|
Name |
Accession |
Description |
Interval |
E-value |
| A_deaminase |
pfam00962 |
Adenosine deaminase; |
7-333 |
6.97e-165 |
|
Adenosine deaminase;
Pssm-ID: 425964 Cd Length: 330 Bit Score: 462.67 E-value: 6.97e-165
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446489639 7 PLTDIHRHLDGNIRPQTILELGRQYNISLPAQSLETLIPHVQVIANEPDLVSFLTKLDWGVKVLASLDACRRVAFENIED 86
Cdd:pfam00962 1 PKAELHLHLDGSLRPDTLLELAKRYGIILPADFPEALEPLFRKYKKERDLQDFLDKYDIGVAVLRSPEDIRRLAFEYAED 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446489639 87 AARHGLHYVELRFSPGYMAMAhQLPVAGVVEAVIDGVREGCRTFGVQAKLIGIMSRTfGEAACQQELEAFLA-HRDQ-IT 164
Cdd:pfam00962 81 VAKDGVVYAEVRYDPQSHASR-GLSPDTVVDAVLDAVDAAEREFGITVRLIVCAMRH-EHPECSREIAELAPrYRDQgIV 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446489639 165 ALDLAGDELGFPGSLFLSH---FNRARDAGWHITVHAGEAAGPESIWQAIRELGAERIGHGVKAIEDRALMDFLAEQQIG 241
Cdd:pfam00962 159 AFGLAGDEKGFPPSLFRDHveaFARARDAGLHLTVHAGEAGGPQSVWEALDDLGAERIGHGVRSAEDPRLLDRLADRQIP 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446489639 242 IESCLTSNIQTSTVAELAAHPLKTFLEHGIRASINTDDPSVQGVDIIHEYTVAAPAAGLSREQIRQAQINGLEMAFLSAE 321
Cdd:pfam00962 239 LEICPTSNVQTGAVASLAEHPLKTFLRAGVPVSLNTDDPLMFGSDLLDEYQVAKRAPGFDEEELARLAKNAVKGSFLPAD 318
|
330
....*....|..
gi 446489639 322 EKRALREKVAAK 333
Cdd:pfam00962 319 EKRALLDEVDKV 330
|
|
| PRK09358 |
PRK09358 |
adenosine deaminase; Provisional |
1-332 |
1.02e-161 |
|
adenosine deaminase; Provisional
Pssm-ID: 236480 Cd Length: 340 Bit Score: 454.63 E-value: 1.02e-161
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446489639 1 MIDTTLPLTDIHRHLDGNIRPQTILELGRQYNISLPAQSLETLIPhVQVIANEPDLVSFLTKLDWGVKVLASLDACRRVA 80
Cdd:PRK09358 5 MIIRSLPKAELHLHLDGSLRPETILELARRNGIALPATDVEELPW-VRAAYDFRDLQSFLDKYDAGVAVLQTEEDLRRLA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446489639 81 FENIEDAARHGLHYVELRFSPGYMAMaHQLPVAGVVEAVIDGVREGCRTFGVQAKLIGIMSRTFGEAACQQELEAFLA-- 158
Cdd:PRK09358 84 FEYLEDAAADGVVYAEIRFDPQLHTE-RGLPLEEVVEAVLDGLRAAEAEFGISVRLILCFMRHFGEEAAARELEALAAry 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446489639 159 HRDQITALDLAGDELGFPGSLFLSHFNRARDAGWHITVHAGEAAGPESIWQAIRELGAERIGHGVKAIEDRALMDFLAEQ 238
Cdd:PRK09358 163 RDDGVVGFDLAGDELGFPPSKFARAFDRARDAGLRLTAHAGEAGGPESIWEALDELGAERIGHGVRAIEDPALMARLADR 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446489639 239 QIGIESCLTSNIQTSTVAELAAHPLKTFLEHGIRASINTDDPSVQGVDIIHEYTVAAPAAGLSREQIRQAQINGLEMAFL 318
Cdd:PRK09358 243 RIPLEVCPTSNVQTGAVPSLAEHPLKTLLDAGVRVTINTDDPLVFGTTLTEEYEALAEAFGLSDEDLAQLARNALEAAFL 322
|
330
....*....|....
gi 446489639 319 SAEEKRALREKVAA 332
Cdd:PRK09358 323 SEEEKAALLAEVDA 336
|
|
| Add |
COG1816 |
Adenosine deaminase [Nucleotide transport and metabolism]; Adenosine deaminase is part of the ... |
7-332 |
1.46e-149 |
|
Adenosine deaminase [Nucleotide transport and metabolism]; Adenosine deaminase is part of the Pathway/BioSystem: Menaquinone biosynthesis
Pssm-ID: 441421 Cd Length: 326 Bit Score: 423.34 E-value: 1.46e-149
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446489639 7 PLTDIHRHLDGNIRPQTILELGRQYNISLPAQSLETLIPHvqviANEPDLVSFLTKLDWGVKVLASLDACRRVAFENIED 86
Cdd:COG1816 1 PKAELHLHLEGSLRPETLLELAARNGIDLPAADVEELRAA----YDFRDLQSFLDTYDAGAAVLQTEEDFRRLAYEYLED 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446489639 87 AARHGLHYVELRFSPgYMAMAHQLPVAGVVEAVIDGVREGCRTFGVQAKLIGIMSRTFGEAACQQELEAFLAHRDQ-ITA 165
Cdd:COG1816 77 AAADGVRYAEIRFDP-QLHTRRGLSLEEVVEAVLDGLREAEREFGISVRLILCALRHLSPEAAFETLELALRYRDRgVVG 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446489639 166 LDLAGDELGFPGSLFLSHFNRARDAGWHITVHAGEAAGPESIWQAIRELGAERIGHGVKAIEDRALMDFLAEQQIGIESC 245
Cdd:COG1816 156 FGLAGDERGFPPEKFAEAFARAREAGLHLTAHAGEAGGPESIWEALDLLGAERIGHGVRAIEDPALVARLADRGIPLEVC 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446489639 246 LTSNIQTSTVAELAAHPLKTFLEHGIRASINTDDPSVQGVDIIHEYTVAAPAAGLSREQIRQAQINGLEMAFLSAEEKRA 325
Cdd:COG1816 236 PTSNVQLGVVPSLAEHPLRRLLDAGVRVTLNTDDPLYFGTTLTDEYELAAEAFGLSDADLAQLARNAIEASFLPEEEKAA 315
|
....*..
gi 446489639 326 LREKVAA 332
Cdd:COG1816 316 LLAELDA 322
|
|
| ADA |
cd01320 |
Adenosine deaminase (ADA) is a monomeric zinc dependent enzyme which catalyzes the ... |
6-330 |
1.19e-145 |
|
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: 413.52 E-value: 1.19e-145
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446489639 6 LPLTDIHRHLDGNIRPQTILELGRQYNISLPAQSLEtLIPHVQVIANEPDLVSFLTKLDWGVKVLASLDACRRVAFENIE 85
Cdd:cd01320 2 LPKAELHLHLDGSLRPETILELAKKNGITLPASDVE-LLELVVAAYNFSDLQDFLAKYDFGLSVLQTEEDFERLAYEYLE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446489639 86 DAARHGLHYVELRFSPGYMaMAHQLPVAGVVEAVIDGVREGCRTFGVQAKLIGIMSRTFGEAACQQELEAFLAHRDQ-IT 164
Cdd:cd01320 81 DAAADGVVYAEIRFSPQLH-TRRGLSFDEVVEAVLRGLDEAEAEFGIKARLILCGLRHLSPESAQETLELALKYRDKgVV 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446489639 165 ALDLAGDELGFPGSLFLSHFNRARDAGWHITVHAGEAAGPESIWQAIRELGAERIGHGVKAIEDRALMDFLAEQQIGIES 244
Cdd:cd01320 160 GFDLAGDEVGFPPEKFVRAFQRAREAGLRLTAHAGEAGGPESVRDALDLLGAERIGHGIRAIEDPELVKRLAERNIPLEV 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446489639 245 CLTSNIQTSTVAELAAHPLKTFLEHGIRASINTDDPSVQGVDIIHEYTVAAPAAGLSREQIRQAQINGLEMAFLSAEEKR 324
Cdd:cd01320 240 CPTSNVQTGAVKSLAEHPLRELLDAGVKVTINTDDPTVFGTYLTDEYELLAEAFGLTEEELKKLARNAVEASFLSEEEKA 319
|
....*.
gi 446489639 325 ALREKV 330
Cdd:cd01320 320 ELLKRI 325
|
|
| aden_deam |
TIGR01430 |
adenosine deaminase; This family includes the experimentally verified adenosine deaminases of ... |
6-330 |
1.88e-128 |
|
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: 369.76 E-value: 1.88e-128
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446489639 6 LPLTDIHRHLDGNIRPQTILELGRQYNISLPaQSLETLIPHVQVIANEPDLVSFLTKLDWGVKVLASLDACRRVAFENIE 85
Cdd:TIGR01430 1 LPKAELHLHLEGSIRPETLLELAQKNGIPLP-ADLQSGEELKEAYDKFRDLQDFLAKYDFGVEVLRTEDDFKRLAYEYVE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446489639 86 DAARHGLHYVELRFSPGYMAMAHQLPVaGVVEAVIDGVREGCRTFGVQAKLIGIMSRTFGEAACQQELEAFLAHRDQ-IT 164
Cdd:TIGR01430 80 KAAKDGVVYAEVFFDPQLHTNRGISPD-TVVEAVLDGLDEAERDFGIKSRLILCGMRHKQPEAAEETLELAKPYKEQtIV 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446489639 165 ALDLAGDELGFPGSLFLSHFNRARDAGWHITVHAGEAAGPESIWQAIRELGAERIGHGVKAIEDRALMDFLAEQQIGIES 244
Cdd:TIGR01430 159 GFGLAGDERGGPPPDFVRAFAIARELGLHLTVHAGELGGPESVREALDDLGATRIGHGVRALEDPELLKRLAQENITLEV 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446489639 245 CLTSNIQTSTVAELAAHPLKTFLEHGIRASINTDDPSVQGVDIIHEYTVAAPAAGLSREQIRQAQINGLEMAFLSAEEKR 324
Cdd:TIGR01430 239 CPTSNVALGVVKSLAEHPLRRFLEAGVKVTLNSDDPAYFGSYLTEEYEIAAKHAGLTEEELKQLARNALEGSFLSDDEKK 318
|
....*.
gi 446489639 325 ALREKV 330
Cdd:TIGR01430 319 ELLAKL 324
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| A_deaminase |
pfam00962 |
Adenosine deaminase; |
7-333 |
6.97e-165 |
|
Adenosine deaminase;
Pssm-ID: 425964 Cd Length: 330 Bit Score: 462.67 E-value: 6.97e-165
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446489639 7 PLTDIHRHLDGNIRPQTILELGRQYNISLPAQSLETLIPHVQVIANEPDLVSFLTKLDWGVKVLASLDACRRVAFENIED 86
Cdd:pfam00962 1 PKAELHLHLDGSLRPDTLLELAKRYGIILPADFPEALEPLFRKYKKERDLQDFLDKYDIGVAVLRSPEDIRRLAFEYAED 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446489639 87 AARHGLHYVELRFSPGYMAMAhQLPVAGVVEAVIDGVREGCRTFGVQAKLIGIMSRTfGEAACQQELEAFLA-HRDQ-IT 164
Cdd:pfam00962 81 VAKDGVVYAEVRYDPQSHASR-GLSPDTVVDAVLDAVDAAEREFGITVRLIVCAMRH-EHPECSREIAELAPrYRDQgIV 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446489639 165 ALDLAGDELGFPGSLFLSH---FNRARDAGWHITVHAGEAAGPESIWQAIRELGAERIGHGVKAIEDRALMDFLAEQQIG 241
Cdd:pfam00962 159 AFGLAGDEKGFPPSLFRDHveaFARARDAGLHLTVHAGEAGGPQSVWEALDDLGAERIGHGVRSAEDPRLLDRLADRQIP 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446489639 242 IESCLTSNIQTSTVAELAAHPLKTFLEHGIRASINTDDPSVQGVDIIHEYTVAAPAAGLSREQIRQAQINGLEMAFLSAE 321
Cdd:pfam00962 239 LEICPTSNVQTGAVASLAEHPLKTFLRAGVPVSLNTDDPLMFGSDLLDEYQVAKRAPGFDEEELARLAKNAVKGSFLPAD 318
|
330
....*....|..
gi 446489639 322 EKRALREKVAAK 333
Cdd:pfam00962 319 EKRALLDEVDKV 330
|
|
| PRK09358 |
PRK09358 |
adenosine deaminase; Provisional |
1-332 |
1.02e-161 |
|
adenosine deaminase; Provisional
Pssm-ID: 236480 Cd Length: 340 Bit Score: 454.63 E-value: 1.02e-161
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446489639 1 MIDTTLPLTDIHRHLDGNIRPQTILELGRQYNISLPAQSLETLIPhVQVIANEPDLVSFLTKLDWGVKVLASLDACRRVA 80
Cdd:PRK09358 5 MIIRSLPKAELHLHLDGSLRPETILELARRNGIALPATDVEELPW-VRAAYDFRDLQSFLDKYDAGVAVLQTEEDLRRLA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446489639 81 FENIEDAARHGLHYVELRFSPGYMAMaHQLPVAGVVEAVIDGVREGCRTFGVQAKLIGIMSRTFGEAACQQELEAFLA-- 158
Cdd:PRK09358 84 FEYLEDAAADGVVYAEIRFDPQLHTE-RGLPLEEVVEAVLDGLRAAEAEFGISVRLILCFMRHFGEEAAARELEALAAry 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446489639 159 HRDQITALDLAGDELGFPGSLFLSHFNRARDAGWHITVHAGEAAGPESIWQAIRELGAERIGHGVKAIEDRALMDFLAEQ 238
Cdd:PRK09358 163 RDDGVVGFDLAGDELGFPPSKFARAFDRARDAGLRLTAHAGEAGGPESIWEALDELGAERIGHGVRAIEDPALMARLADR 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446489639 239 QIGIESCLTSNIQTSTVAELAAHPLKTFLEHGIRASINTDDPSVQGVDIIHEYTVAAPAAGLSREQIRQAQINGLEMAFL 318
Cdd:PRK09358 243 RIPLEVCPTSNVQTGAVPSLAEHPLKTLLDAGVRVTINTDDPLVFGTTLTEEYEALAEAFGLSDEDLAQLARNALEAAFL 322
|
330
....*....|....
gi 446489639 319 SAEEKRALREKVAA 332
Cdd:PRK09358 323 SEEEKAALLAEVDA 336
|
|
| Add |
COG1816 |
Adenosine deaminase [Nucleotide transport and metabolism]; Adenosine deaminase is part of the ... |
7-332 |
1.46e-149 |
|
Adenosine deaminase [Nucleotide transport and metabolism]; Adenosine deaminase is part of the Pathway/BioSystem: Menaquinone biosynthesis
Pssm-ID: 441421 Cd Length: 326 Bit Score: 423.34 E-value: 1.46e-149
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446489639 7 PLTDIHRHLDGNIRPQTILELGRQYNISLPAQSLETLIPHvqviANEPDLVSFLTKLDWGVKVLASLDACRRVAFENIED 86
Cdd:COG1816 1 PKAELHLHLEGSLRPETLLELAARNGIDLPAADVEELRAA----YDFRDLQSFLDTYDAGAAVLQTEEDFRRLAYEYLED 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446489639 87 AARHGLHYVELRFSPgYMAMAHQLPVAGVVEAVIDGVREGCRTFGVQAKLIGIMSRTFGEAACQQELEAFLAHRDQ-ITA 165
Cdd:COG1816 77 AAADGVRYAEIRFDP-QLHTRRGLSLEEVVEAVLDGLREAEREFGISVRLILCALRHLSPEAAFETLELALRYRDRgVVG 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446489639 166 LDLAGDELGFPGSLFLSHFNRARDAGWHITVHAGEAAGPESIWQAIRELGAERIGHGVKAIEDRALMDFLAEQQIGIESC 245
Cdd:COG1816 156 FGLAGDERGFPPEKFAEAFARAREAGLHLTAHAGEAGGPESIWEALDLLGAERIGHGVRAIEDPALVARLADRGIPLEVC 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446489639 246 LTSNIQTSTVAELAAHPLKTFLEHGIRASINTDDPSVQGVDIIHEYTVAAPAAGLSREQIRQAQINGLEMAFLSAEEKRA 325
Cdd:COG1816 236 PTSNVQLGVVPSLAEHPLRRLLDAGVRVTLNTDDPLYFGTTLTDEYELAAEAFGLSDADLAQLARNAIEASFLPEEEKAA 315
|
....*..
gi 446489639 326 LREKVAA 332
Cdd:COG1816 316 LLAELDA 322
|
|
| ADA |
cd01320 |
Adenosine deaminase (ADA) is a monomeric zinc dependent enzyme which catalyzes the ... |
6-330 |
1.19e-145 |
|
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: 413.52 E-value: 1.19e-145
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446489639 6 LPLTDIHRHLDGNIRPQTILELGRQYNISLPAQSLEtLIPHVQVIANEPDLVSFLTKLDWGVKVLASLDACRRVAFENIE 85
Cdd:cd01320 2 LPKAELHLHLDGSLRPETILELAKKNGITLPASDVE-LLELVVAAYNFSDLQDFLAKYDFGLSVLQTEEDFERLAYEYLE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446489639 86 DAARHGLHYVELRFSPGYMaMAHQLPVAGVVEAVIDGVREGCRTFGVQAKLIGIMSRTFGEAACQQELEAFLAHRDQ-IT 164
Cdd:cd01320 81 DAAADGVVYAEIRFSPQLH-TRRGLSFDEVVEAVLRGLDEAEAEFGIKARLILCGLRHLSPESAQETLELALKYRDKgVV 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446489639 165 ALDLAGDELGFPGSLFLSHFNRARDAGWHITVHAGEAAGPESIWQAIRELGAERIGHGVKAIEDRALMDFLAEQQIGIES 244
Cdd:cd01320 160 GFDLAGDEVGFPPEKFVRAFQRAREAGLRLTAHAGEAGGPESVRDALDLLGAERIGHGIRAIEDPELVKRLAERNIPLEV 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446489639 245 CLTSNIQTSTVAELAAHPLKTFLEHGIRASINTDDPSVQGVDIIHEYTVAAPAAGLSREQIRQAQINGLEMAFLSAEEKR 324
Cdd:cd01320 240 CPTSNVQTGAVKSLAEHPLRELLDAGVKVTINTDDPTVFGTYLTDEYELLAEAFGLTEEELKKLARNAVEASFLSEEEKA 319
|
....*.
gi 446489639 325 ALREKV 330
Cdd:cd01320 320 ELLKRI 325
|
|
| aden_deam |
TIGR01430 |
adenosine deaminase; This family includes the experimentally verified adenosine deaminases of ... |
6-330 |
1.88e-128 |
|
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: 369.76 E-value: 1.88e-128
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446489639 6 LPLTDIHRHLDGNIRPQTILELGRQYNISLPaQSLETLIPHVQVIANEPDLVSFLTKLDWGVKVLASLDACRRVAFENIE 85
Cdd:TIGR01430 1 LPKAELHLHLEGSIRPETLLELAQKNGIPLP-ADLQSGEELKEAYDKFRDLQDFLAKYDFGVEVLRTEDDFKRLAYEYVE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446489639 86 DAARHGLHYVELRFSPGYMAMAHQLPVaGVVEAVIDGVREGCRTFGVQAKLIGIMSRTFGEAACQQELEAFLAHRDQ-IT 164
Cdd:TIGR01430 80 KAAKDGVVYAEVFFDPQLHTNRGISPD-TVVEAVLDGLDEAERDFGIKSRLILCGMRHKQPEAAEETLELAKPYKEQtIV 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446489639 165 ALDLAGDELGFPGSLFLSHFNRARDAGWHITVHAGEAAGPESIWQAIRELGAERIGHGVKAIEDRALMDFLAEQQIGIES 244
Cdd:TIGR01430 159 GFGLAGDERGGPPPDFVRAFAIARELGLHLTVHAGELGGPESVREALDDLGATRIGHGVRALEDPELLKRLAQENITLEV 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446489639 245 CLTSNIQTSTVAELAAHPLKTFLEHGIRASINTDDPSVQGVDIIHEYTVAAPAAGLSREQIRQAQINGLEMAFLSAEEKR 324
Cdd:TIGR01430 239 CPTSNVALGVVKSLAEHPLRRFLEAGVKVTLNSDDPAYFGSYLTEEYEIAAKHAGLTEEELKQLARNALEGSFLSDDEKK 318
|
....*.
gi 446489639 325 ALREKV 330
Cdd:TIGR01430 319 ELLAKL 324
|
|
| ADA_AMPD |
cd00443 |
Adenosine/AMP deaminase. Adenosine deaminases (ADAs) are present in pro- and eukaryotic ... |
6-329 |
5.93e-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: 173.69 E-value: 5.93e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446489639 6 LPLTDIHRHLDGNIRPQTILELGRQynisLPAQSLETLIPHVQviaNEPDLvsfltkldwgvkvlasldacRRVAFENIE 85
Cdd:cd00443 1 LPKVELHAHLSGSISPETLLELIKK----EFFEKFLLVHNLLQ---KGEAL--------------------ARALKEVIE 53
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446489639 86 DAARHGLHYVELRFSPGYMAMAHQLPVAGVVEAVIDGVREGCRTF-GVQAKLIGIMSRT------FGEAACQQELEAFLa 158
Cdd:cd00443 54 EFAEDNVQYLELRTTPRLLETEKGLTKEQYWLLVIEGISEAKQWFpPIKVRLILSVDRRgpyvqnYLVASEILELAKFL- 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446489639 159 hRDQITALDLAGDELGFPGSL--FLSHFNRARDAGW-HITVHAGEAAGPESIWQAIrELGAERIGHGVKAIEDRALMDFL 235
Cdd:cd00443 133 -SNYVVGIDLVGDESKGENPLrdFYSYYEYARRLGLlGLTLHCGETGNREELLQAL-LLLPDRIGHGIFLLKHPELIYLV 210
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446489639 236 AEQQIGIESCLTSNIQTSTVAELAAHPLKTFLEHGIRASINTDDPSVQGVDIIHEYTVAAPAAGLSREQIRQAQINGLEM 315
Cdd:cd00443 211 KLRNIPIEVCPTSNVVLGTVQSYEKHPFMRFFKAGLPVSLSTDDPGIFGTSLSEEYSLAAKTFGLTFEDLCELNRNSVLS 290
|
330
....*....|....
gi 446489639 316 AFLSAEEKRALREK 329
Cdd:cd00443 291 SFAKDEEKKSLLEV 304
|
|
| PTZ00124 |
PTZ00124 |
adenosine deaminase; Provisional |
6-329 |
2.48e-39 |
|
adenosine deaminase; Provisional
Pssm-ID: 173415 Cd Length: 362 Bit Score: 142.31 E-value: 2.48e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446489639 6 LPLTDIHRHLDGNIRPQTILELGRQYNISlPAQSLETLIPHVQVIANEPDLVSFLTKLDWGVKVLASLDACRRVAFENIE 85
Cdd:PTZ00124 35 IPKCELHCHLDLCFSVDFFLSCIRKYNLQ-PNLSDEEILDYYLFAKGGKSLGEFVEKAIRVADIFNDYEVIEDLAKHAVF 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446489639 86 DAARHGLHYVELRFSPGYMAMAHQLPVAGVVEAVIDGVREGCRTFG--VQAKLIGIMSRTFGEAACQQELEAFLAHRDQI 163
Cdd:PTZ00124 114 NKYKEGVVLMEFRYSPTFVAFKHNLDIDLIHQAIVKGIKEAVELLDhkIEVGLLCIGDTGHDAAPIKESADFCLKHKADF 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446489639 164 TALDLAGDELGFpgSLFLSHFNRARDAGWHITVHAGEAAGP---ESIWQAIRELGAERIGHGVKAIEDRALMDFLAEQQI 240
Cdd:PTZ00124 194 VGFDHAGHEVDL--KPFKDIFDYVREAGVNLTVHAGEDVTLpnlNTLYSAIQVLKVKRIGHGIRVAESQELIDMVKEKDI 271
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446489639 241 GIESCLTSNIQTSTVAELAAHPLKTFLEHGIRASINTDDPSVQGVDIIHEYTVAAPAAGLSREQIRQAQINGLEMAFLSA 320
Cdd:PTZ00124 272 LLEVCPISNVLLNNAKSMDTHPIRKLYDAGVKVSVNSDDPGMFLTNINDDYEELYTHLNFTLADFMKMNEWALEKSFLDK 351
|
....*....
gi 446489639 321 EEKRALREK 329
Cdd:PTZ00124 352 DIKLKIKKL 360
|
|
| ADGF |
cd01321 |
Adenosine deaminase-related growth factors (ADGF), a novel family of secreted growth-factors ... |
91-333 |
1.79e-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: 78.85 E-value: 1.79e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446489639 91 GLHYVELR--FSPGYMAMAHQLPVAGVVEAVIDGVREGCRT----FGvqAKLIGIMSRTFGEAACQQELEAFLAHR---- 160
Cdd:cd01321 83 NVQYVELRssFSPLYDLDGREYDYEETVQLLEEVVEKFKKThpdfIG--LKIIYATLRNFNDSEIKESMEQCLNLKkkfp 160
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446489639 161 DQITALDLAGDE-LGFPGSLFLSHFNRARDAGWHIT--VHAGEAAGPES-----IWQAIReLGAERIGHGVKAIEDRALM 232
Cdd:cd01321 161 DFIAGFDLVGQEdAGRPLLDFLPQLLWFPKQCAEIPffFHAGETNGDGTetdenLVDALL-LNTKRIGHGFALPKHPLLM 239
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446489639 233 DFLAEQQIGIESCLTSNIQTSTVAELAAHPLKTFLEHGIRASINTDDPSVQGVD-IIHEYTVA----APA-AGLSreQIR 306
Cdd:cd01321 240 DLVKKKNIAIEVCPISNQVLGLVSDLRNHPAAALLARGVPVVISSDDPGFWGAKgLSHDFYQAfmglAPAdAGLR--GLK 317
|
250 260
....*....|....*....|....*..
gi 446489639 307 QAQINGLEMAFLSAEEKRALREKVAAK 333
Cdd:cd01321 318 QLAENSIRYSALSDQEKDEAVAKWEKK 344
|
|
| AMPD |
cd01319 |
AMP deaminase (AMPD) catalyzes the hydrolytic deamination of adensosine monophosphate (AMP) at ... |
181-324 |
5.97e-06 |
|
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: 47.75 E-value: 5.97e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446489639 181 LSHFNRARdaGWHITV---HAGEAAGPESIWQAIreLGAERIGHGVkAIEDRALMDFLAE-QQIGIE-SCLTSNiqtSTV 255
Cdd:cd01319 315 LNSFRKAR--GFNTFVlrpHCGEAGDIDHLASAF--LLAHGISHGI-NLRKVPVLQYLYYlTQIGIAmSPLSNN---SLF 386
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446489639 256 AELAAHPLKTFLEHGIRASINTDDP---SVQGVDIIHEYTVAAPAAGLSREQIRQAQINGLEMAFLSAEEKR 324
Cdd:cd01319 387 LSYEKNPFPEFFKRGLNVSLSTDDPlqfHFTKEPLMEEYSIAAQVWKLSTCDMCELARNSVLQSGFEHSIKR 458
|
|
| metallo-dependent_hydrolases |
cd01292 |
Superfamily of metallo-dependent hydrolases (also called amidohydrolase superfamily) is a ... |
46-284 |
6.42e-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: 46.94 E-value: 6.42e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446489639 46 HVQVIANEPDLVSFLTKLDWGVKVLASLDACRRVafenIEDAARHGLHYVELRFSPGYMAMAhqlpvagvvEAVIDGVRE 125
Cdd:cd01292 7 HLDGSALRGTRLNLELKEAEELSPEDLYEDTLRA----LEALLAGGVTTVVDMGSTPPPTTT---------KAAIEAVAE 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446489639 126 GCRTFGVQAKLI--GIMSRTFGEAACQQEL---EAFLAHRDQITALDLAGDE--LGFPGSLFLSHFNRARDAGWHITVHA 198
Cdd:cd01292 74 AARASAGIRVVLglGIPGVPAAVDEDAEALlleLLRRGLELGAVGLKLAGPYtaTGLSDESLRRVLEEARKLGLPVVIHA 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446489639 199 GEAAGPESIW----QAIRELGAERIGHGVKAIEDraLMDFLAEQQIGIESCLTSNiQTSTVAELAAHPLKTFLEHGIRAS 274
Cdd:cd01292 154 GELPDPTRALedlvALLRLGGRVVIGHVSHLDPE--LLELLKEAGVSLEVCPLSN-YLLGRDGEGAEALRRLLELGIRVT 230
|
250
....*....|
gi 446489639 275 INTDDPSVQG 284
Cdd:cd01292 231 LGTDGPPHPL 240
|
|
| AMP_deaminase |
TIGR01429 |
AMP deaminase; This model describes AMP deaminase, a large, well-conserved eukaryotic protein ... |
181-301 |
1.95e-03 |
|
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: 39.83 E-value: 1.95e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446489639 181 LSHFNRARdaGWHITV---HAGEAAGPESIWQAIreLGAERIGHGVKAIEDRALMDFLAEQQIGIESCLTSNiqTSTVAE 257
Cdd:TIGR01429 427 LNNFRRER--GLNTFLlrpHCGEAGSVDHLVSAF--LTSHGINHGILLRKVPVLQYLYYLTQIPIAMSPLSN--NSLFLE 500
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 446489639 258 LAAHPLKTFLEHGIRASINTDDP---SVQGVDIIHEYTVAAPAAGLS 301
Cdd:TIGR01429 501 YSKNPLPEYLHKGLNVSLSTDDPlqfHYTKEALMEEYAIAAQVWKLS 547
|
|
| |
