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Conserved domains on  [gi|1024336669|ref|NP_001311297|]
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adenosine deaminase-like protein isoform 2 [Homo sapiens]

Protein Classification

adenosine deaminase( domain architecture ID 10087349)

adenosine deaminase (ADA) catalyzes the zinc dependent irreversible deamination of adenosine nucleosides to inosine nucleosides and ammonia

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
ADA_AMPD cd00443
Adenosine/AMP deaminase. Adenosine deaminases (ADAs) are present in pro- and eukaryotic ...
 18-257 9.33e-70

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: 217.22  E-value: 9.33e-70
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024336669  18 LPKVELHAHLNGSISSHTMKKLIAQkpdlkihdqmtvidkgkkrtleECFQMFQTIHQLTSSPEDILMVTKDVIKEFADD 97
Cdd:cd00443     1 LPKVELHAHLSGSISPETLLELIKK----------------------EFFEKFLLVHNLLQKGEALARALKEVIEEFAED 58

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024336669  98 GVKYLELRSTPR-RENATGMTKKTYVESILEGIKQSKQENLDIDVRYLIAVDRRGGP----LVAKETVKLAEEFFLsteg 172
Cdd:cd00443    59 NVQYLELRTTPRlLETEKGLTKEQYWLLVIEGISEAKQWFPPIKVRLILSVDRRGPYvqnyLVASEILELAKFLSN---- 134

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024336669 173 TVLGLDLSGDPTVG--QAKDFLEPLLEAKKAG-LKLALHLSEIPNQKKETQiLLDLLPDRIGHGTFLNSGEggslDLVDF 249
Cdd:cd00443   135 YVVGIDLVGDESKGenPLRDFYSYYEYARRLGlLGLTLHCGETGNREELLQ-ALLLLPDRIGHGIFLLKHP----ELIYL 209


                  ....*...
gi 1024336669 250 VRQHRIPL 257
Cdd:cd00443   210 VKLRNIPI 217
 
Name Accession Description Interval E-value
ADA_AMPD cd00443
Adenosine/AMP deaminase. Adenosine deaminases (ADAs) are present in pro- and eukaryotic ...
 18-257 9.33e-70

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: 217.22  E-value: 9.33e-70
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024336669  18 LPKVELHAHLNGSISSHTMKKLIAQkpdlkihdqmtvidkgkkrtleECFQMFQTIHQLTSSPEDILMVTKDVIKEFADD 97
Cdd:cd00443     1 LPKVELHAHLSGSISPETLLELIKK----------------------EFFEKFLLVHNLLQKGEALARALKEVIEEFAED 58

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024336669  98 GVKYLELRSTPR-RENATGMTKKTYVESILEGIKQSKQENLDIDVRYLIAVDRRGGP----LVAKETVKLAEEFFLsteg 172
Cdd:cd00443    59 NVQYLELRTTPRlLETEKGLTKEQYWLLVIEGISEAKQWFPPIKVRLILSVDRRGPYvqnyLVASEILELAKFLSN---- 134

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024336669 173 TVLGLDLSGDPTVG--QAKDFLEPLLEAKKAG-LKLALHLSEIPNQKKETQiLLDLLPDRIGHGTFLNSGEggslDLVDF 249
Cdd:cd00443   135 YVVGIDLVGDESKGenPLRDFYSYYEYARRLGlLGLTLHCGETGNREELLQ-ALLLLPDRIGHGIFLLKHP----ELIYL 209


                  ....*...
gi 1024336669 250 VRQHRIPL 257
Cdd:cd00443   210 VKLRNIPI 217
PRK09358 PRK09358
adenosine deaminase; Provisional
 13-257 4.16e-31

adenosine deaminase; Provisional


Pssm-ID: 236480  Cd Length: 340  Bit Score: 117.97  E-value: 4.16e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024336669  13 DFYSELPKVELHAHLNGSISSHTMKKLiAQKPDLKIHDQmTVIDKGKKRTLEEC--FQMFQTIHQLTSS----PEDILMV 86
Cdd:PRK09358    5 MIIRSLPKAELHLHLDGSLRPETILEL-ARRNGIALPAT-DVEELPWVRAAYDFrdLQSFLDKYDAGVAvlqtEEDLRRL 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024336669  87 TKDVIKEFADDGVKYLELRSTPRRENATGMTKKTYVESILEGIKQSKQEnLDIDVRYLIAVDRRGG-PLVAKETVKLAEE 165
Cdd:PRK09358   83 AFEYLEDAAADGVVYAEIRFDPQLHTERGLPLEEVVEAVLDGLRAAEAE-FGISVRLILCFMRHFGeEAAARELEALAAR 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024336669 166 FFlstEGTVLGLDLSGDPTVGQAKDFLEPLLEAKKAGLKLALHLSE--IPNQKKETqilLDLL-PDRIGHGTFLNsgegG 242
Cdd:PRK09358  162 YR---DDGVVGFDLAGDELGFPPSKFARAFDRARDAGLRLTAHAGEagGPESIWEA---LDELgAERIGHGVRAI----E 231

                         250
                  ....*....|....*
gi 1024336669 243 SLDLVDFVRQHRIPL 257
Cdd:PRK09358  232 DPALMARLADRRIPL 246
Add COG1816
Adenosine deaminase [Nucleotide transport and metabolism]; Adenosine deaminase is part of the ...
 19-257 8.16e-31

Adenosine deaminase [Nucleotide transport and metabolism]; Adenosine deaminase is part of the Pathway/BioSystem: Menaquinone biosynthesis


Pssm-ID: 441421  Cd Length: 326  Bit Score: 116.72  E-value: 8.16e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024336669  19 PKVELHAHLNGSISSHTMKKLIAQKP-DLKIHDQMTVIDKGKKRTLEECFQMFQTIHQLTSSPEDILMVTKDVIKEFADD 97
Cdd:COG1816     1 PKAELHLHLEGSLRPETLLELAARNGiDLPAADVEELRAAYDFRDLQSFLDTYDAGAAVLQTEEDFRRLAYEYLEDAAAD 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024336669  98 GVKYLELRSTPrrENAT--GMTKKTYVESILEGIKQSKQEnLDIDVRYLIAVDRRGGPLVAKETVKLAEEFflsTEGTVL 175
Cdd:COG1816    81 GVRYAEIRFDP--QLHTrrGLSLEEVVEAVLDGLREAERE-FGISVRLILCALRHLSPEAAFETLELALRY---RDRGVV 154

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024336669 176 GLDLSGDPTVGQAKDFLEPLLEAKKAGLKLALHLSE------IpnqkkeTQILLDLLPDRIGHGTflNSGEggSLDLVDF 249
Cdd:COG1816   155 GFGLAGDERGFPPEKFAEAFARAREAGLHLTAHAGEaggpesI------WEALDLLGAERIGHGV--RAIE--DPALVAR 224


                  ....*...
gi 1024336669 250 VRQHRIPL 257
Cdd:COG1816   225 LADRGIPL 232
A_deaminase pfam00962
Adenosine deaminase;
19-257 6.69e-29

Adenosine deaminase;


Pssm-ID: 425964  Cd Length: 330  Bit Score: 111.75  E-value: 6.69e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024336669  19 PKVELHAHLNGSISSHTMKKLiAQKPDLKIHDQM--TVIDKGKKRTLEECFQMFQTIH----QLTSSPEDILMVTKDVIK 92
Cdd:pfam00962   1 PKAELHLHLDGSLRPDTLLEL-AKRYGIILPADFpeALEPLFRKYKKERDLQDFLDKYdigvAVLRSPEDIRRLAFEYAE 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024336669  93 EFADDGVKYLELRSTPRRENATGMTKKTYVESILEGIKQSKQEnLDIDVRYLIAVDRRGGPLVAKETVKLAEEFflsTEG 172
Cdd:pfam00962  80 DVAKDGVVYAEVRYDPQSHASRGLSPDTVVDAVLDAVDAAERE-FGITVRLIVCAMRHEHPECSREIAELAPRY---RDQ 155

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024336669 173 TVLGLDLSGDPTV---GQAKDFLEPLLEAKKAGLKLALHLSEIPNQKKETQILLDLLPDRIGHGTflNSGEGGSldLVDF 249
Cdd:pfam00962 156 GIVAFGLAGDEKGfppSLFRDHVEAFARARDAGLHLTVHAGEAGGPQSVWEALDDLGAERIGHGV--RSAEDPR--LLDR 231


                  ....*...
gi 1024336669 250 VRQHRIPL 257
Cdd:pfam00962 232 LADRQIPL 239
aden_deam TIGR01430
adenosine deaminase; This family includes the experimentally verified adenosine deaminases of ...
 18-257 6.89e-29

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: 111.68  E-value: 6.89e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024336669  18 LPKVELHAHLNGSISSHTMKKLiAQKPDLKIHDQMTVIDKGKKR-TLEECFQMFQTIH----QLTSSPEDILMVTKDVIK 92
Cdd:TIGR01430   1 LPKAELHLHLEGSIRPETLLEL-AQKNGIPLPADLQSGEELKEAyDKFRDLQDFLAKYdfgvEVLRTEDDFKRLAYEYVE 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024336669  93 EFADDGVKYLELRSTPRRENATGMTKKTYVESILEGIKQSKQEnLDIDVRYLIAVDRRGGPLVAKETVKLAEEFflsTEG 172
Cdd:TIGR01430  80 KAAKDGVVYAEVFFDPQLHTNRGISPDTVVEAVLDGLDEAERD-FGIKSRLILCGMRHKQPEAAEETLELAKPY---KEQ 155

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024336669 173 TVLGLDLSGDPTVGQAKDFLEPLLEAKKAGLKLALHLSEIPNQKKETQILLDLLPDRIGHGTFLNSGEggslDLVDFVRQ 252
Cdd:TIGR01430 156 TIVGFGLAGDERGGPPPDFVRAFAIARELGLHLTVHAGELGGPESVREALDDLGATRIGHGVRALEDP----ELLKRLAQ 231


                  ....*
gi 1024336669 253 HRIPL 257
Cdd:TIGR01430 232 ENITL 236
 
Name Accession Description Interval E-value
ADA_AMPD cd00443
Adenosine/AMP deaminase. Adenosine deaminases (ADAs) are present in pro- and eukaryotic ...
 18-257 9.33e-70

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: 217.22  E-value: 9.33e-70
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024336669  18 LPKVELHAHLNGSISSHTMKKLIAQkpdlkihdqmtvidkgkkrtleECFQMFQTIHQLTSSPEDILMVTKDVIKEFADD 97
Cdd:cd00443     1 LPKVELHAHLSGSISPETLLELIKK----------------------EFFEKFLLVHNLLQKGEALARALKEVIEEFAED 58

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024336669  98 GVKYLELRSTPR-RENATGMTKKTYVESILEGIKQSKQENLDIDVRYLIAVDRRGGP----LVAKETVKLAEEFFLsteg 172
Cdd:cd00443    59 NVQYLELRTTPRlLETEKGLTKEQYWLLVIEGISEAKQWFPPIKVRLILSVDRRGPYvqnyLVASEILELAKFLSN---- 134

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024336669 173 TVLGLDLSGDPTVG--QAKDFLEPLLEAKKAG-LKLALHLSEIPNQKKETQiLLDLLPDRIGHGTFLNSGEggslDLVDF 249
Cdd:cd00443   135 YVVGIDLVGDESKGenPLRDFYSYYEYARRLGlLGLTLHCGETGNREELLQ-ALLLLPDRIGHGIFLLKHP----ELIYL 209


                  ....*...
gi 1024336669 250 VRQHRIPL 257
Cdd:cd00443   210 VKLRNIPI 217
ADA cd01320
Adenosine deaminase (ADA) is a monomeric zinc dependent enzyme which catalyzes the ...
 17-257 3.17e-37

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: 133.87  E-value: 3.17e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024336669  17 ELPKVELHAHLNGSISSHTMKKLIAQK----PDLKIHDQMTVIDKGKKRTLEECFQMFQTIHQLTSSPEDILMVTKDVIK 92
Cdd:cd01320     1 NLPKAELHLHLDGSLRPETILELAKKNgitlPASDVELLELVVAAYNFSDLQDFLAKYDFGLSVLQTEEDFERLAYEYLE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024336669  93 EFADDGVKYLELRSTPRRENATGMTKKTYVESILEGIKQSKqENLDIDVRYLIAVDRRGGPLVAKETVKLAEEFflsTEG 172
Cdd:cd01320    81 DAAADGVVYAEIRFSPQLHTRRGLSFDEVVEAVLRGLDEAE-AEFGIKARLILCGLRHLSPESAQETLELALKY---RDK 156

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024336669 173 TVLGLDLSGDPTVGQAKDFLEPLLEAKKAGLKLALHLSEIPNQKKETQILLDLLPDRIGHGTFLnsgeGGSLDLVDFVRQ 252
Cdd:cd01320   157 GVVGFDLAGDEVGFPPEKFVRAFQRAREAGLRLTAHAGEAGGPESVRDALDLLGAERIGHGIRA----IEDPELVKRLAE 232


                  ....*
gi 1024336669 253 HRIPL 257
Cdd:cd01320   233 RNIPL 237
PRK09358 PRK09358
adenosine deaminase; Provisional
 13-257 4.16e-31

adenosine deaminase; Provisional


Pssm-ID: 236480  Cd Length: 340  Bit Score: 117.97  E-value: 4.16e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024336669  13 DFYSELPKVELHAHLNGSISSHTMKKLiAQKPDLKIHDQmTVIDKGKKRTLEEC--FQMFQTIHQLTSS----PEDILMV 86
Cdd:PRK09358    5 MIIRSLPKAELHLHLDGSLRPETILEL-ARRNGIALPAT-DVEELPWVRAAYDFrdLQSFLDKYDAGVAvlqtEEDLRRL 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024336669  87 TKDVIKEFADDGVKYLELRSTPRRENATGMTKKTYVESILEGIKQSKQEnLDIDVRYLIAVDRRGG-PLVAKETVKLAEE 165
Cdd:PRK09358   83 AFEYLEDAAADGVVYAEIRFDPQLHTERGLPLEEVVEAVLDGLRAAEAE-FGISVRLILCFMRHFGeEAAARELEALAAR 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024336669 166 FFlstEGTVLGLDLSGDPTVGQAKDFLEPLLEAKKAGLKLALHLSE--IPNQKKETqilLDLL-PDRIGHGTFLNsgegG 242
Cdd:PRK09358  162 YR---DDGVVGFDLAGDELGFPPSKFARAFDRARDAGLRLTAHAGEagGPESIWEA---LDELgAERIGHGVRAI----E 231

                         250
                  ....*....|....*
gi 1024336669 243 SLDLVDFVRQHRIPL 257
Cdd:PRK09358  232 DPALMARLADRRIPL 246
Add COG1816
Adenosine deaminase [Nucleotide transport and metabolism]; Adenosine deaminase is part of the ...
 19-257 8.16e-31

Adenosine deaminase [Nucleotide transport and metabolism]; Adenosine deaminase is part of the Pathway/BioSystem: Menaquinone biosynthesis


Pssm-ID: 441421  Cd Length: 326  Bit Score: 116.72  E-value: 8.16e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024336669  19 PKVELHAHLNGSISSHTMKKLIAQKP-DLKIHDQMTVIDKGKKRTLEECFQMFQTIHQLTSSPEDILMVTKDVIKEFADD 97
Cdd:COG1816     1 PKAELHLHLEGSLRPETLLELAARNGiDLPAADVEELRAAYDFRDLQSFLDTYDAGAAVLQTEEDFRRLAYEYLEDAAAD 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024336669  98 GVKYLELRSTPrrENAT--GMTKKTYVESILEGIKQSKQEnLDIDVRYLIAVDRRGGPLVAKETVKLAEEFflsTEGTVL 175
Cdd:COG1816    81 GVRYAEIRFDP--QLHTrrGLSLEEVVEAVLDGLREAERE-FGISVRLILCALRHLSPEAAFETLELALRY---RDRGVV 154

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024336669 176 GLDLSGDPTVGQAKDFLEPLLEAKKAGLKLALHLSE------IpnqkkeTQILLDLLPDRIGHGTflNSGEggSLDLVDF 249
Cdd:COG1816   155 GFGLAGDERGFPPEKFAEAFARAREAGLHLTAHAGEaggpesI------WEALDLLGAERIGHGV--RAIE--DPALVAR 224


                  ....*...
gi 1024336669 250 VRQHRIPL 257
Cdd:COG1816   225 LADRGIPL 232
A_deaminase pfam00962
Adenosine deaminase;
19-257 6.69e-29

Adenosine deaminase;


Pssm-ID: 425964  Cd Length: 330  Bit Score: 111.75  E-value: 6.69e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024336669  19 PKVELHAHLNGSISSHTMKKLiAQKPDLKIHDQM--TVIDKGKKRTLEECFQMFQTIH----QLTSSPEDILMVTKDVIK 92
Cdd:pfam00962   1 PKAELHLHLDGSLRPDTLLEL-AKRYGIILPADFpeALEPLFRKYKKERDLQDFLDKYdigvAVLRSPEDIRRLAFEYAE 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024336669  93 EFADDGVKYLELRSTPRRENATGMTKKTYVESILEGIKQSKQEnLDIDVRYLIAVDRRGGPLVAKETVKLAEEFflsTEG 172
Cdd:pfam00962  80 DVAKDGVVYAEVRYDPQSHASRGLSPDTVVDAVLDAVDAAERE-FGITVRLIVCAMRHEHPECSREIAELAPRY---RDQ 155

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024336669 173 TVLGLDLSGDPTV---GQAKDFLEPLLEAKKAGLKLALHLSEIPNQKKETQILLDLLPDRIGHGTflNSGEGGSldLVDF 249
Cdd:pfam00962 156 GIVAFGLAGDEKGfppSLFRDHVEAFARARDAGLHLTVHAGEAGGPQSVWEALDDLGAERIGHGV--RSAEDPR--LLDR 231


                  ....*...
gi 1024336669 250 VRQHRIPL 257
Cdd:pfam00962 232 LADRQIPL 239
aden_deam TIGR01430
adenosine deaminase; This family includes the experimentally verified adenosine deaminases of ...
 18-257 6.89e-29

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: 111.68  E-value: 6.89e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024336669  18 LPKVELHAHLNGSISSHTMKKLiAQKPDLKIHDQMTVIDKGKKR-TLEECFQMFQTIH----QLTSSPEDILMVTKDVIK 92
Cdd:TIGR01430   1 LPKAELHLHLEGSIRPETLLEL-AQKNGIPLPADLQSGEELKEAyDKFRDLQDFLAKYdfgvEVLRTEDDFKRLAYEYVE 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024336669  93 EFADDGVKYLELRSTPRRENATGMTKKTYVESILEGIKQSKQEnLDIDVRYLIAVDRRGGPLVAKETVKLAEEFflsTEG 172
Cdd:TIGR01430  80 KAAKDGVVYAEVFFDPQLHTNRGISPDTVVEAVLDGLDEAERD-FGIKSRLILCGMRHKQPEAAEETLELAKPY---KEQ 155

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024336669 173 TVLGLDLSGDPTVGQAKDFLEPLLEAKKAGLKLALHLSEIPNQKKETQILLDLLPDRIGHGTFLNSGEggslDLVDFVRQ 252
Cdd:TIGR01430 156 TIVGFGLAGDERGGPPPDFVRAFAIARELGLHLTVHAGELGGPESVREALDDLGATRIGHGVRALEDP----ELLKRLAQ 231


                  ....*
gi 1024336669 253 HRIPL 257
Cdd:TIGR01430 232 ENITL 236
ADGF cd01321
Adenosine deaminase-related growth factors (ADGF), a novel family of secreted growth-factors ...
 23-233 2.23e-07

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: 51.12  E-value: 2.23e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024336669  23 LHAHLNGSISSHTMKKLIAQKPDlkihdqmtvidkgkkrtleecfQMFQTIHQL-TSSPedilmVTKDVI----KEFADD 97
Cdd:cd01321    30 LHVHDTAMVSSDWLIKNATYRFE----------------------QIFDIIDGLlTYLP-----IFRDYYrrllEELYED 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024336669  98 GVKYLELRSTPRRENATGMTKKTYVES--ILEGIKQS-KQENLD-IDVRYLIAVDRRGGPLVAKETVKLAEEFFLSTEGT 173
Cdd:cd01321    83 NVQYVELRSSFSPLYDLDGREYDYEETvqLLEEVVEKfKKTHPDfIGLKIIYATLRNFNDSEIKESMEQCLNLKKKFPDF 162

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1024336669 174 VLGLDLSGDPTVGQA-KDFLEPLLEAKK--AGLKLALHLSEIPNQKKETQI-LLD-LLPD--RIGHG 233
Cdd:cd01321   163 IAGFDLVGQEDAGRPlLDFLPQLLWFPKqcAEIPFFFHAGETNGDGTETDEnLVDaLLLNtkRIGHG 229
PTZ00124 PTZ00124
adenosine deaminase; Provisional
 15-257 9.40e-07

adenosine deaminase; Provisional


Pssm-ID: 173415  Cd Length: 362  Bit Score: 49.09  E-value: 9.40e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024336669  15 YSELPKVELHAHLNGSISshtMKKLIAQKPDLKIHDQMT---VID----KGKKRTLEECFQMFQTIHQLTSSPEDILMVT 87
Cdd:PTZ00124   32 WKRIPKCELHCHLDLCFS---VDFFLSCIRKYNLQPNLSdeeILDyylfAKGGKSLGEFVEKAIRVADIFNDYEVIEDLA 108

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024336669  88 KDVIKEFADDGVKYLELRSTPR-RENATGMTKKTYVESILEGIKQSKQEnldIDVRYLIAVDRRGGPLVAKETVKLAEEF 166
Cdd:PTZ00124  109 KHAVFNKYKEGVVLMEFRYSPTfVAFKHNLDIDLIHQAIVKGIKEAVEL---LDHKIEVGLLCIGDTGHDAAPIKESADF 185

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024336669 167 FLSTEGTVLGLDLSGDPTvgQAKDFLEPLLEAKKAGLKLALHLSE---IPNQKKETQILLDLLPDRIGHGTFLNSgeggS 243
Cdd:PTZ00124  186 CLKHKADFVGFDHAGHEV--DLKPFKDIFDYVREAGVNLTVHAGEdvtLPNLNTLYSAIQVLKVKRIGHGIRVAE----S 259

                         250
                  ....*....|....
gi 1024336669 244 LDLVDFVRQHRIPL 257
Cdd:PTZ00124  260 QELIDMVKEKDILL 273
archeal_chlorohydrolases cd01305
Predicted chlorohydrolases. These metallo-dependent hydrolases from archea are part of the ...
 97-257 4.25e-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: 4.25e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024336669  97 DGVKYLELRSTPRRENATGMtKKT--------------YVESILEGIKQSKQENLDIDVRYLIAVDRRGGPLVAKETVKL 162
Cdd:cd01305    35 DGLKHRLLAQADDRELAEAM-RKVlrdmretgigafadFREGGVEGIELLRRALGKLPVPFEVILGRPTEPDDPEILLEV 113

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024336669 163 AEefflstegtvlGLDLSG--DPtvgqakDFLEPLLEAKKAGLKLALHLSEIPNQKKETQI--LLDLLPDRIGHGTFLNS 238
Cdd:cd01305   114 AD-----------GLGLSSanDV------DLEDILELLRRRGKLFAIHASETRESVGMTDIerALDLEPDLLVHGTHLTD 176

                         170
                  ....*....|....*....
gi 1024336669 239 GEggsldlVDFVRQHRIPL 257
Cdd:cd01305   177 ED------LELVRENGVPV 189
Amidohydro_1 pfam01979
Amidohydrolase family; This family of enzymes are a a large metal dependent hydrolase ...
 112-257 5.55e-04

Amidohydrolase family; This family of enzymes are a a large metal dependent hydrolase superfamily. The family includes Adenine deaminase EC:3.5.4.2 that hydrolyses adenine to form hypoxanthine and ammonia. Adenine deaminases reaction is important for adenine utilization as a purine and also as a nitrogen source. This family also includes dihydroorotase and N-acetylglucosamine-6-phosphate deacetylases, EC:3.5.1.25 These enzymes catalyze the reaction N-acetyl-D-glucosamine 6-phosphate + H2O <=> D-glucosamine 6-phosphate + acetate. This family includes the catalytic domain of urease alpha subunit. Dihydroorotases (EC:3.5.2.3) are also included.


Pssm-ID: 460401 [Multi-domain]  Cd Length: 334  Bit Score: 40.56  E-value: 5.55e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024336669 112 NATGMTKKTYVESILEGIkqskqENLDIDVRYLIAV-------DRRGGPLVAKETVKLAE-EFFLSTEGTVLGLDLSGDP 183
Cdd:pfam01979  48 LDMGATTSTGIEALLEAA-----EELPLGLRFLGPGcsldtdgELEGRKALREKLKAGAEfIKGMADGVVFVGLAPHGAP 122

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1024336669 184 TVGqaKDFLEPLLE-AKKAGLKLALHLSEipnQKKETQILLDLLPDRIGHGTFL-NSGEGGSLDLVDFVRQHRIPL 257
Cdd:pfam01979 123 TFS--DDELKAALEeAKKYGLPVAIHALE---TKGEVEDAIAAFGGGIEHGTHLeVAESGGLLDIIKLILAHGVHL 193
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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