|
Name |
Accession |
Description |
Interval |
E-value |
| PRK09358 |
PRK09358 |
adenosine deaminase; Provisional |
1-333 |
9.80e-157 |
|
adenosine deaminase; Provisional
Pssm-ID: 236480 Cd Length: 340 Bit Score: 442.31 E-value: 9.80e-157
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555038087 1 MIDTRLPLTDIHRHLDGNIRAQTILDLGRQFNLTLPAQTLESLIPhVQVTSNEPDLVSFLSKLDWGVKMLASLDACRRVA 80
Cdd:PRK09358 5 MIIRSLPKAELHLHLDGSLRPETILELARRNGIALPATDVEELPW-VRAAYDFRDLQSFLDKYDAGVAVLQTEEDLRRLA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555038087 81 FENIEDAARNGLHYVELRFSPGYMAMtHNLPVAGVVEAVIEGVREGCKTFDVQARLIGIMSRTFGEAACLQELEALLA-- 158
Cdd:PRK09358 84 FEYLEDAAADGVVYAEIRFDPQLHTE-RGLPLEEVVEAVLDGLRAAEAEFGISVRLILCFMRHFGEEAAARELEALAAry 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555038087 159 HRDAITAVDLAGDELGFPGSLFLSHFNRARDAGWHITVHAGEAAGPESIWQAIRELGAERIGHGVKAVEDRALMDFLAEQ 238
Cdd:PRK09358 163 RDDGVVGFDLAGDELGFPPSKFARAFDRARDAGLRLTAHAGEAGGPESIWEALDELGAERIGHGVRAIEDPALMARLADR 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555038087 239 RIGIESCLTSNIQTSTVATLAHHPLKTFLEHGVLASLNTDDPAVQGVDIIHEYNIAAPQAGLSREQIRQAQINGLEIAFL 318
Cdd:PRK09358 243 RIPLEVCPTSNVQTGAVPSLAEHPLKTLLDAGVRVTINTDDPLVFGTTLTEEYEALAEAFGLSDEDLAQLARNALEAAFL 322
|
330
....*....|....*
gi 555038087 319 TPAEKQALRDKVATA 333
Cdd:PRK09358 323 SEEEKAALLAEVDAW 337
|
|
| A_deaminase |
pfam00962 |
Adenosine deaminase; |
7-333 |
3.03e-149 |
|
Adenosine deaminase;
Pssm-ID: 425964 Cd Length: 330 Bit Score: 422.99 E-value: 3.03e-149
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555038087 7 PLTDIHRHLDGNIRAQTILDLGRQFNLTLPAQTLESLIPHVQVTSNEPDLVSFLSKLDWGVKMLASLDACRRVAFENIED 86
Cdd:pfam00962 1 PKAELHLHLDGSLRPDTLLELAKRYGIILPADFPEALEPLFRKYKKERDLQDFLDKYDIGVAVLRSPEDIRRLAFEYAED 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555038087 87 AARNGLHYVELRFSPGYMAMThNLPVAGVVEAVIEGVREGCKTFDVQARLIGIMSRTfGEAACLQELEALLA-HRD-AIT 164
Cdd:pfam00962 81 VAKDGVVYAEVRYDPQSHASR-GLSPDTVVDAVLDAVDAAEREFGITVRLIVCAMRH-EHPECSREIAELAPrYRDqGIV 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555038087 165 AVDLAGDELGFPGSLFLSH---FNRARDAGWHITVHAGEAAGPESIWQAIRELGAERIGHGVKAVEDRALMDFLAEQRIG 241
Cdd:pfam00962 159 AFGLAGDEKGFPPSLFRDHveaFARARDAGLHLTVHAGEAGGPQSVWEALDDLGAERIGHGVRSAEDPRLLDRLADRQIP 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555038087 242 IESCLTSNIQTSTVATLAHHPLKTFLEHGVLASLNTDDPAVQGVDIIHEYNIAAPQAGLSREQIRQAQINGLEIAFLTPA 321
Cdd:pfam00962 239 LEICPTSNVQTGAVASLAEHPLKTFLRAGVPVSLNTDDPLMFGSDLLDEYQVAKRAPGFDEEELARLAKNAVKGSFLPAD 318
|
330
....*....|..
gi 555038087 322 EKQALRDKVATA 333
Cdd:pfam00962 319 EKRALLDEVDKV 330
|
|
| Add |
COG1816 |
Adenosine deaminase [Nucleotide transport and metabolism]; Adenosine deaminase is part of the ... |
7-331 |
1.16e-144 |
|
Adenosine deaminase [Nucleotide transport and metabolism]; Adenosine deaminase is part of the Pathway/BioSystem: Menaquinone biosynthesis
Pssm-ID: 441421 Cd Length: 326 Bit Score: 411.02 E-value: 1.16e-144
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555038087 7 PLTDIHRHLDGNIRAQTILDLGRQFNLTLPAQTLESLIPhvqvTSNEPDLVSFLSKLDWGVKMLASLDACRRVAFENIED 86
Cdd:COG1816 1 PKAELHLHLEGSLRPETLLELAARNGIDLPAADVEELRA----AYDFRDLQSFLDTYDAGAAVLQTEEDFRRLAYEYLED 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555038087 87 AARNGLHYVELRFSPgYMAMTHNLPVAGVVEAVIEGVREGCKTFDVQARLIGIMSRTFGEAACLQELEALLAHRDA-ITA 165
Cdd:COG1816 77 AAADGVRYAEIRFDP-QLHTRRGLSLEEVVEAVLDGLREAEREFGISVRLILCALRHLSPEAAFETLELALRYRDRgVVG 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555038087 166 VDLAGDELGFPGSLFLSHFNRARDAGWHITVHAGEAAGPESIWQAIRELGAERIGHGVKAVEDRALMDFLAEQRIGIESC 245
Cdd:COG1816 156 FGLAGDERGFPPEKFAEAFARAREAGLHLTAHAGEAGGPESIWEALDLLGAERIGHGVRAIEDPALVARLADRGIPLEVC 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555038087 246 LTSNIQTSTVATLAHHPLKTFLEHGVLASLNTDDPAVQGVDIIHEYNIAAPQAGLSREQIRQAQINGLEIAFLTPAEKQA 325
Cdd:COG1816 236 PTSNVQLGVVPSLAEHPLRRLLDAGVRVTLNTDDPLYFGTTLTDEYELAAEAFGLSDADLAQLARNAIEASFLPEEEKAA 315
|
....*.
gi 555038087 326 LRDKVA 331
Cdd:COG1816 316 LLAELD 321
|
|
| ADA |
cd01320 |
Adenosine deaminase (ADA) is a monomeric zinc dependent enzyme which catalyzes the ... |
5-330 |
1.60e-136 |
|
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: 390.41 E-value: 1.60e-136
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555038087 5 RLPLTDIHRHLDGNIRAQTILDLGRQFNLTLPAQTLEsLIPHVQVTSNEPDLVSFLSKLDWGVKMLASLDACRRVAFENI 84
Cdd:cd01320 1 NLPKAELHLHLDGSLRPETILELAKKNGITLPASDVE-LLELVVAAYNFSDLQDFLAKYDFGLSVLQTEEDFERLAYEYL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555038087 85 EDAARNGLHYVELRFSPGYMaMTHNLPVAGVVEAVIEGVREGCKTFDVQARLIGIMSRTFGEAACLQELEALLAHRDA-I 163
Cdd:cd01320 80 EDAAADGVVYAEIRFSPQLH-TRRGLSFDEVVEAVLRGLDEAEAEFGIKARLILCGLRHLSPESAQETLELALKYRDKgV 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555038087 164 TAVDLAGDELGFPGSLFLSHFNRARDAGWHITVHAGEAAGPESIWQAIRELGAERIGHGVKAVEDRALMDFLAEQRIGIE 243
Cdd:cd01320 159 VGFDLAGDEVGFPPEKFVRAFQRAREAGLRLTAHAGEAGGPESVRDALDLLGAERIGHGIRAIEDPELVKRLAERNIPLE 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555038087 244 SCLTSNIQTSTVATLAHHPLKTFLEHGVLASLNTDDPAVQGVDIIHEYNIAAPQAGLSREQIRQAQINGLEIAFLTPAEK 323
Cdd:cd01320 239 VCPTSNVQTGAVKSLAEHPLRELLDAGVKVTINTDDPTVFGTYLTDEYELLAEAFGLTEEELKKLARNAVEASFLSEEEK 318
|
....*..
gi 555038087 324 QALRDKV 330
Cdd:cd01320 319 AELLKRI 325
|
|
| aden_deam |
TIGR01430 |
adenosine deaminase; This family includes the experimentally verified adenosine deaminases of ... |
6-330 |
2.54e-125 |
|
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: 362.06 E-value: 2.54e-125
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555038087 6 LPLTDIHRHLDGNIRAQTILDLGRQFNLTLPaQTLESLIPHVQVTSNEPDLVSFLSKLDWGVKMLASLDACRRVAFENIE 85
Cdd:TIGR01430 1 LPKAELHLHLEGSIRPETLLELAQKNGIPLP-ADLQSGEELKEAYDKFRDLQDFLAKYDFGVEVLRTEDDFKRLAYEYVE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555038087 86 DAARNGLHYVELRFSPGYMAMTHNLPVaGVVEAVIEGVREGCKTFDVQARLIGIMSRTFGEAACLQELEALLAHRD-AIT 164
Cdd:TIGR01430 80 KAAKDGVVYAEVFFDPQLHTNRGISPD-TVVEAVLDGLDEAERDFGIKSRLILCGMRHKQPEAAEETLELAKPYKEqTIV 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555038087 165 AVDLAGDELGFPGSLFLSHFNRARDAGWHITVHAGEAAGPESIWQAIRELGAERIGHGVKAVEDRALMDFLAEQRIGIES 244
Cdd:TIGR01430 159 GFGLAGDERGGPPPDFVRAFAIARELGLHLTVHAGELGGPESVREALDDLGATRIGHGVRALEDPELLKRLAQENITLEV 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555038087 245 CLTSNIQTSTVATLAHHPLKTFLEHGVLASLNTDDPAVQGVDIIHEYNIAAPQAGLSREQIRQAQINGLEIAFLTPAEKQ 324
Cdd:TIGR01430 239 CPTSNVALGVVKSLAEHPLRRFLEAGVKVTLNSDDPAYFGSYLTEEYEIAAKHAGLTEEELKQLARNALEGSFLSDDEKK 318
|
....*.
gi 555038087 325 ALRDKV 330
Cdd:TIGR01430 319 ELLAKL 324
|
|
|
|
Name |
Accession |
Description |
Interval |
E-value |
| PRK09358 |
PRK09358 |
adenosine deaminase; Provisional |
1-333 |
9.80e-157 |
|
adenosine deaminase; Provisional
Pssm-ID: 236480 Cd Length: 340 Bit Score: 442.31 E-value: 9.80e-157
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555038087 1 MIDTRLPLTDIHRHLDGNIRAQTILDLGRQFNLTLPAQTLESLIPhVQVTSNEPDLVSFLSKLDWGVKMLASLDACRRVA 80
Cdd:PRK09358 5 MIIRSLPKAELHLHLDGSLRPETILELARRNGIALPATDVEELPW-VRAAYDFRDLQSFLDKYDAGVAVLQTEEDLRRLA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555038087 81 FENIEDAARNGLHYVELRFSPGYMAMtHNLPVAGVVEAVIEGVREGCKTFDVQARLIGIMSRTFGEAACLQELEALLA-- 158
Cdd:PRK09358 84 FEYLEDAAADGVVYAEIRFDPQLHTE-RGLPLEEVVEAVLDGLRAAEAEFGISVRLILCFMRHFGEEAAARELEALAAry 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555038087 159 HRDAITAVDLAGDELGFPGSLFLSHFNRARDAGWHITVHAGEAAGPESIWQAIRELGAERIGHGVKAVEDRALMDFLAEQ 238
Cdd:PRK09358 163 RDDGVVGFDLAGDELGFPPSKFARAFDRARDAGLRLTAHAGEAGGPESIWEALDELGAERIGHGVRAIEDPALMARLADR 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555038087 239 RIGIESCLTSNIQTSTVATLAHHPLKTFLEHGVLASLNTDDPAVQGVDIIHEYNIAAPQAGLSREQIRQAQINGLEIAFL 318
Cdd:PRK09358 243 RIPLEVCPTSNVQTGAVPSLAEHPLKTLLDAGVRVTINTDDPLVFGTTLTEEYEALAEAFGLSDEDLAQLARNALEAAFL 322
|
330
....*....|....*
gi 555038087 319 TPAEKQALRDKVATA 333
Cdd:PRK09358 323 SEEEKAALLAEVDAW 337
|
|
| A_deaminase |
pfam00962 |
Adenosine deaminase; |
7-333 |
3.03e-149 |
|
Adenosine deaminase;
Pssm-ID: 425964 Cd Length: 330 Bit Score: 422.99 E-value: 3.03e-149
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555038087 7 PLTDIHRHLDGNIRAQTILDLGRQFNLTLPAQTLESLIPHVQVTSNEPDLVSFLSKLDWGVKMLASLDACRRVAFENIED 86
Cdd:pfam00962 1 PKAELHLHLDGSLRPDTLLELAKRYGIILPADFPEALEPLFRKYKKERDLQDFLDKYDIGVAVLRSPEDIRRLAFEYAED 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555038087 87 AARNGLHYVELRFSPGYMAMThNLPVAGVVEAVIEGVREGCKTFDVQARLIGIMSRTfGEAACLQELEALLA-HRD-AIT 164
Cdd:pfam00962 81 VAKDGVVYAEVRYDPQSHASR-GLSPDTVVDAVLDAVDAAEREFGITVRLIVCAMRH-EHPECSREIAELAPrYRDqGIV 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555038087 165 AVDLAGDELGFPGSLFLSH---FNRARDAGWHITVHAGEAAGPESIWQAIRELGAERIGHGVKAVEDRALMDFLAEQRIG 241
Cdd:pfam00962 159 AFGLAGDEKGFPPSLFRDHveaFARARDAGLHLTVHAGEAGGPQSVWEALDDLGAERIGHGVRSAEDPRLLDRLADRQIP 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555038087 242 IESCLTSNIQTSTVATLAHHPLKTFLEHGVLASLNTDDPAVQGVDIIHEYNIAAPQAGLSREQIRQAQINGLEIAFLTPA 321
Cdd:pfam00962 239 LEICPTSNVQTGAVASLAEHPLKTFLRAGVPVSLNTDDPLMFGSDLLDEYQVAKRAPGFDEEELARLAKNAVKGSFLPAD 318
|
330
....*....|..
gi 555038087 322 EKQALRDKVATA 333
Cdd:pfam00962 319 EKRALLDEVDKV 330
|
|
| Add |
COG1816 |
Adenosine deaminase [Nucleotide transport and metabolism]; Adenosine deaminase is part of the ... |
7-331 |
1.16e-144 |
|
Adenosine deaminase [Nucleotide transport and metabolism]; Adenosine deaminase is part of the Pathway/BioSystem: Menaquinone biosynthesis
Pssm-ID: 441421 Cd Length: 326 Bit Score: 411.02 E-value: 1.16e-144
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555038087 7 PLTDIHRHLDGNIRAQTILDLGRQFNLTLPAQTLESLIPhvqvTSNEPDLVSFLSKLDWGVKMLASLDACRRVAFENIED 86
Cdd:COG1816 1 PKAELHLHLEGSLRPETLLELAARNGIDLPAADVEELRA----AYDFRDLQSFLDTYDAGAAVLQTEEDFRRLAYEYLED 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555038087 87 AARNGLHYVELRFSPgYMAMTHNLPVAGVVEAVIEGVREGCKTFDVQARLIGIMSRTFGEAACLQELEALLAHRDA-ITA 165
Cdd:COG1816 77 AAADGVRYAEIRFDP-QLHTRRGLSLEEVVEAVLDGLREAEREFGISVRLILCALRHLSPEAAFETLELALRYRDRgVVG 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555038087 166 VDLAGDELGFPGSLFLSHFNRARDAGWHITVHAGEAAGPESIWQAIRELGAERIGHGVKAVEDRALMDFLAEQRIGIESC 245
Cdd:COG1816 156 FGLAGDERGFPPEKFAEAFARAREAGLHLTAHAGEAGGPESIWEALDLLGAERIGHGVRAIEDPALVARLADRGIPLEVC 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555038087 246 LTSNIQTSTVATLAHHPLKTFLEHGVLASLNTDDPAVQGVDIIHEYNIAAPQAGLSREQIRQAQINGLEIAFLTPAEKQA 325
Cdd:COG1816 236 PTSNVQLGVVPSLAEHPLRRLLDAGVRVTLNTDDPLYFGTTLTDEYELAAEAFGLSDADLAQLARNAIEASFLPEEEKAA 315
|
....*.
gi 555038087 326 LRDKVA 331
Cdd:COG1816 316 LLAELD 321
|
|
| ADA |
cd01320 |
Adenosine deaminase (ADA) is a monomeric zinc dependent enzyme which catalyzes the ... |
5-330 |
1.60e-136 |
|
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: 390.41 E-value: 1.60e-136
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555038087 5 RLPLTDIHRHLDGNIRAQTILDLGRQFNLTLPAQTLEsLIPHVQVTSNEPDLVSFLSKLDWGVKMLASLDACRRVAFENI 84
Cdd:cd01320 1 NLPKAELHLHLDGSLRPETILELAKKNGITLPASDVE-LLELVVAAYNFSDLQDFLAKYDFGLSVLQTEEDFERLAYEYL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555038087 85 EDAARNGLHYVELRFSPGYMaMTHNLPVAGVVEAVIEGVREGCKTFDVQARLIGIMSRTFGEAACLQELEALLAHRDA-I 163
Cdd:cd01320 80 EDAAADGVVYAEIRFSPQLH-TRRGLSFDEVVEAVLRGLDEAEAEFGIKARLILCGLRHLSPESAQETLELALKYRDKgV 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555038087 164 TAVDLAGDELGFPGSLFLSHFNRARDAGWHITVHAGEAAGPESIWQAIRELGAERIGHGVKAVEDRALMDFLAEQRIGIE 243
Cdd:cd01320 159 VGFDLAGDEVGFPPEKFVRAFQRAREAGLRLTAHAGEAGGPESVRDALDLLGAERIGHGIRAIEDPELVKRLAERNIPLE 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555038087 244 SCLTSNIQTSTVATLAHHPLKTFLEHGVLASLNTDDPAVQGVDIIHEYNIAAPQAGLSREQIRQAQINGLEIAFLTPAEK 323
Cdd:cd01320 239 VCPTSNVQTGAVKSLAEHPLRELLDAGVKVTINTDDPTVFGTYLTDEYELLAEAFGLTEEELKKLARNAVEASFLSEEEK 318
|
....*..
gi 555038087 324 QALRDKV 330
Cdd:cd01320 319 AELLKRI 325
|
|
| aden_deam |
TIGR01430 |
adenosine deaminase; This family includes the experimentally verified adenosine deaminases of ... |
6-330 |
2.54e-125 |
|
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: 362.06 E-value: 2.54e-125
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555038087 6 LPLTDIHRHLDGNIRAQTILDLGRQFNLTLPaQTLESLIPHVQVTSNEPDLVSFLSKLDWGVKMLASLDACRRVAFENIE 85
Cdd:TIGR01430 1 LPKAELHLHLEGSIRPETLLELAQKNGIPLP-ADLQSGEELKEAYDKFRDLQDFLAKYDFGVEVLRTEDDFKRLAYEYVE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555038087 86 DAARNGLHYVELRFSPGYMAMTHNLPVaGVVEAVIEGVREGCKTFDVQARLIGIMSRTFGEAACLQELEALLAHRD-AIT 164
Cdd:TIGR01430 80 KAAKDGVVYAEVFFDPQLHTNRGISPD-TVVEAVLDGLDEAERDFGIKSRLILCGMRHKQPEAAEETLELAKPYKEqTIV 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555038087 165 AVDLAGDELGFPGSLFLSHFNRARDAGWHITVHAGEAAGPESIWQAIRELGAERIGHGVKAVEDRALMDFLAEQRIGIES 244
Cdd:TIGR01430 159 GFGLAGDERGGPPPDFVRAFAIARELGLHLTVHAGELGGPESVREALDDLGATRIGHGVRALEDPELLKRLAQENITLEV 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555038087 245 CLTSNIQTSTVATLAHHPLKTFLEHGVLASLNTDDPAVQGVDIIHEYNIAAPQAGLSREQIRQAQINGLEIAFLTPAEKQ 324
Cdd:TIGR01430 239 CPTSNVALGVVKSLAEHPLRRFLEAGVKVTLNSDDPAYFGSYLTEEYEIAAKHAGLTEEELKQLARNALEGSFLSDDEKK 318
|
....*.
gi 555038087 325 ALRDKV 330
Cdd:TIGR01430 319 ELLAKL 324
|
|
| ADA_AMPD |
cd00443 |
Adenosine/AMP deaminase. Adenosine deaminases (ADAs) are present in pro- and eukaryotic ... |
6-329 |
1.91e-45 |
|
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: 156.74 E-value: 1.91e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555038087 6 LPLTDIHRHLDGNIRAQTILDLG-RQFnltlpAQTLESLIPHVQvtsNEPDLvsflskldwgvkmlasldacRRVAFENI 84
Cdd:cd00443 1 LPKVELHAHLSGSISPETLLELIkKEF-----FEKFLLVHNLLQ---KGEAL--------------------ARALKEVI 52
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555038087 85 EDAARNGLHYVELRFSPGYMAMTHNLPVAGVVEAVIEGVREGCKTF-DVQARLIGIMSRT------FGEAACLQELEALL 157
Cdd:cd00443 53 EEFAEDNVQYLELRTTPRLLETEKGLTKEQYWLLVIEGISEAKQWFpPIKVRLILSVDRRgpyvqnYLVASEILELAKFL 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555038087 158 ahRDAITAVDLAGDELGFPGSL--FLSHFNRARDAGW-HITVHAGEAAGPESIWQAIrELGAERIGHGVKAVEDRALMDF 234
Cdd:cd00443 133 --SNYVVGIDLVGDESKGENPLrdFYSYYEYARRLGLlGLTLHCGETGNREELLQAL-LLLPDRIGHGIFLLKHPELIYL 209
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555038087 235 LAEQRIGIESCLTSNIQTSTVATLAHHPLKTFLEHGVLASLNTDDPAVQGVDIIHEYNIAAPQAGLSREQIRQAQINGLE 314
Cdd:cd00443 210 VKLRNIPIEVCPTSNVVLGTVQSYEKHPFMRFFKAGLPVSLSTDDPGIFGTSLSEEYSLAAKTFGLTFEDLCELNRNSVL 289
|
330
....*....|....*
gi 555038087 315 IAFLTPAEKQALRDK 329
Cdd:cd00443 290 SSFAKDEEKKSLLEV 304
|
|
| PTZ00124 |
PTZ00124 |
adenosine deaminase; Provisional |
5-329 |
1.16e-40 |
|
adenosine deaminase; Provisional
Pssm-ID: 173415 Cd Length: 362 Bit Score: 145.78 E-value: 1.16e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555038087 5 RLPLTDIHRHLDGNIRAQTILDLGRQFNLTlPAQTLESLIPHVQVTSNEPDLVSFLSKLDWGVKMLASLDACRRVAFENI 84
Cdd:PTZ00124 34 RIPKCELHCHLDLCFSVDFFLSCIRKYNLQ-PNLSDEEILDYYLFAKGGKSLGEFVEKAIRVADIFNDYEVIEDLAKHAV 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555038087 85 EDAARNGLHYVELRFSPGYMAMTHNLPVAGVVEAVIEGVREGCKTFD--VQARLIGIMSRTFGEAACLQELEALLAHRDA 162
Cdd:PTZ00124 113 FNKYKEGVVLMEFRYSPTFVAFKHNLDIDLIHQAIVKGIKEAVELLDhkIEVGLLCIGDTGHDAAPIKESADFCLKHKAD 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555038087 163 ITAVDLAGDELGFpgSLFLSHFNRARDAGWHITVHAGEAAGP---ESIWQAIRELGAERIGHGVKAVEDRALMDFLAEQR 239
Cdd:PTZ00124 193 FVGFDHAGHEVDL--KPFKDIFDYVREAGVNLTVHAGEDVTLpnlNTLYSAIQVLKVKRIGHGIRVAESQELIDMVKEKD 270
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555038087 240 IGIESCLTSNIQTSTVATLAHHPLKTFLEHGVLASLNTDDPAVQGVDIIHEYNIAAPQAGLSREQIRQAQINGLEIAFLT 319
Cdd:PTZ00124 271 ILLEVCPISNVLLNNAKSMDTHPIRKLYDAGVKVSVNSDDPGMFLTNINDDYEELYTHLNFTLADFMKMNEWALEKSFLD 350
|
330
....*....|
gi 555038087 320 PAEKQALRDK 329
Cdd:PTZ00124 351 KDIKLKIKKL 360
|
|
| ADGF |
cd01321 |
Adenosine deaminase-related growth factors (ADGF), a novel family of secreted growth-factors ... |
69-329 |
8.04e-17 |
|
Adenosine deaminase-related growth factors (ADGF), a novel family of secreted growth-factors with sequence similarty to adenosine deaminase.
Pssm-ID: 238646 Cd Length: 345 Bit Score: 80.01 E-value: 8.04e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555038087 69 MLASLDACRRVAFENIEDAARNGLHYVELR--FSPGYMAMTHNLPVAGVVEAVIEGVREGCKTFD--VQARLIGIMSRTF 144
Cdd:cd01321 61 LLTYLPIFRDYYRRLLEELYEDNVQYVELRssFSPLYDLDGREYDYEETVQLLEEVVEKFKKTHPdfIGLKIIYATLRNF 140
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555038087 145 GEAACLQELE-ALLAHR---DAITAVDLAGDE-LGFPGSLFLSHFNRARDAGWHIT--VHAGEAAGPES-----IWQAIR 212
Cdd:cd01321 141 NDSEIKESMEqCLNLKKkfpDFIAGFDLVGQEdAGRPLLDFLPQLLWFPKQCAEIPffFHAGETNGDGTetdenLVDALL 220
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555038087 213 eLGAERIGHGVKAVEDRALMDFLAEQRIGIESCLTSNIQTSTVATLAHHPLKTFLEHGVLASLNTDDPAVQGVD-IIHEY 291
Cdd:cd01321 221 -LNTKRIGHGFALPKHPLLMDLVKKKNIAIEVCPISNQVLGLVSDLRNHPAAALLARGVPVVISSDDPGFWGAKgLSHDF 299
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 555038087 292 -----NIAAPQAGLSreQIRQAQINGLEIAFLTPAEKQALRDK 329
Cdd:cd01321 300 yqafmGLAPADAGLR--GLKQLAENSIRYSALSDQEKDEAVAK 340
|
|
| metallo-dependent_hydrolases |
cd01292 |
Superfamily of metallo-dependent hydrolases (also called amidohydrolase superfamily) is a ... |
46-284 |
3.06e-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: 45.02 E-value: 3.06e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555038087 46 HVQVTSNEPDLVSFLSKLDWGVKMLASLDACRRVafenIEDAARNGLHYVELRFSPGYMAMT--HNLPVAGVVEAvIEGV 123
Cdd:cd01292 7 HLDGSALRGTRLNLELKEAEELSPEDLYEDTLRA----LEALLAGGVTTVVDMGSTPPPTTTkaAIEAVAEAARA-SAGI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555038087 124 REGCKTFDVQARLIGIMSRTFGEAAclqelEALLAHRDAITAVDLAGDE--LGFPGSLFLSHFNRARDAGWHITVHAGEA 201
Cdd:cd01292 82 RVVLGLGIPGVPAAVDEDAEALLLE-----LLRRGLELGAVGLKLAGPYtaTGLSDESLRRVLEEARKLGLPVVIHAGEL 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555038087 202 AGPESIW----QAIRELGAERIGHGVKAVEDraLMDFLAEQRIGIESCLTSNIQTSTVATLAHhPLKTFLEHGVLASLNT 277
Cdd:cd01292 157 PDPTRALedlvALLRLGGRVVIGHVSHLDPE--LLELLKEAGVSLEVCPLSNYLLGRDGEGAE-ALRRLLELGIRVTLGT 233
|
....*..
gi 555038087 278 DDPAVQG 284
Cdd:cd01292 234 DGPPHPL 240
|
|
| AMPD |
cd01319 |
AMP deaminase (AMPD) catalyzes the hydrolytic deamination of adensosine monophosphate (AMP) at ... |
181-295 |
5.96e-05 |
|
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: 44.67 E-value: 5.96e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555038087 181 LSHFNRARdaGWHITV---HAGEAAGPESIWQAIreLGAERIGHGVkAVEDRALMDFL--AEQrIGIE-SCLTSNiqtST 254
Cdd:cd01319 315 LNSFRKAR--GFNTFVlrpHCGEAGDIDHLASAF--LLAHGISHGI-NLRKVPVLQYLyyLTQ-IGIAmSPLSNN---SL 385
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 555038087 255 VATLAHHPLKTFLEHGVLASLNTDDP---AVQGVDIIHEYNIAA 295
Cdd:cd01319 386 FLSYEKNPFPEFFKRGLNVSLSTDDPlqfHFTKEPLMEEYSIAA 429
|
|
| AMP_deaminase |
pfam19326 |
AMP deaminase; |
181-295 |
7.15e-04 |
|
AMP deaminase;
Pssm-ID: 437158 [Multi-domain] Cd Length: 622 Bit Score: 41.29 E-value: 7.15e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555038087 181 LSHFNRARdaGWHITV---HAGEAAGPESIWQAIreLGAERIGHGV--KAVEDRALMDFLAEqrIGIE-SCLTSNiqtST 254
Cdd:pfam19326 432 LNSLRKER--GFNTFVlrpHCGEAGDIDHLVSAF--LLAHGISHGIllRKSPVLQYLYYLAQ--IGIAmSPLSNN---SL 502
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 555038087 255 VATLAHHPLKTFLEHGVLASLNTDDP---AVQGVDIIHEYNIAA 295
Cdd:pfam19326 503 FLEYHKNPFPEFFKRGLNVSLSTDDPlqfHFTKEPLMEEYSIAA 546
|
|
|