|
Name |
Accession |
Description |
Interval |
E-value |
| PRK09358 |
PRK09358 |
adenosine deaminase; Provisional |
4-354 |
4.07e-168 |
|
adenosine deaminase; Provisional
Pssm-ID: 236480 Cd Length: 340 Bit Score: 471.97 E-value: 4.07e-168
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503049013 4 ISYEDIVKVPKALLHDHLDGGLRPATIVELAAEVGHELPTTDPAALGVwFTEAANSGSLERYLETFAHTVAVMQTPAALR 83
Cdd:PRK09358 2 NLLMIIRSLPKAELHLHLDGSLRPETILELARRNGIALPATDVEELPW-VRAAYDFRDLQSFLDKYDAGVAVLQTEEDLR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503049013 84 RVARECALDLAADGVVYAEVRFAPEQHLEQNLTLDEVVDAVVTGFRegsalAAEAGTPIRIGTLLTAMRH---AARSQEI 160
Cdd:PRK09358 81 RLAFEYLEDAAADGVVYAEIRFDPQLHTERGLPLEEVVEAVLDGLR-----AAEAEFGISVRLILCFMRHfgeEAAAREL 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503049013 161 AELAVRHRDTGVVGFDIAGAEAGFPPTRHLDAFEYLQRENFHFTIHAGEAFGLPSIWQAIQWCGADRLGHGVRIVDDItp 240
Cdd:PRK09358 156 EALAARYRDDGVVGFDLAGDELGFPPSKFARAFDRARDAGLRLTAHAGEAGGPESIWEALDELGAERIGHGVRAIEDP-- 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503049013 241 gnppvlgRLAAYVRDKRIPLELCPSSNVQTGAAASIADHPIGLLRDLRFRVTVNTDNRLMSGTSMSREMSLLVEAFGYGW 320
Cdd:PRK09358 234 -------ALMARLADRRIPLEVCPTSNVQTGAVPSLAEHPLKTLLDAGVRVTINTDDPLVFGTTLTEEYEALAEAFGLSD 306
|
330 340 350
....*....|....*....|....*....|....
gi 503049013 321 KELQWFTINAMKSAFIPFDERLRIIDEVIKPAYA 354
Cdd:PRK09358 307 EDLAQLARNALEAAFLSEEEKAALLAEVDAWLAA 340
|
|
| Add |
COG1816 |
Adenosine deaminase [Nucleotide transport and metabolism]; Adenosine deaminase is part of the ... |
13-352 |
3.85e-163 |
|
Adenosine deaminase [Nucleotide transport and metabolism]; Adenosine deaminase is part of the Pathway/BioSystem: Menaquinone biosynthesis
Pssm-ID: 441421 Cd Length: 326 Bit Score: 458.78 E-value: 3.85e-163
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503049013 13 PKALLHDHLDGGLRPATIVELAAEVGHELPTTDPAALGvwftEAANSGSLERYLETFAHTVAVMQTPAALRRVARECALD 92
Cdd:COG1816 1 PKAELHLHLEGSLRPETLLELAARNGIDLPAADVEELR----AAYDFRDLQSFLDTYDAGAAVLQTEEDFRRLAYEYLED 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503049013 93 LAADGVVYAEVRFAPEQHLEQNLTLDEVVDAVVTGFREgsalaAEAGTPIRIGTLLTAMRH--AARSQEIAELAVRHRDT 170
Cdd:COG1816 77 AAADGVRYAEIRFDPQLHTRRGLSLEEVVEAVLDGLRE-----AEREFGISVRLILCALRHlsPEAAFETLELALRYRDR 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503049013 171 GVVGFDIAGAEAGFPPTRHLDAFEYLQRENFHFTIHAGEAFGLPSIWQAIQWCGADRLGHGVRIVDDitpgnppvlGRLA 250
Cdd:COG1816 152 GVVGFGLAGDERGFPPEKFAEAFARAREAGLHLTAHAGEAGGPESIWEALDLLGAERIGHGVRAIED---------PALV 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503049013 251 AYVRDKRIPLELCPSSNVQTGAAASIADHPIGLLRDLRFRVTVNTDNRLMSGTSMSREMSLLVEAFGYGWKELQWFTINA 330
Cdd:COG1816 223 ARLADRGIPLEVCPTSNVQLGVVPSLAEHPLRRLLDAGVRVTLNTDDPLYFGTTLTDEYELAAEAFGLSDADLAQLARNA 302
|
330 340
....*....|....*....|..
gi 503049013 331 MKSAFIPFDERLRIIDEVIKPA 352
Cdd:COG1816 303 IEASFLPEEEKAALLAELDAYF 324
|
|
| A_deaminase |
pfam00962 |
Adenosine deaminase; |
13-351 |
3.57e-131 |
|
Adenosine deaminase;
Pssm-ID: 425964 Cd Length: 330 Bit Score: 377.93 E-value: 3.57e-131
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503049013 13 PKALLHDHLDGGLRPATIVELAAEVGHELPTTDPAALGVWFTEAANSGSLERYLETFAHTVAVMQTPAALRRVARECALD 92
Cdd:pfam00962 1 PKAELHLHLDGSLRPDTLLELAKRYGIILPADFPEALEPLFRKYKKERDLQDFLDKYDIGVAVLRSPEDIRRLAFEYAED 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503049013 93 LAADGVVYAEVRFAPEQHLEQNLTLDEVVDAVVTGFREGsalAAEAGTPIRIgtLLTAMR--HAARSQEIAELAVRHRDT 170
Cdd:pfam00962 81 VAKDGVVYAEVRYDPQSHASRGLSPDTVVDAVLDAVDAA---EREFGITVRL--IVCAMRheHPECSREIAELAPRYRDQ 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503049013 171 GVVGFDIAGAEAGFPPTR---HLDAFEYLQRENFHFTIHAGEAFGLPSIWQAIQWCGADRLGHGVRIVDDitpgnppvlG 247
Cdd:pfam00962 156 GIVAFGLAGDEKGFPPSLfrdHVEAFARARDAGLHLTVHAGEAGGPQSVWEALDDLGAERIGHGVRSAED---------P 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503049013 248 RLAAYVRDKRIPLELCPSSNVQTGAAASIADHPIGLLRDLRFRVTVNTDNRLMSGTSMSREMSLLVEAFGYGWKELQWFT 327
Cdd:pfam00962 227 RLLDRLADRQIPLEICPTSNVQTGAVASLAEHPLKTFLRAGVPVSLNTDDPLMFGSDLLDEYQVAKRAPGFDEEELARLA 306
|
330 340
....*....|....*....|....
gi 503049013 328 INAMKSAFIPFDERLRIIDEVIKP 351
Cdd:pfam00962 307 KNAVKGSFLPADEKRALLDEVDKV 330
|
|
| ADA |
cd01320 |
Adenosine deaminase (ADA) is a monomeric zinc dependent enzyme which catalyzes the ... |
11-348 |
3.79e-120 |
|
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: 349.97 E-value: 3.79e-120
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503049013 11 KVPKALLHDHLDGGLRPATIVELAAEVGHELPTTDPAaLGVWFTEAANSGSLERYLETFAHTVAVMQTPAALRRVARECA 90
Cdd:cd01320 1 NLPKAELHLHLDGSLRPETILELAKKNGITLPASDVE-LLELVVAAYNFSDLQDFLAKYDFGLSVLQTEEDFERLAYEYL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503049013 91 LDLAADGVVYAEVRFAPEQHLEQNLTLDEVVDAVVTGFREgsalaAEAGTPIRIGTLLTAMRH--AARSQEIAELAVRHR 168
Cdd:cd01320 80 EDAAADGVVYAEIRFSPQLHTRRGLSFDEVVEAVLRGLDE-----AEAEFGIKARLILCGLRHlsPESAQETLELALKYR 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503049013 169 DTGVVGFDIAGAEAGFPPTRHLDAFEYLQRENFHFTIHAGEAFGLPSIWQAIQWCGADRLGHGVRIVDDItpgnppvlgR 248
Cdd:cd01320 155 DKGVVGFDLAGDEVGFPPEKFVRAFQRAREAGLRLTAHAGEAGGPESVRDALDLLGAERIGHGIRAIEDP---------E 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503049013 249 LAAYVRDKRIPLELCPSSNVQTGAAASIADHPIGLLRDLRFRVTVNTDNRLMSGTSMSREMSLLVEAFGYGWKELQWFTI 328
Cdd:cd01320 226 LVKRLAERNIPLEVCPTSNVQTGAVKSLAEHPLRELLDAGVKVTINTDDPTVFGTYLTDEYELLAEAFGLTEEELKKLAR 305
|
330 340
....*....|....*....|
gi 503049013 329 NAMKSAFIPFDERLRIIDEV 348
Cdd:cd01320 306 NAVEASFLSEEEKAELLKRI 325
|
|
| aden_deam |
TIGR01430 |
adenosine deaminase; This family includes the experimentally verified adenosine deaminases of ... |
13-341 |
1.89e-79 |
|
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: 246.11 E-value: 1.89e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503049013 13 PKALLHDHLDGGLRPATIVELAAEVGHELPTTDPAalGVWFTEAANS-GSLERYLETFAHTVAVMQTPAALRRVARECAL 91
Cdd:TIGR01430 2 PKAELHLHLEGSIRPETLLELAQKNGIPLPADLQS--GEELKEAYDKfRDLQDFLAKYDFGVEVLRTEDDFKRLAYEYVE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503049013 92 DLAADGVVYAEVRFAPEQHLEQNLTLDEVVDAVVTGFREgsalaAEAGTPIRIGTLLTAMRHAA--RSQEIAELAVRHRD 169
Cdd:TIGR01430 80 KAAKDGVVYAEVFFDPQLHTNRGISPDTVVEAVLDGLDE-----AERDFGIKSRLILCGMRHKQpeAAEETLELAKPYKE 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503049013 170 TGVVGFDIAGAEAGFPPTRHLDAFEYLQRENFHFTIHAGEAFGLPSIWQAIQWCGADRLGHGVRIVDDitpgnppvlGRL 249
Cdd:TIGR01430 155 QTIVGFGLAGDERGGPPPDFVRAFAIARELGLHLTVHAGELGGPESVREALDDLGATRIGHGVRALED---------PEL 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503049013 250 AAYVRDKRIPLELCPSSNVQTGAAASIADHPIGLLRDLRFRVTVNTDNRLMSGTSMSREMSLLVEAFGYGWKELQWFTIN 329
Cdd:TIGR01430 226 LKRLAQENITLEVCPTSNVALGVVKSLAEHPLRRFLEAGVKVTLNSDDPAYFGSYLTEEYEIAAKHAGLTEEELKQLARN 305
|
330
....*....|..
gi 503049013 330 AMKSAFIPFDER 341
Cdd:TIGR01430 306 ALEGSFLSDDEK 317
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| PRK09358 |
PRK09358 |
adenosine deaminase; Provisional |
4-354 |
4.07e-168 |
|
adenosine deaminase; Provisional
Pssm-ID: 236480 Cd Length: 340 Bit Score: 471.97 E-value: 4.07e-168
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503049013 4 ISYEDIVKVPKALLHDHLDGGLRPATIVELAAEVGHELPTTDPAALGVwFTEAANSGSLERYLETFAHTVAVMQTPAALR 83
Cdd:PRK09358 2 NLLMIIRSLPKAELHLHLDGSLRPETILELARRNGIALPATDVEELPW-VRAAYDFRDLQSFLDKYDAGVAVLQTEEDLR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503049013 84 RVARECALDLAADGVVYAEVRFAPEQHLEQNLTLDEVVDAVVTGFRegsalAAEAGTPIRIGTLLTAMRH---AARSQEI 160
Cdd:PRK09358 81 RLAFEYLEDAAADGVVYAEIRFDPQLHTERGLPLEEVVEAVLDGLR-----AAEAEFGISVRLILCFMRHfgeEAAAREL 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503049013 161 AELAVRHRDTGVVGFDIAGAEAGFPPTRHLDAFEYLQRENFHFTIHAGEAFGLPSIWQAIQWCGADRLGHGVRIVDDItp 240
Cdd:PRK09358 156 EALAARYRDDGVVGFDLAGDELGFPPSKFARAFDRARDAGLRLTAHAGEAGGPESIWEALDELGAERIGHGVRAIEDP-- 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503049013 241 gnppvlgRLAAYVRDKRIPLELCPSSNVQTGAAASIADHPIGLLRDLRFRVTVNTDNRLMSGTSMSREMSLLVEAFGYGW 320
Cdd:PRK09358 234 -------ALMARLADRRIPLEVCPTSNVQTGAVPSLAEHPLKTLLDAGVRVTINTDDPLVFGTTLTEEYEALAEAFGLSD 306
|
330 340 350
....*....|....*....|....*....|....
gi 503049013 321 KELQWFTINAMKSAFIPFDERLRIIDEVIKPAYA 354
Cdd:PRK09358 307 EDLAQLARNALEAAFLSEEEKAALLAEVDAWLAA 340
|
|
| Add |
COG1816 |
Adenosine deaminase [Nucleotide transport and metabolism]; Adenosine deaminase is part of the ... |
13-352 |
3.85e-163 |
|
Adenosine deaminase [Nucleotide transport and metabolism]; Adenosine deaminase is part of the Pathway/BioSystem: Menaquinone biosynthesis
Pssm-ID: 441421 Cd Length: 326 Bit Score: 458.78 E-value: 3.85e-163
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503049013 13 PKALLHDHLDGGLRPATIVELAAEVGHELPTTDPAALGvwftEAANSGSLERYLETFAHTVAVMQTPAALRRVARECALD 92
Cdd:COG1816 1 PKAELHLHLEGSLRPETLLELAARNGIDLPAADVEELR----AAYDFRDLQSFLDTYDAGAAVLQTEEDFRRLAYEYLED 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503049013 93 LAADGVVYAEVRFAPEQHLEQNLTLDEVVDAVVTGFREgsalaAEAGTPIRIGTLLTAMRH--AARSQEIAELAVRHRDT 170
Cdd:COG1816 77 AAADGVRYAEIRFDPQLHTRRGLSLEEVVEAVLDGLRE-----AEREFGISVRLILCALRHlsPEAAFETLELALRYRDR 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503049013 171 GVVGFDIAGAEAGFPPTRHLDAFEYLQRENFHFTIHAGEAFGLPSIWQAIQWCGADRLGHGVRIVDDitpgnppvlGRLA 250
Cdd:COG1816 152 GVVGFGLAGDERGFPPEKFAEAFARAREAGLHLTAHAGEAGGPESIWEALDLLGAERIGHGVRAIED---------PALV 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503049013 251 AYVRDKRIPLELCPSSNVQTGAAASIADHPIGLLRDLRFRVTVNTDNRLMSGTSMSREMSLLVEAFGYGWKELQWFTINA 330
Cdd:COG1816 223 ARLADRGIPLEVCPTSNVQLGVVPSLAEHPLRRLLDAGVRVTLNTDDPLYFGTTLTDEYELAAEAFGLSDADLAQLARNA 302
|
330 340
....*....|....*....|..
gi 503049013 331 MKSAFIPFDERLRIIDEVIKPA 352
Cdd:COG1816 303 IEASFLPEEEKAALLAELDAYF 324
|
|
| A_deaminase |
pfam00962 |
Adenosine deaminase; |
13-351 |
3.57e-131 |
|
Adenosine deaminase;
Pssm-ID: 425964 Cd Length: 330 Bit Score: 377.93 E-value: 3.57e-131
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503049013 13 PKALLHDHLDGGLRPATIVELAAEVGHELPTTDPAALGVWFTEAANSGSLERYLETFAHTVAVMQTPAALRRVARECALD 92
Cdd:pfam00962 1 PKAELHLHLDGSLRPDTLLELAKRYGIILPADFPEALEPLFRKYKKERDLQDFLDKYDIGVAVLRSPEDIRRLAFEYAED 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503049013 93 LAADGVVYAEVRFAPEQHLEQNLTLDEVVDAVVTGFREGsalAAEAGTPIRIgtLLTAMR--HAARSQEIAELAVRHRDT 170
Cdd:pfam00962 81 VAKDGVVYAEVRYDPQSHASRGLSPDTVVDAVLDAVDAA---EREFGITVRL--IVCAMRheHPECSREIAELAPRYRDQ 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503049013 171 GVVGFDIAGAEAGFPPTR---HLDAFEYLQRENFHFTIHAGEAFGLPSIWQAIQWCGADRLGHGVRIVDDitpgnppvlG 247
Cdd:pfam00962 156 GIVAFGLAGDEKGFPPSLfrdHVEAFARARDAGLHLTVHAGEAGGPQSVWEALDDLGAERIGHGVRSAED---------P 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503049013 248 RLAAYVRDKRIPLELCPSSNVQTGAAASIADHPIGLLRDLRFRVTVNTDNRLMSGTSMSREMSLLVEAFGYGWKELQWFT 327
Cdd:pfam00962 227 RLLDRLADRQIPLEICPTSNVQTGAVASLAEHPLKTFLRAGVPVSLNTDDPLMFGSDLLDEYQVAKRAPGFDEEELARLA 306
|
330 340
....*....|....*....|....
gi 503049013 328 INAMKSAFIPFDERLRIIDEVIKP 351
Cdd:pfam00962 307 KNAVKGSFLPADEKRALLDEVDKV 330
|
|
| ADA |
cd01320 |
Adenosine deaminase (ADA) is a monomeric zinc dependent enzyme which catalyzes the ... |
11-348 |
3.79e-120 |
|
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: 349.97 E-value: 3.79e-120
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503049013 11 KVPKALLHDHLDGGLRPATIVELAAEVGHELPTTDPAaLGVWFTEAANSGSLERYLETFAHTVAVMQTPAALRRVARECA 90
Cdd:cd01320 1 NLPKAELHLHLDGSLRPETILELAKKNGITLPASDVE-LLELVVAAYNFSDLQDFLAKYDFGLSVLQTEEDFERLAYEYL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503049013 91 LDLAADGVVYAEVRFAPEQHLEQNLTLDEVVDAVVTGFREgsalaAEAGTPIRIGTLLTAMRH--AARSQEIAELAVRHR 168
Cdd:cd01320 80 EDAAADGVVYAEIRFSPQLHTRRGLSFDEVVEAVLRGLDE-----AEAEFGIKARLILCGLRHlsPESAQETLELALKYR 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503049013 169 DTGVVGFDIAGAEAGFPPTRHLDAFEYLQRENFHFTIHAGEAFGLPSIWQAIQWCGADRLGHGVRIVDDItpgnppvlgR 248
Cdd:cd01320 155 DKGVVGFDLAGDEVGFPPEKFVRAFQRAREAGLRLTAHAGEAGGPESVRDALDLLGAERIGHGIRAIEDP---------E 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503049013 249 LAAYVRDKRIPLELCPSSNVQTGAAASIADHPIGLLRDLRFRVTVNTDNRLMSGTSMSREMSLLVEAFGYGWKELQWFTI 328
Cdd:cd01320 226 LVKRLAERNIPLEVCPTSNVQTGAVKSLAEHPLRELLDAGVKVTINTDDPTVFGTYLTDEYELLAEAFGLTEEELKKLAR 305
|
330 340
....*....|....*....|
gi 503049013 329 NAMKSAFIPFDERLRIIDEV 348
Cdd:cd01320 306 NAVEASFLSEEEKAELLKRI 325
|
|
| aden_deam |
TIGR01430 |
adenosine deaminase; This family includes the experimentally verified adenosine deaminases of ... |
13-341 |
1.89e-79 |
|
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: 246.11 E-value: 1.89e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503049013 13 PKALLHDHLDGGLRPATIVELAAEVGHELPTTDPAalGVWFTEAANS-GSLERYLETFAHTVAVMQTPAALRRVARECAL 91
Cdd:TIGR01430 2 PKAELHLHLEGSIRPETLLELAQKNGIPLPADLQS--GEELKEAYDKfRDLQDFLAKYDFGVEVLRTEDDFKRLAYEYVE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503049013 92 DLAADGVVYAEVRFAPEQHLEQNLTLDEVVDAVVTGFREgsalaAEAGTPIRIGTLLTAMRHAA--RSQEIAELAVRHRD 169
Cdd:TIGR01430 80 KAAKDGVVYAEVFFDPQLHTNRGISPDTVVEAVLDGLDE-----AERDFGIKSRLILCGMRHKQpeAAEETLELAKPYKE 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503049013 170 TGVVGFDIAGAEAGFPPTRHLDAFEYLQRENFHFTIHAGEAFGLPSIWQAIQWCGADRLGHGVRIVDDitpgnppvlGRL 249
Cdd:TIGR01430 155 QTIVGFGLAGDERGGPPPDFVRAFAIARELGLHLTVHAGELGGPESVREALDDLGATRIGHGVRALED---------PEL 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503049013 250 AAYVRDKRIPLELCPSSNVQTGAAASIADHPIGLLRDLRFRVTVNTDNRLMSGTSMSREMSLLVEAFGYGWKELQWFTIN 329
Cdd:TIGR01430 226 LKRLAQENITLEVCPTSNVALGVVKSLAEHPLRRFLEAGVKVTLNSDDPAYFGSYLTEEYEIAAKHAGLTEEELKQLARN 305
|
330
....*....|..
gi 503049013 330 AMKSAFIPFDER 341
Cdd:TIGR01430 306 ALEGSFLSDDEK 317
|
|
| ADA_AMPD |
cd00443 |
Adenosine/AMP deaminase. Adenosine deaminases (ADAs) are present in pro- and eukaryotic ... |
13-335 |
3.72e-45 |
|
Adenosine/AMP deaminase. Adenosine deaminases (ADAs) are present in pro- and eukaryotic organisms and catalyze the zinc dependent irreversible deamination of adenosine nucleosides to inosine nucleosides and ammonia. The eukaryotic AMP deaminase catalyzes a similar reaction leading to the hydrolytic removal of an amino group at the 6 position of the adenine nucleotide ring, a branch point in the adenylate catabolic pathway.
Pssm-ID: 238250 Cd Length: 305 Bit Score: 156.74 E-value: 3.72e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503049013 13 PKALLHDHLDGGLRPATIVELAAEvghelpttdpaalgvwfteaansgsleRYLETFAHTVAVMQTPAALRRVARECALD 92
Cdd:cd00443 2 PKVELHAHLSGSISPETLLELIKK---------------------------EFFEKFLLVHNLLQKGEALARALKEVIEE 54
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503049013 93 LAADGVVYAEVRFAPeQHLEQN--LTLDEVVDAVVTGFREgsalAAEAGTPIRIGTLLTAMRH------AARSQEIAELA 164
Cdd:cd00443 55 FAEDNVQYLELRTTP-RLLETEkgLTKEQYWLLVIEGISE----AKQWFPPIKVRLILSVDRRgpyvqnYLVASEILELA 129
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503049013 165 VRHRDTgVVGFDIAGAEAGF--PPTRHLDAFEYLQR-ENFHFTIHAGEAFGLPSIWQAIQWCgADRLGHGVRIVDDitpg 241
Cdd:cd00443 130 KFLSNY-VVGIDLVGDESKGenPLRDFYSYYEYARRlGLLGLTLHCGETGNREELLQALLLL-PDRIGHGIFLLKH---- 203
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503049013 242 npPVLGRLaayVRDKRIPLELCPSSNVQTGAAASIADHPIGLLRDLRFRVTVNTDNRLMSGTSMSREMSLLVEAFGYGWK 321
Cdd:cd00443 204 --PELIYL---VKLRNIPIEVCPTSNVVLGTVQSYEKHPFMRFFKAGLPVSLSTDDPGIFGTSLSEEYSLAAKTFGLTFE 278
|
330
....*....|....
gi 503049013 322 ELQWFTINAMKSAF 335
Cdd:cd00443 279 DLCELNRNSVLSSF 292
|
|
| PTZ00124 |
PTZ00124 |
adenosine deaminase; Provisional |
11-345 |
5.08e-38 |
|
adenosine deaminase; Provisional
Pssm-ID: 173415 Cd Length: 362 Bit Score: 139.62 E-value: 5.08e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503049013 11 KVPKALLHDHLDGGLRPATIVELAAEVGHELPTTDPAALGvWFTEAANSGSLERYLETFAHTVAVMQTPAALRRVARECA 90
Cdd:PTZ00124 34 RIPKCELHCHLDLCFSVDFFLSCIRKYNLQPNLSDEEILD-YYLFAKGGKSLGEFVEKAIRVADIFNDYEVIEDLAKHAV 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503049013 91 LDLAADGVVYAEVRFAPEQHLEQ-NLTLDEVVDAVVTGFREGSALAAeagTPIRIGTLLTAM--RHAARSQEIAELAVRH 167
Cdd:PTZ00124 113 FNKYKEGVVLMEFRYSPTFVAFKhNLDIDLIHQAIVKGIKEAVELLD---HKIEVGLLCIGDtgHDAAPIKESADFCLKH 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503049013 168 RDTgVVGFDIAGAEAGFPPTRhlDAFEYLQRENFHFTIHAGEAFGLP---SIWQAIQWCGADRLGHGVRIVDditpgNPP 244
Cdd:PTZ00124 190 KAD-FVGFDHAGHEVDLKPFK--DIFDYVREAGVNLTVHAGEDVTLPnlnTLYSAIQVLKVKRIGHGIRVAE-----SQE 261
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503049013 245 VLGRlaayVRDKRIPLELCPSSNVQTGAAASIADHPIGLLRDLRFRVTVNTDNRLMSGTSMSREMSLLVEAFGYGWKELQ 324
Cdd:PTZ00124 262 LIDM----VKEKDILLEVCPISNVLLNNAKSMDTHPIRKLYDAGVKVSVNSDDPGMFLTNINDDYEELYTHLNFTLADFM 337
|
330 340
....*....|....*....|.
gi 503049013 325 WFTINAMKSAFIPFDERLRII 345
Cdd:PTZ00124 338 KMNEWALEKSFLDKDIKLKIK 358
|
|
| ADGF |
cd01321 |
Adenosine deaminase-related growth factors (ADGF), a novel family of secreted growth-factors ... |
6-297 |
3.53e-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: 63.45 E-value: 3.53e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503049013 6 YEDIVKVPK-ALLHDHLDGGLRPATIVELAaevghelpttdpaalgvwfteaansgsLERYLETFAHTVAVMQTPAALRR 84
Cdd:cd01321 18 FKIIQKMPKgALLHVHDTAMVSSDWLIKNA---------------------------TYRFEQIFDIIDGLLTYLPIFRD 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503049013 85 VARECALDLAADGVVYAEVRFAPEQHLE---QNLTLDEVVDA---VVTGFREgsalaaeagTP-----IRIgtLLTAMRH 153
Cdd:cd01321 71 YYRRLLEELYEDNVQYVELRSSFSPLYDldgREYDYEETVQLleeVVEKFKK---------THpdfigLKI--IYATLRN 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503049013 154 AARSqEIAE-----LAVRHRDTG-VVGFDIAGAE-AGFPPTRHLDAFEYLQRENFH--FTIHAGEafglpSIWQ------ 218
Cdd:cd01321 140 FNDS-EIKEsmeqcLNLKKKFPDfIAGFDLVGQEdAGRPLLDFLPQLLWFPKQCAEipFFFHAGE-----TNGDgtetde 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503049013 219 ----AIqWCGADRLGHGVRIvdditPGNPpvlgRLAAYVRDKRIPLELCPSSNVQTGAAASIADHPIGLLRDLRFRVTVN 294
Cdd:cd01321 214 nlvdAL-LLNTKRIGHGFAL-----PKHP----LLMDLVKKKNIAIEVCPISNQVLGLVSDLRNHPAAALLARGVPVVIS 283
|
...
gi 503049013 295 TDN 297
Cdd:cd01321 284 SDD 286
|
|
| metallo-dependent_hydrolases |
cd01292 |
Superfamily of metallo-dependent hydrolases (also called amidohydrolase superfamily) is a ... |
78-330 |
7.15e-06 |
|
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: 46.94 E-value: 7.15e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503049013 78 TPAALRRVARECALDLAADGVVYAEVR---FAPEQHLEQNLTLDEvvdavvtgfregsalAAEAGTPIRIGTLLTAMRHA 154
Cdd:cd01292 29 SPEDLYEDTLRALEALLAGGVTTVVDMgstPPPTTTKAAIEAVAE---------------AARASAGIRVVLGLGIPGVP 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503049013 155 ARSQEIAELAVRHR-----DTGVVGFDIAGAEAGFPPTR--HLDAFEYLQRENFHFTIHAGEAfglPSIWQAIQWcGADR 227
Cdd:cd01292 94 AAVDEDAEALLLELlrrglELGAVGLKLAGPYTATGLSDesLRRVLEEARKLGLPVVIHAGEL---PDPTRALED-LVAL 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503049013 228 LGHGVRIVddITPGNPPVLGRLAAYVRDKrIPLELCPSSNVQTGAAASIAdHPIGLLRDLRFRVTVNTDNRLM-SGTSMS 306
Cdd:cd01292 170 LRLGGRVV--IGHVSHLDPELLELLKEAG-VSLEVCPLSNYLLGRDGEGA-EALRRLLELGIRVTLGTDGPPHpLGTDLL 245
|
250 260
....*....|....*....|....*..
gi 503049013 307 REMSLLVEAFGYGWKE---LQWFTINA 330
Cdd:cd01292 246 ALLRLLLKVLRLGLSLeeaLRLATINP 272
|
|
| archeal_chlorohydrolases |
cd01305 |
Predicted chlorohydrolases. These metallo-dependent hydrolases from archea are part of the ... |
191-309 |
1.01e-03 |
|
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: 40.46 E-value: 1.01e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503049013 191 DAFEYLQRENFHFTIHAGE---AFGLPSIWQAIQwCGADRLGHGVRIVDDITpgnppvlgrlaAYVRDKRIPLELCPSSN 267
Cdd:cd01305 129 DILELLRRRGKLFAIHASEtreSVGMTDIERALD-LEPDLLVHGTHLTDEDL-----------ELVRENGVPVVLCPRSN 196
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 503049013 268 vqtgAAASIADHPIGLLRDLRFRVTVNTDNRLMSGTSMSREM 309
Cdd:cd01305 197 ----LYFGVGIPPVAELLKLGIKVLLGTDNVMVNEPDMWAEM 234
|
|
| |
