|
Name |
Accession |
Description |
Interval |
E-value |
| A_deaminase |
pfam00962 |
Adenosine deaminase; |
7-333 |
2.16e-153 |
|
Adenosine deaminase;
Pssm-ID: 425964 Cd Length: 330 Bit Score: 434.16 E-value: 2.16e-153
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1A4L_C 7 PKVELHVHLDGAIKPETILYFGKKRGIALPADTVEELRNIIGM-DKPLSLPGFLAKFDYYmPVIAGCREAIKRIAYEFVE 85
Cdd:pfam00962 1 PKAELHLHLDGSLRPDTLLELAKRYGIILPADFPEALEPLFRKyKKERDLQDFLDKYDIG-VAVLRSPEDIRRLAFEYAE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1A4L_C 86 MKAKEGVVYVEVRYSPHLLANSkvdpmpwnqtegDVTPDDVVDLVNQGLQEGEQAFGIKVRSILCCMRH-QPSWSLEVLE 164
Cdd:pfam00962 80 DVAKDGVVYAEVRYDPQSHASR------------GLSPDTVVDAVLDAVDAAEREFGITVRLIVCAMRHeHPECSREIAE 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1A4L_C 165 LCKKYNQKTVVAMDLAGDETIEGSSLFPGHVEAYEGAVKNGIHRTVHAGEVGSPEVVREAVDILKTERVGHGYHTIEDEA 244
Cdd:pfam00962 148 LAPRYRDQGIVAFGLAGDEKGFPPSLFRDHVEAFARARDAGLHLTVHAGEAGGPQSVWEALDDLGAERIGHGVRSAEDPR 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1A4L_C 245 LYNRLLKENMHFEVCPWSSYLTGAWDPKTTHAVVRFKNDKANYSLNTDDPLIFKSTLDTDYQMTKKDMGFTEEEFKRLNI 324
Cdd:pfam00962 228 LLDRLADRQIPLEICPTSNVQTGAVASLAEHPLKTFLRAGVPVSLNTDDPLMFGSDLLDEYQVAKRAPGFDEEELARLAK 307
|
....*....
1A4L_C 325 NAAKSSFLP 333
Cdd:pfam00962 308 NAVKGSFLP 316
|
|
| ADA |
cd01320 |
Adenosine deaminase (ADA) is a monomeric zinc dependent enzyme which catalyzes the ... |
5-333 |
2.18e-147 |
|
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: 418.53 E-value: 2.18e-147
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1A4L_C 5 NKPKVELHVHLDGAIKPETILYFGKKRGIALPADTVEELRNIIGMDKPLSLPGFLAKFDYYMPVIAGcREAIKRIAYEFV 84
Cdd:cd01320 1 NLPKAELHLHLDGSLRPETILELAKKNGITLPASDVELLELVVAAYNFSDLQDFLAKYDFGLSVLQT-EEDFERLAYEYL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1A4L_C 85 EMKAKEGVVYVEVRYSPHLLanskvdpmpwnqTEGDVTPDDVVDLVNQGLQEGEQAFGIKVRSILCCMRHQP-SWSLEVL 163
Cdd:cd01320 80 EDAAADGVVYAEIRFSPQLH------------TRRGLSFDEVVEAVLRGLDEAEAEFGIKARLILCGLRHLSpESAQETL 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1A4L_C 164 ELCKKYNQKTVVAMDLAGDETIEgssLFPGHVEAYEGAVKNGIHRTVHAGEVGSPEVVREAVDILKTERVGHGYHTIEDE 243
Cdd:cd01320 148 ELALKYRDKGVVGFDLAGDEVGF---PPEKFVRAFQRAREAGLRLTAHAGEAGGPESVRDALDLLGAERIGHGIRAIEDP 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1A4L_C 244 ALYNRLLKENMHFEVCPWSSYLTGAWDPKTTHAVVRFKNDKANYSLNTDDPLIFKSTLDTDYQMTKKDMGFTEEEFKRLN 323
Cdd:cd01320 225 ELVKRLAERNIPLEVCPTSNVQTGAVKSLAEHPLRELLDAGVKVTINTDDPTVFGTYLTDEYELLAEAFGLTEEELKKLA 304
|
330
....*....|
1A4L_C 324 INAAKSSFLP 333
Cdd:cd01320 305 RNAVEASFLS 314
|
|
| aden_deam |
TIGR01430 |
adenosine deaminase; This family includes the experimentally verified adenosine deaminases of ... |
6-333 |
1.95e-145 |
|
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: 413.68 E-value: 1.95e-145
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1A4L_C 6 KPKVELHVHLDGAIKPETILYFGKKRGIALPADTVEELRNIIGMDKPLSLPGFLAKFDYYMPVIaGCREAIKRIAYEFVE 85
Cdd:TIGR01430 1 LPKAELHLHLEGSIRPETLLELAQKNGIPLPADLQSGEELKEAYDKFRDLQDFLAKYDFGVEVL-RTEDDFKRLAYEYVE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1A4L_C 86 MKAKEGVVYVEVRYSPHLLANSKVdpmpwnqtegdvTPDDVVDLVNQGLQEGEQAFGIKVRSILCCMRH-QPSWSLEVLE 164
Cdd:TIGR01430 80 KAAKDGVVYAEVFFDPQLHTNRGI------------SPDTVVEAVLDGLDEAERDFGIKSRLILCGMRHkQPEAAEETLE 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1A4L_C 165 LCKKYNQKTVVAMDLAGDETIEGsslFPGHVEAYEGAVKNGIHRTVHAGEVGSPEVVREAVDILKTERVGHGYHTIEDEA 244
Cdd:TIGR01430 148 LAKPYKEQTIVGFGLAGDERGGP---PPDFVRAFAIARELGLHLTVHAGELGGPESVREALDDLGATRIGHGVRALEDPE 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1A4L_C 245 LYNRLLKENMHFEVCPWSSYLTGAWDPKTTHAVVRFKNDKANYSLNTDDPLIFKSTLDTDYQMTKKDMGFTEEEFKRLNI 324
Cdd:TIGR01430 225 LLKRLAQENITLEVCPTSNVALGVVKSLAEHPLRRFLEAGVKVTLNSDDPAYFGSYLTEEYEIAAKHAGLTEEELKQLAR 304
|
....*....
1A4L_C 325 NAAKSSFLP 333
Cdd:TIGR01430 305 NALEGSFLS 313
|
|
| Add |
COG1816 |
Adenosine deaminase [Nucleotide transport and metabolism]; Adenosine deaminase is part of the ... |
7-333 |
7.54e-107 |
|
Adenosine deaminase [Nucleotide transport and metabolism]; Adenosine deaminase is part of the Pathway/BioSystem: Menaquinone biosynthesis
Pssm-ID: 441421 Cd Length: 326 Bit Score: 315.49 E-value: 7.54e-107
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1A4L_C 7 PKVELHVHLDGAIKPETILYFGKKRGIALPADTVEELRNIIGMDkplSLPGFLAKFDYYMPVIAGcREAIKRIAYEFVEM 86
Cdd:COG1816 1 PKAELHLHLEGSLRPETLLELAARNGIDLPAADVEELRAAYDFR---DLQSFLDTYDAGAAVLQT-EEDFRRLAYEYLED 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1A4L_C 87 KAKEGVVYVEVRYSPHLLanskvdpmpwnqTEGDVTPDDVVDLVNQGLQEGEQAFGIKVRSILCCMRHQ-PSWSLEVLEL 165
Cdd:COG1816 77 AAADGVRYAEIRFDPQLH------------TRRGLSLEEVVEAVLDGLREAEREFGISVRLILCALRHLsPEAAFETLEL 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1A4L_C 166 CKKYNQKTVVAMDLAGDETiegssLFPG--HVEAYEGAVKNGIHRTVHAGEVGSPEVVREAVDILKTERVGHGYHTIEDE 243
Cdd:COG1816 145 ALRYRDRGVVGFGLAGDER-----GFPPekFAEAFARAREAGLHLTAHAGEAGGPESIWEALDLLGAERIGHGVRAIEDP 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1A4L_C 244 ALYNRLLKENMHFEVCPWSSYLTGAWDPKTTHAVVRFKNDKANYSLNTDDPLIFKSTLDTDYQMTKKDMGFTEEEFKRLN 323
Cdd:COG1816 220 ALVARLADRGIPLEVCPTSNVQLGVVPSLAEHPLRRLLDAGVRVTLNTDDPLYFGTTLTDEYELAAEAFGLSDADLAQLA 299
|
330
....*....|
1A4L_C 324 INAAKSSFLP 333
Cdd:COG1816 300 RNAIEASFLP 309
|
|
| PRK09358 |
PRK09358 |
adenosine deaminase; Provisional |
7-333 |
3.30e-93 |
|
adenosine deaminase; Provisional
Pssm-ID: 236480 Cd Length: 340 Bit Score: 281.30 E-value: 3.30e-93
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1A4L_C 7 PKVELHVHLDGAIKPETILYFGKKRGIALPADTVEELRNIIGMDKPLSLPGFLAKFDYYMPVIAGcREAIKRIAYEFVEM 86
Cdd:PRK09358 11 PKAELHLHLDGSLRPETILELARRNGIALPATDVEELPWVRAAYDFRDLQSFLDKYDAGVAVLQT-EEDLRRLAFEYLED 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1A4L_C 87 KAKEGVVYVEVRYSPhllanskvdpmpWNQTEGDVTPDDVVDLVNQGLQEGEQAFGIKVRSILCCMRH--QPSWSLEVLE 164
Cdd:PRK09358 90 AAADGVVYAEIRFDP------------QLHTERGLPLEEVVEAVLDGLRAAEAEFGISVRLILCFMRHfgEEAAARELEA 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1A4L_C 165 LCKKYNQKTVVAMDLAGDETIEGSSLFpghVEAYEGAVKNGIHRTVHAGEVGSPEVVREAVDILKTERVGHGYHTIEDEA 244
Cdd:PRK09358 158 LAARYRDDGVVGFDLAGDELGFPPSKF---ARAFDRARDAGLRLTAHAGEAGGPESIWEALDELGAERIGHGVRAIEDPA 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1A4L_C 245 LYNRLLKENMHFEVCPWSSYLTGAWDPKTTHAVVRFKNDKANYSLNTDDPLIFKSTLDTDYQMTKKDMGFTEEEFKRLNI 324
Cdd:PRK09358 235 LMARLADRRIPLEVCPTSNVQTGAVPSLAEHPLKTLLDAGVRVTINTDDPLVFGTTLTEEYEALAEAFGLSDEDLAQLAR 314
|
....*....
1A4L_C 325 NAAKSSFLP 333
Cdd:PRK09358 315 NALEAAFLS 323
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| A_deaminase |
pfam00962 |
Adenosine deaminase; |
7-333 |
2.16e-153 |
|
Adenosine deaminase;
Pssm-ID: 425964 Cd Length: 330 Bit Score: 434.16 E-value: 2.16e-153
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1A4L_C 7 PKVELHVHLDGAIKPETILYFGKKRGIALPADTVEELRNIIGM-DKPLSLPGFLAKFDYYmPVIAGCREAIKRIAYEFVE 85
Cdd:pfam00962 1 PKAELHLHLDGSLRPDTLLELAKRYGIILPADFPEALEPLFRKyKKERDLQDFLDKYDIG-VAVLRSPEDIRRLAFEYAE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1A4L_C 86 MKAKEGVVYVEVRYSPHLLANSkvdpmpwnqtegDVTPDDVVDLVNQGLQEGEQAFGIKVRSILCCMRH-QPSWSLEVLE 164
Cdd:pfam00962 80 DVAKDGVVYAEVRYDPQSHASR------------GLSPDTVVDAVLDAVDAAEREFGITVRLIVCAMRHeHPECSREIAE 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1A4L_C 165 LCKKYNQKTVVAMDLAGDETIEGSSLFPGHVEAYEGAVKNGIHRTVHAGEVGSPEVVREAVDILKTERVGHGYHTIEDEA 244
Cdd:pfam00962 148 LAPRYRDQGIVAFGLAGDEKGFPPSLFRDHVEAFARARDAGLHLTVHAGEAGGPQSVWEALDDLGAERIGHGVRSAEDPR 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1A4L_C 245 LYNRLLKENMHFEVCPWSSYLTGAWDPKTTHAVVRFKNDKANYSLNTDDPLIFKSTLDTDYQMTKKDMGFTEEEFKRLNI 324
Cdd:pfam00962 228 LLDRLADRQIPLEICPTSNVQTGAVASLAEHPLKTFLRAGVPVSLNTDDPLMFGSDLLDEYQVAKRAPGFDEEELARLAK 307
|
....*....
1A4L_C 325 NAAKSSFLP 333
Cdd:pfam00962 308 NAVKGSFLP 316
|
|
| ADA |
cd01320 |
Adenosine deaminase (ADA) is a monomeric zinc dependent enzyme which catalyzes the ... |
5-333 |
2.18e-147 |
|
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: 418.53 E-value: 2.18e-147
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1A4L_C 5 NKPKVELHVHLDGAIKPETILYFGKKRGIALPADTVEELRNIIGMDKPLSLPGFLAKFDYYMPVIAGcREAIKRIAYEFV 84
Cdd:cd01320 1 NLPKAELHLHLDGSLRPETILELAKKNGITLPASDVELLELVVAAYNFSDLQDFLAKYDFGLSVLQT-EEDFERLAYEYL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1A4L_C 85 EMKAKEGVVYVEVRYSPHLLanskvdpmpwnqTEGDVTPDDVVDLVNQGLQEGEQAFGIKVRSILCCMRHQP-SWSLEVL 163
Cdd:cd01320 80 EDAAADGVVYAEIRFSPQLH------------TRRGLSFDEVVEAVLRGLDEAEAEFGIKARLILCGLRHLSpESAQETL 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1A4L_C 164 ELCKKYNQKTVVAMDLAGDETIEgssLFPGHVEAYEGAVKNGIHRTVHAGEVGSPEVVREAVDILKTERVGHGYHTIEDE 243
Cdd:cd01320 148 ELALKYRDKGVVGFDLAGDEVGF---PPEKFVRAFQRAREAGLRLTAHAGEAGGPESVRDALDLLGAERIGHGIRAIEDP 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1A4L_C 244 ALYNRLLKENMHFEVCPWSSYLTGAWDPKTTHAVVRFKNDKANYSLNTDDPLIFKSTLDTDYQMTKKDMGFTEEEFKRLN 323
Cdd:cd01320 225 ELVKRLAERNIPLEVCPTSNVQTGAVKSLAEHPLRELLDAGVKVTINTDDPTVFGTYLTDEYELLAEAFGLTEEELKKLA 304
|
330
....*....|
1A4L_C 324 INAAKSSFLP 333
Cdd:cd01320 305 RNAVEASFLS 314
|
|
| aden_deam |
TIGR01430 |
adenosine deaminase; This family includes the experimentally verified adenosine deaminases of ... |
6-333 |
1.95e-145 |
|
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: 413.68 E-value: 1.95e-145
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1A4L_C 6 KPKVELHVHLDGAIKPETILYFGKKRGIALPADTVEELRNIIGMDKPLSLPGFLAKFDYYMPVIaGCREAIKRIAYEFVE 85
Cdd:TIGR01430 1 LPKAELHLHLEGSIRPETLLELAQKNGIPLPADLQSGEELKEAYDKFRDLQDFLAKYDFGVEVL-RTEDDFKRLAYEYVE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1A4L_C 86 MKAKEGVVYVEVRYSPHLLANSKVdpmpwnqtegdvTPDDVVDLVNQGLQEGEQAFGIKVRSILCCMRH-QPSWSLEVLE 164
Cdd:TIGR01430 80 KAAKDGVVYAEVFFDPQLHTNRGI------------SPDTVVEAVLDGLDEAERDFGIKSRLILCGMRHkQPEAAEETLE 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1A4L_C 165 LCKKYNQKTVVAMDLAGDETIEGsslFPGHVEAYEGAVKNGIHRTVHAGEVGSPEVVREAVDILKTERVGHGYHTIEDEA 244
Cdd:TIGR01430 148 LAKPYKEQTIVGFGLAGDERGGP---PPDFVRAFAIARELGLHLTVHAGELGGPESVREALDDLGATRIGHGVRALEDPE 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1A4L_C 245 LYNRLLKENMHFEVCPWSSYLTGAWDPKTTHAVVRFKNDKANYSLNTDDPLIFKSTLDTDYQMTKKDMGFTEEEFKRLNI 324
Cdd:TIGR01430 225 LLKRLAQENITLEVCPTSNVALGVVKSLAEHPLRRFLEAGVKVTLNSDDPAYFGSYLTEEYEIAAKHAGLTEEELKQLAR 304
|
....*....
1A4L_C 325 NAAKSSFLP 333
Cdd:TIGR01430 305 NALEGSFLS 313
|
|
| Add |
COG1816 |
Adenosine deaminase [Nucleotide transport and metabolism]; Adenosine deaminase is part of the ... |
7-333 |
7.54e-107 |
|
Adenosine deaminase [Nucleotide transport and metabolism]; Adenosine deaminase is part of the Pathway/BioSystem: Menaquinone biosynthesis
Pssm-ID: 441421 Cd Length: 326 Bit Score: 315.49 E-value: 7.54e-107
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1A4L_C 7 PKVELHVHLDGAIKPETILYFGKKRGIALPADTVEELRNIIGMDkplSLPGFLAKFDYYMPVIAGcREAIKRIAYEFVEM 86
Cdd:COG1816 1 PKAELHLHLEGSLRPETLLELAARNGIDLPAADVEELRAAYDFR---DLQSFLDTYDAGAAVLQT-EEDFRRLAYEYLED 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1A4L_C 87 KAKEGVVYVEVRYSPHLLanskvdpmpwnqTEGDVTPDDVVDLVNQGLQEGEQAFGIKVRSILCCMRHQ-PSWSLEVLEL 165
Cdd:COG1816 77 AAADGVRYAEIRFDPQLH------------TRRGLSLEEVVEAVLDGLREAEREFGISVRLILCALRHLsPEAAFETLEL 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1A4L_C 166 CKKYNQKTVVAMDLAGDETiegssLFPG--HVEAYEGAVKNGIHRTVHAGEVGSPEVVREAVDILKTERVGHGYHTIEDE 243
Cdd:COG1816 145 ALRYRDRGVVGFGLAGDER-----GFPPekFAEAFARAREAGLHLTAHAGEAGGPESIWEALDLLGAERIGHGVRAIEDP 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1A4L_C 244 ALYNRLLKENMHFEVCPWSSYLTGAWDPKTTHAVVRFKNDKANYSLNTDDPLIFKSTLDTDYQMTKKDMGFTEEEFKRLN 323
Cdd:COG1816 220 ALVARLADRGIPLEVCPTSNVQLGVVPSLAEHPLRRLLDAGVRVTLNTDDPLYFGTTLTDEYELAAEAFGLSDADLAQLA 299
|
330
....*....|
1A4L_C 324 INAAKSSFLP 333
Cdd:COG1816 300 RNAIEASFLP 309
|
|
| ADA_AMPD |
cd00443 |
Adenosine/AMP deaminase. Adenosine deaminases (ADAs) are present in pro- and eukaryotic ... |
6-333 |
2.99e-100 |
|
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: 298.11 E-value: 2.99e-100
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1A4L_C 6 KPKVELHVHLDGAIKPETILYFGKKrgialpadtveelrniigmdkplslpGFLAKFDYYMPVIaGCREAIKRIAYEFVE 85
Cdd:cd00443 1 LPKVELHAHLSGSISPETLLELIKK--------------------------EFFEKFLLVHNLL-QKGEALARALKEVIE 53
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1A4L_C 86 MKAKEGVVYVEVRYSPHLLANSKvdpmpwnqtegDVTPDDVVDLVNQGLQEGEQAF-GIKVRSILCCMRHQPS-----WS 159
Cdd:cd00443 54 EFAEDNVQYLELRTTPRLLETEK-----------GLTKEQYWLLVIEGISEAKQWFpPIKVRLILSVDRRGPYvqnylVA 122
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1A4L_C 160 LEVLELCKKYNQkTVVAMDLAGDETIEGSsLFPGHVEAYEGAVKNG-IHRTVHAGEVGSPEVVREAVDiLKTERVGHGYH 238
Cdd:cd00443 123 SEILELAKFLSN-YVVGIDLVGDESKGEN-PLRDFYSYYEYARRLGlLGLTLHCGETGNREELLQALL-LLPDRIGHGIF 199
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1A4L_C 239 TIEDEALYNRLLKENMHFEVCPWSSYLTGAWDPKTTHAVVRFKNDKANYSLNTDDPLIFKSTLDTDYQMTKKDMGFTEEE 318
Cdd:cd00443 200 LLKHPELIYLVKLRNIPIEVCPTSNVVLGTVQSYEKHPFMRFFKAGLPVSLSTDDPGIFGTSLSEEYSLAAKTFGLTFED 279
|
330
....*....|....*
1A4L_C 319 FKRLNINAAKSSFLP 333
Cdd:cd00443 280 LCELNRNSVLSSFAK 294
|
|
| PRK09358 |
PRK09358 |
adenosine deaminase; Provisional |
7-333 |
3.30e-93 |
|
adenosine deaminase; Provisional
Pssm-ID: 236480 Cd Length: 340 Bit Score: 281.30 E-value: 3.30e-93
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1A4L_C 7 PKVELHVHLDGAIKPETILYFGKKRGIALPADTVEELRNIIGMDKPLSLPGFLAKFDYYMPVIAGcREAIKRIAYEFVEM 86
Cdd:PRK09358 11 PKAELHLHLDGSLRPETILELARRNGIALPATDVEELPWVRAAYDFRDLQSFLDKYDAGVAVLQT-EEDLRRLAFEYLED 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1A4L_C 87 KAKEGVVYVEVRYSPhllanskvdpmpWNQTEGDVTPDDVVDLVNQGLQEGEQAFGIKVRSILCCMRH--QPSWSLEVLE 164
Cdd:PRK09358 90 AAADGVVYAEIRFDP------------QLHTERGLPLEEVVEAVLDGLRAAEAEFGISVRLILCFMRHfgEEAAARELEA 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1A4L_C 165 LCKKYNQKTVVAMDLAGDETIEGSSLFpghVEAYEGAVKNGIHRTVHAGEVGSPEVVREAVDILKTERVGHGYHTIEDEA 244
Cdd:PRK09358 158 LAARYRDDGVVGFDLAGDELGFPPSKF---ARAFDRARDAGLRLTAHAGEAGGPESIWEALDELGAERIGHGVRAIEDPA 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1A4L_C 245 LYNRLLKENMHFEVCPWSSYLTGAWDPKTTHAVVRFKNDKANYSLNTDDPLIFKSTLDTDYQMTKKDMGFTEEEFKRLNI 324
Cdd:PRK09358 235 LMARLADRRIPLEVCPTSNVQTGAVPSLAEHPLKTLLDAGVRVTINTDDPLVFGTTLTEEYEALAEAFGLSDEDLAQLAR 314
|
....*....
1A4L_C 325 NAAKSSFLP 333
Cdd:PRK09358 315 NALEAAFLS 323
|
|
| PTZ00124 |
PTZ00124 |
adenosine deaminase; Provisional |
7-332 |
5.50e-29 |
|
adenosine deaminase; Provisional
Pssm-ID: 173415 Cd Length: 362 Bit Score: 114.96 E-value: 5.50e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1A4L_C 7 PKVELHVHLDGAIKPETILYFGKKRGIALPADTVEELRNIIGMDKPLSLPGFLAKFDYYMPVIAGcREAIKRIAYEFVEM 86
Cdd:PTZ00124 36 PKCELHCHLDLCFSVDFFLSCIRKYNLQPNLSDEEILDYYLFAKGGKSLGEFVEKAIRVADIFND-YEVIEDLAKHAVFN 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1A4L_C 87 KAKEGVVYVEVRYSPHLLANSKvdpmpwnqtegDVTPDDVVDLVNQGLQEGEQAFGIKVRSILCCMR---HQPSWSLEVL 163
Cdd:PTZ00124 115 KYKEGVVLMEFRYSPTFVAFKH-----------NLDIDLIHQAIVKGIKEAVELLDHKIEVGLLCIGdtgHDAAPIKESA 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1A4L_C 164 ELCKKYNQKtVVAMDLAGDETIegsslFPGHVEAYEGAVKNGIHRTVHAGEVGSPEVVRE---AVDILKTERVGHGYHTI 240
Cdd:PTZ00124 184 DFCLKHKAD-FVGFDHAGHEVD-----LKPFKDIFDYVREAGVNLTVHAGEDVTLPNLNTlysAIQVLKVKRIGHGIRVA 257
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1A4L_C 241 EDEALYNRLLKENMHFEVCPWSSYLTGAWDPKTTHAVVRFKNDKANYSLNTDDPLIFKSTLDTDYQMTKKDMGFTEEEFK 320
Cdd:PTZ00124 258 ESQELIDMVKEKDILLEVCPISNVLLNNAKSMDTHPIRKLYDAGVKVSVNSDDPGMFLTNINDDYEELYTHLNFTLADFM 337
|
330
....*....|..
1A4L_C 321 RLNINAAKSSFL 332
Cdd:PTZ00124 338 KMNEWALEKSFL 349
|
|
| metallo-dependent_hydrolases |
cd01292 |
Superfamily of metallo-dependent hydrolases (also called amidohydrolase superfamily) is a ... |
8-328 |
3.18e-26 |
|
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: 105.49 E-value: 3.18e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1A4L_C 8 KVELHVHLDGAIKPETILYFGKKRGIALpadtveelrniigmdkplslpgflakfdyympviagCREAIKRIAYEFVEMK 87
Cdd:cd01292 1 FIDTHVHLDGSALRGTRLNLELKEAEEL------------------------------------SPEDLYEDTLRALEAL 44
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1A4L_C 88 AKEGVVYVEVRYSPHLlanskvdpmpwnqtegDVTPDDVVDLVNQGLQEGEqafGIKVRSILCCMRHQPSWSLE----VL 163
Cdd:cd01292 45 LAGGVTTVVDMGSTPP----------------PTTTKAAIEAVAEAARASA---GIRVVLGLGIPGVPAAVDEDaealLL 105
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1A4L_C 164 ELCKKYNQKTVVAMDLAGDETIEGSSlFPGHVEAYEGAVKNGIHRTVHAGEVGSP-EVVREAVDILKTE---RVGHGYHT 239
Cdd:cd01292 106 ELLRRGLELGAVGLKLAGPYTATGLS-DESLRRVLEEARKLGLPVVIHAGELPDPtRALEDLVALLRLGgrvVIGHVSHL 184
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1A4L_C 240 ieDEALYNRLLKENMHFEVCPWSSYLTGaWDPKTTHAVVRFKNDKANYSLNTDDPLIF-KSTLDTDYQMTKKDM--GFTE 316
Cdd:cd01292 185 --DPELLELLKEAGVSLEVCPLSNYLLG-RDGEGAEALRRLLELGIRVTLGTDGPPHPlGTDLLALLRLLLKVLrlGLSL 261
|
330
....*....|...
1A4L_C 317 EEFKRL-NINAAK 328
Cdd:cd01292 262 EEALRLaTINPAR 274
|
|
| ADGF |
cd01321 |
Adenosine deaminase-related growth factors (ADGF), a novel family of secreted growth-factors ... |
11-333 |
6.10e-11 |
|
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: 62.68 E-value: 6.10e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1A4L_C 11 LHVHLDGAIKPETILYFGKKRgialpadtveeLRNIIGMdkplsLPGFLAkfdyYMPVIagcREAIKRIAYEFVEmkakE 90
Cdd:cd01321 30 LHVHDTAMVSSDWLIKNATYR-----------FEQIFDI-----IDGLLT----YLPIF---RDYYRRLLEELYE----D 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1A4L_C 91 GVVYVEVRYSPhllanskvdPMPWNQTEGDVTPDDVVDL----VNQGLQEGEQAFGIKVrsILCCMRH-QPSWSLEVLEL 165
Cdd:cd01321 83 NVQYVELRSSF---------SPLYDLDGREYDYEETVQLleevVEKFKKTHPDFIGLKI--IYATLRNfNDSEIKESMEQ 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1A4L_C 166 CKKYNQK---TVVAMDLAGDETiEGSSLFPgHVEAYEGAVKNG--IHRTVHAGE---VGSpEVVREAVD--ILKTERVGH 235
Cdd:cd01321 152 CLNLKKKfpdFIAGFDLVGQED-AGRPLLD-FLPQLLWFPKQCaeIPFFFHAGEtngDGT-ETDENLVDalLLNTKRIGH 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1A4L_C 236 GYHTIEDEALYNRLLKENMHFEVCPWSS-YLTGAWDPKtTHAVVRFKNDKANYSLNTDDPLIFKST-LDTD-YQMTkkdM 312
Cdd:cd01321 229 GFALPKHPLLMDLVKKKNIAIEVCPISNqVLGLVSDLR-NHPAAALLARGVPVVISSDDPGFWGAKgLSHDfYQAF---M 304
|
330 340
....*....|....*....|....*.
1A4L_C 313 GFTEEEF-----KRLNINAAKSSFLP 333
Cdd:cd01321 305 GLAPADAglrglKQLAENSIRYSALS 330
|
|
| adm_rel |
TIGR01431 |
adenosine deaminase-related growth factor; Members of this family have been described as ... |
163-333 |
7.66e-06 |
|
adenosine deaminase-related growth factor; Members of this family have been described as secreted proteins with growth factor activity and regions of adenosine deaminase homology in insects, mollusks, and vertebrates.
Pssm-ID: 273620 [Multi-domain] Cd Length: 479 Bit Score: 47.48 E-value: 7.66e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1A4L_C 163 LELCKKYNQKtVVAMDLAGDETiEGSSLFPGHVEAYEGAVKNGIHRTVHAGEVGS--PEVVREAVD--ILKTERVGHGYH 238
Cdd:TIGR01431 280 MGLRIKYPDF-VAGFDLVGQED-TGHSLLDYKDALLIPSIGVKLPYFFHAGETNWqgTSVDRNLLDalLLNTTRIGHGFA 357
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1A4L_C 239 TIEDEALYNRLLKENMHFEVCPWSSYLTGAWDPKTTHAVVRFKNDKANYSLNTDDPLIFKST-LDTDYQMT-------KK 310
Cdd:TIGR01431 358 LSKHPAVRTYSKERDIPIEVCPISNQVLKLVSDLRNHPVATLMADNYPMVISSDDPAFWGAKgLSYDFYEAfmgiagmKA 437
|
170 180
....*....|....*....|...
1A4L_C 311 DMGFteeeFKRLNINAAKSSFLP 333
Cdd:TIGR01431 438 DLRT----LKQLALNSIKYSALS 456
|
|
| |
