|
Name |
Accession |
Description |
Interval |
E-value |
| adm_rel |
TIGR01431 |
adenosine deaminase-related growth factor; Members of this family have been described as ... |
1-389 |
0e+00 |
|
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: 705.41 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532691763 1 MDWLVRNVTYRPHCHICFTPRGIMQFRFAHPTPRPSEKCSKWILLEDYRKrVQNVTEFDDSLLRNFTLVTQHPEVIYTNQ 80
Cdd:TIGR01431 93 MDWLVRNVTYRPNLHICFTKRNIMVLRFRHPTPRPSECCSKWILLEDYRK-SQNVEEFDDSLLRNFTLVTTHPEVDYTTQ 171
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532691763 81 NVVWSKFETIFFTISGLIHYAPVFRDYVFRSMQEFYEDNVLYMEIRARLLPVYELSGEHHDEEWSVKTYQEVAQKFVETH 160
Cdd:TIGR01431 172 NVVWSRFETIFFTLSGLLHYAPVFRDYYFRALEEFYEDNVQYMELRSRLFPLYELSGTHHDEEWSVKTYKEVTEKFVEEH 251
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532691763 161 PEFIGIKIIYSDHRSKDVAVIAESIRMAMGLRIKFPTVVAGFDLVGHEDTGHSLHDYKEALMIPAkDGVKLPYFFHAGET 240
Cdd:TIGR01431 252 PDFIGIKIIYSDLRSKDVEEIAEYIKMAMGLRIKYPDFVAGFDLVGQEDTGHSLLDYKDALLIPS-IGVKLPYFFHAGET 330
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532691763 241 DWQGTSIDRNILDALMLNTTRIGHGFALSKHPAVRTYSWKKDIPIEVCPISNQVLKLVSDLRNHPVATLMATGHPMVISS 320
Cdd:TIGR01431 331 NWQGTSVDRNLLDALLLNTTRIGHGFALSKHPAVRTYSKERDIPIEVCPISNQVLKLVSDLRNHPVATLMADNYPMVISS 410
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 532691763 321 DDPAMFGAKGLSYDFYEVFMGIGGMKADLRTLKQLAMNSIKYSTLLESEKNTFMEIWKKRWDKFIADVA 389
Cdd:TIGR01431 411 DDPAFWGAKGLSYDFYEAFMGIAGMKADLRTLKQLALNSIKYSALSEEEKNTAMAKWKKQWDKFIDDVL 479
|
|
| ADGF |
cd01321 |
Adenosine deaminase-related growth factors (ADGF), a novel family of secreted growth-factors ... |
81-381 |
1.23e-179 |
|
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: 502.96 E-value: 1.23e-179
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532691763 81 NVVWSKFETIFFTISGLIHYAPVFRDYVFRSMQEFYEDNVLYMEIRARLLPVYELSGEHHDEEWSVKTYQEVAQKFVETH 160
Cdd:cd01321 45 KNATYRFEQIFDIIDGLLTYLPIFRDYYRRLLEELYEDNVQYVELRSSFSPLYDLDGREYDYEETVQLLEEVVEKFKKTH 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532691763 161 PEFIGIKIIYSDHRSKDVAVIAESIRMAMGLRIKFPTVVAGFDLVGHEDTGHSLHDYKEALMIPAKDGVKLPYFFHAGET 240
Cdd:cd01321 125 PDFIGLKIIYATLRNFNDSEIKESMEQCLNLKKKFPDFIAGFDLVGQEDAGRPLLDFLPQLLWFPKQCAEIPFFFHAGET 204
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532691763 241 DWQGTSIDRNILDALMLNTTRIGHGFALSKHPAVRTYSWKKDIPIEVCPISNQVLKLVSDLRNHPVATLMATGHPMVISS 320
Cdd:cd01321 205 NGDGTETDENLVDALLLNTKRIGHGFALPKHPLLMDLVKKKNIAIEVCPISNQVLGLVSDLRNHPAAALLARGVPVVISS 284
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 532691763 321 DDPAMFGAKGLSYDFYEVFMGIGGMKADLRTLKQLAMNSIKYSTLLESEKNTFMEIWKKRW 381
Cdd:cd01321 285 DDPGFWGAKGLSHDFYQAFMGLAPADAGLRGLKQLAENSIRYSALSDQEKDEAVAKWEKKW 345
|
|
| Add |
COG1816 |
Adenosine deaminase [Nucleotide transport and metabolism]; Adenosine deaminase is part of the ... |
108-386 |
8.27e-33 |
|
Adenosine deaminase [Nucleotide transport and metabolism]; Adenosine deaminase is part of the Pathway/BioSystem: Menaquinone biosynthesis
Pssm-ID: 441421 Cd Length: 326 Bit Score: 125.20 E-value: 8.27e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532691763 108 VFRSMQEFY-----------EDNVLYMEIRarLLPVYelsgeHHDEEWSVKTYQE-VAQKFVETHPEF-IGIKIIYSDHR 174
Cdd:COG1816 59 VLQTEEDFRrlayeyledaaADGVRYAEIR--FDPQL-----HTRRGLSLEEVVEaVLDGLREAEREFgISVRLILCALR 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532691763 175 SKDVAVIAESIRMAMGLRIKFptvVAGFDLVGHEDtGHSLHDYKEALMIPAKDGVKLpyFFHAGETD-WQgtsidrNILD 253
Cdd:COG1816 132 HLSPEAAFETLELALRYRDRG---VVGFGLAGDER-GFPPEKFAEAFARAREAGLHL--TAHAGEAGgPE------SIWE 199
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532691763 254 AL-MLNTTRIGHGFALSKHPAVRTYSWKKDIPIEVCPISNQVLKLVSDLRNHPVATLMATGHPMVISSDDPAMFGAkGLS 332
Cdd:COG1816 200 ALdLLGAERIGHGVRAIEDPALVARLADRGIPLEVCPTSNVQLGVVPSLAEHPLRRLLDAGVRVTLNTDDPLYFGT-TLT 278
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 532691763 333 YDfYEVFMGIGGMkaDLRTLKQLAMNSIKYSTLLESEKntfmEIWKKRWDKFIA 386
Cdd:COG1816 279 DE-YELAAEAFGL--SDADLAQLARNAIEASFLPEEEK----AALLAELDAYFA 325
|
|
| PRK09358 |
PRK09358 |
adenosine deaminase; Provisional |
104-370 |
6.11e-29 |
|
adenosine deaminase; Provisional
Pssm-ID: 236480 Cd Length: 340 Bit Score: 115.27 E-value: 6.11e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532691763 104 FRDYVFRSMQEFYEDNVLYMEIR-------ARLLPVYELsgehhdeewsVKTYQEVAQKFVETHPefIGIKIIYSDHRSK 176
Cdd:PRK09358 79 LRRLAFEYLEDAAADGVVYAEIRfdpqlhtERGLPLEEV----------VEAVLDGLRAAEAEFG--ISVRLILCFMRHF 146
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532691763 177 DVAVIAESIrmAMGLRIKFPTVVAGFDLVGHEDtGHSLHDYKEALMIpAKD-GvkLPYFFHAGETDwqGTSidrNILDAL 255
Cdd:PRK09358 147 GEEAAAREL--EALAARYRDDGVVGFDLAGDEL-GFPPSKFARAFDR-ARDaG--LRLTAHAGEAG--GPE---SIWEAL 215
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532691763 256 -MLNTTRIGHGFALSKHPAVRTYSWKKDIPIEVCPISNQVLKLVSDLRNHPVATLMATGHPMVISSDDPAMFGaKGLSyD 334
Cdd:PRK09358 216 dELGAERIGHGVRAIEDPALMARLADRRIPLEVCPTSNVQTGAVPSLAEHPLKTLLDAGVRVTINTDDPLVFG-TTLT-E 293
|
250 260 270
....*....|....*....|....*....|....*.
gi 532691763 335 FYEVFMGIGGMkaDLRTLKQLAMNSIKYSTLLESEK 370
Cdd:PRK09358 294 EYEALAEAFGL--SDEDLAQLARNALEAAFLSEEEK 327
|
|
| A_deaminase |
pfam00962 |
Adenosine deaminase; |
104-371 |
1.53e-19 |
|
Adenosine deaminase;
Pssm-ID: 425964 Cd Length: 330 Bit Score: 88.64 E-value: 1.53e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532691763 104 FRDYVFRSMQEFYEDNVLYMEIRarllpvyeLSGEHH-----DEEWSVKTyqeVAQKFVETHPEF-IGIKIIYSDHRSKD 177
Cdd:pfam00962 70 IRRLAFEYAEDVAKDGVVYAEVR--------YDPQSHasrglSPDTVVDA---VLDAVDAAEREFgITVRLIVCAMRHEH 138
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532691763 178 VAVIAESIRMAMGLRikfPTVVAGFDLVGHEdTGHSLH---DYKEALMIPAKDGVKLPyfFHAGETDWQGTsidrnILDA 254
Cdd:pfam00962 139 PECSREIAELAPRYR---DQGIVAFGLAGDE-KGFPPSlfrDHVEAFARARDAGLHLT--VHAGEAGGPQS-----VWEA 207
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532691763 255 L-MLNTTRIGHGFALSKHPAVRTYSWKKDIPIEVCPISNQVLKLVSDLRNHPVATLMATGHPMVISSDDPAMFGAK-GLS 332
Cdd:pfam00962 208 LdDLGAERIGHGVRSAEDPRLLDRLADRQIPLEICPTSNVQTGAVASLAEHPLKTFLRAGVPVSLNTDDPLMFGSDlLDE 287
|
250 260 270
....*....|....*....|....*....|....*....
gi 532691763 333 YDFYEVFMGIggmkaDLRTLKQLAMNSIKYSTLLESEKN 371
Cdd:pfam00962 288 YQVAKRAPGF-----DEEELARLAKNAVKGSFLPADEKR 321
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| adm_rel |
TIGR01431 |
adenosine deaminase-related growth factor; Members of this family have been described as ... |
1-389 |
0e+00 |
|
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: 705.41 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532691763 1 MDWLVRNVTYRPHCHICFTPRGIMQFRFAHPTPRPSEKCSKWILLEDYRKrVQNVTEFDDSLLRNFTLVTQHPEVIYTNQ 80
Cdd:TIGR01431 93 MDWLVRNVTYRPNLHICFTKRNIMVLRFRHPTPRPSECCSKWILLEDYRK-SQNVEEFDDSLLRNFTLVTTHPEVDYTTQ 171
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532691763 81 NVVWSKFETIFFTISGLIHYAPVFRDYVFRSMQEFYEDNVLYMEIRARLLPVYELSGEHHDEEWSVKTYQEVAQKFVETH 160
Cdd:TIGR01431 172 NVVWSRFETIFFTLSGLLHYAPVFRDYYFRALEEFYEDNVQYMELRSRLFPLYELSGTHHDEEWSVKTYKEVTEKFVEEH 251
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532691763 161 PEFIGIKIIYSDHRSKDVAVIAESIRMAMGLRIKFPTVVAGFDLVGHEDTGHSLHDYKEALMIPAkDGVKLPYFFHAGET 240
Cdd:TIGR01431 252 PDFIGIKIIYSDLRSKDVEEIAEYIKMAMGLRIKYPDFVAGFDLVGQEDTGHSLLDYKDALLIPS-IGVKLPYFFHAGET 330
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532691763 241 DWQGTSIDRNILDALMLNTTRIGHGFALSKHPAVRTYSWKKDIPIEVCPISNQVLKLVSDLRNHPVATLMATGHPMVISS 320
Cdd:TIGR01431 331 NWQGTSVDRNLLDALLLNTTRIGHGFALSKHPAVRTYSKERDIPIEVCPISNQVLKLVSDLRNHPVATLMADNYPMVISS 410
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 532691763 321 DDPAMFGAKGLSYDFYEVFMGIGGMKADLRTLKQLAMNSIKYSTLLESEKNTFMEIWKKRWDKFIADVA 389
Cdd:TIGR01431 411 DDPAFWGAKGLSYDFYEAFMGIAGMKADLRTLKQLALNSIKYSALSEEEKNTAMAKWKKQWDKFIDDVL 479
|
|
| ADGF |
cd01321 |
Adenosine deaminase-related growth factors (ADGF), a novel family of secreted growth-factors ... |
81-381 |
1.23e-179 |
|
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: 502.96 E-value: 1.23e-179
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532691763 81 NVVWSKFETIFFTISGLIHYAPVFRDYVFRSMQEFYEDNVLYMEIRARLLPVYELSGEHHDEEWSVKTYQEVAQKFVETH 160
Cdd:cd01321 45 KNATYRFEQIFDIIDGLLTYLPIFRDYYRRLLEELYEDNVQYVELRSSFSPLYDLDGREYDYEETVQLLEEVVEKFKKTH 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532691763 161 PEFIGIKIIYSDHRSKDVAVIAESIRMAMGLRIKFPTVVAGFDLVGHEDTGHSLHDYKEALMIPAKDGVKLPYFFHAGET 240
Cdd:cd01321 125 PDFIGLKIIYATLRNFNDSEIKESMEQCLNLKKKFPDFIAGFDLVGQEDAGRPLLDFLPQLLWFPKQCAEIPFFFHAGET 204
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532691763 241 DWQGTSIDRNILDALMLNTTRIGHGFALSKHPAVRTYSWKKDIPIEVCPISNQVLKLVSDLRNHPVATLMATGHPMVISS 320
Cdd:cd01321 205 NGDGTETDENLVDALLLNTKRIGHGFALPKHPLLMDLVKKKNIAIEVCPISNQVLGLVSDLRNHPAAALLARGVPVVISS 284
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 532691763 321 DDPAMFGAKGLSYDFYEVFMGIGGMKADLRTLKQLAMNSIKYSTLLESEKNTFMEIWKKRW 381
Cdd:cd01321 285 DDPGFWGAKGLSHDFYQAFMGLAPADAGLRGLKQLAENSIRYSALSDQEKDEAVAKWEKKW 345
|
|
| ADA_AMPD |
cd00443 |
Adenosine/AMP deaminase. Adenosine deaminases (ADAs) are present in pro- and eukaryotic ... |
73-377 |
1.15e-47 |
|
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: 164.44 E-value: 1.15e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532691763 73 PEVIYTNqnvVWSKFETIFFTISGLIHYAPVFRDYVFRSMQEFYEDNVLYMEIRarllpvYELSGEHHDEEWSVKTYQ-- 150
Cdd:cd00443 16 PETLLEL---IKKEFFEKFLLVHNLLQKGEALARALKEVIEEFAEDNVQYLELR------TTPRLLETEKGLTKEQYWll 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532691763 151 --EVAQKFVETHPeFIGIKIIYSDHRSKDV---AVIAESIrmaMGLRIKFPTVVAGFDLVGHEDTGHS-LHDYKEALMIp 224
Cdd:cd00443 87 viEGISEAKQWFP-PIKVRLILSVDRRGPYvqnYLVASEI---LELAKFLSNYVVGIDLVGDESKGENpLRDFYSYYEY- 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532691763 225 AKDGVKLPYFFHAGETDWQGTsidrnILDALMLNTTRIGHGFALSKHPAVRTYSWKKDIPIEVCPISNQVLKLVSDLRNH 304
Cdd:cd00443 162 ARRLGLLGLTLHCGETGNREE-----LLQALLLLPDRIGHGIFLLKHPELIYLVKLRNIPIEVCPTSNVVLGTVQSYEKH 236
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 532691763 305 PVATLMATGHPMVISSDDPAMFGAkGLSYDFYEVFMgigGMKADLRTLKQLAMNSIKYSTLLESEKNTFMEIW 377
Cdd:cd00443 237 PFMRFFKAGLPVSLSTDDPGIFGT-SLSEEYSLAAK---TFGLTFEDLCELNRNSVLSSFAKDEEKKSLLEVL 305
|
|
| Add |
COG1816 |
Adenosine deaminase [Nucleotide transport and metabolism]; Adenosine deaminase is part of the ... |
108-386 |
8.27e-33 |
|
Adenosine deaminase [Nucleotide transport and metabolism]; Adenosine deaminase is part of the Pathway/BioSystem: Menaquinone biosynthesis
Pssm-ID: 441421 Cd Length: 326 Bit Score: 125.20 E-value: 8.27e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532691763 108 VFRSMQEFY-----------EDNVLYMEIRarLLPVYelsgeHHDEEWSVKTYQE-VAQKFVETHPEF-IGIKIIYSDHR 174
Cdd:COG1816 59 VLQTEEDFRrlayeyledaaADGVRYAEIR--FDPQL-----HTRRGLSLEEVVEaVLDGLREAEREFgISVRLILCALR 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532691763 175 SKDVAVIAESIRMAMGLRIKFptvVAGFDLVGHEDtGHSLHDYKEALMIPAKDGVKLpyFFHAGETD-WQgtsidrNILD 253
Cdd:COG1816 132 HLSPEAAFETLELALRYRDRG---VVGFGLAGDER-GFPPEKFAEAFARAREAGLHL--TAHAGEAGgPE------SIWE 199
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532691763 254 AL-MLNTTRIGHGFALSKHPAVRTYSWKKDIPIEVCPISNQVLKLVSDLRNHPVATLMATGHPMVISSDDPAMFGAkGLS 332
Cdd:COG1816 200 ALdLLGAERIGHGVRAIEDPALVARLADRGIPLEVCPTSNVQLGVVPSLAEHPLRRLLDAGVRVTLNTDDPLYFGT-TLT 278
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 532691763 333 YDfYEVFMGIGGMkaDLRTLKQLAMNSIKYSTLLESEKntfmEIWKKRWDKFIA 386
Cdd:COG1816 279 DE-YELAAEAFGL--SDADLAQLARNAIEASFLPEEEK----AALLAELDAYFA 325
|
|
| ADA |
cd01320 |
Adenosine deaminase (ADA) is a monomeric zinc dependent enzyme which catalyzes the ... |
88-371 |
8.77e-30 |
|
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: 116.92 E-value: 8.77e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532691763 88 ETIFFTISGLIHYApVFRDYVFRSMQEFYEDNVLYMEIRarllpvyeLSGEHH-----DEEWSVKTYQEVAQKFVETHPe 162
Cdd:cd01320 56 AKYDFGLSVLQTEE-DFERLAYEYLEDAAADGVVYAEIR--------FSPQLHtrrglSFDEVVEAVLRGLDEAEAEFG- 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532691763 163 fIGIKIIYSDHRSKDVAVIAESIRMAmgLRIKFPTVVaGFDLVGHEdTGHSLHDYKEALMIPAKDGVKLPyfFHAGETDw 242
Cdd:cd01320 126 -IKARLILCGLRHLSPESAQETLELA--LKYRDKGVV-GFDLAGDE-VGFPPEKFVRAFQRAREAGLRLT--AHAGEAG- 197
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532691763 243 qGTSidrNILDAL-MLNTTRIGHGFALSKHPAVRTYSWKKDIPIEVCPISNQVLKLVSDLRNHPVATLMATGHPMVISSD 321
Cdd:cd01320 198 -GPE---SVRDALdLLGAERIGHGIRAIEDPELVKRLAERNIPLEVCPTSNVQTGAVKSLAEHPLRELLDAGVKVTINTD 273
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 532691763 322 DPAMFGAKgLSYDFYEVFMGIGgmkADLRTLKQLAMNSIKYSTLLESEKN 371
Cdd:cd01320 274 DPTVFGTY-LTDEYELLAEAFG---LTEEELKKLARNAVEASFLSEEEKA 319
|
|
| PRK09358 |
PRK09358 |
adenosine deaminase; Provisional |
104-370 |
6.11e-29 |
|
adenosine deaminase; Provisional
Pssm-ID: 236480 Cd Length: 340 Bit Score: 115.27 E-value: 6.11e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532691763 104 FRDYVFRSMQEFYEDNVLYMEIR-------ARLLPVYELsgehhdeewsVKTYQEVAQKFVETHPefIGIKIIYSDHRSK 176
Cdd:PRK09358 79 LRRLAFEYLEDAAADGVVYAEIRfdpqlhtERGLPLEEV----------VEAVLDGLRAAEAEFG--ISVRLILCFMRHF 146
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532691763 177 DVAVIAESIrmAMGLRIKFPTVVAGFDLVGHEDtGHSLHDYKEALMIpAKD-GvkLPYFFHAGETDwqGTSidrNILDAL 255
Cdd:PRK09358 147 GEEAAAREL--EALAARYRDDGVVGFDLAGDEL-GFPPSKFARAFDR-ARDaG--LRLTAHAGEAG--GPE---SIWEAL 215
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532691763 256 -MLNTTRIGHGFALSKHPAVRTYSWKKDIPIEVCPISNQVLKLVSDLRNHPVATLMATGHPMVISSDDPAMFGaKGLSyD 334
Cdd:PRK09358 216 dELGAERIGHGVRAIEDPALMARLADRRIPLEVCPTSNVQTGAVPSLAEHPLKTLLDAGVRVTINTDDPLVFG-TTLT-E 293
|
250 260 270
....*....|....*....|....*....|....*.
gi 532691763 335 FYEVFMGIGGMkaDLRTLKQLAMNSIKYSTLLESEK 370
Cdd:PRK09358 294 EYEALAEAFGL--SDEDLAQLARNALEAAFLSEEEK 327
|
|
| aden_deam |
TIGR01430 |
adenosine deaminase; This family includes the experimentally verified adenosine deaminases of ... |
84-375 |
5.71e-26 |
|
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: 106.67 E-value: 5.71e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532691763 84 WSKFETIFFTISGLIHYAPVFRDYVFRSMQEFYEDNVLYMEIRarllpvyeLSGEHH-DEEWSVKTYQE-----VAQKFV 157
Cdd:TIGR01430 50 LQDFLAKYDFGVEVLRTEDDFKRLAYEYVEKAAKDGVVYAEVF--------FDPQLHtNRGISPDTVVEavldgLDEAER 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532691763 158 ETHpefIGIKIIYSDHRSKDVAVIAESIRMAmgLRIKFPTVVaGFDLVGHEdTGHSLHDYKEALMIPAKDGVKLPyfFHA 237
Cdd:TIGR01430 122 DFG---IKSRLILCGMRHKQPEAAEETLELA--KPYKEQTIV-GFGLAGDE-RGGPPPDFVRAFAIARELGLHLT--VHA 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532691763 238 GETDwqGTSIDRNILDalMLNTTRIGHGFALSKHPAVRTYSWKKDIPIEVCPISNQVLKLVSDLRNHPVATLMATGHPMV 317
Cdd:TIGR01430 193 GELG--GPESVREALD--DLGATRIGHGVRALEDPELLKRLAQENITLEVCPTSNVALGVVKSLAEHPLRRFLEAGVKVT 268
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 532691763 318 ISSDDPAMFGakglSYDFYEVFMGIGGMKADLRTLKQLAMNSIKYSTLLESEKNTFME 375
Cdd:TIGR01430 269 LNSDDPAYFG----SYLTEEYEIAAKHAGLTEEELKQLARNALEGSFLSDDEKKELLA 322
|
|
| A_deaminase |
pfam00962 |
Adenosine deaminase; |
104-371 |
1.53e-19 |
|
Adenosine deaminase;
Pssm-ID: 425964 Cd Length: 330 Bit Score: 88.64 E-value: 1.53e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532691763 104 FRDYVFRSMQEFYEDNVLYMEIRarllpvyeLSGEHH-----DEEWSVKTyqeVAQKFVETHPEF-IGIKIIYSDHRSKD 177
Cdd:pfam00962 70 IRRLAFEYAEDVAKDGVVYAEVR--------YDPQSHasrglSPDTVVDA---VLDAVDAAEREFgITVRLIVCAMRHEH 138
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532691763 178 VAVIAESIRMAMGLRikfPTVVAGFDLVGHEdTGHSLH---DYKEALMIPAKDGVKLPyfFHAGETDWQGTsidrnILDA 254
Cdd:pfam00962 139 PECSREIAELAPRYR---DQGIVAFGLAGDE-KGFPPSlfrDHVEAFARARDAGLHLT--VHAGEAGGPQS-----VWEA 207
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532691763 255 L-MLNTTRIGHGFALSKHPAVRTYSWKKDIPIEVCPISNQVLKLVSDLRNHPVATLMATGHPMVISSDDPAMFGAK-GLS 332
Cdd:pfam00962 208 LdDLGAERIGHGVRSAEDPRLLDRLADRQIPLEICPTSNVQTGAVASLAEHPLKTFLRAGVPVSLNTDDPLMFGSDlLDE 287
|
250 260 270
....*....|....*....|....*....|....*....
gi 532691763 333 YDFYEVFMGIggmkaDLRTLKQLAMNSIKYSTLLESEKN 371
Cdd:pfam00962 288 YQVAKRAPGF-----DEEELARLAKNAVKGSFLPADEKR 321
|
|
| PTZ00124 |
PTZ00124 |
adenosine deaminase; Provisional |
116-357 |
6.99e-15 |
|
adenosine deaminase; Provisional
Pssm-ID: 173415 Cd Length: 362 Bit Score: 75.29 E-value: 6.99e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532691763 116 YEDNVLYMEIRARllPVYELSGEHHDEEWSVKTYQEVAQKFVETHPEFIGIKIIYSDHRSKDVAVIAESIRMAMGLRIKF 195
Cdd:PTZ00124 116 YKEGVVLMEFRYS--PTFVAFKHNLDIDLIHQAIVKGIKEAVELLDHKIEVGLLCIGDTGHDAAPIKESADFCLKHKADF 193
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532691763 196 ptvvAGFDLVGHEdtgHSLHDYKEALMIPAKDGVKLPyfFHAGEtDWQGTSIDRNILDALMLNTTRIGHGFALSKHPAVR 275
Cdd:PTZ00124 194 ----VGFDHAGHE---VDLKPFKDIFDYVREAGVNLT--VHAGE-DVTLPNLNTLYSAIQVLKVKRIGHGIRVAESQELI 263
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532691763 276 TYSWKKDIPIEVCPISNQVLKLVSDLRNHPVATLMATGHPMVISSDDPAMFgAKGLSYDFYEVFMGIGGMKADLRTLKQL 355
Cdd:PTZ00124 264 DMVKEKDILLEVCPISNVLLNNAKSMDTHPIRKLYDAGVKVSVNSDDPGMF-LTNINDDYEELYTHLNFTLADFMKMNEW 342
|
..
gi 532691763 356 AM 357
Cdd:PTZ00124 343 AL 344
|
|
| metallo-dependent_hydrolases |
cd01292 |
Superfamily of metallo-dependent hydrolases (also called amidohydrolase superfamily) is a ... |
195-362 |
1.72e-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: 61.20 E-value: 1.72e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532691763 195 FPTVVAGFDLVGHE-DTGHSLHDYKEALMIPAKDGvkLPYFFHAGETDWQGTSIDRNILDALMLNTTRIGHGFALSKHpA 273
Cdd:cd01292 112 LELGAVGLKLAGPYtATGLSDESLRRVLEEARKLG--LPVVIHAGELPDPTRALEDLVALLRLGGRVVIGHVSHLDPE-L 188
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532691763 274 VRTYSwKKDIPIEVCPISNQVLKLvSDLRNHPVATLMATGHPMVISSDDPAMFGAKGLSYDFYEVFMgIGGMKADLRTLK 353
Cdd:cd01292 189 LELLK-EAGVSLEVCPLSNYLLGR-DGEGAEALRRLLELGIRVTLGTDGPPHPLGTDLLALLRLLLK-VLRLGLSLEEAL 265
|
170
....*....|
gi 532691763 354 QLA-MNSIKY 362
Cdd:cd01292 266 RLAtINPARA 275
|
|
| AMPD |
cd01319 |
AMP deaminase (AMPD) catalyzes the hydrolytic deamination of adensosine monophosphate (AMP) at ... |
261-326 |
1.17e-03 |
|
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: 40.81 E-value: 1.17e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 532691763 261 RIGHGFALSKHPAVRTYSWKKDIPIEVCPISNQVLKLvsDLRNHPVATLMATGHPMVISSDDPAMF 326
Cdd:cd01319 351 GISHGINLRKVPVLQYLYYLTQIGIAMSPLSNNSLFL--SYEKNPFPEFFKRGLNVSLSTDDPLQF 414
|
|
| PLN03055 |
PLN03055 |
AMP deaminase; Provisional |
236-325 |
2.33e-03 |
|
AMP deaminase; Provisional
Pssm-ID: 178613 Cd Length: 602 Bit Score: 39.85 E-value: 2.33e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532691763 236 HAGETDwqgtsiDRNILDALMLNTTRIGHGFALSKHPAVRTYSWKKDIPIEVCPISNQVLKLvsDLRNHPVATLMATGHP 315
Cdd:PLN03055 422 HAGEAG------DIDHLAAAFLLAHNIAHGNNLRKSPGLQYLYYLAQIGLAMSPLSNNSLFL--DYHRNPFPMFFARGLN 493
|
90
....*....|
gi 532691763 316 MVISSDDPAM 325
Cdd:PLN03055 494 VSLSTDDPLQ 503
|
|
| AMP_deaminase |
TIGR01429 |
AMP deaminase; This model describes AMP deaminase, a large, well-conserved eukaryotic protein ... |
232-326 |
7.80e-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: 38.29 E-value: 7.80e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532691763 232 PYFFHAGETDWQGTSidrnildalMLNTTRIGHGFALSKHPAVRTYSWKKDIPIEVCPISNQVLKLVSDlRNhPVATLMA 311
Cdd:TIGR01429 443 PHCGEAGSVDHLVSA---------FLTSHGINHGILLRKVPVLQYLYYLTQIPIAMSPLSNNSLFLEYS-KN-PLPEYLH 511
|
90
....*....|....*
gi 532691763 312 TGHPMVISSDDPAMF 326
Cdd:TIGR01429 512 KGLNVSLSTDDPLQF 526
|
|
| |
