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Conserved domains on  [gi|555038087|gb|ESL82402|]
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adenosine deaminase [Enterobacter roggenkampii]

Protein Classification

adenosine deaminase family protein( domain architecture ID 10013192)

adenosine deaminase family protein such as adenosine deaminase, which catalyzes the zinc-dependent irreversible hydrolytic deamination of adenosine as well as desoxyadenosine, to ammonia and inosine or desoxyinosine, respectively

CATH:  3.20.20.140
EC:  3.5.4.-
Gene Ontology:  GO:0008270
PubMed:  11223861
SCOP:  4003205

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
PRK09358 PRK09358
adenosine deaminase; Provisional
1-333 9.80e-157

adenosine deaminase; Provisional


:

Pssm-ID: 236480  Cd Length: 340  Bit Score: 442.31  E-value: 9.80e-157
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555038087   1 MIDTRLPLTDIHRHLDGNIRAQTILDLGRQFNLTLPAQTLESLIPhVQVTSNEPDLVSFLSKLDWGVKMLASLDACRRVA 80
Cdd:PRK09358   5 MIIRSLPKAELHLHLDGSLRPETILELARRNGIALPATDVEELPW-VRAAYDFRDLQSFLDKYDAGVAVLQTEEDLRRLA 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555038087  81 FENIEDAARNGLHYVELRFSPGYMAMtHNLPVAGVVEAVIEGVREGCKTFDVQARLIGIMSRTFGEAACLQELEALLA-- 158
Cdd:PRK09358  84 FEYLEDAAADGVVYAEIRFDPQLHTE-RGLPLEEVVEAVLDGLRAAEAEFGISVRLILCFMRHFGEEAAARELEALAAry 162
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555038087 159 HRDAITAVDLAGDELGFPGSLFLSHFNRARDAGWHITVHAGEAAGPESIWQAIRELGAERIGHGVKAVEDRALMDFLAEQ 238
Cdd:PRK09358 163 RDDGVVGFDLAGDELGFPPSKFARAFDRARDAGLRLTAHAGEAGGPESIWEALDELGAERIGHGVRAIEDPALMARLADR 242
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555038087 239 RIGIESCLTSNIQTSTVATLAHHPLKTFLEHGVLASLNTDDPAVQGVDIIHEYNIAAPQAGLSREQIRQAQINGLEIAFL 318
Cdd:PRK09358 243 RIPLEVCPTSNVQTGAVPSLAEHPLKTLLDAGVRVTINTDDPLVFGTTLTEEYEALAEAFGLSDEDLAQLARNALEAAFL 322
                        330
                 ....*....|....*
gi 555038087 319 TPAEKQALRDKVATA 333
Cdd:PRK09358 323 SEEEKAALLAEVDAW 337
 
Name Accession Description Interval E-value
PRK09358 PRK09358
adenosine deaminase; Provisional
1-333 9.80e-157

adenosine deaminase; Provisional


Pssm-ID: 236480  Cd Length: 340  Bit Score: 442.31  E-value: 9.80e-157
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555038087   1 MIDTRLPLTDIHRHLDGNIRAQTILDLGRQFNLTLPAQTLESLIPhVQVTSNEPDLVSFLSKLDWGVKMLASLDACRRVA 80
Cdd:PRK09358   5 MIIRSLPKAELHLHLDGSLRPETILELARRNGIALPATDVEELPW-VRAAYDFRDLQSFLDKYDAGVAVLQTEEDLRRLA 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555038087  81 FENIEDAARNGLHYVELRFSPGYMAMtHNLPVAGVVEAVIEGVREGCKTFDVQARLIGIMSRTFGEAACLQELEALLA-- 158
Cdd:PRK09358  84 FEYLEDAAADGVVYAEIRFDPQLHTE-RGLPLEEVVEAVLDGLRAAEAEFGISVRLILCFMRHFGEEAAARELEALAAry 162
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555038087 159 HRDAITAVDLAGDELGFPGSLFLSHFNRARDAGWHITVHAGEAAGPESIWQAIRELGAERIGHGVKAVEDRALMDFLAEQ 238
Cdd:PRK09358 163 RDDGVVGFDLAGDELGFPPSKFARAFDRARDAGLRLTAHAGEAGGPESIWEALDELGAERIGHGVRAIEDPALMARLADR 242
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555038087 239 RIGIESCLTSNIQTSTVATLAHHPLKTFLEHGVLASLNTDDPAVQGVDIIHEYNIAAPQAGLSREQIRQAQINGLEIAFL 318
Cdd:PRK09358 243 RIPLEVCPTSNVQTGAVPSLAEHPLKTLLDAGVRVTINTDDPLVFGTTLTEEYEALAEAFGLSDEDLAQLARNALEAAFL 322
                        330
                 ....*....|....*
gi 555038087 319 TPAEKQALRDKVATA 333
Cdd:PRK09358 323 SEEEKAALLAEVDAW 337
A_deaminase pfam00962
Adenosine deaminase;
7-333 3.03e-149

Adenosine deaminase;


Pssm-ID: 425964  Cd Length: 330  Bit Score: 422.99  E-value: 3.03e-149
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555038087    7 PLTDIHRHLDGNIRAQTILDLGRQFNLTLPAQTLESLIPHVQVTSNEPDLVSFLSKLDWGVKMLASLDACRRVAFENIED 86
Cdd:pfam00962   1 PKAELHLHLDGSLRPDTLLELAKRYGIILPADFPEALEPLFRKYKKERDLQDFLDKYDIGVAVLRSPEDIRRLAFEYAED 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555038087   87 AARNGLHYVELRFSPGYMAMThNLPVAGVVEAVIEGVREGCKTFDVQARLIGIMSRTfGEAACLQELEALLA-HRD-AIT 164
Cdd:pfam00962  81 VAKDGVVYAEVRYDPQSHASR-GLSPDTVVDAVLDAVDAAEREFGITVRLIVCAMRH-EHPECSREIAELAPrYRDqGIV 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555038087  165 AVDLAGDELGFPGSLFLSH---FNRARDAGWHITVHAGEAAGPESIWQAIRELGAERIGHGVKAVEDRALMDFLAEQRIG 241
Cdd:pfam00962 159 AFGLAGDEKGFPPSLFRDHveaFARARDAGLHLTVHAGEAGGPQSVWEALDDLGAERIGHGVRSAEDPRLLDRLADRQIP 238
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555038087  242 IESCLTSNIQTSTVATLAHHPLKTFLEHGVLASLNTDDPAVQGVDIIHEYNIAAPQAGLSREQIRQAQINGLEIAFLTPA 321
Cdd:pfam00962 239 LEICPTSNVQTGAVASLAEHPLKTFLRAGVPVSLNTDDPLMFGSDLLDEYQVAKRAPGFDEEELARLAKNAVKGSFLPAD 318
                         330
                  ....*....|..
gi 555038087  322 EKQALRDKVATA 333
Cdd:pfam00962 319 EKRALLDEVDKV 330
Add COG1816
Adenosine deaminase [Nucleotide transport and metabolism]; Adenosine deaminase is part of the ...
7-331 1.16e-144

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


Pssm-ID: 441421  Cd Length: 326  Bit Score: 411.02  E-value: 1.16e-144
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555038087   7 PLTDIHRHLDGNIRAQTILDLGRQFNLTLPAQTLESLIPhvqvTSNEPDLVSFLSKLDWGVKMLASLDACRRVAFENIED 86
Cdd:COG1816    1 PKAELHLHLEGSLRPETLLELAARNGIDLPAADVEELRA----AYDFRDLQSFLDTYDAGAAVLQTEEDFRRLAYEYLED 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555038087  87 AARNGLHYVELRFSPgYMAMTHNLPVAGVVEAVIEGVREGCKTFDVQARLIGIMSRTFGEAACLQELEALLAHRDA-ITA 165
Cdd:COG1816   77 AAADGVRYAEIRFDP-QLHTRRGLSLEEVVEAVLDGLREAEREFGISVRLILCALRHLSPEAAFETLELALRYRDRgVVG 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555038087 166 VDLAGDELGFPGSLFLSHFNRARDAGWHITVHAGEAAGPESIWQAIRELGAERIGHGVKAVEDRALMDFLAEQRIGIESC 245
Cdd:COG1816  156 FGLAGDERGFPPEKFAEAFARAREAGLHLTAHAGEAGGPESIWEALDLLGAERIGHGVRAIEDPALVARLADRGIPLEVC 235
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555038087 246 LTSNIQTSTVATLAHHPLKTFLEHGVLASLNTDDPAVQGVDIIHEYNIAAPQAGLSREQIRQAQINGLEIAFLTPAEKQA 325
Cdd:COG1816  236 PTSNVQLGVVPSLAEHPLRRLLDAGVRVTLNTDDPLYFGTTLTDEYELAAEAFGLSDADLAQLARNAIEASFLPEEEKAA 315

                 ....*.
gi 555038087 326 LRDKVA 331
Cdd:COG1816  316 LLAELD 321
ADA cd01320
Adenosine deaminase (ADA) is a monomeric zinc dependent enzyme which catalyzes the ...
5-330 1.60e-136

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: 390.41  E-value: 1.60e-136
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555038087   5 RLPLTDIHRHLDGNIRAQTILDLGRQFNLTLPAQTLEsLIPHVQVTSNEPDLVSFLSKLDWGVKMLASLDACRRVAFENI 84
Cdd:cd01320    1 NLPKAELHLHLDGSLRPETILELAKKNGITLPASDVE-LLELVVAAYNFSDLQDFLAKYDFGLSVLQTEEDFERLAYEYL 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555038087  85 EDAARNGLHYVELRFSPGYMaMTHNLPVAGVVEAVIEGVREGCKTFDVQARLIGIMSRTFGEAACLQELEALLAHRDA-I 163
Cdd:cd01320   80 EDAAADGVVYAEIRFSPQLH-TRRGLSFDEVVEAVLRGLDEAEAEFGIKARLILCGLRHLSPESAQETLELALKYRDKgV 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555038087 164 TAVDLAGDELGFPGSLFLSHFNRARDAGWHITVHAGEAAGPESIWQAIRELGAERIGHGVKAVEDRALMDFLAEQRIGIE 243
Cdd:cd01320  159 VGFDLAGDEVGFPPEKFVRAFQRAREAGLRLTAHAGEAGGPESVRDALDLLGAERIGHGIRAIEDPELVKRLAERNIPLE 238
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555038087 244 SCLTSNIQTSTVATLAHHPLKTFLEHGVLASLNTDDPAVQGVDIIHEYNIAAPQAGLSREQIRQAQINGLEIAFLTPAEK 323
Cdd:cd01320  239 VCPTSNVQTGAVKSLAEHPLRELLDAGVKVTINTDDPTVFGTYLTDEYELLAEAFGLTEEELKKLARNAVEASFLSEEEK 318

                 ....*..
gi 555038087 324 QALRDKV 330
Cdd:cd01320  319 AELLKRI 325
aden_deam TIGR01430
adenosine deaminase; This family includes the experimentally verified adenosine deaminases of ...
6-330 2.54e-125

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: 362.06  E-value: 2.54e-125
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555038087    6 LPLTDIHRHLDGNIRAQTILDLGRQFNLTLPaQTLESLIPHVQVTSNEPDLVSFLSKLDWGVKMLASLDACRRVAFENIE 85
Cdd:TIGR01430   1 LPKAELHLHLEGSIRPETLLELAQKNGIPLP-ADLQSGEELKEAYDKFRDLQDFLAKYDFGVEVLRTEDDFKRLAYEYVE 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555038087   86 DAARNGLHYVELRFSPGYMAMTHNLPVaGVVEAVIEGVREGCKTFDVQARLIGIMSRTFGEAACLQELEALLAHRD-AIT 164
Cdd:TIGR01430  80 KAAKDGVVYAEVFFDPQLHTNRGISPD-TVVEAVLDGLDEAERDFGIKSRLILCGMRHKQPEAAEETLELAKPYKEqTIV 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555038087  165 AVDLAGDELGFPGSLFLSHFNRARDAGWHITVHAGEAAGPESIWQAIRELGAERIGHGVKAVEDRALMDFLAEQRIGIES 244
Cdd:TIGR01430 159 GFGLAGDERGGPPPDFVRAFAIARELGLHLTVHAGELGGPESVREALDDLGATRIGHGVRALEDPELLKRLAQENITLEV 238
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555038087  245 CLTSNIQTSTVATLAHHPLKTFLEHGVLASLNTDDPAVQGVDIIHEYNIAAPQAGLSREQIRQAQINGLEIAFLTPAEKQ 324
Cdd:TIGR01430 239 CPTSNVALGVVKSLAEHPLRRFLEAGVKVTLNSDDPAYFGSYLTEEYEIAAKHAGLTEEELKQLARNALEGSFLSDDEKK 318

                  ....*.
gi 555038087  325 ALRDKV 330
Cdd:TIGR01430 319 ELLAKL 324
 
Name Accession Description Interval E-value
PRK09358 PRK09358
adenosine deaminase; Provisional
1-333 9.80e-157

adenosine deaminase; Provisional


Pssm-ID: 236480  Cd Length: 340  Bit Score: 442.31  E-value: 9.80e-157
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555038087   1 MIDTRLPLTDIHRHLDGNIRAQTILDLGRQFNLTLPAQTLESLIPhVQVTSNEPDLVSFLSKLDWGVKMLASLDACRRVA 80
Cdd:PRK09358   5 MIIRSLPKAELHLHLDGSLRPETILELARRNGIALPATDVEELPW-VRAAYDFRDLQSFLDKYDAGVAVLQTEEDLRRLA 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555038087  81 FENIEDAARNGLHYVELRFSPGYMAMtHNLPVAGVVEAVIEGVREGCKTFDVQARLIGIMSRTFGEAACLQELEALLA-- 158
Cdd:PRK09358  84 FEYLEDAAADGVVYAEIRFDPQLHTE-RGLPLEEVVEAVLDGLRAAEAEFGISVRLILCFMRHFGEEAAARELEALAAry 162
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555038087 159 HRDAITAVDLAGDELGFPGSLFLSHFNRARDAGWHITVHAGEAAGPESIWQAIRELGAERIGHGVKAVEDRALMDFLAEQ 238
Cdd:PRK09358 163 RDDGVVGFDLAGDELGFPPSKFARAFDRARDAGLRLTAHAGEAGGPESIWEALDELGAERIGHGVRAIEDPALMARLADR 242
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555038087 239 RIGIESCLTSNIQTSTVATLAHHPLKTFLEHGVLASLNTDDPAVQGVDIIHEYNIAAPQAGLSREQIRQAQINGLEIAFL 318
Cdd:PRK09358 243 RIPLEVCPTSNVQTGAVPSLAEHPLKTLLDAGVRVTINTDDPLVFGTTLTEEYEALAEAFGLSDEDLAQLARNALEAAFL 322
                        330
                 ....*....|....*
gi 555038087 319 TPAEKQALRDKVATA 333
Cdd:PRK09358 323 SEEEKAALLAEVDAW 337
A_deaminase pfam00962
Adenosine deaminase;
7-333 3.03e-149

Adenosine deaminase;


Pssm-ID: 425964  Cd Length: 330  Bit Score: 422.99  E-value: 3.03e-149
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555038087    7 PLTDIHRHLDGNIRAQTILDLGRQFNLTLPAQTLESLIPHVQVTSNEPDLVSFLSKLDWGVKMLASLDACRRVAFENIED 86
Cdd:pfam00962   1 PKAELHLHLDGSLRPDTLLELAKRYGIILPADFPEALEPLFRKYKKERDLQDFLDKYDIGVAVLRSPEDIRRLAFEYAED 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555038087   87 AARNGLHYVELRFSPGYMAMThNLPVAGVVEAVIEGVREGCKTFDVQARLIGIMSRTfGEAACLQELEALLA-HRD-AIT 164
Cdd:pfam00962  81 VAKDGVVYAEVRYDPQSHASR-GLSPDTVVDAVLDAVDAAEREFGITVRLIVCAMRH-EHPECSREIAELAPrYRDqGIV 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555038087  165 AVDLAGDELGFPGSLFLSH---FNRARDAGWHITVHAGEAAGPESIWQAIRELGAERIGHGVKAVEDRALMDFLAEQRIG 241
Cdd:pfam00962 159 AFGLAGDEKGFPPSLFRDHveaFARARDAGLHLTVHAGEAGGPQSVWEALDDLGAERIGHGVRSAEDPRLLDRLADRQIP 238
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555038087  242 IESCLTSNIQTSTVATLAHHPLKTFLEHGVLASLNTDDPAVQGVDIIHEYNIAAPQAGLSREQIRQAQINGLEIAFLTPA 321
Cdd:pfam00962 239 LEICPTSNVQTGAVASLAEHPLKTFLRAGVPVSLNTDDPLMFGSDLLDEYQVAKRAPGFDEEELARLAKNAVKGSFLPAD 318
                         330
                  ....*....|..
gi 555038087  322 EKQALRDKVATA 333
Cdd:pfam00962 319 EKRALLDEVDKV 330
Add COG1816
Adenosine deaminase [Nucleotide transport and metabolism]; Adenosine deaminase is part of the ...
7-331 1.16e-144

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


Pssm-ID: 441421  Cd Length: 326  Bit Score: 411.02  E-value: 1.16e-144
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555038087   7 PLTDIHRHLDGNIRAQTILDLGRQFNLTLPAQTLESLIPhvqvTSNEPDLVSFLSKLDWGVKMLASLDACRRVAFENIED 86
Cdd:COG1816    1 PKAELHLHLEGSLRPETLLELAARNGIDLPAADVEELRA----AYDFRDLQSFLDTYDAGAAVLQTEEDFRRLAYEYLED 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555038087  87 AARNGLHYVELRFSPgYMAMTHNLPVAGVVEAVIEGVREGCKTFDVQARLIGIMSRTFGEAACLQELEALLAHRDA-ITA 165
Cdd:COG1816   77 AAADGVRYAEIRFDP-QLHTRRGLSLEEVVEAVLDGLREAEREFGISVRLILCALRHLSPEAAFETLELALRYRDRgVVG 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555038087 166 VDLAGDELGFPGSLFLSHFNRARDAGWHITVHAGEAAGPESIWQAIRELGAERIGHGVKAVEDRALMDFLAEQRIGIESC 245
Cdd:COG1816  156 FGLAGDERGFPPEKFAEAFARAREAGLHLTAHAGEAGGPESIWEALDLLGAERIGHGVRAIEDPALVARLADRGIPLEVC 235
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555038087 246 LTSNIQTSTVATLAHHPLKTFLEHGVLASLNTDDPAVQGVDIIHEYNIAAPQAGLSREQIRQAQINGLEIAFLTPAEKQA 325
Cdd:COG1816  236 PTSNVQLGVVPSLAEHPLRRLLDAGVRVTLNTDDPLYFGTTLTDEYELAAEAFGLSDADLAQLARNAIEASFLPEEEKAA 315

                 ....*.
gi 555038087 326 LRDKVA 331
Cdd:COG1816  316 LLAELD 321
ADA cd01320
Adenosine deaminase (ADA) is a monomeric zinc dependent enzyme which catalyzes the ...
5-330 1.60e-136

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: 390.41  E-value: 1.60e-136
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555038087   5 RLPLTDIHRHLDGNIRAQTILDLGRQFNLTLPAQTLEsLIPHVQVTSNEPDLVSFLSKLDWGVKMLASLDACRRVAFENI 84
Cdd:cd01320    1 NLPKAELHLHLDGSLRPETILELAKKNGITLPASDVE-LLELVVAAYNFSDLQDFLAKYDFGLSVLQTEEDFERLAYEYL 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555038087  85 EDAARNGLHYVELRFSPGYMaMTHNLPVAGVVEAVIEGVREGCKTFDVQARLIGIMSRTFGEAACLQELEALLAHRDA-I 163
Cdd:cd01320   80 EDAAADGVVYAEIRFSPQLH-TRRGLSFDEVVEAVLRGLDEAEAEFGIKARLILCGLRHLSPESAQETLELALKYRDKgV 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555038087 164 TAVDLAGDELGFPGSLFLSHFNRARDAGWHITVHAGEAAGPESIWQAIRELGAERIGHGVKAVEDRALMDFLAEQRIGIE 243
Cdd:cd01320  159 VGFDLAGDEVGFPPEKFVRAFQRAREAGLRLTAHAGEAGGPESVRDALDLLGAERIGHGIRAIEDPELVKRLAERNIPLE 238
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555038087 244 SCLTSNIQTSTVATLAHHPLKTFLEHGVLASLNTDDPAVQGVDIIHEYNIAAPQAGLSREQIRQAQINGLEIAFLTPAEK 323
Cdd:cd01320  239 VCPTSNVQTGAVKSLAEHPLRELLDAGVKVTINTDDPTVFGTYLTDEYELLAEAFGLTEEELKKLARNAVEASFLSEEEK 318

                 ....*..
gi 555038087 324 QALRDKV 330
Cdd:cd01320  319 AELLKRI 325
aden_deam TIGR01430
adenosine deaminase; This family includes the experimentally verified adenosine deaminases of ...
6-330 2.54e-125

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: 362.06  E-value: 2.54e-125
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555038087    6 LPLTDIHRHLDGNIRAQTILDLGRQFNLTLPaQTLESLIPHVQVTSNEPDLVSFLSKLDWGVKMLASLDACRRVAFENIE 85
Cdd:TIGR01430   1 LPKAELHLHLEGSIRPETLLELAQKNGIPLP-ADLQSGEELKEAYDKFRDLQDFLAKYDFGVEVLRTEDDFKRLAYEYVE 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555038087   86 DAARNGLHYVELRFSPGYMAMTHNLPVaGVVEAVIEGVREGCKTFDVQARLIGIMSRTFGEAACLQELEALLAHRD-AIT 164
Cdd:TIGR01430  80 KAAKDGVVYAEVFFDPQLHTNRGISPD-TVVEAVLDGLDEAERDFGIKSRLILCGMRHKQPEAAEETLELAKPYKEqTIV 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555038087  165 AVDLAGDELGFPGSLFLSHFNRARDAGWHITVHAGEAAGPESIWQAIRELGAERIGHGVKAVEDRALMDFLAEQRIGIES 244
Cdd:TIGR01430 159 GFGLAGDERGGPPPDFVRAFAIARELGLHLTVHAGELGGPESVREALDDLGATRIGHGVRALEDPELLKRLAQENITLEV 238
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555038087  245 CLTSNIQTSTVATLAHHPLKTFLEHGVLASLNTDDPAVQGVDIIHEYNIAAPQAGLSREQIRQAQINGLEIAFLTPAEKQ 324
Cdd:TIGR01430 239 CPTSNVALGVVKSLAEHPLRRFLEAGVKVTLNSDDPAYFGSYLTEEYEIAAKHAGLTEEELKQLARNALEGSFLSDDEKK 318

                  ....*.
gi 555038087  325 ALRDKV 330
Cdd:TIGR01430 319 ELLAKL 324
ADA_AMPD cd00443
Adenosine/AMP deaminase. Adenosine deaminases (ADAs) are present in pro- and eukaryotic ...
6-329 1.91e-45

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: 156.74  E-value: 1.91e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555038087   6 LPLTDIHRHLDGNIRAQTILDLG-RQFnltlpAQTLESLIPHVQvtsNEPDLvsflskldwgvkmlasldacRRVAFENI 84
Cdd:cd00443    1 LPKVELHAHLSGSISPETLLELIkKEF-----FEKFLLVHNLLQ---KGEAL--------------------ARALKEVI 52
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555038087  85 EDAARNGLHYVELRFSPGYMAMTHNLPVAGVVEAVIEGVREGCKTF-DVQARLIGIMSRT------FGEAACLQELEALL 157
Cdd:cd00443   53 EEFAEDNVQYLELRTTPRLLETEKGLTKEQYWLLVIEGISEAKQWFpPIKVRLILSVDRRgpyvqnYLVASEILELAKFL 132
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555038087 158 ahRDAITAVDLAGDELGFPGSL--FLSHFNRARDAGW-HITVHAGEAAGPESIWQAIrELGAERIGHGVKAVEDRALMDF 234
Cdd:cd00443  133 --SNYVVGIDLVGDESKGENPLrdFYSYYEYARRLGLlGLTLHCGETGNREELLQAL-LLLPDRIGHGIFLLKHPELIYL 209
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555038087 235 LAEQRIGIESCLTSNIQTSTVATLAHHPLKTFLEHGVLASLNTDDPAVQGVDIIHEYNIAAPQAGLSREQIRQAQINGLE 314
Cdd:cd00443  210 VKLRNIPIEVCPTSNVVLGTVQSYEKHPFMRFFKAGLPVSLSTDDPGIFGTSLSEEYSLAAKTFGLTFEDLCELNRNSVL 289
                        330
                 ....*....|....*
gi 555038087 315 IAFLTPAEKQALRDK 329
Cdd:cd00443  290 SSFAKDEEKKSLLEV 304
PTZ00124 PTZ00124
adenosine deaminase; Provisional
5-329 1.16e-40

adenosine deaminase; Provisional


Pssm-ID: 173415  Cd Length: 362  Bit Score: 145.78  E-value: 1.16e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555038087   5 RLPLTDIHRHLDGNIRAQTILDLGRQFNLTlPAQTLESLIPHVQVTSNEPDLVSFLSKLDWGVKMLASLDACRRVAFENI 84
Cdd:PTZ00124  34 RIPKCELHCHLDLCFSVDFFLSCIRKYNLQ-PNLSDEEILDYYLFAKGGKSLGEFVEKAIRVADIFNDYEVIEDLAKHAV 112
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555038087  85 EDAARNGLHYVELRFSPGYMAMTHNLPVAGVVEAVIEGVREGCKTFD--VQARLIGIMSRTFGEAACLQELEALLAHRDA 162
Cdd:PTZ00124 113 FNKYKEGVVLMEFRYSPTFVAFKHNLDIDLIHQAIVKGIKEAVELLDhkIEVGLLCIGDTGHDAAPIKESADFCLKHKAD 192
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555038087 163 ITAVDLAGDELGFpgSLFLSHFNRARDAGWHITVHAGEAAGP---ESIWQAIRELGAERIGHGVKAVEDRALMDFLAEQR 239
Cdd:PTZ00124 193 FVGFDHAGHEVDL--KPFKDIFDYVREAGVNLTVHAGEDVTLpnlNTLYSAIQVLKVKRIGHGIRVAESQELIDMVKEKD 270
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555038087 240 IGIESCLTSNIQTSTVATLAHHPLKTFLEHGVLASLNTDDPAVQGVDIIHEYNIAAPQAGLSREQIRQAQINGLEIAFLT 319
Cdd:PTZ00124 271 ILLEVCPISNVLLNNAKSMDTHPIRKLYDAGVKVSVNSDDPGMFLTNINDDYEELYTHLNFTLADFMKMNEWALEKSFLD 350
                        330
                 ....*....|
gi 555038087 320 PAEKQALRDK 329
Cdd:PTZ00124 351 KDIKLKIKKL 360
ADGF cd01321
Adenosine deaminase-related growth factors (ADGF), a novel family of secreted growth-factors ...
69-329 8.04e-17

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: 80.01  E-value: 8.04e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555038087  69 MLASLDACRRVAFENIEDAARNGLHYVELR--FSPGYMAMTHNLPVAGVVEAVIEGVREGCKTFD--VQARLIGIMSRTF 144
Cdd:cd01321   61 LLTYLPIFRDYYRRLLEELYEDNVQYVELRssFSPLYDLDGREYDYEETVQLLEEVVEKFKKTHPdfIGLKIIYATLRNF 140
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555038087 145 GEAACLQELE-ALLAHR---DAITAVDLAGDE-LGFPGSLFLSHFNRARDAGWHIT--VHAGEAAGPES-----IWQAIR 212
Cdd:cd01321  141 NDSEIKESMEqCLNLKKkfpDFIAGFDLVGQEdAGRPLLDFLPQLLWFPKQCAEIPffFHAGETNGDGTetdenLVDALL 220
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555038087 213 eLGAERIGHGVKAVEDRALMDFLAEQRIGIESCLTSNIQTSTVATLAHHPLKTFLEHGVLASLNTDDPAVQGVD-IIHEY 291
Cdd:cd01321  221 -LNTKRIGHGFALPKHPLLMDLVKKKNIAIEVCPISNQVLGLVSDLRNHPAAALLARGVPVVISSDDPGFWGAKgLSHDF 299
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|...
gi 555038087 292 -----NIAAPQAGLSreQIRQAQINGLEIAFLTPAEKQALRDK 329
Cdd:cd01321  300 yqafmGLAPADAGLR--GLKQLAENSIRYSALSDQEKDEAVAK 340
metallo-dependent_hydrolases cd01292
Superfamily of metallo-dependent hydrolases (also called amidohydrolase superfamily) is a ...
46-284 3.06e-05

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: 45.02  E-value: 3.06e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555038087  46 HVQVTSNEPDLVSFLSKLDWGVKMLASLDACRRVafenIEDAARNGLHYVELRFSPGYMAMT--HNLPVAGVVEAvIEGV 123
Cdd:cd01292    7 HLDGSALRGTRLNLELKEAEELSPEDLYEDTLRA----LEALLAGGVTTVVDMGSTPPPTTTkaAIEAVAEAARA-SAGI 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555038087 124 REGCKTFDVQARLIGIMSRTFGEAAclqelEALLAHRDAITAVDLAGDE--LGFPGSLFLSHFNRARDAGWHITVHAGEA 201
Cdd:cd01292   82 RVVLGLGIPGVPAAVDEDAEALLLE-----LLRRGLELGAVGLKLAGPYtaTGLSDESLRRVLEEARKLGLPVVIHAGEL 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555038087 202 AGPESIW----QAIRELGAERIGHGVKAVEDraLMDFLAEQRIGIESCLTSNIQTSTVATLAHhPLKTFLEHGVLASLNT 277
Cdd:cd01292  157 PDPTRALedlvALLRLGGRVVIGHVSHLDPE--LLELLKEAGVSLEVCPLSNYLLGRDGEGAE-ALRRLLELGIRVTLGT 233

                 ....*..
gi 555038087 278 DDPAVQG 284
Cdd:cd01292  234 DGPPHPL 240
AMPD cd01319
AMP deaminase (AMPD) catalyzes the hydrolytic deamination of adensosine monophosphate (AMP) at ...
181-295 5.96e-05

AMP deaminase (AMPD) catalyzes the hydrolytic deamination of adensosine monophosphate (AMP) at position 6 of the adenine nucleotide ring. AMPD is a diverse and highly regulated eukaryotic key enzyme of the adenylate catabolic pathway.


Pssm-ID: 238644  Cd Length: 496  Bit Score: 44.67  E-value: 5.96e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555038087 181 LSHFNRARdaGWHITV---HAGEAAGPESIWQAIreLGAERIGHGVkAVEDRALMDFL--AEQrIGIE-SCLTSNiqtST 254
Cdd:cd01319  315 LNSFRKAR--GFNTFVlrpHCGEAGDIDHLASAF--LLAHGISHGI-NLRKVPVLQYLyyLTQ-IGIAmSPLSNN---SL 385
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 555038087 255 VATLAHHPLKTFLEHGVLASLNTDDP---AVQGVDIIHEYNIAA 295
Cdd:cd01319  386 FLSYEKNPFPEFFKRGLNVSLSTDDPlqfHFTKEPLMEEYSIAA 429
AMP_deaminase pfam19326
AMP deaminase;
181-295 7.15e-04

AMP deaminase;


Pssm-ID: 437158 [Multi-domain]  Cd Length: 622  Bit Score: 41.29  E-value: 7.15e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555038087  181 LSHFNRARdaGWHITV---HAGEAAGPESIWQAIreLGAERIGHGV--KAVEDRALMDFLAEqrIGIE-SCLTSNiqtST 254
Cdd:pfam19326 432 LNSLRKER--GFNTFVlrpHCGEAGDIDHLVSAF--LLAHGISHGIllRKSPVLQYLYYLAQ--IGIAmSPLSNN---SL 502
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 555038087  255 VATLAHHPLKTFLEHGVLASLNTDDP---AVQGVDIIHEYNIAA 295
Cdd:pfam19326 503 FLEYHKNPFPEFFKRGLNVSLSTDDPlqfHFTKEPLMEEYSIAA 546
 
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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