|
Name |
Accession |
Description |
Interval |
E-value |
| ADA_AMPD |
cd00443 |
Adenosine/AMP deaminase. Adenosine deaminases (ADAs) are present in pro- and eukaryotic ... |
17-344 |
4.00e-107 |
|
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: 316.21 E-value: 4.00e-107
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568918764 17 LPKVELHAHLNGSISSSTMKKLIAKkphlnvhghmtmidkgkkrtlqECFQMFQVIHQLTTSAEDILMVTKDVIKEFADD 96
Cdd:cd00443 1 LPKVELHAHLSGSISPETLLELIKK----------------------EFFEKFLLVHNLLQKGEALARALKEVIEEFAED 58
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568918764 97 GVKYLELRSTPRE-ENATGMTRKTYVESVLEGIKQCKQENLDIDVRYLMAIDRRGGP----TIARETVELAKEFFlsteN 171
Cdd:cd00443 59 NVQYLELRTTPRLlETEKGLTKEQYWLLVIEGISEAKQWFPPIKVRLILSVDRRGPYvqnyLVASEILELAKFLS----N 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568918764 172 TVLGLDLSGDPTIG--QANDFLEPLLEAKKAG-LKLALHLAEIPNREKENQMLLsLLPDRIGHGTFLSASEagalDQVDF 248
Cdd:cd00443 135 YVVGIDLVGDESKGenPLRDFYSYYEYARRLGlLGLTLHCGETGNREELLQALL-LLPDRIGHGIFLLKHP----ELIYL 209
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568918764 249 VRQHQIPLELCLTSNIKSQTVPSYDQHHFGFWYSIAHPSVICTDDKGVFATYLSQEYQLAAETFNLTPFQVWDLSYESIN 328
Cdd:cd00443 210 VKLRNIPIEVCPTSNVVLGTVQSYEKHPFMRFFKAGLPVSLSTDDPGIFGTSLSEEYSLAAKTFGLTFEDLCELNRNSVL 289
|
330
....*....|....*.
gi 568918764 329 YIFACDNTRSELRKRW 344
Cdd:cd00443 290 SSFAKDEEKKSLLEVL 305
|
|
| Add |
COG1816 |
Adenosine deaminase [Nucleotide transport and metabolism]; Adenosine deaminase is part of the ... |
18-344 |
3.53e-58 |
|
Adenosine deaminase [Nucleotide transport and metabolism]; Adenosine deaminase is part of the Pathway/BioSystem: Menaquinone biosynthesis
Pssm-ID: 441421 Cd Length: 326 Bit Score: 191.45 E-value: 3.53e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568918764 18 PKVELHAHLNGSISSSTMKKLiAKKphlnvHGH---MTMIDKGKK----RTLQECFQMFQVIHQLTTSAEDILMVTKDVI 90
Cdd:COG1816 1 PKAELHLHLEGSLRPETLLEL-AAR-----NGIdlpAADVEELRAaydfRDLQSFLDTYDAGAAVLQTEEDFRRLAYEYL 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568918764 91 KEFADDGVKYLELRSTPreENAT--GMTRKTYVESVLEGIKQCKQEnLDIDVRYLMAIDRRGGPTIARETVELAKEFfls 168
Cdd:COG1816 75 EDAAADGVRYAEIRFDP--QLHTrrGLSLEEVVEAVLDGLREAERE-FGISVRLILCALRHLSPEAAFETLELALRY--- 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568918764 169 TENTVLGLDLSGDPTIGQANDFLEPLLEAKKAGLKLALHLAEIPNREKENQMLLSLLPDRIGHGTflSASEAGALdqVDF 248
Cdd:COG1816 149 RDRGVVGFGLAGDERGFPPEKFAEAFARAREAGLHLTAHAGEAGGPESIWEALDLLGAERIGHGV--RAIEDPAL--VAR 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568918764 249 VRQHQIPLELCLTSNIKSQTVPSYDQHHF------GFwysiahPSVICTDDKGVFATYLSQEYQLAAETFNLTPFQVWDL 322
Cdd:COG1816 225 LADRGIPLEVCPTSNVQLGVVPSLAEHPLrrlldaGV------RVTLNTDDPLYFGTTLTDEYELAAEAFGLSDADLAQL 298
|
330 340
....*....|....*....|..
gi 568918764 323 SYESINYIFACDNTRSELRKRW 344
Cdd:COG1816 299 ARNAIEASFLPEEEKAALLAEL 320
|
|
| PRK09358 |
PRK09358 |
adenosine deaminase; Provisional |
12-343 |
4.60e-53 |
|
adenosine deaminase; Provisional
Pssm-ID: 236480 Cd Length: 340 Bit Score: 178.45 E-value: 4.60e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568918764 12 DFYLQLPKVELHAHLNGSISSSTMKKLIAKK----PHLNVHGHMTMIDKGKKRTLQECFQMF-QVIHQLTTsAEDILMVT 86
Cdd:PRK09358 5 MIIRSLPKAELHLHLDGSLRPETILELARRNgialPATDVEELPWVRAAYDFRDLQSFLDKYdAGVAVLQT-EEDLRRLA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568918764 87 KDVIKEFADDGVKYLELRSTPREENATGMTRKTYVESVLEGIKQCKQEnLDIDVRYLMAIDRRGGPT-IARETVELAKEF 165
Cdd:PRK09358 84 FEYLEDAAADGVVYAEIRFDPQLHTERGLPLEEVVEAVLDGLRAAEAE-FGISVRLILCFMRHFGEEaAARELEALAARY 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568918764 166 FlstENTVLGLDLSGDPTIGQANDFLEPLLEAKKAGLKLALH------LAEIpnREkenqmLLSLL-PDRIGHGTflSAS 238
Cdd:PRK09358 163 R---DDGVVGFDLAGDELGFPPSKFARAFDRARDAGLRLTAHageaggPESI--WE-----ALDELgAERIGHGV--RAI 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568918764 239 EAGALdqVDFVRQHQIPLELCLTSNIKSQTVPSYDQHHF------GFWYSIAhpsvicTDDKGVFATYLSQEYQLAAETF 312
Cdd:PRK09358 231 EDPAL--MARLADRRIPLEVCPTSNVQTGAVPSLAEHPLktlldaGVRVTIN------TDDPLVFGTTLTEEYEALAEAF 302
|
330 340 350
....*....|....*....|....*....|.
gi 568918764 313 NLTPFQVWDLSYESINYIFACDNTRSELRKR 343
Cdd:PRK09358 303 GLSDEDLAQLARNALEAAFLSEEEKAALLAE 333
|
|
| A_deaminase |
pfam00962 |
Adenosine deaminase; |
18-343 |
1.52e-45 |
|
Adenosine deaminase;
Pssm-ID: 425964 Cd Length: 330 Bit Score: 158.75 E-value: 1.52e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568918764 18 PKVELHAHLNGSISSSTMKKLIAKK----PHLNVHG---HMTMIDKgkKRTLQECFQMFQVIHQLTTSAEDILMVTKDVI 90
Cdd:pfam00962 1 PKAELHLHLDGSLRPDTLLELAKRYgiilPADFPEAlepLFRKYKK--ERDLQDFLDKYDIGVAVLRSPEDIRRLAFEYA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568918764 91 KEFADDGVKYLELRSTPREENATGMTRKTYVESVLEGIKQCKQEnLDIDVRYLMAIDRRGGPTIARETVELAKEFflsTE 170
Cdd:pfam00962 79 EDVAKDGVVYAEVRYDPQSHASRGLSPDTVVDAVLDAVDAAERE-FGITVRLIVCAMRHEHPECSREIAELAPRY---RD 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568918764 171 NTVLGLDLSGDPTI---GQANDFLEPLLEAKKAGLKLALHLAEIPNREKENQMLLSLLPDRIGHGTflSASEAGALdqVD 247
Cdd:pfam00962 155 QGIVAFGLAGDEKGfppSLFRDHVEAFARARDAGLHLTVHAGEAGGPQSVWEALDDLGAERIGHGV--RSAEDPRL--LD 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568918764 248 FVRQHQIPLELCLTSNIKSQTVPSYDQHHFGFWYSIAHPSVICTDDKGVFATYLSQEYQLAAETFNLTPFQVWDLSYESI 327
Cdd:pfam00962 231 RLADRQIPLEICPTSNVQTGAVASLAEHPLKTFLRAGVPVSLNTDDPLMFGSDLLDEYQVAKRAPGFDEEELARLAKNAV 310
|
330
....*....|....*.
gi 568918764 328 NYIFACDNTRSELRKR 343
Cdd:pfam00962 311 KGSFLPADEKRALLDE 326
|
|
| aden_deam |
TIGR01430 |
adenosine deaminase; This family includes the experimentally verified adenosine deaminases of ... |
17-340 |
1.70e-45 |
|
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: 158.29 E-value: 1.70e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568918764 17 LPKVELHAHLNGSISSSTMKKLiAKK-----PHLNVHGHMTMIDKGKKRTLQECFQMFQVIHQLTTSAEDILMVTKDVIK 91
Cdd:TIGR01430 1 LPKAELHLHLEGSIRPETLLEL-AQKngiplPADLQSGEELKEAYDKFRDLQDFLAKYDFGVEVLRTEDDFKRLAYEYVE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568918764 92 EFADDGVKYLELRSTPREENATGMTRKTYVESVLEGIKQCKQEnLDIDVRYLMAIDRRGGPTIARETVELAKEFflsTEN 171
Cdd:TIGR01430 80 KAAKDGVVYAEVFFDPQLHTNRGISPDTVVEAVLDGLDEAERD-FGIKSRLILCGMRHKQPEAAEETLELAKPY---KEQ 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568918764 172 TVLGLDLSGDPTIGQANDFLEPLLEAKKAGLKLALHLAEIPNREKENQMLLSLLPDRIGHGtfLSASEAGALdqVDFVRQ 251
Cdd:TIGR01430 156 TIVGFGLAGDERGGPPPDFVRAFAIARELGLHLTVHAGELGGPESVREALDDLGATRIGHG--VRALEDPEL--LKRLAQ 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568918764 252 HQIPLELCLTSNIKSQTVPSYDQHHFGFWYSIAHPSVICTDDKGVFATYLSQEYQLAAETFNLTPFQVWDLSYESINYIF 331
Cdd:TIGR01430 232 ENITLEVCPTSNVALGVVKSLAEHPLRRFLEAGVKVTLNSDDPAYFGSYLTEEYEIAAKHAGLTEEELKQLARNALEGSF 311
|
....*....
gi 568918764 332 ACDNTRSEL 340
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 ... |
17-344 |
4.00e-107 |
|
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: 316.21 E-value: 4.00e-107
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568918764 17 LPKVELHAHLNGSISSSTMKKLIAKkphlnvhghmtmidkgkkrtlqECFQMFQVIHQLTTSAEDILMVTKDVIKEFADD 96
Cdd:cd00443 1 LPKVELHAHLSGSISPETLLELIKK----------------------EFFEKFLLVHNLLQKGEALARALKEVIEEFAED 58
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568918764 97 GVKYLELRSTPRE-ENATGMTRKTYVESVLEGIKQCKQENLDIDVRYLMAIDRRGGP----TIARETVELAKEFFlsteN 171
Cdd:cd00443 59 NVQYLELRTTPRLlETEKGLTKEQYWLLVIEGISEAKQWFPPIKVRLILSVDRRGPYvqnyLVASEILELAKFLS----N 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568918764 172 TVLGLDLSGDPTIG--QANDFLEPLLEAKKAG-LKLALHLAEIPNREKENQMLLsLLPDRIGHGTFLSASEagalDQVDF 248
Cdd:cd00443 135 YVVGIDLVGDESKGenPLRDFYSYYEYARRLGlLGLTLHCGETGNREELLQALL-LLPDRIGHGIFLLKHP----ELIYL 209
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568918764 249 VRQHQIPLELCLTSNIKSQTVPSYDQHHFGFWYSIAHPSVICTDDKGVFATYLSQEYQLAAETFNLTPFQVWDLSYESIN 328
Cdd:cd00443 210 VKLRNIPIEVCPTSNVVLGTVQSYEKHPFMRFFKAGLPVSLSTDDPGIFGTSLSEEYSLAAKTFGLTFEDLCELNRNSVL 289
|
330
....*....|....*.
gi 568918764 329 YIFACDNTRSELRKRW 344
Cdd:cd00443 290 SSFAKDEEKKSLLEVL 305
|
|
| ADA |
cd01320 |
Adenosine deaminase (ADA) is a monomeric zinc dependent enzyme which catalyzes the ... |
16-343 |
6.36e-60 |
|
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: 195.89 E-value: 6.36e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568918764 16 QLPKVELHAHLNGSISSSTMKKLIAKK----PHLNVHGHMTMIDKGKKRTLQECFQMFQVIHQLTTSAEDILMVTKDVIK 91
Cdd:cd01320 1 NLPKAELHLHLDGSLRPETILELAKKNgitlPASDVELLELVVAAYNFSDLQDFLAKYDFGLSVLQTEEDFERLAYEYLE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568918764 92 EFADDGVKYLELRSTPREENATGMTRKTYVESVLEGIKQCKqENLDIDVRYLMAIDRRGGPTIARETVELAKEFflsTEN 171
Cdd:cd01320 81 DAAADGVVYAEIRFSPQLHTRRGLSFDEVVEAVLRGLDEAE-AEFGIKARLILCGLRHLSPESAQETLELALKY---RDK 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568918764 172 TVLGLDLSGDPTIGQANDFLEPLLEAKKAGLKLALHLAEIPNREKENQMLLSLLPDRIGHGTFLSASEAgaldQVDFVRQ 251
Cdd:cd01320 157 GVVGFDLAGDEVGFPPEKFVRAFQRAREAGLRLTAHAGEAGGPESVRDALDLLGAERIGHGIRAIEDPE----LVKRLAE 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568918764 252 HQIPLELCLTSNIKSQTVPSYDQHHFGFWYSIAHPSVICTDDKGVFATYLSQEYQLAAETFNLTPFQVWDLSYESINYIF 331
Cdd:cd01320 233 RNIPLEVCPTSNVQTGAVKSLAEHPLRELLDAGVKVTINTDDPTVFGTYLTDEYELLAEAFGLTEEELKKLARNAVEASF 312
|
330
....*....|..
gi 568918764 332 ACDNTRSELRKR 343
Cdd:cd01320 313 LSEEEKAELLKR 324
|
|
| Add |
COG1816 |
Adenosine deaminase [Nucleotide transport and metabolism]; Adenosine deaminase is part of the ... |
18-344 |
3.53e-58 |
|
Adenosine deaminase [Nucleotide transport and metabolism]; Adenosine deaminase is part of the Pathway/BioSystem: Menaquinone biosynthesis
Pssm-ID: 441421 Cd Length: 326 Bit Score: 191.45 E-value: 3.53e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568918764 18 PKVELHAHLNGSISSSTMKKLiAKKphlnvHGH---MTMIDKGKK----RTLQECFQMFQVIHQLTTSAEDILMVTKDVI 90
Cdd:COG1816 1 PKAELHLHLEGSLRPETLLEL-AAR-----NGIdlpAADVEELRAaydfRDLQSFLDTYDAGAAVLQTEEDFRRLAYEYL 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568918764 91 KEFADDGVKYLELRSTPreENAT--GMTRKTYVESVLEGIKQCKQEnLDIDVRYLMAIDRRGGPTIARETVELAKEFfls 168
Cdd:COG1816 75 EDAAADGVRYAEIRFDP--QLHTrrGLSLEEVVEAVLDGLREAERE-FGISVRLILCALRHLSPEAAFETLELALRY--- 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568918764 169 TENTVLGLDLSGDPTIGQANDFLEPLLEAKKAGLKLALHLAEIPNREKENQMLLSLLPDRIGHGTflSASEAGALdqVDF 248
Cdd:COG1816 149 RDRGVVGFGLAGDERGFPPEKFAEAFARAREAGLHLTAHAGEAGGPESIWEALDLLGAERIGHGV--RAIEDPAL--VAR 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568918764 249 VRQHQIPLELCLTSNIKSQTVPSYDQHHF------GFwysiahPSVICTDDKGVFATYLSQEYQLAAETFNLTPFQVWDL 322
Cdd:COG1816 225 LADRGIPLEVCPTSNVQLGVVPSLAEHPLrrlldaGV------RVTLNTDDPLYFGTTLTDEYELAAEAFGLSDADLAQL 298
|
330 340
....*....|....*....|..
gi 568918764 323 SYESINYIFACDNTRSELRKRW 344
Cdd:COG1816 299 ARNAIEASFLPEEEKAALLAEL 320
|
|
| PRK09358 |
PRK09358 |
adenosine deaminase; Provisional |
12-343 |
4.60e-53 |
|
adenosine deaminase; Provisional
Pssm-ID: 236480 Cd Length: 340 Bit Score: 178.45 E-value: 4.60e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568918764 12 DFYLQLPKVELHAHLNGSISSSTMKKLIAKK----PHLNVHGHMTMIDKGKKRTLQECFQMF-QVIHQLTTsAEDILMVT 86
Cdd:PRK09358 5 MIIRSLPKAELHLHLDGSLRPETILELARRNgialPATDVEELPWVRAAYDFRDLQSFLDKYdAGVAVLQT-EEDLRRLA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568918764 87 KDVIKEFADDGVKYLELRSTPREENATGMTRKTYVESVLEGIKQCKQEnLDIDVRYLMAIDRRGGPT-IARETVELAKEF 165
Cdd:PRK09358 84 FEYLEDAAADGVVYAEIRFDPQLHTERGLPLEEVVEAVLDGLRAAEAE-FGISVRLILCFMRHFGEEaAARELEALAARY 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568918764 166 FlstENTVLGLDLSGDPTIGQANDFLEPLLEAKKAGLKLALH------LAEIpnREkenqmLLSLL-PDRIGHGTflSAS 238
Cdd:PRK09358 163 R---DDGVVGFDLAGDELGFPPSKFARAFDRARDAGLRLTAHageaggPESI--WE-----ALDELgAERIGHGV--RAI 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568918764 239 EAGALdqVDFVRQHQIPLELCLTSNIKSQTVPSYDQHHF------GFWYSIAhpsvicTDDKGVFATYLSQEYQLAAETF 312
Cdd:PRK09358 231 EDPAL--MARLADRRIPLEVCPTSNVQTGAVPSLAEHPLktlldaGVRVTIN------TDDPLVFGTTLTEEYEALAEAF 302
|
330 340 350
....*....|....*....|....*....|.
gi 568918764 313 NLTPFQVWDLSYESINYIFACDNTRSELRKR 343
Cdd:PRK09358 303 GLSDEDLAQLARNALEAAFLSEEEKAALLAE 333
|
|
| A_deaminase |
pfam00962 |
Adenosine deaminase; |
18-343 |
1.52e-45 |
|
Adenosine deaminase;
Pssm-ID: 425964 Cd Length: 330 Bit Score: 158.75 E-value: 1.52e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568918764 18 PKVELHAHLNGSISSSTMKKLIAKK----PHLNVHG---HMTMIDKgkKRTLQECFQMFQVIHQLTTSAEDILMVTKDVI 90
Cdd:pfam00962 1 PKAELHLHLDGSLRPDTLLELAKRYgiilPADFPEAlepLFRKYKK--ERDLQDFLDKYDIGVAVLRSPEDIRRLAFEYA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568918764 91 KEFADDGVKYLELRSTPREENATGMTRKTYVESVLEGIKQCKQEnLDIDVRYLMAIDRRGGPTIARETVELAKEFflsTE 170
Cdd:pfam00962 79 EDVAKDGVVYAEVRYDPQSHASRGLSPDTVVDAVLDAVDAAERE-FGITVRLIVCAMRHEHPECSREIAELAPRY---RD 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568918764 171 NTVLGLDLSGDPTI---GQANDFLEPLLEAKKAGLKLALHLAEIPNREKENQMLLSLLPDRIGHGTflSASEAGALdqVD 247
Cdd:pfam00962 155 QGIVAFGLAGDEKGfppSLFRDHVEAFARARDAGLHLTVHAGEAGGPQSVWEALDDLGAERIGHGV--RSAEDPRL--LD 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568918764 248 FVRQHQIPLELCLTSNIKSQTVPSYDQHHFGFWYSIAHPSVICTDDKGVFATYLSQEYQLAAETFNLTPFQVWDLSYESI 327
Cdd:pfam00962 231 RLADRQIPLEICPTSNVQTGAVASLAEHPLKTFLRAGVPVSLNTDDPLMFGSDLLDEYQVAKRAPGFDEEELARLAKNAV 310
|
330
....*....|....*.
gi 568918764 328 NYIFACDNTRSELRKR 343
Cdd:pfam00962 311 KGSFLPADEKRALLDE 326
|
|
| aden_deam |
TIGR01430 |
adenosine deaminase; This family includes the experimentally verified adenosine deaminases of ... |
17-340 |
1.70e-45 |
|
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: 158.29 E-value: 1.70e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568918764 17 LPKVELHAHLNGSISSSTMKKLiAKK-----PHLNVHGHMTMIDKGKKRTLQECFQMFQVIHQLTTSAEDILMVTKDVIK 91
Cdd:TIGR01430 1 LPKAELHLHLEGSIRPETLLEL-AQKngiplPADLQSGEELKEAYDKFRDLQDFLAKYDFGVEVLRTEDDFKRLAYEYVE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568918764 92 EFADDGVKYLELRSTPREENATGMTRKTYVESVLEGIKQCKQEnLDIDVRYLMAIDRRGGPTIARETVELAKEFflsTEN 171
Cdd:TIGR01430 80 KAAKDGVVYAEVFFDPQLHTNRGISPDTVVEAVLDGLDEAERD-FGIKSRLILCGMRHKQPEAAEETLELAKPY---KEQ 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568918764 172 TVLGLDLSGDPTIGQANDFLEPLLEAKKAGLKLALHLAEIPNREKENQMLLSLLPDRIGHGtfLSASEAGALdqVDFVRQ 251
Cdd:TIGR01430 156 TIVGFGLAGDERGGPPPDFVRAFAIARELGLHLTVHAGELGGPESVREALDDLGATRIGHG--VRALEDPEL--LKRLAQ 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568918764 252 HQIPLELCLTSNIKSQTVPSYDQHHFGFWYSIAHPSVICTDDKGVFATYLSQEYQLAAETFNLTPFQVWDLSYESINYIF 331
Cdd:TIGR01430 232 ENITLEVCPTSNVALGVVKSLAEHPLRRFLEAGVKVTLNSDDPAYFGSYLTEEYEIAAKHAGLTEEELKQLARNALEGSF 311
|
....*....
gi 568918764 332 ACDNTRSEL 340
Cdd:TIGR01430 312 LSDDEKKEL 320
|
|
| ADGF |
cd01321 |
Adenosine deaminase-related growth factors (ADGF), a novel family of secreted growth-factors ... |
30-344 |
2.57e-16 |
|
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: 78.85 E-value: 2.57e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568918764 30 ISSSTMKKLIAKKP---HLnvHGHMT-------MIDKGKKRtlqecF-QMFQVIHQLTTsaedILMVTKDVI----KEFA 94
Cdd:cd01321 12 IENSTLFKIIQKMPkgaLL--HVHDTamvssdwLIKNATYR-----FeQIFDIIDGLLT----YLPIFRDYYrrllEELY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568918764 95 DDGVKYLELRSTPREENATGMTRKTYvesvLEGIKQCKQENLD--------IDVRYLMAIDRRGGPTIARETVELAKEFF 166
Cdd:cd01321 81 EDNVQYVELRSSFSPLYDLDGREYDY----EETVQLLEEVVEKfkkthpdfIGLKIIYATLRNFNDSEIKESMEQCLNLK 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568918764 167 LSTENTVLGLDLSGDPTIGQA-NDFLEPLLEAKK--AGLKLALHLAEIP---NREKENqMLLSLLPD--RIGHGTflsas 238
Cdd:cd01321 157 KKFPDFIAGFDLVGQEDAGRPlLDFLPQLLWFPKqcAEIPFFFHAGETNgdgTETDEN-LVDALLLNtkRIGHGF----- 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568918764 239 eagALDQ----VDFVRQHQIPLELCLTSNIKSQTVPSYDQHHFGFWYSIAHPSVICTDDKGVF-ATYLSQE-YQ----LA 308
Cdd:cd01321 231 ---ALPKhpllMDLVKKKNIAIEVCPISNQVLGLVSDLRNHPAAALLARGVPVVISSDDPGFWgAKGLSHDfYQafmgLA 307
|
330 340 350 360
....*....|....*....|....*....|....*....|..
gi 568918764 309 AETFNLTpfQVWDLSYESINYifAC------DNTRSELRKRW 344
Cdd:cd01321 308 PADAGLR--GLKQLAENSIRY--SAlsdqekDEAVAKWEKKW 345
|
|
| PTZ00124 |
PTZ00124 |
adenosine deaminase; Provisional |
16-315 |
3.92e-13 |
|
adenosine deaminase; Provisional
Pssm-ID: 173415 Cd Length: 362 Bit Score: 69.51 E-value: 3.92e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568918764 16 QLPKVELHAHLNGSISSSTMKKLIAK---KPHLNVHGHMTMIDKGKK-RTLQECFQMFQVIHQLTTSAEDILMVTKDVIK 91
Cdd:PTZ00124 34 RIPKCELHCHLDLCFSVDFFLSCIRKynlQPNLSDEEILDYYLFAKGgKSLGEFVEKAIRVADIFNDYEVIEDLAKHAVF 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568918764 92 EFADDGVKYLELRSTPR-EENATGMTRKTYVESVLEGIKQCKQEnldIDVRYLMAIDRRGGPTIARETVELAKEFFLSTE 170
Cdd:PTZ00124 114 NKYKEGVVLMEFRYSPTfVAFKHNLDIDLIHQAIVKGIKEAVEL---LDHKIEVGLLCIGDTGHDAAPIKESADFCLKHK 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568918764 171 NTVLGLDLSGDPTigQANDFLEPLLEAKKAGLKLALHLAE---IPNREKENQMLLSLLPDRIGHGTFLSASEagalDQVD 247
Cdd:PTZ00124 191 ADFVGFDHAGHEV--DLKPFKDIFDYVREAGVNLTVHAGEdvtLPNLNTLYSAIQVLKVKRIGHGIRVAESQ----ELID 264
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 568918764 248 FVRQHQIPLELCLTSNIKSQTVPSYDQHHFGFWYSIAHPSVICTDDKGVFATYLSQEYQLAAETFNLT 315
Cdd:PTZ00124 265 MVKEKDILLEVCPISNVLLNNAKSMDTHPIRKLYDAGVKVSVNSDDPGMFLTNINDDYEELYTHLNFT 332
|
|
| metallo-dependent_hydrolases |
cd01292 |
Superfamily of metallo-dependent hydrolases (also called amidohydrolase superfamily) is a ... |
78-310 |
1.05e-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: 49.64 E-value: 1.05e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568918764 78 SAEDILMVTKDVIKEFADDGVKYLELRSTPReenatgmTRKTYVESVLEGIKQCkQENLDIDVRYLMAIDRRGGPTIARE 157
Cdd:cd01292 29 SPEDLYEDTLRALEALLAGGVTTVVDMGSTP-------PPTTTKAAIEAVAEAA-RASAGIRVVLGLGIPGVPAAVDEDA 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568918764 158 TVELAKEFFLSTENTVLGLDLSGDPTIGQAND--FLEPLLEAKKAGLKLALHLAEIPNREKENQMLLSLL----PDRIGH 231
Cdd:cd01292 101 EALLLELLRRGLELGAVGLKLAGPYTATGLSDesLRRVLEEARKLGLPVVIHAGELPDPTRALEDLVALLrlggRVVIGH 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568918764 232 GTFLSASEAGALdqvdfvRQHQIPLELCLTSNIKSqTVPSYDQHHFGFWYSIAHPSVICTDDKGVF-ATYLSQEYQLAAE 310
Cdd:cd01292 181 VSHLDPELLELL------KEAGVSLEVCPLSNYLL-GRDGEGAEALRRLLELGIRVTLGTDGPPHPlGTDLLALLRLLLK 253
|
|
| archeal_chlorohydrolases |
cd01305 |
Predicted chlorohydrolases. These metallo-dependent hydrolases from archea are part of the ... |
96-264 |
4.25e-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: 4.25e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568918764 96 DGVKYLELRSTPREENATGMtRKT--------------YVESVLEGIKQCKQENLDIDVRYLMAIDRRGGPTIARETVEL 161
Cdd:cd01305 35 DGLKHRLLAQADDRELAEAM-RKVlrdmretgigafadFREGGVEGIELLRRALGKLPVPFEVILGRPTEPDDPEILLEV 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568918764 162 AKefflstentvlGLDLSGdptigqANDFLEPLL--EAKKAGLKLALHLAEipNREK----ENQMLLSLLPDRIGHGTFL 235
Cdd:cd01305 114 AD-----------GLGLSS------ANDVDLEDIleLLRRRGKLFAIHASE--TRESvgmtDIERALDLEPDLLVHGTHL 174
|
170 180
....*....|....*....|....*....
gi 568918764 236 SASEagaldqVDFVRQHQIPLELCLTSNI 264
Cdd:cd01305 175 TDED------LELVRENGVPVVLCPRSNL 197
|
|
| Amidohydro_1 |
pfam01979 |
Amidohydrolase family; This family of enzymes are a a large metal dependent hydrolase ... |
111-257 |
8.31e-05 |
|
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: 44.03 E-value: 8.31e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568918764 111 NATGMTRKTYVESVLEGIKQCKQeNLDIDVRYLMAIDRRGGPTIARETVELAKEF----FLSTENTVLGLDLSGDPTIGQ 186
Cdd:pfam01979 48 LDMGATTSTGIEALLEAAEELPL-GLRFLGPGCSLDTDGELEGRKALREKLKAGAefikGMADGVVFVGLAPHGAPTFSD 126
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 568918764 187 anDFLEPLLE-AKKAGLKLALHLAEIpnrEKENQMLLSLLPDRIGHGTFLS-ASEAGALDQVDFVRQHQIPLE 257
Cdd:pfam01979 127 --DELKAALEeAKKYGLPVAIHALET---KGEVEDAIAAFGGGIEHGTHLEvAESGGLLDIIKLILAHGVHLS 194
|
|
| |
