIPVGLGDMLALNQ 581
Cdd:cd02648 3 PIIIDTDPGVDDVLAILLALSSP-EEVDVALISLTfgnttlDHALRNVLRL---FHVLerERAWRATPGVRYRAFSADAE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239586 582 SdPIFP-----PVGGCKYVKAIprgcggFLDSDTLYGLARDLPR-SPRRYTAENSVTHGAPRDTdrpelrqpLAIEVWQN 655
Cdd:cd02648 79 K-PIVAsgsdqPLEGERLTASY------FHGRDGLSGVHWLHPDfTPVETWIPEIVAPLTPSDK--------PAYDVILD 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239586 656 LTKSGNGVSkITVLTNGPLTNLAKIISSDKKSSSLIKEVYIVGGHINReksdKGNIFTIpsnayAEFNMFLDPLAAKTVL 735
Cdd:cd02648 144 ILREEPDHT-VTIAALGPLTNLAAAARKDPETFAKVGEVVVMGGAIDV----PGNTSPV-----AEFNCFADPYAAAVVI 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239586 736 ESA----------LNITLVPL--ATQHKLSS----FQTMLDRLYSSTKTPEARFvkrLLVRLQALHQKHRRYTHIDMFLG 799
Cdd:cd02648 214 DEPpstapearrkLPLQVFPLdiTTGHTLPYsslfATYVTPRDAPERGSPLARW---LEHVFISTFLTHPRAFTPEEFLP 290
|
.
gi 15239586 800 E 800
Cdd:cd02648 291 D 291
|
|
| nuc_hydro_CjNH |
cd02654 |
nuc_hydro_CjNH. Nucleoside hydrolases similar to Campylobacter jejuni nucleoside hydrolase. ... |
666-776 |
1.48e-05 |
|
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: 47.93 E-value: 1.48e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239586 666 ITVLTNGPLTNLAKIISSDKKSSSLIKEVYIVGGHINREKSdkgnifTIPSNAYAEFNMFLDPLAAKTVLES-------A 738
Cdd:cd02654 131 VSIVAAGPLTNLALALRIDPDFAPLAKELVIMGGYLDDIGE------FVNRHYASDFNLIMDPEAASIVLTApwksitiP 204
|
90 100 110
....*....|....*....|....*....|....*...
gi 15239586 739 LNITLVPLATQHKLSSFQTMLDRLYSSTKTPEARFVKR 776
Cdd:cd02654 205 GNVTNRTCLTPEQIKADDPLRDFIRETLDLPIDYAKEF 242
|
|
| PTZ00313 |
PTZ00313 |
inosine-adenosine-guanosine-nucleoside hydrolase; Provisional |
246-380 |
2.34e-05 |
|
inosine-adenosine-guanosine-nucleoside hydrolase; Provisional
Pssm-ID: 140334 [Multi-domain] Cd Length: 326 Bit Score: 47.55 E-value: 2.34e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239586 246 RGNLFTDYTSNPySEFNIFADPFAAYQVFH-SGVPVTLVPLDATNTIPINQKFFETFennyqrtyEAQYVFLSLKIARDT 324
Cdd:PTZ00313 171 GGNVFLPGTDGS-AEWNIYWDPPAAKTVLMcPHIRKVLFSLDSTNSVPVTSEVVKKF--------GAQNKYLLSQFVGST 241
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15239586 325 WFDDEFYK------SYFMWDSFTAGVAVsimrnsanknnkngENDFAEMEYMNITVVTSNKP 380
Cdd:PTZ00313 242 WAMCTHHEllrpgdGYYAWDVLTAAYVI--------------ERNLAELEPVPLEVVVEKAK 289
|
|
| rihB |
PRK09955 |
ribosylpyrimidine nucleosidase; |
666-762 |
1.64e-03 |
|
ribosylpyrimidine nucleosidase;
Pssm-ID: 182166 [Multi-domain] Cd Length: 313 Bit Score: 41.47 E-value: 1.64e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239586 666 ITVLTNGPLTNLAKIISSDKKSSSLIKEVYIVGGHINreksdKGNiFTiPSnayAEFNMFLDPLAAKTVLESALNITLVP 745
Cdd:PRK09955 119 ITLVPVGPLSNIAVAMRMQPAILPKIREIVLMGGAYG-----TGN-FT-PS---AEFNIFADPEAARVVFTSGVPLVMMG 188
|
90
....*....|....*..
gi 15239586 746 LATQHKLSSFQTMLDRL 762
Cdd:PRK09955 189 LDLTNQTVCTPDVIARM 205
|
|
|