|
Name |
Accession |
Description |
Interval |
E-value |
| aden_deam |
TIGR01430 |
adenosine deaminase; This family includes the experimentally verified adenosine deaminases of ... |
15-337 |
1.68e-167 |
|
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: 469.15 E-value: 1.68e-167
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284955 15 LPKIELHCHLDGSIRPTTLRTIAEKQNIPLPQDEQALKELVVAPEKCTDLNDYLTRFDFVLTCLQTAEALQAAAYDVISQ 94
Cdd:TIGR01430 1 LPKAELHLHLEGSIRPETLLELAQKNGIPLPADLQSGEELKEAYDKFRDLQDFLAKYDFGVEVLRTEDDFKRLAYEYVEK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284955 95 AAEDGVAYIEVRFAPSQHTEKGLRLPEIVTAVLTGLKQGEEDFGVKSNALLCGMRHDQQQAIEKIVHLAHDFRETGVVGF 174
Cdd:TIGR01430 81 AAKDGVVYAEVFFDPQLHTNRGISPDTVVEAVLDGLDEAERDFGIKSRLILCGMRHKQPEAAEETLELAKPYKEQTIVGF 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284955 175 DLAGNEVDFPPYTFEDVLALANQLSIPLTLHAGEC-GCGKNVADAVTLGATRIGHGIALKDTPEYLALLKEKKVLLEMCP 253
Cdd:TIGR01430 161 GLAGDERGGPPPDFVRAFAIARELGLHLTVHAGELgGPESVREALDDLGATRIGHGVRALEDPELLKRLAQENITLEVCP 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284955 254 TSNFQTGTVKTLAEYPFQQFIEAGLAVCINTDNRTVSDTTLTKEFMKLATWYQLSYDEMKQLTKNALAGAFLSPDEKKLL 333
Cdd:TIGR01430 241 TSNVALGVVKSLAEHPLRRFLEAGVKVTLNSDDPAYFGSYLTEEYEIAAKHAGLTEEELKQLARNALEGSFLSDDEKKEL 320
|
....
gi 488284955 334 NQKI 337
Cdd:TIGR01430 321 LAKL 324
|
|
| ADA |
cd01320 |
Adenosine deaminase (ADA) is a monomeric zinc dependent enzyme which catalyzes the ... |
14-337 |
2.30e-161 |
|
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: 453.58 E-value: 2.30e-161
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284955 14 QLPKIELHCHLDGSIRPTTLRTIAEKQNIPLPQDEQALKELVVAPEKCTDLNDYLTRFDFVLTCLQTAEALQAAAYDVIS 93
Cdd:cd01320 1 NLPKAELHLHLDGSLRPETILELAKKNGITLPASDVELLELVVAAYNFSDLQDFLAKYDFGLSVLQTEEDFERLAYEYLE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284955 94 QAAEDGVAYIEVRFAPSQHTEKGLRLPEIVTAVLTGLKQGEEDFGVKSNALLCGMRHDQQQAIEKIVHLAHDFRETGVVG 173
Cdd:cd01320 81 DAAADGVVYAEIRFSPQLHTRRGLSFDEVVEAVLRGLDEAEAEFGIKARLILCGLRHLSPESAQETLELALKYRDKGVVG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284955 174 FDLAGNEVDFPPYTFEDVLALANQLSIPLTLHAGECGCGKNVADAV-TLGATRIGHGIALKDTPEYLALLKEKKVLLEMC 252
Cdd:cd01320 161 FDLAGDEVGFPPEKFVRAFQRAREAGLRLTAHAGEAGGPESVRDALdLLGAERIGHGIRAIEDPELVKRLAERNIPLEVC 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284955 253 PTSNFQTGTVKTLAEYPFQQFIEAGLAVCINTDNRTVSDTTLTKEFMKLATWYQLSYDEMKQLTKNALAGAFLSPDEKKL 332
Cdd:cd01320 241 PTSNVQTGAVKSLAEHPLRELLDAGVKVTINTDDPTVFGTYLTDEYELLAEAFGLTEEELKKLARNAVEASFLSEEEKAE 320
|
....*
gi 488284955 333 LNQKI 337
Cdd:cd01320 321 LLKRI 325
|
|
| PRK09358 |
PRK09358 |
adenosine deaminase; Provisional |
12-341 |
4.41e-142 |
|
adenosine deaminase; Provisional
Pssm-ID: 236480 Cd Length: 340 Bit Score: 405.33 E-value: 4.41e-142
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284955 12 VRQLPKIELHCHLDGSIRPTTLRTIAEKQNIPLP-QDEQALKElVVAPEKCTDLNDYLTRFDFVLTCLQTAEALQAAAYD 90
Cdd:PRK09358 7 IRSLPKAELHLHLDGSLRPETILELARRNGIALPaTDVEELPW-VRAAYDFRDLQSFLDKYDAGVAVLQTEEDLRRLAFE 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284955 91 VISQAAEDGVAYIEVRFAPSQHTEKGLRLPEIVTAVLTGLKQGEEDFGVKSNALLCGMRH-DQQQAIEKIVHLAHDFRET 169
Cdd:PRK09358 86 YLEDAAADGVVYAEIRFDPQLHTERGLPLEEVVEAVLDGLRAAEAEFGISVRLILCFMRHfGEEAAARELEALAARYRDD 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284955 170 GVVGFDLAGNEVDFPPYTFEDVLALANQLSIPLTLHAGECGCGKNVADAV-TLGATRIGHGIALKDTPEYLALLKEKKVL 248
Cdd:PRK09358 166 GVVGFDLAGDELGFPPSKFARAFDRARDAGLRLTAHAGEAGGPESIWEALdELGAERIGHGVRAIEDPALMARLADRRIP 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284955 249 LEMCPTSNFQTGTVKTLAEYPFQQFIEAGLAVCINTDNRTVSDTTLTKEFMKLATWYQLSYDEMKQLTKNALAGAFLSPD 328
Cdd:PRK09358 246 LEVCPTSNVQTGAVPSLAEHPLKTLLDAGVRVTINTDDPLVFGTTLTEEYEALAEAFGLSDEDLAQLARNALEAAFLSEE 325
|
330
....*....|...
gi 488284955 329 EKKLLNQKIDQAY 341
Cdd:PRK09358 326 EKAALLAEVDAWL 338
|
|
| Add |
COG1816 |
Adenosine deaminase [Nucleotide transport and metabolism]; Adenosine deaminase is part of the ... |
16-341 |
3.47e-140 |
|
Adenosine deaminase [Nucleotide transport and metabolism]; Adenosine deaminase is part of the Pathway/BioSystem: Menaquinone biosynthesis
Pssm-ID: 441421 Cd Length: 326 Bit Score: 400.23 E-value: 3.47e-140
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284955 16 PKIELHCHLDGSIRPTTLRTIAEKQNIPLP-QDEQALKelvvAPEKCTDLNDYLTRFDFVLTCLQTAEALQAAAYDVISQ 94
Cdd:COG1816 1 PKAELHLHLEGSLRPETLLELAARNGIDLPaADVEELR----AAYDFRDLQSFLDTYDAGAAVLQTEEDFRRLAYEYLED 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284955 95 AAEDGVAYIEVRFAPSQHTEKGLRLPEIVTAVLTGLKQGEEDFGVKSNALLCGMRHDQQQAIEKIVHLAHDFRETGVVGF 174
Cdd:COG1816 77 AAADGVRYAEIRFDPQLHTRRGLSLEEVVEAVLDGLREAEREFGISVRLILCALRHLSPEAAFETLELALRYRDRGVVGF 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284955 175 DLAGNEVDFPPYTFEDVLALANQLSIPLTLHAGECGCGKNVADAVT-LGATRIGHGIALKDTPEYLALLKEKKVLLEMCP 253
Cdd:COG1816 157 GLAGDERGFPPEKFAEAFARAREAGLHLTAHAGEAGGPESIWEALDlLGAERIGHGVRAIEDPALVARLADRGIPLEVCP 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284955 254 TSNFQTGTVKTLAEYPFQQFIEAGLAVCINTDNRTVSDTTLTKEFMKLATWYQLSYDEMKQLTKNALAGAFLSPDEKKLL 333
Cdd:COG1816 237 TSNVQLGVVPSLAEHPLRRLLDAGVRVTLNTDDPLYFGTTLTDEYELAAEAFGLSDADLAQLARNAIEASFLPEEEKAAL 316
|
....*...
gi 488284955 334 NQKIDQAY 341
Cdd:COG1816 317 LAELDAYF 324
|
|
| A_deaminase |
pfam00962 |
Adenosine deaminase; |
16-340 |
1.45e-91 |
|
Adenosine deaminase;
Pssm-ID: 425964 Cd Length: 330 Bit Score: 276.62 E-value: 1.45e-91
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284955 16 PKIELHCHLDGSIRPTTLRTIAEKQNIPLP-QDEQALKELVVAPEKCTDLNDYLTRFDFVLTCLQTAEALQAAAYDVISQ 94
Cdd:pfam00962 1 PKAELHLHLDGSLRPDTLLELAKRYGIILPaDFPEALEPLFRKYKKERDLQDFLDKYDIGVAVLRSPEDIRRLAFEYAED 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284955 95 AAEDGVAYIEVRFAPSQHTEKGLRLPEIVTAVLTGLKQGEEDFGVKSNALLCGMRHDQQQAIEKIVHLAHDFRETGVVGF 174
Cdd:pfam00962 81 VAKDGVVYAEVRYDPQSHASRGLSPDTVVDAVLDAVDAAEREFGITVRLIVCAMRHEHPECSREIAELAPRYRDQGIVAF 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284955 175 DLAGNEVDFPPYTFEDVL---ALANQLSIPLTLHAGECGCGKNVADAV-TLGATRIGHGIALKDTPEYLALLKEKKVLLE 250
Cdd:pfam00962 161 GLAGDEKGFPPSLFRDHVeafARARDAGLHLTVHAGEAGGPQSVWEALdDLGAERIGHGVRSAEDPRLLDRLADRQIPLE 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284955 251 MCPTSNFQTGTVKTLAEYPFQQFIEAGLAVCINTDNRTVSDTTLTKEFMKLATWYQLSYDEMKQLTKNALAGAFLSPDEK 330
Cdd:pfam00962 241 ICPTSNVQTGAVASLAEHPLKTFLRAGVPVSLNTDDPLMFGSDLLDEYQVAKRAPGFDEEELARLAKNAVKGSFLPADEK 320
|
330
....*....|
gi 488284955 331 KLLNQKIDQA 340
Cdd:pfam00962 321 RALLDEVDKV 330
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| aden_deam |
TIGR01430 |
adenosine deaminase; This family includes the experimentally verified adenosine deaminases of ... |
15-337 |
1.68e-167 |
|
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: 469.15 E-value: 1.68e-167
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284955 15 LPKIELHCHLDGSIRPTTLRTIAEKQNIPLPQDEQALKELVVAPEKCTDLNDYLTRFDFVLTCLQTAEALQAAAYDVISQ 94
Cdd:TIGR01430 1 LPKAELHLHLEGSIRPETLLELAQKNGIPLPADLQSGEELKEAYDKFRDLQDFLAKYDFGVEVLRTEDDFKRLAYEYVEK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284955 95 AAEDGVAYIEVRFAPSQHTEKGLRLPEIVTAVLTGLKQGEEDFGVKSNALLCGMRHDQQQAIEKIVHLAHDFRETGVVGF 174
Cdd:TIGR01430 81 AAKDGVVYAEVFFDPQLHTNRGISPDTVVEAVLDGLDEAERDFGIKSRLILCGMRHKQPEAAEETLELAKPYKEQTIVGF 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284955 175 DLAGNEVDFPPYTFEDVLALANQLSIPLTLHAGEC-GCGKNVADAVTLGATRIGHGIALKDTPEYLALLKEKKVLLEMCP 253
Cdd:TIGR01430 161 GLAGDERGGPPPDFVRAFAIARELGLHLTVHAGELgGPESVREALDDLGATRIGHGVRALEDPELLKRLAQENITLEVCP 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284955 254 TSNFQTGTVKTLAEYPFQQFIEAGLAVCINTDNRTVSDTTLTKEFMKLATWYQLSYDEMKQLTKNALAGAFLSPDEKKLL 333
Cdd:TIGR01430 241 TSNVALGVVKSLAEHPLRRFLEAGVKVTLNSDDPAYFGSYLTEEYEIAAKHAGLTEEELKQLARNALEGSFLSDDEKKEL 320
|
....
gi 488284955 334 NQKI 337
Cdd:TIGR01430 321 LAKL 324
|
|
| ADA |
cd01320 |
Adenosine deaminase (ADA) is a monomeric zinc dependent enzyme which catalyzes the ... |
14-337 |
2.30e-161 |
|
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: 453.58 E-value: 2.30e-161
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284955 14 QLPKIELHCHLDGSIRPTTLRTIAEKQNIPLPQDEQALKELVVAPEKCTDLNDYLTRFDFVLTCLQTAEALQAAAYDVIS 93
Cdd:cd01320 1 NLPKAELHLHLDGSLRPETILELAKKNGITLPASDVELLELVVAAYNFSDLQDFLAKYDFGLSVLQTEEDFERLAYEYLE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284955 94 QAAEDGVAYIEVRFAPSQHTEKGLRLPEIVTAVLTGLKQGEEDFGVKSNALLCGMRHDQQQAIEKIVHLAHDFRETGVVG 173
Cdd:cd01320 81 DAAADGVVYAEIRFSPQLHTRRGLSFDEVVEAVLRGLDEAEAEFGIKARLILCGLRHLSPESAQETLELALKYRDKGVVG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284955 174 FDLAGNEVDFPPYTFEDVLALANQLSIPLTLHAGECGCGKNVADAV-TLGATRIGHGIALKDTPEYLALLKEKKVLLEMC 252
Cdd:cd01320 161 FDLAGDEVGFPPEKFVRAFQRAREAGLRLTAHAGEAGGPESVRDALdLLGAERIGHGIRAIEDPELVKRLAERNIPLEVC 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284955 253 PTSNFQTGTVKTLAEYPFQQFIEAGLAVCINTDNRTVSDTTLTKEFMKLATWYQLSYDEMKQLTKNALAGAFLSPDEKKL 332
Cdd:cd01320 241 PTSNVQTGAVKSLAEHPLRELLDAGVKVTINTDDPTVFGTYLTDEYELLAEAFGLTEEELKKLARNAVEASFLSEEEKAE 320
|
....*
gi 488284955 333 LNQKI 337
Cdd:cd01320 321 LLKRI 325
|
|
| PRK09358 |
PRK09358 |
adenosine deaminase; Provisional |
12-341 |
4.41e-142 |
|
adenosine deaminase; Provisional
Pssm-ID: 236480 Cd Length: 340 Bit Score: 405.33 E-value: 4.41e-142
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284955 12 VRQLPKIELHCHLDGSIRPTTLRTIAEKQNIPLP-QDEQALKElVVAPEKCTDLNDYLTRFDFVLTCLQTAEALQAAAYD 90
Cdd:PRK09358 7 IRSLPKAELHLHLDGSLRPETILELARRNGIALPaTDVEELPW-VRAAYDFRDLQSFLDKYDAGVAVLQTEEDLRRLAFE 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284955 91 VISQAAEDGVAYIEVRFAPSQHTEKGLRLPEIVTAVLTGLKQGEEDFGVKSNALLCGMRH-DQQQAIEKIVHLAHDFRET 169
Cdd:PRK09358 86 YLEDAAADGVVYAEIRFDPQLHTERGLPLEEVVEAVLDGLRAAEAEFGISVRLILCFMRHfGEEAAARELEALAARYRDD 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284955 170 GVVGFDLAGNEVDFPPYTFEDVLALANQLSIPLTLHAGECGCGKNVADAV-TLGATRIGHGIALKDTPEYLALLKEKKVL 248
Cdd:PRK09358 166 GVVGFDLAGDELGFPPSKFARAFDRARDAGLRLTAHAGEAGGPESIWEALdELGAERIGHGVRAIEDPALMARLADRRIP 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284955 249 LEMCPTSNFQTGTVKTLAEYPFQQFIEAGLAVCINTDNRTVSDTTLTKEFMKLATWYQLSYDEMKQLTKNALAGAFLSPD 328
Cdd:PRK09358 246 LEVCPTSNVQTGAVPSLAEHPLKTLLDAGVRVTINTDDPLVFGTTLTEEYEALAEAFGLSDEDLAQLARNALEAAFLSEE 325
|
330
....*....|...
gi 488284955 329 EKKLLNQKIDQAY 341
Cdd:PRK09358 326 EKAALLAEVDAWL 338
|
|
| Add |
COG1816 |
Adenosine deaminase [Nucleotide transport and metabolism]; Adenosine deaminase is part of the ... |
16-341 |
3.47e-140 |
|
Adenosine deaminase [Nucleotide transport and metabolism]; Adenosine deaminase is part of the Pathway/BioSystem: Menaquinone biosynthesis
Pssm-ID: 441421 Cd Length: 326 Bit Score: 400.23 E-value: 3.47e-140
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284955 16 PKIELHCHLDGSIRPTTLRTIAEKQNIPLP-QDEQALKelvvAPEKCTDLNDYLTRFDFVLTCLQTAEALQAAAYDVISQ 94
Cdd:COG1816 1 PKAELHLHLEGSLRPETLLELAARNGIDLPaADVEELR----AAYDFRDLQSFLDTYDAGAAVLQTEEDFRRLAYEYLED 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284955 95 AAEDGVAYIEVRFAPSQHTEKGLRLPEIVTAVLTGLKQGEEDFGVKSNALLCGMRHDQQQAIEKIVHLAHDFRETGVVGF 174
Cdd:COG1816 77 AAADGVRYAEIRFDPQLHTRRGLSLEEVVEAVLDGLREAEREFGISVRLILCALRHLSPEAAFETLELALRYRDRGVVGF 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284955 175 DLAGNEVDFPPYTFEDVLALANQLSIPLTLHAGECGCGKNVADAVT-LGATRIGHGIALKDTPEYLALLKEKKVLLEMCP 253
Cdd:COG1816 157 GLAGDERGFPPEKFAEAFARAREAGLHLTAHAGEAGGPESIWEALDlLGAERIGHGVRAIEDPALVARLADRGIPLEVCP 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284955 254 TSNFQTGTVKTLAEYPFQQFIEAGLAVCINTDNRTVSDTTLTKEFMKLATWYQLSYDEMKQLTKNALAGAFLSPDEKKLL 333
Cdd:COG1816 237 TSNVQLGVVPSLAEHPLRRLLDAGVRVTLNTDDPLYFGTTLTDEYELAAEAFGLSDADLAQLARNAIEASFLPEEEKAAL 316
|
....*...
gi 488284955 334 NQKIDQAY 341
Cdd:COG1816 317 LAELDAYF 324
|
|
| A_deaminase |
pfam00962 |
Adenosine deaminase; |
16-340 |
1.45e-91 |
|
Adenosine deaminase;
Pssm-ID: 425964 Cd Length: 330 Bit Score: 276.62 E-value: 1.45e-91
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284955 16 PKIELHCHLDGSIRPTTLRTIAEKQNIPLP-QDEQALKELVVAPEKCTDLNDYLTRFDFVLTCLQTAEALQAAAYDVISQ 94
Cdd:pfam00962 1 PKAELHLHLDGSLRPDTLLELAKRYGIILPaDFPEALEPLFRKYKKERDLQDFLDKYDIGVAVLRSPEDIRRLAFEYAED 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284955 95 AAEDGVAYIEVRFAPSQHTEKGLRLPEIVTAVLTGLKQGEEDFGVKSNALLCGMRHDQQQAIEKIVHLAHDFRETGVVGF 174
Cdd:pfam00962 81 VAKDGVVYAEVRYDPQSHASRGLSPDTVVDAVLDAVDAAEREFGITVRLIVCAMRHEHPECSREIAELAPRYRDQGIVAF 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284955 175 DLAGNEVDFPPYTFEDVL---ALANQLSIPLTLHAGECGCGKNVADAV-TLGATRIGHGIALKDTPEYLALLKEKKVLLE 250
Cdd:pfam00962 161 GLAGDEKGFPPSLFRDHVeafARARDAGLHLTVHAGEAGGPQSVWEALdDLGAERIGHGVRSAEDPRLLDRLADRQIPLE 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284955 251 MCPTSNFQTGTVKTLAEYPFQQFIEAGLAVCINTDNRTVSDTTLTKEFMKLATWYQLSYDEMKQLTKNALAGAFLSPDEK 330
Cdd:pfam00962 241 ICPTSNVQTGAVASLAEHPLKTFLRAGVPVSLNTDDPLMFGSDLLDEYQVAKRAPGFDEEELARLAKNAVKGSFLPADEK 320
|
330
....*....|
gi 488284955 331 KLLNQKIDQA 340
Cdd:pfam00962 321 RALLDEVDKV 330
|
|
| ADA_AMPD |
cd00443 |
Adenosine/AMP deaminase. Adenosine deaminases (ADAs) are present in pro- and eukaryotic ... |
15-335 |
4.94e-56 |
|
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: 184.47 E-value: 4.94e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284955 15 LPKIELHCHLDGSIRPTTLRTIAEKQniplpqdeqalkelvvapekctdlndYLTRFDFVLTCLQTAEALQAAAYDVISQ 94
Cdd:cd00443 1 LPKVELHAHLSGSISPETLLELIKKE--------------------------FFEKFLLVHNLLQKGEALARALKEVIEE 54
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284955 95 AAEDGVAYIEVRFAPSQ-HTEKGLRLPEIVTAVLTGLKQGEEDF-GVKSNALLCGMRH---DQQQAIEK-IVHLAHDFRE 168
Cdd:cd00443 55 FAEDNVQYLELRTTPRLlETEKGLTKEQYWLLVIEGISEAKQWFpPIKVRLILSVDRRgpyVQNYLVASeILELAKFLSN 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284955 169 TgVVGFDLAGNEVDF--PPYTFEDVLALANQL-SIPLTLHAGECGCGKNVADAVTLGATRIGHGIALKDTPEYLALLKEK 245
Cdd:cd00443 135 Y-VVGIDLVGDESKGenPLRDFYSYYEYARRLgLLGLTLHCGETGNREELLQALLLLPDRIGHGIFLLKHPELIYLVKLR 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284955 246 KVLLEMCPTSNFQTGTVKTLAEYPFQQFIEAGLAVCINTDNRTVSDTTLTKEFMKLATWYQLSYDEMKQLTKNALAGAFL 325
Cdd:cd00443 214 NIPIEVCPTSNVVLGTVQSYEKHPFMRFFKAGLPVSLSTDDPGIFGTSLSEEYSLAAKTFGLTFEDLCELNRNSVLSSFA 293
|
330
....*....|.
gi 488284955 326 SPDEKK-LLNQ 335
Cdd:cd00443 294 KDEEKKsLLEV 304
|
|
| PTZ00124 |
PTZ00124 |
adenosine deaminase; Provisional |
13-341 |
3.93e-46 |
|
adenosine deaminase; Provisional
Pssm-ID: 173415 Cd Length: 362 Bit Score: 160.42 E-value: 3.93e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284955 13 RQLPKIELHCHLDGSIRPTTLRTIAEKQNI-PLPQDEQALKELVVApEKCTDLNDYLTRFDFVLTCLQTAEALQAAAYDV 91
Cdd:PTZ00124 33 KRIPKCELHCHLDLCFSVDFFLSCIRKYNLqPNLSDEEILDYYLFA-KGGKSLGEFVEKAIRVADIFNDYEVIEDLAKHA 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284955 92 ISQAAEDGVAYIEVRFAPSQHTEK-GLRLPEIVTAVLTGLKQGEEDFGVKSN-ALLC----GMRH-DQQQAIEKIVHLAH 164
Cdd:PTZ00124 112 VFNKYKEGVVLMEFRYSPTFVAFKhNLDIDLIHQAIVKGIKEAVELLDHKIEvGLLCigdtGHDAaPIKESADFCLKHKA 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284955 165 DFretgvVGFDLAGNEVDFPPytFEDVLALANQLSIPLTLHAGEC----GCGKNVADAVTLGATRIGHGIALKDTPEYLA 240
Cdd:PTZ00124 192 DF-----VGFDHAGHEVDLKP--FKDIFDYVREAGVNLTVHAGEDvtlpNLNTLYSAIQVLKVKRIGHGIRVAESQELID 264
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284955 241 LLKEKKVLLEMCPTSNFQTGTVKTLAEYPFQQFIEAGLAVCINTDNRTVSDTTLTKEFMKLATWYQLSYDEMKQLTKNAL 320
Cdd:PTZ00124 265 MVKEKDILLEVCPISNVLLNNAKSMDTHPIRKLYDAGVKVSVNSDDPGMFLTNINDDYEELYTHLNFTLADFMKMNEWAL 344
|
330 340
....*....|....*....|.
gi 488284955 321 AGAFLSPDEKkllnQKIDQAY 341
Cdd:PTZ00124 345 EKSFLDKDIK----LKIKKLY 361
|
|
| ADGF |
cd01321 |
Adenosine deaminase-related growth factors (ADGF), a novel family of secreted growth-factors ... |
6-336 |
7.90e-28 |
|
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: 111.21 E-value: 7.90e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284955 6 FMEESRV----RQLPK-IELHCHLDGSIRPTTLrtiaekqniplpqdeqaLKELVVAPEKCTDLNDYLtrfdfvltcLQT 80
Cdd:cd01321 11 LIENSTLfkiiQKMPKgALLHVHDTAMVSSDWL-----------------IKNATYRFEQIFDIIDGL---------LTY 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284955 81 AEALQAAAYDVISQAAEDGVAYIEVRFAPSQHTEKGLRLP------EIVTAVLTGLKQGEEDF-GVKsnALLCGMRHDQQ 153
Cdd:cd01321 65 LPIFRDYYRRLLEELYEDNVQYVELRSSFSPLYDLDGREYdyeetvQLLEEVVEKFKKTHPDFiGLK--IIYATLRNFND 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284955 154 QAIEKIVHLAHDFRETG---VVGFDLAGNE-VDFPPYTFEDVLALANQLS--IPLTLHAGECGC-----GKNVADAVTLG 222
Cdd:cd01321 143 SEIKESMEQCLNLKKKFpdfIAGFDLVGQEdAGRPLLDFLPQLLWFPKQCaeIPFFFHAGETNGdgtetDENLVDALLLN 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284955 223 ATRIGHGIALKDTPEYLALLKEKKVLLEMCPTSNFQTGTVKTLAEYPFQQFIEAGLAVCINTDNRTVSDTT-LTKEF--- 298
Cdd:cd01321 223 TKRIGHGFALPKHPLLMDLVKKKNIAIEVCPISNQVLGLVSDLRNHPAAALLARGVPVVISSDDPGFWGAKgLSHDFyqa 302
|
330 340 350
....*....|....*....|....*....|....*....
gi 488284955 299 -MKLATwYQLSYDEMKQLTKNALAGAFLSPDEKKLLNQK 336
Cdd:cd01321 303 fMGLAP-ADAGLRGLKQLAENSIRYSALSDQEKDEAVAK 340
|
|
| metallo-dependent_hydrolases |
cd01292 |
Superfamily of metallo-dependent hydrolases (also called amidohydrolase superfamily) is a ... |
62-285 |
5.86e-13 |
|
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: 68.13 E-value: 5.86e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284955 62 TDLNDYLTRFDFVLTCLQTAEALQAAAYDVISQAAEDGVAYIEVRFapsqHTEKGLRLPEIVTAVLTGLKQGEedfGVKS 141
Cdd:cd01292 11 SALRGTRLNLELKEAEELSPEDLYEDTLRALEALLAGGVTTVVDMG----STPPPTTTKAAIEAVAEAARASA---GIRV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284955 142 NALLCGMRHDQQQAIEKIVH---LAHDFRETGVVGFDLAGNE--VDFPPYTFEDVLALANQLSIPLTLHAGEcgcGKNVA 216
Cdd:cd01292 84 VLGLGIPGVPAAVDEDAEALlleLLRRGLELGAVGLKLAGPYtaTGLSDESLRRVLEEARKLGLPVVIHAGE---LPDPT 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 488284955 217 DAVT--------LGATRIGHGIALkdTPEYLALLKEKKVLLEMCPTSNFQTGTVKTLAEyPFQQFIEAGLAVCINTD 285
Cdd:cd01292 161 RALEdlvallrlGGRVVIGHVSHL--DPELLELLKEAGVSLEVCPLSNYLLGRDGEGAE-ALRRLLELGIRVTLGTD 234
|
|
| AMPD |
cd01319 |
AMP deaminase (AMPD) catalyzes the hydrolytic deamination of adensosine monophosphate (AMP) at ... |
171-331 |
6.43e-08 |
|
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: 53.91 E-value: 6.43e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284955 171 VVGFDLAGNEVDF-------------------PPYTF------EDVLALaNQLSI-----PLTL--HAGECGCGKNVADA 218
Cdd:cd01319 267 VIGFDSVDDESKSerrftrkfpkpeewtseenPPYSYylyymyANITTL-NSFRKargfnTFVLrpHCGEAGDIDHLASA 345
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284955 219 VTLgATRIGHGIALKDTP--EYLALLkeKKVLLEMCPTSNfqTGTVKTLAEYPFQQFIEAGLAVCINTDNRTVSDTT--- 293
Cdd:cd01319 346 FLL-AHGISHGINLRKVPvlQYLYYL--TQIGIAMSPLSN--NSLFLSYEKNPFPEFFKRGLNVSLSTDDPLQFHFTkep 420
|
170 180 190
....*....|....*....|....*....|....*...
gi 488284955 294 LTKEFMKLATWYQLSYDEMKQLTKNALAGAFLSPDEKK 331
Cdd:cd01319 421 LMEEYSIAAQVWKLSTCDMCELARNSVLQSGFEHSIKR 458
|
|
| archeal_chlorohydrolases |
cd01305 |
Predicted chlorohydrolases. These metallo-dependent hydrolases from archea are part of the ... |
141-343 |
3.19e-05 |
|
Predicted chlorohydrolases. These metallo-dependent hydrolases from archea are part of the superfamily of metallo-dependent hydrolases, a large group of proteins that show conservation in their 3-dimensional fold (TIM barrel) and in details of their active site. They 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. Some members of this subgroup are predicted to be chlorohyrolases.
Pssm-ID: 238630 [Multi-domain] Cd Length: 263 Bit Score: 44.70 E-value: 3.19e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284955 141 SNALLCGMRHDQQQAIEKIVHLAHDFRETGVVGF--------DLAGNEV---DFPPY----------------------T 187
Cdd:cd01305 47 DRELAEAMRKVLRDMRETGIGAFADFREGGVEGIellrralgKLPVPFEvilGRPTEpddpeillevadglglssandvD 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284955 188 FEDVLALANQLSIPLTLHAGECGCGKNVAD---AVTLGATRIGHGIALKDtpEYLALLKEKKVLLEMCPTSNFQTGtvkt 264
Cdd:cd01305 127 LEDILELLRRRGKLFAIHASETRESVGMTDierALDLEPDLLVHGTHLTD--EDLELVRENGVPVVLCPRSNLYFG---- 200
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 488284955 265 LAEYPFQQFIEAGLAVCINTDNRTVSDTTLtkefmklatwyqlsYDEMKQLTKnaLAGAFLSPDEKKLLNQKIDQAYLF 343
Cdd:cd01305 201 VGIPPVAELLKLGIKVLLGTDNVMVNEPDM--------------WAEMEFLAK--YSRLQGYLSPLEILRMATVNAAEF 263
|
|
| AMP_deaminase |
pfam19326 |
AMP deaminase; |
186-331 |
1.96e-04 |
|
AMP deaminase;
Pssm-ID: 437158 [Multi-domain] Cd Length: 622 Bit Score: 43.21 E-value: 1.96e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284955 186 YTFEDVLALaNQL-------SIPLTLHAGECGCGKNVADAVTLgATRIGHGIALKDTP--EYLALLKEkkVLLEMCPTSN 256
Cdd:pfam19326 424 YMYANIAVL-NSLrkergfnTFVLRPHCGEAGDIDHLVSAFLL-AHGISHGILLRKSPvlQYLYYLAQ--IGIAMSPLSN 499
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 488284955 257 fqTGTVKTLAEYPFQQFIEAGLAVCINTDNRTVSDTT---LTKEFMKLATWYQLSYDEMKQLTKNALAGAFLSPDEKK 331
Cdd:pfam19326 500 --NSLFLEYHKNPFPEFFKRGLNVSLSTDDPLQFHFTkepLMEEYSIAAQVWKLSACDMCELARNSVLQSGFSHQLKS 575
|
|
| AMP_deaminase |
TIGR01429 |
AMP deaminase; This model describes AMP deaminase, a large, well-conserved eukaryotic protein ... |
184-330 |
2.01e-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: 43.29 E-value: 2.01e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284955 184 PPYTFEDVLALANQLSI------------PLTLHAGECGCGKNVADAVTLgATRIGHGIALKDTP--EYLALLKEkkVLL 249
Cdd:TIGR01429 411 PPYSYYLYYMYANIMVLnnfrrerglntfLLRPHCGEAGSVDHLVSAFLT-SHGINHGILLRKVPvlQYLYYLTQ--IPI 487
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284955 250 EMCPTSNfqTGTVKTLAEYPFQQFIEAGLAVCINTDNRTVSDTT---LTKEFMKLATWYQLSYDEMKQLTKNALAGAFLS 326
Cdd:TIGR01429 488 AMSPLSN--NSLFLEYSKNPLPEYLHKGLNVSLSTDDPLQFHYTkeaLMEEYAIAAQVWKLSTCDMCELARNSVLQSGFE 565
|
....
gi 488284955 327 PDEK 330
Cdd:TIGR01429 566 HQVK 569
|
|
| PLN03055 |
PLN03055 |
AMP deaminase; Provisional |
205-320 |
3.45e-04 |
|
AMP deaminase; Provisional
Pssm-ID: 178613 Cd Length: 602 Bit Score: 42.55 E-value: 3.45e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284955 205 HAGECGCGKNVADAVTLgATRIGHGIALKDTP--EYLALLKEkkVLLEMCPTSNfqtgtVKTLAEY---PFQQFIEAGLA 279
Cdd:PLN03055 422 HAGEAGDIDHLAAAFLL-AHNIAHGNNLRKSPglQYLYYLAQ--IGLAMSPLSN-----NSLFLDYhrnPFPMFFARGLN 493
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 488284955 280 VCINTDNRTVSDTT---LTKEFMKLATWYQLSYDEMKQLTKNAL 320
Cdd:PLN03055 494 VSLSTDDPLQIHLTkepLVEEYSIAAQVWKLSSCDLCEIARNSV 537
|
|
| Imidazolone-5PH |
cd01296 |
Imidazolonepropionase/imidazolone-5-propionate hydrolase (Imidazolone-5PH) catalyzes the third ... |
191-323 |
4.05e-04 |
|
Imidazolonepropionase/imidazolone-5-propionate hydrolase (Imidazolone-5PH) catalyzes the third step in the histidine degradation pathway, the hydrolysis of (S)-3-(5-oxo-4,5-dihydro-3H-imidazol-4-yl)propanoate to N-formimidoyl-L-glutamate. In bacteria, the enzyme is part of histidine utilization (hut) operon.
Pssm-ID: 238621 [Multi-domain] Cd Length: 371 Bit Score: 41.86 E-value: 4.05e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284955 191 VLALANQLSIPLTLHAGECGCGKNVADAVTLGATRIGHGIALKDtpEYLALLKEKKVLLEMCPTSNFQTGtvktLAEYPF 270
Cdd:cd01296 198 ILEAAKEAGLPVKIHADELSNIGGAELAAELGALSADHLEHTSD--EGIAALAEAGTVAVLLPGTAFSLR----ETYPPA 271
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 488284955 271 QQFIEAGLAVCINTD-NRTVSDTTLTKEFMKLA-TWYQLSYDEmkqltknALAGA 323
Cdd:cd01296 272 RKLIDAGVPVALGTDfNPGSSPTSSMPLVMHLAcRLMRMTPEE-------ALTAA 319
|
|
| PLN02768 |
PLN02768 |
AMP deaminase |
199-320 |
3.52e-03 |
|
AMP deaminase
Pssm-ID: 215411 Cd Length: 835 Bit Score: 39.46 E-value: 3.52e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284955 199 SIPLTLHAGECGCGKNVAdAVTLGATRIGHGIALKDTP--EYLALLKEkkVLLEMCPTSNfqtgtVKTLAEY---PFQQF 273
Cdd:PLN02768 649 TIKFRPHSGEAGDIDHLA-ATFLTCHNIAHGINLRKSPvlQYLYYLAQ--IGLAMSPLSN-----NSLFLDYhrnPFPMF 720
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 488284955 274 IEAGLAVCINTDNRT---VSDTTLTKEFMKLATWYQLSYDEMKQLTKNAL 320
Cdd:PLN02768 721 FLRGLNVSLSTDDPLqihLTKEPLVEEYSIAASVWKLSSCDLCEIARNSV 770
|
|
| PTZ00310 |
PTZ00310 |
AMP deaminase; Provisional |
205-319 |
3.80e-03 |
|
AMP deaminase; Provisional
Pssm-ID: 240354 [Multi-domain] Cd Length: 1453 Bit Score: 39.41 E-value: 3.80e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284955 205 HAGECGCGKNVADAVTLgATRIGHGIALKDTP--EYLALLKEkkVLLEMCPTSNfqTGTVKTLAEYPFQQFIEAGLAVCI 282
Cdd:PTZ00310 1115 HCGESGSMDHLYGAFLC-ANSICHGINLRNDPpmQYLYYLAQ--IGLHVSPLSN--NALFLAFLENPFPVFFHRGLNVSL 1189
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 488284955 283 NTDNRTVSDTT---LTKEFMKLATWYQLSYDEMKQLTKNA 319
Cdd:PTZ00310 1190 STDDPLMFHQTqepLIEEYSIAARVWGLSLNDLCEIARNS 1229
|
|
| PRK09045 |
PRK09045 |
TRZ/ATZ family hydrolase; |
185-285 |
4.15e-03 |
|
TRZ/ATZ family hydrolase;
Pssm-ID: 236366 [Multi-domain] Cd Length: 443 Bit Score: 38.74 E-value: 4.15e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284955 185 PYT-----FEDVLALANQLSIPLTLH----AGEcgcgknVADAVT---------------LGATRIG-HGIALKDtpEYL 239
Cdd:PRK09045 196 PYTvsdenLERIRTLAEQLDLPIHIHlhetAQE------IADSLKqhgqrplarlarlglLGPRLIAvHMTQLTD--AEI 267
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 488284955 240 ALLKEKKVLLEMCPTSNFQtgtvktLAE--YPFQQFIEAGLAVCINTD 285
Cdd:PRK09045 268 ALLAETGCSVVHCPESNLK------LASgfCPVAKLLQAGVNVALGTD 309
|
|
| |
