|
Name |
Accession |
Description |
Interval |
E-value |
| ADA |
cd01320 |
Adenosine deaminase (ADA) is a monomeric zinc dependent enzyme which catalyzes the ... |
12-342 |
5.06e-164 |
|
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: 461.67 E-value: 5.06e-164
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111863 12 KLPKCEHHVHLEGCLSPDLVFRLAKKNGITLPSDDAAyttPSTLLASYEHFGCLDDFLRYYYIAVSVLIEASDFEALAYE 91
Cdd:cd01320 1 NLPKAELHLHLDGSLRPETILELAKKNGITLPASDVE---LLELVVAAYNFSDLQDFLAKYDFGLSVLQTEEDFERLAYE 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111863 92 YFSIAHSQGVHHAEVFFDPQTHTSRGISYDVVVSGFSAACERANRDFGMSTNLIMCFLRHLPSEAAHETFAEALKRNDFE 171
Cdd:cd01320 78 YLEDAAADGVVYAEIRFSPQLHTRRGLSFDEVVEAVLRGLDEAEAEFGIKARLILCGLRHLSPESAQETLELALKYRDKG 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111863 172 ngiVAGVGLDSSEVDFPPELFQEVYKLAAEKGIRRTGHAGEEGDPSYIRSGLDNLSLQRIDHGIRLVEDKELMKRVAEEN 251
Cdd:cd01320 158 ---VVGFDLAGDEVGFPPEKFVRAFQRAREAGLRLTAHAGEAGGPESVRDALDLLGAERIGHGIRAIEDPELVKRLAERN 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111863 252 IMLTMCPLSNLKLRCVNSIAELPVREFLEAGVPFSINCDDPAYFGGYTLENYFAIQKHFNLTVKEWVFIANAAINGSWIS 331
Cdd:cd01320 235 IPLEVCPTSNVQTGAVKSLAEHPLRELLDAGVKVTINTDDPTVFGTYLTDEYELLAEAFGLTEEELKKLARNAVEASFLS 314
|
330
....*....|.
gi 19111863 332 GKRKEELLSSV 342
Cdd:cd01320 315 EEEKAELLKRI 325
|
|
| Add |
COG1816 |
Adenosine deaminase [Nucleotide transport and metabolism]; Adenosine deaminase is part of the ... |
14-346 |
3.69e-135 |
|
Adenosine deaminase [Nucleotide transport and metabolism]; Adenosine deaminase is part of the Pathway/BioSystem: Menaquinone biosynthesis
Pssm-ID: 441421 Cd Length: 326 Bit Score: 388.29 E-value: 3.69e-135
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111863 14 PKCEHHVHLEGCLSPDLVFRLAKKNGITLPsddaaYTTPSTLLASYeHFGCLDDFLRYYYIAVSVLIEASDFEALAYEYF 93
Cdd:COG1816 1 PKAELHLHLEGSLRPETLLELAARNGIDLP-----AADVEELRAAY-DFRDLQSFLDTYDAGAAVLQTEEDFRRLAYEYL 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111863 94 SIAHSQGVHHAEVFFDPQTHTSRGISYDVVVSGFSAACERANRDFGMSTNLIMCFLRHLPSEAAHETFAEALK-RNDFen 172
Cdd:COG1816 75 EDAAADGVRYAEIRFDPQLHTRRGLSLEEVVEAVLDGLREAEREFGISVRLILCALRHLSPEAAFETLELALRyRDRG-- 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111863 173 giVAGVGLDSSEVDFPPELFQEVYKLAAEKGIRRTGHAGEEGDPSYIRSGLDNLSLQRIDHGIRLVEDKELMKRVAEENI 252
Cdd:COG1816 153 --VVGFGLAGDERGFPPEKFAEAFARAREAGLHLTAHAGEAGGPESIWEALDLLGAERIGHGVRAIEDPALVARLADRGI 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111863 253 MLTMCPLSNLKLRCVNSIAELPVREFLEAGVPFSINCDDPAYFGGYTLENYFAIQKHFNLTVKEWVFIANAAINGSWISG 332
Cdd:COG1816 231 PLEVCPTSNVQLGVVPSLAEHPLRRLLDAGVRVTLNTDDPLYFGTTLTDEYELAAEAFGLSDADLAQLARNAIEASFLPE 310
|
330
....*....|....
gi 19111863 333 KRKEELLSSVQKCV 346
Cdd:COG1816 311 EEKAALLAELDAYF 324
|
|
| aden_deam |
TIGR01430 |
adenosine deaminase; This family includes the experimentally verified adenosine deaminases of ... |
13-342 |
1.07e-134 |
|
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: 387.10 E-value: 1.07e-134
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111863 13 LPKCEHHVHLEGCLSPDLVFRLAKKNGITLPSDDAAYTTPstlLASYEHFGCLDDFLRYYYIAVSVLIEASDFEALAYEY 92
Cdd:TIGR01430 1 LPKAELHLHLEGSIRPETLLELAQKNGIPLPADLQSGEEL---KEAYDKFRDLQDFLAKYDFGVEVLRTEDDFKRLAYEY 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111863 93 FSIAHSQGVHHAEVFFDPQTHTSRGISYDVVVSGFSAACERANRDFGMSTNLIMCFLRHLPSEAAHETFAEALKrndFEN 172
Cdd:TIGR01430 78 VEKAAKDGVVYAEVFFDPQLHTNRGISPDTVVEAVLDGLDEAERDFGIKSRLILCGMRHKQPEAAEETLELAKP---YKE 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111863 173 GIVAGVGLDSSEVDFPPELFQEVYKLAAEKGIRRTGHAGEEGDPSYIRSGLDNLSLQRIDHGIRLVEDKELMKRVAEENI 252
Cdd:TIGR01430 155 QTIVGFGLAGDERGGPPPDFVRAFAIARELGLHLTVHAGELGGPESVREALDDLGATRIGHGVRALEDPELLKRLAQENI 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111863 253 MLTMCPLSNLKLRCVNSIAELPVREFLEAGVPFSINCDDPAYFGGYTLENYFAIQKHFNLTVKEWVFIANAAINGSWISG 332
Cdd:TIGR01430 235 TLEVCPTSNVALGVVKSLAEHPLRRFLEAGVKVTLNSDDPAYFGSYLTEEYEIAAKHAGLTEEELKQLARNALEGSFLSD 314
|
330
....*....|
gi 19111863 333 KRKEELLSSV 342
Cdd:TIGR01430 315 DEKKELLAKL 324
|
|
| PRK09358 |
PRK09358 |
adenosine deaminase; Provisional |
5-344 |
1.76e-126 |
|
adenosine deaminase; Provisional
Pssm-ID: 236480 Cd Length: 340 Bit Score: 366.81 E-value: 1.76e-126
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111863 5 PIYNFIRKLPKCEHHVHLEGCLSPDLVFRLAKKNGITLPSDDAAYTTPstlLASYEHFGCLDDFLRYYYIAVSVLIEASD 84
Cdd:PRK09358 2 NLLMIIRSLPKAELHLHLDGSLRPETILELARRNGIALPATDVEELPW---VRAAYDFRDLQSFLDKYDAGVAVLQTEED 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111863 85 FEALAYEYFSIAHSQGVHHAEVFFDPQTHTSRGISYDVVVSGFSAACERANRDFGMSTNLIMCFLRHLPSEAAHETFAEA 164
Cdd:PRK09358 79 LRRLAFEYLEDAAADGVVYAEIRFDPQLHTERGLPLEEVVEAVLDGLRAAEAEFGISVRLILCFMRHFGEEAAARELEAL 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111863 165 LKRndFENGIVAGVGLDSSEVDFPPELFQEVYKLAAEKGIRRTGHAGEEGDPSYIRSGLDNLSLQRIDHGIRLVEDKELM 244
Cdd:PRK09358 159 AAR--YRDDGVVGFDLAGDELGFPPSKFARAFDRARDAGLRLTAHAGEAGGPESIWEALDELGAERIGHGVRAIEDPALM 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111863 245 KRVAEENIMLTMCPLSNLKLRCVNSIAELPVREFLEAGVPFSINCDDPAYFGGYTLENYFAIQKHFNLTVKEWVFIANAA 324
Cdd:PRK09358 237 ARLADRRIPLEVCPTSNVQTGAVPSLAEHPLKTLLDAGVRVTINTDDPLVFGTTLTEEYEALAEAFGLSDEDLAQLARNA 316
|
330 340
....*....|....*....|
gi 19111863 325 INGSWISGKRKEELLSSVQK 344
Cdd:PRK09358 317 LEAAFLSEEEKAALLAEVDA 336
|
|
| A_deaminase |
pfam00962 |
Adenosine deaminase; |
14-344 |
1.96e-108 |
|
Adenosine deaminase;
Pssm-ID: 425964 Cd Length: 330 Bit Score: 320.53 E-value: 1.96e-108
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111863 14 PKCEHHVHLEGCLSPDLVFRLAKKNGITLPSDDaayttPSTL---LASYEHFGCLDDFLRYYYIAVSVLIEASDFEALAY 90
Cdd:pfam00962 1 PKAELHLHLDGSLRPDTLLELAKRYGIILPADF-----PEALeplFRKYKKERDLQDFLDKYDIGVAVLRSPEDIRRLAF 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111863 91 EYFSIAHSQGVHHAEVFFDPQTHTSRGISYDVVVSGFSAACERANRDFGMSTNLIMCFLRHLPSEAAHETfAEALKRndF 170
Cdd:pfam00962 76 EYAEDVAKDGVVYAEVRYDPQSHASRGLSPDTVVDAVLDAVDAAEREFGITVRLIVCAMRHEHPECSREI-AELAPR--Y 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111863 171 ENGIVAGVGLDSSEVDFPPELFQ---EVYKLAAEKGIRRTGHAGEEGDPSYIRSGLDNLSLQRIDHGIRLVEDKELMKRV 247
Cdd:pfam00962 153 RDQGIVAFGLAGDEKGFPPSLFRdhvEAFARARDAGLHLTVHAGEAGGPQSVWEALDDLGAERIGHGVRSAEDPRLLDRL 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111863 248 AEENIMLTMCPLSNLKLRCVNSIAELPVREFLEAGVPFSINCDDPAYFGGYTLENYFAIQKHFNLTVKEWVFIANAAING 327
Cdd:pfam00962 233 ADRQIPLEICPTSNVQTGAVASLAEHPLKTFLRAGVPVSLNTDDPLMFGSDLLDEYQVAKRAPGFDEEELARLAKNAVKG 312
|
330
....*....|....*..
gi 19111863 328 SWISGKRKEELLSSVQK 344
Cdd:pfam00962 313 SFLPADEKRALLDEVDK 329
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| ADA |
cd01320 |
Adenosine deaminase (ADA) is a monomeric zinc dependent enzyme which catalyzes the ... |
12-342 |
5.06e-164 |
|
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: 461.67 E-value: 5.06e-164
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111863 12 KLPKCEHHVHLEGCLSPDLVFRLAKKNGITLPSDDAAyttPSTLLASYEHFGCLDDFLRYYYIAVSVLIEASDFEALAYE 91
Cdd:cd01320 1 NLPKAELHLHLDGSLRPETILELAKKNGITLPASDVE---LLELVVAAYNFSDLQDFLAKYDFGLSVLQTEEDFERLAYE 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111863 92 YFSIAHSQGVHHAEVFFDPQTHTSRGISYDVVVSGFSAACERANRDFGMSTNLIMCFLRHLPSEAAHETFAEALKRNDFE 171
Cdd:cd01320 78 YLEDAAADGVVYAEIRFSPQLHTRRGLSFDEVVEAVLRGLDEAEAEFGIKARLILCGLRHLSPESAQETLELALKYRDKG 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111863 172 ngiVAGVGLDSSEVDFPPELFQEVYKLAAEKGIRRTGHAGEEGDPSYIRSGLDNLSLQRIDHGIRLVEDKELMKRVAEEN 251
Cdd:cd01320 158 ---VVGFDLAGDEVGFPPEKFVRAFQRAREAGLRLTAHAGEAGGPESVRDALDLLGAERIGHGIRAIEDPELVKRLAERN 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111863 252 IMLTMCPLSNLKLRCVNSIAELPVREFLEAGVPFSINCDDPAYFGGYTLENYFAIQKHFNLTVKEWVFIANAAINGSWIS 331
Cdd:cd01320 235 IPLEVCPTSNVQTGAVKSLAEHPLRELLDAGVKVTINTDDPTVFGTYLTDEYELLAEAFGLTEEELKKLARNAVEASFLS 314
|
330
....*....|.
gi 19111863 332 GKRKEELLSSV 342
Cdd:cd01320 315 EEEKAELLKRI 325
|
|
| Add |
COG1816 |
Adenosine deaminase [Nucleotide transport and metabolism]; Adenosine deaminase is part of the ... |
14-346 |
3.69e-135 |
|
Adenosine deaminase [Nucleotide transport and metabolism]; Adenosine deaminase is part of the Pathway/BioSystem: Menaquinone biosynthesis
Pssm-ID: 441421 Cd Length: 326 Bit Score: 388.29 E-value: 3.69e-135
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111863 14 PKCEHHVHLEGCLSPDLVFRLAKKNGITLPsddaaYTTPSTLLASYeHFGCLDDFLRYYYIAVSVLIEASDFEALAYEYF 93
Cdd:COG1816 1 PKAELHLHLEGSLRPETLLELAARNGIDLP-----AADVEELRAAY-DFRDLQSFLDTYDAGAAVLQTEEDFRRLAYEYL 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111863 94 SIAHSQGVHHAEVFFDPQTHTSRGISYDVVVSGFSAACERANRDFGMSTNLIMCFLRHLPSEAAHETFAEALK-RNDFen 172
Cdd:COG1816 75 EDAAADGVRYAEIRFDPQLHTRRGLSLEEVVEAVLDGLREAEREFGISVRLILCALRHLSPEAAFETLELALRyRDRG-- 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111863 173 giVAGVGLDSSEVDFPPELFQEVYKLAAEKGIRRTGHAGEEGDPSYIRSGLDNLSLQRIDHGIRLVEDKELMKRVAEENI 252
Cdd:COG1816 153 --VVGFGLAGDERGFPPEKFAEAFARAREAGLHLTAHAGEAGGPESIWEALDLLGAERIGHGVRAIEDPALVARLADRGI 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111863 253 MLTMCPLSNLKLRCVNSIAELPVREFLEAGVPFSINCDDPAYFGGYTLENYFAIQKHFNLTVKEWVFIANAAINGSWISG 332
Cdd:COG1816 231 PLEVCPTSNVQLGVVPSLAEHPLRRLLDAGVRVTLNTDDPLYFGTTLTDEYELAAEAFGLSDADLAQLARNAIEASFLPE 310
|
330
....*....|....
gi 19111863 333 KRKEELLSSVQKCV 346
Cdd:COG1816 311 EEKAALLAELDAYF 324
|
|
| aden_deam |
TIGR01430 |
adenosine deaminase; This family includes the experimentally verified adenosine deaminases of ... |
13-342 |
1.07e-134 |
|
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: 387.10 E-value: 1.07e-134
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111863 13 LPKCEHHVHLEGCLSPDLVFRLAKKNGITLPSDDAAYTTPstlLASYEHFGCLDDFLRYYYIAVSVLIEASDFEALAYEY 92
Cdd:TIGR01430 1 LPKAELHLHLEGSIRPETLLELAQKNGIPLPADLQSGEEL---KEAYDKFRDLQDFLAKYDFGVEVLRTEDDFKRLAYEY 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111863 93 FSIAHSQGVHHAEVFFDPQTHTSRGISYDVVVSGFSAACERANRDFGMSTNLIMCFLRHLPSEAAHETFAEALKrndFEN 172
Cdd:TIGR01430 78 VEKAAKDGVVYAEVFFDPQLHTNRGISPDTVVEAVLDGLDEAERDFGIKSRLILCGMRHKQPEAAEETLELAKP---YKE 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111863 173 GIVAGVGLDSSEVDFPPELFQEVYKLAAEKGIRRTGHAGEEGDPSYIRSGLDNLSLQRIDHGIRLVEDKELMKRVAEENI 252
Cdd:TIGR01430 155 QTIVGFGLAGDERGGPPPDFVRAFAIARELGLHLTVHAGELGGPESVREALDDLGATRIGHGVRALEDPELLKRLAQENI 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111863 253 MLTMCPLSNLKLRCVNSIAELPVREFLEAGVPFSINCDDPAYFGGYTLENYFAIQKHFNLTVKEWVFIANAAINGSWISG 332
Cdd:TIGR01430 235 TLEVCPTSNVALGVVKSLAEHPLRRFLEAGVKVTLNSDDPAYFGSYLTEEYEIAAKHAGLTEEELKQLARNALEGSFLSD 314
|
330
....*....|
gi 19111863 333 KRKEELLSSV 342
Cdd:TIGR01430 315 DEKKELLAKL 324
|
|
| PRK09358 |
PRK09358 |
adenosine deaminase; Provisional |
5-344 |
1.76e-126 |
|
adenosine deaminase; Provisional
Pssm-ID: 236480 Cd Length: 340 Bit Score: 366.81 E-value: 1.76e-126
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111863 5 PIYNFIRKLPKCEHHVHLEGCLSPDLVFRLAKKNGITLPSDDAAYTTPstlLASYEHFGCLDDFLRYYYIAVSVLIEASD 84
Cdd:PRK09358 2 NLLMIIRSLPKAELHLHLDGSLRPETILELARRNGIALPATDVEELPW---VRAAYDFRDLQSFLDKYDAGVAVLQTEED 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111863 85 FEALAYEYFSIAHSQGVHHAEVFFDPQTHTSRGISYDVVVSGFSAACERANRDFGMSTNLIMCFLRHLPSEAAHETFAEA 164
Cdd:PRK09358 79 LRRLAFEYLEDAAADGVVYAEIRFDPQLHTERGLPLEEVVEAVLDGLRAAEAEFGISVRLILCFMRHFGEEAAARELEAL 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111863 165 LKRndFENGIVAGVGLDSSEVDFPPELFQEVYKLAAEKGIRRTGHAGEEGDPSYIRSGLDNLSLQRIDHGIRLVEDKELM 244
Cdd:PRK09358 159 AAR--YRDDGVVGFDLAGDELGFPPSKFARAFDRARDAGLRLTAHAGEAGGPESIWEALDELGAERIGHGVRAIEDPALM 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111863 245 KRVAEENIMLTMCPLSNLKLRCVNSIAELPVREFLEAGVPFSINCDDPAYFGGYTLENYFAIQKHFNLTVKEWVFIANAA 324
Cdd:PRK09358 237 ARLADRRIPLEVCPTSNVQTGAVPSLAEHPLKTLLDAGVRVTINTDDPLVFGTTLTEEYEALAEAFGLSDEDLAQLARNA 316
|
330 340
....*....|....*....|
gi 19111863 325 INGSWISGKRKEELLSSVQK 344
Cdd:PRK09358 317 LEAAFLSEEEKAALLAEVDA 336
|
|
| A_deaminase |
pfam00962 |
Adenosine deaminase; |
14-344 |
1.96e-108 |
|
Adenosine deaminase;
Pssm-ID: 425964 Cd Length: 330 Bit Score: 320.53 E-value: 1.96e-108
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111863 14 PKCEHHVHLEGCLSPDLVFRLAKKNGITLPSDDaayttPSTL---LASYEHFGCLDDFLRYYYIAVSVLIEASDFEALAY 90
Cdd:pfam00962 1 PKAELHLHLDGSLRPDTLLELAKRYGIILPADF-----PEALeplFRKYKKERDLQDFLDKYDIGVAVLRSPEDIRRLAF 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111863 91 EYFSIAHSQGVHHAEVFFDPQTHTSRGISYDVVVSGFSAACERANRDFGMSTNLIMCFLRHLPSEAAHETfAEALKRndF 170
Cdd:pfam00962 76 EYAEDVAKDGVVYAEVRYDPQSHASRGLSPDTVVDAVLDAVDAAEREFGITVRLIVCAMRHEHPECSREI-AELAPR--Y 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111863 171 ENGIVAGVGLDSSEVDFPPELFQ---EVYKLAAEKGIRRTGHAGEEGDPSYIRSGLDNLSLQRIDHGIRLVEDKELMKRV 247
Cdd:pfam00962 153 RDQGIVAFGLAGDEKGFPPSLFRdhvEAFARARDAGLHLTVHAGEAGGPQSVWEALDDLGAERIGHGVRSAEDPRLLDRL 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111863 248 AEENIMLTMCPLSNLKLRCVNSIAELPVREFLEAGVPFSINCDDPAYFGGYTLENYFAIQKHFNLTVKEWVFIANAAING 327
Cdd:pfam00962 233 ADRQIPLEICPTSNVQTGAVASLAEHPLKTFLRAGVPVSLNTDDPLMFGSDLLDEYQVAKRAPGFDEEELARLAKNAVKG 312
|
330
....*....|....*..
gi 19111863 328 SWISGKRKEELLSSVQK 344
Cdd:pfam00962 313 SFLPADEKRALLDEVDK 329
|
|
| ADA_AMPD |
cd00443 |
Adenosine/AMP deaminase. Adenosine deaminases (ADAs) are present in pro- and eukaryotic ... |
13-339 |
2.14e-38 |
|
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: 139.40 E-value: 2.14e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111863 13 LPKCEHHVHLEGCLSPDLVFRLAKKngitlpsddaayttpstllasyehfGCLDDFLRYYyiavSVLIEASDFEALAYEY 92
Cdd:cd00443 1 LPKVELHAHLSGSISPETLLELIKK-------------------------EFFEKFLLVH----NLLQKGEALARALKEV 51
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111863 93 FSIAHSQGVHHAEVFFDPQ-THTSRGISY----DVVVSGFSAAcERANRdfGMSTNLIMCFLRHLPSEAAHETFAEALKR 167
Cdd:cd00443 52 IEEFAEDNVQYLELRTTPRlLETEKGLTKeqywLLVIEGISEA-KQWFP--PIKVRLILSVDRRGPYVQNYLVASEILEL 128
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111863 168 NDFENGIVAG---VGLDSSEVDFPPELFQEVYKLAAEKGIRRTGHAGEEGDPSYIRSGLDnLSLQRIDHGIRLVEDKELM 244
Cdd:cd00443 129 AKFLSNYVVGidlVGDESKGENPLRDFYSYYEYARRLGLLGLTLHCGETGNREELLQALL-LLPDRIGHGIFLLKHPELI 207
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111863 245 KRVAEENIMLTMCPLSNLKLRCVNSIAELPVREFLEAGVPFSINCDDPAYFGGYTLENYFAIQKHFNLTVKEWVFIANAA 324
Cdd:cd00443 208 YLVKLRNIPIEVCPTSNVVLGTVQSYEKHPFMRFFKAGLPVSLSTDDPGIFGTSLSEEYSLAAKTFGLTFEDLCELNRNS 287
|
330
....*....|....*
gi 19111863 325 INGSWISGKRKEELL 339
Cdd:cd00443 288 VLSSFAKDEEKKSLL 302
|
|
| PTZ00124 |
PTZ00124 |
adenosine deaminase; Provisional |
1-340 |
2.61e-31 |
|
adenosine deaminase; Provisional
Pssm-ID: 173415 Cd Length: 362 Bit Score: 121.51 E-value: 2.61e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111863 1 MSNLPIYNFIRKLPKCEHHVHLEGCLSPDLVFRLAKKngitlpSDDAAYTTPSTLLASY---EHFGCLDDFLRYYYIAVS 77
Cdd:PTZ00124 23 MDKKERYKIWKRIPKCELHCHLDLCFSVDFFLSCIRK------YNLQPNLSDEEILDYYlfaKGGKSLGEFVEKAIRVAD 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111863 78 VLIEASDFEALAYEYFSIAHSQGVHHAEVFFDPqTHTSRGISYDV------VVSGFSAACERANRDFGMStnlIMCF--- 148
Cdd:PTZ00124 97 IFNDYEVIEDLAKHAVFNKYKEGVVLMEFRYSP-TFVAFKHNLDIdlihqaIVKGIKEAVELLDHKIEVG---LLCIgdt 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111863 149 -LRHLPSEAAHETFAEalKRNDFengivagVGLDSS--EVDFPPelFQEVYKLAAEKGIRRTGHAGEEGDP---SYIRSG 222
Cdd:PTZ00124 173 gHDAAPIKESADFCLK--HKADF-------VGFDHAghEVDLKP--FKDIFDYVREAGVNLTVHAGEDVTLpnlNTLYSA 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111863 223 LDNLSLQRIDHGIRLVEDKELMKRVAEENIMLTMCPLSNLKLRCVNSIAELPVREFLEAGVPFSINCDDPAYFGGYTLEN 302
Cdd:PTZ00124 242 IQVLKVKRIGHGIRVAESQELIDMVKEKDILLEVCPISNVLLNNAKSMDTHPIRKLYDAGVKVSVNSDDPGMFLTNINDD 321
|
330 340 350
....*....|....*....|....*....|....*...
gi 19111863 303 YFAIQKHFNLTVKEWVFIANAAINGSWISGKRKEELLS 340
Cdd:PTZ00124 322 YEELYTHLNFTLADFMKMNEWALEKSFLDKDIKLKIKK 359
|
|
| ADGF |
cd01321 |
Adenosine deaminase-related growth factors (ADGF), a novel family of secreted growth-factors ... |
1-307 |
2.51e-21 |
|
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: 93.49 E-value: 2.51e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111863 1 MSNLPIYNFIRKLPKCEH-HVHLEGCLSPDLVFRLAKKngitlpsddaayttpstllASYEHFGCLDDFLRYYYIavsvl 79
Cdd:cd01321 12 IENSTLFKIIQKMPKGALlHVHDTAMVSSDWLIKNATY-------------------RFEQIFDIIDGLLTYLPI----- 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111863 80 ieasdFEALAYEYFSIAHSQGVHHAEV---FFDPQTHTSRGISYDvvvsGFSAACERANRDFgMSTN-------LIMCFL 149
Cdd:cd01321 68 -----FRDYYRRLLEELYEDNVQYVELrssFSPLYDLDGREYDYE----ETVQLLEEVVEKF-KKTHpdfiglkIIYATL 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111863 150 RHLPSEAAHETFAEALK-RNDFENgIVAGVGLDSSE------VDFPPELFQevyklaaekgIRRTG-------HAGE-EG 214
Cdd:cd01321 138 RNFNDSEIKESMEQCLNlKKKFPD-FIAGFDLVGQEdagrplLDFLPQLLW----------FPKQCaeipfffHAGEtNG 206
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111863 215 DPSYIRSGL-DNLSLQ--RIDHGIRLVEDKELMKRVAEENIMLTMCPLSNLKLRCVNSIAELPVREFLEAGVPFSINCDD 291
Cdd:cd01321 207 DGTETDENLvDALLLNtkRIGHGFALPKHPLLMDLVKKKNIAIEVCPISNQVLGLVSDLRNHPAAALLARGVPVVISSDD 286
|
330
....*....|....*...
gi 19111863 292 PAYFG--GYTLENYFAIQ 307
Cdd:cd01321 287 PGFWGakGLSHDFYQAFM 304
|
|
| metallo-dependent_hydrolases |
cd01292 |
Superfamily of metallo-dependent hydrolases (also called amidohydrolase superfamily) is a ... |
146-300 |
2.12e-12 |
|
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: 66.59 E-value: 2.12e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111863 146 MCFLRHLPSEAAHETFAEALKRndFENGIVAGVGLDSSE--VDFPPELFQEVYKLAAEKGIRRTGHAGEEGDPSY----- 218
Cdd:cd01292 89 IPGVPAAVDEDAEALLLELLRR--GLELGAVGLKLAGPYtaTGLSDESLRRVLEEARKLGLPVVIHAGELPDPTRaledl 166
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111863 219 IRSGLDNLSLqRIDHGIRLveDKELMKRVAEENIMLTMCPLSNLKLrCVNSIAELPVREFLEAGVPFSINCDDPAYFGGY 298
Cdd:cd01292 167 VALLRLGGRV-VIGHVSHL--DPELLELLKEAGVSLEVCPLSNYLL-GRDGEGAEALRRLLELGIRVTLGTDGPPHPLGT 242
|
..
gi 19111863 299 TL 300
Cdd:cd01292 243 DL 244
|
|
| ATZ_TRZ_like |
cd01298 |
TRZ/ATZ family contains enzymes from the atrazine degradation pathway and related hydrolases. ... |
188-293 |
5.77e-09 |
|
TRZ/ATZ family contains enzymes from the atrazine degradation pathway and related hydrolases. Atrazine, a chlorinated herbizide, can be catabolized by a variety of different bacteria. The first three steps of the atrazine dehalogenation pathway are catalyzed by atrazine chlorohydrolase (AtzA), hydroxyatrazine ethylaminohydrolase (AtzB), and N-isopropylammelide N-isopropylaminohydrolase (AtzC). All three enzymes belong to the superfamily of metal dependent hydrolases. AtzA and AtzB, beside other related enzymes are represented in this CD.
Pssm-ID: 238623 [Multi-domain] Cd Length: 411 Bit Score: 57.21 E-value: 5.77e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111863 188 PPELFQEVYKLAAEKGIRRTGHAGE---EGDPSYIRSGLDNLS-LQRID---------HGIrLVEDKElMKRVAEENIML 254
Cdd:cd01298 192 SDELLREVAELAREYGVPLHIHLAEtedEVEESLEKYGKRPVEyLEELGllgpdvvlaHCV-WLTDEE-IELLAETGTGV 269
|
90 100 110
....*....|....*....|....*....|....*....
gi 19111863 255 TMCPLSNLKLrcVNSIAelPVREFLEAGVPFSINCDDPA 293
Cdd:cd01298 270 AHNPASNMKL--ASGIA--PVPEMLEAGVNVGLGTDGAA 304
|
|
| SsnA |
COG0402 |
Cytosine/adenosine deaminase or related metal-dependent hydrolase [Nucleotide transport and ... |
188-293 |
7.46e-08 |
|
Cytosine/adenosine deaminase or related metal-dependent hydrolase [Nucleotide transport and metabolism, General function prediction only]; Cytosine/adenosine deaminase or related metal-dependent hydrolase is part of the Pathway/BioSystem: Pyrimidine salvage
Pssm-ID: 440171 [Multi-domain] Cd Length: 416 Bit Score: 53.68 E-value: 7.46e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111863 188 PPELFQEVYKLAAEKGIRRTGHAGE---EGDPSYIRSGLDNLS-LQRID---------HGIRLvEDKElMKRVAEENIML 254
Cdd:COG0402 200 SPELLRAAAALARELGLPLHTHLAEtrdEVEWVLELYGKRPVEyLDELGllgprtllaHCVHL-TDEE-IALLAETGASV 277
|
90 100 110
....*....|....*....|....*....|....*....
gi 19111863 255 TMCPLSNLKLRcvNSIAelPVREFLEAGVPFSINCDDPA 293
Cdd:COG0402 278 AHCPTSNLKLG--SGIA--PVPRLLAAGVRVGLGTDGAA 312
|
|
| AMPD |
cd01319 |
AMP deaminase (AMPD) catalyzes the hydrolytic deamination of adensosine monophosphate (AMP) at ... |
209-339 |
3.17e-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: 48.90 E-value: 3.17e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111863 209 HAGEEGDPSYIRSGLdnLSLQRIDHGIRLVEDKELMKRVAEENIMLTMCPLSNLKLRCvnSIAELPVREFLEAGVPFSIN 288
Cdd:cd01319 332 HCGEAGDIDHLASAF--LLAHGISHGINLRKVPVLQYLYYLTQIGIAMSPLSNNSLFL--SYEKNPFPEFFKRGLNVSLS 407
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 19111863 289 CDDPAYFgGYT----LENYFAIQKHFNLTVKEWVFIANAAINGSWISGKRKEELL 339
Cdd:cd01319 408 TDDPLQF-HFTkeplMEEYSIAAQVWKLSTCDMCELARNSVLQSGFEHSIKRHWL 461
|
|
| PRK07228 |
PRK07228 |
5'-deoxyadenosine deaminase; |
189-292 |
2.90e-05 |
|
5'-deoxyadenosine deaminase;
Pssm-ID: 180895 [Multi-domain] Cd Length: 445 Bit Score: 45.76 E-value: 2.90e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111863 189 PELFQEVYKLAAEKGIRRTGHAGEEGDPSYI---RSGLDN------LSLQRID----HGIRLveDKELMKRVAEENIMLT 255
Cdd:PRK07228 198 EELLRGVRDLADEYGVRIHTHASENRGEIETveeETGMRNihyldeVGLTGEDlilaHCVWL--DEEEREILAETGTHVT 275
|
90 100 110
....*....|....*....|....*....|....*..
gi 19111863 256 MCPLSNLKLrcVNSIAelPVREFLEAGVPFSINCDDP 292
Cdd:PRK07228 276 HCPSSNLKL--ASGIA--PVPDLLERGINVALGADGA 308
|
|
| AMP_deaminase |
TIGR01429 |
AMP deaminase; This model describes AMP deaminase, a large, well-conserved eukaryotic protein ... |
209-301 |
7.13e-04 |
|
AMP deaminase; This model describes AMP deaminase, a large, well-conserved eukaryotic protein involved in energy metabolism. Most members of the family have an additional, poorly alignable region of 150 amino acids or more N-terminal to the region included in the model.
Pssm-ID: 273618 [Multi-domain] Cd Length: 611 Bit Score: 41.37 E-value: 7.13e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111863 209 HAGEEGDPSYIRSGLdnLSLQRIDHGIRLVEDKELMKRVAEENIMLTMCPLSNLKLRCvnSIAELPVREFLEAGVPFSIN 288
Cdd:TIGR01429 444 HCGEAGSVDHLVSAF--LTSHGINHGILLRKVPVLQYLYYLTQIPIAMSPLSNNSLFL--EYSKNPLPEYLHKGLNVSLS 519
|
90
....*....|...
gi 19111863 289 CDDPAYFgGYTLE 301
Cdd:TIGR01429 520 TDDPLQF-HYTKE 531
|
|
| Amidohydro_1 |
pfam01979 |
Amidohydrolase family; This family of enzymes are a a large metal dependent hydrolase ... |
162-325 |
1.73e-03 |
|
Amidohydrolase family; This family of enzymes are a a large metal dependent hydrolase superfamily. The family includes Adenine deaminase EC:3.5.4.2 that hydrolyses adenine to form hypoxanthine and ammonia. Adenine deaminases reaction is important for adenine utilization as a purine and also as a nitrogen source. This family also includes dihydroorotase and N-acetylglucosamine-6-phosphate deacetylases, EC:3.5.1.25 These enzymes catalyze the reaction N-acetyl-D-glucosamine 6-phosphate + H2O <=> D-glucosamine 6-phosphate + acetate. This family includes the catalytic domain of urease alpha subunit. Dihydroorotases (EC:3.5.2.3) are also included.
Pssm-ID: 460401 [Multi-domain] Cd Length: 334 Bit Score: 39.79 E-value: 1.73e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111863 162 AEALKRNDFENGIVAGVGLDSSEVDFPPELFQEVYKLAAEKGIRRTGHAGEE-GDPSYIR----------SGLDNL---- 226
Cdd:pfam01979 99 AGAEFIKGMADGVVFVGLAPHGAPTFSDDELKAALEEAKKYGLPVAIHALETkGEVEDAIaafgggiehgTHLEVAesgg 178
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111863 227 ----SLQRIDHGIRLVEDKELMKRVAEENIMLTMCPLSNLKLRcVNSIAelpVREFLEAGVPFSINCDDPAyfGGYTLEN 302
Cdd:pfam01979 179 lldiIKLILAHGVHLSPTEANLLAEHLKGAGVAHCPFSNSKLR-SGRIA---LRKALEDGVKVGLGTDGAG--SGNSLNM 252
|
170 180 190
....*....|....*....|....*....|...
gi 19111863 303 Y----FAIQKHF----NLTVKEWVFIA--NAAI 325
Cdd:pfam01979 253 LeelrLALELQFdpegGLSPLEALRMAtiNPAK 285
|
|
| AMP_deaminase |
pfam19326 |
AMP deaminase; |
209-301 |
4.77e-03 |
|
AMP deaminase;
Pssm-ID: 437158 [Multi-domain] Cd Length: 622 Bit Score: 38.98 E-value: 4.77e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111863 209 HAGEEGDPSYIRSGLdnLSLQRIDHGIRLVEDKELMKRVAEENIMLTMCPLSNlklrcvNSI----AELPVREFLEAGVP 284
Cdd:pfam19326 449 HCGEAGDIDHLVSAF--LLAHGISHGILLRKSPVLQYLYYLAQIGIAMSPLSN------NSLfleyHKNPFPEFFKRGLN 520
|
90
....*....|....*..
gi 19111863 285 FSINCDDPAYFgGYTLE 301
Cdd:pfam19326 521 VSLSTDDPLQF-HFTKE 536
|
|
| PRK12393 |
PRK12393 |
amidohydrolase; Provisional |
188-293 |
4.85e-03 |
|
amidohydrolase; Provisional
Pssm-ID: 237088 [Multi-domain] Cd Length: 457 Bit Score: 38.89 E-value: 4.85e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111863 188 PPELFQEVYKLAAEKGIRRTGHAGEEGDpsYIRSGLDNlslqridHGIRLVE---DKE----------LMKRVAEENIML 254
Cdd:PRK12393 216 PPELLREVARAARGMGLRLHSHLSETVD--YVDFCREK-------YGMTPVQfvaEHDwlgpdvwfahLVKLDAEEIALL 286
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 19111863 255 -------TMCPLSNLKLRcvNSIAelPVREFLEAGVPFSINCDDPA 293
Cdd:PRK12393 287 aqtgtgiAHCPQSNGRLG--SGIA--PALAMEAAGVPVSLGVDGAA 328
|
|
| |
