|
Name |
Accession |
Description |
Interval |
E-value |
| Add |
COG1816 |
Adenosine deaminase [Nucleotide transport and metabolism]; Adenosine deaminase is part of the ... |
36-334 |
6.58e-58 |
|
Adenosine deaminase [Nucleotide transport and metabolism]; Adenosine deaminase is part of the Pathway/BioSystem: Menaquinone biosynthesis
Pssm-ID: 441421 Cd Length: 326 Bit Score: 190.30 E-value: 6.58e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489200611 36 ELHVHMNGAIPVSTIQDiLADEL-TELPSGFLIErdLLRHTPCQSLASYL----TPWQVLRlfpkKRENLDRLSLAVVTS 110
Cdd:COG1816 4 ELHLHLEGSLRPETLLE-LAARNgIDLPAADVEE--LRAAYDFRDLQSFLdtydAGAAVLQ----TEEDFRRLAYEYLED 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489200611 111 LAENNVRFVELRSSvLYLATLQNCSPTQALERLIESSRAASDLFGMRLGLILTVTRGDYSSVGLSALLQAYQNLGepDEV 190
Cdd:COG1816 77 AAADGVRYAEIRFD-PQLHTRRGLSLEEVVEAVLDGLREAEREFGISVRLILCALRHLSPEAAFETLELALRYRD--RGV 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489200611 191 VGLDLAGDEEIAHPAELPSLFRKAKDRfGLGITIHAGETGRVDNVRAAVELFGADRIGHGTAASKDPHLLDLLAKQDICV 270
Cdd:COG1816 154 VGFGLAGDERGFPPEKFAEAFARAREA-GLHLTAHAGEAGGPESIWEALDLLGAERIGHGVRAIEDPALVARLADRGIPL 232
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 489200611 271 EVCPISNRLTGAVPVDEAHPLLEFRRHQVPFVICSDNPAIHQRGLADDHTTAMIE-GLSASDIYE 334
Cdd:COG1816 233 EVCPTSNVQLGVVPSLAEHPLRRLLDAGVRVTLNTDDPLYFGTTLTDEYELAAEAfGLSDADLAQ 297
|
|
| ADA |
cd01320 |
Adenosine deaminase (ADA) is a monomeric zinc dependent enzyme which catalyzes the ... |
36-332 |
8.64e-55 |
|
Adenosine deaminase (ADA) is a monomeric zinc dependent enzyme which catalyzes the irreversible hydrolytic deamination of both adenosine, as well as desoxyadenosine, to ammonia and inosine or desoxyinosine, respectively. ADA plays an important role in the purine pathway. Low, as well as high levels of ADA activity have been linked to several diseases.
Pssm-ID: 238645 Cd Length: 325 Bit Score: 182.02 E-value: 8.64e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489200611 36 ELHVHMNGAIPVSTIQDILADELTELPSGFLIERDLLR-HTPCQSLASYLT----PWQVLRlfpkKRENLDRLSLAVVTS 110
Cdd:cd01320 6 ELHLHLDGSLRPETILELAKKNGITLPASDVELLELVVaAYNFSDLQDFLAkydfGLSVLQ----TEEDFERLAYEYLED 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489200611 111 LAENNVRFVELRSSVLyLATLQNCSPTQALERLIESSRAASDLFGMRLGLILTVTRGDYSSVGLSALLQA--YQNLGepd 188
Cdd:cd01320 82 AAADGVVYAEIRFSPQ-LHTRRGLSFDEVVEAVLRGLDEAEAEFGIKARLILCGLRHLSPESAQETLELAlkYRDKG--- 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489200611 189 eVVGLDLAGDEEIAHPAELPSLFRKAKDRfGLGITIHAGETGRVDNVRAAVELFGADRIGHGTAASKDPHLLDLLAKQDI 268
Cdd:cd01320 158 -VVGFDLAGDEVGFPPEKFVRAFQRAREA-GLRLTAHAGEAGGPESVRDALDLLGAERIGHGIRAIEDPELVKRLAERNI 235
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 489200611 269 CVEVCPISNRLTGAVPVDEAHPLLEFRRHQVPFVICSDNPAIHQRGLADDHT-TAMIEGLSASDI 332
Cdd:cd01320 236 PLEVCPTSNVQTGAVKSLAEHPLRELLDAGVKVTINTDDPTVFGTYLTDEYElLAEAFGLTEEEL 300
|
|
| PRK09358 |
PRK09358 |
adenosine deaminase; Provisional |
36-334 |
1.34e-54 |
|
adenosine deaminase; Provisional
Pssm-ID: 236480 Cd Length: 340 Bit Score: 182.30 E-value: 1.34e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489200611 36 ELHVHMNGAIPVSTIQDILADELTELPSgFLIE--RDLLRHTPCQSLASYLTPW----QVLRlfpkKRENLDRLSLAVVT 109
Cdd:PRK09358 14 ELHLHLDGSLRPETILELARRNGIALPA-TDVEelPWVRAAYDFRDLQSFLDKYdagvAVLQ----TEEDLRRLAFEYLE 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489200611 110 SLAENNVRFVELRSSVlYLATLQNCSPTQALERLIESSRAASDLFGMRLGLILTVTRG---DYSSVGLSALLQAYQnlge 186
Cdd:PRK09358 89 DAAADGVVYAEIRFDP-QLHTERGLPLEEVVEAVLDGLRAAEAEFGISVRLILCFMRHfgeEAAARELEALAARYR---- 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489200611 187 PDEVVGLDLAGDEEIAHPAELPSLFRKAKDRfGLGITIHAGETGRVDNVRAAVELFGADRIGHGTAASKDPHLLDLLAKQ 266
Cdd:PRK09358 164 DDGVVGFDLAGDELGFPPSKFARAFDRARDA-GLRLTAHAGEAGGPESIWEALDELGAERIGHGVRAIEDPALMARLADR 242
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 489200611 267 DICVEVCPISNRLTGAVPVDEAHPLLEFRRHQVPFVICSDNPAIHQRGLADDHTTAMIE-GLSASDIYE 334
Cdd:PRK09358 243 RIPLEVCPTSNVQTGAVPSLAEHPLKTLLDAGVRVTINTDDPLVFGTTLTEEYEALAEAfGLSDEDLAQ 311
|
|
| A_deaminase |
pfam00962 |
Adenosine deaminase; |
36-322 |
3.23e-43 |
|
Adenosine deaminase;
Pssm-ID: 425964 Cd Length: 330 Bit Score: 152.20 E-value: 3.23e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489200611 36 ELHVHMNGAIPVSTIQDILADELTELPSGFL-IERDLLR-HTPCQSLASYLTPWQVLRLFPKKRENLDRLSLAVVTSLAE 113
Cdd:pfam00962 4 ELHLHLDGSLRPDTLLELAKRYGIILPADFPeALEPLFRkYKKERDLQDFLDKYDIGVAVLRSPEDIRRLAFEYAEDVAK 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489200611 114 NNVRFVELRSSVLYLATLQnCSPTQALERLIESSRAASDLFGMRLGLILTVTR--GDYSSVGLSALLQAYQNLGepdeVV 191
Cdd:pfam00962 84 DGVVYAEVRYDPQSHASRG-LSPDTVVDAVLDAVDAAEREFGITVRLIVCAMRheHPECSREIAELAPRYRDQG----IV 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489200611 192 GLDLAGDEeIAHPaelPSLFRKAKDRF------GLGITIHAGETGRVDNVRAAVELFGADRIGHGTAASKDPHLLDLLAK 265
Cdd:pfam00962 159 AFGLAGDE-KGFP---PSLFRDHVEAFarardaGLHLTVHAGEAGGPQSVWEALDDLGAERIGHGVRSAEDPRLLDRLAD 234
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 489200611 266 QDICVEVCPISNRLTGAVPVDEAHPLLEFRRHQVPFVICSDNPAIHQRGLADDHTTA 322
Cdd:pfam00962 235 RQIPLEICPTSNVQTGAVASLAEHPLKTFLRAGVPVSLNTDDPLMFGSDLLDEYQVA 291
|
|
| aden_deam |
TIGR01430 |
adenosine deaminase; This family includes the experimentally verified adenosine deaminases of ... |
36-322 |
6.16e-43 |
|
adenosine deaminase; This family includes the experimentally verified adenosine deaminases of mammals and E. coli. Other members of this family are predicted also to be adenosine deaminase, an enzyme of nucleotide degradation. This family is distantly related to AMP deaminase.
Pssm-ID: 273619 Cd Length: 324 Bit Score: 151.36 E-value: 6.16e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489200611 36 ELHVHMNGAIPVSTI------QDI-LADELTELpsgfliERDLLRHTPCQSLASYLTPWQVLRLFPKKRENLDRLSLAVV 108
Cdd:TIGR01430 5 ELHLHLEGSIRPETLlelaqkNGIpLPADLQSG------EELKEAYDKFRDLQDFLAKYDFGVEVLRTEDDFKRLAYEYV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489200611 109 TSLAENNVRFVELRSSVlYLATLQNCSPTQALERLIESSRAASDLFGMRLGLILTVTRGDYSSVGLSALLQA--YQNLGe 186
Cdd:TIGR01430 79 EKAAKDGVVYAEVFFDP-QLHTNRGISPDTVVEAVLDGLDEAERDFGIKSRLILCGMRHKQPEAAEETLELAkpYKEQT- 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489200611 187 pdeVVGLDLAGDEEIAHPAELPSLFRKAKDRfGLGITIHAGETGRVDNVRAAVELFGADRIGHGTAASKDPHLLDLLAKQ 266
Cdd:TIGR01430 157 ---IVGFGLAGDERGGPPPDFVRAFAIAREL-GLHLTVHAGELGGPESVREALDDLGATRIGHGVRALEDPELLKRLAQE 232
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 489200611 267 DICVEVCPISNRLTGAVPVDEAHPLLEFRRHQVPFVICSDNPAIHQRGLADDHTTA 322
Cdd:TIGR01430 233 NITLEVCPTSNVALGVVKSLAEHPLRRFLEAGVKVTLNSDDPAYFGSYLTEEYEIA 288
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| Add |
COG1816 |
Adenosine deaminase [Nucleotide transport and metabolism]; Adenosine deaminase is part of the ... |
36-334 |
6.58e-58 |
|
Adenosine deaminase [Nucleotide transport and metabolism]; Adenosine deaminase is part of the Pathway/BioSystem: Menaquinone biosynthesis
Pssm-ID: 441421 Cd Length: 326 Bit Score: 190.30 E-value: 6.58e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489200611 36 ELHVHMNGAIPVSTIQDiLADEL-TELPSGFLIErdLLRHTPCQSLASYL----TPWQVLRlfpkKRENLDRLSLAVVTS 110
Cdd:COG1816 4 ELHLHLEGSLRPETLLE-LAARNgIDLPAADVEE--LRAAYDFRDLQSFLdtydAGAAVLQ----TEEDFRRLAYEYLED 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489200611 111 LAENNVRFVELRSSvLYLATLQNCSPTQALERLIESSRAASDLFGMRLGLILTVTRGDYSSVGLSALLQAYQNLGepDEV 190
Cdd:COG1816 77 AAADGVRYAEIRFD-PQLHTRRGLSLEEVVEAVLDGLREAEREFGISVRLILCALRHLSPEAAFETLELALRYRD--RGV 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489200611 191 VGLDLAGDEEIAHPAELPSLFRKAKDRfGLGITIHAGETGRVDNVRAAVELFGADRIGHGTAASKDPHLLDLLAKQDICV 270
Cdd:COG1816 154 VGFGLAGDERGFPPEKFAEAFARAREA-GLHLTAHAGEAGGPESIWEALDLLGAERIGHGVRAIEDPALVARLADRGIPL 232
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 489200611 271 EVCPISNRLTGAVPVDEAHPLLEFRRHQVPFVICSDNPAIHQRGLADDHTTAMIE-GLSASDIYE 334
Cdd:COG1816 233 EVCPTSNVQLGVVPSLAEHPLRRLLDAGVRVTLNTDDPLYFGTTLTDEYELAAEAfGLSDADLAQ 297
|
|
| ADA |
cd01320 |
Adenosine deaminase (ADA) is a monomeric zinc dependent enzyme which catalyzes the ... |
36-332 |
8.64e-55 |
|
Adenosine deaminase (ADA) is a monomeric zinc dependent enzyme which catalyzes the irreversible hydrolytic deamination of both adenosine, as well as desoxyadenosine, to ammonia and inosine or desoxyinosine, respectively. ADA plays an important role in the purine pathway. Low, as well as high levels of ADA activity have been linked to several diseases.
Pssm-ID: 238645 Cd Length: 325 Bit Score: 182.02 E-value: 8.64e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489200611 36 ELHVHMNGAIPVSTIQDILADELTELPSGFLIERDLLR-HTPCQSLASYLT----PWQVLRlfpkKRENLDRLSLAVVTS 110
Cdd:cd01320 6 ELHLHLDGSLRPETILELAKKNGITLPASDVELLELVVaAYNFSDLQDFLAkydfGLSVLQ----TEEDFERLAYEYLED 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489200611 111 LAENNVRFVELRSSVLyLATLQNCSPTQALERLIESSRAASDLFGMRLGLILTVTRGDYSSVGLSALLQA--YQNLGepd 188
Cdd:cd01320 82 AAADGVVYAEIRFSPQ-LHTRRGLSFDEVVEAVLRGLDEAEAEFGIKARLILCGLRHLSPESAQETLELAlkYRDKG--- 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489200611 189 eVVGLDLAGDEEIAHPAELPSLFRKAKDRfGLGITIHAGETGRVDNVRAAVELFGADRIGHGTAASKDPHLLDLLAKQDI 268
Cdd:cd01320 158 -VVGFDLAGDEVGFPPEKFVRAFQRAREA-GLRLTAHAGEAGGPESVRDALDLLGAERIGHGIRAIEDPELVKRLAERNI 235
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 489200611 269 CVEVCPISNRLTGAVPVDEAHPLLEFRRHQVPFVICSDNPAIHQRGLADDHT-TAMIEGLSASDI 332
Cdd:cd01320 236 PLEVCPTSNVQTGAVKSLAEHPLRELLDAGVKVTINTDDPTVFGTYLTDEYElLAEAFGLTEEEL 300
|
|
| PRK09358 |
PRK09358 |
adenosine deaminase; Provisional |
36-334 |
1.34e-54 |
|
adenosine deaminase; Provisional
Pssm-ID: 236480 Cd Length: 340 Bit Score: 182.30 E-value: 1.34e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489200611 36 ELHVHMNGAIPVSTIQDILADELTELPSgFLIE--RDLLRHTPCQSLASYLTPW----QVLRlfpkKRENLDRLSLAVVT 109
Cdd:PRK09358 14 ELHLHLDGSLRPETILELARRNGIALPA-TDVEelPWVRAAYDFRDLQSFLDKYdagvAVLQ----TEEDLRRLAFEYLE 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489200611 110 SLAENNVRFVELRSSVlYLATLQNCSPTQALERLIESSRAASDLFGMRLGLILTVTRG---DYSSVGLSALLQAYQnlge 186
Cdd:PRK09358 89 DAAADGVVYAEIRFDP-QLHTERGLPLEEVVEAVLDGLRAAEAEFGISVRLILCFMRHfgeEAAARELEALAARYR---- 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489200611 187 PDEVVGLDLAGDEEIAHPAELPSLFRKAKDRfGLGITIHAGETGRVDNVRAAVELFGADRIGHGTAASKDPHLLDLLAKQ 266
Cdd:PRK09358 164 DDGVVGFDLAGDELGFPPSKFARAFDRARDA-GLRLTAHAGEAGGPESIWEALDELGAERIGHGVRAIEDPALMARLADR 242
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 489200611 267 DICVEVCPISNRLTGAVPVDEAHPLLEFRRHQVPFVICSDNPAIHQRGLADDHTTAMIE-GLSASDIYE 334
Cdd:PRK09358 243 RIPLEVCPTSNVQTGAVPSLAEHPLKTLLDAGVRVTINTDDPLVFGTTLTEEYEALAEAfGLSDEDLAQ 311
|
|
| A_deaminase |
pfam00962 |
Adenosine deaminase; |
36-322 |
3.23e-43 |
|
Adenosine deaminase;
Pssm-ID: 425964 Cd Length: 330 Bit Score: 152.20 E-value: 3.23e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489200611 36 ELHVHMNGAIPVSTIQDILADELTELPSGFL-IERDLLR-HTPCQSLASYLTPWQVLRLFPKKRENLDRLSLAVVTSLAE 113
Cdd:pfam00962 4 ELHLHLDGSLRPDTLLELAKRYGIILPADFPeALEPLFRkYKKERDLQDFLDKYDIGVAVLRSPEDIRRLAFEYAEDVAK 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489200611 114 NNVRFVELRSSVLYLATLQnCSPTQALERLIESSRAASDLFGMRLGLILTVTR--GDYSSVGLSALLQAYQNLGepdeVV 191
Cdd:pfam00962 84 DGVVYAEVRYDPQSHASRG-LSPDTVVDAVLDAVDAAEREFGITVRLIVCAMRheHPECSREIAELAPRYRDQG----IV 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489200611 192 GLDLAGDEeIAHPaelPSLFRKAKDRF------GLGITIHAGETGRVDNVRAAVELFGADRIGHGTAASKDPHLLDLLAK 265
Cdd:pfam00962 159 AFGLAGDE-KGFP---PSLFRDHVEAFarardaGLHLTVHAGEAGGPQSVWEALDDLGAERIGHGVRSAEDPRLLDRLAD 234
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 489200611 266 QDICVEVCPISNRLTGAVPVDEAHPLLEFRRHQVPFVICSDNPAIHQRGLADDHTTA 322
Cdd:pfam00962 235 RQIPLEICPTSNVQTGAVASLAEHPLKTFLRAGVPVSLNTDDPLMFGSDLLDEYQVA 291
|
|
| aden_deam |
TIGR01430 |
adenosine deaminase; This family includes the experimentally verified adenosine deaminases of ... |
36-322 |
6.16e-43 |
|
adenosine deaminase; This family includes the experimentally verified adenosine deaminases of mammals and E. coli. Other members of this family are predicted also to be adenosine deaminase, an enzyme of nucleotide degradation. This family is distantly related to AMP deaminase.
Pssm-ID: 273619 Cd Length: 324 Bit Score: 151.36 E-value: 6.16e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489200611 36 ELHVHMNGAIPVSTI------QDI-LADELTELpsgfliERDLLRHTPCQSLASYLTPWQVLRLFPKKRENLDRLSLAVV 108
Cdd:TIGR01430 5 ELHLHLEGSIRPETLlelaqkNGIpLPADLQSG------EELKEAYDKFRDLQDFLAKYDFGVEVLRTEDDFKRLAYEYV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489200611 109 TSLAENNVRFVELRSSVlYLATLQNCSPTQALERLIESSRAASDLFGMRLGLILTVTRGDYSSVGLSALLQA--YQNLGe 186
Cdd:TIGR01430 79 EKAAKDGVVYAEVFFDP-QLHTNRGISPDTVVEAVLDGLDEAERDFGIKSRLILCGMRHKQPEAAEETLELAkpYKEQT- 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489200611 187 pdeVVGLDLAGDEEIAHPAELPSLFRKAKDRfGLGITIHAGETGRVDNVRAAVELFGADRIGHGTAASKDPHLLDLLAKQ 266
Cdd:TIGR01430 157 ---IVGFGLAGDERGGPPPDFVRAFAIAREL-GLHLTVHAGELGGPESVREALDDLGATRIGHGVRALEDPELLKRLAQE 232
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 489200611 267 DICVEVCPISNRLTGAVPVDEAHPLLEFRRHQVPFVICSDNPAIHQRGLADDHTTA 322
Cdd:TIGR01430 233 NITLEVCPTSNVALGVVKSLAEHPLRRFLEAGVKVTLNSDDPAYFGSYLTEEYEIA 288
|
|
| ADA_AMPD |
cd00443 |
Adenosine/AMP deaminase. Adenosine deaminases (ADAs) are present in pro- and eukaryotic ... |
35-347 |
2.30e-42 |
|
Adenosine/AMP deaminase. Adenosine deaminases (ADAs) are present in pro- and eukaryotic organisms and catalyze the zinc dependent irreversible deamination of adenosine nucleosides to inosine nucleosides and ammonia. The eukaryotic AMP deaminase catalyzes a similar reaction leading to the hydrolytic removal of an amino group at the 6 position of the adenine nucleotide ring, a branch point in the adenylate catabolic pathway.
Pssm-ID: 238250 Cd Length: 305 Bit Score: 149.03 E-value: 2.30e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489200611 35 GELHVHMNGAIPVSTIQDiladeltelpsgfLIERDLLRhtpcqslaSYLTPWQVLRlfpkKRENLDRLSLAVVTSLAEN 114
Cdd:cd00443 4 VELHAHLSGSISPETLLE-------------LIKKEFFE--------KFLLVHNLLQ----KGEALARALKEVIEEFAED 58
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489200611 115 NVRFVELRSSVLYLATLQNCSPTQALERLIESSRAASDLF-GMRLGLILTV-TRGDYSSVGLSALLQAYQNLGEPDEVVG 192
Cdd:cd00443 59 NVQYLELRTTPRLLETEKGLTKEQYWLLVIEGISEAKQWFpPIKVRLILSVdRRGPYVQNYLVASEILELAKFLSNYVVG 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489200611 193 LDLAGDEEIaHPAELPSL---FRKAKDRFGLGITIHAGETGRVDNVRAAVeLFGADRIGHGTAASKDPHLLDLLAKQDIC 269
Cdd:cd00443 139 IDLVGDESK-GENPLRDFysyYEYARRLGLLGLTLHCGETGNREELLQAL-LLLPDRIGHGIFLLKHPELIYLVKLRNIP 216
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 489200611 270 VEVCPISNRLTGAVPVDEAHPLLEFRRHQVPFVICSDNPAIHQRGLADD-HTTAMIEGLSASDIYEQFDVAKRYSFIEG 347
Cdd:cd00443 217 IEVCPTSNVVLGTVQSYEKHPFMRFFKAGLPVSLSTDDPGIFGTSLSEEySLAAKTFGLTFEDLCELNRNSVLSSFAKD 295
|
|
| ADGF |
cd01321 |
Adenosine deaminase-related growth factors (ADGF), a novel family of secreted growth-factors ... |
28-318 |
1.31e-32 |
|
Adenosine deaminase-related growth factors (ADGF), a novel family of secreted growth-factors with sequence similarty to adenosine deaminase.
Pssm-ID: 238646 Cd Length: 345 Bit Score: 124.31 E-value: 1.31e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489200611 28 EFSKLYR--------GELHVHMNGAipVSTiqDILADELTE-LPSGFLIERDLLRHTPcqSLASYLtpWQVLRLFpkkre 98
Cdd:cd01321 13 ENSTLFKiiqkmpkgALLHVHDTAM--VSS--DWLIKNATYrFEQIFDIIDGLLTYLP--IFRDYY--RRLLEEL----- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489200611 99 nldrlslavvtslAENNVRFVELRSSVLYLATLQNCSPT-----QALERLIESSRAA-SDLFGMRLglILTVTRG-DYSS 171
Cdd:cd01321 80 -------------YEDNVQYVELRSSFSPLYDLDGREYDyeetvQLLEEVVEKFKKThPDFIGLKI--IYATLRNfNDSE 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489200611 172 VGLSalLQAYQNLGE--PDEVVGLDLAGDEEIAHPAE--LPSLFRKAKDRFGLGITIHAGET----GRVD-NVRAAVeLF 242
Cdd:cd01321 145 IKES--MEQCLNLKKkfPDFIAGFDLVGQEDAGRPLLdfLPQLLWFPKQCAEIPFFFHAGETngdgTETDeNLVDAL-LL 221
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 489200611 243 GADRIGHGTAASKDPHLLDLLAKQDICVEVCPISNRLTGAVPVDEAHPLLEFRRHQVPFVICSDNPAI-HQRGLADD 318
Cdd:cd01321 222 NTKRIGHGFALPKHPLLMDLVKKKNIAIEVCPISNQVLGLVSDLRNHPAAALLARGVPVVISSDDPGFwGAKGLSHD 298
|
|
| adm_rel |
TIGR01431 |
adenosine deaminase-related growth factor; Members of this family have been described as ... |
113-309 |
1.88e-21 |
|
adenosine deaminase-related growth factor; Members of this family have been described as secreted proteins with growth factor activity and regions of adenosine deaminase homology in insects, mollusks, and vertebrates.
Pssm-ID: 273620 [Multi-domain] Cd Length: 479 Bit Score: 94.86 E-value: 1.88e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489200611 113 ENNVRFVELRSSVLYLATLQNCSPT------QALERLIESSRAASDLFGMRLglILTVTRGDySSVGLSALLQAYQNLGE 186
Cdd:TIGR01431 208 EDNVQYMELRSRLFPLYELSGTHHDeewsvkTYKEVTEKFVEEHPDFIGIKI--IYSDLRSK-DVEEIAEYIKMAMGLRI 284
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489200611 187 --PDEVVGLDLAGDEEIAHPAE--LPSLFRKAkDRFGLGITIHAGET----GRVD-NVRAAVeLFGADRIGHGTAASKDP 257
Cdd:TIGR01431 285 kyPDFVAGFDLVGQEDTGHSLLdyKDALLIPS-IGVKLPYFFHAGETnwqgTSVDrNLLDAL-LLNTTRIGHGFALSKHP 362
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 489200611 258 HLLDLLAKQDICVEVCPISNRLTGAVPVDEAHPLLEFRRHQVPFVICSDNPA 309
Cdd:TIGR01431 363 AVRTYSKERDIPIEVCPISNQVLKLVSDLRNHPVATLMADNYPMVISSDDPA 414
|
|
| PTZ00124 |
PTZ00124 |
adenosine deaminase; Provisional |
31-319 |
9.35e-19 |
|
adenosine deaminase; Provisional
Pssm-ID: 173415 Cd Length: 362 Bit Score: 86.07 E-value: 9.35e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489200611 31 KLYRGELHVHMNGAIPVSTIQDILADeLTELPSgfLIERDLLRHTPC----QSLASYLTPWQVLRLFPKKRENLDRLSLA 106
Cdd:PTZ00124 34 RIPKCELHCHLDLCFSVDFFLSCIRK-YNLQPN--LSDEEILDYYLFakggKSLGEFVEKAIRVADIFNDYEVIEDLAKH 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489200611 107 VVTSLAENNVRFVELRSSVLYLATLQNCSPTQALERLIESSRAASDLFGMRLGL-ILTVTRGDYSSVGLSALLQAYqnLG 185
Cdd:PTZ00124 111 AVFNKYKEGVVLMEFRYSPTFVAFKHNLDIDLIHQAIVKGIKEAVELLDHKIEVgLLCIGDTGHDAAPIKESADFC--LK 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489200611 186 EPDEVVGLDLAGdeeiaHPAELP---SLFRKAKDRfGLGITIHAGETGRVDNVR---AAVELFGADRIGHGTAASKDPHL 259
Cdd:PTZ00124 189 HKADFVGFDHAG-----HEVDLKpfkDIFDYVREA-GVNLTVHAGEDVTLPNLNtlySAIQVLKVKRIGHGIRVAESQEL 262
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 489200611 260 LDLLAKQDICVEVCPISNRLTGAVPVDEAHPLLEFRRHQVPFVICSDNPAIHQRGLADDH 319
Cdd:PTZ00124 263 IDMVKEKDILLEVCPISNVLLNNAKSMDTHPIRKLYDAGVKVSVNSDDPGMFLTNINDDY 322
|
|
| metallo-dependent_hydrolases |
cd01292 |
Superfamily of metallo-dependent hydrolases (also called amidohydrolase superfamily) is a ... |
97-310 |
1.78e-10 |
|
Superfamily of metallo-dependent hydrolases (also called amidohydrolase superfamily) is a large group of proteins that show conservation in their 3-dimensional fold (TIM barrel) and in details of their active site. The vast majority of the members have a conserved metal binding site, involving four histidines and one aspartic acid residue. In the common reaction mechanism, the metal ion (or ions) deprotonate a water molecule for a nucleophilic attack on the substrate. The family includes urease alpha, adenosine deaminase, phosphotriesterase dihydroorotases, allantoinases, hydantoinases, AMP-, adenine and cytosine deaminases, imidazolonepropionase, aryldialkylphosphatase, chlorohydrolases, formylmethanofuran dehydrogenases and others.
Pssm-ID: 238617 [Multi-domain] Cd Length: 275 Bit Score: 60.81 E-value: 1.78e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489200611 97 RENLDRLSLAVVTSLAENNVRFVELRSSvlylatlqNCSPTQALERLIESSRAASDLFGMRLGLILTVTRGDYSSVGLS- 175
Cdd:cd01292 30 PEDLYEDTLRALEALLAGGVTTVVDMGS--------TPPPTTTKAAIEAVAEAARASAGIRVVLGLGIPGVPAAVDEDAe 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489200611 176 ALLQAYQNLGEPDEVVGLDLAGDEEiAHPAELPSLFRKAK--DRFGLGITIHAGET----GRVDNVRAAVELFGADRIGH 249
Cdd:cd01292 102 ALLLELLRRGLELGAVGLKLAGPYT-ATGLSDESLRRVLEeaRKLGLPVVIHAGELpdptRALEDLVALLRLGGRVVIGH 180
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 489200611 250 GTAAskDPHLLDLLAKQDICVEVCPISNRLTGAVPVDeAHPLLEFRRHQVPFVICSDNPAI 310
Cdd:cd01292 181 VSHL--DPELLELLKEAGVSLEVCPLSNYLLGRDGEG-AEALRRLLELGIRVTLGTDGPPH 238
|
|
| SsnA |
COG0402 |
Cytosine/adenosine deaminase or related metal-dependent hydrolase [Nucleotide transport and ... |
208-309 |
1.58e-05 |
|
Cytosine/adenosine deaminase or related metal-dependent hydrolase [Nucleotide transport and metabolism, General function prediction only]; Cytosine/adenosine deaminase or related metal-dependent hydrolase is part of the Pathway/BioSystem: Pyrimidine salvage
Pssm-ID: 440171 [Multi-domain] Cd Length: 416 Bit Score: 46.36 E-value: 1.58e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489200611 208 PSLFRKAKD---RFGLGITIHAGETgrVDNVRAAVELFGA------DRIG---------HGTAAskDPHLLDLLAKQDIC 269
Cdd:COG0402 201 PELLRAAAAlarELGLPLHTHLAET--RDEVEWVLELYGKrpveylDELGllgprtllaHCVHL--TDEEIALLAETGAS 276
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 489200611 270 VEVCPISNRLTGavpvDEAHPLLEFRRHQVPFVICSDNPA 309
Cdd:COG0402 277 VAHCPTSNLKLG----SGIAPVPRLLAAGVRVGLGTDGAA 312
|
|
| archeal_chlorohydrolases |
cd01305 |
Predicted chlorohydrolases. These metallo-dependent hydrolases from archea are part of the ... |
184-307 |
6.78e-05 |
|
Predicted chlorohydrolases. These metallo-dependent hydrolases from archea are part of the superfamily of metallo-dependent hydrolases, a large group of proteins that show conservation in their 3-dimensional fold (TIM barrel) and in details of their active site. They have a conserved metal binding site, involving four histidines and one aspartic acid residue. In the common reaction mechanism, the metal ion (or ions) deprotonate a water molecule for a nucleophilic attack on the substrate. Some members of this subgroup are predicted to be chlorohyrolases.
Pssm-ID: 238630 [Multi-domain] Cd Length: 263 Bit Score: 43.93 E-value: 6.78e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489200611 184 LGEPDEVVGLD--LAGDEEIAHPAE----LPSLFRKAKDRFGLgITIHAGETGRV---DNVRAAVELfGADRIGHGTAAS 254
Cdd:cd01305 98 LGRPTEPDDPEilLEVADGLGLSSAndvdLEDILELLRRRGKL-FAIHASETRESvgmTDIERALDL-EPDLLVHGTHLT 175
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 489200611 255 KDPhlLDLLAKQDICVEVCPISNRLTGA-VPvdeahPLLEFRRHQVPFVICSDN 307
Cdd:cd01305 176 DED--LELVRENGVPVVLCPRSNLYFGVgIP-----PVAELLKLGIKVLLGTDN 222
|
|
| ATZ_TRZ_like |
cd01298 |
TRZ/ATZ family contains enzymes from the atrazine degradation pathway and related hydrolases. ... |
208-309 |
1.19e-03 |
|
TRZ/ATZ family contains enzymes from the atrazine degradation pathway and related hydrolases. Atrazine, a chlorinated herbizide, can be catabolized by a variety of different bacteria. The first three steps of the atrazine dehalogenation pathway are catalyzed by atrazine chlorohydrolase (AtzA), hydroxyatrazine ethylaminohydrolase (AtzB), and N-isopropylammelide N-isopropylaminohydrolase (AtzC). All three enzymes belong to the superfamily of metal dependent hydrolases. AtzA and AtzB, beside other related enzymes are represented in this CD.
Pssm-ID: 238623 [Multi-domain] Cd Length: 411 Bit Score: 40.65 E-value: 1.19e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489200611 208 PSLFRKAK---DRFGLGITIHAGETgrVDNVRAAVELFG------ADRIG---------HGTAAskDPHLLDLLAKQDIC 269
Cdd:cd01298 193 DELLREVAelaREYGVPLHIHLAET--EDEVEESLEKYGkrpveyLEELGllgpdvvlaHCVWL--TDEEIELLAETGTG 268
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 489200611 270 VEVCPISN-RLTGAVPvdeahPLLEFRRHQVPFVICSDNPA 309
Cdd:cd01298 269 VAHNPASNmKLASGIA-----PVPEMLEAGVNVGLGTDGAA 304
|
|
| DRE_TIM_metallolyase |
cd03174 |
DRE-TIM metallolyase superfamily; The DRE-TIM metallolyase superfamily includes ... |
85-253 |
2.78e-03 |
|
DRE-TIM metallolyase superfamily; The DRE-TIM metallolyase superfamily includes 2-isopropylmalate synthase (IPMS), alpha-isopropylmalate synthase (LeuA), 3-hydroxy-3-methylglutaryl-CoA lyase, homocitrate synthase, citramalate synthase, 4-hydroxy-2-oxovalerate aldolase, re-citrate synthase, transcarboxylase 5S, pyruvate carboxylase, AksA, and FrbC. These members all share a conserved triose-phosphate isomerase (TIM) barrel domain consisting of a core beta(8)-alpha(8) motif with the eight parallel beta strands forming an enclosed barrel surrounded by eight alpha helices. The domain has a catalytic center containing a divalent cation-binding site formed by a cluster of invariant residues that cap the core of the barrel. In addition, the catalytic site includes three invariant residues - an aspartate (D), an arginine (R), and a glutamate (E) - which is the basis for the domain name "DRE-TIM".
Pssm-ID: 163674 [Multi-domain] Cd Length: 265 Bit Score: 38.98 E-value: 2.78e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489200611 85 TPWQVLRLFPKKRENldrlslAVVTSLAENNVRFVEL-------------RSSVLYLATLQNCSPTQALERLIESSRAAS 151
Cdd:cd03174 52 DDWEVLRAIRKLVPN------VKLQALVRNREKGIERaleagvdevrifdSASETHSRKNLNKSREEDLENAEEAIEAAK 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489200611 152 DLfGMRLGLIL-TVTRGDYSSVGLSALLQAYQNLGePDEVVGLDLAGdeeIAHPAELPSLFRKAKDRFG-LGITIHA--- 226
Cdd:cd03174 126 EA-GLEVEGSLeDAFGCKTDPEYVLEVAKALEEAG-ADEISLKDTVG---LATPEEVAELVKALREALPdVPLGLHThnt 200
|
170 180
....*....|....*....|....*..
gi 489200611 227 GETGrVDNVRAAVELfGADRIgHGTAA 253
Cdd:cd03174 201 LGLA-VANSLAALEA-GADRV-DGSVN 224
|
|
| PHP_HisPPase_Hisj_like |
cd12110 |
Polymerase and Histidinol Phosphatase domain of Histidinol phosphate phosphatase of Hisj like; ... |
233-306 |
5.11e-03 |
|
Polymerase and Histidinol Phosphatase domain of Histidinol phosphate phosphatase of Hisj like; Bacillus subtilis YtvP HisJ has strong histidinol phosphate phosphatase (HisPPase) activity. The PHP (also called histidinol phosphatase-2/HIS2) domain is associated with several types of DNA polymerases, such as PolIIIA and family X DNA polymerases, stand alone histidinol phosphate phosphatases (HisPPases), and a number of uncharacterized protein families. HisPPase catalyzes the eighth step of histidine biosynthesis, in which L-histidinol phosphate undergoes dephosphorylation to produce histidinol. The PHP domain has four conserved sequence motifs and contains an invariant histidine that is involved in metal ion coordination. The PHP domain of HisPPase is structurally homologous to other members of the PHP family that have a distorted (beta/alpha)7 barrel fold with a trinuclear metal site on the C-terminal side of the barrel.
Pssm-ID: 213994 [Multi-domain] Cd Length: 244 Bit Score: 37.93 E-value: 5.11e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489200611 233 DNVRAAVELFGADRIGH-------GTAASKDPHL-------LDLLAKQDICVEVcpisNrlTGAV--PVDEAHPLLEF-- 294
Cdd:cd12110 141 DLVEKAIESGLFDIIGHpdlikkfGKNDEPDEDYeelieriLRAIAEAGVALEI----N--TAGLrkPVGEPYPSPEFle 214
|
90
....*....|....
gi 489200611 295 --RRHQVPFVICSD 306
Cdd:cd12110 215 laKELGIPVTLGSD 228
|
|
| PRK07213 |
PRK07213 |
chlorohydrolase; Provisional |
192-307 |
5.67e-03 |
|
chlorohydrolase; Provisional
Pssm-ID: 235969 [Multi-domain] Cd Length: 375 Bit Score: 38.48 E-value: 5.67e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489200611 192 GLDLAGDEEIAHpaELPSLFRKAKDRFGLGITIHAGE-----------TGRVDNVRAAVELFGADRIGHGTAASKDPhlL 260
Cdd:PRK07213 167 GIGLSGANEYSD--EELKFICKECKREKKIFSIHAAEhkgsveyslekYGMTEIERLINLGFKPDFIVHATHPSNDD--L 242
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 489200611 261 DLLAKQDICVEVCPISN-RLTGAVPvdeahPLLEFRRHQVPFVICSDN 307
Cdd:PRK07213 243 ELLKENNIPVVVCPRANaSFNVGLP-----PLNEMLEKGILLGIGTDN 285
|
|
| |
