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Conserved domains on  [gi|17538512|ref|NP_501087|]
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adenosine deaminase [Caenorhabditis elegans]

Protein Classification

adenosine deaminase( domain architecture ID 10101442)

adenosine deaminase catalyzes the irreversible hydrolytic deamination of both adenosine and desoxyadenosine to ammonia and inosine or desoxyinosine, respectively, in a zinc-dependent manner

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
ADA cd01320
Adenosine deaminase (ADA) is a monomeric zinc dependent enzyme which catalyzes the ...
48-383 3.30e-125

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: 363.83  E-value: 3.30e-125
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17538512  48 NFPKVELHLHLDGAVRFDTLIDLSQQKGIPLAGAkTVEELKKVLVTHEPANLSKVLEAFEIFLPVIRgDLAAIERVAYEL 127
Cdd:cd01320   1 NLPKAELHLHLDGSLRPETILELAKKNGITLPAS-DVELLELVVAAYNFSDLQDFLAKYDFGLSVLQ-TEEDFERLAYEY 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17538512 128 CEDQHNNGVVYFEGRYSPHLLLCNDYPEVTAAHVVAavkKGFDRGEKQFGIKARSILCCIRGLDKKFPQLILDLATDLKQ 207
Cdd:cd01320  79 LEDAAADGVVYAEIRFSPQLHTRRGLSFDEVVEAVL---RGLDEAEAEFGIKARLILCGLRHLSPESAQETLELALKYRD 155
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17538512 208 LGVVAIDVAGSAHGAdeqYEPEVVAAFQEAHKRGIHRTVHAGESGGPKEVIKAIEDMYAERIGHGYRVMRDEEmyLEHFV 287
Cdd:cd01320 156 KGVVGFDLAGDEVGF---PPEKFVRAFQRAREAGLRLTAHAGEAGGPESVRDALDLLGAERIGHGIRAIEDPE--LVKRL 230
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17538512 288 NSKNVHLEACPYSSVMTGAVPlDWKNHPIARWAKDDVNFSVSRDDPTCFDNSMLSELTLVHKQIGLDVHQLWKAQLNAAR 367
Cdd:cd01320 231 AERNIPLEVCPTSNVQTGAVK-SLAEHPLRELLDAGVKVTINTDDPTVFGTYLTDEYELLAEAFGLTEEELKKLARNAVE 309
                       330
                ....*....|....*.
gi 17538512 368 SCFLPEDEKAELVKRV 383
Cdd:cd01320 310 ASFLSEEEKAELLKRI 325
 
Name Accession Description Interval E-value
ADA cd01320
Adenosine deaminase (ADA) is a monomeric zinc dependent enzyme which catalyzes the ...
48-383 3.30e-125

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: 363.83  E-value: 3.30e-125
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17538512  48 NFPKVELHLHLDGAVRFDTLIDLSQQKGIPLAGAkTVEELKKVLVTHEPANLSKVLEAFEIFLPVIRgDLAAIERVAYEL 127
Cdd:cd01320   1 NLPKAELHLHLDGSLRPETILELAKKNGITLPAS-DVELLELVVAAYNFSDLQDFLAKYDFGLSVLQ-TEEDFERLAYEY 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17538512 128 CEDQHNNGVVYFEGRYSPHLLLCNDYPEVTAAHVVAavkKGFDRGEKQFGIKARSILCCIRGLDKKFPQLILDLATDLKQ 207
Cdd:cd01320  79 LEDAAADGVVYAEIRFSPQLHTRRGLSFDEVVEAVL---RGLDEAEAEFGIKARLILCGLRHLSPESAQETLELALKYRD 155
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17538512 208 LGVVAIDVAGSAHGAdeqYEPEVVAAFQEAHKRGIHRTVHAGESGGPKEVIKAIEDMYAERIGHGYRVMRDEEmyLEHFV 287
Cdd:cd01320 156 KGVVGFDLAGDEVGF---PPEKFVRAFQRAREAGLRLTAHAGEAGGPESVRDALDLLGAERIGHGIRAIEDPE--LVKRL 230
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17538512 288 NSKNVHLEACPYSSVMTGAVPlDWKNHPIARWAKDDVNFSVSRDDPTCFDNSMLSELTLVHKQIGLDVHQLWKAQLNAAR 367
Cdd:cd01320 231 AERNIPLEVCPTSNVQTGAVK-SLAEHPLRELLDAGVKVTINTDDPTVFGTYLTDEYELLAEAFGLTEEELKKLARNAVE 309
                       330
                ....*....|....*.
gi 17538512 368 SCFLPEDEKAELVKRV 383
Cdd:cd01320 310 ASFLSEEEKAELLKRI 325
Add COG1816
Adenosine deaminase [Nucleotide transport and metabolism]; Adenosine deaminase is part of the ...
50-385 5.80e-86

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


Pssm-ID: 441421  Cd Length: 326  Bit Score: 263.87  E-value: 5.80e-86
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17538512  50 PKVELHLHLDGAVRFDTLIDLSQQKGIPLAgAKTVEELKKVLVTHepaNLSKVLEAFEIFLPVIRgDLAAIERVAYELCE 129
Cdd:COG1816   1 PKAELHLHLEGSLRPETLLELAARNGIDLP-AADVEELRAAYDFR---DLQSFLDTYDAGAAVLQ-TEEDFRRLAYEYLE 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17538512 130 DQHNNGVVYFEGRYSPHLLLCN--DYPEVTAAHVvaavkKGFDRGEKQFGIKARSILCCIRGLDKKFPQLILDLATDLKQ 207
Cdd:COG1816  76 DAAADGVRYAEIRFDPQLHTRRglSLEEVVEAVL-----DGLREAEREFGISVRLILCALRHLSPEAAFETLELALRYRD 150
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17538512 208 LGVVAIDVAGSAHGAD-EQYEPevvaAFQEAHKRGIHRTVHAGESGGPKEVIKAIEDMYAERIGHGYRVMRDEEmyLEHF 286
Cdd:COG1816 151 RGVVGFGLAGDERGFPpEKFAE----AFARAREAGLHLTAHAGEAGGPESIWEALDLLGAERIGHGVRAIEDPA--LVAR 224
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17538512 287 VNSKNVHLEACPYSSVMTGAVPlDWKNHPIARWAKDDVNFSVSRDDPTCFDNSMLSELTLVHKQIGLDVHQLWKAQLNAA 366
Cdd:COG1816 225 LADRGIPLEVCPTSNVQLGVVP-SLAEHPLRRLLDAGVRVTLNTDDPLYFGTTLTDEYELAAEAFGLSDADLAQLARNAI 303
                       330
                ....*....|....*....
gi 17538512 367 RSCFLPEDEKAELVKRVEA 385
Cdd:COG1816 304 EASFLPEEEKAALLAELDA 322
aden_deam TIGR01430
adenosine deaminase; This family includes the experimentally verified adenosine deaminases of ...
50-383 8.15e-75

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: 235.33  E-value: 8.15e-75
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17538512    50 PKVELHLHLDGAVRFDTLIDLSQQKGIPLAGAKTVEELKKVLVTHEPaNLSKVLEAFEIFLPVIRgDLAAIERVAYELCE 129
Cdd:TIGR01430   2 PKAELHLHLEGSIRPETLLELAQKNGIPLPADLQSGEELKEAYDKFR-DLQDFLAKYDFGVEVLR-TEDDFKRLAYEYVE 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17538512   130 DQHNNGVVYFEGRYSPHLLLCNdypEVTAAHVVAAVKKGFDRGEKQFGIKARSILCCIRGLDKKFPQLILDLATDLKQLG 209
Cdd:TIGR01430  80 KAAKDGVVYAEVFFDPQLHTNR---GISPDTVVEAVLDGLDEAERDFGIKSRLILCGMRHKQPEAAEETLELAKPYKEQT 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17538512   210 VVAIDVAGsahgaDEQYEP--EVVAAFQEAHKRGIHRTVHAGESGGPKEVIKAIEDMYAERIGHGYRVMRDEEMYleHFV 287
Cdd:TIGR01430 157 IVGFGLAG-----DERGGPppDFVRAFAIARELGLHLTVHAGELGGPESVREALDDLGATRIGHGVRALEDPELL--KRL 229
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17538512   288 NSKNVHLEACPYSSVMTGAVPLDwKNHPIARWAKDDVNFSVSRDDPTCFDNSMLSELTLVHKQIGLDVHQLWKAQLNAAR 367
Cdd:TIGR01430 230 AQENITLEVCPTSNVALGVVKSL-AEHPLRRFLEAGVKVTLNSDDPAYFGSYLTEEYEIAAKHAGLTEEELKQLARNALE 308
                         330
                  ....*....|....*.
gi 17538512   368 SCFLPEDEKAELVKRV 383
Cdd:TIGR01430 309 GSFLSDDEKKELLAKL 324
PRK09358 PRK09358
adenosine deaminase; Provisional
50-385 5.31e-74

adenosine deaminase; Provisional


Pssm-ID: 236480  Cd Length: 340  Bit Score: 233.53  E-value: 5.31e-74
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17538512   50 PKVELHLHLDGAVRFDTLIDLSQQKGIPLAgAKTVEELKKVLVTHEPANLSKVLEAFEIFLPVIRgDLAAIERVAYELCE 129
Cdd:PRK09358  11 PKAELHLHLDGSLRPETILELARRNGIALP-ATDVEELPWVRAAYDFRDLQSFLDKYDAGVAVLQ-TEEDLRRLAFEYLE 88
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17538512  130 DQHNNGVVYFEGRYSP--HL---LLCNDYPEVTAahvvaavkKGFDRGEKQFGIKARSILCCIRGLDKKFPQLILD-LAT 203
Cdd:PRK09358  89 DAAADGVVYAEIRFDPqlHTergLPLEEVVEAVL--------DGLRAAEAEFGISVRLILCFMRHFGEEAAARELEaLAA 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17538512  204 DLKQLGVVAIDVAGSAHGAD-EQYEPevvaAFQEAHKRGIHRTVHAGESGGPKEVIKAIEDMYAERIGHGYRVMRDEEMY 282
Cdd:PRK09358 161 RYRDDGVVGFDLAGDELGFPpSKFAR----AFDRARDAGLRLTAHAGEAGGPESIWEALDELGAERIGHGVRAIEDPALM 236
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17538512  283 leHFVNSKNVHLEACPYSSVMTGAVPlDWKNHPIARWAKDDVNFSVSRDDPTCFDNSMLSELTLVHKQIGLDVHQLWKAQ 362
Cdd:PRK09358 237 --ARLADRRIPLEVCPTSNVQTGAVP-SLAEHPLKTLLDAGVRVTINTDDPLVFGTTLTEEYEALAEAFGLSDEDLAQLA 313
                        330       340
                 ....*....|....*....|...
gi 17538512  363 LNAARSCFLPEDEKAELVKRVEA 385
Cdd:PRK09358 314 RNALEAAFLSEEEKAALLAEVDA 336
A_deaminase pfam00962
Adenosine deaminase;
50-385 2.59e-73

Adenosine deaminase;


Pssm-ID: 425964  Cd Length: 330  Bit Score: 231.55  E-value: 2.59e-73
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17538512    50 PKVELHLHLDGAVRFDTLIDLSQQKGIPLAGAKTVEELKKVLVTHEPANLSKVLEAFEIFLPVIRgDLAAIERVAYELCE 129
Cdd:pfam00962   1 PKAELHLHLDGSLRPDTLLELAKRYGIILPADFPEALEPLFRKYKKERDLQDFLDKYDIGVAVLR-SPEDIRRLAFEYAE 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17538512   130 DQHNNGVVYFEGRYSPHLLLCNDYPEVTAAHVVAavkKGFDRGEKQFGIKARSILCCIRGLDKKFPQLILDLATDLKQLG 209
Cdd:pfam00962  80 DVAKDGVVYAEVRYDPQSHASRGLSPDTVVDAVL---DAVDAAEREFGITVRLIVCAMRHEHPECSREIAELAPRYRDQG 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17538512   210 VVAIDVAGSAHGADEQYEPEVVAAFQEAHKRGIHRTVHAGESGGPKEVIKAIEDMYAERIGHGYRVMRDEEMYleHFVNS 289
Cdd:pfam00962 157 IVAFGLAGDEKGFPPSLFRDHVEAFARARDAGLHLTVHAGEAGGPQSVWEALDDLGAERIGHGVRSAEDPRLL--DRLAD 234
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17538512   290 KNVHLEACPYSSVMTGAV-PLDwkNHPIARWAKDDVNFSVSRDDPTCFDNSMLSELTLVHKQIGLDVHQLWKAQLNAARS 368
Cdd:pfam00962 235 RQIPLEICPTSNVQTGAVaSLA--EHPLKTFLRAGVPVSLNTDDPLMFGSDLLDEYQVAKRAPGFDEEELARLAKNAVKG 312
                         330
                  ....*....|....*..
gi 17538512   369 CFLPEDEKAELVKRVEA 385
Cdd:pfam00962 313 SFLPADEKRALLDEVDK 329
 
Name Accession Description Interval E-value
ADA cd01320
Adenosine deaminase (ADA) is a monomeric zinc dependent enzyme which catalyzes the ...
48-383 3.30e-125

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: 363.83  E-value: 3.30e-125
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17538512  48 NFPKVELHLHLDGAVRFDTLIDLSQQKGIPLAGAkTVEELKKVLVTHEPANLSKVLEAFEIFLPVIRgDLAAIERVAYEL 127
Cdd:cd01320   1 NLPKAELHLHLDGSLRPETILELAKKNGITLPAS-DVELLELVVAAYNFSDLQDFLAKYDFGLSVLQ-TEEDFERLAYEY 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17538512 128 CEDQHNNGVVYFEGRYSPHLLLCNDYPEVTAAHVVAavkKGFDRGEKQFGIKARSILCCIRGLDKKFPQLILDLATDLKQ 207
Cdd:cd01320  79 LEDAAADGVVYAEIRFSPQLHTRRGLSFDEVVEAVL---RGLDEAEAEFGIKARLILCGLRHLSPESAQETLELALKYRD 155
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17538512 208 LGVVAIDVAGSAHGAdeqYEPEVVAAFQEAHKRGIHRTVHAGESGGPKEVIKAIEDMYAERIGHGYRVMRDEEmyLEHFV 287
Cdd:cd01320 156 KGVVGFDLAGDEVGF---PPEKFVRAFQRAREAGLRLTAHAGEAGGPESVRDALDLLGAERIGHGIRAIEDPE--LVKRL 230
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17538512 288 NSKNVHLEACPYSSVMTGAVPlDWKNHPIARWAKDDVNFSVSRDDPTCFDNSMLSELTLVHKQIGLDVHQLWKAQLNAAR 367
Cdd:cd01320 231 AERNIPLEVCPTSNVQTGAVK-SLAEHPLRELLDAGVKVTINTDDPTVFGTYLTDEYELLAEAFGLTEEELKKLARNAVE 309
                       330
                ....*....|....*.
gi 17538512 368 SCFLPEDEKAELVKRV 383
Cdd:cd01320 310 ASFLSEEEKAELLKRI 325
Add COG1816
Adenosine deaminase [Nucleotide transport and metabolism]; Adenosine deaminase is part of the ...
50-385 5.80e-86

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


Pssm-ID: 441421  Cd Length: 326  Bit Score: 263.87  E-value: 5.80e-86
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17538512  50 PKVELHLHLDGAVRFDTLIDLSQQKGIPLAgAKTVEELKKVLVTHepaNLSKVLEAFEIFLPVIRgDLAAIERVAYELCE 129
Cdd:COG1816   1 PKAELHLHLEGSLRPETLLELAARNGIDLP-AADVEELRAAYDFR---DLQSFLDTYDAGAAVLQ-TEEDFRRLAYEYLE 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17538512 130 DQHNNGVVYFEGRYSPHLLLCN--DYPEVTAAHVvaavkKGFDRGEKQFGIKARSILCCIRGLDKKFPQLILDLATDLKQ 207
Cdd:COG1816  76 DAAADGVRYAEIRFDPQLHTRRglSLEEVVEAVL-----DGLREAEREFGISVRLILCALRHLSPEAAFETLELALRYRD 150
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17538512 208 LGVVAIDVAGSAHGAD-EQYEPevvaAFQEAHKRGIHRTVHAGESGGPKEVIKAIEDMYAERIGHGYRVMRDEEmyLEHF 286
Cdd:COG1816 151 RGVVGFGLAGDERGFPpEKFAE----AFARAREAGLHLTAHAGEAGGPESIWEALDLLGAERIGHGVRAIEDPA--LVAR 224
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17538512 287 VNSKNVHLEACPYSSVMTGAVPlDWKNHPIARWAKDDVNFSVSRDDPTCFDNSMLSELTLVHKQIGLDVHQLWKAQLNAA 366
Cdd:COG1816 225 LADRGIPLEVCPTSNVQLGVVP-SLAEHPLRRLLDAGVRVTLNTDDPLYFGTTLTDEYELAAEAFGLSDADLAQLARNAI 303
                       330
                ....*....|....*....
gi 17538512 367 RSCFLPEDEKAELVKRVEA 385
Cdd:COG1816 304 EASFLPEEEKAALLAELDA 322
aden_deam TIGR01430
adenosine deaminase; This family includes the experimentally verified adenosine deaminases of ...
50-383 8.15e-75

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: 235.33  E-value: 8.15e-75
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17538512    50 PKVELHLHLDGAVRFDTLIDLSQQKGIPLAGAKTVEELKKVLVTHEPaNLSKVLEAFEIFLPVIRgDLAAIERVAYELCE 129
Cdd:TIGR01430   2 PKAELHLHLEGSIRPETLLELAQKNGIPLPADLQSGEELKEAYDKFR-DLQDFLAKYDFGVEVLR-TEDDFKRLAYEYVE 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17538512   130 DQHNNGVVYFEGRYSPHLLLCNdypEVTAAHVVAAVKKGFDRGEKQFGIKARSILCCIRGLDKKFPQLILDLATDLKQLG 209
Cdd:TIGR01430  80 KAAKDGVVYAEVFFDPQLHTNR---GISPDTVVEAVLDGLDEAERDFGIKSRLILCGMRHKQPEAAEETLELAKPYKEQT 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17538512   210 VVAIDVAGsahgaDEQYEP--EVVAAFQEAHKRGIHRTVHAGESGGPKEVIKAIEDMYAERIGHGYRVMRDEEMYleHFV 287
Cdd:TIGR01430 157 IVGFGLAG-----DERGGPppDFVRAFAIARELGLHLTVHAGELGGPESVREALDDLGATRIGHGVRALEDPELL--KRL 229
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17538512   288 NSKNVHLEACPYSSVMTGAVPLDwKNHPIARWAKDDVNFSVSRDDPTCFDNSMLSELTLVHKQIGLDVHQLWKAQLNAAR 367
Cdd:TIGR01430 230 AQENITLEVCPTSNVALGVVKSL-AEHPLRRFLEAGVKVTLNSDDPAYFGSYLTEEYEIAAKHAGLTEEELKQLARNALE 308
                         330
                  ....*....|....*.
gi 17538512   368 SCFLPEDEKAELVKRV 383
Cdd:TIGR01430 309 GSFLSDDEKKELLAKL 324
PRK09358 PRK09358
adenosine deaminase; Provisional
50-385 5.31e-74

adenosine deaminase; Provisional


Pssm-ID: 236480  Cd Length: 340  Bit Score: 233.53  E-value: 5.31e-74
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17538512   50 PKVELHLHLDGAVRFDTLIDLSQQKGIPLAgAKTVEELKKVLVTHEPANLSKVLEAFEIFLPVIRgDLAAIERVAYELCE 129
Cdd:PRK09358  11 PKAELHLHLDGSLRPETILELARRNGIALP-ATDVEELPWVRAAYDFRDLQSFLDKYDAGVAVLQ-TEEDLRRLAFEYLE 88
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17538512  130 DQHNNGVVYFEGRYSP--HL---LLCNDYPEVTAahvvaavkKGFDRGEKQFGIKARSILCCIRGLDKKFPQLILD-LAT 203
Cdd:PRK09358  89 DAAADGVVYAEIRFDPqlHTergLPLEEVVEAVL--------DGLRAAEAEFGISVRLILCFMRHFGEEAAARELEaLAA 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17538512  204 DLKQLGVVAIDVAGSAHGAD-EQYEPevvaAFQEAHKRGIHRTVHAGESGGPKEVIKAIEDMYAERIGHGYRVMRDEEMY 282
Cdd:PRK09358 161 RYRDDGVVGFDLAGDELGFPpSKFAR----AFDRARDAGLRLTAHAGEAGGPESIWEALDELGAERIGHGVRAIEDPALM 236
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17538512  283 leHFVNSKNVHLEACPYSSVMTGAVPlDWKNHPIARWAKDDVNFSVSRDDPTCFDNSMLSELTLVHKQIGLDVHQLWKAQ 362
Cdd:PRK09358 237 --ARLADRRIPLEVCPTSNVQTGAVP-SLAEHPLKTLLDAGVRVTINTDDPLVFGTTLTEEYEALAEAFGLSDEDLAQLA 313
                        330       340
                 ....*....|....*....|...
gi 17538512  363 LNAARSCFLPEDEKAELVKRVEA 385
Cdd:PRK09358 314 RNALEAAFLSEEEKAALLAEVDA 336
A_deaminase pfam00962
Adenosine deaminase;
50-385 2.59e-73

Adenosine deaminase;


Pssm-ID: 425964  Cd Length: 330  Bit Score: 231.55  E-value: 2.59e-73
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17538512    50 PKVELHLHLDGAVRFDTLIDLSQQKGIPLAGAKTVEELKKVLVTHEPANLSKVLEAFEIFLPVIRgDLAAIERVAYELCE 129
Cdd:pfam00962   1 PKAELHLHLDGSLRPDTLLELAKRYGIILPADFPEALEPLFRKYKKERDLQDFLDKYDIGVAVLR-SPEDIRRLAFEYAE 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17538512   130 DQHNNGVVYFEGRYSPHLLLCNDYPEVTAAHVVAavkKGFDRGEKQFGIKARSILCCIRGLDKKFPQLILDLATDLKQLG 209
Cdd:pfam00962  80 DVAKDGVVYAEVRYDPQSHASRGLSPDTVVDAVL---DAVDAAEREFGITVRLIVCAMRHEHPECSREIAELAPRYRDQG 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17538512   210 VVAIDVAGSAHGADEQYEPEVVAAFQEAHKRGIHRTVHAGESGGPKEVIKAIEDMYAERIGHGYRVMRDEEMYleHFVNS 289
Cdd:pfam00962 157 IVAFGLAGDEKGFPPSLFRDHVEAFARARDAGLHLTVHAGEAGGPQSVWEALDDLGAERIGHGVRSAEDPRLL--DRLAD 234
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17538512   290 KNVHLEACPYSSVMTGAV-PLDwkNHPIARWAKDDVNFSVSRDDPTCFDNSMLSELTLVHKQIGLDVHQLWKAQLNAARS 368
Cdd:pfam00962 235 RQIPLEICPTSNVQTGAVaSLA--EHPLKTFLRAGVPVSLNTDDPLMFGSDLLDEYQVAKRAPGFDEEELARLAKNAVKG 312
                         330
                  ....*....|....*..
gi 17538512   369 CFLPEDEKAELVKRVEA 385
Cdd:pfam00962 313 SFLPADEKRALLDEVDK 329
ADA_AMPD cd00443
Adenosine/AMP deaminase. Adenosine deaminases (ADAs) are present in pro- and eukaryotic ...
50-382 1.03e-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: 159.05  E-value: 1.03e-45
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17538512  50 PKVELHLHLDGAVRFDTLIDLSQQKgiplagaktveelkkvlvthepanlskVLEAFEIFLPVIRgDLAAIERVAYELCE 129
Cdd:cd00443   2 PKVELHAHLSGSISPETLLELIKKE---------------------------FFEKFLLVHNLLQ-KGEALARALKEVIE 53
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17538512 130 DQHNNGVVYFEGRYSPHLLLCND--YPEVTAAHVVaavkKGFDRGEKQF-GIKARSILCCIRGLDKKFPQL----ILDLA 202
Cdd:cd00443  54 EFAEDNVQYLELRTTPRLLETEKglTKEQYWLLVI----EGISEAKQWFpPIKVRLILSVDRRGPYVQNYLvaseILELA 129
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17538512 203 TDLKQlGVVAIDVAGSAHGaDEQYEPEVVAAFQEAHKRG-IHRTVHAGESGGPkEVIKAIEDMYAERIGHGYRVMRDEEm 281
Cdd:cd00443 130 KFLSN-YVVGIDLVGDESK-GENPLRDFYSYYEYARRLGlLGLTLHCGETGNR-EELLQALLLLPDRIGHGIFLLKHPE- 205
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17538512 282 yLEHFVNSKNVHLEACPYSSVMTGAVPlDWKNHPIARWAKDDVNFSVSRDDPTCFDNSMLSELTLVHKQIGLDVHQLWKA 361
Cdd:cd00443 206 -LIYLVKLRNIPIEVCPTSNVVLGTVQ-SYEKHPFMRFFKAGLPVSLSTDDPGIFGTSLSEEYSLAAKTFGLTFEDLCEL 283
                       330       340
                ....*....|....*....|.
gi 17538512 362 QLNAARSCFLPEDEKAELVKR 382
Cdd:cd00443 284 NRNSVLSSFAKDEEKKSLLEV 304
PTZ00124 PTZ00124
adenosine deaminase; Provisional
50-381 3.35e-21

adenosine deaminase; Provisional


Pssm-ID: 173415  Cd Length: 362  Bit Score: 93.78  E-value: 3.35e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17538512   50 PKVELHLHLDGAVRFDTLIDLSQQKGIPlAGAKTVEELKKVLVTHEPANLSKVLEAfEIFLPVIRGDLAAIERVAYELCE 129
Cdd:PTZ00124  36 PKCELHCHLDLCFSVDFFLSCIRKYNLQ-PNLSDEEILDYYLFAKGGKSLGEFVEK-AIRVADIFNDYEVIEDLAKHAVF 113
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17538512  130 DQHNNGVVYFEGRYSPHLLL--CN-DYPEVTAAHVvaavkKGFDRGEKQFGIKARSILCCI--RGLDKKFPQLILDLATD 204
Cdd:PTZ00124 114 NKYKEGVVLMEFRYSPTFVAfkHNlDIDLIHQAIV-----KGIKEAVELLDHKIEVGLLCIgdTGHDAAPIKESADFCLK 188
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17538512  205 LKQlgvvaiDVAGSAHGADEQYEPEVVAAFQEAHKRGIHRTVHAGESGGP---KEVIKAIEDMYAERIGHGYRVMRDEEM 281
Cdd:PTZ00124 189 HKA------DFVGFDHAGHEVDLKPFKDIFDYVREAGVNLTVHAGEDVTLpnlNTLYSAIQVLKVKRIGHGIRVAESQEL 262
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17538512  282 YleHFVNSKNVHLEACPYSSVMTGAVpLDWKNHPIARWAKDDVNFSVSRDDPTCFDNSMLSELTLVHKQIGLDVHQLWKA 361
Cdd:PTZ00124 263 I--DMVKEKDILLEVCPISNVLLNNA-KSMDTHPIRKLYDAGVKVSVNSDDPGMFLTNINDDYEELYTHLNFTLADFMKM 339
                        330       340
                 ....*....|....*....|
gi 17538512  362 QLNAARSCFLPEDEKAELVK 381
Cdd:PTZ00124 340 NEWALEKSFLDKDIKLKIKK 359
metallo-dependent_hydrolases cd01292
Superfamily of metallo-dependent hydrolases (also called amidohydrolase superfamily) is a ...
133-367 2.25e-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: 2.25e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17538512 133 NNGVVYFEGRYSPHLLlcndypevtaAHVVAAVKKGFDRGEKQFGIKARSILCCIRG---LDKKFPQLILDLATDLKQLG 209
Cdd:cd01292  46 AGGVTTVVDMGSTPPP----------TTTKAAIEAVAEAARASAGIRVVLGLGIPGVpaaVDEDAEALLLELLRRGLELG 115
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17538512 210 VVAIDVAGsAHGADEQYEPEVVAAFQEAHKRGIHRTVHAGESGGP----KEVIKAIEDMYAERIGHGYRvMRDEEMYL-- 283
Cdd:cd01292 116 AVGLKLAG-PYTATGLSDESLRRVLEEARKLGLPVVIHAGELPDPtralEDLVALLRLGGRVVIGHVSH-LDPELLELlk 193
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17538512 284 EHfvnskNVHLEACPYSSVMTGAVPLDWknHPIARWAKDDVNFSVSRDDPTCFDNS-MLSELTLVHKQIGLDVHQ---LW 359
Cdd:cd01292 194 EA-----GVSLEVCPLSNYLLGRDGEGA--EALRRLLELGIRVTLGTDGPPHPLGTdLLALLRLLLKVLRLGLSLeeaLR 266

                ....*...
gi 17538512 360 KAQLNAAR 367
Cdd:cd01292 267 LATINPAR 274
ADGF cd01321
Adenosine deaminase-related growth factors (ADGF), a novel family of secreted growth-factors ...
54-342 3.88e-09

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: 57.67  E-value: 3.88e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17538512  54 LHLHLDGAVRFDTLIDLsqqkgiplagaktveelkkvlvthepanlskVLEAFE-IFLpVIRGDLA---AIERVAYELCE 129
Cdd:cd01321  30 LHVHDTAMVSSDWLIKN-------------------------------ATYRFEqIFD-IIDGLLTylpIFRDYYRRLLE 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17538512 130 DQHNNGVVYFEGRYSPHLLLC-----NDYPEVTAAHVVAAVKkgFDRGEKQFgIKARSILCCIRGLDKKFPQLILDLATD 204
Cdd:cd01321  78 ELYEDNVQYVELRSSFSPLYDldgreYDYEETVQLLEEVVEK--FKKTHPDF-IGLKIIYATLRNFNDSEIKESMEQCLN 154
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17538512 205 LKQlgvvaidvagsahgadeqYEPEVVAAF----QEAHKRGIHRTV-----------------HAGESGGP-----KEVI 258
Cdd:cd01321 155 LKK------------------KFPDFIAGFdlvgQEDAGRPLLDFLpqllwfpkqcaeipfffHAGETNGDgtetdENLV 216
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17538512 259 KAIEdMYAERIGHGYRVMRDEemYLEHFVNSKNVHLEACPYSSVMTGAVPlDWKNHPIARWAKDDVNFSVSRDDPTCFDN 338
Cdd:cd01321 217 DALL-LNTKRIGHGFALPKHP--LLMDLVKKKNIAIEVCPISNQVLGLVS-DLRNHPAAALLARGVPVVISSDDPGFWGA 292

                ....
gi 17538512 339 SMLS 342
Cdd:cd01321 293 KGLS 296
adm_rel TIGR01431
adenosine deaminase-related growth factor; Members of this family have been described as ...
268-376 6.17e-05

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: 44.79  E-value: 6.17e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17538512   268 RIGHGYRVMRDEEmyLEHFVNSKNVHLEACPYSSVMTGAVPlDWKNHPIARWAKDDVNFSVSRDDPTCFDNSMLS-ELTL 346
Cdd:TIGR01431 351 RIGHGFALSKHPA--VRTYSKERDIPIEVCPISNQVLKLVS-DLRNHPVATLMADNYPMVISSDDPAFWGAKGLSyDFYE 427
                          90       100       110
                  ....*....|....*....|....*....|...
gi 17538512   347 VHKQIG---LDVHQLWKAQLNAARSCFLPEDEK 376
Cdd:TIGR01431 428 AFMGIAgmkADLRTLKQLALNSIKYSALSEEEK 460
Amidohydro_1 pfam01979
Amidohydrolase family; This family of enzymes are a a large metal dependent hydrolase ...
196-275 2.34e-03

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: 39.79  E-value: 2.34e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17538512   196 QLILDLATDLKQLGVVAIDVAGSAHGADEQYEPEVVAAFQEAHKRGIHRTVHAGESggpKEVIKAIEDMYAERIGHGYRV 275
Cdd:pfam01979  95 EKLKAGAEFIKGMADGVVFVGLAPHGAPTFSDDELKAALEEAKKYGLPVAIHALET---KGEVEDAIAAFGGGIEHGTHL 171
 
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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