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Conserved domains on  [gi|532691757|ref|NP_001269155|]
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adenosine deaminase 2 isoform a precursor [Homo sapiens]

Protein Classification

adm_rel family protein( domain architecture ID 11492499)

adm_rel family protein

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
adm_rel TIGR01431
adenosine deaminase-related growth factor; Members of this family have been described as ...
 30-509 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: 856.79  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532691757   30 IDETRAHLLLKEKMMRLGGRLVLNTKEELANERLMTLKIAEMKEAMRT-LIFPPSMHFFQAKHLIERSQVFNILRMMPKG 108
Cdd:TIGR01431   1 YDETRNHLILKEKSMRLGGKLVLTTKEKLANERIMTLKIAEMKEAMRTpLIFPPSMHFFQAKHLIERSQVFKILRMMPKG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532691757  109 AALHLHDIGIVTMDWLVRNVTYRPHCHICFTPRGIMQFRFAHPTPRPSEKCSKWILLEDYRKrVQNVTEFDDSLLRNFTL 188
Cdd:TIGR01431  81 AALHLHDLGIVSMDWLVRNVTYRPNLHICFTKRNIMVLRFRHPTPRPSECCSKWILLEDYRK-SQNVEEFDDSLLRNFTL 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532691757  189 VTQHPEVIYTNQNVVWSKFETIFFTISGLIHYAPVFRDYVFRSMQEFYEDNVLYMEIRARLLPVYELSGEHHDEEWSVKT 268
Cdd:TIGR01431 160 VTTHPEVDYTTQNVVWSRFETIFFTLSGLLHYAPVFRDYYFRALEEFYEDNVQYMELRSRLFPLYELSGTHHDEEWSVKT 239

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532691757  269 YQEVAQKFVETHPEFIGIKIIYSDHRSKDVAVIAESIRMAMGLRIKFPTVVAGFDLVGHEDTGHSLHDYKEALMIPAkDG 348
Cdd:TIGR01431 240 YKEVTEKFVEEHPDFIGIKIIYSDLRSKDVEEIAEYIKMAMGLRIKYPDFVAGFDLVGQEDTGHSLLDYKDALLIPS-IG 318

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532691757  349 VKLPYFFHAGETDWQGTSIDRNILDALMLNTTRIGHGFALSKHPAVRTYSWKKDIPIEVCPISNQVLKLVSDLRNHPVAT 428
Cdd:TIGR01431 319 VKLPYFFHAGETNWQGTSVDRNLLDALLLNTTRIGHGFALSKHPAVRTYSKERDIPIEVCPISNQVLKLVSDLRNHPVAT 398

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532691757  429 LMATGHPMVISSDDPAMFGAKGLSYDFYEVFMGIGGMKADLRTLKQLAMNSIKYSTLLESEKNTFMEIWKKRWDKFIADV 508
Cdd:TIGR01431 399 LMADNYPMVISSDDPAFWGAKGLSYDFYEAFMGIAGMKADLRTLKQLALNSIKYSALSEEEKNTAMAKWKKQWDKFIDDV 478


                  .
gi 532691757  509 A 509
Cdd:TIGR01431 479 L 479
 
Name Accession Description Interval E-value
adm_rel TIGR01431
adenosine deaminase-related growth factor; Members of this family have been described as ...
 30-509 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: 856.79  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532691757   30 IDETRAHLLLKEKMMRLGGRLVLNTKEELANERLMTLKIAEMKEAMRT-LIFPPSMHFFQAKHLIERSQVFNILRMMPKG 108
Cdd:TIGR01431   1 YDETRNHLILKEKSMRLGGKLVLTTKEKLANERIMTLKIAEMKEAMRTpLIFPPSMHFFQAKHLIERSQVFKILRMMPKG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532691757  109 AALHLHDIGIVTMDWLVRNVTYRPHCHICFTPRGIMQFRFAHPTPRPSEKCSKWILLEDYRKrVQNVTEFDDSLLRNFTL 188
Cdd:TIGR01431  81 AALHLHDLGIVSMDWLVRNVTYRPNLHICFTKRNIMVLRFRHPTPRPSECCSKWILLEDYRK-SQNVEEFDDSLLRNFTL 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532691757  189 VTQHPEVIYTNQNVVWSKFETIFFTISGLIHYAPVFRDYVFRSMQEFYEDNVLYMEIRARLLPVYELSGEHHDEEWSVKT 268
Cdd:TIGR01431 160 VTTHPEVDYTTQNVVWSRFETIFFTLSGLLHYAPVFRDYYFRALEEFYEDNVQYMELRSRLFPLYELSGTHHDEEWSVKT 239

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532691757  269 YQEVAQKFVETHPEFIGIKIIYSDHRSKDVAVIAESIRMAMGLRIKFPTVVAGFDLVGHEDTGHSLHDYKEALMIPAkDG 348
Cdd:TIGR01431 240 YKEVTEKFVEEHPDFIGIKIIYSDLRSKDVEEIAEYIKMAMGLRIKYPDFVAGFDLVGQEDTGHSLLDYKDALLIPS-IG 318

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532691757  349 VKLPYFFHAGETDWQGTSIDRNILDALMLNTTRIGHGFALSKHPAVRTYSWKKDIPIEVCPISNQVLKLVSDLRNHPVAT 428
Cdd:TIGR01431 319 VKLPYFFHAGETNWQGTSVDRNLLDALLLNTTRIGHGFALSKHPAVRTYSKERDIPIEVCPISNQVLKLVSDLRNHPVAT 398

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532691757  429 LMATGHPMVISSDDPAMFGAKGLSYDFYEVFMGIGGMKADLRTLKQLAMNSIKYSTLLESEKNTFMEIWKKRWDKFIADV 508
Cdd:TIGR01431 399 LMADNYPMVISSDDPAFWGAKGLSYDFYEAFMGIAGMKADLRTLKQLALNSIKYSALSEEEKNTAMAKWKKQWDKFIDDV 478


                  .
gi 532691757  509 A 509
Cdd:TIGR01431 479 L 479
ADGF cd01321
Adenosine deaminase-related growth factors (ADGF), a novel family of secreted growth-factors ...
 82-501 0e+00

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: 563.05  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532691757  82 PSMHFFQAKHLIERSQVFNILRMMPKGAALHLHDIGIVTMDWLVRNVTYRphchicftprgimqfrfahptprpsekcsk 161
Cdd:cd01321    1 PGMHFFKAKDLIENSTLFKIIQKMPKGALLHVHDTAMVSSDWLIKNATYR------------------------------ 50

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532691757 162 willedyrkrvqnvtefddsllrnftlvtqhpeviytnqnvvwskFETIFFTISGLIHYAPVFRDYVFRSMQEFYEDNVL 241
Cdd:cd01321   51 ---------------------------------------------FEQIFDIIDGLLTYLPIFRDYYRRLLEELYEDNVQ 85

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532691757 242 YMEIRARLLPVYELSGEHHDEEWSVKTYQEVAQKFVETHPEFIGIKIIYSDHRSKDVAVIAESIRMAMGLRIKFPTVVAG 321
Cdd:cd01321   86 YVELRSSFSPLYDLDGREYDYEETVQLLEEVVEKFKKTHPDFIGLKIIYATLRNFNDSEIKESMEQCLNLKKKFPDFIAG 165

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532691757 322 FDLVGHEDTGHSLHDYKEALMIPAKDGVKLPYFFHAGETDWQGTSIDRNILDALMLNTTRIGHGFALSKHPAVRTYSWKK 401
Cdd:cd01321  166 FDLVGQEDAGRPLLDFLPQLLWFPKQCAEIPFFFHAGETNGDGTETDENLVDALLLNTKRIGHGFALPKHPLLMDLVKKK 245

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532691757 402 DIPIEVCPISNQVLKLVSDLRNHPVATLMATGHPMVISSDDPAMFGAKGLSYDFYEVFMGIGGMKADLRTLKQLAMNSIK 481
Cdd:cd01321  246 NIAIEVCPISNQVLGLVSDLRNHPAAALLARGVPVVISSDDPGFWGAKGLSHDFYQAFMGLAPADAGLRGLKQLAENSIR 325

                        410       420
                 ....*....|....*....|
gi 532691757 482 YSTLLESEKNTFMEIWKKRW 501
Cdd:cd01321  326 YSALSDQEKDEAVAKWEKKW 345
Add COG1816
Adenosine deaminase [Nucleotide transport and metabolism]; Adenosine deaminase is part of the ...
 228-506 3.45e-31

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


Pssm-ID: 441421  Cd Length: 326  Bit Score: 122.89  E-value: 3.45e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532691757 228 VFRSMQEFY-----------EDNVLYMEIRarLLPVYelsgeHHDEEWSVKTYQE-VAQKFVETHPEF-IGIKIIYSDHR 294
Cdd:COG1816   59 VLQTEEDFRrlayeyledaaADGVRYAEIR--FDPQL-----HTRRGLSLEEVVEaVLDGLREAEREFgISVRLILCALR 131

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532691757 295 SKDVAVIAESIRMAMGLRIKFptvVAGFDLVGHEDtGHSLHDYKEALMIPAKDGVKLpyFFHAGETD-WQgtsidrNILD 373
Cdd:COG1816  132 HLSPEAAFETLELALRYRDRG---VVGFGLAGDER-GFPPEKFAEAFARAREAGLHL--TAHAGEAGgPE------SIWE 199

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532691757 374 AL-MLNTTRIGHGFALSKHPAVRTYSWKKDIPIEVCPISNQVLKLVSDLRNHPVATLMATGHPMVISSDDPAMFGAkGLS 452
Cdd:COG1816  200 ALdLLGAERIGHGVRAIEDPALVARLADRGIPLEVCPTSNVQLGVVPSLAEHPLRRLLDAGVRVTLNTDDPLYFGT-TLT 278

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....
gi 532691757 453 YDfYEVFMGIGGMkaDLRTLKQLAMNSIKYSTLLESEKntfmEIWKKRWDKFIA 506
Cdd:COG1816  279 DE-YELAAEAFGL--SDADLAQLARNAIEASFLPEEEK----AALLAELDAYFA 325
PRK09358 PRK09358
adenosine deaminase; Provisional
 224-490 1.79e-27

adenosine deaminase; Provisional


Pssm-ID: 236480  Cd Length: 340  Bit Score: 112.96  E-value: 1.79e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532691757 224 FRDYVFRSMQEFYEDNVLYMEIR-------ARLLPVYELsgehhdeewsVKTYQEVAQKFVETHPefIGIKIIYSDHRSK 296
Cdd:PRK09358  79 LRRLAFEYLEDAAADGVVYAEIRfdpqlhtERGLPLEEV----------VEAVLDGLRAAEAEFG--ISVRLILCFMRHF 146

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532691757 297 DVAVIAESIrmAMGLRIKFPTVVAGFDLVGHEDtGHSLHDYKEALMIpAKD-GvkLPYFFHAGETDwqGTSidrNILDAL 375
Cdd:PRK09358 147 GEEAAAREL--EALAARYRDDGVVGFDLAGDEL-GFPPSKFARAFDR-ARDaG--LRLTAHAGEAG--GPE---SIWEAL 215

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532691757 376 -MLNTTRIGHGFALSKHPAVRTYSWKKDIPIEVCPISNQVLKLVSDLRNHPVATLMATGHPMVISSDDPAMFGaKGLSyD 454
Cdd:PRK09358 216 dELGAERIGHGVRAIEDPALMARLADRRIPLEVCPTSNVQTGAVPSLAEHPLKTLLDAGVRVTINTDDPLVFG-TTLT-E 293

                        250       260       270
                 ....*....|....*....|....*....|....*.
gi 532691757 455 FYEVFMGIGGMkaDLRTLKQLAMNSIKYSTLLESEK 490
Cdd:PRK09358 294 EYEALAEAFGL--SDEDLAQLARNALEAAFLSEEEK 327
A_deaminase_N pfam08451
Adenosine/AMP deaminase N-terminal; This domain is found to the N-terminus of the Adenosine ...
 12-102 1.50e-21

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: 88.90  E-value: 1.50e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532691757   12 LCFLLLAVAMSFFGSALSIDETRAHLLLKEKMMRLGGRLVLNTKEELANERLMTLKIAEMKEAMRTLI-FPPSMHFFQAK 90
Cdd:pfam08451   4 LALLYLSLLYYSRPTEERYERLRQALLSKEERLRLGGNLELSPLEEKANDILMAIKQVELAEGFRNWEnYPPAPHFFLAK 83

                          90
                  ....*....|..
gi 532691757   91 HLIERSQVFNIL 102
Cdd:pfam08451  84 DLINESDLFKFL 95
 
Name Accession Description Interval E-value
adm_rel TIGR01431
adenosine deaminase-related growth factor; Members of this family have been described as ...
 30-509 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: 856.79  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532691757   30 IDETRAHLLLKEKMMRLGGRLVLNTKEELANERLMTLKIAEMKEAMRT-LIFPPSMHFFQAKHLIERSQVFNILRMMPKG 108
Cdd:TIGR01431   1 YDETRNHLILKEKSMRLGGKLVLTTKEKLANERIMTLKIAEMKEAMRTpLIFPPSMHFFQAKHLIERSQVFKILRMMPKG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532691757  109 AALHLHDIGIVTMDWLVRNVTYRPHCHICFTPRGIMQFRFAHPTPRPSEKCSKWILLEDYRKrVQNVTEFDDSLLRNFTL 188
Cdd:TIGR01431  81 AALHLHDLGIVSMDWLVRNVTYRPNLHICFTKRNIMVLRFRHPTPRPSECCSKWILLEDYRK-SQNVEEFDDSLLRNFTL 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532691757  189 VTQHPEVIYTNQNVVWSKFETIFFTISGLIHYAPVFRDYVFRSMQEFYEDNVLYMEIRARLLPVYELSGEHHDEEWSVKT 268
Cdd:TIGR01431 160 VTTHPEVDYTTQNVVWSRFETIFFTLSGLLHYAPVFRDYYFRALEEFYEDNVQYMELRSRLFPLYELSGTHHDEEWSVKT 239

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532691757  269 YQEVAQKFVETHPEFIGIKIIYSDHRSKDVAVIAESIRMAMGLRIKFPTVVAGFDLVGHEDTGHSLHDYKEALMIPAkDG 348
Cdd:TIGR01431 240 YKEVTEKFVEEHPDFIGIKIIYSDLRSKDVEEIAEYIKMAMGLRIKYPDFVAGFDLVGQEDTGHSLLDYKDALLIPS-IG 318

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532691757  349 VKLPYFFHAGETDWQGTSIDRNILDALMLNTTRIGHGFALSKHPAVRTYSWKKDIPIEVCPISNQVLKLVSDLRNHPVAT 428
Cdd:TIGR01431 319 VKLPYFFHAGETNWQGTSVDRNLLDALLLNTTRIGHGFALSKHPAVRTYSKERDIPIEVCPISNQVLKLVSDLRNHPVAT 398

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532691757  429 LMATGHPMVISSDDPAMFGAKGLSYDFYEVFMGIGGMKADLRTLKQLAMNSIKYSTLLESEKNTFMEIWKKRWDKFIADV 508
Cdd:TIGR01431 399 LMADNYPMVISSDDPAFWGAKGLSYDFYEAFMGIAGMKADLRTLKQLALNSIKYSALSEEEKNTAMAKWKKQWDKFIDDV 478


                  .
gi 532691757  509 A 509
Cdd:TIGR01431 479 L 479
ADGF cd01321
Adenosine deaminase-related growth factors (ADGF), a novel family of secreted growth-factors ...
 82-501 0e+00

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: 563.05  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532691757  82 PSMHFFQAKHLIERSQVFNILRMMPKGAALHLHDIGIVTMDWLVRNVTYRphchicftprgimqfrfahptprpsekcsk 161
Cdd:cd01321    1 PGMHFFKAKDLIENSTLFKIIQKMPKGALLHVHDTAMVSSDWLIKNATYR------------------------------ 50

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532691757 162 willedyrkrvqnvtefddsllrnftlvtqhpeviytnqnvvwskFETIFFTISGLIHYAPVFRDYVFRSMQEFYEDNVL 241
Cdd:cd01321   51 ---------------------------------------------FEQIFDIIDGLLTYLPIFRDYYRRLLEELYEDNVQ 85

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532691757 242 YMEIRARLLPVYELSGEHHDEEWSVKTYQEVAQKFVETHPEFIGIKIIYSDHRSKDVAVIAESIRMAMGLRIKFPTVVAG 321
Cdd:cd01321   86 YVELRSSFSPLYDLDGREYDYEETVQLLEEVVEKFKKTHPDFIGLKIIYATLRNFNDSEIKESMEQCLNLKKKFPDFIAG 165

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532691757 322 FDLVGHEDTGHSLHDYKEALMIPAKDGVKLPYFFHAGETDWQGTSIDRNILDALMLNTTRIGHGFALSKHPAVRTYSWKK 401
Cdd:cd01321  166 FDLVGQEDAGRPLLDFLPQLLWFPKQCAEIPFFFHAGETNGDGTETDENLVDALLLNTKRIGHGFALPKHPLLMDLVKKK 245

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532691757 402 DIPIEVCPISNQVLKLVSDLRNHPVATLMATGHPMVISSDDPAMFGAKGLSYDFYEVFMGIGGMKADLRTLKQLAMNSIK 481
Cdd:cd01321  246 NIAIEVCPISNQVLGLVSDLRNHPAAALLARGVPVVISSDDPGFWGAKGLSHDFYQAFMGLAPADAGLRGLKQLAENSIR 325

                        410       420
                 ....*....|....*....|
gi 532691757 482 YSTLLESEKNTFMEIWKKRW 501
Cdd:cd01321  326 YSALSDQEKDEAVAKWEKKW 345
ADA_AMPD cd00443
Adenosine/AMP deaminase. Adenosine deaminases (ADAs) are present in pro- and eukaryotic ...
 193-497 2.89e-46

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: 163.67  E-value: 2.89e-46
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532691757 193 PEVIYTNqnvVWSKFETIFFTISGLIHYAPVFRDYVFRSMQEFYEDNVLYMEIRarllpvYELSGEHHDEEWSVKTYQ-- 270
Cdd:cd00443   16 PETLLEL---IKKEFFEKFLLVHNLLQKGEALARALKEVIEEFAEDNVQYLELR------TTPRLLETEKGLTKEQYWll 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532691757 271 --EVAQKFVETHPeFIGIKIIYSDHRSKDV---AVIAESIrmaMGLRIKFPTVVAGFDLVGHEDTGHS-LHDYKEALMIp 344
Cdd:cd00443   87 viEGISEAKQWFP-PIKVRLILSVDRRGPYvqnYLVASEI---LELAKFLSNYVVGIDLVGDESKGENpLRDFYSYYEY- 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532691757 345 AKDGVKLPYFFHAGETDWQGTsidrnILDALMLNTTRIGHGFALSKHPAVRTYSWKKDIPIEVCPISNQVLKLVSDLRNH 424
Cdd:cd00443  162 ARRLGLLGLTLHCGETGNREE-----LLQALLLLPDRIGHGIFLLKHPELIYLVKLRNIPIEVCPTSNVVLGTVQSYEKH 236

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 532691757 425 PVATLMATGHPMVISSDDPAMFGAkGLSYDFYEVFMgigGMKADLRTLKQLAMNSIKYSTLLESEKNTFMEIW 497
Cdd:cd00443  237 PFMRFFKAGLPVSLSTDDPGIFGT-SLSEEYSLAAK---TFGLTFEDLCELNRNSVLSSFAKDEEKKSLLEVL 305
Add COG1816
Adenosine deaminase [Nucleotide transport and metabolism]; Adenosine deaminase is part of the ...
 228-506 3.45e-31

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


Pssm-ID: 441421  Cd Length: 326  Bit Score: 122.89  E-value: 3.45e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532691757 228 VFRSMQEFY-----------EDNVLYMEIRarLLPVYelsgeHHDEEWSVKTYQE-VAQKFVETHPEF-IGIKIIYSDHR 294
Cdd:COG1816   59 VLQTEEDFRrlayeyledaaADGVRYAEIR--FDPQL-----HTRRGLSLEEVVEaVLDGLREAEREFgISVRLILCALR 131

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532691757 295 SKDVAVIAESIRMAMGLRIKFptvVAGFDLVGHEDtGHSLHDYKEALMIPAKDGVKLpyFFHAGETD-WQgtsidrNILD 373
Cdd:COG1816  132 HLSPEAAFETLELALRYRDRG---VVGFGLAGDER-GFPPEKFAEAFARAREAGLHL--TAHAGEAGgPE------SIWE 199

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532691757 374 AL-MLNTTRIGHGFALSKHPAVRTYSWKKDIPIEVCPISNQVLKLVSDLRNHPVATLMATGHPMVISSDDPAMFGAkGLS 452
Cdd:COG1816  200 ALdLLGAERIGHGVRAIEDPALVARLADRGIPLEVCPTSNVQLGVVPSLAEHPLRRLLDAGVRVTLNTDDPLYFGT-TLT 278

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....
gi 532691757 453 YDfYEVFMGIGGMkaDLRTLKQLAMNSIKYSTLLESEKntfmEIWKKRWDKFIA 506
Cdd:COG1816  279 DE-YELAAEAFGL--SDADLAQLARNAIEASFLPEEEK----AALLAELDAYFA 325
ADA cd01320
Adenosine deaminase (ADA) is a monomeric zinc dependent enzyme which catalyzes the ...
 208-491 1.74e-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: 115.38  E-value: 1.74e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532691757 208 ETIFFTISGLIHYApVFRDYVFRSMQEFYEDNVLYMEIRarllpvyeLSGEHH-----DEEWSVKTYQEVAQKFVETHPe 282
Cdd:cd01320   56 AKYDFGLSVLQTEE-DFERLAYEYLEDAAADGVVYAEIR--------FSPQLHtrrglSFDEVVEAVLRGLDEAEAEFG- 125

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532691757 283 fIGIKIIYSDHRSKDVAVIAESIRMAmgLRIKFPTVVaGFDLVGHEdTGHSLHDYKEALMIPAKDGVKLPyfFHAGETDw 362
Cdd:cd01320  126 -IKARLILCGLRHLSPESAQETLELA--LKYRDKGVV-GFDLAGDE-VGFPPEKFVRAFQRAREAGLRLT--AHAGEAG- 197

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532691757 363 qGTSidrNILDAL-MLNTTRIGHGFALSKHPAVRTYSWKKDIPIEVCPISNQVLKLVSDLRNHPVATLMATGHPMVISSD 441
Cdd:cd01320  198 -GPE---SVRDALdLLGAERIGHGIRAIEDPELVKRLAERNIPLEVCPTSNVQTGAVKSLAEHPLRELLDAGVKVTINTD 273

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|
gi 532691757 442 DPAMFGAKgLSYDFYEVFMGIGgmkADLRTLKQLAMNSIKYSTLLESEKN 491
Cdd:cd01320  274 DPTVFGTY-LTDEYELLAEAFG---LTEEELKKLARNAVEASFLSEEEKA 319
PRK09358 PRK09358
adenosine deaminase; Provisional
 224-490 1.79e-27

adenosine deaminase; Provisional


Pssm-ID: 236480  Cd Length: 340  Bit Score: 112.96  E-value: 1.79e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532691757 224 FRDYVFRSMQEFYEDNVLYMEIR-------ARLLPVYELsgehhdeewsVKTYQEVAQKFVETHPefIGIKIIYSDHRSK 296
Cdd:PRK09358  79 LRRLAFEYLEDAAADGVVYAEIRfdpqlhtERGLPLEEV----------VEAVLDGLRAAEAEFG--ISVRLILCFMRHF 146

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532691757 297 DVAVIAESIrmAMGLRIKFPTVVAGFDLVGHEDtGHSLHDYKEALMIpAKD-GvkLPYFFHAGETDwqGTSidrNILDAL 375
Cdd:PRK09358 147 GEEAAAREL--EALAARYRDDGVVGFDLAGDEL-GFPPSKFARAFDR-ARDaG--LRLTAHAGEAG--GPE---SIWEAL 215

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532691757 376 -MLNTTRIGHGFALSKHPAVRTYSWKKDIPIEVCPISNQVLKLVSDLRNHPVATLMATGHPMVISSDDPAMFGaKGLSyD 454
Cdd:PRK09358 216 dELGAERIGHGVRAIEDPALMARLADRRIPLEVCPTSNVQTGAVPSLAEHPLKTLLDAGVRVTINTDDPLVFG-TTLT-E 293

                        250       260       270
                 ....*....|....*....|....*....|....*.
gi 532691757 455 FYEVFMGIGGMkaDLRTLKQLAMNSIKYSTLLESEK 490
Cdd:PRK09358 294 EYEALAEAFGL--SDEDLAQLARNALEAAFLSEEEK 327
aden_deam TIGR01430
adenosine deaminase; This family includes the experimentally verified adenosine deaminases of ...
 204-495 4.37e-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: 105.52  E-value: 4.37e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532691757  204 WSKFETIFFTISGLIHYAPVFRDYVFRSMQEFYEDNVLYMEIRarllpvyeLSGEHHDEE-WSVKTYQE-----VAQKFV 277
Cdd:TIGR01430  50 LQDFLAKYDFGVEVLRTEDDFKRLAYEYVEKAAKDGVVYAEVF--------FDPQLHTNRgISPDTVVEavldgLDEAER 121

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532691757  278 ETHpefIGIKIIYSDHRSKDVAVIAESIRMAmgLRIKFPTVVaGFDLVGHEdTGHSLHDYKEALMIPAKDGVKLPyfFHA 357
Cdd:TIGR01430 122 DFG---IKSRLILCGMRHKQPEAAEETLELA--KPYKEQTIV-GFGLAGDE-RGGPPPDFVRAFAIARELGLHLT--VHA 192

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532691757  358 GETDwqGTSIDRNILDalMLNTTRIGHGFALSKHPAVRTYSWKKDIPIEVCPISNQVLKLVSDLRNHPVATLMATGHPMV 437
Cdd:TIGR01430 193 GELG--GPESVREALD--DLGATRIGHGVRALEDPELLKRLAQENITLEVCPTSNVALGVVKSLAEHPLRRFLEAGVKVT 268

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 532691757  438 ISSDDPAMFGakglSYDFYEVFMGIGGMKADLRTLKQLAMNSIKYSTLLESEKNTFME 495
Cdd:TIGR01430 269 LNSDDPAYFG----SYLTEEYEIAAKHAGLTEEELKQLARNALEGSFLSDDEKKELLA 322
A_deaminase_N pfam08451
Adenosine/AMP deaminase N-terminal; This domain is found to the N-terminus of the Adenosine ...
 12-102 1.50e-21

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: 88.90  E-value: 1.50e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532691757   12 LCFLLLAVAMSFFGSALSIDETRAHLLLKEKMMRLGGRLVLNTKEELANERLMTLKIAEMKEAMRTLI-FPPSMHFFQAK 90
Cdd:pfam08451   4 LALLYLSLLYYSRPTEERYERLRQALLSKEERLRLGGNLELSPLEEKANDILMAIKQVELAEGFRNWEnYPPAPHFFLAK 83

                          90
                  ....*....|..
gi 532691757   91 HLIERSQVFNIL 102
Cdd:pfam08451  84 DLINESDLFKFL 95
A_deaminase pfam00962
Adenosine deaminase;
224-491 7.32e-19

Adenosine deaminase;


Pssm-ID: 425964  Cd Length: 330  Bit Score: 87.49  E-value: 7.32e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532691757  224 FRDYVFRSMQEFYEDNVLYMEIRarllpvyeLSGEHH-----DEEWSVKTyqeVAQKFVETHPEF-IGIKIIYSDHRSKD 297
Cdd:pfam00962  70 IRRLAFEYAEDVAKDGVVYAEVR--------YDPQSHasrglSPDTVVDA---VLDAVDAAEREFgITVRLIVCAMRHEH 138

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532691757  298 VAVIAESIRMAMGLRikfPTVVAGFDLVGHEdTGHSLH---DYKEALMIPAKDGVKLPyfFHAGETDWQGTsidrnILDA 374
Cdd:pfam00962 139 PECSREIAELAPRYR---DQGIVAFGLAGDE-KGFPPSlfrDHVEAFARARDAGLHLT--VHAGEAGGPQS-----VWEA 207

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532691757  375 L-MLNTTRIGHGFALSKHPAVRTYSWKKDIPIEVCPISNQVLKLVSDLRNHPVATLMATGHPMVISSDDPAMFGAK-GLS 452
Cdd:pfam00962 208 LdDLGAERIGHGVRSAEDPRLLDRLADRQIPLEICPTSNVQTGAVASLAEHPLKTFLRAGVPVSLNTDDPLMFGSDlLDE 287

                         250       260       270
                  ....*....|....*....|....*....|....*....
gi 532691757  453 YDFYEVFMGIggmkaDLRTLKQLAMNSIKYSTLLESEKN 491
Cdd:pfam00962 288 YQVAKRAPGF-----DEEELARLAKNAVKGSFLPADEKR 321
PTZ00124 PTZ00124
adenosine deaminase; Provisional
 236-477 1.21e-14

adenosine deaminase; Provisional


Pssm-ID: 173415  Cd Length: 362  Bit Score: 75.29  E-value: 1.21e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532691757 236 YEDNVLYMEIRARllPVYELSGEHHDEEWSVKTYQEVAQKFVETHPEFIGIKIIYSDHRSKDVAVIAESIRMAMGLRIKF 315
Cdd:PTZ00124 116 YKEGVVLMEFRYS--PTFVAFKHNLDIDLIHQAIVKGIKEAVELLDHKIEVGLLCIGDTGHDAAPIKESADFCLKHKADF 193

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532691757 316 ptvvAGFDLVGHEdtgHSLHDYKEALMIPAKDGVKLPyfFHAGEtDWQGTSIDRNILDALMLNTTRIGHGFALSKHPAVR 395
Cdd:PTZ00124 194 ----VGFDHAGHE---VDLKPFKDIFDYVREAGVNLT--VHAGE-DVTLPNLNTLYSAIQVLKVKRIGHGIRVAESQELI 263

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532691757 396 TYSWKKDIPIEVCPISNQVLKLVSDLRNHPVATLMATGHPMVISSDDPAMFgAKGLSYDFYEVFMGIGGMKADLRTLKQL 475
Cdd:PTZ00124 264 DMVKEKDILLEVCPISNVLLNNAKSMDTHPIRKLYDAGVKVSVNSDDPGMF-LTNINDDYEELYTHLNFTLADFMKMNEW 342


                 ..
gi 532691757 476 AM 477
Cdd:PTZ00124 343 AL 344
metallo-dependent_hydrolases cd01292
Superfamily of metallo-dependent hydrolases (also called amidohydrolase superfamily) is a ...
 315-482 7.78e-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: 7.78e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532691757 315 FPTVVAGFDLVGHE-DTGHSLHDYKEALMIPAKDGvkLPYFFHAGETDWQGTSIDRNILDALMLNTTRIGHGFALSKHpA 393
Cdd:cd01292  112 LELGAVGLKLAGPYtATGLSDESLRRVLEEARKLG--LPVVIHAGELPDPTRALEDLVALLRLGGRVVIGHVSHLDPE-L 188

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532691757 394 VRTYSwKKDIPIEVCPISNQVLKLvSDLRNHPVATLMATGHPMVISSDDPAMFGAKGLSYDFYEVFMgIGGMKADLRTLK 473
Cdd:cd01292  189 LELLK-EAGVSLEVCPLSNYLLGR-DGEGAEALRRLLELGIRVTLGTDGPPHPLGTDLLALLRLLLK-VLRLGLSLEEAL 265

                        170
                 ....*....|
gi 532691757 474 QLA-MNSIKY 482
Cdd:cd01292  266 RLAtINPARA 275
AMPD cd01319
AMP deaminase (AMPD) catalyzes the hydrolytic deamination of adensosine monophosphate (AMP) at ...
 381-446 1.66e-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: 1.66e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 532691757 381 RIGHGFALSKHPAVRTYSWKKDIPIEVCPISNQVLKLvsDLRNHPVATLMATGHPMVISSDDPAMF 446
Cdd:cd01319  351 GISHGINLRKVPVLQYLYYLTQIGIAMSPLSNNSLFL--SYEKNPFPEFFKRGLNVSLSTDDPLQF 414
PLN03055 PLN03055
AMP deaminase; Provisional
 356-445 2.93e-03

AMP deaminase; Provisional


Pssm-ID: 178613  Cd Length: 602  Bit Score: 40.23  E-value: 2.93e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532691757 356 HAGETDwqgtsiDRNILDALMLNTTRIGHGFALSKHPAVRTYSWKKDIPIEVCPISNQVLKLvsDLRNHPVATLMATGHP 435
Cdd:PLN03055 422 HAGEAG------DIDHLAAAFLLAHNIAHGNNLRKSPGLQYLYYLAQIGLAMSPLSNNSLFL--DYHRNPFPMFFARGLN 493

                         90
                 ....*....|
gi 532691757 436 MVISSDDPAM 445
Cdd:PLN03055 494 VSLSTDDPLQ 503
AMP_deaminase TIGR01429
AMP deaminase; This model describes AMP deaminase, a large, well-conserved eukaryotic protein ...
 352-446 9.58e-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: 38.67  E-value: 9.58e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532691757  352 PYFFHAGETDWQGTSidrnildalMLNTTRIGHGFALSKHPAVRTYSWKKDIPIEVCPISNQVLKLVSDlRNhPVATLMA 431
Cdd:TIGR01429 443 PHCGEAGSVDHLVSA---------FLTSHGINHGILLRKVPVLQYLYYLTQIPIAMSPLSNNSLFLEYS-KN-PLPEYLH 511

                          90
                  ....*....|....*
gi 532691757  432 TGHPMVISSDDPAMF 446
Cdd:TIGR01429 512 KGLNVSLSTDDPLQF 526
 
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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