|
Name |
Accession |
Description |
Interval |
E-value |
| PRK09358 |
PRK09358 |
adenosine deaminase; Provisional |
1-332 |
1.41e-156 |
|
adenosine deaminase; Provisional
Pssm-ID: 236480 Cd Length: 340 Bit Score: 441.92 E-value: 1.41e-156
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490253202 1 MIDSSLPLTDIHRHLDGNIRAQTILDLGREFNIALPATTLDTLRPhVQVTSLEPDLVSFLAKLDWGVKVLASLEACRRVA 80
Cdd:PRK09358 5 MIIRSLPKAELHLHLDGSLRPETILELARRNGIALPATDVEELPW-VRAAYDFRDLQSFLDKYDAGVAVLQTEEDLRRLA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490253202 81 YENVEDAARNGLHYVELRFSPRYMAMtHRLPVDGVVEAVIAGVQEGCRDFQVDARLIGILSRTFGEAACQEELAALLA-- 158
Cdd:PRK09358 84 FEYLEDAAADGVVYAEIRFDPQLHTE-RGLPLEEVVEAVLDGLRAAEAEFGISVRLILCFMRHFGEEAAARELEALAAry 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490253202 159 HREGITALDLAGDELGFPGTLFRNHFNQARDAGWHITVHAGEAAGPESIWQAIRELGAERIGHGVKAVEDPALMDYLAEH 238
Cdd:PRK09358 163 RDDGVVGFDLAGDELGFPPSKFARAFDRARDAGLRLTAHAGEAGGPESIWEALDELGAERIGHGVRAIEDPALMARLADR 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490253202 239 RIGIESCLTSNVQTSTVASLAQHPLKQFLEHGVLASLNTDDPAVQGVDIIHEYTVAAPAAGLSREQIRQAQINGLTLAFL 318
Cdd:PRK09358 243 RIPLEVCPTSNVQTGAVPSLAEHPLKTLLDAGVRVTINTDDPLVFGTTLTEEYEALAEAFGLSDEDLAQLARNALEAAFL 322
|
330
....*....|....
gi 490253202 319 GEQEKAALIQRVAK 332
Cdd:PRK09358 323 SEEEKAALLAEVDA 336
|
|
| Add |
COG1816 |
Adenosine deaminase [Nucleotide transport and metabolism]; Adenosine deaminase is part of the ... |
7-332 |
3.22e-148 |
|
Adenosine deaminase [Nucleotide transport and metabolism]; Adenosine deaminase is part of the Pathway/BioSystem: Menaquinone biosynthesis
Pssm-ID: 441421 Cd Length: 326 Bit Score: 419.87 E-value: 3.22e-148
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490253202 7 PLTDIHRHLDGNIRAQTILDLGREFNIALPATTLDTLRPHVQvtslEPDLVSFLAKLDWGVKVLASLEACRRVAYENVED 86
Cdd:COG1816 1 PKAELHLHLEGSLRPETLLELAARNGIDLPAADVEELRAAYD----FRDLQSFLDTYDAGAAVLQTEEDFRRLAYEYLED 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490253202 87 AARNGLHYVELRFSPrYMAMTHRLPVDGVVEAVIAGVQEGCRDFQVDARLIGILSRTFGEAACQEELAALLAHRE-GITA 165
Cdd:COG1816 77 AAADGVRYAEIRFDP-QLHTRRGLSLEEVVEAVLDGLREAEREFGISVRLILCALRHLSPEAAFETLELALRYRDrGVVG 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490253202 166 LDLAGDELGFPGTLFRNHFNQARDAGWHITVHAGEAAGPESIWQAIRELGAERIGHGVKAVEDPALMDYLAEHRIGIESC 245
Cdd:COG1816 156 FGLAGDERGFPPEKFAEAFARAREAGLHLTAHAGEAGGPESIWEALDLLGAERIGHGVRAIEDPALVARLADRGIPLEVC 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490253202 246 LTSNVQTSTVASLAQHPLKQFLEHGVLASLNTDDPAVQGVDIIHEYTVAAPAAGLSREQIRQAQINGLTLAFLGEQEKAA 325
Cdd:COG1816 236 PTSNVQLGVVPSLAEHPLRRLLDAGVRVTLNTDDPLYFGTTLTDEYELAAEAFGLSDADLAQLARNAIEASFLPEEEKAA 315
|
....*..
gi 490253202 326 LIQRVAK 332
Cdd:COG1816 316 LLAELDA 322
|
|
| A_deaminase |
pfam00962 |
Adenosine deaminase; |
7-332 |
4.32e-146 |
|
Adenosine deaminase;
Pssm-ID: 425964 Cd Length: 330 Bit Score: 414.90 E-value: 4.32e-146
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490253202 7 PLTDIHRHLDGNIRAQTILDLGREFNIALPATTLDTLRPHVQVTSLEPDLVSFLAKLDWGVKVLASLEACRRVAYENVED 86
Cdd:pfam00962 1 PKAELHLHLDGSLRPDTLLELAKRYGIILPADFPEALEPLFRKYKKERDLQDFLDKYDIGVAVLRSPEDIRRLAFEYAED 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490253202 87 AARNGLHYVELRFSPRYMAMTHrLPVDGVVEAVIAGVQEGCRDFQVDARLIGILSRTfGEAACQEELAALLA-HRE-GIT 164
Cdd:pfam00962 81 VAKDGVVYAEVRYDPQSHASRG-LSPDTVVDAVLDAVDAAEREFGITVRLIVCAMRH-EHPECSREIAELAPrYRDqGIV 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490253202 165 ALDLAGDELGFPGTLFRNH---FNQARDAGWHITVHAGEAAGPESIWQAIRELGAERIGHGVKAVEDPALMDYLAEHRIG 241
Cdd:pfam00962 159 AFGLAGDEKGFPPSLFRDHveaFARARDAGLHLTVHAGEAGGPQSVWEALDDLGAERIGHGVRSAEDPRLLDRLADRQIP 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490253202 242 IESCLTSNVQTSTVASLAQHPLKQFLEHGVLASLNTDDPAVQGVDIIHEYTVAAPAAGLSREQIRQAQINGLTLAFLGEQ 321
Cdd:pfam00962 239 LEICPTSNVQTGAVASLAEHPLKTFLRAGVPVSLNTDDPLMFGSDLLDEYQVAKRAPGFDEEELARLAKNAVKGSFLPAD 318
|
330
....*....|.
gi 490253202 322 EKAALIQRVAK 332
Cdd:pfam00962 319 EKRALLDEVDK 329
|
|
| ADA |
cd01320 |
Adenosine deaminase (ADA) is a monomeric zinc dependent enzyme which catalyzes the ... |
6-330 |
3.12e-135 |
|
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: 386.94 E-value: 3.12e-135
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490253202 6 LPLTDIHRHLDGNIRAQTILDLGREFNIALPATTLDtLRPHVQVTSLEPDLVSFLAKLDWGVKVLASLEACRRVAYENVE 85
Cdd:cd01320 2 LPKAELHLHLDGSLRPETILELAKKNGITLPASDVE-LLELVVAAYNFSDLQDFLAKYDFGLSVLQTEEDFERLAYEYLE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490253202 86 DAARNGLHYVELRFSPRYMaMTHRLPVDGVVEAVIAGVQEGCRDFQVDARLIGILSRTFGEAACQEELAALLAHRE-GIT 164
Cdd:cd01320 81 DAAADGVVYAEIRFSPQLH-TRRGLSFDEVVEAVLRGLDEAEAEFGIKARLILCGLRHLSPESAQETLELALKYRDkGVV 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490253202 165 ALDLAGDELGFPGTLFRNHFNQARDAGWHITVHAGEAAGPESIWQAIRELGAERIGHGVKAVEDPALMDYLAEHRIGIES 244
Cdd:cd01320 160 GFDLAGDEVGFPPEKFVRAFQRAREAGLRLTAHAGEAGGPESVRDALDLLGAERIGHGIRAIEDPELVKRLAERNIPLEV 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490253202 245 CLTSNVQTSTVASLAQHPLKQFLEHGVLASLNTDDPAVQGVDIIHEYTVAAPAAGLSREQIRQAQINGLTLAFLGEQEKA 324
Cdd:cd01320 240 CPTSNVQTGAVKSLAEHPLRELLDAGVKVTINTDDPTVFGTYLTDEYELLAEAFGLTEEELKKLARNAVEASFLSEEEKA 319
|
....*.
gi 490253202 325 ALIQRV 330
Cdd:cd01320 320 ELLKRI 325
|
|
| aden_deam |
TIGR01430 |
adenosine deaminase; This family includes the experimentally verified adenosine deaminases of ... |
6-330 |
7.36e-129 |
|
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: 370.92 E-value: 7.36e-129
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490253202 6 LPLTDIHRHLDGNIRAQTILDLGREFNIALPATtLDTLRPHVQVTSLEPDLVSFLAKLDWGVKVLASLEACRRVAYENVE 85
Cdd:TIGR01430 1 LPKAELHLHLEGSIRPETLLELAQKNGIPLPAD-LQSGEELKEAYDKFRDLQDFLAKYDFGVEVLRTEDDFKRLAYEYVE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490253202 86 DAARNGLHYVELRFSPRYMAMTHRLPvDGVVEAVIAGVQEGCRDFQVDARLIGILSRTFGEAACQEELAALLAHRE-GIT 164
Cdd:TIGR01430 80 KAAKDGVVYAEVFFDPQLHTNRGISP-DTVVEAVLDGLDEAERDFGIKSRLILCGMRHKQPEAAEETLELAKPYKEqTIV 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490253202 165 ALDLAGDELGFPGTLFRNHFNQARDAGWHITVHAGEAAGPESIWQAIRELGAERIGHGVKAVEDPALMDYLAEHRIGIES 244
Cdd:TIGR01430 159 GFGLAGDERGGPPPDFVRAFAIARELGLHLTVHAGELGGPESVREALDDLGATRIGHGVRALEDPELLKRLAQENITLEV 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490253202 245 CLTSNVQTSTVASLAQHPLKQFLEHGVLASLNTDDPAVQGVDIIHEYTVAAPAAGLSREQIRQAQINGLTLAFLGEQEKA 324
Cdd:TIGR01430 239 CPTSNVALGVVKSLAEHPLRRFLEAGVKVTLNSDDPAYFGSYLTEEYEIAAKHAGLTEEELKQLARNALEGSFLSDDEKK 318
|
....*.
gi 490253202 325 ALIQRV 330
Cdd:TIGR01430 319 ELLAKL 324
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| PRK09358 |
PRK09358 |
adenosine deaminase; Provisional |
1-332 |
1.41e-156 |
|
adenosine deaminase; Provisional
Pssm-ID: 236480 Cd Length: 340 Bit Score: 441.92 E-value: 1.41e-156
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490253202 1 MIDSSLPLTDIHRHLDGNIRAQTILDLGREFNIALPATTLDTLRPhVQVTSLEPDLVSFLAKLDWGVKVLASLEACRRVA 80
Cdd:PRK09358 5 MIIRSLPKAELHLHLDGSLRPETILELARRNGIALPATDVEELPW-VRAAYDFRDLQSFLDKYDAGVAVLQTEEDLRRLA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490253202 81 YENVEDAARNGLHYVELRFSPRYMAMtHRLPVDGVVEAVIAGVQEGCRDFQVDARLIGILSRTFGEAACQEELAALLA-- 158
Cdd:PRK09358 84 FEYLEDAAADGVVYAEIRFDPQLHTE-RGLPLEEVVEAVLDGLRAAEAEFGISVRLILCFMRHFGEEAAARELEALAAry 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490253202 159 HREGITALDLAGDELGFPGTLFRNHFNQARDAGWHITVHAGEAAGPESIWQAIRELGAERIGHGVKAVEDPALMDYLAEH 238
Cdd:PRK09358 163 RDDGVVGFDLAGDELGFPPSKFARAFDRARDAGLRLTAHAGEAGGPESIWEALDELGAERIGHGVRAIEDPALMARLADR 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490253202 239 RIGIESCLTSNVQTSTVASLAQHPLKQFLEHGVLASLNTDDPAVQGVDIIHEYTVAAPAAGLSREQIRQAQINGLTLAFL 318
Cdd:PRK09358 243 RIPLEVCPTSNVQTGAVPSLAEHPLKTLLDAGVRVTINTDDPLVFGTTLTEEYEALAEAFGLSDEDLAQLARNALEAAFL 322
|
330
....*....|....
gi 490253202 319 GEQEKAALIQRVAK 332
Cdd:PRK09358 323 SEEEKAALLAEVDA 336
|
|
| Add |
COG1816 |
Adenosine deaminase [Nucleotide transport and metabolism]; Adenosine deaminase is part of the ... |
7-332 |
3.22e-148 |
|
Adenosine deaminase [Nucleotide transport and metabolism]; Adenosine deaminase is part of the Pathway/BioSystem: Menaquinone biosynthesis
Pssm-ID: 441421 Cd Length: 326 Bit Score: 419.87 E-value: 3.22e-148
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490253202 7 PLTDIHRHLDGNIRAQTILDLGREFNIALPATTLDTLRPHVQvtslEPDLVSFLAKLDWGVKVLASLEACRRVAYENVED 86
Cdd:COG1816 1 PKAELHLHLEGSLRPETLLELAARNGIDLPAADVEELRAAYD----FRDLQSFLDTYDAGAAVLQTEEDFRRLAYEYLED 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490253202 87 AARNGLHYVELRFSPrYMAMTHRLPVDGVVEAVIAGVQEGCRDFQVDARLIGILSRTFGEAACQEELAALLAHRE-GITA 165
Cdd:COG1816 77 AAADGVRYAEIRFDP-QLHTRRGLSLEEVVEAVLDGLREAEREFGISVRLILCALRHLSPEAAFETLELALRYRDrGVVG 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490253202 166 LDLAGDELGFPGTLFRNHFNQARDAGWHITVHAGEAAGPESIWQAIRELGAERIGHGVKAVEDPALMDYLAEHRIGIESC 245
Cdd:COG1816 156 FGLAGDERGFPPEKFAEAFARAREAGLHLTAHAGEAGGPESIWEALDLLGAERIGHGVRAIEDPALVARLADRGIPLEVC 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490253202 246 LTSNVQTSTVASLAQHPLKQFLEHGVLASLNTDDPAVQGVDIIHEYTVAAPAAGLSREQIRQAQINGLTLAFLGEQEKAA 325
Cdd:COG1816 236 PTSNVQLGVVPSLAEHPLRRLLDAGVRVTLNTDDPLYFGTTLTDEYELAAEAFGLSDADLAQLARNAIEASFLPEEEKAA 315
|
....*..
gi 490253202 326 LIQRVAK 332
Cdd:COG1816 316 LLAELDA 322
|
|
| A_deaminase |
pfam00962 |
Adenosine deaminase; |
7-332 |
4.32e-146 |
|
Adenosine deaminase;
Pssm-ID: 425964 Cd Length: 330 Bit Score: 414.90 E-value: 4.32e-146
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490253202 7 PLTDIHRHLDGNIRAQTILDLGREFNIALPATTLDTLRPHVQVTSLEPDLVSFLAKLDWGVKVLASLEACRRVAYENVED 86
Cdd:pfam00962 1 PKAELHLHLDGSLRPDTLLELAKRYGIILPADFPEALEPLFRKYKKERDLQDFLDKYDIGVAVLRSPEDIRRLAFEYAED 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490253202 87 AARNGLHYVELRFSPRYMAMTHrLPVDGVVEAVIAGVQEGCRDFQVDARLIGILSRTfGEAACQEELAALLA-HRE-GIT 164
Cdd:pfam00962 81 VAKDGVVYAEVRYDPQSHASRG-LSPDTVVDAVLDAVDAAEREFGITVRLIVCAMRH-EHPECSREIAELAPrYRDqGIV 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490253202 165 ALDLAGDELGFPGTLFRNH---FNQARDAGWHITVHAGEAAGPESIWQAIRELGAERIGHGVKAVEDPALMDYLAEHRIG 241
Cdd:pfam00962 159 AFGLAGDEKGFPPSLFRDHveaFARARDAGLHLTVHAGEAGGPQSVWEALDDLGAERIGHGVRSAEDPRLLDRLADRQIP 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490253202 242 IESCLTSNVQTSTVASLAQHPLKQFLEHGVLASLNTDDPAVQGVDIIHEYTVAAPAAGLSREQIRQAQINGLTLAFLGEQ 321
Cdd:pfam00962 239 LEICPTSNVQTGAVASLAEHPLKTFLRAGVPVSLNTDDPLMFGSDLLDEYQVAKRAPGFDEEELARLAKNAVKGSFLPAD 318
|
330
....*....|.
gi 490253202 322 EKAALIQRVAK 332
Cdd:pfam00962 319 EKRALLDEVDK 329
|
|
| ADA |
cd01320 |
Adenosine deaminase (ADA) is a monomeric zinc dependent enzyme which catalyzes the ... |
6-330 |
3.12e-135 |
|
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: 386.94 E-value: 3.12e-135
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490253202 6 LPLTDIHRHLDGNIRAQTILDLGREFNIALPATTLDtLRPHVQVTSLEPDLVSFLAKLDWGVKVLASLEACRRVAYENVE 85
Cdd:cd01320 2 LPKAELHLHLDGSLRPETILELAKKNGITLPASDVE-LLELVVAAYNFSDLQDFLAKYDFGLSVLQTEEDFERLAYEYLE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490253202 86 DAARNGLHYVELRFSPRYMaMTHRLPVDGVVEAVIAGVQEGCRDFQVDARLIGILSRTFGEAACQEELAALLAHRE-GIT 164
Cdd:cd01320 81 DAAADGVVYAEIRFSPQLH-TRRGLSFDEVVEAVLRGLDEAEAEFGIKARLILCGLRHLSPESAQETLELALKYRDkGVV 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490253202 165 ALDLAGDELGFPGTLFRNHFNQARDAGWHITVHAGEAAGPESIWQAIRELGAERIGHGVKAVEDPALMDYLAEHRIGIES 244
Cdd:cd01320 160 GFDLAGDEVGFPPEKFVRAFQRAREAGLRLTAHAGEAGGPESVRDALDLLGAERIGHGIRAIEDPELVKRLAERNIPLEV 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490253202 245 CLTSNVQTSTVASLAQHPLKQFLEHGVLASLNTDDPAVQGVDIIHEYTVAAPAAGLSREQIRQAQINGLTLAFLGEQEKA 324
Cdd:cd01320 240 CPTSNVQTGAVKSLAEHPLRELLDAGVKVTINTDDPTVFGTYLTDEYELLAEAFGLTEEELKKLARNAVEASFLSEEEKA 319
|
....*.
gi 490253202 325 ALIQRV 330
Cdd:cd01320 320 ELLKRI 325
|
|
| aden_deam |
TIGR01430 |
adenosine deaminase; This family includes the experimentally verified adenosine deaminases of ... |
6-330 |
7.36e-129 |
|
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: 370.92 E-value: 7.36e-129
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490253202 6 LPLTDIHRHLDGNIRAQTILDLGREFNIALPATtLDTLRPHVQVTSLEPDLVSFLAKLDWGVKVLASLEACRRVAYENVE 85
Cdd:TIGR01430 1 LPKAELHLHLEGSIRPETLLELAQKNGIPLPAD-LQSGEELKEAYDKFRDLQDFLAKYDFGVEVLRTEDDFKRLAYEYVE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490253202 86 DAARNGLHYVELRFSPRYMAMTHRLPvDGVVEAVIAGVQEGCRDFQVDARLIGILSRTFGEAACQEELAALLAHRE-GIT 164
Cdd:TIGR01430 80 KAAKDGVVYAEVFFDPQLHTNRGISP-DTVVEAVLDGLDEAERDFGIKSRLILCGMRHKQPEAAEETLELAKPYKEqTIV 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490253202 165 ALDLAGDELGFPGTLFRNHFNQARDAGWHITVHAGEAAGPESIWQAIRELGAERIGHGVKAVEDPALMDYLAEHRIGIES 244
Cdd:TIGR01430 159 GFGLAGDERGGPPPDFVRAFAIARELGLHLTVHAGELGGPESVREALDDLGATRIGHGVRALEDPELLKRLAQENITLEV 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490253202 245 CLTSNVQTSTVASLAQHPLKQFLEHGVLASLNTDDPAVQGVDIIHEYTVAAPAAGLSREQIRQAQINGLTLAFLGEQEKA 324
Cdd:TIGR01430 239 CPTSNVALGVVKSLAEHPLRRFLEAGVKVTLNSDDPAYFGSYLTEEYEIAAKHAGLTEEELKQLARNALEGSFLSDDEKK 318
|
....*.
gi 490253202 325 ALIQRV 330
Cdd:TIGR01430 319 ELLAKL 324
|
|
| ADA_AMPD |
cd00443 |
Adenosine/AMP deaminase. Adenosine deaminases (ADAs) are present in pro- and eukaryotic ... |
6-329 |
3.95e-52 |
|
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: 174.07 E-value: 3.95e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490253202 6 LPLTDIHRHLDGNIRAQTILDLG-REFnialpATTLDTLRPHVQvtslepdlvsflakldwgvkvlaSLEACRRVAYENV 84
Cdd:cd00443 1 LPKVELHAHLSGSISPETLLELIkKEF-----FEKFLLVHNLLQ-----------------------KGEALARALKEVI 52
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490253202 85 EDAARNGLHYVELRFSPRYMAMTHRLPVDGVVEAVIAGVQEGCRDF-QVDARLIGILSRT------FGEAACQEELAALL 157
Cdd:cd00443 53 EEFAEDNVQYLELRTTPRLLETEKGLTKEQYWLLVIEGISEAKQWFpPIKVRLILSVDRRgpyvqnYLVASEILELAKFL 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490253202 158 ahREGITALDLAGDELGfPGTLFRNH---FNQARDAGW-HITVHAGEAAGPESIWQAIrELGAERIGHGVKAVEDPALMD 233
Cdd:cd00443 133 --SNYVVGIDLVGDESK-GENPLRDFysyYEYARRLGLlGLTLHCGETGNREELLQAL-LLLPDRIGHGIFLLKHPELIY 208
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490253202 234 YLAEHRIGIESCLTSNVQTSTVASLAQHPLKQFLEHGVLASLNTDDPAVQGVDIIHEYTVAAPAAGLSREQIRQAQINGL 313
Cdd:cd00443 209 LVKLRNIPIEVCPTSNVVLGTVQSYEKHPFMRFFKAGLPVSLSTDDPGIFGTSLSEEYSLAAKTFGLTFEDLCELNRNSV 288
|
330
....*....|....*.
gi 490253202 314 TLAFLGEQEKAALIQR 329
Cdd:cd00443 289 LSSFAKDEEKKSLLEV 304
|
|
| PTZ00124 |
PTZ00124 |
adenosine deaminase; Provisional |
6-291 |
4.55e-39 |
|
adenosine deaminase; Provisional
Pssm-ID: 173415 Cd Length: 362 Bit Score: 141.54 E-value: 4.55e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490253202 6 LPLTDIHRHLDGNIRAQTILDLGREFNIALPATTLDTLRPHVQVTSLEpDLVSFLAKLDWGVKVLASLEACRRVAYENVE 85
Cdd:PTZ00124 35 IPKCELHCHLDLCFSVDFFLSCIRKYNLQPNLSDEEILDYYLFAKGGK-SLGEFVEKAIRVADIFNDYEVIEDLAKHAVF 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490253202 86 DAARNGLHYVELRFSPRYMAMTHRLPVDGVVEAVIAGVQEGCR--DFQVDARLIGILSRTFGEAACQEELAALLAHREGI 163
Cdd:PTZ00124 114 NKYKEGVVLMEFRYSPTFVAFKHNLDIDLIHQAIVKGIKEAVEllDHKIEVGLLCIGDTGHDAAPIKESADFCLKHKADF 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490253202 164 TALDLAGDELGFPGtlFRNHFNQARDAGWHITVHAGEAAGP---ESIWQAIRELGAERIGHGVKAVEDPALMDYLAEHRI 240
Cdd:PTZ00124 194 VGFDHAGHEVDLKP--FKDIFDYVREAGVNLTVHAGEDVTLpnlNTLYSAIQVLKVKRIGHGIRVAESQELIDMVKEKDI 271
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 490253202 241 GIESCLTSNVQTSTVASLAQHPLKQFLEHGVLASLNTDDPAVQGVDIIHEY 291
Cdd:PTZ00124 272 LLEVCPISNVLLNNAKSMDTHPIRKLYDAGVKVSVNSDDPGMFLTNINDDY 322
|
|
| ADGF |
cd01321 |
Adenosine deaminase-related growth factors (ADGF), a novel family of secreted growth-factors ... |
91-323 |
1.91e-18 |
|
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: 84.63 E-value: 1.91e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490253202 91 GLHYVELR--FSPRYMAMTHRLPVDGVVEAVIAGVQEGCR---DFQvDARLIGILSRTFGEAACQEELA-ALLAHR---E 161
Cdd:cd01321 83 NVQYVELRssFSPLYDLDGREYDYEETVQLLEEVVEKFKKthpDFI-GLKIIYATLRNFNDSEIKESMEqCLNLKKkfpD 161
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490253202 162 GITALDLAGDE-LGFPGTLFRNHFNQARDAGWHIT--VHAGEAAGPES-----IWQAIReLGAERIGHGVKAVEDPALMD 233
Cdd:cd01321 162 FIAGFDLVGQEdAGRPLLDFLPQLLWFPKQCAEIPffFHAGETNGDGTetdenLVDALL-LNTKRIGHGFALPKHPLLMD 240
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490253202 234 YLAEHRIGIESCLTSNVQTSTVASLAQHPLKQFLEHGVLASLNTDDPAVQGVD-IIHEYTVA----APA-AGLSreQIRQ 307
Cdd:cd01321 241 LVKKKNIAIEVCPISNQVLGLVSDLRNHPAAALLARGVPVVISSDDPGFWGAKgLSHDFYQAfmglAPAdAGLR--GLKQ 318
|
250
....*....|....*.
gi 490253202 308 AQINGLTLAFLGEQEK 323
Cdd:cd01321 319 LAENSIRYSALSDQEK 334
|
|
| AMPD |
cd01319 |
AMP deaminase (AMPD) catalyzes the hydrolytic deamination of adensosine monophosphate (AMP) at ... |
182-301 |
3.56e-07 |
|
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: 51.60 E-value: 3.56e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490253202 182 NHFNQARdaGWHITV---HAGEAAGPESIWQAIreLGAERIGHGVKAVEDPAL--MDYLAEhrIGIE-SCLTSNvqtSTV 255
Cdd:cd01319 316 NSFRKAR--GFNTFVlrpHCGEAGDIDHLASAF--LLAHGISHGINLRKVPVLqyLYYLTQ--IGIAmSPLSNN---SLF 386
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 490253202 256 ASLAQHPLKQFLEHGVLASLNTDDP---AVQGVDIIHEYTVAAPAAGLS 301
Cdd:cd01319 387 LSYEKNPFPEFFKRGLNVSLSTDDPlqfHFTKEPLMEEYSIAAQVWKLS 435
|
|
| metallo-dependent_hydrolases |
cd01292 |
Superfamily of metallo-dependent hydrolases (also called amidohydrolase superfamily) is a ... |
46-284 |
1.37e-06 |
|
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: 48.87 E-value: 1.37e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490253202 46 HVQVTSLEPDLVSFLAKLDWGVKVLASLEACRRVAyenvEDAARNGLHYVELRFSPRYMAMThrlpvdgvvEAVIAGVQE 125
Cdd:cd01292 7 HLDGSALRGTRLNLELKEAEELSPEDLYEDTLRAL----EALLAGGVTTVVDMGSTPPPTTT---------KAAIEAVAE 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490253202 126 GCRDFQ-VDARLI-GILSRTFGEAACQEEL---AALLAHREGITALDLAGDELGFPGTL--FRNHFNQARDAGWHITVHA 198
Cdd:cd01292 74 AARASAgIRVVLGlGIPGVPAAVDEDAEALlleLLRRGLELGAVGLKLAGPYTATGLSDesLRRVLEEARKLGLPVVIHA 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490253202 199 GEAAGPESIW----QAIRELGAERIGHGVkaVEDPALMDYLAEHRIGIESCLTSNvQTSTVASLAQHPLKQFLEHGVLAS 274
Cdd:cd01292 154 GELPDPTRALedlvALLRLGGRVVIGHVS--HLDPELLELLKEAGVSLEVCPLSN-YLLGRDGEGAEALRRLLELGIRVT 230
|
250
....*....|
gi 490253202 275 LNTDDPAVQG 284
Cdd:cd01292 231 LGTDGPPHPL 240
|
|
| AMP_deaminase |
pfam19326 |
AMP deaminase; |
197-301 |
1.54e-05 |
|
AMP deaminase;
Pssm-ID: 437158 [Multi-domain] Cd Length: 622 Bit Score: 46.68 E-value: 1.54e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490253202 197 HAGEAAGPESIWQAIreLGAERIGHGVKAVEDPAL--MDYLAEhrIGIE-SCLTSNvqtSTVASLAQHPLKQFLEHGVLA 273
Cdd:pfam19326 449 HCGEAGDIDHLVSAF--LLAHGISHGILLRKSPVLqyLYYLAQ--IGIAmSPLSNN---SLFLEYHKNPFPEFFKRGLNV 521
|
90 100 110
....*....|....*....|....*....|.
gi 490253202 274 SLNTDDP---AVQGVDIIHEYTVAAPAAGLS 301
Cdd:pfam19326 522 SLSTDDPlqfHFTKEPLMEEYSIAAQVWKLS 552
|
|
| AMP_deaminase |
TIGR01429 |
AMP deaminase; This model describes AMP deaminase, a large, well-conserved eukaryotic protein ... |
197-301 |
4.01e-04 |
|
AMP deaminase; This model describes AMP deaminase, a large, well-conserved eukaryotic protein involved in energy metabolism. Most members of the family have an additional, poorly alignable region of 150 amino acids or more N-terminal to the region included in the model.
Pssm-ID: 273618 [Multi-domain] Cd Length: 611 Bit Score: 42.14 E-value: 4.01e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490253202 197 HAGEAAGPESIWQAIreLGAERIGHGVKAVEDPAL--MDYLAEhrIGIESCLTSNvqTSTVASLAQHPLKQFLEHGVLAS 274
Cdd:TIGR01429 444 HCGEAGSVDHLVSAF--LTSHGINHGILLRKVPVLqyLYYLTQ--IPIAMSPLSN--NSLFLEYSKNPLPEYLHKGLNVS 517
|
90 100 110
....*....|....*....|....*....|
gi 490253202 275 LNTDDP---AVQGVDIIHEYTVAAPAAGLS 301
Cdd:TIGR01429 518 LSTDDPlqfHYTKEALMEEYAIAAQVWKLS 547
|
|
| PTZ00310 |
PTZ00310 |
AMP deaminase; Provisional |
197-301 |
9.27e-04 |
|
AMP deaminase; Provisional
Pssm-ID: 240354 [Multi-domain] Cd Length: 1453 Bit Score: 41.33 E-value: 9.27e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490253202 197 HAGEAAGPESIWQAIreLGAERIGHGVKAVEDPAL--MDYLAehRIGIESCLTSNvqTSTVASLAQHPLKQFLEHGVLAS 274
Cdd:PTZ00310 1115 HCGESGSMDHLYGAF--LCANSICHGINLRNDPPMqyLYYLA--QIGLHVSPLSN--NALFLAFLENPFPVFFHRGLNVS 1188
|
90 100 110
....*....|....*....|....*....|
gi 490253202 275 LNTDDPAV--QGVD-IIHEYTVAAPAAGLS 301
Cdd:PTZ00310 1189 LSTDDPLMfhQTQEpLIEEYSIAARVWGLS 1218
|
|
| PLN03055 |
PLN03055 |
AMP deaminase; Provisional |
197-301 |
2.44e-03 |
|
AMP deaminase; Provisional
Pssm-ID: 178613 Cd Length: 602 Bit Score: 39.46 E-value: 2.44e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490253202 197 HAGEAAGPESIWQAIreLGAERIGHGVKAVEDPAL--MDYLAEhrIGIESCLTSNvqTSTVASLAQHPLKQFLEHGVLAS 274
Cdd:PLN03055 422 HAGEAGDIDHLAAAF--LLAHNIAHGNNLRKSPGLqyLYYLAQ--IGLAMSPLSN--NSLFLDYHRNPFPMFFARGLNVS 495
|
90 100 110
....*....|....*....|....*....|
gi 490253202 275 LNTDDPA---VQGVDIIHEYTVAAPAAGLS 301
Cdd:PLN03055 496 LSTDDPLqihLTKEPLVEEYSIAAQVWKLS 525
|
|
| |
