|
Name |
Accession |
Description |
Interval |
E-value |
| ADA |
cd01320 |
Adenosine deaminase (ADA) is a monomeric zinc dependent enzyme which catalyzes the ... |
48-383 |
3.30e-125 |
|
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: 363.83 E-value: 3.30e-125
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17538512 48 NFPKVELHLHLDGAVRFDTLIDLSQQKGIPLAGAkTVEELKKVLVTHEPANLSKVLEAFEIFLPVIRgDLAAIERVAYEL 127
Cdd:cd01320 1 NLPKAELHLHLDGSLRPETILELAKKNGITLPAS-DVELLELVVAAYNFSDLQDFLAKYDFGLSVLQ-TEEDFERLAYEY 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17538512 128 CEDQHNNGVVYFEGRYSPHLLLCNDYPEVTAAHVVAavkKGFDRGEKQFGIKARSILCCIRGLDKKFPQLILDLATDLKQ 207
Cdd:cd01320 79 LEDAAADGVVYAEIRFSPQLHTRRGLSFDEVVEAVL---RGLDEAEAEFGIKARLILCGLRHLSPESAQETLELALKYRD 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17538512 208 LGVVAIDVAGSAHGAdeqYEPEVVAAFQEAHKRGIHRTVHAGESGGPKEVIKAIEDMYAERIGHGYRVMRDEEmyLEHFV 287
Cdd:cd01320 156 KGVVGFDLAGDEVGF---PPEKFVRAFQRAREAGLRLTAHAGEAGGPESVRDALDLLGAERIGHGIRAIEDPE--LVKRL 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17538512 288 NSKNVHLEACPYSSVMTGAVPlDWKNHPIARWAKDDVNFSVSRDDPTCFDNSMLSELTLVHKQIGLDVHQLWKAQLNAAR 367
Cdd:cd01320 231 AERNIPLEVCPTSNVQTGAVK-SLAEHPLRELLDAGVKVTINTDDPTVFGTYLTDEYELLAEAFGLTEEELKKLARNAVE 309
|
330
....*....|....*.
gi 17538512 368 SCFLPEDEKAELVKRV 383
Cdd:cd01320 310 ASFLSEEEKAELLKRI 325
|
|
| Add |
COG1816 |
Adenosine deaminase [Nucleotide transport and metabolism]; Adenosine deaminase is part of the ... |
50-385 |
5.80e-86 |
|
Adenosine deaminase [Nucleotide transport and metabolism]; Adenosine deaminase is part of the Pathway/BioSystem: Menaquinone biosynthesis
Pssm-ID: 441421 Cd Length: 326 Bit Score: 263.87 E-value: 5.80e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17538512 50 PKVELHLHLDGAVRFDTLIDLSQQKGIPLAgAKTVEELKKVLVTHepaNLSKVLEAFEIFLPVIRgDLAAIERVAYELCE 129
Cdd:COG1816 1 PKAELHLHLEGSLRPETLLELAARNGIDLP-AADVEELRAAYDFR---DLQSFLDTYDAGAAVLQ-TEEDFRRLAYEYLE 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17538512 130 DQHNNGVVYFEGRYSPHLLLCN--DYPEVTAAHVvaavkKGFDRGEKQFGIKARSILCCIRGLDKKFPQLILDLATDLKQ 207
Cdd:COG1816 76 DAAADGVRYAEIRFDPQLHTRRglSLEEVVEAVL-----DGLREAEREFGISVRLILCALRHLSPEAAFETLELALRYRD 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17538512 208 LGVVAIDVAGSAHGAD-EQYEPevvaAFQEAHKRGIHRTVHAGESGGPKEVIKAIEDMYAERIGHGYRVMRDEEmyLEHF 286
Cdd:COG1816 151 RGVVGFGLAGDERGFPpEKFAE----AFARAREAGLHLTAHAGEAGGPESIWEALDLLGAERIGHGVRAIEDPA--LVAR 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17538512 287 VNSKNVHLEACPYSSVMTGAVPlDWKNHPIARWAKDDVNFSVSRDDPTCFDNSMLSELTLVHKQIGLDVHQLWKAQLNAA 366
Cdd:COG1816 225 LADRGIPLEVCPTSNVQLGVVP-SLAEHPLRRLLDAGVRVTLNTDDPLYFGTTLTDEYELAAEAFGLSDADLAQLARNAI 303
|
330
....*....|....*....
gi 17538512 367 RSCFLPEDEKAELVKRVEA 385
Cdd:COG1816 304 EASFLPEEEKAALLAELDA 322
|
|
| aden_deam |
TIGR01430 |
adenosine deaminase; This family includes the experimentally verified adenosine deaminases of ... |
50-383 |
8.15e-75 |
|
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: 235.33 E-value: 8.15e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17538512 50 PKVELHLHLDGAVRFDTLIDLSQQKGIPLAGAKTVEELKKVLVTHEPaNLSKVLEAFEIFLPVIRgDLAAIERVAYELCE 129
Cdd:TIGR01430 2 PKAELHLHLEGSIRPETLLELAQKNGIPLPADLQSGEELKEAYDKFR-DLQDFLAKYDFGVEVLR-TEDDFKRLAYEYVE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17538512 130 DQHNNGVVYFEGRYSPHLLLCNdypEVTAAHVVAAVKKGFDRGEKQFGIKARSILCCIRGLDKKFPQLILDLATDLKQLG 209
Cdd:TIGR01430 80 KAAKDGVVYAEVFFDPQLHTNR---GISPDTVVEAVLDGLDEAERDFGIKSRLILCGMRHKQPEAAEETLELAKPYKEQT 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17538512 210 VVAIDVAGsahgaDEQYEP--EVVAAFQEAHKRGIHRTVHAGESGGPKEVIKAIEDMYAERIGHGYRVMRDEEMYleHFV 287
Cdd:TIGR01430 157 IVGFGLAG-----DERGGPppDFVRAFAIARELGLHLTVHAGELGGPESVREALDDLGATRIGHGVRALEDPELL--KRL 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17538512 288 NSKNVHLEACPYSSVMTGAVPLDwKNHPIARWAKDDVNFSVSRDDPTCFDNSMLSELTLVHKQIGLDVHQLWKAQLNAAR 367
Cdd:TIGR01430 230 AQENITLEVCPTSNVALGVVKSL-AEHPLRRFLEAGVKVTLNSDDPAYFGSYLTEEYEIAAKHAGLTEEELKQLARNALE 308
|
330
....*....|....*.
gi 17538512 368 SCFLPEDEKAELVKRV 383
Cdd:TIGR01430 309 GSFLSDDEKKELLAKL 324
|
|
| PRK09358 |
PRK09358 |
adenosine deaminase; Provisional |
50-385 |
5.31e-74 |
|
adenosine deaminase; Provisional
Pssm-ID: 236480 Cd Length: 340 Bit Score: 233.53 E-value: 5.31e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17538512 50 PKVELHLHLDGAVRFDTLIDLSQQKGIPLAgAKTVEELKKVLVTHEPANLSKVLEAFEIFLPVIRgDLAAIERVAYELCE 129
Cdd:PRK09358 11 PKAELHLHLDGSLRPETILELARRNGIALP-ATDVEELPWVRAAYDFRDLQSFLDKYDAGVAVLQ-TEEDLRRLAFEYLE 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17538512 130 DQHNNGVVYFEGRYSP--HL---LLCNDYPEVTAahvvaavkKGFDRGEKQFGIKARSILCCIRGLDKKFPQLILD-LAT 203
Cdd:PRK09358 89 DAAADGVVYAEIRFDPqlHTergLPLEEVVEAVL--------DGLRAAEAEFGISVRLILCFMRHFGEEAAARELEaLAA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17538512 204 DLKQLGVVAIDVAGSAHGAD-EQYEPevvaAFQEAHKRGIHRTVHAGESGGPKEVIKAIEDMYAERIGHGYRVMRDEEMY 282
Cdd:PRK09358 161 RYRDDGVVGFDLAGDELGFPpSKFAR----AFDRARDAGLRLTAHAGEAGGPESIWEALDELGAERIGHGVRAIEDPALM 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17538512 283 leHFVNSKNVHLEACPYSSVMTGAVPlDWKNHPIARWAKDDVNFSVSRDDPTCFDNSMLSELTLVHKQIGLDVHQLWKAQ 362
Cdd:PRK09358 237 --ARLADRRIPLEVCPTSNVQTGAVP-SLAEHPLKTLLDAGVRVTINTDDPLVFGTTLTEEYEALAEAFGLSDEDLAQLA 313
|
330 340
....*....|....*....|...
gi 17538512 363 LNAARSCFLPEDEKAELVKRVEA 385
Cdd:PRK09358 314 RNALEAAFLSEEEKAALLAEVDA 336
|
|
| A_deaminase |
pfam00962 |
Adenosine deaminase; |
50-385 |
2.59e-73 |
|
Adenosine deaminase;
Pssm-ID: 425964 Cd Length: 330 Bit Score: 231.55 E-value: 2.59e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17538512 50 PKVELHLHLDGAVRFDTLIDLSQQKGIPLAGAKTVEELKKVLVTHEPANLSKVLEAFEIFLPVIRgDLAAIERVAYELCE 129
Cdd:pfam00962 1 PKAELHLHLDGSLRPDTLLELAKRYGIILPADFPEALEPLFRKYKKERDLQDFLDKYDIGVAVLR-SPEDIRRLAFEYAE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17538512 130 DQHNNGVVYFEGRYSPHLLLCNDYPEVTAAHVVAavkKGFDRGEKQFGIKARSILCCIRGLDKKFPQLILDLATDLKQLG 209
Cdd:pfam00962 80 DVAKDGVVYAEVRYDPQSHASRGLSPDTVVDAVL---DAVDAAEREFGITVRLIVCAMRHEHPECSREIAELAPRYRDQG 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17538512 210 VVAIDVAGSAHGADEQYEPEVVAAFQEAHKRGIHRTVHAGESGGPKEVIKAIEDMYAERIGHGYRVMRDEEMYleHFVNS 289
Cdd:pfam00962 157 IVAFGLAGDEKGFPPSLFRDHVEAFARARDAGLHLTVHAGEAGGPQSVWEALDDLGAERIGHGVRSAEDPRLL--DRLAD 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17538512 290 KNVHLEACPYSSVMTGAV-PLDwkNHPIARWAKDDVNFSVSRDDPTCFDNSMLSELTLVHKQIGLDVHQLWKAQLNAARS 368
Cdd:pfam00962 235 RQIPLEICPTSNVQTGAVaSLA--EHPLKTFLRAGVPVSLNTDDPLMFGSDLLDEYQVAKRAPGFDEEELARLAKNAVKG 312
|
330
....*....|....*..
gi 17538512 369 CFLPEDEKAELVKRVEA 385
Cdd:pfam00962 313 SFLPADEKRALLDEVDK 329
|
|
| ADA_AMPD |
cd00443 |
Adenosine/AMP deaminase. Adenosine deaminases (ADAs) are present in pro- and eukaryotic ... |
50-382 |
1.03e-45 |
|
Adenosine/AMP deaminase. Adenosine deaminases (ADAs) are present in pro- and eukaryotic organisms and catalyze the zinc dependent irreversible deamination of adenosine nucleosides to inosine nucleosides and ammonia. The eukaryotic AMP deaminase catalyzes a similar reaction leading to the hydrolytic removal of an amino group at the 6 position of the adenine nucleotide ring, a branch point in the adenylate catabolic pathway.
Pssm-ID: 238250 Cd Length: 305 Bit Score: 159.05 E-value: 1.03e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17538512 50 PKVELHLHLDGAVRFDTLIDLSQQKgiplagaktveelkkvlvthepanlskVLEAFEIFLPVIRgDLAAIERVAYELCE 129
Cdd:cd00443 2 PKVELHAHLSGSISPETLLELIKKE---------------------------FFEKFLLVHNLLQ-KGEALARALKEVIE 53
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17538512 130 DQHNNGVVYFEGRYSPHLLLCND--YPEVTAAHVVaavkKGFDRGEKQF-GIKARSILCCIRGLDKKFPQL----ILDLA 202
Cdd:cd00443 54 EFAEDNVQYLELRTTPRLLETEKglTKEQYWLLVI----EGISEAKQWFpPIKVRLILSVDRRGPYVQNYLvaseILELA 129
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17538512 203 TDLKQlGVVAIDVAGSAHGaDEQYEPEVVAAFQEAHKRG-IHRTVHAGESGGPkEVIKAIEDMYAERIGHGYRVMRDEEm 281
Cdd:cd00443 130 KFLSN-YVVGIDLVGDESK-GENPLRDFYSYYEYARRLGlLGLTLHCGETGNR-EELLQALLLLPDRIGHGIFLLKHPE- 205
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17538512 282 yLEHFVNSKNVHLEACPYSSVMTGAVPlDWKNHPIARWAKDDVNFSVSRDDPTCFDNSMLSELTLVHKQIGLDVHQLWKA 361
Cdd:cd00443 206 -LIYLVKLRNIPIEVCPTSNVVLGTVQ-SYEKHPFMRFFKAGLPVSLSTDDPGIFGTSLSEEYSLAAKTFGLTFEDLCEL 283
|
330 340
....*....|....*....|.
gi 17538512 362 QLNAARSCFLPEDEKAELVKR 382
Cdd:cd00443 284 NRNSVLSSFAKDEEKKSLLEV 304
|
|
| PTZ00124 |
PTZ00124 |
adenosine deaminase; Provisional |
50-381 |
3.35e-21 |
|
adenosine deaminase; Provisional
Pssm-ID: 173415 Cd Length: 362 Bit Score: 93.78 E-value: 3.35e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17538512 50 PKVELHLHLDGAVRFDTLIDLSQQKGIPlAGAKTVEELKKVLVTHEPANLSKVLEAfEIFLPVIRGDLAAIERVAYELCE 129
Cdd:PTZ00124 36 PKCELHCHLDLCFSVDFFLSCIRKYNLQ-PNLSDEEILDYYLFAKGGKSLGEFVEK-AIRVADIFNDYEVIEDLAKHAVF 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17538512 130 DQHNNGVVYFEGRYSPHLLL--CN-DYPEVTAAHVvaavkKGFDRGEKQFGIKARSILCCI--RGLDKKFPQLILDLATD 204
Cdd:PTZ00124 114 NKYKEGVVLMEFRYSPTFVAfkHNlDIDLIHQAIV-----KGIKEAVELLDHKIEVGLLCIgdTGHDAAPIKESADFCLK 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17538512 205 LKQlgvvaiDVAGSAHGADEQYEPEVVAAFQEAHKRGIHRTVHAGESGGP---KEVIKAIEDMYAERIGHGYRVMRDEEM 281
Cdd:PTZ00124 189 HKA------DFVGFDHAGHEVDLKPFKDIFDYVREAGVNLTVHAGEDVTLpnlNTLYSAIQVLKVKRIGHGIRVAESQEL 262
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17538512 282 YleHFVNSKNVHLEACPYSSVMTGAVpLDWKNHPIARWAKDDVNFSVSRDDPTCFDNSMLSELTLVHKQIGLDVHQLWKA 361
Cdd:PTZ00124 263 I--DMVKEKDILLEVCPISNVLLNNA-KSMDTHPIRKLYDAGVKVSVNSDDPGMFLTNINDDYEELYTHLNFTLADFMKM 339
|
330 340
....*....|....*....|
gi 17538512 362 QLNAARSCFLPEDEKAELVK 381
Cdd:PTZ00124 340 NEWALEKSFLDKDIKLKIKK 359
|
|
| metallo-dependent_hydrolases |
cd01292 |
Superfamily of metallo-dependent hydrolases (also called amidohydrolase superfamily) is a ... |
133-367 |
2.25e-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: 60.81 E-value: 2.25e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17538512 133 NNGVVYFEGRYSPHLLlcndypevtaAHVVAAVKKGFDRGEKQFGIKARSILCCIRG---LDKKFPQLILDLATDLKQLG 209
Cdd:cd01292 46 AGGVTTVVDMGSTPPP----------TTTKAAIEAVAEAARASAGIRVVLGLGIPGVpaaVDEDAEALLLELLRRGLELG 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17538512 210 VVAIDVAGsAHGADEQYEPEVVAAFQEAHKRGIHRTVHAGESGGP----KEVIKAIEDMYAERIGHGYRvMRDEEMYL-- 283
Cdd:cd01292 116 AVGLKLAG-PYTATGLSDESLRRVLEEARKLGLPVVIHAGELPDPtralEDLVALLRLGGRVVIGHVSH-LDPELLELlk 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17538512 284 EHfvnskNVHLEACPYSSVMTGAVPLDWknHPIARWAKDDVNFSVSRDDPTCFDNS-MLSELTLVHKQIGLDVHQ---LW 359
Cdd:cd01292 194 EA-----GVSLEVCPLSNYLLGRDGEGA--EALRRLLELGIRVTLGTDGPPHPLGTdLLALLRLLLKVLRLGLSLeeaLR 266
|
....*...
gi 17538512 360 KAQLNAAR 367
Cdd:cd01292 267 LATINPAR 274
|
|
| ADGF |
cd01321 |
Adenosine deaminase-related growth factors (ADGF), a novel family of secreted growth-factors ... |
54-342 |
3.88e-09 |
|
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: 57.67 E-value: 3.88e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17538512 54 LHLHLDGAVRFDTLIDLsqqkgiplagaktveelkkvlvthepanlskVLEAFE-IFLpVIRGDLA---AIERVAYELCE 129
Cdd:cd01321 30 LHVHDTAMVSSDWLIKN-------------------------------ATYRFEqIFD-IIDGLLTylpIFRDYYRRLLE 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17538512 130 DQHNNGVVYFEGRYSPHLLLC-----NDYPEVTAAHVVAAVKkgFDRGEKQFgIKARSILCCIRGLDKKFPQLILDLATD 204
Cdd:cd01321 78 ELYEDNVQYVELRSSFSPLYDldgreYDYEETVQLLEEVVEK--FKKTHPDF-IGLKIIYATLRNFNDSEIKESMEQCLN 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17538512 205 LKQlgvvaidvagsahgadeqYEPEVVAAF----QEAHKRGIHRTV-----------------HAGESGGP-----KEVI 258
Cdd:cd01321 155 LKK------------------KFPDFIAGFdlvgQEDAGRPLLDFLpqllwfpkqcaeipfffHAGETNGDgtetdENLV 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17538512 259 KAIEdMYAERIGHGYRVMRDEemYLEHFVNSKNVHLEACPYSSVMTGAVPlDWKNHPIARWAKDDVNFSVSRDDPTCFDN 338
Cdd:cd01321 217 DALL-LNTKRIGHGFALPKHP--LLMDLVKKKNIAIEVCPISNQVLGLVS-DLRNHPAAALLARGVPVVISSDDPGFWGA 292
|
....
gi 17538512 339 SMLS 342
Cdd:cd01321 293 KGLS 296
|
|
| adm_rel |
TIGR01431 |
adenosine deaminase-related growth factor; Members of this family have been described as ... |
268-376 |
6.17e-05 |
|
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: 44.79 E-value: 6.17e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17538512 268 RIGHGYRVMRDEEmyLEHFVNSKNVHLEACPYSSVMTGAVPlDWKNHPIARWAKDDVNFSVSRDDPTCFDNSMLS-ELTL 346
Cdd:TIGR01431 351 RIGHGFALSKHPA--VRTYSKERDIPIEVCPISNQVLKLVS-DLRNHPVATLMADNYPMVISSDDPAFWGAKGLSyDFYE 427
|
90 100 110
....*....|....*....|....*....|...
gi 17538512 347 VHKQIG---LDVHQLWKAQLNAARSCFLPEDEK 376
Cdd:TIGR01431 428 AFMGIAgmkADLRTLKQLALNSIKYSALSEEEK 460
|
|
| Amidohydro_1 |
pfam01979 |
Amidohydrolase family; This family of enzymes are a a large metal dependent hydrolase ... |
196-275 |
2.34e-03 |
|
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: 39.79 E-value: 2.34e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17538512 196 QLILDLATDLKQLGVVAIDVAGSAHGADEQYEPEVVAAFQEAHKRGIHRTVHAGESggpKEVIKAIEDMYAERIGHGYRV 275
Cdd:pfam01979 95 EKLKAGAEFIKGMADGVVFVGLAPHGAPTFSDDELKAALEEAKKYGLPVAIHALET---KGEVEDAIAAFGGGIEHGTHL 171
|
|
|