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Conserved domains on  [gi|116007828|ref|NP_001036612|]
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adenosine deaminase-related growth factor A2, isoform B [Drosophila melanogaster]

Protein Classification

amidohydrolase family protein; amidohydrolase/deacetylase family metallohydrolase( domain architecture ID 10552997)

metal-dependent amidohydrolase family protein having a conserved metal binding site, usually involving four histidines and one aspartic acid residue| amidohydrolase/deacetylase family metallohydrolase similar to Bradyrhizobium diazoefficiens dihydroorotase which converts carbamoyl aspartic acid into 4,5-dihydroorotic acid in the biosynthesis of pyrimidines

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
ADGF cd01321
Adenosine deaminase-related growth factors (ADGF), a novel family of secreted growth-factors ...
 116-529 3.18e-163

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: 467.13  E-value: 3.18e-163
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116007828 116 PPFLKHLNIID-TNLYAALKSMPKGGLLHVHDSGMLRMEILIDLIYRdnlwvcvnleqdfedfrfsryfphippaedyqc 194
Cdd:cd01321    3 MHFFKAKDLIEnSTLFKIIQKMPKGALLHVHDTAMVSSDWLIKNATY--------------------------------- 49

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116007828 195 nwmlmsnffqlesrlefenrlrktltvrpegykssselarHLRRHQRIIHGLITFRPIWSEFIFTMLSDFYADGVHYVEL 274
Cdd:cd01321   50 ----------------------------------------RFEQIFDIIDGLLTYLPIFRDYYRRLLEELYEDNVQYVEL 89

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116007828 275 RSSLPNMYDLDGNNFTILETAEALVSVSNIFKNSFKDFIGIKLIYAPSRNLNDSRMDEYLENARLLKLHFPNFFAGFDLN 354
Cdd:cd01321   90 RSSFSPLYDLDGREYDYEETVQLLEEVVEKFKKTHPDFIGLKIIYATLRNFNDSEIKESMEQCLNLKKKFPDFIAGFDLV 169

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116007828 355 TFGDEcNLPLLENVTQLLRIGKN---IDFYFHAGESRCpDSSRPDANLLEALLLQSKRIGNAVNLPFHPEIMKVMKRLSI 431
Cdd:cd01321  170 GQEDA-GRPLLDFLPQLLWFPKQcaeIPFFFHAGETNG-DGTETDENLVDALLLNTKRIGHGFALPKHPLLMDLVKKKNI 247

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116007828 432 AVEICPLSNHYLQYFNDFRQHPAAYLIAAGFPIVIGSDYPCFWNSAPLTDDFYVAFVGVISGWGDLRLLKQFALNSFLFS 511
Cdd:cd01321  248 AIEVCPISNQVLGLVSDLRNHPAAALLARGVPVVISSDDPGFWGAKGLSHDFYQAFMGLAPADAGLRGLKQLAENSIRYS 327

                        410
                 ....*....|....*...
gi 116007828 512 SLSETEKNMAVSKWQCSW 529
Cdd:cd01321  328 ALSDQEKDEAVAKWEKKW 345
A_deaminase_N pfam08451
Adenosine/AMP deaminase N-terminal; This domain is found to the N-terminus of the Adenosine ...
 40-133 6.64e-31

Adenosine/AMP deaminase N-terminal; This domain is found to the N-terminus of the Adenosine/AMP deaminase domain (pfam00962) in metazoan proteins such as the Cat eye syndrome critical region protein 1 and its homologs.


:

Pssm-ID: 462481  Cd Length: 95  Bit Score: 115.48  E-value: 6.64e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116007828   40 LVLICSAPLGENMSNLTSEERHARLRQIYIEKERRQRLGSRMGLSPLEEEANDRLMAIRQVDE-EFYNLWRNYHSQPPPF 118
Cdd:pfam08451   1 LLLLALLYLSLLYYSRPTEERYERLRQALLSKEERLRLGGNLELSPLEEKANDILMAIKQVELaEGFRNWENYPPAPHFF 80

                          90
                  ....*....|....*
gi 116007828  119 LKHLNIIDTNLYAAL 133
Cdd:pfam08451  81 LAKDLINESDLFKFL 95
 
Name Accession Description Interval E-value
ADGF cd01321
Adenosine deaminase-related growth factors (ADGF), a novel family of secreted growth-factors ...
 116-529 3.18e-163

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: 467.13  E-value: 3.18e-163
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116007828 116 PPFLKHLNIID-TNLYAALKSMPKGGLLHVHDSGMLRMEILIDLIYRdnlwvcvnleqdfedfrfsryfphippaedyqc 194
Cdd:cd01321    3 MHFFKAKDLIEnSTLFKIIQKMPKGALLHVHDTAMVSSDWLIKNATY--------------------------------- 49

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116007828 195 nwmlmsnffqlesrlefenrlrktltvrpegykssselarHLRRHQRIIHGLITFRPIWSEFIFTMLSDFYADGVHYVEL 274
Cdd:cd01321   50 ----------------------------------------RFEQIFDIIDGLLTYLPIFRDYYRRLLEELYEDNVQYVEL 89

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116007828 275 RSSLPNMYDLDGNNFTILETAEALVSVSNIFKNSFKDFIGIKLIYAPSRNLNDSRMDEYLENARLLKLHFPNFFAGFDLN 354
Cdd:cd01321   90 RSSFSPLYDLDGREYDYEETVQLLEEVVEKFKKTHPDFIGLKIIYATLRNFNDSEIKESMEQCLNLKKKFPDFIAGFDLV 169

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116007828 355 TFGDEcNLPLLENVTQLLRIGKN---IDFYFHAGESRCpDSSRPDANLLEALLLQSKRIGNAVNLPFHPEIMKVMKRLSI 431
Cdd:cd01321  170 GQEDA-GRPLLDFLPQLLWFPKQcaeIPFFFHAGETNG-DGTETDENLVDALLLNTKRIGHGFALPKHPLLMDLVKKKNI 247

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116007828 432 AVEICPLSNHYLQYFNDFRQHPAAYLIAAGFPIVIGSDYPCFWNSAPLTDDFYVAFVGVISGWGDLRLLKQFALNSFLFS 511
Cdd:cd01321  248 AIEVCPISNQVLGLVSDLRNHPAAALLARGVPVVISSDDPGFWGAKGLSHDFYQAFMGLAPADAGLRGLKQLAENSIRYS 327

                        410
                 ....*....|....*...
gi 116007828 512 SLSETEKNMAVSKWQCSW 529
Cdd:cd01321  328 ALSDQEKDEAVAKWEKKW 345
A_deaminase_N pfam08451
Adenosine/AMP deaminase N-terminal; This domain is found to the N-terminus of the Adenosine ...
 40-133 6.64e-31

Adenosine/AMP deaminase N-terminal; This domain is found to the N-terminus of the Adenosine/AMP deaminase domain (pfam00962) in metazoan proteins such as the Cat eye syndrome critical region protein 1 and its homologs.


Pssm-ID: 462481  Cd Length: 95  Bit Score: 115.48  E-value: 6.64e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116007828   40 LVLICSAPLGENMSNLTSEERHARLRQIYIEKERRQRLGSRMGLSPLEEEANDRLMAIRQVDE-EFYNLWRNYHSQPPPF 118
Cdd:pfam08451   1 LLLLALLYLSLLYYSRPTEERYERLRQALLSKEERLRLGGNLELSPLEEKANDILMAIKQVELaEGFRNWENYPPAPHFF 80

                          90
                  ....*....|....*
gi 116007828  119 LKHLNIIDTNLYAAL 133
Cdd:pfam08451  81 LAKDLINESDLFKFL 95
Add COG1816
Adenosine deaminase [Nucleotide transport and metabolism]; Adenosine deaminase is part of the ...
 266-518 1.55e-20

Adenosine deaminase [Nucleotide transport and metabolism]; Adenosine deaminase is part of the Pathway/BioSystem: Menaquinone biosynthesis


Pssm-ID: 441421  Cd Length: 326  Bit Score: 92.45  E-value: 1.55e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116007828 266 ADGVHYVELRSSlPNMYDLDGnnftiLETAEALVSVSNIFKNSFKDF-IGIKLIYAPSRNLNDSRMdeyLENARLLKLHF 344
Cdd:COG1816   79 ADGVRYAEIRFD-PQLHTRRG-----LSLEEVVEAVLDGLREAEREFgISVRLILCALRHLSPEAA---FETLELALRYR 149

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116007828 345 PNFFAGFDLNtfGDECNLPLlENVTQLLRIGKNIDFYF--HAGESRCPDSSRpdanllEAL-LLQSKRIGNAVNLPFHPE 421
Cdd:COG1816  150 DRGVVGFGLA--GDERGFPP-EKFAEAFARAREAGLHLtaHAGEAGGPESIW------EALdLLGAERIGHGVRAIEDPA 220

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116007828 422 IMKVMKRLSIAVEICPLSNHYLQYFNDFRQHPAAYLIAAGFPIVIGSDYPCFWNSaPLTDDFYVAFvgVISGWgDLRLLK 501
Cdd:COG1816  221 LVARLADRGIPLEVCPTSNVQLGVVPSLAEHPLRRLLDAGVRVTLNTDDPLYFGT-TLTDEYELAA--EAFGL-SDADLA 296

                        250
                 ....*....|....*..
gi 116007828 502 QFALNSFLFSSLSETEK 518
Cdd:COG1816  297 QLARNAIEASFLPEEEK 313
PRK09358 PRK09358
adenosine deaminase; Provisional
 257-518 8.16e-20

adenosine deaminase; Provisional


Pssm-ID: 236480  Cd Length: 340  Bit Score: 90.62  E-value: 8.16e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116007828 257 IFTMLSDFYADGVHYVELRSSlPNMYDLDGNNF-TILETA-EALVSVSNIFKnsfkdfIGIKLIYAPSRNLNDSRMDEYL 334
Cdd:PRK09358  83 AFEYLEDAAADGVVYAEIRFD-PQLHTERGLPLeEVVEAVlDGLRAAEAEFG------ISVRLILCFMRHFGEEAAAREL 155

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116007828 335 EnaRLLKLHFPNFFAGFDLNtfGDECNLP--LLENVTQLLRIgKNIDFYFHAGESRCPDSSRpdanllEAL-LLQSKRIG 411
Cdd:PRK09358 156 E--ALAARYRDDGVVGFDLA--GDELGFPpsKFARAFDRARD-AGLRLTAHAGEAGGPESIW------EALdELGAERIG 224

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116007828 412 NAVNLPFHPEIMKVMKRLSIAVEICPLSNHYLQYFNDFRQHPAAYLIAAGFPIVIGSDYPCFWNSApLTDDFYVAFVGVI 491
Cdd:PRK09358 225 HGVRAIEDPALMARLADRRIPLEVCPTSNVQTGAVPSLAEHPLKTLLDAGVRVTINTDDPLVFGTT-LTEEYEALAEAFG 303

                        250       260
                 ....*....|....*....|....*..
gi 116007828 492 SGWGDLRllkQFALNSFLFSSLSETEK 518
Cdd:PRK09358 304 LSDEDLA---QLARNALEAAFLSEEEK 327
A_deaminase pfam00962
Adenosine deaminase;
263-519 2.62e-16

Adenosine deaminase;


Pssm-ID: 425964  Cd Length: 330  Bit Score: 80.17  E-value: 2.62e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116007828  263 DFYADGVHYVELRSSlPNMYDLDGnnftiLETAEALVSVSNIFKNSFKDF-IGIKLIYAPSRN--LNDSRmdeylENARL 339
Cdd:pfam00962  80 DVAKDGVVYAEVRYD-PQSHASRG-----LSPDTVVDAVLDAVDAAEREFgITVRLIVCAMRHehPECSR-----EIAEL 148

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116007828  340 LKLHFPNFFAGFDLNtfGDECNLP--LLENVTQLLRIGKNIDFYF--HAGESRCPDSSRpdanllEAL-LLQSKRIGNAV 414
Cdd:pfam00962 149 APRYRDQGIVAFGLA--GDEKGFPpsLFRDHVEAFARARDAGLHLtvHAGEAGGPQSVW------EALdDLGAERIGHGV 220

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116007828  415 NLPFHPEIMKVMKRLSIAVEICPLSNHYLQYFNDFRQHPAAYLIAAGFPIVIGSDYPCFWNSApLTDDFYVAfvGVISGW 494
Cdd:pfam00962 221 RSAEDPRLLDRLADRQIPLEICPTSNVQTGAVASLAEHPLKTFLRAGVPVSLNTDDPLMFGSD-LLDEYQVA--KRAPGF 297

                         250       260
                  ....*....|....*....|....*
gi 116007828  495 GDlRLLKQFALNSFLFSSLSETEKN 519
Cdd:pfam00962 298 DE-EELARLAKNAVKGSFLPADEKR 321
aden_deam TIGR01430
adenosine deaminase; This family includes the experimentally verified adenosine deaminases of ...
 224-519 1.29e-14

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: 75.09  E-value: 1.29e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116007828  224 EGYKSSSELARHLRRHQRIIHGLIT---FRPIWSEFiftmLSDFYADGVHYVELRSSlPNMYDLDGnnftiLETAEALVS 300
Cdd:TIGR01430  42 EAYDKFRDLQDFLAKYDFGVEVLRTeddFKRLAYEY----VEKAAKDGVVYAEVFFD-PQLHTNRG-----ISPDTVVEA 111

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116007828  301 VSNIFKNSFKDF-IGIKLIYAPSRNLNDSRMDEYLENARLLKLHFpnfFAGFDLNtfGDECNLPLLENVtQLLRIGKNID 379
Cdd:TIGR01430 112 VLDGLDEAERDFgIKSRLILCGMRHKQPEAAEETLELAKPYKEQT---IVGFGLA--GDERGGPPPDFV-RAFAIARELG 185

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116007828  380 FYF--HAGESRCPDSSRPDANLLEAlllqsKRIGNAVNLPFHPEIMKVMKRLSIAVEICPLSNHYLQYFNDFRQHPAAYL 457
Cdd:TIGR01430 186 LHLtvHAGELGGPESVREALDDLGA-----TRIGHGVRALEDPELLKRLAQENITLEVCPTSNVALGVVKSLAEHPLRRF 260

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 116007828  458 IAAGFPIVIGSDYPC-FWNSapLTDDFYVAFVGVisGWGDlRLLKQFALNSFLFSSLSETEKN 519
Cdd:TIGR01430 261 LEAGVKVTLNSDDPAyFGSY--LTEEYEIAAKHA--GLTE-EELKQLARNALEGSFLSDDEKK 318
 
Name Accession Description Interval E-value
ADGF cd01321
Adenosine deaminase-related growth factors (ADGF), a novel family of secreted growth-factors ...
 116-529 3.18e-163

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: 467.13  E-value: 3.18e-163
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116007828 116 PPFLKHLNIID-TNLYAALKSMPKGGLLHVHDSGMLRMEILIDLIYRdnlwvcvnleqdfedfrfsryfphippaedyqc 194
Cdd:cd01321    3 MHFFKAKDLIEnSTLFKIIQKMPKGALLHVHDTAMVSSDWLIKNATY--------------------------------- 49

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116007828 195 nwmlmsnffqlesrlefenrlrktltvrpegykssselarHLRRHQRIIHGLITFRPIWSEFIFTMLSDFYADGVHYVEL 274
Cdd:cd01321   50 ----------------------------------------RFEQIFDIIDGLLTYLPIFRDYYRRLLEELYEDNVQYVEL 89

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116007828 275 RSSLPNMYDLDGNNFTILETAEALVSVSNIFKNSFKDFIGIKLIYAPSRNLNDSRMDEYLENARLLKLHFPNFFAGFDLN 354
Cdd:cd01321   90 RSSFSPLYDLDGREYDYEETVQLLEEVVEKFKKTHPDFIGLKIIYATLRNFNDSEIKESMEQCLNLKKKFPDFIAGFDLV 169

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116007828 355 TFGDEcNLPLLENVTQLLRIGKN---IDFYFHAGESRCpDSSRPDANLLEALLLQSKRIGNAVNLPFHPEIMKVMKRLSI 431
Cdd:cd01321  170 GQEDA-GRPLLDFLPQLLWFPKQcaeIPFFFHAGETNG-DGTETDENLVDALLLNTKRIGHGFALPKHPLLMDLVKKKNI 247

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116007828 432 AVEICPLSNHYLQYFNDFRQHPAAYLIAAGFPIVIGSDYPCFWNSAPLTDDFYVAFVGVISGWGDLRLLKQFALNSFLFS 511
Cdd:cd01321  248 AIEVCPISNQVLGLVSDLRNHPAAALLARGVPVVISSDDPGFWGAKGLSHDFYQAFMGLAPADAGLRGLKQLAENSIRYS 327

                        410
                 ....*....|....*...
gi 116007828 512 SLSETEKNMAVSKWQCSW 529
Cdd:cd01321  328 ALSDQEKDEAVAKWEKKW 345
A_deaminase_N pfam08451
Adenosine/AMP deaminase N-terminal; This domain is found to the N-terminus of the Adenosine ...
 40-133 6.64e-31

Adenosine/AMP deaminase N-terminal; This domain is found to the N-terminus of the Adenosine/AMP deaminase domain (pfam00962) in metazoan proteins such as the Cat eye syndrome critical region protein 1 and its homologs.


Pssm-ID: 462481  Cd Length: 95  Bit Score: 115.48  E-value: 6.64e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116007828   40 LVLICSAPLGENMSNLTSEERHARLRQIYIEKERRQRLGSRMGLSPLEEEANDRLMAIRQVDE-EFYNLWRNYHSQPPPF 118
Cdd:pfam08451   1 LLLLALLYLSLLYYSRPTEERYERLRQALLSKEERLRLGGNLELSPLEEKANDILMAIKQVELaEGFRNWENYPPAPHFF 80

                          90
                  ....*....|....*
gi 116007828  119 LKHLNIIDTNLYAAL 133
Cdd:pfam08451  81 LAKDLINESDLFKFL 95
ADA_AMPD cd00443
Adenosine/AMP deaminase. Adenosine deaminases (ADAs) are present in pro- and eukaryotic ...
 243-525 2.88e-30

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: 120.14  E-value: 2.88e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116007828 243 IHGLITFRPIWSEFIFTMLSDFYADGVHYVELRSSLPNMYDLDGnnftiLETAEALVSVSNIFKNSFKDF--IGIKLIYA 320
Cdd:cd00443   34 VHNLLQKGEALARALKEVIEEFAEDNVQYLELRTTPRLLETEKG-----LTKEQYWLLVIEGISEAKQWFppIKVRLILS 108

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116007828 321 PSRNLNdsRMDEYLENARLLKLH--FPNFFAGFDLNtfGDE-CNLPLLENVTQLL---RIGKNIDFYFHAGESRCPDSsr 394
Cdd:cd00443  109 VDRRGP--YVQNYLVASEILELAkfLSNYVVGIDLV--GDEsKGENPLRDFYSYYeyaRRLGLLGLTLHCGETGNREE-- 182

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116007828 395 pdanLLEALLLQSKRIGNAVNLPFHPEIMKVMKRLSIAVEICPLSNHYLQYFNDFRQHPAAYLIAAGFPIVIGSDYPCFW 474
Cdd:cd00443  183 ----LLQALLLLPDRIGHGIFLLKHPELIYLVKLRNIPIEVCPTSNVVLGTVQSYEKHPFMRFFKAGLPVSLSTDDPGIF 258

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|.
gi 116007828 475 NSaPLTDDFYVAFVGVISGWGDlrlLKQFALNSFLFSSLSETEKNMAVSKW 525
Cdd:cd00443  259 GT-SLSEEYSLAAKTFGLTFED---LCELNRNSVLSSFAKDEEKKSLLEVL 305
ADA cd01320
Adenosine deaminase (ADA) is a monomeric zinc dependent enzyme which catalyzes the ...
 258-519 8.14e-22

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: 96.50  E-value: 8.14e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116007828 258 FTMLSDFYADGVHYVELRSSlPNMYDLDGnnftiLETAEALVSVSNIFKNSFKDF-IGIKLIYAPSRNLNDSRMdeyLEN 336
Cdd:cd01320   76 YEYLEDAAADGVVYAEIRFS-PQLHTRRG-----LSFDEVVEAVLRGLDEAEAEFgIKARLILCGLRHLSPESA---QET 146

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116007828 337 ARLLKLHFPNFFAGFDLNtfGDECNLP--LLENVTQLLRIgKNIDFYFHAGESRCPDSSRpdanllEAL-LLQSKRIGNA 413
Cdd:cd01320  147 LELALKYRDKGVVGFDLA--GDEVGFPpeKFVRAFQRARE-AGLRLTAHAGEAGGPESVR------DALdLLGAERIGHG 217

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116007828 414 VNLPFHPEIMKVMKRLSIAVEICPLSNHYLQYFNDFRQHPAAYLIAAGFPIVIGSDYP-CFWNSapLTDDFYVAfvgviS 492
Cdd:cd01320  218 IRAIEDPELVKRLAERNIPLEVCPTSNVQTGAVKSLAEHPLRELLDAGVKVTINTDDPtVFGTY--LTDEYELL-----A 290

                        250       260
                 ....*....|....*....|....*....
gi 116007828 493 GWGDLRL--LKQFALNSFLFSSLSETEKN 519
Cdd:cd01320  291 EAFGLTEeeLKKLARNAVEASFLSEEEKA 319
Add COG1816
Adenosine deaminase [Nucleotide transport and metabolism]; Adenosine deaminase is part of the ...
 266-518 1.55e-20

Adenosine deaminase [Nucleotide transport and metabolism]; Adenosine deaminase is part of the Pathway/BioSystem: Menaquinone biosynthesis


Pssm-ID: 441421  Cd Length: 326  Bit Score: 92.45  E-value: 1.55e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116007828 266 ADGVHYVELRSSlPNMYDLDGnnftiLETAEALVSVSNIFKNSFKDF-IGIKLIYAPSRNLNDSRMdeyLENARLLKLHF 344
Cdd:COG1816   79 ADGVRYAEIRFD-PQLHTRRG-----LSLEEVVEAVLDGLREAEREFgISVRLILCALRHLSPEAA---FETLELALRYR 149

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116007828 345 PNFFAGFDLNtfGDECNLPLlENVTQLLRIGKNIDFYF--HAGESRCPDSSRpdanllEAL-LLQSKRIGNAVNLPFHPE 421
Cdd:COG1816  150 DRGVVGFGLA--GDERGFPP-EKFAEAFARAREAGLHLtaHAGEAGGPESIW------EALdLLGAERIGHGVRAIEDPA 220

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116007828 422 IMKVMKRLSIAVEICPLSNHYLQYFNDFRQHPAAYLIAAGFPIVIGSDYPCFWNSaPLTDDFYVAFvgVISGWgDLRLLK 501
Cdd:COG1816  221 LVARLADRGIPLEVCPTSNVQLGVVPSLAEHPLRRLLDAGVRVTLNTDDPLYFGT-TLTDEYELAA--EAFGL-SDADLA 296

                        250
                 ....*....|....*..
gi 116007828 502 QFALNSFLFSSLSETEK 518
Cdd:COG1816  297 QLARNAIEASFLPEEEK 313
PRK09358 PRK09358
adenosine deaminase; Provisional
 257-518 8.16e-20

adenosine deaminase; Provisional


Pssm-ID: 236480  Cd Length: 340  Bit Score: 90.62  E-value: 8.16e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116007828 257 IFTMLSDFYADGVHYVELRSSlPNMYDLDGNNF-TILETA-EALVSVSNIFKnsfkdfIGIKLIYAPSRNLNDSRMDEYL 334
Cdd:PRK09358  83 AFEYLEDAAADGVVYAEIRFD-PQLHTERGLPLeEVVEAVlDGLRAAEAEFG------ISVRLILCFMRHFGEEAAAREL 155

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116007828 335 EnaRLLKLHFPNFFAGFDLNtfGDECNLP--LLENVTQLLRIgKNIDFYFHAGESRCPDSSRpdanllEAL-LLQSKRIG 411
Cdd:PRK09358 156 E--ALAARYRDDGVVGFDLA--GDELGFPpsKFARAFDRARD-AGLRLTAHAGEAGGPESIW------EALdELGAERIG 224

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116007828 412 NAVNLPFHPEIMKVMKRLSIAVEICPLSNHYLQYFNDFRQHPAAYLIAAGFPIVIGSDYPCFWNSApLTDDFYVAFVGVI 491
Cdd:PRK09358 225 HGVRAIEDPALMARLADRRIPLEVCPTSNVQTGAVPSLAEHPLKTLLDAGVRVTINTDDPLVFGTT-LTEEYEALAEAFG 303

                        250       260
                 ....*....|....*....|....*..
gi 116007828 492 SGWGDLRllkQFALNSFLFSSLSETEK 518
Cdd:PRK09358 304 LSDEDLA---QLARNALEAAFLSEEEK 327
A_deaminase pfam00962
Adenosine deaminase;
263-519 2.62e-16

Adenosine deaminase;


Pssm-ID: 425964  Cd Length: 330  Bit Score: 80.17  E-value: 2.62e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116007828  263 DFYADGVHYVELRSSlPNMYDLDGnnftiLETAEALVSVSNIFKNSFKDF-IGIKLIYAPSRN--LNDSRmdeylENARL 339
Cdd:pfam00962  80 DVAKDGVVYAEVRYD-PQSHASRG-----LSPDTVVDAVLDAVDAAEREFgITVRLIVCAMRHehPECSR-----EIAEL 148

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116007828  340 LKLHFPNFFAGFDLNtfGDECNLP--LLENVTQLLRIGKNIDFYF--HAGESRCPDSSRpdanllEAL-LLQSKRIGNAV 414
Cdd:pfam00962 149 APRYRDQGIVAFGLA--GDEKGFPpsLFRDHVEAFARARDAGLHLtvHAGEAGGPQSVW------EALdDLGAERIGHGV 220

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116007828  415 NLPFHPEIMKVMKRLSIAVEICPLSNHYLQYFNDFRQHPAAYLIAAGFPIVIGSDYPCFWNSApLTDDFYVAfvGVISGW 494
Cdd:pfam00962 221 RSAEDPRLLDRLADRQIPLEICPTSNVQTGAVASLAEHPLKTFLRAGVPVSLNTDDPLMFGSD-LLDEYQVA--KRAPGF 297

                         250       260
                  ....*....|....*....|....*
gi 116007828  495 GDlRLLKQFALNSFLFSSLSETEKN 519
Cdd:pfam00962 298 DE-EELARLAKNAVKGSFLPADEKR 321
aden_deam TIGR01430
adenosine deaminase; This family includes the experimentally verified adenosine deaminases of ...
 224-519 1.29e-14

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: 75.09  E-value: 1.29e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116007828  224 EGYKSSSELARHLRRHQRIIHGLIT---FRPIWSEFiftmLSDFYADGVHYVELRSSlPNMYDLDGnnftiLETAEALVS 300
Cdd:TIGR01430  42 EAYDKFRDLQDFLAKYDFGVEVLRTeddFKRLAYEY----VEKAAKDGVVYAEVFFD-PQLHTNRG-----ISPDTVVEA 111

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116007828  301 VSNIFKNSFKDF-IGIKLIYAPSRNLNDSRMDEYLENARLLKLHFpnfFAGFDLNtfGDECNLPLLENVtQLLRIGKNID 379
Cdd:TIGR01430 112 VLDGLDEAERDFgIKSRLILCGMRHKQPEAAEETLELAKPYKEQT---IVGFGLA--GDERGGPPPDFV-RAFAIARELG 185

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116007828  380 FYF--HAGESRCPDSSRPDANLLEAlllqsKRIGNAVNLPFHPEIMKVMKRLSIAVEICPLSNHYLQYFNDFRQHPAAYL 457
Cdd:TIGR01430 186 LHLtvHAGELGGPESVREALDDLGA-----TRIGHGVRALEDPELLKRLAQENITLEVCPTSNVALGVVKSLAEHPLRRF 260

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 116007828  458 IAAGFPIVIGSDYPC-FWNSapLTDDFYVAFVGVisGWGDlRLLKQFALNSFLFSSLSETEKN 519
Cdd:TIGR01430 261 LEAGVKVTLNSDDPAyFGSY--LTEEYEIAAKHA--GLTE-EELKQLARNALEGSFLSDDEKK 318
PTZ00124 PTZ00124
adenosine deaminase; Provisional
 265-520 2.89e-12

adenosine deaminase; Provisional


Pssm-ID: 173415  Cd Length: 362  Bit Score: 68.35  E-value: 2.89e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116007828 265 YADGVHYVELRSSlPNmYDLDGNNFTILETAEALVSVSNIFKNSFKDFIGIKLIYAPSRNLNDSRMDEYLEnarlLKLHF 344
Cdd:PTZ00124 116 YKEGVVLMEFRYS-PT-FVAFKHNLDIDLIHQAIVKGIKEAVELLDHKIEVGLLCIGDTGHDAAPIKESAD----FCLKH 189

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116007828 345 PNFFAGFDlnTFGDECNLPLLENVTQLLRIGkNIDFYFHAGEsrcpDSSRPDANLL--EALLLQSKRIGNAVNLPFHPEI 422
Cdd:PTZ00124 190 KADFVGFD--HAGHEVDLKPFKDIFDYVREA-GVNLTVHAGE----DVTLPNLNTLysAIQVLKVKRIGHGIRVAESQEL 262

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116007828 423 MKVMKRLSIAVEICPLSNHYLQYFNDFRQHPAAYLIAAGFPIVIGSDYP-CFWNSapLTDDFYVAFVGVISGWGDLRLLK 501
Cdd:PTZ00124 263 IDMVKEKDILLEVCPISNVLLNNAKSMDTHPIRKLYDAGVKVSVNSDDPgMFLTN--INDDYEELYTHLNFTLADFMKMN 340

                        250       260
                 ....*....|....*....|
gi 116007828 502 QFAL-NSFLFSSLSETEKNM 520
Cdd:PTZ00124 341 EWALeKSFLDKDIKLKIKKL 360
metallo-dependent_hydrolases cd01292
Superfamily of metallo-dependent hydrolases (also called amidohydrolase superfamily) is a ...
 261-507 1.35e-11

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: 65.05  E-value: 1.35e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116007828 261 LSDFYADGVHYVELRSSLPNMYDLDGNNFTILETAEALvsvsnifknsfkDFIGIKLIYAPSRNLNDSRMDEYLENARLL 340
Cdd:cd01292   41 LEALLAGGVTTVVDMGSTPPPTTTKAAIEAVAEAARAS------------AGIRVVLGLGIPGVPAAVDEDAEALLLELL 108

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116007828 341 KLHFPNFFAGFDLNTFG--DECNLPLLENVTQLLR-IGKNIDFyfHAGESrcPDSSRPDANLLEALLLQSK-RIGNAVNL 416
Cdd:cd01292  109 RRGLELGAVGLKLAGPYtaTGLSDESLRRVLEEARkLGLPVVI--HAGEL--PDPTRALEDLVALLRLGGRvVIGHVSHL 184

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116007828 417 PfhPEIMKVMKRLSIAVEICPLSNHYLQYFNDFRqHPAAYLIAAGFPIVIGSDYPCFWNSAPLTDDFYVAFVGVISGWGD 496
Cdd:cd01292  185 D--PELLELLKEAGVSLEVCPLSNYLLGRDGEGA-EALRRLLELGIRVTLGTDGPPHPLGTDLLALLRLLLKVLRLGLSL 261

                        250
                 ....*....|.
gi 116007828 497 LRLLKQFALNS 507
Cdd:cd01292  262 EEALRLATINP 272
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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