|
Name |
Accession |
Description |
Interval |
E-value |
| PRK09358 |
PRK09358 |
adenosine deaminase; Provisional |
1-333 |
8.05e-151 |
|
adenosine deaminase; Provisional
Pssm-ID: 236480 Cd Length: 340 Bit Score: 427.29 E-value: 8.05e-151
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333956788 1 MIDTRLPLTDLHRHLDGNIRAQTILDLGRQFNLALPADTLETLRPhVQITKNEPDLVSFLAKLDWGVKVLGSLEACRRVA 80
Cdd:PRK09358 5 MIIRSLPKAELHLHLDGSLRPETILELARRNGIALPATDVEELPW-VRAAYDFRDLQSFLDKYDAGVAVLQTEEDLRRLA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333956788 81 YENMEDAARNGLHYVELRFSPGYMAMtHNLPIAGVVEAVIDGVRQGSRDYGVDARLIGILSRTFGEEACVAELDGLLA-- 158
Cdd:PRK09358 84 FEYLEDAAADGVVYAEIRFDPQLHTE-RGLPLEEVVEAVLDGLRAAEAEFGISVRLILCFMRHFGEEAAARELEALAAry 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333956788 159 HRDHITALDLAGDELGFPGSLFLNHFNRGRDAGWHITVHAGEAAGPESIWQAIRELGAERIGHGVKAVEDPALMDFLAEQ 238
Cdd:PRK09358 163 RDDGVVGFDLAGDELGFPPSKFARAFDRARDAGLRLTAHAGEAGGPESIWEALDELGAERIGHGVRAIEDPALMARLADR 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333956788 239 GIGIESCLTSNIQTSTVASLAHHPLKTFLEHNILATINTDDPGVQGVDIRHEYEVAAPAAGLSAAQIRTAQENGLKIAFL 318
Cdd:PRK09358 243 RIPLEVCPTSNVQTGAVPSLAEHPLKTLLDAGVRVTINTDDPLVFGTTLTEEYEALAEAFGLSDEDLAQLARNALEAAFL 322
|
330
....*....|....*
gi 333956788 319 TDAEKQALVAKVSAA 333
Cdd:PRK09358 323 SEEEKAALLAEVDAW 337
|
|
| Add |
COG1816 |
Adenosine deaminase [Nucleotide transport and metabolism]; Adenosine deaminase is part of the ... |
7-333 |
6.90e-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: 409.09 E-value: 6.90e-144
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333956788 7 PLTDLHRHLDGNIRAQTILDLGRQFNLALPADTLETLRPhvqiTKNEPDLVSFLAKLDWGVKVLGSLEACRRVAYENMED 86
Cdd:COG1816 1 PKAELHLHLEGSLRPETLLELAARNGIDLPAADVEELRA----AYDFRDLQSFLDTYDAGAAVLQTEEDFRRLAYEYLED 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333956788 87 AARNGLHYVELRFSPgYMAMTHNLPIAGVVEAVIDGVRQGSRDYGVDARLIGILSRTFGEEACVAELDGLLAHRDH-ITA 165
Cdd:COG1816 77 AAADGVRYAEIRFDP-QLHTRRGLSLEEVVEAVLDGLREAEREFGISVRLILCALRHLSPEAAFETLELALRYRDRgVVG 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333956788 166 LDLAGDELGFPGSLFLNHFNRGRDAGWHITVHAGEAAGPESIWQAIRELGAERIGHGVKAVEDPALMDFLAEQGIGIESC 245
Cdd:COG1816 156 FGLAGDERGFPPEKFAEAFARAREAGLHLTAHAGEAGGPESIWEALDLLGAERIGHGVRAIEDPALVARLADRGIPLEVC 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333956788 246 LTSNIQTSTVASLAHHPLKTFLEHNILATINTDDPGVQGVDIRHEYEVAAPAAGLSAAQIRTAQENGLKIAFLTDAEKQA 325
Cdd:COG1816 236 PTSNVQLGVVPSLAEHPLRRLLDAGVRVTLNTDDPLYFGTTLTDEYELAAEAFGLSDADLAQLARNAIEASFLPEEEKAA 315
|
....*...
gi 333956788 326 LVAKVSAA 333
Cdd:COG1816 316 LLAELDAY 323
|
|
| A_deaminase |
pfam00962 |
Adenosine deaminase; |
7-333 |
4.34e-136 |
|
Adenosine deaminase;
Pssm-ID: 425964 Cd Length: 330 Bit Score: 389.48 E-value: 4.34e-136
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333956788 7 PLTDLHRHLDGNIRAQTILDLGRQFNLALPADTLETLRPHVQITKNEPDLVSFLAKLDWGVKVLGSLEACRRVAYENMED 86
Cdd:pfam00962 1 PKAELHLHLDGSLRPDTLLELAKRYGIILPADFPEALEPLFRKYKKERDLQDFLDKYDIGVAVLRSPEDIRRLAFEYAED 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333956788 87 AARNGLHYVELRFSPGYMAMThNLPIAGVVEAVIDGVRQGSRDYGVDARLIGILSRTfGEEACVAELDGLLA-HRDH-IT 164
Cdd:pfam00962 81 VAKDGVVYAEVRYDPQSHASR-GLSPDTVVDAVLDAVDAAEREFGITVRLIVCAMRH-EHPECSREIAELAPrYRDQgIV 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333956788 165 ALDLAGDELGFPGSLFLNH---FNRGRDAGWHITVHAGEAAGPESIWQAIRELGAERIGHGVKAVEDPALMDFLAEQGIG 241
Cdd:pfam00962 159 AFGLAGDEKGFPPSLFRDHveaFARARDAGLHLTVHAGEAGGPQSVWEALDDLGAERIGHGVRSAEDPRLLDRLADRQIP 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333956788 242 IESCLTSNIQTSTVASLAHHPLKTFLEHNILATINTDDPGVQGVDIRHEYEVAAPAAGLSAAQIRTAQENGLKIAFLTDA 321
Cdd:pfam00962 239 LEICPTSNVQTGAVASLAEHPLKTFLRAGVPVSLNTDDPLMFGSDLLDEYQVAKRAPGFDEEELARLAKNAVKGSFLPAD 318
|
330
....*....|..
gi 333956788 322 EKQALVAKVSAA 333
Cdd:pfam00962 319 EKRALLDEVDKV 330
|
|
| ADA |
cd01320 |
Adenosine deaminase (ADA) is a monomeric zinc dependent enzyme which catalyzes the ... |
5-330 |
3.65e-129 |
|
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: 371.54 E-value: 3.65e-129
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333956788 5 RLPLTDLHRHLDGNIRAQTILDLGRQFNLALPADTLEtLRPHVQITKNEPDLVSFLAKLDWGVKVLGSLEACRRVAYENM 84
Cdd:cd01320 1 NLPKAELHLHLDGSLRPETILELAKKNGITLPASDVE-LLELVVAAYNFSDLQDFLAKYDFGLSVLQTEEDFERLAYEYL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333956788 85 EDAARNGLHYVELRFSPGYMaMTHNLPIAGVVEAVIDGVRQGSRDYGVDARLIGILSRTFGEEACVAELDGLLAHRD-HI 163
Cdd:cd01320 80 EDAAADGVVYAEIRFSPQLH-TRRGLSFDEVVEAVLRGLDEAEAEFGIKARLILCGLRHLSPESAQETLELALKYRDkGV 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333956788 164 TALDLAGDELGFPGSLFLNHFNRGRDAGWHITVHAGEAAGPESIWQAIRELGAERIGHGVKAVEDPALMDFLAEQGIGIE 243
Cdd:cd01320 159 VGFDLAGDEVGFPPEKFVRAFQRAREAGLRLTAHAGEAGGPESVRDALDLLGAERIGHGIRAIEDPELVKRLAERNIPLE 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333956788 244 SCLTSNIQTSTVASLAHHPLKTFLEHNILATINTDDPGVQGVDIRHEYEVAAPAAGLSAAQIRTAQENGLKIAFLTDAEK 323
Cdd:cd01320 239 VCPTSNVQTGAVKSLAEHPLRELLDAGVKVTINTDDPTVFGTYLTDEYELLAEAFGLTEEELKKLARNAVEASFLSEEEK 318
|
....*..
gi 333956788 324 QALVAKV 330
Cdd:cd01320 319 AELLKRI 325
|
|
| aden_deam |
TIGR01430 |
adenosine deaminase; This family includes the experimentally verified adenosine deaminases of ... |
6-330 |
3.81e-121 |
|
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: 351.27 E-value: 3.81e-121
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333956788 6 LPLTDLHRHLDGNIRAQTILDLGRQFNLALPADtLETLRPHVQITKNEPDLVSFLAKLDWGVKVLGSLEACRRVAYENME 85
Cdd:TIGR01430 1 LPKAELHLHLEGSIRPETLLELAQKNGIPLPAD-LQSGEELKEAYDKFRDLQDFLAKYDFGVEVLRTEDDFKRLAYEYVE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333956788 86 DAARNGLHYVELRFSPGYMAMTHNLPIaGVVEAVIDGVRQGSRDYGVDARLIGILSRTFGEEACVAELDGLLAHRDH-IT 164
Cdd:TIGR01430 80 KAAKDGVVYAEVFFDPQLHTNRGISPD-TVVEAVLDGLDEAERDFGIKSRLILCGMRHKQPEAAEETLELAKPYKEQtIV 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333956788 165 ALDLAGDELGFPGSLFLNHFNRGRDAGWHITVHAGEAAGPESIWQAIRELGAERIGHGVKAVEDPALMDFLAEQGIGIES 244
Cdd:TIGR01430 159 GFGLAGDERGGPPPDFVRAFAIARELGLHLTVHAGELGGPESVREALDDLGATRIGHGVRALEDPELLKRLAQENITLEV 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333956788 245 CLTSNIQTSTVASLAHHPLKTFLEHNILATINTDDPGVQGVDIRHEYEVAAPAAGLSAAQIRTAQENGLKIAFLTDAEKQ 324
Cdd:TIGR01430 239 CPTSNVALGVVKSLAEHPLRRFLEAGVKVTLNSDDPAYFGSYLTEEYEIAAKHAGLTEEELKQLARNALEGSFLSDDEKK 318
|
....*.
gi 333956788 325 ALVAKV 330
Cdd:TIGR01430 319 ELLAKL 324
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| PRK09358 |
PRK09358 |
adenosine deaminase; Provisional |
1-333 |
8.05e-151 |
|
adenosine deaminase; Provisional
Pssm-ID: 236480 Cd Length: 340 Bit Score: 427.29 E-value: 8.05e-151
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333956788 1 MIDTRLPLTDLHRHLDGNIRAQTILDLGRQFNLALPADTLETLRPhVQITKNEPDLVSFLAKLDWGVKVLGSLEACRRVA 80
Cdd:PRK09358 5 MIIRSLPKAELHLHLDGSLRPETILELARRNGIALPATDVEELPW-VRAAYDFRDLQSFLDKYDAGVAVLQTEEDLRRLA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333956788 81 YENMEDAARNGLHYVELRFSPGYMAMtHNLPIAGVVEAVIDGVRQGSRDYGVDARLIGILSRTFGEEACVAELDGLLA-- 158
Cdd:PRK09358 84 FEYLEDAAADGVVYAEIRFDPQLHTE-RGLPLEEVVEAVLDGLRAAEAEFGISVRLILCFMRHFGEEAAARELEALAAry 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333956788 159 HRDHITALDLAGDELGFPGSLFLNHFNRGRDAGWHITVHAGEAAGPESIWQAIRELGAERIGHGVKAVEDPALMDFLAEQ 238
Cdd:PRK09358 163 RDDGVVGFDLAGDELGFPPSKFARAFDRARDAGLRLTAHAGEAGGPESIWEALDELGAERIGHGVRAIEDPALMARLADR 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333956788 239 GIGIESCLTSNIQTSTVASLAHHPLKTFLEHNILATINTDDPGVQGVDIRHEYEVAAPAAGLSAAQIRTAQENGLKIAFL 318
Cdd:PRK09358 243 RIPLEVCPTSNVQTGAVPSLAEHPLKTLLDAGVRVTINTDDPLVFGTTLTEEYEALAEAFGLSDEDLAQLARNALEAAFL 322
|
330
....*....|....*
gi 333956788 319 TDAEKQALVAKVSAA 333
Cdd:PRK09358 323 SEEEKAALLAEVDAW 337
|
|
| Add |
COG1816 |
Adenosine deaminase [Nucleotide transport and metabolism]; Adenosine deaminase is part of the ... |
7-333 |
6.90e-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: 409.09 E-value: 6.90e-144
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333956788 7 PLTDLHRHLDGNIRAQTILDLGRQFNLALPADTLETLRPhvqiTKNEPDLVSFLAKLDWGVKVLGSLEACRRVAYENMED 86
Cdd:COG1816 1 PKAELHLHLEGSLRPETLLELAARNGIDLPAADVEELRA----AYDFRDLQSFLDTYDAGAAVLQTEEDFRRLAYEYLED 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333956788 87 AARNGLHYVELRFSPgYMAMTHNLPIAGVVEAVIDGVRQGSRDYGVDARLIGILSRTFGEEACVAELDGLLAHRDH-ITA 165
Cdd:COG1816 77 AAADGVRYAEIRFDP-QLHTRRGLSLEEVVEAVLDGLREAEREFGISVRLILCALRHLSPEAAFETLELALRYRDRgVVG 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333956788 166 LDLAGDELGFPGSLFLNHFNRGRDAGWHITVHAGEAAGPESIWQAIRELGAERIGHGVKAVEDPALMDFLAEQGIGIESC 245
Cdd:COG1816 156 FGLAGDERGFPPEKFAEAFARAREAGLHLTAHAGEAGGPESIWEALDLLGAERIGHGVRAIEDPALVARLADRGIPLEVC 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333956788 246 LTSNIQTSTVASLAHHPLKTFLEHNILATINTDDPGVQGVDIRHEYEVAAPAAGLSAAQIRTAQENGLKIAFLTDAEKQA 325
Cdd:COG1816 236 PTSNVQLGVVPSLAEHPLRRLLDAGVRVTLNTDDPLYFGTTLTDEYELAAEAFGLSDADLAQLARNAIEASFLPEEEKAA 315
|
....*...
gi 333956788 326 LVAKVSAA 333
Cdd:COG1816 316 LLAELDAY 323
|
|
| A_deaminase |
pfam00962 |
Adenosine deaminase; |
7-333 |
4.34e-136 |
|
Adenosine deaminase;
Pssm-ID: 425964 Cd Length: 330 Bit Score: 389.48 E-value: 4.34e-136
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333956788 7 PLTDLHRHLDGNIRAQTILDLGRQFNLALPADTLETLRPHVQITKNEPDLVSFLAKLDWGVKVLGSLEACRRVAYENMED 86
Cdd:pfam00962 1 PKAELHLHLDGSLRPDTLLELAKRYGIILPADFPEALEPLFRKYKKERDLQDFLDKYDIGVAVLRSPEDIRRLAFEYAED 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333956788 87 AARNGLHYVELRFSPGYMAMThNLPIAGVVEAVIDGVRQGSRDYGVDARLIGILSRTfGEEACVAELDGLLA-HRDH-IT 164
Cdd:pfam00962 81 VAKDGVVYAEVRYDPQSHASR-GLSPDTVVDAVLDAVDAAEREFGITVRLIVCAMRH-EHPECSREIAELAPrYRDQgIV 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333956788 165 ALDLAGDELGFPGSLFLNH---FNRGRDAGWHITVHAGEAAGPESIWQAIRELGAERIGHGVKAVEDPALMDFLAEQGIG 241
Cdd:pfam00962 159 AFGLAGDEKGFPPSLFRDHveaFARARDAGLHLTVHAGEAGGPQSVWEALDDLGAERIGHGVRSAEDPRLLDRLADRQIP 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333956788 242 IESCLTSNIQTSTVASLAHHPLKTFLEHNILATINTDDPGVQGVDIRHEYEVAAPAAGLSAAQIRTAQENGLKIAFLTDA 321
Cdd:pfam00962 239 LEICPTSNVQTGAVASLAEHPLKTFLRAGVPVSLNTDDPLMFGSDLLDEYQVAKRAPGFDEEELARLAKNAVKGSFLPAD 318
|
330
....*....|..
gi 333956788 322 EKQALVAKVSAA 333
Cdd:pfam00962 319 EKRALLDEVDKV 330
|
|
| ADA |
cd01320 |
Adenosine deaminase (ADA) is a monomeric zinc dependent enzyme which catalyzes the ... |
5-330 |
3.65e-129 |
|
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: 371.54 E-value: 3.65e-129
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333956788 5 RLPLTDLHRHLDGNIRAQTILDLGRQFNLALPADTLEtLRPHVQITKNEPDLVSFLAKLDWGVKVLGSLEACRRVAYENM 84
Cdd:cd01320 1 NLPKAELHLHLDGSLRPETILELAKKNGITLPASDVE-LLELVVAAYNFSDLQDFLAKYDFGLSVLQTEEDFERLAYEYL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333956788 85 EDAARNGLHYVELRFSPGYMaMTHNLPIAGVVEAVIDGVRQGSRDYGVDARLIGILSRTFGEEACVAELDGLLAHRD-HI 163
Cdd:cd01320 80 EDAAADGVVYAEIRFSPQLH-TRRGLSFDEVVEAVLRGLDEAEAEFGIKARLILCGLRHLSPESAQETLELALKYRDkGV 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333956788 164 TALDLAGDELGFPGSLFLNHFNRGRDAGWHITVHAGEAAGPESIWQAIRELGAERIGHGVKAVEDPALMDFLAEQGIGIE 243
Cdd:cd01320 159 VGFDLAGDEVGFPPEKFVRAFQRAREAGLRLTAHAGEAGGPESVRDALDLLGAERIGHGIRAIEDPELVKRLAERNIPLE 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333956788 244 SCLTSNIQTSTVASLAHHPLKTFLEHNILATINTDDPGVQGVDIRHEYEVAAPAAGLSAAQIRTAQENGLKIAFLTDAEK 323
Cdd:cd01320 239 VCPTSNVQTGAVKSLAEHPLRELLDAGVKVTINTDDPTVFGTYLTDEYELLAEAFGLTEEELKKLARNAVEASFLSEEEK 318
|
....*..
gi 333956788 324 QALVAKV 330
Cdd:cd01320 319 AELLKRI 325
|
|
| aden_deam |
TIGR01430 |
adenosine deaminase; This family includes the experimentally verified adenosine deaminases of ... |
6-330 |
3.81e-121 |
|
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: 351.27 E-value: 3.81e-121
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333956788 6 LPLTDLHRHLDGNIRAQTILDLGRQFNLALPADtLETLRPHVQITKNEPDLVSFLAKLDWGVKVLGSLEACRRVAYENME 85
Cdd:TIGR01430 1 LPKAELHLHLEGSIRPETLLELAQKNGIPLPAD-LQSGEELKEAYDKFRDLQDFLAKYDFGVEVLRTEDDFKRLAYEYVE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333956788 86 DAARNGLHYVELRFSPGYMAMTHNLPIaGVVEAVIDGVRQGSRDYGVDARLIGILSRTFGEEACVAELDGLLAHRDH-IT 164
Cdd:TIGR01430 80 KAAKDGVVYAEVFFDPQLHTNRGISPD-TVVEAVLDGLDEAERDFGIKSRLILCGMRHKQPEAAEETLELAKPYKEQtIV 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333956788 165 ALDLAGDELGFPGSLFLNHFNRGRDAGWHITVHAGEAAGPESIWQAIRELGAERIGHGVKAVEDPALMDFLAEQGIGIES 244
Cdd:TIGR01430 159 GFGLAGDERGGPPPDFVRAFAIARELGLHLTVHAGELGGPESVREALDDLGATRIGHGVRALEDPELLKRLAQENITLEV 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333956788 245 CLTSNIQTSTVASLAHHPLKTFLEHNILATINTDDPGVQGVDIRHEYEVAAPAAGLSAAQIRTAQENGLKIAFLTDAEKQ 324
Cdd:TIGR01430 239 CPTSNVALGVVKSLAEHPLRRFLEAGVKVTLNSDDPAYFGSYLTEEYEIAAKHAGLTEEELKQLARNALEGSFLSDDEKK 318
|
....*.
gi 333956788 325 ALVAKV 330
Cdd:TIGR01430 319 ELLAKL 324
|
|
| PTZ00124 |
PTZ00124 |
adenosine deaminase; Provisional |
5-292 |
8.04e-42 |
|
adenosine deaminase; Provisional
Pssm-ID: 173415 Cd Length: 362 Bit Score: 148.86 E-value: 8.04e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333956788 5 RLPLTDLHRHLDGNIRAQTILDLGRQFNLAlPADTLETLRPHVQITKNEPDLVSFLAKLDWGVKVLGSLEACRRVAYENM 84
Cdd:PTZ00124 34 RIPKCELHCHLDLCFSVDFFLSCIRKYNLQ-PNLSDEEILDYYLFAKGGKSLGEFVEKAIRVADIFNDYEVIEDLAKHAV 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333956788 85 EDAARNGLHYVELRFSPGYMAMTHNLPIAGVVEAVIDGVRQGSR--DYGVDARLIGILSRTFGEEACVAELDGLLAHRDH 162
Cdd:PTZ00124 113 FNKYKEGVVLMEFRYSPTFVAFKHNLDIDLIHQAIVKGIKEAVEllDHKIEVGLLCIGDTGHDAAPIKESADFCLKHKAD 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333956788 163 ITALDLAGDELGFpgSLFLNHFNRGRDAGWHITVHAGEAAGP---ESIWQAIRELGAERIGHGVKAVEDPALMDFLAEQG 239
Cdd:PTZ00124 193 FVGFDHAGHEVDL--KPFKDIFDYVREAGVNLTVHAGEDVTLpnlNTLYSAIQVLKVKRIGHGIRVAESQELIDMVKEKD 270
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 333956788 240 IGIESCLTSNIQTSTVASLAHHPLKTFLEHNILATINTDDPGVQGVDIRHEYE 292
Cdd:PTZ00124 271 ILLEVCPISNVLLNNAKSMDTHPIRKLYDAGVKVSVNSDDPGMFLTNINDDYE 323
|
|
| ADA_AMPD |
cd00443 |
Adenosine/AMP deaminase. Adenosine deaminases (ADAs) are present in pro- and eukaryotic ... |
6-327 |
9.62e-42 |
|
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: 147.11 E-value: 9.62e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333956788 6 LPLTDLHRHLDGNIRAQTILDLGRQfnlalpadtletlrphvqitknepdlvSFLAKLDWGVKVLGSLEACRRVAYENME 85
Cdd:cd00443 1 LPKVELHAHLSGSISPETLLELIKK---------------------------EFFEKFLLVHNLLQKGEALARALKEVIE 53
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333956788 86 DAARNGLHYVELRFSPGYMAMTHNLPIAGVVEAVIDGVRQGSRDY-GVDARLI-GILSR-TFGEEACVA-ELDGLLAH-R 160
Cdd:cd00443 54 EFAEDNVQYLELRTTPRLLETEKGLTKEQYWLLVIEGISEAKQWFpPIKVRLIlSVDRRgPYVQNYLVAsEILELAKFlS 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333956788 161 DHITALDLAGDELGFPGSL--FLNHFNRGRDAGW-HITVHAGEAAGPESIWQAIrELGAERIGHGVKAVEDPALMDFLAE 237
Cdd:cd00443 134 NYVVGIDLVGDESKGENPLrdFYSYYEYARRLGLlGLTLHCGETGNREELLQAL-LLLPDRIGHGIFLLKHPELIYLVKL 212
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333956788 238 QGIGIESCLTSNIQTSTVASLAHHPLKTFLEHNILATINTDDPGVQGVDIRHEYEVAAPAAGLSAAQIRTAQENGLKIAF 317
Cdd:cd00443 213 RNIPIEVCPTSNVVLGTVQSYEKHPFMRFFKAGLPVSLSTDDPGIFGTSLSEEYSLAAKTFGLTFEDLCELNRNSVLSSF 292
|
330
....*....|
gi 333956788 318 LTDAEKQALV 327
Cdd:cd00443 293 AKDEEKKSLL 302
|
|
| ADGF |
cd01321 |
Adenosine deaminase-related growth factors (ADGF), a novel family of secreted growth-factors ... |
91-329 |
2.34e-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: 2.34e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333956788 91 GLHYVELR--FSPGYMAMTHNLPIAGVV---EAVIDGVRQGSRDYgVDARLIGILSRTFGEEACVAELDGLLAHR----D 161
Cdd:cd01321 83 NVQYVELRssFSPLYDLDGREYDYEETVqllEEVVEKFKKTHPDF-IGLKIIYATLRNFNDSEIKESMEQCLNLKkkfpD 161
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333956788 162 HITALDLAGDE-LGFPGSLFLNHFNRGRDAGWHIT--VHAGEAAGPES-----IWQAIReLGAERIGHGVKAVEDPALMD 233
Cdd:cd01321 162 FIAGFDLVGQEdAGRPLLDFLPQLLWFPKQCAEIPffFHAGETNGDGTetdenLVDALL-LNTKRIGHGFALPKHPLLMD 240
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333956788 234 FLAEQGIGIESCLTSNIQTSTVASLAHHPLKTFLEHNILATINTDDPGVQGVD-IRHEYEVAAPAAGLSAAQIRT-AQ-- 309
Cdd:cd01321 241 LVKKKNIAIEVCPISNQVLGLVSDLRNHPAAALLARGVPVVISSDDPGFWGAKgLSHDFYQAFMGLAPADAGLRGlKQla 320
|
250 260
....*....|....*....|
gi 333956788 310 ENGLKIAFLTDAEKQALVAK 329
Cdd:cd01321 321 ENSIRYSALSDQEKDEAVAK 340
|
|
| AMPD |
cd01319 |
AMP deaminase (AMPD) catalyzes the hydrolytic deamination of adensosine monophosphate (AMP) at ... |
181-280 |
2.43e-04 |
|
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: 42.74 E-value: 2.43e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333956788 181 LNHFNRGRdaGWHITV---HAGEAAGPESIWQAIreLGAERIGHGVKAVEDPAL--MDFLAEQGIGIeSCLTSNiqtSTV 255
Cdd:cd01319 315 LNSFRKAR--GFNTFVlrpHCGEAGDIDHLASAF--LLAHGISHGINLRKVPVLqyLYYLTQIGIAM-SPLSNN---SLF 386
|
90 100
....*....|....*....|....*
gi 333956788 256 ASLAHHPLKTFLEHNILATINTDDP 280
Cdd:cd01319 387 LSYEKNPFPEFFKRGLNVSLSTDDP 411
|
|
| metallo-dependent_hydrolases |
cd01292 |
Superfamily of metallo-dependent hydrolases (also called amidohydrolase superfamily) is a ... |
53-284 |
3.73e-04 |
|
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: 41.55 E-value: 3.73e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333956788 53 EPDLVSFLAKLDWGVKVLGSLEACRRVAYENMEDAARNGLHYVELRFSPGYMAMThnlpiagvvEAVIDGVRQGSRDY-G 131
Cdd:cd01292 10 GSALRGTRLNLELKEAEELSPEDLYEDTLRALEALLAGGVTTVVDMGSTPPPTTT---------KAAIEAVAEAARASaG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333956788 132 VDARLIGILSRTFGEEACVAELDGL----LAHRDHITALDLAGDE--LGFPGSLFLNHFNRGRDAGWHITVHAGEAAGPE 205
Cdd:cd01292 81 IRVVLGLGIPGVPAAVDEDAEALLLellrRGLELGAVGLKLAGPYtaTGLSDESLRRVLEEARKLGLPVVIHAGELPDPT 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333956788 206 SIW----QAIRELGAERIGHGVkaVEDPALMDFLAEQGIGIESCLTSNiQTSTVASLAHHPLKTFLEHNILATINTDDPG 281
Cdd:cd01292 161 RALedlvALLRLGGRVVIGHVS--HLDPELLELLKEAGVSLEVCPLSN-YLLGRDGEGAEALRRLLELGIRVTLGTDGPP 237
|
...
gi 333956788 282 VQG 284
Cdd:cd01292 238 HPL 240
|
|
| |
