NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|767983456|ref|XP_011519593|]
View 

adenosine deaminase-like protein isoform X1 [Homo sapiens]

Protein Classification

adenosine deaminase( domain architecture ID 10087349)

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

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

Name Accession Description Interval E-value
ADA_AMPD cd00443
Adenosine/AMP deaminase. Adenosine deaminases (ADAs) are present in pro- and eukaryotic ...
18-345 5.61e-115

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: 335.86  E-value: 5.61e-115
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767983456  18 LPKVELHAHLNGSISSHTMKKLIAQkpdlkihdqmtvidkgkkrtleECFQMFQTIHQLTSSPEDILMVTKDVIKEFADD 97
Cdd:cd00443    1 LPKVELHAHLSGSISPETLLELIKK----------------------EFFEKFLLVHNLLQKGEALARALKEVIEEFAED 58
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767983456  98 GVKYLELRSTPR-RENATGMTKKTYVESILEGIKQSKQENLDIDVRYLIAVDRRGGP----LVAKETVKLAEEFFLsteg 172
Cdd:cd00443   59 NVQYLELRTTPRlLETEKGLTKEQYWLLVIEGISEAKQWFPPIKVRLILSVDRRGPYvqnyLVASEILELAKFLSN---- 134
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767983456 173 TVLGLDLSGDPTVG--QAKDFLEPLLEAKKAG-LKLALHLSEIPNQKKETQiLLDLLPDRIGHGTFLNSGEggslDLVDF 249
Cdd:cd00443  135 YVVGIDLVGDESKGenPLRDFYSYYEYARRLGlLGLTLHCGETGNREELLQ-ALLLLPDRIGHGIFLLKHP----ELIYL 209
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767983456 250 VRQHRIPLELCLTSNVKSQTVPSYDQHHFGFWYSIAHPSVICTDDKGVFATHLSQEYQLAAETFNLTQSQVWDLSYESIN 329
Cdd:cd00443  210 VKLRNIPIEVCPTSNVVLGTVQSYEKHPFMRFFKAGLPVSLSTDDPGIFGTSLSEEYSLAAKTFGLTFEDLCELNRNSVL 289
                        330
                 ....*....|....*.
gi 767983456 330 YIFASDSTRSELRKKW 345
Cdd:cd00443  290 SSFAKDEEKKSLLEVL 305
 
Name Accession Description Interval E-value
ADA_AMPD cd00443
Adenosine/AMP deaminase. Adenosine deaminases (ADAs) are present in pro- and eukaryotic ...
18-345 5.61e-115

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: 335.86  E-value: 5.61e-115
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767983456  18 LPKVELHAHLNGSISSHTMKKLIAQkpdlkihdqmtvidkgkkrtleECFQMFQTIHQLTSSPEDILMVTKDVIKEFADD 97
Cdd:cd00443    1 LPKVELHAHLSGSISPETLLELIKK----------------------EFFEKFLLVHNLLQKGEALARALKEVIEEFAED 58
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767983456  98 GVKYLELRSTPR-RENATGMTKKTYVESILEGIKQSKQENLDIDVRYLIAVDRRGGP----LVAKETVKLAEEFFLsteg 172
Cdd:cd00443   59 NVQYLELRTTPRlLETEKGLTKEQYWLLVIEGISEAKQWFPPIKVRLILSVDRRGPYvqnyLVASEILELAKFLSN---- 134
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767983456 173 TVLGLDLSGDPTVG--QAKDFLEPLLEAKKAG-LKLALHLSEIPNQKKETQiLLDLLPDRIGHGTFLNSGEggslDLVDF 249
Cdd:cd00443  135 YVVGIDLVGDESKGenPLRDFYSYYEYARRLGlLGLTLHCGETGNREELLQ-ALLLLPDRIGHGIFLLKHP----ELIYL 209
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767983456 250 VRQHRIPLELCLTSNVKSQTVPSYDQHHFGFWYSIAHPSVICTDDKGVFATHLSQEYQLAAETFNLTQSQVWDLSYESIN 329
Cdd:cd00443  210 VKLRNIPIEVCPTSNVVLGTVQSYEKHPFMRFFKAGLPVSLSTDDPGIFGTSLSEEYSLAAKTFGLTFEDLCELNRNSVL 289
                        330
                 ....*....|....*.
gi 767983456 330 YIFASDSTRSELRKKW 345
Cdd:cd00443  290 SSFAKDEEKKSLLEVL 305
Add COG1816
Adenosine deaminase [Nucleotide transport and metabolism]; Adenosine deaminase is part of the ...
19-345 1.94e-57

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


Pssm-ID: 441421  Cd Length: 326  Bit Score: 189.14  E-value: 1.94e-57
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767983456  19 PKVELHAHLNGSISSHTMKKLIAQKP-DLKIHDQMTVIDKGKKRTLEECFQMFQTIHQLTSSPEDILMVTKDVIKEFADD 97
Cdd:COG1816    1 PKAELHLHLEGSLRPETLLELAARNGiDLPAADVEELRAAYDFRDLQSFLDTYDAGAAVLQTEEDFRRLAYEYLEDAAAD 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767983456  98 GVKYLELRSTPrrENAT--GMTKKTYVESILEGIKQSKQEnLDIDVRYLIAVDRRGGPLVAKETVKLAEEFflsTEGTVL 175
Cdd:COG1816   81 GVRYAEIRFDP--QLHTrrGLSLEEVVEAVLDGLREAERE-FGISVRLILCALRHLSPEAAFETLELALRY---RDRGVV 154
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767983456 176 GLDLSGDPTVGQAKDFLEPLLEAKKAGLKLALHLSE------IpnqkkeTQILLDLLPDRIGHGTflNSGEggSLDLVDF 249
Cdd:COG1816  155 GFGLAGDERGFPPEKFAEAFARAREAGLHLTAHAGEaggpesI------WEALDLLGAERIGHGV--RAIE--DPALVAR 224
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767983456 250 VRQHRIPLELCLTSNVKSQTVPSYDQHHF------GFwysiahPSVICTDDKGVFATHLSQEYQLAAETFNLTQSQVWDL 323
Cdd:COG1816  225 LADRGIPLEVCPTSNVQLGVVPSLAEHPLrrlldaGV------RVTLNTDDPLYFGTTLTDEYELAAEAFGLSDADLAQL 298
                        330       340
                 ....*....|....*....|..
gi 767983456 324 SYESINYIFASDSTRSELRKKW 345
Cdd:COG1816  299 ARNAIEASFLPEEEKAALLAEL 320
PRK09358 PRK09358
adenosine deaminase; Provisional
13-344 2.46e-55

adenosine deaminase; Provisional


Pssm-ID: 236480  Cd Length: 340  Bit Score: 184.22  E-value: 2.46e-55
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767983456  13 DFYSELPKVELHAHLNGSISSHTMKKLiAQKPDLKIHDQmTVIDKGKKRTLEEC--FQMFQTIHQLTSS----PEDILMV 86
Cdd:PRK09358   5 MIIRSLPKAELHLHLDGSLRPETILEL-ARRNGIALPAT-DVEELPWVRAAYDFrdLQSFLDKYDAGVAvlqtEEDLRRL 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767983456  87 TKDVIKEFADDGVKYLELRSTPRRENATGMTKKTYVESILEGIKQSKQEnLDIDVRYLIAVDRRGG-PLVAKETVKLAEE 165
Cdd:PRK09358  83 AFEYLEDAAADGVVYAEIRFDPQLHTERGLPLEEVVEAVLDGLRAAEAE-FGISVRLILCFMRHFGeEAAARELEALAAR 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767983456 166 FFlstEGTVLGLDLSGDPTVGQAKDFLEPLLEAKKAGLKLALHLSE--IPNQKKETqilLDLL-PDRIGHGTFLNsgegG 242
Cdd:PRK09358 162 YR---DDGVVGFDLAGDELGFPPSKFARAFDRARDAGLRLTAHAGEagGPESIWEA---LDELgAERIGHGVRAI----E 231
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767983456 243 SLDLVDFVRQHRIPLELCLTSNVKSQTVPSYDQHHF------GFWYSIAhpsvicTDDKGVFATHLSQEYQLAAETFNLT 316
Cdd:PRK09358 232 DPALMARLADRRIPLEVCPTSNVQTGAVPSLAEHPLktlldaGVRVTIN------TDDPLVFGTTLTEEYEALAEAFGLS 305
                        330       340
                 ....*....|....*....|....*...
gi 767983456 317 QSQVWDLSYESINYIFASDSTRSELRKK 344
Cdd:PRK09358 306 DEDLAQLARNALEAAFLSEEEKAALLAE 333
A_deaminase pfam00962
Adenosine deaminase;
19-344 9.46e-48

Adenosine deaminase;


Pssm-ID: 425964  Cd Length: 330  Bit Score: 164.14  E-value: 9.46e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767983456   19 PKVELHAHLNGSISSHTMKKLiAQKPDLKIHDQM--TVIDKGKKRTLEECFQMFQTIH----QLTSSPEDILMVTKDVIK 92
Cdd:pfam00962   1 PKAELHLHLDGSLRPDTLLEL-AKRYGIILPADFpeALEPLFRKYKKERDLQDFLDKYdigvAVLRSPEDIRRLAFEYAE 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767983456   93 EFADDGVKYLELRSTPRRENATGMTKKTYVESILEGIKQSKQEnLDIDVRYLIAVDRRGGPLVAKETVKLAEEFflsTEG 172
Cdd:pfam00962  80 DVAKDGVVYAEVRYDPQSHASRGLSPDTVVDAVLDAVDAAERE-FGITVRLIVCAMRHEHPECSREIAELAPRY---RDQ 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767983456  173 TVLGLDLSGDPTV---GQAKDFLEPLLEAKKAGLKLALHLSEIPNQKKETQILLDLLPDRIGHGTflNSGEGGSLdlVDF 249
Cdd:pfam00962 156 GIVAFGLAGDEKGfppSLFRDHVEAFARARDAGLHLTVHAGEAGGPQSVWEALDDLGAERIGHGV--RSAEDPRL--LDR 231
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767983456  250 VRQHRIPLELCLTSNVKSQTVPSYDQHHFGFWYSIAHPSVICTDDKGVFATHLSQEYQLAAETFNLTQSQVWDLSYESIN 329
Cdd:pfam00962 232 LADRQIPLEICPTSNVQTGAVASLAEHPLKTFLRAGVPVSLNTDDPLMFGSDLLDEYQVAKRAPGFDEEELARLAKNAVK 311
                         330
                  ....*....|....*
gi 767983456  330 YIFASDSTRSELRKK 344
Cdd:pfam00962 312 GSFLPADEKRALLDE 326
aden_deam TIGR01430
adenosine deaminase; This family includes the experimentally verified adenosine deaminases of ...
18-341 1.45e-47

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: 163.68  E-value: 1.45e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767983456   18 LPKVELHAHLNGSISSHTMKKLiAQKPDLKIHDQMTVIDKGKKR-TLEECFQMFQTIH----QLTSSPEDILMVTKDVIK 92
Cdd:TIGR01430   1 LPKAELHLHLEGSIRPETLLEL-AQKNGIPLPADLQSGEELKEAyDKFRDLQDFLAKYdfgvEVLRTEDDFKRLAYEYVE 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767983456   93 EFADDGVKYLELRSTPRRENATGMTKKTYVESILEGIKQSKQEnLDIDVRYLIAVDRRGGPLVAKETVKLAEEFflsTEG 172
Cdd:TIGR01430  80 KAAKDGVVYAEVFFDPQLHTNRGISPDTVVEAVLDGLDEAERD-FGIKSRLILCGMRHKQPEAAEETLELAKPY---KEQ 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767983456  173 TVLGLDLSGDPTVGQAKDFLEPLLEAKKAGLKLALHLSEIPNQKKETQILLDLLPDRIGHGTFLNSGEggslDLVDFVRQ 252
Cdd:TIGR01430 156 TIVGFGLAGDERGGPPPDFVRAFAIARELGLHLTVHAGELGGPESVREALDDLGATRIGHGVRALEDP----ELLKRLAQ 231
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767983456  253 HRIPLELCLTSNVKSQTVPSYDQHHFGFWYSIAHPSVICTDDKGVFATHLSQEYQLAAETFNLTQSQVWDLSYESINYIF 332
Cdd:TIGR01430 232 ENITLEVCPTSNVALGVVKSLAEHPLRRFLEAGVKVTLNSDDPAYFGSYLTEEYEIAAKHAGLTEEELKQLARNALEGSF 311

                  ....*....
gi 767983456  333 ASDSTRSEL 341
Cdd:TIGR01430 312 LSDDEKKEL 320
 
Name Accession Description Interval E-value
ADA_AMPD cd00443
Adenosine/AMP deaminase. Adenosine deaminases (ADAs) are present in pro- and eukaryotic ...
18-345 5.61e-115

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: 335.86  E-value: 5.61e-115
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767983456  18 LPKVELHAHLNGSISSHTMKKLIAQkpdlkihdqmtvidkgkkrtleECFQMFQTIHQLTSSPEDILMVTKDVIKEFADD 97
Cdd:cd00443    1 LPKVELHAHLSGSISPETLLELIKK----------------------EFFEKFLLVHNLLQKGEALARALKEVIEEFAED 58
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767983456  98 GVKYLELRSTPR-RENATGMTKKTYVESILEGIKQSKQENLDIDVRYLIAVDRRGGP----LVAKETVKLAEEFFLsteg 172
Cdd:cd00443   59 NVQYLELRTTPRlLETEKGLTKEQYWLLVIEGISEAKQWFPPIKVRLILSVDRRGPYvqnyLVASEILELAKFLSN---- 134
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767983456 173 TVLGLDLSGDPTVG--QAKDFLEPLLEAKKAG-LKLALHLSEIPNQKKETQiLLDLLPDRIGHGTFLNSGEggslDLVDF 249
Cdd:cd00443  135 YVVGIDLVGDESKGenPLRDFYSYYEYARRLGlLGLTLHCGETGNREELLQ-ALLLLPDRIGHGIFLLKHP----ELIYL 209
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767983456 250 VRQHRIPLELCLTSNVKSQTVPSYDQHHFGFWYSIAHPSVICTDDKGVFATHLSQEYQLAAETFNLTQSQVWDLSYESIN 329
Cdd:cd00443  210 VKLRNIPIEVCPTSNVVLGTVQSYEKHPFMRFFKAGLPVSLSTDDPGIFGTSLSEEYSLAAKTFGLTFEDLCELNRNSVL 289
                        330
                 ....*....|....*.
gi 767983456 330 YIFASDSTRSELRKKW 345
Cdd:cd00443  290 SSFAKDEEKKSLLEVL 305
ADA cd01320
Adenosine deaminase (ADA) is a monomeric zinc dependent enzyme which catalyzes the ...
17-344 3.27e-62

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: 201.66  E-value: 3.27e-62
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767983456  17 ELPKVELHAHLNGSISSHTMKKLIAQK----PDLKIHDQMTVIDKGKKRTLEECFQMFQTIHQLTSSPEDILMVTKDVIK 92
Cdd:cd01320    1 NLPKAELHLHLDGSLRPETILELAKKNgitlPASDVELLELVVAAYNFSDLQDFLAKYDFGLSVLQTEEDFERLAYEYLE 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767983456  93 EFADDGVKYLELRSTPRRENATGMTKKTYVESILEGIKQSKqENLDIDVRYLIAVDRRGGPLVAKETVKLAEEFflsTEG 172
Cdd:cd01320   81 DAAADGVVYAEIRFSPQLHTRRGLSFDEVVEAVLRGLDEAE-AEFGIKARLILCGLRHLSPESAQETLELALKY---RDK 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767983456 173 TVLGLDLSGDPTVGQAKDFLEPLLEAKKAGLKLALHLSEIPNQKKETQILLDLLPDRIGHGTFLnsgeGGSLDLVDFVRQ 252
Cdd:cd01320  157 GVVGFDLAGDEVGFPPEKFVRAFQRAREAGLRLTAHAGEAGGPESVRDALDLLGAERIGHGIRA----IEDPELVKRLAE 232
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767983456 253 HRIPLELCLTSNVKSQTVPSYDQHHFGFWYSIAHPSVICTDDKGVFATHLSQEYQLAAETFNLTQSQVWDLSYESINYIF 332
Cdd:cd01320  233 RNIPLEVCPTSNVQTGAVKSLAEHPLRELLDAGVKVTINTDDPTVFGTYLTDEYELLAEAFGLTEEELKKLARNAVEASF 312
                        330
                 ....*....|..
gi 767983456 333 ASDSTRSELRKK 344
Cdd:cd01320  313 LSEEEKAELLKR 324
Add COG1816
Adenosine deaminase [Nucleotide transport and metabolism]; Adenosine deaminase is part of the ...
19-345 1.94e-57

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


Pssm-ID: 441421  Cd Length: 326  Bit Score: 189.14  E-value: 1.94e-57
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767983456  19 PKVELHAHLNGSISSHTMKKLIAQKP-DLKIHDQMTVIDKGKKRTLEECFQMFQTIHQLTSSPEDILMVTKDVIKEFADD 97
Cdd:COG1816    1 PKAELHLHLEGSLRPETLLELAARNGiDLPAADVEELRAAYDFRDLQSFLDTYDAGAAVLQTEEDFRRLAYEYLEDAAAD 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767983456  98 GVKYLELRSTPrrENAT--GMTKKTYVESILEGIKQSKQEnLDIDVRYLIAVDRRGGPLVAKETVKLAEEFflsTEGTVL 175
Cdd:COG1816   81 GVRYAEIRFDP--QLHTrrGLSLEEVVEAVLDGLREAERE-FGISVRLILCALRHLSPEAAFETLELALRY---RDRGVV 154
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767983456 176 GLDLSGDPTVGQAKDFLEPLLEAKKAGLKLALHLSE------IpnqkkeTQILLDLLPDRIGHGTflNSGEggSLDLVDF 249
Cdd:COG1816  155 GFGLAGDERGFPPEKFAEAFARAREAGLHLTAHAGEaggpesI------WEALDLLGAERIGHGV--RAIE--DPALVAR 224
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767983456 250 VRQHRIPLELCLTSNVKSQTVPSYDQHHF------GFwysiahPSVICTDDKGVFATHLSQEYQLAAETFNLTQSQVWDL 323
Cdd:COG1816  225 LADRGIPLEVCPTSNVQLGVVPSLAEHPLrrlldaGV------RVTLNTDDPLYFGTTLTDEYELAAEAFGLSDADLAQL 298
                        330       340
                 ....*....|....*....|..
gi 767983456 324 SYESINYIFASDSTRSELRKKW 345
Cdd:COG1816  299 ARNAIEASFLPEEEKAALLAEL 320
PRK09358 PRK09358
adenosine deaminase; Provisional
13-344 2.46e-55

adenosine deaminase; Provisional


Pssm-ID: 236480  Cd Length: 340  Bit Score: 184.22  E-value: 2.46e-55
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767983456  13 DFYSELPKVELHAHLNGSISSHTMKKLiAQKPDLKIHDQmTVIDKGKKRTLEEC--FQMFQTIHQLTSS----PEDILMV 86
Cdd:PRK09358   5 MIIRSLPKAELHLHLDGSLRPETILEL-ARRNGIALPAT-DVEELPWVRAAYDFrdLQSFLDKYDAGVAvlqtEEDLRRL 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767983456  87 TKDVIKEFADDGVKYLELRSTPRRENATGMTKKTYVESILEGIKQSKQEnLDIDVRYLIAVDRRGG-PLVAKETVKLAEE 165
Cdd:PRK09358  83 AFEYLEDAAADGVVYAEIRFDPQLHTERGLPLEEVVEAVLDGLRAAEAE-FGISVRLILCFMRHFGeEAAARELEALAAR 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767983456 166 FFlstEGTVLGLDLSGDPTVGQAKDFLEPLLEAKKAGLKLALHLSE--IPNQKKETqilLDLL-PDRIGHGTFLNsgegG 242
Cdd:PRK09358 162 YR---DDGVVGFDLAGDELGFPPSKFARAFDRARDAGLRLTAHAGEagGPESIWEA---LDELgAERIGHGVRAI----E 231
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767983456 243 SLDLVDFVRQHRIPLELCLTSNVKSQTVPSYDQHHF------GFWYSIAhpsvicTDDKGVFATHLSQEYQLAAETFNLT 316
Cdd:PRK09358 232 DPALMARLADRRIPLEVCPTSNVQTGAVPSLAEHPLktlldaGVRVTIN------TDDPLVFGTTLTEEYEALAEAFGLS 305
                        330       340
                 ....*....|....*....|....*...
gi 767983456 317 QSQVWDLSYESINYIFASDSTRSELRKK 344
Cdd:PRK09358 306 DEDLAQLARNALEAAFLSEEEKAALLAE 333
A_deaminase pfam00962
Adenosine deaminase;
19-344 9.46e-48

Adenosine deaminase;


Pssm-ID: 425964  Cd Length: 330  Bit Score: 164.14  E-value: 9.46e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767983456   19 PKVELHAHLNGSISSHTMKKLiAQKPDLKIHDQM--TVIDKGKKRTLEECFQMFQTIH----QLTSSPEDILMVTKDVIK 92
Cdd:pfam00962   1 PKAELHLHLDGSLRPDTLLEL-AKRYGIILPADFpeALEPLFRKYKKERDLQDFLDKYdigvAVLRSPEDIRRLAFEYAE 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767983456   93 EFADDGVKYLELRSTPRRENATGMTKKTYVESILEGIKQSKQEnLDIDVRYLIAVDRRGGPLVAKETVKLAEEFflsTEG 172
Cdd:pfam00962  80 DVAKDGVVYAEVRYDPQSHASRGLSPDTVVDAVLDAVDAAERE-FGITVRLIVCAMRHEHPECSREIAELAPRY---RDQ 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767983456  173 TVLGLDLSGDPTV---GQAKDFLEPLLEAKKAGLKLALHLSEIPNQKKETQILLDLLPDRIGHGTflNSGEGGSLdlVDF 249
Cdd:pfam00962 156 GIVAFGLAGDEKGfppSLFRDHVEAFARARDAGLHLTVHAGEAGGPQSVWEALDDLGAERIGHGV--RSAEDPRL--LDR 231
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767983456  250 VRQHRIPLELCLTSNVKSQTVPSYDQHHFGFWYSIAHPSVICTDDKGVFATHLSQEYQLAAETFNLTQSQVWDLSYESIN 329
Cdd:pfam00962 232 LADRQIPLEICPTSNVQTGAVASLAEHPLKTFLRAGVPVSLNTDDPLMFGSDLLDEYQVAKRAPGFDEEELARLAKNAVK 311
                         330
                  ....*....|....*
gi 767983456  330 YIFASDSTRSELRKK 344
Cdd:pfam00962 312 GSFLPADEKRALLDE 326
aden_deam TIGR01430
adenosine deaminase; This family includes the experimentally verified adenosine deaminases of ...
18-341 1.45e-47

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: 163.68  E-value: 1.45e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767983456   18 LPKVELHAHLNGSISSHTMKKLiAQKPDLKIHDQMTVIDKGKKR-TLEECFQMFQTIH----QLTSSPEDILMVTKDVIK 92
Cdd:TIGR01430   1 LPKAELHLHLEGSIRPETLLEL-AQKNGIPLPADLQSGEELKEAyDKFRDLQDFLAKYdfgvEVLRTEDDFKRLAYEYVE 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767983456   93 EFADDGVKYLELRSTPRRENATGMTKKTYVESILEGIKQSKQEnLDIDVRYLIAVDRRGGPLVAKETVKLAEEFflsTEG 172
Cdd:TIGR01430  80 KAAKDGVVYAEVFFDPQLHTNRGISPDTVVEAVLDGLDEAERD-FGIKSRLILCGMRHKQPEAAEETLELAKPY---KEQ 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767983456  173 TVLGLDLSGDPTVGQAKDFLEPLLEAKKAGLKLALHLSEIPNQKKETQILLDLLPDRIGHGTFLNSGEggslDLVDFVRQ 252
Cdd:TIGR01430 156 TIVGFGLAGDERGGPPPDFVRAFAIARELGLHLTVHAGELGGPESVREALDDLGATRIGHGVRALEDP----ELLKRLAQ 231
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767983456  253 HRIPLELCLTSNVKSQTVPSYDQHHFGFWYSIAHPSVICTDDKGVFATHLSQEYQLAAETFNLTQSQVWDLSYESINYIF 332
Cdd:TIGR01430 232 ENITLEVCPTSNVALGVVKSLAEHPLRRFLEAGVKVTLNSDDPAYFGSYLTEEYEIAAKHAGLTEEELKQLARNALEGSF 311

                  ....*....
gi 767983456  333 ASDSTRSEL 341
Cdd:TIGR01430 312 LSDDEKKEL 320
ADGF cd01321
Adenosine deaminase-related growth factors (ADGF), a novel family of secreted growth-factors ...
23-346 4.17e-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: 81.16  E-value: 4.17e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767983456  23 LHAHLNGSISSHTMKKLIAQKPDlkihdqmtvidkgkkrtleecfQMFQTIHQL-TSSPedilmVTKDVI----KEFADD 97
Cdd:cd01321   30 LHVHDTAMVSSDWLIKNATYRFE----------------------QIFDIIDGLlTYLP-----IFRDYYrrllEELYED 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767983456  98 GVKYLELRSTPRRENATGMTKKTYVES--ILEGI--KQSKQENLDIDVRYLIAVDRRGGPLVAKETVKLAEEFFLSTEGT 173
Cdd:cd01321   83 NVQYVELRSSFSPLYDLDGREYDYEETvqLLEEVveKFKKTHPDFIGLKIIYATLRNFNDSEIKESMEQCLNLKKKFPDF 162
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767983456 174 VLGLDLSGDPTVGQA-KDFLEPLLEAKK--AGLKLALHLSEIPNQKKETQI-LLD-LLPD--RIGHGTflnsgeggSL-- 244
Cdd:cd01321  163 IAGFDLVGQEDAGRPlLDFLPQLLWFPKqcAEIPFFFHAGETNGDGTETDEnLVDaLLLNtkRIGHGF--------ALpk 234
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767983456 245 --DLVDFVRQHRIPLELCLTSNVKSQTVPSYDQHHFGFWYSIAHPSVICTDDKGVF-ATHLSQE-YQ----LAAETFNLT 316
Cdd:cd01321  235 hpLLMDLVKKKNIAIEVCPISNQVLGLVSDLRNHPAAALLARGVPVVISSDDPGFWgAKGLSHDfYQafmgLAPADAGLR 314
                        330       340       350
                 ....*....|....*....|....*....|..
gi 767983456 317 Q--SQVWDlsyeSINYIFASDSTRSELRKKWN 346
Cdd:cd01321  315 GlkQLAEN----SIRYSALSDQEKDEAVAKWE 342
PTZ00124 PTZ00124
adenosine deaminase; Provisional
15-345 5.59e-16

adenosine deaminase; Provisional


Pssm-ID: 173415  Cd Length: 362  Bit Score: 77.98  E-value: 5.59e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767983456  15 YSELPKVELHAHLNGSISshtMKKLIAQKPDLKIHDQMT---VID----KGKKRTLEECFQMFQTIHQLTSSPEDILMVT 87
Cdd:PTZ00124  32 WKRIPKCELHCHLDLCFS---VDFFLSCIRKYNLQPNLSdeeILDyylfAKGGKSLGEFVEKAIRVADIFNDYEVIEDLA 108
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767983456  88 KDVIKEFADDGVKYLELRSTPR-RENATGMTKKTYVESILEGIKQSKQEnldIDVRYLIAVDRRGGPLVAKETVKLAEEF 166
Cdd:PTZ00124 109 KHAVFNKYKEGVVLMEFRYSPTfVAFKHNLDIDLIHQAIVKGIKEAVEL---LDHKIEVGLLCIGDTGHDAAPIKESADF 185
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767983456 167 FLSTEGTVLGLDLSGDPTvgQAKDFLEPLLEAKKAGLKLALHLSE---IPNQKKETQILLDLLPDRIGHGTFLNSgeggS 243
Cdd:PTZ00124 186 CLKHKADFVGFDHAGHEV--DLKPFKDIFDYVREAGVNLTVHAGEdvtLPNLNTLYSAIQVLKVKRIGHGIRVAE----S 259
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767983456 244 LDLVDFVRQHRIPLELCLTSNVKSQTVPSYDQHHFGFWYSIAHPSVICTDDKGVFATHLSQEYQLAAETFNLTQSQVWDL 323
Cdd:PTZ00124 260 QELIDMVKEKDILLEVCPISNVLLNNAKSMDTHPIRKLYDAGVKVSVNSDDPGMFLTNINDDYEELYTHLNFTLADFMKM 339
                        330       340
                 ....*....|....*....|..
gi 767983456 324 SYESINYIFASDSTRSELRKKW 345
Cdd:PTZ00124 340 NEWALEKSFLDKDIKLKIKKLY 361
archeal_chlorohydrolases cd01305
Predicted chlorohydrolases. These metallo-dependent hydrolases from archea are part of the ...
97-264 3.07e-07

Predicted chlorohydrolases. These metallo-dependent hydrolases from archea are part of the superfamily of metallo-dependent hydrolases, a large group of proteins that show conservation in their 3-dimensional fold (TIM barrel) and in details of their active site. They have a conserved metal binding site, involving four histidines and one aspartic acid residue. In the common reaction mechanism, the metal ion (or ions) deprotonate a water molecule for a nucleophilic attack on the substrate. Some members of this subgroup are predicted to be chlorohyrolases.


Pssm-ID: 238630 [Multi-domain]  Cd Length: 263  Bit Score: 50.86  E-value: 3.07e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767983456  97 DGVKYLELRSTPRRENATGMtKKT--------------YVESILEGIKQSKQENLDIDVRYLIAVDRRGGPLVAKETVKL 162
Cdd:cd01305   35 DGLKHRLLAQADDRELAEAM-RKVlrdmretgigafadFREGGVEGIELLRRALGKLPVPFEVILGRPTEPDDPEILLEV 113
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767983456 163 AEefflstegtvlGLDLSG--DPtvgqakDFLEPLLEAKKAGLKLALHLSEIPNQKKETQI--LLDLLPDRIGHGTFLNS 238
Cdd:cd01305  114 AD-----------GLGLSSanDV------DLEDILELLRRRGKLFAIHASETRESVGMTDIerALDLEPDLLVHGTHLTD 176
                        170       180
                 ....*....|....*....|....*.
gi 767983456 239 GEggsldlVDFVRQHRIPLELCLTSN 264
Cdd:cd01305  177 ED------LELVRENGVPVVLCPRSN 196
metallo-dependent_hydrolases cd01292
Superfamily of metallo-dependent hydrolases (also called amidohydrolase superfamily) is a ...
79-311 5.85e-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: 44.25  E-value: 5.85e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767983456  79 SPEDILMVTKDVIKEFADDGVKYLELRSTprreNATGMTKKTYVESILEGIkqskQENLDIDVRYLIAVDRRGGPLVAKE 158
Cdd:cd01292   29 SPEDLYEDTLRALEALLAGGVTTVVDMGS----TPPPTTTKAAIEAVAEAA----RASAGIRVVLGLGIPGVPAAVDEDA 100
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767983456 159 TVKLAEEFFLSTEGTVLGLDLSGDPTVGQAKD--FLEPLLEAKKAGLKLALHLSEIPNQKKETQILLDLL----PDRIGH 232
Cdd:cd01292  101 EALLLELLRRGLELGAVGLKLAGPYTATGLSDesLRRVLEEARKLGLPVVIHAGELPDPTRALEDLVALLrlggRVVIGH 180
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767983456 233 GTFLnsgeggSLDLVDFVRQHRIPLELCLTSNVKSqTVPSYDQHHFGFWYSIAHPSVICTDDKGVF-ATHLSQEYQLAAE 311
Cdd:cd01292  181 VSHL------DPELLELLKEAGVSLEVCPLSNYLL-GRDGEGAEALRRLLELGIRVTLGTDGPPHPlGTDLLALLRLLLK 253
Amidohydro_1 pfam01979
Amidohydrolase family; This family of enzymes are a a large metal dependent hydrolase ...
112-258 4.29e-04

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


Pssm-ID: 460401 [Multi-domain]  Cd Length: 334  Bit Score: 41.72  E-value: 4.29e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767983456  112 NATGMTKKTYVESILEGIkqskqENLDIDVRYLIAV-------DRRGGPLVAKETVKLAE-EFFLSTEGTVLGLDLSGDP 183
Cdd:pfam01979  48 LDMGATTSTGIEALLEAA-----EELPLGLRFLGPGcsldtdgELEGRKALREKLKAGAEfIKGMADGVVFVGLAPHGAP 122
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 767983456  184 TVGqaKDFLEPLLE-AKKAGLKLALHLSEipnQKKETQILLDLLPDRIGHGTFL-NSGEGGSLDLVDFVRQHRIPLE 258
Cdd:pfam01979 123 TFS--DDELKAALEeAKKYGLPVAIHALE---TKGEVEDAIAAFGGGIEHGTHLeVAESGGLLDIIKLILAHGVHLS 194
 
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH