|
Name |
Accession |
Description |
Interval |
E-value |
| adm_rel |
TIGR01431 |
adenosine deaminase-related growth factor; Members of this family have been described as ... |
11-268 |
2.94e-171 |
|
adenosine deaminase-related growth factor; Members of this family have been described as secreted proteins with growth factor activity and regions of adenosine deaminase homology in insects, mollusks, and vertebrates.
Pssm-ID: 273620 [Multi-domain] Cd Length: 479 Bit Score: 481.60 E-value: 2.94e-171
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29029552 11 VYELSGEHHDEEWSVKTYQEVAQKFVETHPEFIGIKIIYSDHRSKDVAVIAESIRMAMGLRIKFPTVVAGFDLVGHEDTG 90
Cdd:TIGR01431 223 LYELSGTHHDEEWSVKTYKEVTEKFVEEHPDFIGIKIIYSDLRSKDVEEIAEYIKMAMGLRIKYPDFVAGFDLVGQEDTG 302
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29029552 91 HSLHDYKEALMIPAkDGVKLPYFFHAGETDWQGTSIDRNILDALMLNTTRIGHGFALSKHPAVRTYSWKKDIPIEVCPIS 170
Cdd:TIGR01431 303 HSLLDYKDALLIPS-IGVKLPYFFHAGETNWQGTSVDRNLLDALLLNTTRIGHGFALSKHPAVRTYSKERDIPIEVCPIS 381
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29029552 171 NQVLKLVSDLRNHPVATLMATGHPMVISSDDPAMFGAKGLSYDFYEVFMGIGGMKADLRTLKQLAMNSIKYSTLLESEKN 250
Cdd:TIGR01431 382 NQVLKLVSDLRNHPVATLMADNYPMVISSDDPAFWGAKGLSYDFYEAFMGIAGMKADLRTLKQLALNSIKYSALSEEEKN 461
|
250
....*....|....*...
gi 29029552 251 TFMEIWKKRWDKFIADVA 268
Cdd:TIGR01431 462 TAMAKWKKQWDKFIDDVL 479
|
|
| ADGF |
cd01321 |
Adenosine deaminase-related growth factors (ADGF), a novel family of secreted growth-factors ... |
7-260 |
7.13e-153 |
|
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: 429.77 E-value: 7.13e-153
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29029552 7 NWALVYELSGEHHDEEWSVKTYQEVAQKFVETHPEFIGIKIIYSDHRSKDVAVIAESIRMAMGLRIKFPTVVAGFDLVGH 86
Cdd:cd01321 92 SFSPLYDLDGREYDYEETVQLLEEVVEKFKKTHPDFIGLKIIYATLRNFNDSEIKESMEQCLNLKKKFPDFIAGFDLVGQ 171
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29029552 87 EDTGHSLHDYKEALMIPAKDGVKLPYFFHAGETDWQGTSIDRNILDALMLNTTRIGHGFALSKHPAVRTYSWKKDIPIEV 166
Cdd:cd01321 172 EDAGRPLLDFLPQLLWFPKQCAEIPFFFHAGETNGDGTETDENLVDALLLNTKRIGHGFALPKHPLLMDLVKKKNIAIEV 251
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29029552 167 CPISNQVLKLVSDLRNHPVATLMATGHPMVISSDDPAMFGAKGLSYDFYEVFMGIGGMKADLRTLKQLAMNSIKYSTLLE 246
Cdd:cd01321 252 CPISNQVLGLVSDLRNHPAAALLARGVPVVISSDDPGFWGAKGLSHDFYQAFMGLAPADAGLRGLKQLAENSIRYSALSD 331
|
250
....*....|....
gi 29029552 247 SEKNTFMEIWKKRW 260
Cdd:cd01321 332 QEKDEAVAKWEKKW 345
|
|
| Add |
COG1816 |
Adenosine deaminase [Nucleotide transport and metabolism]; Adenosine deaminase is part of the ... |
43-265 |
2.37e-32 |
|
Adenosine deaminase [Nucleotide transport and metabolism]; Adenosine deaminase is part of the Pathway/BioSystem: Menaquinone biosynthesis
Pssm-ID: 441421 Cd Length: 326 Bit Score: 120.96 E-value: 2.37e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29029552 43 IGIKIIYSDHRSKDVAVIAESIRMAMGLRIKFptvVAGFDLVGHEDtGHSLHDYKEALMIPAKDGVKLpyFFHAGETD-W 121
Cdd:COG1816 121 ISVRLILCALRHLSPEAAFETLELALRYRDRG---VVGFGLAGDER-GFPPEKFAEAFARAREAGLHL--TAHAGEAGgP 194
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29029552 122 QgtsidrNILDAL-MLNTTRIGHGFALSKHPAVRTYSWKKDIPIEVCPISNQVLKLVSDLRNHPVATLMATGHPMVISSD 200
Cdd:COG1816 195 E------SIWEALdLLGAERIGHGVRAIEDPALVARLADRGIPLEVCPTSNVQLGVVPSLAEHPLRRLLDAGVRVTLNTD 268
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 29029552 201 DPAMFGAkGLSYDfYEVFMGIGGMkaDLRTLKQLAMNSIKYSTLLESEKntfmEIWKKRWDKFIA 265
Cdd:COG1816 269 DPLYFGT-TLTDE-YELAAEAFGL--SDADLAQLARNAIEASFLPEEEK----AALLAELDAYFA 325
|
|
| PRK09358 |
PRK09358 |
adenosine deaminase; Provisional |
43-249 |
1.54e-26 |
|
adenosine deaminase; Provisional
Pssm-ID: 236480 Cd Length: 340 Bit Score: 105.64 E-value: 1.54e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29029552 43 IGIKIIYSDHRSKDVAVIAESIrmAMGLRIKFPTVVAGFDLVGHEDtGHSLHDYKEALMIpAKD-GvkLPYFFHAGETDw 121
Cdd:PRK09358 134 ISVRLILCFMRHFGEEAAAREL--EALAARYRDDGVVGFDLAGDEL-GFPPSKFARAFDR-ARDaG--LRLTAHAGEAG- 206
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29029552 122 qGTSidrNILDAL-MLNTTRIGHGFALSKHPAVRTYSWKKDIPIEVCPISNQVLKLVSDLRNHPVATLMATGHPMVISSD 200
Cdd:PRK09358 207 -GPE---SIWEALdELGAERIGHGVRAIEDPALMARLADRRIPLEVCPTSNVQTGAVPSLAEHPLKTLLDAGVRVTINTD 282
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 29029552 201 DPAMFGaKGLSyDFYEVFMGIGGMkaDLRTLKQLAMNSIKYSTLLESEK 249
Cdd:PRK09358 283 DPLVFG-TTLT-EEYEALAEAFGL--SDEDLAQLARNALEAAFLSEEEK 327
|
|
| A_deaminase |
pfam00962 |
Adenosine deaminase; |
43-250 |
4.58e-19 |
|
Adenosine deaminase;
Pssm-ID: 425964 Cd Length: 330 Bit Score: 85.17 E-value: 4.58e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29029552 43 IGIKIIYSDHRSKDVAVIAESIRMAMGLRikfPTVVAGFDLVGHEdTGHSLH---DYKEALMIPAKDGVKLPyfFHAGET 119
Cdd:pfam00962 125 ITVRLIVCAMRHEHPECSREIAELAPRYR---DQGIVAFGLAGDE-KGFPPSlfrDHVEAFARARDAGLHLT--VHAGEA 198
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29029552 120 DWQGTsidrnILDAL-MLNTTRIGHGFALSKHPAVRTYSWKKDIPIEVCPISNQVLKLVSDLRNHPVATLMATGHPMVIS 198
Cdd:pfam00962 199 GGPQS-----VWEALdDLGAERIGHGVRSAEDPRLLDRLADRQIPLEICPTSNVQTGAVASLAEHPLKTFLRAGVPVSLN 273
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 29029552 199 SDDPAMFGAK-GLSYDFYEVFMGIggmkaDLRTLKQLAMNSIKYSTLLESEKN 250
Cdd:pfam00962 274 TDDPLMFGSDlLDEYQVAKRAPGF-----DEEELARLAKNAVKGSFLPADEKR 321
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| adm_rel |
TIGR01431 |
adenosine deaminase-related growth factor; Members of this family have been described as ... |
11-268 |
2.94e-171 |
|
adenosine deaminase-related growth factor; Members of this family have been described as secreted proteins with growth factor activity and regions of adenosine deaminase homology in insects, mollusks, and vertebrates.
Pssm-ID: 273620 [Multi-domain] Cd Length: 479 Bit Score: 481.60 E-value: 2.94e-171
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29029552 11 VYELSGEHHDEEWSVKTYQEVAQKFVETHPEFIGIKIIYSDHRSKDVAVIAESIRMAMGLRIKFPTVVAGFDLVGHEDTG 90
Cdd:TIGR01431 223 LYELSGTHHDEEWSVKTYKEVTEKFVEEHPDFIGIKIIYSDLRSKDVEEIAEYIKMAMGLRIKYPDFVAGFDLVGQEDTG 302
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29029552 91 HSLHDYKEALMIPAkDGVKLPYFFHAGETDWQGTSIDRNILDALMLNTTRIGHGFALSKHPAVRTYSWKKDIPIEVCPIS 170
Cdd:TIGR01431 303 HSLLDYKDALLIPS-IGVKLPYFFHAGETNWQGTSVDRNLLDALLLNTTRIGHGFALSKHPAVRTYSKERDIPIEVCPIS 381
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29029552 171 NQVLKLVSDLRNHPVATLMATGHPMVISSDDPAMFGAKGLSYDFYEVFMGIGGMKADLRTLKQLAMNSIKYSTLLESEKN 250
Cdd:TIGR01431 382 NQVLKLVSDLRNHPVATLMADNYPMVISSDDPAFWGAKGLSYDFYEAFMGIAGMKADLRTLKQLALNSIKYSALSEEEKN 461
|
250
....*....|....*...
gi 29029552 251 TFMEIWKKRWDKFIADVA 268
Cdd:TIGR01431 462 TAMAKWKKQWDKFIDDVL 479
|
|
| ADGF |
cd01321 |
Adenosine deaminase-related growth factors (ADGF), a novel family of secreted growth-factors ... |
7-260 |
7.13e-153 |
|
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: 429.77 E-value: 7.13e-153
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29029552 7 NWALVYELSGEHHDEEWSVKTYQEVAQKFVETHPEFIGIKIIYSDHRSKDVAVIAESIRMAMGLRIKFPTVVAGFDLVGH 86
Cdd:cd01321 92 SFSPLYDLDGREYDYEETVQLLEEVVEKFKKTHPDFIGLKIIYATLRNFNDSEIKESMEQCLNLKKKFPDFIAGFDLVGQ 171
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29029552 87 EDTGHSLHDYKEALMIPAKDGVKLPYFFHAGETDWQGTSIDRNILDALMLNTTRIGHGFALSKHPAVRTYSWKKDIPIEV 166
Cdd:cd01321 172 EDAGRPLLDFLPQLLWFPKQCAEIPFFFHAGETNGDGTETDENLVDALLLNTKRIGHGFALPKHPLLMDLVKKKNIAIEV 251
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29029552 167 CPISNQVLKLVSDLRNHPVATLMATGHPMVISSDDPAMFGAKGLSYDFYEVFMGIGGMKADLRTLKQLAMNSIKYSTLLE 246
Cdd:cd01321 252 CPISNQVLGLVSDLRNHPAAALLARGVPVVISSDDPGFWGAKGLSHDFYQAFMGLAPADAGLRGLKQLAENSIRYSALSD 331
|
250
....*....|....
gi 29029552 247 SEKNTFMEIWKKRW 260
Cdd:cd01321 332 QEKDEAVAKWEKKW 345
|
|
| ADA_AMPD |
cd00443 |
Adenosine/AMP deaminase. Adenosine deaminases (ADAs) are present in pro- and eukaryotic ... |
12-256 |
1.01e-38 |
|
Adenosine/AMP deaminase. Adenosine deaminases (ADAs) are present in pro- and eukaryotic organisms and catalyze the zinc dependent irreversible deamination of adenosine nucleosides to inosine nucleosides and ammonia. The eukaryotic AMP deaminase catalyzes a similar reaction leading to the hydrolytic removal of an amino group at the 6 position of the adenine nucleotide ring, a branch point in the adenylate catabolic pathway.
Pssm-ID: 238250 Cd Length: 305 Bit Score: 137.09 E-value: 1.01e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29029552 12 YELSGEHHDEEWSVKTYQ----EVAQKFVETHPeFIGIKIIYSDHRSKDV---AVIAESIrmaMGLRIKFPTVVAGFDLV 84
Cdd:cd00443 67 TTPRLLETEKGLTKEQYWllviEGISEAKQWFP-PIKVRLILSVDRRGPYvqnYLVASEI---LELAKFLSNYVVGIDLV 142
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29029552 85 GHEDTGHS-LHDYKEALMIpAKDGVKLPYFFHAGETDWQGTsidrnILDALMLNTTRIGHGFALSKHPAVRTYSWKKDIP 163
Cdd:cd00443 143 GDESKGENpLRDFYSYYEY-ARRLGLLGLTLHCGETGNREE-----LLQALLLLPDRIGHGIFLLKHPELIYLVKLRNIP 216
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29029552 164 IEVCPISNQVLKLVSDLRNHPVATLMATGHPMVISSDDPAMFGAkGLSYDFYEVFMgigGMKADLRTLKQLAMNSIKYST 243
Cdd:cd00443 217 IEVCPTSNVVLGTVQSYEKHPFMRFFKAGLPVSLSTDDPGIFGT-SLSEEYSLAAK---TFGLTFEDLCELNRNSVLSSF 292
|
250
....*....|...
gi 29029552 244 LLESEKNTFMEIW 256
Cdd:cd00443 293 AKDEEKKSLLEVL 305
|
|
| Add |
COG1816 |
Adenosine deaminase [Nucleotide transport and metabolism]; Adenosine deaminase is part of the ... |
43-265 |
2.37e-32 |
|
Adenosine deaminase [Nucleotide transport and metabolism]; Adenosine deaminase is part of the Pathway/BioSystem: Menaquinone biosynthesis
Pssm-ID: 441421 Cd Length: 326 Bit Score: 120.96 E-value: 2.37e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29029552 43 IGIKIIYSDHRSKDVAVIAESIRMAMGLRIKFptvVAGFDLVGHEDtGHSLHDYKEALMIPAKDGVKLpyFFHAGETD-W 121
Cdd:COG1816 121 ISVRLILCALRHLSPEAAFETLELALRYRDRG---VVGFGLAGDER-GFPPEKFAEAFARAREAGLHL--TAHAGEAGgP 194
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29029552 122 QgtsidrNILDAL-MLNTTRIGHGFALSKHPAVRTYSWKKDIPIEVCPISNQVLKLVSDLRNHPVATLMATGHPMVISSD 200
Cdd:COG1816 195 E------SIWEALdLLGAERIGHGVRAIEDPALVARLADRGIPLEVCPTSNVQLGVVPSLAEHPLRRLLDAGVRVTLNTD 268
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 29029552 201 DPAMFGAkGLSYDfYEVFMGIGGMkaDLRTLKQLAMNSIKYSTLLESEKntfmEIWKKRWDKFIA 265
Cdd:COG1816 269 DPLYFGT-TLTDE-YELAAEAFGL--SDADLAQLARNAIEASFLPEEEK----AALLAELDAYFA 325
|
|
| ADA |
cd01320 |
Adenosine deaminase (ADA) is a monomeric zinc dependent enzyme which catalyzes the ... |
78-250 |
7.68e-28 |
|
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: 108.83 E-value: 7.68e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29029552 78 VAGFDLVGHEdTGHSLHDYKEALMIPAKDGVKLPyfFHAGETDwqGTSidrNILDAL-MLNTTRIGHGFALSKHPAVRTY 156
Cdd:cd01320 158 VVGFDLAGDE-VGFPPEKFVRAFQRAREAGLRLT--AHAGEAG--GPE---SVRDALdLLGAERIGHGIRAIEDPELVKR 229
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29029552 157 SWKKDIPIEVCPISNQVLKLVSDLRNHPVATLMATGHPMVISSDDPAMFGAKgLSYDFYEVFMGIGgmkADLRTLKQLAM 236
Cdd:cd01320 230 LAERNIPLEVCPTSNVQTGAVKSLAEHPLRELLDAGVKVTINTDDPTVFGTY-LTDEYELLAEAFG---LTEEELKKLAR 305
|
170
....*....|....
gi 29029552 237 NSIKYSTLLESEKN 250
Cdd:cd01320 306 NAVEASFLSEEEKA 319
|
|
| PRK09358 |
PRK09358 |
adenosine deaminase; Provisional |
43-249 |
1.54e-26 |
|
adenosine deaminase; Provisional
Pssm-ID: 236480 Cd Length: 340 Bit Score: 105.64 E-value: 1.54e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29029552 43 IGIKIIYSDHRSKDVAVIAESIrmAMGLRIKFPTVVAGFDLVGHEDtGHSLHDYKEALMIpAKD-GvkLPYFFHAGETDw 121
Cdd:PRK09358 134 ISVRLILCFMRHFGEEAAAREL--EALAARYRDDGVVGFDLAGDEL-GFPPSKFARAFDR-ARDaG--LRLTAHAGEAG- 206
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29029552 122 qGTSidrNILDAL-MLNTTRIGHGFALSKHPAVRTYSWKKDIPIEVCPISNQVLKLVSDLRNHPVATLMATGHPMVISSD 200
Cdd:PRK09358 207 -GPE---SIWEALdELGAERIGHGVRAIEDPALMARLADRRIPLEVCPTSNVQTGAVPSLAEHPLKTLLDAGVRVTINTD 282
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 29029552 201 DPAMFGaKGLSyDFYEVFMGIGGMkaDLRTLKQLAMNSIKYSTLLESEK 249
Cdd:PRK09358 283 DPLVFG-TTLT-EEYEALAEAFGL--SDEDLAQLARNALEAAFLSEEEK 327
|
|
| aden_deam |
TIGR01430 |
adenosine deaminase; This family includes the experimentally verified adenosine deaminases of ... |
43-254 |
1.84e-25 |
|
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: 102.44 E-value: 1.84e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29029552 43 IGIKIIYSDHRSKDVAVIAESIRMAmgLRIKFPTVVaGFDLVGHEdTGHSLHDYKEALMIPAKDGVKLPyfFHAGETDwq 122
Cdd:TIGR01430 125 IKSRLILCGMRHKQPEAAEETLELA--KPYKEQTIV-GFGLAGDE-RGGPPPDFVRAFAIARELGLHLT--VHAGELG-- 196
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29029552 123 GTSIDRNILDalMLNTTRIGHGFALSKHPAVRTYSWKKDIPIEVCPISNQVLKLVSDLRNHPVATLMATGHPMVISSDDP 202
Cdd:TIGR01430 197 GPESVREALD--DLGATRIGHGVRALEDPELLKRLAQENITLEVCPTSNVALGVVKSLAEHPLRRFLEAGVKVTLNSDDP 274
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 29029552 203 AMFGakglSYDFYEVFMGIGGMKADLRTLKQLAMNSIKYSTLLESEKNTFME 254
Cdd:TIGR01430 275 AYFG----SYLTEEYEIAAKHAGLTEEELKQLARNALEGSFLSDDEKKELLA 322
|
|
| A_deaminase |
pfam00962 |
Adenosine deaminase; |
43-250 |
4.58e-19 |
|
Adenosine deaminase;
Pssm-ID: 425964 Cd Length: 330 Bit Score: 85.17 E-value: 4.58e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29029552 43 IGIKIIYSDHRSKDVAVIAESIRMAMGLRikfPTVVAGFDLVGHEdTGHSLH---DYKEALMIPAKDGVKLPyfFHAGET 119
Cdd:pfam00962 125 ITVRLIVCAMRHEHPECSREIAELAPRYR---DQGIVAFGLAGDE-KGFPPSlfrDHVEAFARARDAGLHLT--VHAGEA 198
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29029552 120 DWQGTsidrnILDAL-MLNTTRIGHGFALSKHPAVRTYSWKKDIPIEVCPISNQVLKLVSDLRNHPVATLMATGHPMVIS 198
Cdd:pfam00962 199 GGPQS-----VWEALdDLGAERIGHGVRSAEDPRLLDRLADRQIPLEICPTSNVQTGAVASLAEHPLKTFLRAGVPVSLN 273
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 29029552 199 SDDPAMFGAK-GLSYDFYEVFMGIggmkaDLRTLKQLAMNSIKYSTLLESEKN 250
Cdd:pfam00962 274 TDDPLMFGSDlLDEYQVAKRAPGF-----DEEELARLAKNAVKGSFLPADEKR 321
|
|
| PTZ00124 |
PTZ00124 |
adenosine deaminase; Provisional |
43-236 |
2.35e-14 |
|
adenosine deaminase; Provisional
Pssm-ID: 173415 Cd Length: 362 Bit Score: 71.82 E-value: 2.35e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29029552 43 IGIKIIYSDHRSKDVAVIAESIRMAMGLRIKFptvvAGFDLVGHEdtgHSLHDYKEALMIPAKDGVKLPyfFHAGEtDWQ 122
Cdd:PTZ00124 162 IEVGLLCIGDTGHDAAPIKESADFCLKHKADF----VGFDHAGHE---VDLKPFKDIFDYVREAGVNLT--VHAGE-DVT 231
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29029552 123 GTSIDRNILDALMLNTTRIGHGFALSKHPAVRTYSWKKDIPIEVCPISNQVLKLVSDLRNHPVATLMATGHPMVISSDDP 202
Cdd:PTZ00124 232 LPNLNTLYSAIQVLKVKRIGHGIRVAESQELIDMVKEKDILLEVCPISNVLLNNAKSMDTHPIRKLYDAGVKVSVNSDDP 311
|
170 180 190
....*....|....*....|....*....|....
gi 29029552 203 AMFgAKGLSYDFYEVFMGIGGMKADLRTLKQLAM 236
Cdd:PTZ00124 312 GMF-LTNINDDYEELYTHLNFTLADFMKMNEWAL 344
|
|
| metallo-dependent_hydrolases |
cd01292 |
Superfamily of metallo-dependent hydrolases (also called amidohydrolase superfamily) is a ... |
74-241 |
2.62e-10 |
|
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: 59.65 E-value: 2.62e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29029552 74 FPTVVAGFDLVGHE-DTGHSLHDYKEALMIPAKDGvkLPYFFHAGETDWQGTSIDRNILDALMLNTTRIGHGFALSKHpA 152
Cdd:cd01292 112 LELGAVGLKLAGPYtATGLSDESLRRVLEEARKLG--LPVVIHAGELPDPTRALEDLVALLRLGGRVVIGHVSHLDPE-L 188
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29029552 153 VRTYSwKKDIPIEVCPISNQVLKLvSDLRNHPVATLMATGHPMVISSDDPAMFGAKGLSYDFYEVFMgIGGMKADLRTLK 232
Cdd:cd01292 189 LELLK-EAGVSLEVCPLSNYLLGR-DGEGAEALRRLLELGIRVTLGTDGPPHPLGTDLLALLRLLLK-VLRLGLSLEEAL 265
|
170
....*....|
gi 29029552 233 QLA-MNSIKY 241
Cdd:cd01292 266 RLAtINPARA 275
|
|
| AMPD |
cd01319 |
AMP deaminase (AMPD) catalyzes the hydrolytic deamination of adensosine monophosphate (AMP) at ... |
115-205 |
3.76e-04 |
|
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: 41.58 E-value: 3.76e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29029552 115 HAGETDwqgtSIDrNILDALMLnTTRIGHGFALSKHPAVRTYSWKKDIPIEVCPISNQVLKLvsDLRNHPVATLMATGHP 194
Cdd:cd01319 332 HCGEAG----DID-HLASAFLL-AHGISHGINLRKVPVLQYLYYLTQIGIAMSPLSNNSLFL--SYEKNPFPEFFKRGLN 403
|
90
....*....|.
gi 29029552 195 MVISSDDPAMF 205
Cdd:cd01319 404 VSLSTDDPLQF 414
|
|
| PLN03055 |
PLN03055 |
AMP deaminase; Provisional |
115-204 |
6.90e-04 |
|
AMP deaminase; Provisional
Pssm-ID: 178613 Cd Length: 602 Bit Score: 40.62 E-value: 6.90e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29029552 115 HAGETDwqgtsiDRNILDALMLNTTRIGHGFALSKHPAVRTYSWKKDIPIEVCPISNQVLKLvsDLRNHPVATLMATGHP 194
Cdd:PLN03055 422 HAGEAG------DIDHLAAAFLLAHNIAHGNNLRKSPGLQYLYYLAQIGLAMSPLSNNSLFL--DYHRNPFPMFFARGLN 493
|
90
....*....|
gi 29029552 195 MVISSDDPAM 204
Cdd:PLN03055 494 VSLSTDDPLQ 503
|
|
| AMP_deaminase |
TIGR01429 |
AMP deaminase; This model describes AMP deaminase, a large, well-conserved eukaryotic protein ... |
111-205 |
2.47e-03 |
|
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: 39.06 E-value: 2.47e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29029552 111 PYFFHAGETDWQGTSidrnildalMLNTTRIGHGFALSKHPAVRTYSWKKDIPIEVCPISNQVLKLVSDlRNhPVATLMA 190
Cdd:TIGR01429 443 PHCGEAGSVDHLVSA---------FLTSHGINHGILLRKVPVLQYLYYLTQIPIAMSPLSNNSLFLEYS-KN-PLPEYLH 511
|
90
....*....|....*
gi 29029552 191 TGHPMVISSDDPAMF 205
Cdd:TIGR01429 512 KGLNVSLSTDDPLQF 526
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