|
Name |
Accession |
Description |
Interval |
E-value |
| PRK09358 |
PRK09358 |
adenosine deaminase; Provisional |
1-326 |
5.35e-128 |
|
adenosine deaminase; Provisional
Pssm-ID: 236480 Cd Length: 340 Bit Score: 369.51 E-value: 5.35e-128
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113478613 1 MIYPDLPLIDLHRHLEGNLRLETVLELARKFNVTLPADTVEGLRPyVQVSSRQPGVMAFIEKFNLLMKVLGNEQACFRIA 80
Cdd:PRK09358 5 MIIRSLPKAELHLHLDGSLRPETILELARRNGIALPATDVEELPW-VRAAYDFRDLQSFLDKYDAGVAVLQTEEDLRRLA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113478613 81 QEAVLDAANEGIDYLELRFSPVFMAaDHQLNPSAVVEAVLAGIQAAAAESGIQVNPLGIISRTYGPQVAEQELSALLSYA 160
Cdd:PRK09358 84 FEYLEDAAADGVVYAEIRFDPQLHT-ERGLPLEEVVEAVLDGLRAAEAEFGISVRLILCFMRHFGEEAAARELEALAARY 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113478613 161 --DKIRGLDLAGDEANFPAQLFLPHFKKARDVGWHITVHAGEADGPQSIWDSIRLLGAERIGHGLAARHDAQLLKYLLDH 238
Cdd:PRK09358 163 rdDGVVGFDLAGDELGFPPSKFARAFDRARDAGLRLTAHAGEAGGPESIWEALDELGAERIGHGVRAIEDPALMARLADR 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113478613 239 QIGIECNLTSNVQTSSVADYVSHPLKFFLEKRLLASINSDDPGISAIDLPYEYNVAAPKAGLSETQIRQAQLNALESAFL 318
Cdd:PRK09358 243 RIPLEVCPTSNVQTGAVPSLAEHPLKTLLDAGVRVTINTDDPLVFGTTLTEEYEALAEAFGLSDEDLAQLARNALEAAFL 322
|
....*...
gi 1113478613 319 NSQEKLAL 326
Cdd:PRK09358 323 SEEEKAAL 330
|
|
| Add |
COG1816 |
Adenosine deaminase [Nucleotide transport and metabolism]; Adenosine deaminase is part of the ... |
7-326 |
1.70e-127 |
|
Adenosine deaminase [Nucleotide transport and metabolism]; Adenosine deaminase is part of the Pathway/BioSystem: Menaquinone biosynthesis
Pssm-ID: 441421 Cd Length: 326 Bit Score: 367.49 E-value: 1.70e-127
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113478613 7 PLIDLHRHLEGNLRLETVLELARKFNVTLPADTVEGLRPyvqvSSRQPGVMAFIEKFNLLMKVLGNEQACFRIAQEAVLD 86
Cdd:COG1816 1 PKAELHLHLEGSLRPETLLELAARNGIDLPAADVEELRA----AYDFRDLQSFLDTYDAGAAVLQTEEDFRRLAYEYLED 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113478613 87 AANEGIDYLELRFSPVFmAADHQLNPSAVVEAVLAGIQAAAAESGIQVNPLGIISRTYGPQVAEQELSALLSYADK-IRG 165
Cdd:COG1816 77 AAADGVRYAEIRFDPQL-HTRRGLSLEEVVEAVLDGLREAEREFGISVRLILCALRHLSPEAAFETLELALRYRDRgVVG 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113478613 166 LDLAGDEANFPAQLFLPHFKKARDVGWHITVHAGEADGPQSIWDSIRLLGAERIGHGLAARHDAQLLKYLLDHQIGIECN 245
Cdd:COG1816 156 FGLAGDERGFPPEKFAEAFARAREAGLHLTAHAGEAGGPESIWEALDLLGAERIGHGVRAIEDPALVARLADRGIPLEVC 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113478613 246 LTSNVQTSSVADYVSHPLKFFLEKRLLASINSDDPGISAIDLPYEYNVAAPKAGLSETQIRQAQLNALESAFLNSQEKLA 325
Cdd:COG1816 236 PTSNVQLGVVPSLAEHPLRRLLDAGVRVTLNTDDPLYFGTTLTDEYELAAEAFGLSDADLAQLARNAIEASFLPEEEKAA 315
|
.
gi 1113478613 326 L 326
Cdd:COG1816 316 L 316
|
|
| ADA |
cd01320 |
Adenosine deaminase (ADA) is a monomeric zinc dependent enzyme which catalyzes the ... |
5-326 |
5.08e-114 |
|
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: 333.40 E-value: 5.08e-114
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113478613 5 DLPLIDLHRHLEGNLRLETVLELARKFNVTLPADTVEgLRPYVQVSSRQPGVMAFIEKFNLLMKVLGNEQACFRIAQEAV 84
Cdd:cd01320 1 NLPKAELHLHLDGSLRPETILELAKKNGITLPASDVE-LLELVVAAYNFSDLQDFLAKYDFGLSVLQTEEDFERLAYEYL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113478613 85 LDAANEGIDYLELRFSPVFMAaDHQLNPSAVVEAVLAGIQAAAAESGIQVNPLGIISRTYGPQVAEQELSALLSYADK-I 163
Cdd:cd01320 80 EDAAADGVVYAEIRFSPQLHT-RRGLSFDEVVEAVLRGLDEAEAEFGIKARLILCGLRHLSPESAQETLELALKYRDKgV 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113478613 164 RGLDLAGDEANFPAQLFLPHFKKARDVGWHITVHAGEADGPQSIWDSIRLLGAERIGHGLAARHDAQLLKYLLDHQIGIE 243
Cdd:cd01320 159 VGFDLAGDEVGFPPEKFVRAFQRAREAGLRLTAHAGEAGGPESVRDALDLLGAERIGHGIRAIEDPELVKRLAERNIPLE 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113478613 244 CNLTSNVQTSSVADYVSHPLKFFLEKRLLASINSDDPGISAIDLPYEYNVAAPKAGLSETQIRQAQLNALESAFLNSQEK 323
Cdd:cd01320 239 VCPTSNVQTGAVKSLAEHPLRELLDAGVKVTINTDDPTVFGTYLTDEYELLAEAFGLTEEELKKLARNAVEASFLSEEEK 318
|
...
gi 1113478613 324 LAL 326
Cdd:cd01320 319 AEL 321
|
|
| aden_deam |
TIGR01430 |
adenosine deaminase; This family includes the experimentally verified adenosine deaminases of ... |
6-329 |
1.68e-107 |
|
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: 316.99 E-value: 1.68e-107
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113478613 6 LPLIDLHRHLEGNLRLETVLELARKFNVTLPADTVEGLrPYVQVSSRQPGVMAFIEKFNLLMKVLGNEQACFRIAQEAVL 85
Cdd:TIGR01430 1 LPKAELHLHLEGSIRPETLLELAQKNGIPLPADLQSGE-ELKEAYDKFRDLQDFLAKYDFGVEVLRTEDDFKRLAYEYVE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113478613 86 DAANEGIDYLELRFSPVFMAADHqLNPSAVVEAVLAGIQAAAAESGIQVNPLGIISRTYGPQVAEQELSALLSYADK-IR 164
Cdd:TIGR01430 80 KAAKDGVVYAEVFFDPQLHTNRG-ISPDTVVEAVLDGLDEAERDFGIKSRLILCGMRHKQPEAAEETLELAKPYKEQtIV 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113478613 165 GLDLAGDEANFPAQLFLPHFKKARDVGWHITVHAGEADGPQSIWDSIRLLGAERIGHGLAARHDAQLLKYLLDHQIGIEC 244
Cdd:TIGR01430 159 GFGLAGDERGGPPPDFVRAFAIARELGLHLTVHAGELGGPESVREALDDLGATRIGHGVRALEDPELLKRLAQENITLEV 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113478613 245 NLTSNVQTSSVADYVSHPLKFFLEKRLLASINSDDPGISAIDLPYEYNVAAPKAGLSETQIRQAQLNALESAFLNSQEKL 324
Cdd:TIGR01430 239 CPTSNVALGVVKSLAEHPLRRFLEAGVKVTLNSDDPAYFGSYLTEEYEIAAKHAGLTEEELKQLARNALEGSFLSDDEKK 318
|
....*
gi 1113478613 325 ALFTK 329
Cdd:TIGR01430 319 ELLAK 323
|
|
| A_deaminase |
pfam00962 |
Adenosine deaminase; |
7-326 |
3.83e-105 |
|
Adenosine deaminase;
Pssm-ID: 425964 Cd Length: 330 Bit Score: 310.90 E-value: 3.83e-105
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113478613 7 PLIDLHRHLEGNLRLETVLELARKFNVTLPADTVEGLRPYVQVSSRQPGVMAFIEKFNLLMKVLGNEQACFRIAQEAVLD 86
Cdd:pfam00962 1 PKAELHLHLDGSLRPDTLLELAKRYGIILPADFPEALEPLFRKYKKERDLQDFLDKYDIGVAVLRSPEDIRRLAFEYAED 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113478613 87 AANEGIDYLELRFSPVFMAAdHQLNPSAVVEAVLAGIQAAAAESGIQVNPLGIISRTYGPQVAEQELSALLSYADK-IRG 165
Cdd:pfam00962 81 VAKDGVVYAEVRYDPQSHAS-RGLSPDTVVDAVLDAVDAAEREFGITVRLIVCAMRHEHPECSREIAELAPRYRDQgIVA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113478613 166 LDLAGDEANFPAQLFLPH---FKKARDVGWHITVHAGEADGPQSIWDSIRLLGAERIGHGLAARHDAQLLKYLLDHQIGI 242
Cdd:pfam00962 160 FGLAGDEKGFPPSLFRDHveaFARARDAGLHLTVHAGEAGGPQSVWEALDDLGAERIGHGVRSAEDPRLLDRLADRQIPL 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113478613 243 ECNLTSNVQTSSVADYVSHPLKFFLEKRLLASINSDDPGISAIDLPYEYNVAAPKAGLSETQIRQAQLNALESAFLNSQE 322
Cdd:pfam00962 240 EICPTSNVQTGAVASLAEHPLKTFLRAGVPVSLNTDDPLMFGSDLLDEYQVAKRAPGFDEEELARLAKNAVKGSFLPADE 319
|
....
gi 1113478613 323 KLAL 326
Cdd:pfam00962 320 KRAL 323
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| PRK09358 |
PRK09358 |
adenosine deaminase; Provisional |
1-326 |
5.35e-128 |
|
adenosine deaminase; Provisional
Pssm-ID: 236480 Cd Length: 340 Bit Score: 369.51 E-value: 5.35e-128
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113478613 1 MIYPDLPLIDLHRHLEGNLRLETVLELARKFNVTLPADTVEGLRPyVQVSSRQPGVMAFIEKFNLLMKVLGNEQACFRIA 80
Cdd:PRK09358 5 MIIRSLPKAELHLHLDGSLRPETILELARRNGIALPATDVEELPW-VRAAYDFRDLQSFLDKYDAGVAVLQTEEDLRRLA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113478613 81 QEAVLDAANEGIDYLELRFSPVFMAaDHQLNPSAVVEAVLAGIQAAAAESGIQVNPLGIISRTYGPQVAEQELSALLSYA 160
Cdd:PRK09358 84 FEYLEDAAADGVVYAEIRFDPQLHT-ERGLPLEEVVEAVLDGLRAAEAEFGISVRLILCFMRHFGEEAAARELEALAARY 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113478613 161 --DKIRGLDLAGDEANFPAQLFLPHFKKARDVGWHITVHAGEADGPQSIWDSIRLLGAERIGHGLAARHDAQLLKYLLDH 238
Cdd:PRK09358 163 rdDGVVGFDLAGDELGFPPSKFARAFDRARDAGLRLTAHAGEAGGPESIWEALDELGAERIGHGVRAIEDPALMARLADR 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113478613 239 QIGIECNLTSNVQTSSVADYVSHPLKFFLEKRLLASINSDDPGISAIDLPYEYNVAAPKAGLSETQIRQAQLNALESAFL 318
Cdd:PRK09358 243 RIPLEVCPTSNVQTGAVPSLAEHPLKTLLDAGVRVTINTDDPLVFGTTLTEEYEALAEAFGLSDEDLAQLARNALEAAFL 322
|
....*...
gi 1113478613 319 NSQEKLAL 326
Cdd:PRK09358 323 SEEEKAAL 330
|
|
| Add |
COG1816 |
Adenosine deaminase [Nucleotide transport and metabolism]; Adenosine deaminase is part of the ... |
7-326 |
1.70e-127 |
|
Adenosine deaminase [Nucleotide transport and metabolism]; Adenosine deaminase is part of the Pathway/BioSystem: Menaquinone biosynthesis
Pssm-ID: 441421 Cd Length: 326 Bit Score: 367.49 E-value: 1.70e-127
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113478613 7 PLIDLHRHLEGNLRLETVLELARKFNVTLPADTVEGLRPyvqvSSRQPGVMAFIEKFNLLMKVLGNEQACFRIAQEAVLD 86
Cdd:COG1816 1 PKAELHLHLEGSLRPETLLELAARNGIDLPAADVEELRA----AYDFRDLQSFLDTYDAGAAVLQTEEDFRRLAYEYLED 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113478613 87 AANEGIDYLELRFSPVFmAADHQLNPSAVVEAVLAGIQAAAAESGIQVNPLGIISRTYGPQVAEQELSALLSYADK-IRG 165
Cdd:COG1816 77 AAADGVRYAEIRFDPQL-HTRRGLSLEEVVEAVLDGLREAEREFGISVRLILCALRHLSPEAAFETLELALRYRDRgVVG 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113478613 166 LDLAGDEANFPAQLFLPHFKKARDVGWHITVHAGEADGPQSIWDSIRLLGAERIGHGLAARHDAQLLKYLLDHQIGIECN 245
Cdd:COG1816 156 FGLAGDERGFPPEKFAEAFARAREAGLHLTAHAGEAGGPESIWEALDLLGAERIGHGVRAIEDPALVARLADRGIPLEVC 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113478613 246 LTSNVQTSSVADYVSHPLKFFLEKRLLASINSDDPGISAIDLPYEYNVAAPKAGLSETQIRQAQLNALESAFLNSQEKLA 325
Cdd:COG1816 236 PTSNVQLGVVPSLAEHPLRRLLDAGVRVTLNTDDPLYFGTTLTDEYELAAEAFGLSDADLAQLARNAIEASFLPEEEKAA 315
|
.
gi 1113478613 326 L 326
Cdd:COG1816 316 L 316
|
|
| ADA |
cd01320 |
Adenosine deaminase (ADA) is a monomeric zinc dependent enzyme which catalyzes the ... |
5-326 |
5.08e-114 |
|
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: 333.40 E-value: 5.08e-114
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113478613 5 DLPLIDLHRHLEGNLRLETVLELARKFNVTLPADTVEgLRPYVQVSSRQPGVMAFIEKFNLLMKVLGNEQACFRIAQEAV 84
Cdd:cd01320 1 NLPKAELHLHLDGSLRPETILELAKKNGITLPASDVE-LLELVVAAYNFSDLQDFLAKYDFGLSVLQTEEDFERLAYEYL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113478613 85 LDAANEGIDYLELRFSPVFMAaDHQLNPSAVVEAVLAGIQAAAAESGIQVNPLGIISRTYGPQVAEQELSALLSYADK-I 163
Cdd:cd01320 80 EDAAADGVVYAEIRFSPQLHT-RRGLSFDEVVEAVLRGLDEAEAEFGIKARLILCGLRHLSPESAQETLELALKYRDKgV 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113478613 164 RGLDLAGDEANFPAQLFLPHFKKARDVGWHITVHAGEADGPQSIWDSIRLLGAERIGHGLAARHDAQLLKYLLDHQIGIE 243
Cdd:cd01320 159 VGFDLAGDEVGFPPEKFVRAFQRAREAGLRLTAHAGEAGGPESVRDALDLLGAERIGHGIRAIEDPELVKRLAERNIPLE 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113478613 244 CNLTSNVQTSSVADYVSHPLKFFLEKRLLASINSDDPGISAIDLPYEYNVAAPKAGLSETQIRQAQLNALESAFLNSQEK 323
Cdd:cd01320 239 VCPTSNVQTGAVKSLAEHPLRELLDAGVKVTINTDDPTVFGTYLTDEYELLAEAFGLTEEELKKLARNAVEASFLSEEEK 318
|
...
gi 1113478613 324 LAL 326
Cdd:cd01320 319 AEL 321
|
|
| aden_deam |
TIGR01430 |
adenosine deaminase; This family includes the experimentally verified adenosine deaminases of ... |
6-329 |
1.68e-107 |
|
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: 316.99 E-value: 1.68e-107
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113478613 6 LPLIDLHRHLEGNLRLETVLELARKFNVTLPADTVEGLrPYVQVSSRQPGVMAFIEKFNLLMKVLGNEQACFRIAQEAVL 85
Cdd:TIGR01430 1 LPKAELHLHLEGSIRPETLLELAQKNGIPLPADLQSGE-ELKEAYDKFRDLQDFLAKYDFGVEVLRTEDDFKRLAYEYVE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113478613 86 DAANEGIDYLELRFSPVFMAADHqLNPSAVVEAVLAGIQAAAAESGIQVNPLGIISRTYGPQVAEQELSALLSYADK-IR 164
Cdd:TIGR01430 80 KAAKDGVVYAEVFFDPQLHTNRG-ISPDTVVEAVLDGLDEAERDFGIKSRLILCGMRHKQPEAAEETLELAKPYKEQtIV 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113478613 165 GLDLAGDEANFPAQLFLPHFKKARDVGWHITVHAGEADGPQSIWDSIRLLGAERIGHGLAARHDAQLLKYLLDHQIGIEC 244
Cdd:TIGR01430 159 GFGLAGDERGGPPPDFVRAFAIARELGLHLTVHAGELGGPESVREALDDLGATRIGHGVRALEDPELLKRLAQENITLEV 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113478613 245 NLTSNVQTSSVADYVSHPLKFFLEKRLLASINSDDPGISAIDLPYEYNVAAPKAGLSETQIRQAQLNALESAFLNSQEKL 324
Cdd:TIGR01430 239 CPTSNVALGVVKSLAEHPLRRFLEAGVKVTLNSDDPAYFGSYLTEEYEIAAKHAGLTEEELKQLARNALEGSFLSDDEKK 318
|
....*
gi 1113478613 325 ALFTK 329
Cdd:TIGR01430 319 ELLAK 323
|
|
| A_deaminase |
pfam00962 |
Adenosine deaminase; |
7-326 |
3.83e-105 |
|
Adenosine deaminase;
Pssm-ID: 425964 Cd Length: 330 Bit Score: 310.90 E-value: 3.83e-105
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113478613 7 PLIDLHRHLEGNLRLETVLELARKFNVTLPADTVEGLRPYVQVSSRQPGVMAFIEKFNLLMKVLGNEQACFRIAQEAVLD 86
Cdd:pfam00962 1 PKAELHLHLDGSLRPDTLLELAKRYGIILPADFPEALEPLFRKYKKERDLQDFLDKYDIGVAVLRSPEDIRRLAFEYAED 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113478613 87 AANEGIDYLELRFSPVFMAAdHQLNPSAVVEAVLAGIQAAAAESGIQVNPLGIISRTYGPQVAEQELSALLSYADK-IRG 165
Cdd:pfam00962 81 VAKDGVVYAEVRYDPQSHAS-RGLSPDTVVDAVLDAVDAAEREFGITVRLIVCAMRHEHPECSREIAELAPRYRDQgIVA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113478613 166 LDLAGDEANFPAQLFLPH---FKKARDVGWHITVHAGEADGPQSIWDSIRLLGAERIGHGLAARHDAQLLKYLLDHQIGI 242
Cdd:pfam00962 160 FGLAGDEKGFPPSLFRDHveaFARARDAGLHLTVHAGEAGGPQSVWEALDDLGAERIGHGVRSAEDPRLLDRLADRQIPL 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113478613 243 ECNLTSNVQTSSVADYVSHPLKFFLEKRLLASINSDDPGISAIDLPYEYNVAAPKAGLSETQIRQAQLNALESAFLNSQE 322
Cdd:pfam00962 240 EICPTSNVQTGAVASLAEHPLKTFLRAGVPVSLNTDDPLMFGSDLLDEYQVAKRAPGFDEEELARLAKNAVKGSFLPADE 319
|
....
gi 1113478613 323 KLAL 326
Cdd:pfam00962 320 KRAL 323
|
|
| ADA_AMPD |
cd00443 |
Adenosine/AMP deaminase. Adenosine deaminases (ADAs) are present in pro- and eukaryotic ... |
6-323 |
8.53e-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: 173.30 E-value: 8.53e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113478613 6 LPLIDLHRHLEGNLRLETVLELARKfnvtlpadtveglrpyvqvssrqpgvmAFIEKFNLLMKVLGNEQACFRIAQEAVL 85
Cdd:cd00443 1 LPKVELHAHLSGSISPETLLELIKK---------------------------EFFEKFLLVHNLLQKGEALARALKEVIE 53
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113478613 86 DAANEGIDYLELRFSPVFMAADHQLNPSAVVEAVLAGIQAAA-AESGIQVNPLGIISRTYGPQVAEQELSALLSYA---- 160
Cdd:cd00443 54 EFAEDNVQYLELRTTPRLLETEKGLTKEQYWLLVIEGISEAKqWFPPIKVRLILSVDRRGPYVQNYLVASEILELAkfls 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113478613 161 DKIRGLDLAGDEANFPAQL--FLPHFKKARDVGW-HITVHAGEADGPQSIWDSIrLLGAERIGHGLAARHDAQLLKYLLD 237
Cdd:cd00443 134 NYVVGIDLVGDESKGENPLrdFYSYYEYARRLGLlGLTLHCGETGNREELLQAL-LLLPDRIGHGIFLLKHPELIYLVKL 212
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113478613 238 HQIGIECNLTSNVQTSSVADYVSHPLKFFLEKRLLASINSDDPGISAIDLPYEYNVAAPKAGLSETQIRQAQLNALESAF 317
Cdd:cd00443 213 RNIPIEVCPTSNVVLGTVQSYEKHPFMRFFKAGLPVSLSTDDPGIFGTSLSEEYSLAAKTFGLTFEDLCELNRNSVLSSF 292
|
....*.
gi 1113478613 318 LNSQEK 323
Cdd:cd00443 293 AKDEEK 298
|
|
| PTZ00124 |
PTZ00124 |
adenosine deaminase; Provisional |
2-326 |
1.59e-38 |
|
adenosine deaminase; Provisional
Pssm-ID: 173415 Cd Length: 362 Bit Score: 140.39 E-value: 1.59e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113478613 2 IYPDLPLIDLHRHLEGNLRLETVLELARKFNVTlPADTVEGLRPYVQVSSRQPGVMAFIEKFNLLMKVLGNEQACFRIAQ 81
Cdd:PTZ00124 31 IWKRIPKCELHCHLDLCFSVDFFLSCIRKYNLQ-PNLSDEEILDYYLFAKGGKSLGEFVEKAIRVADIFNDYEVIEDLAK 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113478613 82 EAVLDAANEGIDYLELRFSPVFMAADHQLNPSAVVEAVLAGIQAAAA--ESGIQVNPLGIISRTYGPQVAEQELSALLSY 159
Cdd:PTZ00124 110 HAVFNKYKEGVVLMEFRYSPTFVAFKHNLDIDLIHQAIVKGIKEAVEllDHKIEVGLLCIGDTGHDAAPIKESADFCLKH 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113478613 160 ADKIRGLDLAGDEANFPAqlFLPHFKKARDVGWHITVHAGEADGP---QSIWDSIRLLGAERIGHGLAARHDAQLLKYLL 236
Cdd:PTZ00124 190 KADFVGFDHAGHEVDLKP--FKDIFDYVREAGVNLTVHAGEDVTLpnlNTLYSAIQVLKVKRIGHGIRVAESQELIDMVK 267
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113478613 237 DHQIGIECNLTSNVQTSSVADYVSHPLKFFLEKRLLASINSDDPGISAIDLPYEYNVAAPKAGLSETQIRQAQLNALESA 316
Cdd:PTZ00124 268 EKDILLEVCPISNVLLNNAKSMDTHPIRKLYDAGVKVSVNSDDPGMFLTNINDDYEELYTHLNFTLADFMKMNEWALEKS 347
|
330
....*....|
gi 1113478613 317 FLNSQEKLAL 326
Cdd:PTZ00124 348 FLDKDIKLKI 357
|
|
| ADGF |
cd01321 |
Adenosine deaminase-related growth factors (ADGF), a novel family of secreted growth-factors ... |
11-323 |
4.12e-20 |
|
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: 89.64 E-value: 4.12e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113478613 11 LHRHLEGNLRLETVLELA-RKFNVTLpaDTVEGLRPYvqvssrQPGVMAFIekfnllmkvlgneqacFRIAQEAVldaaN 89
Cdd:cd01321 30 LHVHDTAMVSSDWLIKNAtYRFEQIF--DIIDGLLTY------LPIFRDYY----------------RRLLEELY----E 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113478613 90 EGIDYLELR--FSPVFMAADHQLNPSAVVEAVLAGIQAAAAES----GIQVnpLGIISRTYGPQVAEQELSALLS----Y 159
Cdd:cd01321 82 DNVQYVELRssFSPLYDLDGREYDYEETVQLLEEVVEKFKKTHpdfiGLKI--IYATLRNFNDSEIKESMEQCLNlkkkF 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113478613 160 ADKIRGLDLAGDE-ANFPAQLFLPHFKKARDVGWHIT--VHAGEADGP-----QSIWDSIrLLGAERIGHGLA-ARHdAQ 230
Cdd:cd01321 160 PDFIAGFDLVGQEdAGRPLLDFLPQLLWFPKQCAEIPffFHAGETNGDgtetdENLVDAL-LLNTKRIGHGFAlPKH-PL 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113478613 231 LLKYLLDHQIGIECNLTSNVQTSSVADYVSHPLKFFLEKRLLASINSDDPGI-SAIDLPYEYNVA-----APKAGLSetQ 304
Cdd:cd01321 238 LMDLVKKKNIAIEVCPISNQVLGLVSDLRNHPAAALLARGVPVVISSDDPGFwGAKGLSHDFYQAfmglaPADAGLR--G 315
|
330
....*....|....*....
gi 1113478613 305 IRQAQLNALESAFLNSQEK 323
Cdd:cd01321 316 LKQLAENSIRYSALSDQEK 334
|
|
| metallo-dependent_hydrolases |
cd01292 |
Superfamily of metallo-dependent hydrolases (also called amidohydrolase superfamily) is a ... |
52-300 |
1.85e-09 |
|
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: 57.73 E-value: 1.85e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113478613 52 RQPGVMAFIEKFNLLMKVLGNEQACFRIAQEAVLDAANEGIDYLELRFSPVfmaadhqlNPSAVVEAVLAGIQAAAAESG 131
Cdd:cd01292 9 DGSALRGTRLNLELKEAEELSPEDLYEDTLRALEALLAGGVTTVVDMGSTP--------PPTTTKAAIEAVAEAARASAG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113478613 132 IQVNPLGIISRTYGPQVAEQELS----ALLSYADKIRGLDLAGDEANF--PAQLFLPHFKKARDVGWHITVHAGEA-DGP 204
Cdd:cd01292 81 IRVVLGLGIPGVPAAVDEDAEALllelLRRGLELGAVGLKLAGPYTATglSDESLRRVLEEARKLGLPVVIHAGELpDPT 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113478613 205 QSIWDSIRLLGAE---RIGHGlaARHDAQLLKYLLDHQIGIECNLTSNvQTSSVADYVSHPLKFFLEKRLLASINSDDPG 281
Cdd:cd01292 161 RALEDLVALLRLGgrvVIGHV--SHLDPELLELLKEAGVSLEVCPLSN-YLLGRDGEGAEALRRLLELGIRVTLGTDGPP 237
|
250 260
....*....|....*....|
gi 1113478613 282 I-SAIDLPYEYNVAAPKAGL 300
Cdd:cd01292 238 HpLGTDLLALLRLLLKVLRL 257
|
|
| AMPD |
cd01319 |
AMP deaminase (AMPD) catalyzes the hydrolytic deamination of adensosine monophosphate (AMP) at ... |
181-295 |
4.79e-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: 48.13 E-value: 4.79e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113478613 181 LPHFKKARdvGWHITV---HAGEADGPQSIWDSirLLGAERIGHGLAARHDA--QLLKYLldHQIGIECNLTSNvqTSSV 255
Cdd:cd01319 315 LNSFRKAR--GFNTFVlrpHCGEAGDIDHLASA--FLLAHGISHGINLRKVPvlQYLYYL--TQIGIAMSPLSN--NSLF 386
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 1113478613 256 ADYVSHPLKFFLEKRLLASINSDDPGISAID---LPYEYNVAA 295
Cdd:cd01319 387 LSYEKNPFPEFFKRGLNVSLSTDDPLQFHFTkepLMEEYSIAA 429
|
|
| PLN03055 |
PLN03055 |
AMP deaminase; Provisional |
197-317 |
2.59e-03 |
|
AMP deaminase; Provisional
Pssm-ID: 178613 Cd Length: 602 Bit Score: 39.46 E-value: 2.59e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113478613 197 HAGEADGPQSIWDSIRLlgAERIGHGLAARHDA--QLLKYLldHQIGIECNLTSNvqTSSVADYVSHPLKFFLEKRLLAS 274
Cdd:PLN03055 422 HAGEAGDIDHLAAAFLL--AHNIAHGNNLRKSPglQYLYYL--AQIGLAMSPLSN--NSLFLDYHRNPFPMFFARGLNVS 495
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 1113478613 275 INSDDP---GISAIDLPYEYNVAAPKAGLSETQIRQ-AQLNALESAF 317
Cdd:PLN03055 496 LSTDDPlqiHLTKEPLVEEYSIAAQVWKLSSCDLCEiARNSVLQSGF 542
|
|
| |
