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Conserved domains on  [gi|2462542973|ref|XP_054233368|]
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adenosine deaminase-like protein isoform X3 [Homo sapiens]

Protein Classification

adenosine deaminase( domain architecture ID 10087349)

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

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
ADA_AMPD cd00443
Adenosine/AMP deaminase. Adenosine deaminases (ADAs) are present in pro- and eukaryotic ...
 29-310 8.06e-104

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: 306.20  E-value: 8.06e-104
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462542973  29 EECFQMFQTIHQLTSSPEDILMVTKDVIKEFADDGVKYLELRSTPR-RENATGMTKKTYVESILEGIKQSKQENLDIDVR 107
Cdd:cd00443    25 KEFFEKFLLVHNLLQKGEALARALKEVIEEFAEDNVQYLELRTTPRlLETEKGLTKEQYWLLVIEGISEAKQWFPPIKVR 104

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462542973 108 YLIAVDRRGGP----LVAKETVKLAEEFFLstegTVLGLDLSGDPTVG--QAKDFLEPLLEAKKAG-LKLALHLSEIPNQ 180
Cdd:cd00443   105 LILSVDRRGPYvqnyLVASEILELAKFLSN----YVVGIDLVGDESKGenPLRDFYSYYEYARRLGlLGLTLHCGETGNR 180

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462542973 181 KKETQiLLDLLPDRIGHGTFLNSGEggslDLVDFVRQHRIPLELCLTSNVKSQTVPSYDQHHFGFWYSIAHPSVICTDDK 260
Cdd:cd00443   181 EELLQ-ALLLLPDRIGHGIFLLKHP----ELIYLVKLRNIPIEVCPTSNVVLGTVQSYEKHPFMRFFKAGLPVSLSTDDP 255

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|
gi 2462542973 261 GVFATHLSQEYQLAAETFNLTQSQVWDLSYESINYIFASDSTRSELRKKW 310
Cdd:cd00443   256 GIFGTSLSEEYSLAAKTFGLTFEDLCELNRNSVLSSFAKDEEKKSLLEVL 305
 
Name Accession Description Interval E-value
ADA_AMPD cd00443
Adenosine/AMP deaminase. Adenosine deaminases (ADAs) are present in pro- and eukaryotic ...
 29-310 8.06e-104

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: 306.20  E-value: 8.06e-104
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462542973  29 EECFQMFQTIHQLTSSPEDILMVTKDVIKEFADDGVKYLELRSTPR-RENATGMTKKTYVESILEGIKQSKQENLDIDVR 107
Cdd:cd00443    25 KEFFEKFLLVHNLLQKGEALARALKEVIEEFAEDNVQYLELRTTPRlLETEKGLTKEQYWLLVIEGISEAKQWFPPIKVR 104

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462542973 108 YLIAVDRRGGP----LVAKETVKLAEEFFLstegTVLGLDLSGDPTVG--QAKDFLEPLLEAKKAG-LKLALHLSEIPNQ 180
Cdd:cd00443   105 LILSVDRRGPYvqnyLVASEILELAKFLSN----YVVGIDLVGDESKGenPLRDFYSYYEYARRLGlLGLTLHCGETGNR 180

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462542973 181 KKETQiLLDLLPDRIGHGTFLNSGEggslDLVDFVRQHRIPLELCLTSNVKSQTVPSYDQHHFGFWYSIAHPSVICTDDK 260
Cdd:cd00443   181 EELLQ-ALLLLPDRIGHGIFLLKHP----ELIYLVKLRNIPIEVCPTSNVVLGTVQSYEKHPFMRFFKAGLPVSLSTDDP 255

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|
gi 2462542973 261 GVFATHLSQEYQLAAETFNLTQSQVWDLSYESINYIFASDSTRSELRKKW 310
Cdd:cd00443   256 GIFGTSLSEEYSLAAKTFGLTFEDLCELNRNSVLSSFAKDEEKKSLLEVL 305
Add COG1816
Adenosine deaminase [Nucleotide transport and metabolism]; Adenosine deaminase is part of the ...
 44-310 4.22e-50

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


Pssm-ID: 441421  Cd Length: 326  Bit Score: 169.11  E-value: 4.22e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462542973  44 SPEDILMVTKDVIKEFADDGVKYLELRSTPrrENAT--GMTKKTYVESILEGIKQSKQEnLDIDVRYLIAVDRRGGPLVA 121
Cdd:COG1816    62 TEEDFRRLAYEYLEDAAADGVRYAEIRFDP--QLHTrrGLSLEEVVEAVLDGLREAERE-FGISVRLILCALRHLSPEAA 138

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462542973 122 KETVKLAEEFflsTEGTVLGLDLSGDPTVGQAKDFLEPLLEAKKAGLKLALHLSE------IpnqkkeTQILLDLLPDRI 195
Cdd:COG1816   139 FETLELALRY---RDRGVVGFGLAGDERGFPPEKFAEAFARAREAGLHLTAHAGEaggpesI------WEALDLLGAERI 209

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462542973 196 GHGTflNSGEggSLDLVDFVRQHRIPLELCLTSNVKSQTVPSYDQHHF------GFwysiahPSVICTDDKGVFATHLSQ 269
Cdd:COG1816   210 GHGV--RAIE--DPALVARLADRGIPLEVCPTSNVQLGVVPSLAEHPLrrlldaGV------RVTLNTDDPLYFGTTLTD 279

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|.
gi 2462542973 270 EYQLAAETFNLTQSQVWDLSYESINYIFASDSTRSELRKKW 310
Cdd:COG1816   280 EYELAAEAFGLSDADLAQLARNAIEASFLPEEEKAALLAEL 320
PRK09358 PRK09358
adenosine deaminase; Provisional
 26-309 9.92e-45

adenosine deaminase; Provisional


Pssm-ID: 236480  Cd Length: 340  Bit Score: 155.33  E-value: 9.92e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462542973  26 RTLEECFQMF-QTIHQLTSsPEDILMVTKDVIKEFADDGVKYLELRSTPRRENATGMTKKTYVESILEGIKQSKQEnLDI 104
Cdd:PRK09358   57 RDLQSFLDKYdAGVAVLQT-EEDLRRLAFEYLEDAAADGVVYAEIRFDPQLHTERGLPLEEVVEAVLDGLRAAEAE-FGI 134

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462542973 105 DVRYLIAVDRRGG-PLVAKETVKLAEEFFlstEGTVLGLDLSGDPTVGQAKDFLEPLLEAKKAGLKLALHLSE--IPNQK 181
Cdd:PRK09358  135 SVRLILCFMRHFGeEAAARELEALAARYR---DDGVVGFDLAGDELGFPPSKFARAFDRARDAGLRLTAHAGEagGPESI 211

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462542973 182 KETqilLDLL-PDRIGHGTFLNsgegGSLDLVDFVRQHRIPLELCLTSNVKSQTVPSYDQHHF------GFWYSIAhpsv 254
Cdd:PRK09358  212 WEA---LDELgAERIGHGVRAI----EDPALMARLADRRIPLEVCPTSNVQTGAVPSLAEHPLktlldaGVRVTIN---- 280

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 2462542973 255 icTDDKGVFATHLSQEYQLAAETFNLTQSQVWDLSYESINYIFASDSTRSELRKK 309
Cdd:PRK09358  281 --TDDPLVFGTTLTEEYEALAEAFGLSDEDLAQLARNALEAAFLSEEEKAALLAE 333
A_deaminase pfam00962
Adenosine deaminase;
24-309 3.68e-41

Adenosine deaminase;


Pssm-ID: 425964  Cd Length: 330  Bit Score: 146.04  E-value: 3.68e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462542973  24 KKRTLEECFQMFQTIHQLTSSPEDILMVTKDVIKEFADDGVKYLELRSTPRRENATGMTKKTYVESILEGIKQSKQEnLD 103
Cdd:pfam00962  46 KERDLQDFLDKYDIGVAVLRSPEDIRRLAFEYAEDVAKDGVVYAEVRYDPQSHASRGLSPDTVVDAVLDAVDAAERE-FG 124

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462542973 104 IDVRYLIAVDRRGGPLVAKETVKLAEEFflsTEGTVLGLDLSGDPTV---GQAKDFLEPLLEAKKAGLKLALHLSEIPNQ 180
Cdd:pfam00962 125 ITVRLIVCAMRHEHPECSREIAELAPRY---RDQGIVAFGLAGDEKGfppSLFRDHVEAFARARDAGLHLTVHAGEAGGP 201

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462542973 181 KKETQILLDLLPDRIGHGTflNSGEGGSLdlVDFVRQHRIPLELCLTSNVKSQTVPSYDQHHFGFWYSIAHPSVICTDDK 260
Cdd:pfam00962 202 QSVWEALDDLGAERIGHGV--RSAEDPRL--LDRLADRQIPLEICPTSNVQTGAVASLAEHPLKTFLRAGVPVSLNTDDP 277

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*....
gi 2462542973 261 GVFATHLSQEYQLAAETFNLTQSQVWDLSYESINYIFASDSTRSELRKK 309
Cdd:pfam00962 278 LMFGSDLLDEYQVAKRAPGFDEEELARLAKNAVKGSFLPADEKRALLDE 326
 
Name Accession Description Interval E-value
ADA_AMPD cd00443
Adenosine/AMP deaminase. Adenosine deaminases (ADAs) are present in pro- and eukaryotic ...
 29-310 8.06e-104

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: 306.20  E-value: 8.06e-104
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462542973  29 EECFQMFQTIHQLTSSPEDILMVTKDVIKEFADDGVKYLELRSTPR-RENATGMTKKTYVESILEGIKQSKQENLDIDVR 107
Cdd:cd00443    25 KEFFEKFLLVHNLLQKGEALARALKEVIEEFAEDNVQYLELRTTPRlLETEKGLTKEQYWLLVIEGISEAKQWFPPIKVR 104

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462542973 108 YLIAVDRRGGP----LVAKETVKLAEEFFLstegTVLGLDLSGDPTVG--QAKDFLEPLLEAKKAG-LKLALHLSEIPNQ 180
Cdd:cd00443   105 LILSVDRRGPYvqnyLVASEILELAKFLSN----YVVGIDLVGDESKGenPLRDFYSYYEYARRLGlLGLTLHCGETGNR 180

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462542973 181 KKETQiLLDLLPDRIGHGTFLNSGEggslDLVDFVRQHRIPLELCLTSNVKSQTVPSYDQHHFGFWYSIAHPSVICTDDK 260
Cdd:cd00443   181 EELLQ-ALLLLPDRIGHGIFLLKHP----ELIYLVKLRNIPIEVCPTSNVVLGTVQSYEKHPFMRFFKAGLPVSLSTDDP 255

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|
gi 2462542973 261 GVFATHLSQEYQLAAETFNLTQSQVWDLSYESINYIFASDSTRSELRKKW 310
Cdd:cd00443   256 GIFGTSLSEEYSLAAKTFGLTFEDLCELNRNSVLSSFAKDEEKKSLLEVL 305
ADA cd01320
Adenosine deaminase (ADA) is a monomeric zinc dependent enzyme which catalyzes the ...
 44-309 1.40e-51

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: 172.77  E-value: 1.40e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462542973  44 SPEDILMVTKDVIKEFADDGVKYLELRSTPRRENATGMTKKTYVESILEGIKQSKqENLDIDVRYLIAVDRRGGPLVAKE 123
Cdd:cd01320    67 TEEDFERLAYEYLEDAAADGVVYAEIRFSPQLHTRRGLSFDEVVEAVLRGLDEAE-AEFGIKARLILCGLRHLSPESAQE 145

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462542973 124 TVKLAEEFflsTEGTVLGLDLSGDPTVGQAKDFLEPLLEAKKAGLKLALHLSEIPNQKKETQILLDLLPDRIGHGTFLns 203
Cdd:cd01320   146 TLELALKY---RDKGVVGFDLAGDEVGFPPEKFVRAFQRAREAGLRLTAHAGEAGGPESVRDALDLLGAERIGHGIRA-- 220

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462542973 204 geGGSLDLVDFVRQHRIPLELCLTSNVKSQTVPSYDQHHFGFWYSIAHPSVICTDDKGVFATHLSQEYQLAAETFNLTQS 283
Cdd:cd01320   221 --IEDPELVKRLAERNIPLEVCPTSNVQTGAVKSLAEHPLRELLDAGVKVTINTDDPTVFGTYLTDEYELLAEAFGLTEE 298

                         250       260
                  ....*....|....*....|....*.
gi 2462542973 284 QVWDLSYESINYIFASDSTRSELRKK 309
Cdd:cd01320   299 ELKKLARNAVEASFLSEEEKAELLKR 324
Add COG1816
Adenosine deaminase [Nucleotide transport and metabolism]; Adenosine deaminase is part of the ...
 44-310 4.22e-50

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


Pssm-ID: 441421  Cd Length: 326  Bit Score: 169.11  E-value: 4.22e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462542973  44 SPEDILMVTKDVIKEFADDGVKYLELRSTPrrENAT--GMTKKTYVESILEGIKQSKQEnLDIDVRYLIAVDRRGGPLVA 121
Cdd:COG1816    62 TEEDFRRLAYEYLEDAAADGVRYAEIRFDP--QLHTrrGLSLEEVVEAVLDGLREAERE-FGISVRLILCALRHLSPEAA 138

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462542973 122 KETVKLAEEFflsTEGTVLGLDLSGDPTVGQAKDFLEPLLEAKKAGLKLALHLSE------IpnqkkeTQILLDLLPDRI 195
Cdd:COG1816   139 FETLELALRY---RDRGVVGFGLAGDERGFPPEKFAEAFARAREAGLHLTAHAGEaggpesI------WEALDLLGAERI 209

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462542973 196 GHGTflNSGEggSLDLVDFVRQHRIPLELCLTSNVKSQTVPSYDQHHF------GFwysiahPSVICTDDKGVFATHLSQ 269
Cdd:COG1816   210 GHGV--RAIE--DPALVARLADRGIPLEVCPTSNVQLGVVPSLAEHPLrrlldaGV------RVTLNTDDPLYFGTTLTD 279

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|.
gi 2462542973 270 EYQLAAETFNLTQSQVWDLSYESINYIFASDSTRSELRKKW 310
Cdd:COG1816   280 EYELAAEAFGLSDADLAQLARNAIEASFLPEEEKAALLAEL 320
PRK09358 PRK09358
adenosine deaminase; Provisional
 26-309 9.92e-45

adenosine deaminase; Provisional


Pssm-ID: 236480  Cd Length: 340  Bit Score: 155.33  E-value: 9.92e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462542973  26 RTLEECFQMF-QTIHQLTSsPEDILMVTKDVIKEFADDGVKYLELRSTPRRENATGMTKKTYVESILEGIKQSKQEnLDI 104
Cdd:PRK09358   57 RDLQSFLDKYdAGVAVLQT-EEDLRRLAFEYLEDAAADGVVYAEIRFDPQLHTERGLPLEEVVEAVLDGLRAAEAE-FGI 134

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462542973 105 DVRYLIAVDRRGG-PLVAKETVKLAEEFFlstEGTVLGLDLSGDPTVGQAKDFLEPLLEAKKAGLKLALHLSE--IPNQK 181
Cdd:PRK09358  135 SVRLILCFMRHFGeEAAARELEALAARYR---DDGVVGFDLAGDELGFPPSKFARAFDRARDAGLRLTAHAGEagGPESI 211

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462542973 182 KETqilLDLL-PDRIGHGTFLNsgegGSLDLVDFVRQHRIPLELCLTSNVKSQTVPSYDQHHF------GFWYSIAhpsv 254
Cdd:PRK09358  212 WEA---LDELgAERIGHGVRAI----EDPALMARLADRRIPLEVCPTSNVQTGAVPSLAEHPLktlldaGVRVTIN---- 280

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 2462542973 255 icTDDKGVFATHLSQEYQLAAETFNLTQSQVWDLSYESINYIFASDSTRSELRKK 309
Cdd:PRK09358  281 --TDDPLVFGTTLTEEYEALAEAFGLSDEDLAQLARNALEAAFLSEEEKAALLAE 333
A_deaminase pfam00962
Adenosine deaminase;
24-309 3.68e-41

Adenosine deaminase;


Pssm-ID: 425964  Cd Length: 330  Bit Score: 146.04  E-value: 3.68e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462542973  24 KKRTLEECFQMFQTIHQLTSSPEDILMVTKDVIKEFADDGVKYLELRSTPRRENATGMTKKTYVESILEGIKQSKQEnLD 103
Cdd:pfam00962  46 KERDLQDFLDKYDIGVAVLRSPEDIRRLAFEYAEDVAKDGVVYAEVRYDPQSHASRGLSPDTVVDAVLDAVDAAERE-FG 124

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462542973 104 IDVRYLIAVDRRGGPLVAKETVKLAEEFflsTEGTVLGLDLSGDPTV---GQAKDFLEPLLEAKKAGLKLALHLSEIPNQ 180
Cdd:pfam00962 125 ITVRLIVCAMRHEHPECSREIAELAPRY---RDQGIVAFGLAGDEKGfppSLFRDHVEAFARARDAGLHLTVHAGEAGGP 201

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462542973 181 KKETQILLDLLPDRIGHGTflNSGEGGSLdlVDFVRQHRIPLELCLTSNVKSQTVPSYDQHHFGFWYSIAHPSVICTDDK 260
Cdd:pfam00962 202 QSVWEALDDLGAERIGHGV--RSAEDPRL--LDRLADRQIPLEICPTSNVQTGAVASLAEHPLKTFLRAGVPVSLNTDDP 277

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*....
gi 2462542973 261 GVFATHLSQEYQLAAETFNLTQSQVWDLSYESINYIFASDSTRSELRKK 309
Cdd:pfam00962 278 LMFGSDLLDEYQVAKRAPGFDEEELARLAKNAVKGSFLPADEKRALLDE 326
ADGF cd01321
Adenosine deaminase-related growth factors (ADGF), a novel family of secreted growth-factors ...
 33-311 2.48e-16

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: 78.47  E-value: 2.48e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462542973  33 QMFQTIHQL-TSSPedilmVTKDVI----KEFADDGVKYLELRSTPRRENATGMTKKTYVES--ILEGI--KQSKQENLD 103
Cdd:cd01321    53 QIFDIIDGLlTYLP-----IFRDYYrrllEELYEDNVQYVELRSSFSPLYDLDGREYDYEETvqLLEEVveKFKKTHPDF 127

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462542973 104 IDVRYLIAVDRRGGPLVAKETVKLAEEFFLSTEGTVLGLDLSGDPTVGQA-KDFLEPLLEAKK--AGLKLALHLSEIPNQ 180
Cdd:cd01321   128 IGLKIIYATLRNFNDSEIKESMEQCLNLKKKFPDFIAGFDLVGQEDAGRPlLDFLPQLLWFPKqcAEIPFFFHAGETNGD 207

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462542973 181 KKETQI-LLD-LLPD--RIGHGTflnsgeggSL----DLVDFVRQHRIPLELCLTSNVKSQTVPSYDQHHFGFWYSIAHP 252
Cdd:cd01321   208 GTETDEnLVDaLLLNtkRIGHGF--------ALpkhpLLMDLVKKKNIAIEVCPISNQVLGLVSDLRNHPAAALLARGVP 279

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2462542973 253 SVICTDDKGVF-ATHLSQE-YQ----LAAETFNLTQ--SQVWDlsyeSINYIFASDSTRSELRKKWN 311
Cdd:cd01321   280 VVISSDDPGFWgAKGLSHDfYQafmgLAPADAGLRGlkQLAEN----SIRYSALSDQEKDEAVAKWE 342
PTZ00124 PTZ00124
adenosine deaminase; Provisional
 62-310 5.65e-14

adenosine deaminase; Provisional


Pssm-ID: 173415  Cd Length: 362  Bit Score: 71.82  E-value: 5.65e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462542973  62 DGVKYLELRSTPR-RENATGMTKKTYVESILEGIKQSKQEnldIDVRYLIAVDRRGGPLVAKETVKLAEEFFLSTEGTVL 140
Cdd:PTZ00124  118 EGVVLMEFRYSPTfVAFKHNLDIDLIHQAIVKGIKEAVEL---LDHKIEVGLLCIGDTGHDAAPIKESADFCLKHKADFV 194

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462542973 141 GLDLSGDPTvgQAKDFLEPLLEAKKAGLKLALHLSE---IPNQKKETQILLDLLPDRIGHGTFLNSgeggSLDLVDFVRQ 217
Cdd:PTZ00124  195 GFDHAGHEV--DLKPFKDIFDYVREAGVNLTVHAGEdvtLPNLNTLYSAIQVLKVKRIGHGIRVAE----SQELIDMVKE 268

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462542973 218 HRIPLELCLTSNVKSQTVPSYDQHHFGFWYSIAHPSVICTDDKGVFATHLSQEYQLAAETFNLTQSQVWDLSYESINYIF 297
Cdd:PTZ00124  269 KDILLEVCPISNVLLNNAKSMDTHPIRKLYDAGVKVSVNSDDPGMFLTNINDDYEELYTHLNFTLADFMKMNEWALEKSF 348

                         250
                  ....*....|...
gi 2462542973 298 ASDSTRSELRKKW 310
Cdd:PTZ00124  349 LDKDIKLKIKKLY 361
archeal_chlorohydrolases cd01305
Predicted chlorohydrolases. These metallo-dependent hydrolases from archea are part of the ...
 62-229 2.54e-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: 2.54e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462542973  62 DGVKYLELRSTPRRENATGMtKKT--------------YVESILEGIKQSKQENLDIDVRYLIAVDRRGGPLVAKETVKL 127
Cdd:cd01305    35 DGLKHRLLAQADDRELAEAM-RKVlrdmretgigafadFREGGVEGIELLRRALGKLPVPFEVILGRPTEPDDPEILLEV 113

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462542973 128 AEefflstegtvlGLDLSG--DPtvgqakDFLEPLLEAKKAGLKLALHLSEIPNQKKETQI--LLDLLPDRIGHGTFLNS 203
Cdd:cd01305   114 AD-----------GLGLSSanDV------DLEDILELLRRRGKLFAIHASETRESVGMTDIerALDLEPDLLVHGTHLTD 176

                         170       180
                  ....*....|....*....|....*.
gi 2462542973 204 GEggsldlVDFVRQHRIPLELCLTSN 229
Cdd:cd01305   177 ED------LELVRENGVPVVLCPRSN 196
metallo-dependent_hydrolases cd01292
Superfamily of metallo-dependent hydrolases (also called amidohydrolase superfamily) is a ...
 44-276 4.36e-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: 4.36e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462542973  44 SPEDILMVTKDVIKEFADDGVKYLELRSTprreNATGMTKKTYVESILEGIkqskQENLDIDVRYLIAVDRRGGPLVAKE 123
Cdd:cd01292    29 SPEDLYEDTLRALEALLAGGVTTVVDMGS----TPPPTTTKAAIEAVAEAA----RASAGIRVVLGLGIPGVPAAVDEDA 100

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462542973 124 TVKLAEEFFLSTEGTVLGLDLSGDPTVGQAKD--FLEPLLEAKKAGLKLALHLSEIPNQKKETQILLDLL----PDRIGH 197
Cdd:cd01292   101 EALLLELLRRGLELGAVGLKLAGPYTATGLSDesLRRVLEEARKLGLPVVIHAGELPDPTRALEDLVALLrlggRVVIGH 180

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462542973 198 GTFLnsgeggSLDLVDFVRQHRIPLELCLTSNVKSqTVPSYDQHHFGFWYSIAHPSVICTDDKGVF-ATHLSQEYQLAAE 276
Cdd:cd01292   181 VSHL------DPELLELLKEAGVSLEVCPLSNYLL-GRDGEGAEALRRLLELGIRVTLGTDGPPHPlGTDLLALLRLLLK 253
Amidohydro_1 pfam01979
Amidohydrolase family; This family of enzymes are a a large metal dependent hydrolase ...
 77-223 3.00e-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: 42.10  E-value: 3.00e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462542973  77 NATGMTKKTYVESILEGIkqskqENLDIDVRYLIAV-------DRRGGPLVAKETVKLAE-EFFLSTEGTVLGLDLSGDP 148
Cdd:pfam01979  48 LDMGATTSTGIEALLEAA-----EELPLGLRFLGPGcsldtdgELEGRKALREKLKAGAEfIKGMADGVVFVGLAPHGAP 122

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2462542973 149 TVGqaKDFLEPLLE-AKKAGLKLALHLSEipnQKKETQILLDLLPDRIGHGTFL-NSGEGGSLDLVDFVRQHRIPLE 223
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.
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