|
Name |
Accession |
Description |
Interval |
E-value |
| ADA_AMPD |
cd00443 |
Adenosine/AMP deaminase. Adenosine deaminases (ADAs) are present in pro- and eukaryotic ... |
18-345 |
5.61e-115 |
|
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: 335.86 E-value: 5.61e-115
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767983456 18 LPKVELHAHLNGSISSHTMKKLIAQkpdlkihdqmtvidkgkkrtleECFQMFQTIHQLTSSPEDILMVTKDVIKEFADD 97
Cdd:cd00443 1 LPKVELHAHLSGSISPETLLELIKK----------------------EFFEKFLLVHNLLQKGEALARALKEVIEEFAED 58
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767983456 98 GVKYLELRSTPR-RENATGMTKKTYVESILEGIKQSKQENLDIDVRYLIAVDRRGGP----LVAKETVKLAEEFFLsteg 172
Cdd:cd00443 59 NVQYLELRTTPRlLETEKGLTKEQYWLLVIEGISEAKQWFPPIKVRLILSVDRRGPYvqnyLVASEILELAKFLSN---- 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767983456 173 TVLGLDLSGDPTVG--QAKDFLEPLLEAKKAG-LKLALHLSEIPNQKKETQiLLDLLPDRIGHGTFLNSGEggslDLVDF 249
Cdd:cd00443 135 YVVGIDLVGDESKGenPLRDFYSYYEYARRLGlLGLTLHCGETGNREELLQ-ALLLLPDRIGHGIFLLKHP----ELIYL 209
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767983456 250 VRQHRIPLELCLTSNVKSQTVPSYDQHHFGFWYSIAHPSVICTDDKGVFATHLSQEYQLAAETFNLTQSQVWDLSYESIN 329
Cdd:cd00443 210 VKLRNIPIEVCPTSNVVLGTVQSYEKHPFMRFFKAGLPVSLSTDDPGIFGTSLSEEYSLAAKTFGLTFEDLCELNRNSVL 289
|
330
....*....|....*.
gi 767983456 330 YIFASDSTRSELRKKW 345
Cdd:cd00443 290 SSFAKDEEKKSLLEVL 305
|
|
| Add |
COG1816 |
Adenosine deaminase [Nucleotide transport and metabolism]; Adenosine deaminase is part of the ... |
19-345 |
1.94e-57 |
|
Adenosine deaminase [Nucleotide transport and metabolism]; Adenosine deaminase is part of the Pathway/BioSystem: Menaquinone biosynthesis
Pssm-ID: 441421 Cd Length: 326 Bit Score: 189.14 E-value: 1.94e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767983456 19 PKVELHAHLNGSISSHTMKKLIAQKP-DLKIHDQMTVIDKGKKRTLEECFQMFQTIHQLTSSPEDILMVTKDVIKEFADD 97
Cdd:COG1816 1 PKAELHLHLEGSLRPETLLELAARNGiDLPAADVEELRAAYDFRDLQSFLDTYDAGAAVLQTEEDFRRLAYEYLEDAAAD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767983456 98 GVKYLELRSTPrrENAT--GMTKKTYVESILEGIKQSKQEnLDIDVRYLIAVDRRGGPLVAKETVKLAEEFflsTEGTVL 175
Cdd:COG1816 81 GVRYAEIRFDP--QLHTrrGLSLEEVVEAVLDGLREAERE-FGISVRLILCALRHLSPEAAFETLELALRY---RDRGVV 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767983456 176 GLDLSGDPTVGQAKDFLEPLLEAKKAGLKLALHLSE------IpnqkkeTQILLDLLPDRIGHGTflNSGEggSLDLVDF 249
Cdd:COG1816 155 GFGLAGDERGFPPEKFAEAFARAREAGLHLTAHAGEaggpesI------WEALDLLGAERIGHGV--RAIE--DPALVAR 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767983456 250 VRQHRIPLELCLTSNVKSQTVPSYDQHHF------GFwysiahPSVICTDDKGVFATHLSQEYQLAAETFNLTQSQVWDL 323
Cdd:COG1816 225 LADRGIPLEVCPTSNVQLGVVPSLAEHPLrrlldaGV------RVTLNTDDPLYFGTTLTDEYELAAEAFGLSDADLAQL 298
|
330 340
....*....|....*....|..
gi 767983456 324 SYESINYIFASDSTRSELRKKW 345
Cdd:COG1816 299 ARNAIEASFLPEEEKAALLAEL 320
|
|
| PRK09358 |
PRK09358 |
adenosine deaminase; Provisional |
13-344 |
2.46e-55 |
|
adenosine deaminase; Provisional
Pssm-ID: 236480 Cd Length: 340 Bit Score: 184.22 E-value: 2.46e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767983456 13 DFYSELPKVELHAHLNGSISSHTMKKLiAQKPDLKIHDQmTVIDKGKKRTLEEC--FQMFQTIHQLTSS----PEDILMV 86
Cdd:PRK09358 5 MIIRSLPKAELHLHLDGSLRPETILEL-ARRNGIALPAT-DVEELPWVRAAYDFrdLQSFLDKYDAGVAvlqtEEDLRRL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767983456 87 TKDVIKEFADDGVKYLELRSTPRRENATGMTKKTYVESILEGIKQSKQEnLDIDVRYLIAVDRRGG-PLVAKETVKLAEE 165
Cdd:PRK09358 83 AFEYLEDAAADGVVYAEIRFDPQLHTERGLPLEEVVEAVLDGLRAAEAE-FGISVRLILCFMRHFGeEAAARELEALAAR 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767983456 166 FFlstEGTVLGLDLSGDPTVGQAKDFLEPLLEAKKAGLKLALHLSE--IPNQKKETqilLDLL-PDRIGHGTFLNsgegG 242
Cdd:PRK09358 162 YR---DDGVVGFDLAGDELGFPPSKFARAFDRARDAGLRLTAHAGEagGPESIWEA---LDELgAERIGHGVRAI----E 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767983456 243 SLDLVDFVRQHRIPLELCLTSNVKSQTVPSYDQHHF------GFWYSIAhpsvicTDDKGVFATHLSQEYQLAAETFNLT 316
Cdd:PRK09358 232 DPALMARLADRRIPLEVCPTSNVQTGAVPSLAEHPLktlldaGVRVTIN------TDDPLVFGTTLTEEYEALAEAFGLS 305
|
330 340
....*....|....*....|....*...
gi 767983456 317 QSQVWDLSYESINYIFASDSTRSELRKK 344
Cdd:PRK09358 306 DEDLAQLARNALEAAFLSEEEKAALLAE 333
|
|
| A_deaminase |
pfam00962 |
Adenosine deaminase; |
19-344 |
9.46e-48 |
|
Adenosine deaminase;
Pssm-ID: 425964 Cd Length: 330 Bit Score: 164.14 E-value: 9.46e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767983456 19 PKVELHAHLNGSISSHTMKKLiAQKPDLKIHDQM--TVIDKGKKRTLEECFQMFQTIH----QLTSSPEDILMVTKDVIK 92
Cdd:pfam00962 1 PKAELHLHLDGSLRPDTLLEL-AKRYGIILPADFpeALEPLFRKYKKERDLQDFLDKYdigvAVLRSPEDIRRLAFEYAE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767983456 93 EFADDGVKYLELRSTPRRENATGMTKKTYVESILEGIKQSKQEnLDIDVRYLIAVDRRGGPLVAKETVKLAEEFflsTEG 172
Cdd:pfam00962 80 DVAKDGVVYAEVRYDPQSHASRGLSPDTVVDAVLDAVDAAERE-FGITVRLIVCAMRHEHPECSREIAELAPRY---RDQ 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767983456 173 TVLGLDLSGDPTV---GQAKDFLEPLLEAKKAGLKLALHLSEIPNQKKETQILLDLLPDRIGHGTflNSGEGGSLdlVDF 249
Cdd:pfam00962 156 GIVAFGLAGDEKGfppSLFRDHVEAFARARDAGLHLTVHAGEAGGPQSVWEALDDLGAERIGHGV--RSAEDPRL--LDR 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767983456 250 VRQHRIPLELCLTSNVKSQTVPSYDQHHFGFWYSIAHPSVICTDDKGVFATHLSQEYQLAAETFNLTQSQVWDLSYESIN 329
Cdd:pfam00962 232 LADRQIPLEICPTSNVQTGAVASLAEHPLKTFLRAGVPVSLNTDDPLMFGSDLLDEYQVAKRAPGFDEEELARLAKNAVK 311
|
330
....*....|....*
gi 767983456 330 YIFASDSTRSELRKK 344
Cdd:pfam00962 312 GSFLPADEKRALLDE 326
|
|
| aden_deam |
TIGR01430 |
adenosine deaminase; This family includes the experimentally verified adenosine deaminases of ... |
18-341 |
1.45e-47 |
|
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: 163.68 E-value: 1.45e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767983456 18 LPKVELHAHLNGSISSHTMKKLiAQKPDLKIHDQMTVIDKGKKR-TLEECFQMFQTIH----QLTSSPEDILMVTKDVIK 92
Cdd:TIGR01430 1 LPKAELHLHLEGSIRPETLLEL-AQKNGIPLPADLQSGEELKEAyDKFRDLQDFLAKYdfgvEVLRTEDDFKRLAYEYVE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767983456 93 EFADDGVKYLELRSTPRRENATGMTKKTYVESILEGIKQSKQEnLDIDVRYLIAVDRRGGPLVAKETVKLAEEFflsTEG 172
Cdd:TIGR01430 80 KAAKDGVVYAEVFFDPQLHTNRGISPDTVVEAVLDGLDEAERD-FGIKSRLILCGMRHKQPEAAEETLELAKPY---KEQ 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767983456 173 TVLGLDLSGDPTVGQAKDFLEPLLEAKKAGLKLALHLSEIPNQKKETQILLDLLPDRIGHGTFLNSGEggslDLVDFVRQ 252
Cdd:TIGR01430 156 TIVGFGLAGDERGGPPPDFVRAFAIARELGLHLTVHAGELGGPESVREALDDLGATRIGHGVRALEDP----ELLKRLAQ 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767983456 253 HRIPLELCLTSNVKSQTVPSYDQHHFGFWYSIAHPSVICTDDKGVFATHLSQEYQLAAETFNLTQSQVWDLSYESINYIF 332
Cdd:TIGR01430 232 ENITLEVCPTSNVALGVVKSLAEHPLRRFLEAGVKVTLNSDDPAYFGSYLTEEYEIAAKHAGLTEEELKQLARNALEGSF 311
|
....*....
gi 767983456 333 ASDSTRSEL 341
Cdd:TIGR01430 312 LSDDEKKEL 320
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| ADA_AMPD |
cd00443 |
Adenosine/AMP deaminase. Adenosine deaminases (ADAs) are present in pro- and eukaryotic ... |
18-345 |
5.61e-115 |
|
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: 335.86 E-value: 5.61e-115
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767983456 18 LPKVELHAHLNGSISSHTMKKLIAQkpdlkihdqmtvidkgkkrtleECFQMFQTIHQLTSSPEDILMVTKDVIKEFADD 97
Cdd:cd00443 1 LPKVELHAHLSGSISPETLLELIKK----------------------EFFEKFLLVHNLLQKGEALARALKEVIEEFAED 58
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767983456 98 GVKYLELRSTPR-RENATGMTKKTYVESILEGIKQSKQENLDIDVRYLIAVDRRGGP----LVAKETVKLAEEFFLsteg 172
Cdd:cd00443 59 NVQYLELRTTPRlLETEKGLTKEQYWLLVIEGISEAKQWFPPIKVRLILSVDRRGPYvqnyLVASEILELAKFLSN---- 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767983456 173 TVLGLDLSGDPTVG--QAKDFLEPLLEAKKAG-LKLALHLSEIPNQKKETQiLLDLLPDRIGHGTFLNSGEggslDLVDF 249
Cdd:cd00443 135 YVVGIDLVGDESKGenPLRDFYSYYEYARRLGlLGLTLHCGETGNREELLQ-ALLLLPDRIGHGIFLLKHP----ELIYL 209
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767983456 250 VRQHRIPLELCLTSNVKSQTVPSYDQHHFGFWYSIAHPSVICTDDKGVFATHLSQEYQLAAETFNLTQSQVWDLSYESIN 329
Cdd:cd00443 210 VKLRNIPIEVCPTSNVVLGTVQSYEKHPFMRFFKAGLPVSLSTDDPGIFGTSLSEEYSLAAKTFGLTFEDLCELNRNSVL 289
|
330
....*....|....*.
gi 767983456 330 YIFASDSTRSELRKKW 345
Cdd:cd00443 290 SSFAKDEEKKSLLEVL 305
|
|
| ADA |
cd01320 |
Adenosine deaminase (ADA) is a monomeric zinc dependent enzyme which catalyzes the ... |
17-344 |
3.27e-62 |
|
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: 201.66 E-value: 3.27e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767983456 17 ELPKVELHAHLNGSISSHTMKKLIAQK----PDLKIHDQMTVIDKGKKRTLEECFQMFQTIHQLTSSPEDILMVTKDVIK 92
Cdd:cd01320 1 NLPKAELHLHLDGSLRPETILELAKKNgitlPASDVELLELVVAAYNFSDLQDFLAKYDFGLSVLQTEEDFERLAYEYLE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767983456 93 EFADDGVKYLELRSTPRRENATGMTKKTYVESILEGIKQSKqENLDIDVRYLIAVDRRGGPLVAKETVKLAEEFflsTEG 172
Cdd:cd01320 81 DAAADGVVYAEIRFSPQLHTRRGLSFDEVVEAVLRGLDEAE-AEFGIKARLILCGLRHLSPESAQETLELALKY---RDK 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767983456 173 TVLGLDLSGDPTVGQAKDFLEPLLEAKKAGLKLALHLSEIPNQKKETQILLDLLPDRIGHGTFLnsgeGGSLDLVDFVRQ 252
Cdd:cd01320 157 GVVGFDLAGDEVGFPPEKFVRAFQRAREAGLRLTAHAGEAGGPESVRDALDLLGAERIGHGIRA----IEDPELVKRLAE 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767983456 253 HRIPLELCLTSNVKSQTVPSYDQHHFGFWYSIAHPSVICTDDKGVFATHLSQEYQLAAETFNLTQSQVWDLSYESINYIF 332
Cdd:cd01320 233 RNIPLEVCPTSNVQTGAVKSLAEHPLRELLDAGVKVTINTDDPTVFGTYLTDEYELLAEAFGLTEEELKKLARNAVEASF 312
|
330
....*....|..
gi 767983456 333 ASDSTRSELRKK 344
Cdd:cd01320 313 LSEEEKAELLKR 324
|
|
| Add |
COG1816 |
Adenosine deaminase [Nucleotide transport and metabolism]; Adenosine deaminase is part of the ... |
19-345 |
1.94e-57 |
|
Adenosine deaminase [Nucleotide transport and metabolism]; Adenosine deaminase is part of the Pathway/BioSystem: Menaquinone biosynthesis
Pssm-ID: 441421 Cd Length: 326 Bit Score: 189.14 E-value: 1.94e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767983456 19 PKVELHAHLNGSISSHTMKKLIAQKP-DLKIHDQMTVIDKGKKRTLEECFQMFQTIHQLTSSPEDILMVTKDVIKEFADD 97
Cdd:COG1816 1 PKAELHLHLEGSLRPETLLELAARNGiDLPAADVEELRAAYDFRDLQSFLDTYDAGAAVLQTEEDFRRLAYEYLEDAAAD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767983456 98 GVKYLELRSTPrrENAT--GMTKKTYVESILEGIKQSKQEnLDIDVRYLIAVDRRGGPLVAKETVKLAEEFflsTEGTVL 175
Cdd:COG1816 81 GVRYAEIRFDP--QLHTrrGLSLEEVVEAVLDGLREAERE-FGISVRLILCALRHLSPEAAFETLELALRY---RDRGVV 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767983456 176 GLDLSGDPTVGQAKDFLEPLLEAKKAGLKLALHLSE------IpnqkkeTQILLDLLPDRIGHGTflNSGEggSLDLVDF 249
Cdd:COG1816 155 GFGLAGDERGFPPEKFAEAFARAREAGLHLTAHAGEaggpesI------WEALDLLGAERIGHGV--RAIE--DPALVAR 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767983456 250 VRQHRIPLELCLTSNVKSQTVPSYDQHHF------GFwysiahPSVICTDDKGVFATHLSQEYQLAAETFNLTQSQVWDL 323
Cdd:COG1816 225 LADRGIPLEVCPTSNVQLGVVPSLAEHPLrrlldaGV------RVTLNTDDPLYFGTTLTDEYELAAEAFGLSDADLAQL 298
|
330 340
....*....|....*....|..
gi 767983456 324 SYESINYIFASDSTRSELRKKW 345
Cdd:COG1816 299 ARNAIEASFLPEEEKAALLAEL 320
|
|
| PRK09358 |
PRK09358 |
adenosine deaminase; Provisional |
13-344 |
2.46e-55 |
|
adenosine deaminase; Provisional
Pssm-ID: 236480 Cd Length: 340 Bit Score: 184.22 E-value: 2.46e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767983456 13 DFYSELPKVELHAHLNGSISSHTMKKLiAQKPDLKIHDQmTVIDKGKKRTLEEC--FQMFQTIHQLTSS----PEDILMV 86
Cdd:PRK09358 5 MIIRSLPKAELHLHLDGSLRPETILEL-ARRNGIALPAT-DVEELPWVRAAYDFrdLQSFLDKYDAGVAvlqtEEDLRRL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767983456 87 TKDVIKEFADDGVKYLELRSTPRRENATGMTKKTYVESILEGIKQSKQEnLDIDVRYLIAVDRRGG-PLVAKETVKLAEE 165
Cdd:PRK09358 83 AFEYLEDAAADGVVYAEIRFDPQLHTERGLPLEEVVEAVLDGLRAAEAE-FGISVRLILCFMRHFGeEAAARELEALAAR 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767983456 166 FFlstEGTVLGLDLSGDPTVGQAKDFLEPLLEAKKAGLKLALHLSE--IPNQKKETqilLDLL-PDRIGHGTFLNsgegG 242
Cdd:PRK09358 162 YR---DDGVVGFDLAGDELGFPPSKFARAFDRARDAGLRLTAHAGEagGPESIWEA---LDELgAERIGHGVRAI----E 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767983456 243 SLDLVDFVRQHRIPLELCLTSNVKSQTVPSYDQHHF------GFWYSIAhpsvicTDDKGVFATHLSQEYQLAAETFNLT 316
Cdd:PRK09358 232 DPALMARLADRRIPLEVCPTSNVQTGAVPSLAEHPLktlldaGVRVTIN------TDDPLVFGTTLTEEYEALAEAFGLS 305
|
330 340
....*....|....*....|....*...
gi 767983456 317 QSQVWDLSYESINYIFASDSTRSELRKK 344
Cdd:PRK09358 306 DEDLAQLARNALEAAFLSEEEKAALLAE 333
|
|
| A_deaminase |
pfam00962 |
Adenosine deaminase; |
19-344 |
9.46e-48 |
|
Adenosine deaminase;
Pssm-ID: 425964 Cd Length: 330 Bit Score: 164.14 E-value: 9.46e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767983456 19 PKVELHAHLNGSISSHTMKKLiAQKPDLKIHDQM--TVIDKGKKRTLEECFQMFQTIH----QLTSSPEDILMVTKDVIK 92
Cdd:pfam00962 1 PKAELHLHLDGSLRPDTLLEL-AKRYGIILPADFpeALEPLFRKYKKERDLQDFLDKYdigvAVLRSPEDIRRLAFEYAE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767983456 93 EFADDGVKYLELRSTPRRENATGMTKKTYVESILEGIKQSKQEnLDIDVRYLIAVDRRGGPLVAKETVKLAEEFflsTEG 172
Cdd:pfam00962 80 DVAKDGVVYAEVRYDPQSHASRGLSPDTVVDAVLDAVDAAERE-FGITVRLIVCAMRHEHPECSREIAELAPRY---RDQ 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767983456 173 TVLGLDLSGDPTV---GQAKDFLEPLLEAKKAGLKLALHLSEIPNQKKETQILLDLLPDRIGHGTflNSGEGGSLdlVDF 249
Cdd:pfam00962 156 GIVAFGLAGDEKGfppSLFRDHVEAFARARDAGLHLTVHAGEAGGPQSVWEALDDLGAERIGHGV--RSAEDPRL--LDR 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767983456 250 VRQHRIPLELCLTSNVKSQTVPSYDQHHFGFWYSIAHPSVICTDDKGVFATHLSQEYQLAAETFNLTQSQVWDLSYESIN 329
Cdd:pfam00962 232 LADRQIPLEICPTSNVQTGAVASLAEHPLKTFLRAGVPVSLNTDDPLMFGSDLLDEYQVAKRAPGFDEEELARLAKNAVK 311
|
330
....*....|....*
gi 767983456 330 YIFASDSTRSELRKK 344
Cdd:pfam00962 312 GSFLPADEKRALLDE 326
|
|
| aden_deam |
TIGR01430 |
adenosine deaminase; This family includes the experimentally verified adenosine deaminases of ... |
18-341 |
1.45e-47 |
|
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: 163.68 E-value: 1.45e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767983456 18 LPKVELHAHLNGSISSHTMKKLiAQKPDLKIHDQMTVIDKGKKR-TLEECFQMFQTIH----QLTSSPEDILMVTKDVIK 92
Cdd:TIGR01430 1 LPKAELHLHLEGSIRPETLLEL-AQKNGIPLPADLQSGEELKEAyDKFRDLQDFLAKYdfgvEVLRTEDDFKRLAYEYVE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767983456 93 EFADDGVKYLELRSTPRRENATGMTKKTYVESILEGIKQSKQEnLDIDVRYLIAVDRRGGPLVAKETVKLAEEFflsTEG 172
Cdd:TIGR01430 80 KAAKDGVVYAEVFFDPQLHTNRGISPDTVVEAVLDGLDEAERD-FGIKSRLILCGMRHKQPEAAEETLELAKPY---KEQ 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767983456 173 TVLGLDLSGDPTVGQAKDFLEPLLEAKKAGLKLALHLSEIPNQKKETQILLDLLPDRIGHGTFLNSGEggslDLVDFVRQ 252
Cdd:TIGR01430 156 TIVGFGLAGDERGGPPPDFVRAFAIARELGLHLTVHAGELGGPESVREALDDLGATRIGHGVRALEDP----ELLKRLAQ 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767983456 253 HRIPLELCLTSNVKSQTVPSYDQHHFGFWYSIAHPSVICTDDKGVFATHLSQEYQLAAETFNLTQSQVWDLSYESINYIF 332
Cdd:TIGR01430 232 ENITLEVCPTSNVALGVVKSLAEHPLRRFLEAGVKVTLNSDDPAYFGSYLTEEYEIAAKHAGLTEEELKQLARNALEGSF 311
|
....*....
gi 767983456 333 ASDSTRSEL 341
Cdd:TIGR01430 312 LSDDEKKEL 320
|
|
| ADGF |
cd01321 |
Adenosine deaminase-related growth factors (ADGF), a novel family of secreted growth-factors ... |
23-346 |
4.17e-17 |
|
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: 81.16 E-value: 4.17e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767983456 23 LHAHLNGSISSHTMKKLIAQKPDlkihdqmtvidkgkkrtleecfQMFQTIHQL-TSSPedilmVTKDVI----KEFADD 97
Cdd:cd01321 30 LHVHDTAMVSSDWLIKNATYRFE----------------------QIFDIIDGLlTYLP-----IFRDYYrrllEELYED 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767983456 98 GVKYLELRSTPRRENATGMTKKTYVES--ILEGI--KQSKQENLDIDVRYLIAVDRRGGPLVAKETVKLAEEFFLSTEGT 173
Cdd:cd01321 83 NVQYVELRSSFSPLYDLDGREYDYEETvqLLEEVveKFKKTHPDFIGLKIIYATLRNFNDSEIKESMEQCLNLKKKFPDF 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767983456 174 VLGLDLSGDPTVGQA-KDFLEPLLEAKK--AGLKLALHLSEIPNQKKETQI-LLD-LLPD--RIGHGTflnsgeggSL-- 244
Cdd:cd01321 163 IAGFDLVGQEDAGRPlLDFLPQLLWFPKqcAEIPFFFHAGETNGDGTETDEnLVDaLLLNtkRIGHGF--------ALpk 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767983456 245 --DLVDFVRQHRIPLELCLTSNVKSQTVPSYDQHHFGFWYSIAHPSVICTDDKGVF-ATHLSQE-YQ----LAAETFNLT 316
Cdd:cd01321 235 hpLLMDLVKKKNIAIEVCPISNQVLGLVSDLRNHPAAALLARGVPVVISSDDPGFWgAKGLSHDfYQafmgLAPADAGLR 314
|
330 340 350
....*....|....*....|....*....|..
gi 767983456 317 Q--SQVWDlsyeSINYIFASDSTRSELRKKWN 346
Cdd:cd01321 315 GlkQLAEN----SIRYSALSDQEKDEAVAKWE 342
|
|
| PTZ00124 |
PTZ00124 |
adenosine deaminase; Provisional |
15-345 |
5.59e-16 |
|
adenosine deaminase; Provisional
Pssm-ID: 173415 Cd Length: 362 Bit Score: 77.98 E-value: 5.59e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767983456 15 YSELPKVELHAHLNGSISshtMKKLIAQKPDLKIHDQMT---VID----KGKKRTLEECFQMFQTIHQLTSSPEDILMVT 87
Cdd:PTZ00124 32 WKRIPKCELHCHLDLCFS---VDFFLSCIRKYNLQPNLSdeeILDyylfAKGGKSLGEFVEKAIRVADIFNDYEVIEDLA 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767983456 88 KDVIKEFADDGVKYLELRSTPR-RENATGMTKKTYVESILEGIKQSKQEnldIDVRYLIAVDRRGGPLVAKETVKLAEEF 166
Cdd:PTZ00124 109 KHAVFNKYKEGVVLMEFRYSPTfVAFKHNLDIDLIHQAIVKGIKEAVEL---LDHKIEVGLLCIGDTGHDAAPIKESADF 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767983456 167 FLSTEGTVLGLDLSGDPTvgQAKDFLEPLLEAKKAGLKLALHLSE---IPNQKKETQILLDLLPDRIGHGTFLNSgeggS 243
Cdd:PTZ00124 186 CLKHKADFVGFDHAGHEV--DLKPFKDIFDYVREAGVNLTVHAGEdvtLPNLNTLYSAIQVLKVKRIGHGIRVAE----S 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767983456 244 LDLVDFVRQHRIPLELCLTSNVKSQTVPSYDQHHFGFWYSIAHPSVICTDDKGVFATHLSQEYQLAAETFNLTQSQVWDL 323
Cdd:PTZ00124 260 QELIDMVKEKDILLEVCPISNVLLNNAKSMDTHPIRKLYDAGVKVSVNSDDPGMFLTNINDDYEELYTHLNFTLADFMKM 339
|
330 340
....*....|....*....|..
gi 767983456 324 SYESINYIFASDSTRSELRKKW 345
Cdd:PTZ00124 340 NEWALEKSFLDKDIKLKIKKLY 361
|
|
| archeal_chlorohydrolases |
cd01305 |
Predicted chlorohydrolases. These metallo-dependent hydrolases from archea are part of the ... |
97-264 |
3.07e-07 |
|
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: 50.86 E-value: 3.07e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767983456 97 DGVKYLELRSTPRRENATGMtKKT--------------YVESILEGIKQSKQENLDIDVRYLIAVDRRGGPLVAKETVKL 162
Cdd:cd01305 35 DGLKHRLLAQADDRELAEAM-RKVlrdmretgigafadFREGGVEGIELLRRALGKLPVPFEVILGRPTEPDDPEILLEV 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767983456 163 AEefflstegtvlGLDLSG--DPtvgqakDFLEPLLEAKKAGLKLALHLSEIPNQKKETQI--LLDLLPDRIGHGTFLNS 238
Cdd:cd01305 114 AD-----------GLGLSSanDV------DLEDILELLRRRGKLFAIHASETRESVGMTDIerALDLEPDLLVHGTHLTD 176
|
170 180
....*....|....*....|....*.
gi 767983456 239 GEggsldlVDFVRQHRIPLELCLTSN 264
Cdd:cd01305 177 ED------LELVRENGVPVVLCPRSN 196
|
|
| metallo-dependent_hydrolases |
cd01292 |
Superfamily of metallo-dependent hydrolases (also called amidohydrolase superfamily) is a ... |
79-311 |
5.85e-05 |
|
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: 44.25 E-value: 5.85e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767983456 79 SPEDILMVTKDVIKEFADDGVKYLELRSTprreNATGMTKKTYVESILEGIkqskQENLDIDVRYLIAVDRRGGPLVAKE 158
Cdd:cd01292 29 SPEDLYEDTLRALEALLAGGVTTVVDMGS----TPPPTTTKAAIEAVAEAA----RASAGIRVVLGLGIPGVPAAVDEDA 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767983456 159 TVKLAEEFFLSTEGTVLGLDLSGDPTVGQAKD--FLEPLLEAKKAGLKLALHLSEIPNQKKETQILLDLL----PDRIGH 232
Cdd:cd01292 101 EALLLELLRRGLELGAVGLKLAGPYTATGLSDesLRRVLEEARKLGLPVVIHAGELPDPTRALEDLVALLrlggRVVIGH 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767983456 233 GTFLnsgeggSLDLVDFVRQHRIPLELCLTSNVKSqTVPSYDQHHFGFWYSIAHPSVICTDDKGVF-ATHLSQEYQLAAE 311
Cdd:cd01292 181 VSHL------DPELLELLKEAGVSLEVCPLSNYLL-GRDGEGAEALRRLLELGIRVTLGTDGPPHPlGTDLLALLRLLLK 253
|
|
| Amidohydro_1 |
pfam01979 |
Amidohydrolase family; This family of enzymes are a a large metal dependent hydrolase ... |
112-258 |
4.29e-04 |
|
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: 41.72 E-value: 4.29e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767983456 112 NATGMTKKTYVESILEGIkqskqENLDIDVRYLIAV-------DRRGGPLVAKETVKLAE-EFFLSTEGTVLGLDLSGDP 183
Cdd:pfam01979 48 LDMGATTSTGIEALLEAA-----EELPLGLRFLGPGcsldtdgELEGRKALREKLKAGAEfIKGMADGVVFVGLAPHGAP 122
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 767983456 184 TVGqaKDFLEPLLE-AKKAGLKLALHLSEipnQKKETQILLDLLPDRIGHGTFL-NSGEGGSLDLVDFVRQHRIPLE 258
Cdd:pfam01979 123 TFS--DDELKAALEeAKKYGLPVAIHALE---TKGEVEDAIAAFGGGIEHGTHLeVAESGGLLDIIKLILAHGVHLS 194
|
|
| |
