|
Name |
Accession |
Description |
Interval |
E-value |
| nuc_hydro |
cd00455 |
nuc_hydro: Nucleoside hydrolases. Nucleoside hydrolases cleave the N-glycosidic bond in ... |
5-305 |
1.32e-101 |
|
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: 300.02 E-value: 1.32e-101
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446438822 5 ILFFGDFGIDDTIAIIYAHLTDKIDVIGIVADYGNVPKAEVVRNVRFLLKSVGKEYIKVFGGAEHSMSSEAETFYPEVHG 84
Cdd:cd00455 1 VILDTDPGIDDAFALMYALLHPEIELVGIVATYGNVTLEQATQNAAYLLELLGRLDIPVYAGATRPLTGEIPAAYPEIHG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446438822 85 KFGIGPIYPGL-EIQTFENFFEVLTLIKQHKNELIIVNTGRLTSLATLFLLYGDVMEYVHSYYIMGGAFLYPGNVTPIAE 163
Cdd:cd00455 81 EGGLGLPIPPIiEADDPEAVQLLIDLIRKYPDEITIVALGPLTNLAMAFILDPDIKDRVKEIVIMGGAFLVPGNVTPVAE 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446438822 164 ANFYGDPGSANIVMRYAKNLSIYPLNVTQSAIVTPEMVNYIHSKGkTKFLKPLLDYYYYQFYQKKVPGIQGSPVHDALTL 243
Cdd:cd00455 161 ANFYGDPEAANIVFNSAKNLTIVPLDVTNQAVLTPPMVERIFEQG-TSIGLLIKPMIDYYYKAYQKPGIEGSPIHDPLAV 239
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446438822 244 IAINRDDIFTYHHSAVTVNVLDTVRGQSIGDFRStfepetFGNRPKHRIAIQMNYEQFFKEF 305
Cdd:cd00455 240 AYLLNPSMFDYSKVPVDVDTDGLTRGQTIADFRE------NPGNGVTRVAVNLDYPDFIELI 295
|
|
| URH1 |
COG1957 |
Inosine-uridine nucleoside N-ribohydrolase [Nucleotide transport and metabolism]; ... |
1-311 |
3.57e-82 |
|
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: 250.84 E-value: 3.57e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446438822 1 MGKKILFFGDFGIDDTIAIIYAHLTDKIDVIGIVADYGNVPKAEVVRNVRFLLKSVGKEYIKVFGGAEHSMSSEAETfYP 80
Cdd:COG1957 1 MMRKVIIDTDPGIDDALALLLALASPEIDLLGITTVAGNVPLEQTTRNALKLLELAGRTDVPVAAGAARPLVRPLVT-AE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446438822 81 EVHGKFGIGPIY---PGLEIQTfENFFEVL-TLIKQHKNELIIVNTGRLTSLATLFLLYGDVMEYVHSYYIMGGAFLYPG 156
Cdd:COG1957 80 HVHGEDGLGGVDlpePTRPPEP-EHAVDFIiETLRAAPGEVTLVALGPLTNLALALRKDPELAERIKRIVIMGGAFFVPG 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446438822 157 NVTPIAEANFYGDPGSANIVMRYAKNLSIYPLNVTQSAIVTPEMVNYIHSKGK--TKFLKPLLDyyYYQFYQKKVPGIQG 234
Cdd:COG1957 159 NVTPVAEFNIYVDPEAAKIVFASGIPITMVGLDVTHQALLTPEDLARLAALGTplGRFLADLLD--FYLDFYRERYGLDG 236
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446438822 235 SPVHDALTLIAINRDDIFTYHHSAVTVnVLD--TVRGQSIGDFRStfepeTFGNRPKHRIAIQMNYEQFFKEFMTVMTG 311
Cdd:COG1957 237 CPLHDPLAVAYLLDPELFTTRPAPVDV-ETDgeLTRGQTVVDWRG-----VTGRPPNARVALDVDAERFLDLLLERLAR 309
|
|
| IU_nuc_hydro |
pfam01156 |
Inosine-uridine preferring nucleoside hydrolase; |
5-303 |
1.42e-56 |
|
Inosine-uridine preferring nucleoside hydrolase;
Pssm-ID: 460086 [Multi-domain] Cd Length: 253 Bit Score: 183.18 E-value: 1.42e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446438822 5 ILFFGDFGIDDTIAIIYAHLTDKIDVIGIVADYGNVPKAEVVRNVRFLLKSVGKEYIkvfggaehsmsseaetfypevhg 84
Cdd:pfam01156 1 VIIDTDPGIDDALALLLALASPEIELLGITTVAGNVSLEQTTRNALRLLELGGRDDI----------------------- 57
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446438822 85 kfgigPIYPGleiqtfenffevlTLIKQHkNELIIVNTGRLTSLATLFLLYGDVMEYVHSYYIMGGAFLYPGNVTPIAEA 164
Cdd:pfam01156 58 -----PVYAG-------------EAIREP-GEVTLVATGPLTNLALALRLDPELAKKIKELVIMGGAFGVRGNVTPAAEF 118
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446438822 165 NFYGDPGSANIVMRYAKNLSIYPLNVTQSAIVTPEMVNYIHSKGK--TKFLKPLLDyyYYQFYQKKVPGIQGSPVHDALT 242
Cdd:pfam01156 119 NIFVDPEAAKIVFTSGLPITMVPLDVTHQALLTPEDLERLAALGTplGRFLADLLR--FYAEFYRERFGIDGPPLHDPLA 196
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446438822 243 LIAINRDDIFTYHHSAVTVNVLDTV-RGQSIGDFRStfepeTFGNRPKHRIAIQMNYEQFFK 303
Cdd:pfam01156 197 VAVALDPELFTTRRLNVDVETTGGLtRGQTVVDDRG-----GWGKPPNVRVATDVDVDRFWE 253
|
|
| PLN02717 |
PLN02717 |
uridine nucleosidase |
3-274 |
2.14e-34 |
|
uridine nucleosidase
Pssm-ID: 178319 [Multi-domain] Cd Length: 316 Bit Score: 127.42 E-value: 2.14e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446438822 3 KKILFFGDFGIDDTIAIIYAHLTDKIDVIGIVADYGNVPKAEVVRNVRFLLKSVGKEYIKVFGGAEHSMSSEAETFYPE- 81
Cdd:PLN02717 1 KKLIIDTDPGIDDAMAILMALRSPEVEVIGLTTIFGNVTTKLATRNALHLLEMAGRPDVPVAEGSHEPLKGGTKPRIADf 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446438822 82 VHGKFGIGPIYP----GLEIQTFENFFEVLTlIKQHKNELIIVNTGRLTSLATLFLLYGDVMEYVHSYYIMGGAFLYPGN 157
Cdd:PLN02717 81 VHGSDGLGNTNLpppkGKKIEKSAAEFLVEK-VSEYPGEVTVVALGPLTNLALAIKLDPSFAKKVGQIVVLGGAFFVNGN 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446438822 158 VTPIAEANFYGDPGSANIVMRYAKNLSIYPLNVTQSAIVT-PEMVNYIHSKGK-TKFLKPLLDYYYYQFYQKKvpGIQGS 235
Cdd:PLN02717 160 VNPAAEANIFGDPEAADIVFTSGADITVVGINVTTQVVLTdADLEELRDSKGKyAQFLCDICKFYRDWHRKSY--GIDGI 237
|
250 260 270
....*....|....*....|....*....|....*....
gi 446438822 236 PVHDALTLIAINRDDIFTYHHSAVTVNVLDTVRGQSIGD 274
Cdd:PLN02717 238 YLHDPTALLAAVRPSLFTYKEGVVRVETEGICRGLTLFD 276
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| nuc_hydro |
cd00455 |
nuc_hydro: Nucleoside hydrolases. Nucleoside hydrolases cleave the N-glycosidic bond in ... |
5-305 |
1.32e-101 |
|
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: 300.02 E-value: 1.32e-101
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446438822 5 ILFFGDFGIDDTIAIIYAHLTDKIDVIGIVADYGNVPKAEVVRNVRFLLKSVGKEYIKVFGGAEHSMSSEAETFYPEVHG 84
Cdd:cd00455 1 VILDTDPGIDDAFALMYALLHPEIELVGIVATYGNVTLEQATQNAAYLLELLGRLDIPVYAGATRPLTGEIPAAYPEIHG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446438822 85 KFGIGPIYPGL-EIQTFENFFEVLTLIKQHKNELIIVNTGRLTSLATLFLLYGDVMEYVHSYYIMGGAFLYPGNVTPIAE 163
Cdd:cd00455 81 EGGLGLPIPPIiEADDPEAVQLLIDLIRKYPDEITIVALGPLTNLAMAFILDPDIKDRVKEIVIMGGAFLVPGNVTPVAE 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446438822 164 ANFYGDPGSANIVMRYAKNLSIYPLNVTQSAIVTPEMVNYIHSKGkTKFLKPLLDYYYYQFYQKKVPGIQGSPVHDALTL 243
Cdd:cd00455 161 ANFYGDPEAANIVFNSAKNLTIVPLDVTNQAVLTPPMVERIFEQG-TSIGLLIKPMIDYYYKAYQKPGIEGSPIHDPLAV 239
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446438822 244 IAINRDDIFTYHHSAVTVNVLDTVRGQSIGDFRStfepetFGNRPKHRIAIQMNYEQFFKEF 305
Cdd:cd00455 240 AYLLNPSMFDYSKVPVDVDTDGLTRGQTIADFRE------NPGNGVTRVAVNLDYPDFIELI 295
|
|
| URH1 |
COG1957 |
Inosine-uridine nucleoside N-ribohydrolase [Nucleotide transport and metabolism]; ... |
1-311 |
3.57e-82 |
|
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: 250.84 E-value: 3.57e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446438822 1 MGKKILFFGDFGIDDTIAIIYAHLTDKIDVIGIVADYGNVPKAEVVRNVRFLLKSVGKEYIKVFGGAEHSMSSEAETfYP 80
Cdd:COG1957 1 MMRKVIIDTDPGIDDALALLLALASPEIDLLGITTVAGNVPLEQTTRNALKLLELAGRTDVPVAAGAARPLVRPLVT-AE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446438822 81 EVHGKFGIGPIY---PGLEIQTfENFFEVL-TLIKQHKNELIIVNTGRLTSLATLFLLYGDVMEYVHSYYIMGGAFLYPG 156
Cdd:COG1957 80 HVHGEDGLGGVDlpePTRPPEP-EHAVDFIiETLRAAPGEVTLVALGPLTNLALALRKDPELAERIKRIVIMGGAFFVPG 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446438822 157 NVTPIAEANFYGDPGSANIVMRYAKNLSIYPLNVTQSAIVTPEMVNYIHSKGK--TKFLKPLLDyyYYQFYQKKVPGIQG 234
Cdd:COG1957 159 NVTPVAEFNIYVDPEAAKIVFASGIPITMVGLDVTHQALLTPEDLARLAALGTplGRFLADLLD--FYLDFYRERYGLDG 236
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446438822 235 SPVHDALTLIAINRDDIFTYHHSAVTVnVLD--TVRGQSIGDFRStfepeTFGNRPKHRIAIQMNYEQFFKEFMTVMTG 311
Cdd:COG1957 237 CPLHDPLAVAYLLDPELFTTRPAPVDV-ETDgeLTRGQTVVDWRG-----VTGRPPNARVALDVDAERFLDLLLERLAR 309
|
|
| IU_nuc_hydro |
pfam01156 |
Inosine-uridine preferring nucleoside hydrolase; |
5-303 |
1.42e-56 |
|
Inosine-uridine preferring nucleoside hydrolase;
Pssm-ID: 460086 [Multi-domain] Cd Length: 253 Bit Score: 183.18 E-value: 1.42e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446438822 5 ILFFGDFGIDDTIAIIYAHLTDKIDVIGIVADYGNVPKAEVVRNVRFLLKSVGKEYIkvfggaehsmsseaetfypevhg 84
Cdd:pfam01156 1 VIIDTDPGIDDALALLLALASPEIELLGITTVAGNVSLEQTTRNALRLLELGGRDDI----------------------- 57
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446438822 85 kfgigPIYPGleiqtfenffevlTLIKQHkNELIIVNTGRLTSLATLFLLYGDVMEYVHSYYIMGGAFLYPGNVTPIAEA 164
Cdd:pfam01156 58 -----PVYAG-------------EAIREP-GEVTLVATGPLTNLALALRLDPELAKKIKELVIMGGAFGVRGNVTPAAEF 118
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446438822 165 NFYGDPGSANIVMRYAKNLSIYPLNVTQSAIVTPEMVNYIHSKGK--TKFLKPLLDyyYYQFYQKKVPGIQGSPVHDALT 242
Cdd:pfam01156 119 NIFVDPEAAKIVFTSGLPITMVPLDVTHQALLTPEDLERLAALGTplGRFLADLLR--FYAEFYRERFGIDGPPLHDPLA 196
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446438822 243 LIAINRDDIFTYHHSAVTVNVLDTV-RGQSIGDFRStfepeTFGNRPKHRIAIQMNYEQFFK 303
Cdd:pfam01156 197 VAVALDPELFTTRRLNVDVETTGGLtRGQTVVDDRG-----GWGKPPNVRVATDVDVDRFWE 253
|
|
| nuc_hydro_CaPnhB |
cd02650 |
NH_hydro_CaPnhB: A subgroup of nucleoside hydrolases similar to Corynebacterium ammoniagenes ... |
4-306 |
5.57e-46 |
|
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: 157.44 E-value: 5.57e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446438822 4 KILFFGDFGIDDTIAIIYAHLTDKIDVIGIVADYGNVPKAEVVRNVRFLLKSVGKEYIKVFGGAEHSMSSEAETFYPEVH 83
Cdd:cd02650 1 KLILDTDPGIDDAMALAYALAHPDVDLIGVTTVYGNVTIETATRNALALLELFGRPDVPVAEGAAKPLTRPPFRIATFVH 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446438822 84 GKFGIG------PIYPGLEIQTFENFFEvltLIKQHKNELIIVNTGRLTSLATLFLLYGDVMEYVHSYYIMGGAFLYPGN 157
Cdd:cd02650 81 GDNGLGdvelpaPPRQPEDESAADFLIE---LANEYPGELTLVAVGPLTNLALALARDPDFAKLVKQVVVMGGAFTVPGN 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446438822 158 VTPIAEANFYGDPGSANIVMRYAKNLSIYPLNVTQSAIVTPEMVNYIH-SKGK-TKFLKPLLDyyYYQFYQKKVPGIQGS 235
Cdd:cd02650 158 VTPAAEANIHGDPEAADIVFTAGADLTMVGLDVTTQTLLTREDLDELRdSGGKaGQFLADMLD--YYIDFYQESPGLRGC 235
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446438822 236 PVHDALTLIAINRDDIFTYHHSAVTVNVLDTVRGQSIGDFRSTFEpetFGNRPKHRIAIQMN-YEQFFKEFM 306
Cdd:cd02650 236 ALHDPLAVAAAVDPSLFTTREGVVRVETEGPTRGRTIGDRDGRRF---WDSSPNATVAVDVDvDERFLKRLM 304
|
|
| nuc_hydro_IU_UC_XIUA |
cd02651 |
nuc_hydro_IU_UC_XIUA: inosine-uridine preferring, ... |
10-303 |
9.64e-44 |
|
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: 151.54 E-value: 9.64e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446438822 10 DFGIDDTIAIIYAHLTDKIDVIGIVADYGNVPKAEVVRNVRFLLKSVGKEYIKVFGGAEHSMSSEAETfYPEVHGKFGI- 88
Cdd:cd02651 7 DPGHDDAVAILLALFHPELDLLGITTVAGNVPLEKTTRNALKLLTLLGRTDVPVAAGAARPLVRPLIT-ASDIHGESGLd 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446438822 89 GPIYPglEIQTFE---NFFEVL-TLIKQHKNELIIVNTGRLTSLATLFLLYGDVMEYVHSYYIMGGAFLYpGNVTPIAEA 164
Cdd:cd02651 86 GADLP--PPPRRPediHAVDAIiDTLRASPEPITLVATGPLTNIALLLRKYPELAERIKEIVLMGGALGR-GNITPAAEF 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446438822 165 NFYGDPGSANIVMRYAKNLSIYPLNVTQSAIVTPEMVNYIHSKGK--TKFLKPLLDYYYYQFYQKKVPGIqgsPVHDALT 242
Cdd:cd02651 163 NIFVDPEAAKIVFNSGIPITMVPLDVTHKALATPEVIERIRALGNpvGKMLAELLDFFAETYGSAFTEGP---PLHDPCA 239
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446438822 243 LIAINRDDIFTYHHSAVTVNVLDTV-RGQSIGDFRSTfepetfGNRPKH-RIAIQMNYEQFFK 303
Cdd:cd02651 240 VAYLLDPELFTTKRANVDVETEGELtRGRTVVDLRGV------TGRPANaQVAVDVDVEKFWD 296
|
|
| nuc_hydro_CeIAG |
cd02649 |
nuc_hydro_CeIAG: Nucleoside hydrolases similar to the inosine-adenosine-guanosine-preferring ... |
10-278 |
6.13e-37 |
|
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: 133.92 E-value: 6.13e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446438822 10 DFGIDDTIAIIYAHLTDKIDVIGIVADYGNVPKAEVVRNVRFLLKSVGKEYIKVFGGAEHSMSSEAETFYpEVHGKFGIG 89
Cdd:cd02649 8 DCGGDDAWALLMALASPNVEVLAITCVHGNTNVEQVVKNALRVLEACGRRDIPVYRGASKPLLGPGPTAA-YFHGKDGFG 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446438822 90 ----PIYPGLEIQTFEN-FFEVLTLIKQHKNELIIVNTGRLTSLATLFLLYGDVMEYVHSYYIMGGAFLYPGNVTPIAEA 164
Cdd:cd02649 87 dvgfPEPKDELELQKEHaVDAIIRLVREYPGEITLVALGPLTNLALAYRLDPSLPQKIKRLYIMGGNREGVGNTTPAAEF 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446438822 165 NFYGDPGSANIVM-RYAKNLSIYPLNVTQSAIVTP-EMVNYIHSKGKTKFLKPLLdYYYYQFYQKKVPGIQGSPVHDALT 242
Cdd:cd02649 167 NFHVDPEAAHIVLnSFGCPITIVPWETTLLAFPLDwEFEDKWANRLEKALFAESL-NRREYAFASEGLGGDGWVPCDALA 245
|
250 260 270
....*....|....*....|....*....|....*...
gi 446438822 243 L-IAINRDDIFTYHHSAVTVNVLDTV-RGQSIGDFRST 278
Cdd:cd02649 246 VaAALDPSIITRRLTYAVDVELHGELtRGQMVVDWLGT 283
|
|
| PLN02717 |
PLN02717 |
uridine nucleosidase |
3-274 |
2.14e-34 |
|
uridine nucleosidase
Pssm-ID: 178319 [Multi-domain] Cd Length: 316 Bit Score: 127.42 E-value: 2.14e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446438822 3 KKILFFGDFGIDDTIAIIYAHLTDKIDVIGIVADYGNVPKAEVVRNVRFLLKSVGKEYIKVFGGAEHSMSSEAETFYPE- 81
Cdd:PLN02717 1 KKLIIDTDPGIDDAMAILMALRSPEVEVIGLTTIFGNVTTKLATRNALHLLEMAGRPDVPVAEGSHEPLKGGTKPRIADf 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446438822 82 VHGKFGIGPIYP----GLEIQTFENFFEVLTlIKQHKNELIIVNTGRLTSLATLFLLYGDVMEYVHSYYIMGGAFLYPGN 157
Cdd:PLN02717 81 VHGSDGLGNTNLpppkGKKIEKSAAEFLVEK-VSEYPGEVTVVALGPLTNLALAIKLDPSFAKKVGQIVVLGGAFFVNGN 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446438822 158 VTPIAEANFYGDPGSANIVMRYAKNLSIYPLNVTQSAIVT-PEMVNYIHSKGK-TKFLKPLLDYYYYQFYQKKvpGIQGS 235
Cdd:PLN02717 160 VNPAAEANIFGDPEAADIVFTSGADITVVGINVTTQVVLTdADLEELRDSKGKyAQFLCDICKFYRDWHRKSY--GIDGI 237
|
250 260 270
....*....|....*....|....*....|....*....
gi 446438822 236 PVHDALTLIAINRDDIFTYHHSAVTVNVLDTVRGQSIGD 274
Cdd:PLN02717 238 YLHDPTALLAAVRPSLFTYKEGVVRVETEGICRGLTLFD 276
|
|
| nuc_hydro_3 |
cd02653 |
NH_3: A subgroup of nucleoside hydrolases. This group contains eukaryotic and bacterial ... |
10-308 |
1.69e-31 |
|
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: 119.79 E-value: 1.69e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446438822 10 DFGIDDTIAIIYAHLTDKIDVIGIVADYGNVPKAEVVRNVRFLLKSVGKEYIKVFGGAEHSMSSEAETfYPEVHGKFGIG 89
Cdd:cd02653 7 DPGIDDALALLYLLASPDLDVVGITTTAGNVPVEQVAANALGVLELLGRTDIPVYLGADKPLAGPLTT-AQDTHGPDGLG 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446438822 90 piY-----PGLEIQTFENFFEVLTLIKQHkNELIIVNTGRLTSLATLFLLYGDVMEYVHSYYIMGGAFLYPGNVTPIAEA 164
Cdd:cd02653 86 --YaelpaSTRTLSDESAAQAWVDLARAH-PDLIGLATGPLTNLALALREEPELPRLLRRLVIMGGAFNSRGNTSPVAEW 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446438822 165 NFYGDPGSANIVM----RYAKNLSIYPLNVTQSAIVTPEMVNYIHSKGK------TKFLKPLLDYYYYQFYqkkvpgIQG 234
Cdd:cd02653 163 NYWVDPEAAKEVLaafgGHPVRPTICGLDVTRAVVLTPNLLERLARAKDsvgafiEDALRFYFEFHWAYGH------GYG 236
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 446438822 235 SPVHDALTLI-AINRDDIFTYhHSAVTVNVLDTVRGQSIGDfrstfEPETFGNRPKHRIAIQMNYEQFFKEFMTV 308
Cdd:cd02653 237 AVIHDPLAAAvALNPNLARGR-PAYVDVECTGVLTGQTVVD-----WAGFWGKGANAEILTKVDSQDFMALFIER 305
|
|
| rihA |
PRK10443 |
ribonucleoside hydrolase 1; Provisional |
1-253 |
1.07e-22 |
|
ribonucleoside hydrolase 1; Provisional
Pssm-ID: 182465 [Multi-domain] Cd Length: 311 Bit Score: 95.89 E-value: 1.07e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446438822 1 MGKKILFFGDFGIDDTIAIIYAHLTDKIDVIGIVADYGNVPKAEVVRNVRFLLKSVGKEYIKVFGGAEHSMSSEAETfYP 80
Cdd:PRK10443 1 MALPIILDCDPGHDDAIALVLALASPELDVKAVTTSAGNQTPEKTLRNALRMLTLLNRTDIPVAGGAVKPLMRELII-AD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446438822 81 EVHGKFGI-GPIYP--GLEIQTFENFFEVLTLIKQHKNELIIVNTGRLTSLATLFLLYGDVMEYVHSYYIMGGAfLYPGN 157
Cdd:PRK10443 80 NVHGESGLdGPALPepTFAPQNCTAVELMAKTLRESAEPVTLVSTGPQTNVALLLASHPELHSKIARIVIMGGA-MGLGN 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446438822 158 VTPIAEANFYGDPGSANIVMRYAKNLSIYPLNVTQSAIVTPEMVNYIHSKGK--TKFLKPLLDYYYYQFYQKKVpGIQGS 235
Cdd:PRK10443 159 WTPAAEFNIYVDPEAAEIVFQSGIPIVMAGLDVTHKAQIMDEDIERIRAIGNpvATIVAELLDFFMEYHKDEKW-GFVGA 237
|
250
....*....|....*...
gi 446438822 236 PVHDALTLIAINRDDIFT 253
Cdd:PRK10443 238 PLHDPCTIAWLLKPELFT 255
|
|
| rihB |
PRK09955 |
ribosylpyrimidine nucleosidase; |
3-302 |
2.68e-19 |
|
ribosylpyrimidine nucleosidase;
Pssm-ID: 182166 [Multi-domain] Cd Length: 313 Bit Score: 86.54 E-value: 2.68e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446438822 3 KKILFFGDFGIDDTIAIIYAHLTDKIDVIGIVADYGNVPKAEVVRNVRFLLKSVGKEyIKVFGGAEHSMSSEaETFYPEV 82
Cdd:PRK09955 4 RKIILDCDPGHDDAIAMMMAAKHPAIDLLGITIVAGNQTLDKTLINGLNVCQKLEIN-VPVYAGMPQPIMRQ-QIVADNI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446438822 83 HGKFGI-GPIYPGLEIQTfENFFEVLTLIKQ---HKNELIIVNTGRLTSLATLFLLYGDVMEYVHSYYIMGGAFlYPGNV 158
Cdd:PRK09955 82 HGETGLdGPVFEPLTRQA-ESTHAVKYIIDTlmaSDGDITLVPVGPLSNIAVAMRMQPAILPKIREIVLMGGAY-GTGNF 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446438822 159 TPIAEANFYGDPGSANIVMRYAKNLSIYPLNVTQSAIVTPEMVNYIHSKGKT--KFLKPLLDYYYYQFYQKKvpGIQGSP 236
Cdd:PRK09955 160 TPSAEFNIFADPEAARVVFTSGVPLVMMGLDLTNQTVCTPDVIARMERAGGPagELFSDIMNFTLKTQFENY--GLAGGP 237
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 446438822 237 VHDALTLIAINRDDIFTYHHSAVTVNV-LDTVRGQSIGDfrstfEPETFGNRPKHRIAIQMNYEQFF 302
Cdd:PRK09955 238 VHDATCIGYLINPDGIKTQEMYVEVDVnSGPCYGRTVCD-----ELGVLGKPANTKVGITIDTDWFW 299
|
|
| nuc_hydro_1 |
cd02648 |
NH_1: A subgroup of nucleoside hydrolases. This group contains fungal proteins similar to ... |
4-203 |
3.07e-14 |
|
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: 72.22 E-value: 3.07e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446438822 4 KILFFGDFGIDDTIAIIYA-HLTDKIDVIGIVADYGNVPKAEVVRNVRFLL----------KSVGKEY---------IKV 63
Cdd:cd02648 3 PIIIDTDPGVDDVLAILLAlSSPEEVDVALISLTFGNTTLDHALRNVLRLFhvlererawrATPGVRYrafsadaekPIV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446438822 64 FGGAEHSMSSE---AETFypevHGKFGIG------PIYPGLEIQTFEN-----------FFEVLTLIKQHKNELI-IVNT 122
Cdd:cd02648 83 ASGSDQPLEGErltASYF----HGRDGLSgvhwlhPDFTPVETWIPEIvapltpsdkpaYDVILDILREEPDHTVtIAAL 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446438822 123 GRLTSLATLFLLYGDVMEYVHSYYIMGGAFLYPGNVTPIAEANFYGDPGSANIVMRYA----------KNLSIYPLNVTq 192
Cdd:cd02648 159 GPLTNLAAAARKDPETFAKVGEVVVMGGAIDVPGNTSPVAEFNCFADPYAAAVVIDEPpstapearrkLPLQVFPLDIT- 237
|
250
....*....|.
gi 446438822 193 saivTPEMVNY 203
Cdd:cd02648 238 ----TGHTLPY 244
|
|
| nuc_hydro_CjNH |
cd02654 |
nuc_hydro_CjNH. Nucleoside hydrolases similar to Campylobacter jejuni nucleoside hydrolase. ... |
7-247 |
6.80e-14 |
|
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: 71.05 E-value: 6.80e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446438822 7 FFGDFGIDDTIAIIYAHLTDKIDVIGIVADYGNVPKAEVVRNVRFLLKSVGKEYIKVFGGAEHSMSSEA------ETFYP 80
Cdd:cd02654 8 IAMGRDTDDGLALALLLWSPEVELLGLSAVSGNCWLSAVTYNVLRMLELAGADAIPVYAGANTPLGRTNrafhawESLYG 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446438822 81 EVHGKFGIGPIY----PGLEIQTFENF---FEVLTLIKQHKNELIIVNTGRLTSLATLFLLYGDVMEYVHSYYIMGGAFL 153
Cdd:cd02654 88 AYLWQGAWSPEYsdmyTNASIIRNASIpaaLFMIEMVRKHPHEVSIVAAGPLTNLALALRIDPDFAPLAKELVIMGGYLD 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446438822 154 YPGN-VTPI--AEANFYGDPGSANIVMRYAKNLSIYPLNVTQSAIVTPEmvnyihskgKTKFLKPLLDYYYYQFYQK--- 227
Cdd:cd02654 168 DIGEfVNRHyaSDFNLIMDPEAASIVLTAPWKSITIPGNVTNRTCLTPE---------QIKADDPLRDFIRETLDLPidy 238
|
250 260
....*....|....*....|....
gi 446438822 228 ---KVPGIQGSPVHDALTL-IAIN 247
Cdd:cd02654 239 akeFVGTGDGLPMWDELASaVALD 262
|
|
| nuc_hydro_TvIAG |
cd02647 |
nuc_hydro_ TvIAG: Nucleoside hydrolases similar to the Inosine-adenosine-guanosine-preferring ... |
3-201 |
1.53e-09 |
|
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: 58.20 E-value: 1.53e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446438822 3 KKILFFGDFGIDDTIAIIYAHLTDKID-----VIGIVADYGNVPKAEVVRNVRFLLKS-----VGK-EYIKV--FGGAEH 69
Cdd:cd02647 1 KNVIFDHDGNVDDLVALLLLLKNEKVDlkgigVSGIDADCYVEPAVSVTRKLIDRLGQrdaipVGKgGSRAVnpFPRSWR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446438822 70 SMSSEAETFYPEVHGKFGIGPIYPGLEIQtfenffEVLT-LIKQHKNELIIVNTGRLTSLATLFLLYGDVMEYVHSYYIM 148
Cdd:cd02647 81 RDAAFSVDHLPILNERYTVETPLAEETAQ------LVLIeKIKASLEPVTLLVTGPLTNLARALDSDPDISSNIEEVYIM 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 446438822 149 GGAFLYPGNV-----TPIAEANFYGDPGSANIVMRYAKNLSIYPLNVTQSAIVTPEMV 201
Cdd:cd02647 155 GGGVDAPGNVftppsNGTAEFNIFWDPLAAKTVFDSGLKITLVPLDATNTVPLTREFL 212
|
|
| nuc_hydro_2 |
cd02652 |
NH_2: A subgroup of nucleoside hydrolases. This group contains eukaryotic and bacterial ... |
5-193 |
1.62e-03 |
|
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: 39.41 E-value: 1.62e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446438822 5 ILFFGDFG--IDDTIAIIYAHLTDKIDVIGIVADYGNV-PKAEVVRNVRFLLK---SVGKEYIKVFGGAEHSMSSEAETF 78
Cdd:cd02652 1 LILDTDIGgdPDDALALALAHALQKCDLLAVTITLADAsARRAIDAVNRFYGRgdiPIGADYHGWPEDAKDHAKFLLEGD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446438822 79 ypEVHGKFGIGPIYPgleiqtfeNFFEVL--TLIKQHKNELIIVNTGRLTSLATLFLLYGD-------VMEYVHSYYIMG 149
Cdd:cd02652 81 --RLHHDLESAEDAL--------DAVKALrrLLASAEDASVTIVSIGPLTNLAALLDADADpltgpelVRQKVKRLVVMG 150
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 446438822 150 GAFLYPGNVTPIAEANFYGDPGSANIVMRYAKNLSIyPLNVTQS 193
Cdd:cd02652 151 GAFYDPDGNVQHREYNFVTDPKAAQRVAGRAQHLGI-PVRIVWS 193
|
|
| PTZ00313 |
PTZ00313 |
inosine-adenosine-guanosine-nucleoside hydrolase; Provisional |
109-201 |
2.25e-03 |
|
inosine-adenosine-guanosine-nucleoside hydrolase; Provisional
Pssm-ID: 140334 [Multi-domain] Cd Length: 326 Bit Score: 39.08 E-value: 2.25e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446438822 109 LIKQHKNELIIVNTGRLTSLATLFLLYGDVM-EYVHSYYIMGGAFLYPGNV-----TPIAEANFYGDPGSANIVMRYA-- 180
Cdd:PTZ00313 124 LVMSSPEKVTICVTGPLSNVAWCIEKYGEEFtKKVEECVIMGGAVDVGGNVflpgtDGSAEWNIYWDPPAAKTVLMCPhi 203
|
90 100
....*....|....*....|.
gi 446438822 181 KNLsIYPLNVTQSAIVTPEMV 201
Cdd:PTZ00313 204 RKV-LFSLDSTNSVPVTSEVV 223
|
|
| PI-PLCc_Rv2075c_like |
cd08590 |
Catalytic domain of uncharacterized Mycobacterium tuberculosis Rv2075c-like proteins; This ... |
119-204 |
3.47e-03 |
|
Catalytic domain of uncharacterized Mycobacterium tuberculosis Rv2075c-like proteins; This subfamily corresponds to the catalytic domain present in uncharacterized Mycobacterium tuberculosis Rv2075c and its homologs. Members in this family are more closely related to the Streptomyces antibioticus phosphatidylinositol-specific phospholipase C1(SaPLC1)-like proteins rather than the typical bacterial phosphatidylinositol-specific phospholipase C (PI-PLC, EC 4.6.1.13), which participate in Ca2+-independent PI metabolism, hydrolyzing the membrane lipid phosphatidylinositol (PI) to produce phosphorylated myo-inositol and diacylglycerol (DAG). In contrast, SaPLC1-like proteins have two Ca2+-chelating amino acid substitutions which convert them to metal-dependent bacterial PI-PLC. Rv2075c and its homologs have the same amino acid substitutions as well, which might suggest they have metal-dependent PI-PLC activity.
Pssm-ID: 176532 Cd Length: 267 Bit Score: 38.54 E-value: 3.47e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446438822 119 IVNTGRLTSLATLFLLYGDVMEYVHSYYimggAFLYPGNVTPIAEANFYgdPGSANIVMRYAK---NLSIYPLNVTQsAI 195
Cdd:cd08590 158 MLNSGKQVVLATGGGCSGAQGMYNRKEF----ADTQPSNFRPYPECAFA--MGNNTSLVRVYEdstNYSSAAGDPGG-PF 230
|
....*....
gi 446438822 196 VTPEMVNYI 204
Cdd:cd08590 231 KNGNILNAM 239
|
|
| |
