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Conserved domains on  [gi|2157343652|ref|WP_230470153|]
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adenosine deaminase [Lujinxingia vulgaris]

Protein Classification

adenosine deaminase( domain architecture ID 10004592)

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

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
Add COG1816
Adenosine deaminase [Nucleotide transport and metabolism]; Adenosine deaminase is part of the ...
 12-343 3.85e-154

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


:

Pssm-ID: 441421  Cd Length: 326  Bit Score: 438.36  E-value: 3.85e-154
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2157343652  12 PKTDLHVHLDGSMRLSTILELAEKEGIALPgnPQTEDELARAINigaiCEDLTDYLKAFDVTLSVMQTEESLYRAAFELG 91
Cdd:COG1816     1 PKAELHLHLEGSLRPETLLELAARNGIDLP--AADVEELRAAYD----FRDLQSFLDTYDAGAAVLQTEEDFRRLAYEYL 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2157343652  92 EDAARENVKYMEVRYSPLLHTRNGLSYPVIVEAVAEGLREAKRRYGLMSGQIICGIRHMTPESSLRMAELCVAFKNRGVV 171
Cdd:COG1816    75 EDAAADGVRYAEIRFDPQLHTRRGLSLEEVVEAVLDGLREAEREFGISVRLILCALRHLSPEAAFETLELALRYRDRGVV 154

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2157343652 172 GFDLAGAEADNPAKDYREAFYLIRNNNVNLTIHAGEAYGPESIHQAIHLGGAHRIGHGTRLREDGDLLNFLNDHRIPLEV 251
Cdd:COG1816   155 GFGLAGDERGFPPEKFAEAFARAREAGLHLTAHAGEAGGPESIWEALDLLGAERIGHGVRAIEDPALVARLADRGIPLEV 234

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2157343652 252 CLTSNVQTRAAKSFESHPLPFYMSYGLRCTINTDNRLITDTTMTDEFWRAVQHYDLNIGDLRKLMIDGFKSAFMPYRKKR 331
Cdd:COG1816   235 CPTSNVQLGVVPSLAEHPLRRLLDAGVRVTLNTDDPLYFGTTLTDEYELAAEAFGLSDADLAQLARNAIEASFLPEEEKA 314

                         330
                  ....*....|..
gi 2157343652 332 TVTAQACAEFDA 343
Cdd:COG1816   315 ALLAELDAYFAA 326
 
Name Accession Description Interval E-value
Add COG1816
Adenosine deaminase [Nucleotide transport and metabolism]; Adenosine deaminase is part of the ...
 12-343 3.85e-154

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


Pssm-ID: 441421  Cd Length: 326  Bit Score: 438.36  E-value: 3.85e-154
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2157343652  12 PKTDLHVHLDGSMRLSTILELAEKEGIALPgnPQTEDELARAINigaiCEDLTDYLKAFDVTLSVMQTEESLYRAAFELG 91
Cdd:COG1816     1 PKAELHLHLEGSLRPETLLELAARNGIDLP--AADVEELRAAYD----FRDLQSFLDTYDAGAAVLQTEEDFRRLAYEYL 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2157343652  92 EDAARENVKYMEVRYSPLLHTRNGLSYPVIVEAVAEGLREAKRRYGLMSGQIICGIRHMTPESSLRMAELCVAFKNRGVV 171
Cdd:COG1816    75 EDAAADGVRYAEIRFDPQLHTRRGLSLEEVVEAVLDGLREAEREFGISVRLILCALRHLSPEAAFETLELALRYRDRGVV 154

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2157343652 172 GFDLAGAEADNPAKDYREAFYLIRNNNVNLTIHAGEAYGPESIHQAIHLGGAHRIGHGTRLREDGDLLNFLNDHRIPLEV 251
Cdd:COG1816   155 GFGLAGDERGFPPEKFAEAFARAREAGLHLTAHAGEAGGPESIWEALDLLGAERIGHGVRAIEDPALVARLADRGIPLEV 234

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2157343652 252 CLTSNVQTRAAKSFESHPLPFYMSYGLRCTINTDNRLITDTTMTDEFWRAVQHYDLNIGDLRKLMIDGFKSAFMPYRKKR 331
Cdd:COG1816   235 CPTSNVQLGVVPSLAEHPLRRLLDAGVRVTLNTDDPLYFGTTLTDEYELAAEAFGLSDADLAQLARNAIEASFLPEEEKA 314

                         330
                  ....*....|..
gi 2157343652 332 TVTAQACAEFDA 343
Cdd:COG1816   315 ALLAELDAYFAA 326
PRK09358 PRK09358
adenosine deaminase; Provisional
 3-326 8.05e-135

adenosine deaminase; Provisional


Pssm-ID: 236480  Cd Length: 340  Bit Score: 389.92  E-value: 8.05e-135
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2157343652   3 ITRDFIHRMPKTDLHVHLDGSMRLSTILELAEKEGIALPgnPQTEDELaRAINIGAICEDLTDYLKAFDVTLSVMQTEES 82
Cdd:PRK09358    2 NLLMIIRSLPKAELHLHLDGSLRPETILELARRNGIALP--ATDVEEL-PWVRAAYDFRDLQSFLDKYDAGVAVLQTEED 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2157343652  83 LYRAAFELGEDAARENVKYMEVRYSPLLHTRNGLSYPVIVEAVAEGLREAKRRYGLMSGQIICGIRHMTPESSLR-MAEL 161
Cdd:PRK09358   79 LRRLAFEYLEDAAADGVVYAEIRFDPQLHTERGLPLEEVVEAVLDGLRAAEAEFGISVRLILCFMRHFGEEAAAReLEAL 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2157343652 162 CVAFKNRGVVGFDLAGAEADNPAKDYREAFYLIRNNNVNLTIHAGEAYGPESIHQAIHLGGAHRIGHGTRLREDGDLLNF 241
Cdd:PRK09358  159 AARYRDDGVVGFDLAGDELGFPPSKFARAFDRARDAGLRLTAHAGEAGGPESIWEALDELGAERIGHGVRAIEDPALMAR 238

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2157343652 242 LNDHRIPLEVCLTSNVQTRAAKSFESHPLPFYMSYGLRCTINTDNRLITDTTMTDEFWRAVQHYDLNIGDLRKLMIDGFK 321
Cdd:PRK09358  239 LADRRIPLEVCPTSNVQTGAVPSLAEHPLKTLLDAGVRVTINTDDPLVFGTTLTEEYEALAEAFGLSDEDLAQLARNALE 318


                  ....*
gi 2157343652 322 SAFMP 326
Cdd:PRK09358  319 AAFLS 323
ADA cd01320
Adenosine deaminase (ADA) is a monomeric zinc dependent enzyme which catalyzes the ...
 10-326 4.79e-132

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: 382.32  E-value: 4.79e-132
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2157343652  10 RMPKTDLHVHLDGSMRLSTILELAEKEGIALPGNPQTEDELARAInigAICEDLTDYLKAFDVTLSVMQTEESLYRAAFE 89
Cdd:cd01320     1 NLPKAELHLHLDGSLRPETILELAKKNGITLPASDVELLELVVAA---YNFSDLQDFLAKYDFGLSVLQTEEDFERLAYE 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2157343652  90 LGEDAARENVKYMEVRYSPLLHTRNGLSYPVIVEAVAEGLREAKRRYGLMSGQIICGIRHMTPESSLRMAELCVAFKNRG 169
Cdd:cd01320    78 YLEDAAADGVVYAEIRFSPQLHTRRGLSFDEVVEAVLRGLDEAEAEFGIKARLILCGLRHLSPESAQETLELALKYRDKG 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2157343652 170 VVGFDLAGAEADNPAKDYREAFYLIRNNNVNLTIHAGEAYGPESIHQAIHLGGAHRIGHGTRLREDGDLLNFLNDHRIPL 249
Cdd:cd01320   158 VVGFDLAGDEVGFPPEKFVRAFQRAREAGLRLTAHAGEAGGPESVRDALDLLGAERIGHGIRAIEDPELVKRLAERNIPL 237

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2157343652 250 EVCLTSNVQTRAAKSFESHPLPFYMSYGLRCTINTDNRLITDTTMTDEFWRAVQHYDLNIGDLRKLMIDGFKSAFMP 326
Cdd:cd01320   238 EVCPTSNVQTGAVKSLAEHPLRELLDAGVKVTINTDDPTVFGTYLTDEYELLAEAFGLTEEELKKLARNAVEASFLS 314
aden_deam TIGR01430
adenosine deaminase; This family includes the experimentally verified adenosine deaminases of ...
 11-335 8.76e-105

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: 312.75  E-value: 8.76e-105
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2157343652  11 MPKTDLHVHLDGSMRLSTILELAEKEGIALPGNPQTEDELARAINIgaiCEDLTDYLKAFDVTLSVMQTEESLYRAAFEL 90
Cdd:TIGR01430   1 LPKAELHLHLEGSIRPETLLELAQKNGIPLPADLQSGEELKEAYDK---FRDLQDFLAKYDFGVEVLRTEDDFKRLAYEY 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2157343652  91 GEDAARENVKYMEVRYSPLLHTRNGLSYPVIVEAVAEGLREAKRRYGLMSGQIICGIRHMTPESSLRMAELCVAFKNRGV 170
Cdd:TIGR01430  78 VEKAAKDGVVYAEVFFDPQLHTNRGISPDTVVEAVLDGLDEAERDFGIKSRLILCGMRHKQPEAAEETLELAKPYKEQTI 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2157343652 171 VGFDLAGAEADNPAKDYREAFYLIRNNNVNLTIHAGEAYGPESIHQAIHLGGAHRIGHGTRLREDGDLLNFLNDHRIPLE 250
Cdd:TIGR01430 158 VGFGLAGDERGGPPPDFVRAFAIARELGLHLTVHAGELGGPESVREALDDLGATRIGHGVRALEDPELLKRLAQENITLE 237

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2157343652 251 VCLTSNVQTRAAKSFESHPLPFYMSYGLRCTINTDNRLITDTTMTDEFWRAVQHYDLNIGDLRKLMIDGFKSAFMPYRKK 330
Cdd:TIGR01430 238 VCPTSNVALGVVKSLAEHPLRRFLEAGVKVTLNSDDPAYFGSYLTEEYEIAAKHAGLTEEELKQLARNALEGSFLSDDEK 317


                  ....*
gi 2157343652 331 RTVTA 335
Cdd:TIGR01430 318 KELLA 322
A_deaminase pfam00962
Adenosine deaminase;
12-331 4.16e-98

Adenosine deaminase;


Pssm-ID: 425964  Cd Length: 330  Bit Score: 295.88  E-value: 4.16e-98
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2157343652  12 PKTDLHVHLDGSMRLSTILELAEKEGIALPGnpQTEDELARAINIGAICEDLTDYLKAFDVTLSVMQTEESLYRAAFELG 91
Cdd:pfam00962   1 PKAELHLHLDGSLRPDTLLELAKRYGIILPA--DFPEALEPLFRKYKKERDLQDFLDKYDIGVAVLRSPEDIRRLAFEYA 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2157343652  92 EDAARENVKYMEVRYSPLLHTRNGLSYPVIVEAVAEGLREAKRRYGLMSGQIICGIRHMTPESSLRMAELCVAFKNRGVV 171
Cdd:pfam00962  79 EDVAKDGVVYAEVRYDPQSHASRGLSPDTVVDAVLDAVDAAEREFGITVRLIVCAMRHEHPECSREIAELAPRYRDQGIV 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2157343652 172 GFDLAGAEADNP---AKDYREAFYLIRNNNVNLTIHAGEAYGPESIHQAIHLGGAHRIGHGTRLREDGDLLNFLNDHRIP 248
Cdd:pfam00962 159 AFGLAGDEKGFPpslFRDHVEAFARARDAGLHLTVHAGEAGGPQSVWEALDDLGAERIGHGVRSAEDPRLLDRLADRQIP 238

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2157343652 249 LEVCLTSNVQTRAAKSFESHPLPFYMSYGLRCTINTDNRLITDTTMTDEFWRAVQHYDLNIGDLRKLMIDGFKSAFMPYR 328
Cdd:pfam00962 239 LEICPTSNVQTGAVASLAEHPLKTFLRAGVPVSLNTDDPLMFGSDLLDEYQVAKRAPGFDEEELARLAKNAVKGSFLPAD 318


                  ...
gi 2157343652 329 KKR 331
Cdd:pfam00962 319 EKR 321
 
Name Accession Description Interval E-value
Add COG1816
Adenosine deaminase [Nucleotide transport and metabolism]; Adenosine deaminase is part of the ...
 12-343 3.85e-154

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


Pssm-ID: 441421  Cd Length: 326  Bit Score: 438.36  E-value: 3.85e-154
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2157343652  12 PKTDLHVHLDGSMRLSTILELAEKEGIALPgnPQTEDELARAINigaiCEDLTDYLKAFDVTLSVMQTEESLYRAAFELG 91
Cdd:COG1816     1 PKAELHLHLEGSLRPETLLELAARNGIDLP--AADVEELRAAYD----FRDLQSFLDTYDAGAAVLQTEEDFRRLAYEYL 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2157343652  92 EDAARENVKYMEVRYSPLLHTRNGLSYPVIVEAVAEGLREAKRRYGLMSGQIICGIRHMTPESSLRMAELCVAFKNRGVV 171
Cdd:COG1816    75 EDAAADGVRYAEIRFDPQLHTRRGLSLEEVVEAVLDGLREAEREFGISVRLILCALRHLSPEAAFETLELALRYRDRGVV 154

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2157343652 172 GFDLAGAEADNPAKDYREAFYLIRNNNVNLTIHAGEAYGPESIHQAIHLGGAHRIGHGTRLREDGDLLNFLNDHRIPLEV 251
Cdd:COG1816   155 GFGLAGDERGFPPEKFAEAFARAREAGLHLTAHAGEAGGPESIWEALDLLGAERIGHGVRAIEDPALVARLADRGIPLEV 234

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2157343652 252 CLTSNVQTRAAKSFESHPLPFYMSYGLRCTINTDNRLITDTTMTDEFWRAVQHYDLNIGDLRKLMIDGFKSAFMPYRKKR 331
Cdd:COG1816   235 CPTSNVQLGVVPSLAEHPLRRLLDAGVRVTLNTDDPLYFGTTLTDEYELAAEAFGLSDADLAQLARNAIEASFLPEEEKA 314

                         330
                  ....*....|..
gi 2157343652 332 TVTAQACAEFDA 343
Cdd:COG1816   315 ALLAELDAYFAA 326
PRK09358 PRK09358
adenosine deaminase; Provisional
 3-326 8.05e-135

adenosine deaminase; Provisional


Pssm-ID: 236480  Cd Length: 340  Bit Score: 389.92  E-value: 8.05e-135
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2157343652   3 ITRDFIHRMPKTDLHVHLDGSMRLSTILELAEKEGIALPgnPQTEDELaRAINIGAICEDLTDYLKAFDVTLSVMQTEES 82
Cdd:PRK09358    2 NLLMIIRSLPKAELHLHLDGSLRPETILELARRNGIALP--ATDVEEL-PWVRAAYDFRDLQSFLDKYDAGVAVLQTEED 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2157343652  83 LYRAAFELGEDAARENVKYMEVRYSPLLHTRNGLSYPVIVEAVAEGLREAKRRYGLMSGQIICGIRHMTPESSLR-MAEL 161
Cdd:PRK09358   79 LRRLAFEYLEDAAADGVVYAEIRFDPQLHTERGLPLEEVVEAVLDGLRAAEAEFGISVRLILCFMRHFGEEAAAReLEAL 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2157343652 162 CVAFKNRGVVGFDLAGAEADNPAKDYREAFYLIRNNNVNLTIHAGEAYGPESIHQAIHLGGAHRIGHGTRLREDGDLLNF 241
Cdd:PRK09358  159 AARYRDDGVVGFDLAGDELGFPPSKFARAFDRARDAGLRLTAHAGEAGGPESIWEALDELGAERIGHGVRAIEDPALMAR 238

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2157343652 242 LNDHRIPLEVCLTSNVQTRAAKSFESHPLPFYMSYGLRCTINTDNRLITDTTMTDEFWRAVQHYDLNIGDLRKLMIDGFK 321
Cdd:PRK09358  239 LADRRIPLEVCPTSNVQTGAVPSLAEHPLKTLLDAGVRVTINTDDPLVFGTTLTEEYEALAEAFGLSDEDLAQLARNALE 318


                  ....*
gi 2157343652 322 SAFMP 326
Cdd:PRK09358  319 AAFLS 323
ADA cd01320
Adenosine deaminase (ADA) is a monomeric zinc dependent enzyme which catalyzes the ...
 10-326 4.79e-132

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: 382.32  E-value: 4.79e-132
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2157343652  10 RMPKTDLHVHLDGSMRLSTILELAEKEGIALPGNPQTEDELARAInigAICEDLTDYLKAFDVTLSVMQTEESLYRAAFE 89
Cdd:cd01320     1 NLPKAELHLHLDGSLRPETILELAKKNGITLPASDVELLELVVAA---YNFSDLQDFLAKYDFGLSVLQTEEDFERLAYE 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2157343652  90 LGEDAARENVKYMEVRYSPLLHTRNGLSYPVIVEAVAEGLREAKRRYGLMSGQIICGIRHMTPESSLRMAELCVAFKNRG 169
Cdd:cd01320    78 YLEDAAADGVVYAEIRFSPQLHTRRGLSFDEVVEAVLRGLDEAEAEFGIKARLILCGLRHLSPESAQETLELALKYRDKG 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2157343652 170 VVGFDLAGAEADNPAKDYREAFYLIRNNNVNLTIHAGEAYGPESIHQAIHLGGAHRIGHGTRLREDGDLLNFLNDHRIPL 249
Cdd:cd01320   158 VVGFDLAGDEVGFPPEKFVRAFQRAREAGLRLTAHAGEAGGPESVRDALDLLGAERIGHGIRAIEDPELVKRLAERNIPL 237

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2157343652 250 EVCLTSNVQTRAAKSFESHPLPFYMSYGLRCTINTDNRLITDTTMTDEFWRAVQHYDLNIGDLRKLMIDGFKSAFMP 326
Cdd:cd01320   238 EVCPTSNVQTGAVKSLAEHPLRELLDAGVKVTINTDDPTVFGTYLTDEYELLAEAFGLTEEELKKLARNAVEASFLS 314
aden_deam TIGR01430
adenosine deaminase; This family includes the experimentally verified adenosine deaminases of ...
 11-335 8.76e-105

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: 312.75  E-value: 8.76e-105
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2157343652  11 MPKTDLHVHLDGSMRLSTILELAEKEGIALPGNPQTEDELARAINIgaiCEDLTDYLKAFDVTLSVMQTEESLYRAAFEL 90
Cdd:TIGR01430   1 LPKAELHLHLEGSIRPETLLELAQKNGIPLPADLQSGEELKEAYDK---FRDLQDFLAKYDFGVEVLRTEDDFKRLAYEY 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2157343652  91 GEDAARENVKYMEVRYSPLLHTRNGLSYPVIVEAVAEGLREAKRRYGLMSGQIICGIRHMTPESSLRMAELCVAFKNRGV 170
Cdd:TIGR01430  78 VEKAAKDGVVYAEVFFDPQLHTNRGISPDTVVEAVLDGLDEAERDFGIKSRLILCGMRHKQPEAAEETLELAKPYKEQTI 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2157343652 171 VGFDLAGAEADNPAKDYREAFYLIRNNNVNLTIHAGEAYGPESIHQAIHLGGAHRIGHGTRLREDGDLLNFLNDHRIPLE 250
Cdd:TIGR01430 158 VGFGLAGDERGGPPPDFVRAFAIARELGLHLTVHAGELGGPESVREALDDLGATRIGHGVRALEDPELLKRLAQENITLE 237

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2157343652 251 VCLTSNVQTRAAKSFESHPLPFYMSYGLRCTINTDNRLITDTTMTDEFWRAVQHYDLNIGDLRKLMIDGFKSAFMPYRKK 330
Cdd:TIGR01430 238 VCPTSNVALGVVKSLAEHPLRRFLEAGVKVTLNSDDPAYFGSYLTEEYEIAAKHAGLTEEELKQLARNALEGSFLSDDEK 317


                  ....*
gi 2157343652 331 RTVTA 335
Cdd:TIGR01430 318 KELLA 322
A_deaminase pfam00962
Adenosine deaminase;
12-331 4.16e-98

Adenosine deaminase;


Pssm-ID: 425964  Cd Length: 330  Bit Score: 295.88  E-value: 4.16e-98
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2157343652  12 PKTDLHVHLDGSMRLSTILELAEKEGIALPGnpQTEDELARAINIGAICEDLTDYLKAFDVTLSVMQTEESLYRAAFELG 91
Cdd:pfam00962   1 PKAELHLHLDGSLRPDTLLELAKRYGIILPA--DFPEALEPLFRKYKKERDLQDFLDKYDIGVAVLRSPEDIRRLAFEYA 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2157343652  92 EDAARENVKYMEVRYSPLLHTRNGLSYPVIVEAVAEGLREAKRRYGLMSGQIICGIRHMTPESSLRMAELCVAFKNRGVV 171
Cdd:pfam00962  79 EDVAKDGVVYAEVRYDPQSHASRGLSPDTVVDAVLDAVDAAEREFGITVRLIVCAMRHEHPECSREIAELAPRYRDQGIV 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2157343652 172 GFDLAGAEADNP---AKDYREAFYLIRNNNVNLTIHAGEAYGPESIHQAIHLGGAHRIGHGTRLREDGDLLNFLNDHRIP 248
Cdd:pfam00962 159 AFGLAGDEKGFPpslFRDHVEAFARARDAGLHLTVHAGEAGGPQSVWEALDDLGAERIGHGVRSAEDPRLLDRLADRQIP 238

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2157343652 249 LEVCLTSNVQTRAAKSFESHPLPFYMSYGLRCTINTDNRLITDTTMTDEFWRAVQHYDLNIGDLRKLMIDGFKSAFMPYR 328
Cdd:pfam00962 239 LEICPTSNVQTGAVASLAEHPLKTFLRAGVPVSLNTDDPLMFGSDLLDEYQVAKRAPGFDEEELARLAKNAVKGSFLPAD 318


                  ...
gi 2157343652 329 KKR 331
Cdd:pfam00962 319 EKR 321
ADA_AMPD cd00443
Adenosine/AMP deaminase. Adenosine deaminases (ADAs) are present in pro- and eukaryotic ...
 11-324 7.93e-59

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: 194.10  E-value: 7.93e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2157343652  11 MPKTDLHVHLDGSMRLSTILELAEKEgialpgnpqtedelarainigaicedltdYLKAFDVTLSVMQTEESLYRAAFEL 90
Cdd:cd00443     1 LPKVELHAHLSGSISPETLLELIKKE-----------------------------FFEKFLLVHNLLQKGEALARALKEV 51

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2157343652  91 GEDAARENVKYMEVRYSP-LLHTRNGLSYPVIVEAVAEGLREAKRRYGLMSG-QIICGIRHMTPESSLRMA----ELCVA 164
Cdd:cd00443    52 IEEFAEDNVQYLELRTTPrLLETEKGLTKEQYWLLVIEGISEAKQWFPPIKVrLILSVDRRGPYVQNYLVAseilELAKF 131

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2157343652 165 FKNrGVVGFDLAGAEAD--NPAKDYREAF-YLIRNNNVNLTIHAGEAYGPESIHQAIHLGgAHRIGHGTRLREDGDLLNF 241
Cdd:cd00443   132 LSN-YVVGIDLVGDESKgeNPLRDFYSYYeYARRLGLLGLTLHCGETGNREELLQALLLL-PDRIGHGIFLLKHPELIYL 209

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2157343652 242 LNDHRIPLEVCLTSNVQTRAAKSFESHPLPFYMSYGLRCTINTDNRLITDTTMTDEFWRAVQHYDLNIGDLRKLMIDGFK 321
Cdd:cd00443   210 VKLRNIPIEVCPTSNVVLGTVQSYEKHPFMRFFKAGLPVSLSTDDPGIFGTSLSEEYSLAAKTFGLTFEDLCELNRNSVL 289


                  ...
gi 2157343652 322 SAF 324
Cdd:cd00443   290 SSF 292
PTZ00124 PTZ00124
adenosine deaminase; Provisional
 10-333 5.86e-37

adenosine deaminase; Provisional


Pssm-ID: 173415  Cd Length: 362  Bit Score: 138.07  E-value: 5.86e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2157343652  10 RMPKTDLHVHLDGSMRLSTILELAEKEGIalpgNPQ-TEDELARAINIGAICEDLTDYLKAFDVTLSVMQTEESLYRAAF 88
Cdd:PTZ00124   34 RIPKCELHCHLDLCFSVDFFLSCIRKYNL----QPNlSDEEILDYYLFAKGGKSLGEFVEKAIRVADIFNDYEVIEDLAK 109

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2157343652  89 ELGEDAARENVKYMEVRYSP-LLHTRNGLSYPVIVEAVAEGLREAKR--RYGLMSGQIICGIRHMTPESSLRMAELCVAF 165
Cdd:PTZ00124  110 HAVFNKYKEGVVLMEFRYSPtFVAFKHNLDIDLIHQAIVKGIKEAVEllDHKIEVGLLCIGDTGHDAAPIKESADFCLKH 189

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2157343652 166 KNRgVVGFDLAGAEADnpAKDYREAFYLIRNNNVNLTIHAGEAYGP---ESIHQAIHLGGAHRIGHGTRLREDGDLLNFL 242
Cdd:PTZ00124  190 KAD-FVGFDHAGHEVD--LKPFKDIFDYVREAGVNLTVHAGEDVTLpnlNTLYSAIQVLKVKRIGHGIRVAESQELIDMV 266

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2157343652 243 NDHRIPLEVCLTSNVQTRAAKSFESHPLPFYMSYGLRCTINTDNRLITDTTMTDEFWRAVQHYDLNIGDLRKLMIDGFKS 322
Cdd:PTZ00124  267 KEKDILLEVCPISNVLLNNAKSMDTHPIRKLYDAGVKVSVNSDDPGMFLTNINDDYEELYTHLNFTLADFMKMNEWALEK 346

                         330
                  ....*....|.
gi 2157343652 323 AFMPYRKKRTV 333
Cdd:PTZ00124  347 SFLDKDIKLKI 357
ADGF cd01321
Adenosine deaminase-related growth factors (ADGF), a novel family of secreted growth-factors ...
 7-335 5.17e-26

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: 107.36  E-value: 5.17e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2157343652   7 FIHRMPK-TDLHVHLDGSMRLSTILELAekegialpgnpqtedeLARAINIGAICEDLTDYLKAFDvtlsvmqteESLYR 85
Cdd:cd01321    20 IIQKMPKgALLHVHDTAMVSSDWLIKNA----------------TYRFEQIFDIIDGLLTYLPIFR---------DYYRR 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2157343652  86 AAFELGEDaareNVKYMEVRYS-PLLHTRNGLSYP------VIVEAVAEGLREAKRRYGLmsgQII-CGIRHMTPESSLR 157
Cdd:cd01321    75 LLEELYED----NVQYVELRSSfSPLYDLDGREYDyeetvqLLEEVVEKFKKTHPDFIGL---KIIyATLRNFNDSEIKE 147

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2157343652 158 MAELCVAFKNRG---VVGFDLAGAEADN-PAKDYREAFYLIRNNNVNLT--IHAGEAYGPES-----IHQAIHLGgAHRI 226
Cdd:cd01321   148 SMEQCLNLKKKFpdfIAGFDLVGQEDAGrPLLDFLPQLLWFPKQCAEIPffFHAGETNGDGTetdenLVDALLLN-TKRI 226

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2157343652 227 GHGTRLREDGDLLNFLNDHRIPLEVCLTSNVQTRAAKSFESHPLPFYMSYGLRCTINTDNRLITDTT-MTDEFWRAVQ-- 303
Cdd:cd01321   227 GHGFALPKHPLLMDLVKKKNIAIEVCPISNQVLGLVSDLRNHPAAALLARGVPVVISSDDPGFWGAKgLSHDFYQAFMgl 306

                         330       340       350
                  ....*....|....*....|....*....|....
gi 2157343652 304 -HYDLNIGDLRKLMIDGFK-SAFMPYRKKRTVTA 335
Cdd:cd01321   307 aPADAGLRGLKQLAENSIRySALSDQEKDEAVAK 340
metallo-dependent_hydrolases cd01292
Superfamily of metallo-dependent hydrolases (also called amidohydrolase superfamily) is a ...
 79-294 6.04e-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: 59.65  E-value: 6.04e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2157343652  79 TEESLYRAAFELGEDAARENVKYMEVRYSPLLHTRNGLSYpvivEAVAEGLREAKRRYGLMSGQIICGIRHMTPESSLRM 158
Cdd:cd01292    29 SPEDLYEDTLRALEALLAGGVTTVVDMGSTPPPTTTKAAI----EAVAEAARASAGIRVVLGLGIPGVPAAVDEDAEALL 104

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2157343652 159 AELCVAFKNRGVVGFDLAGAEADNPAKD--YREAFYLIRNNNVNLTIHAGEAYGPESIH----QAIHLGGAHRIGHGTRL 232
Cdd:cd01292   105 LELLRRGLELGAVGLKLAGPYTATGLSDesLRRVLEEARKLGLPVVIHAGELPDPTRALedlvALLRLGGRVVIGHVSHL 184

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2157343652 233 REdgDLLNFLNDHRIPLEVCLTSNVQTRAAKSFeSHPLPFYMSYGLRCTINTDNRLITDTTM 294
Cdd:cd01292   185 DP--ELLELLKEAGVSLEVCPLSNYLLGRDGEG-AEALRRLLELGIRVTLGTDGPPHPLGTD 243
PLN03055 PLN03055
AMP deaminase; Provisional
 170-331 5.24e-04

AMP deaminase; Provisional


Pssm-ID: 178613  Cd Length: 602  Bit Score: 42.16  E-value: 5.24e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2157343652 170 VVGFDLAGAEAD-------------------NPAKDYReAFYLIRN-------------NNVNLTIHAGEAygPESIHQA 217
Cdd:PLN03055  357 VVGFDMVDDESKperrptkhmqtpeqwdipfNPAYSYW-AYYVYANlytlnklreskglNTIKFRPHAGEA--GDIDHLA 433

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2157343652 218 IHLGGAHRIGHGTRLREDGDLLNFLNDHRIPLEVCLTSNvqTRAAKSFESHPLPFYMSYGLRCTINTDNRL---ITDTTM 294
Cdd:PLN03055  434 AAFLLAHNIAHGNNLRKSPGLQYLYYLAQIGLAMSPLSN--NSLFLDYHRNPFPMFFARGLNVSLSTDDPLqihLTKEPL 511

                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 2157343652 295 TDEFWRAVQHYDLNIGDLRKLMIDGFKSAFMPYRKKR 331
Cdd:PLN03055  512 VEEYSIAAQVWKLSSCDLCEIARNSVLQSGFPHASKK 548
AMPD cd01319
AMP deaminase (AMPD) catalyzes the hydrolytic deamination of adensosine monophosphate (AMP) at ...
 170-312 2.75e-03

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: 39.66  E-value: 2.75e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2157343652 170 VVGFDLAGAEAD-------------------NPAKDYReAFYLIRN-------------NNVNLTIHAGEAYGPESIHQA 217
Cdd:cd01319   267 VIGFDSVDDESKserrftrkfpkpeewtseeNPPYSYY-LYYMYANittlnsfrkargfNTFVLRPHCGEAGDIDHLASA 345

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2157343652 218 IHLggAHRIGHGTRLREDGDL--LNFLNdhRIPLEVCLTSNvqTRAAKSFESHPLPFYMSYGLRCTINTDNRLI---TDT 292
Cdd:cd01319   346 FLL--AHGISHGINLRKVPVLqyLYYLT--QIGIAMSPLSN--NSLFLSYEKNPFPEFFKRGLNVSLSTDDPLQfhfTKE 419

                         170       180
                  ....*....|....*....|
gi 2157343652 293 TMTDEFWRAVQHYDLNIGDL 312
Cdd:cd01319   420 PLMEEYSIAAQVWKLSTCDM 439
 
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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