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Conserved domains on  [gi|1039757181|ref|XP_017173553|]
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guanine deaminase isoform X2 [Mus musculus]

Protein Classification

amidohydrolase family protein( domain architecture ID 330)

metal-dependent amidohydrolase family protein having a conserved metal binding site, usually involving four histidines and one aspartic acid residue

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
metallo-dependent_hydrolases super family cl00281
Superfamily of metallo-dependent hydrolases (also called amidohydrolase superfamily) is a ...
 1-370 0e+00

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.


The actual alignment was detected with superfamily member cd01303:

Pssm-ID: 469705 [Multi-domain]  Cd Length: 429  Bit Score: 561.51  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039757181   1 MPGLVDTHIHAPQYAFAGSNVDLPLLEWLNKYTFPTEQRFRSTDVAEEVYTRVVRRTLKNGTTTACYFGTIHTDSSLILA 80
Cdd:cd01303    64 LPGFIDTHIHAPQYANIGSGLGEPLLDWLETYTFPEEAKFADPAYAREVYGRFLDELLRNGTTTACYFATIHPESTEALF 143

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039757181  81 EITDKFGQRAFVGKVCMDLNDtvPEYK-ETTEESVKETERFVSEMLQKnYPRVKPIVTPRFTLSCTETLMSELGNIAKTH 159
Cdd:cd01303   144 EEAAKRGQRAIAGKVCMDRNA--PEYYrDTAESSYRDTKRLIERWHGK-SGRVKPAITPRFAPSCSEELLAALGKLAKEH 220

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039757181 160 -DLYIQSHISENREEIEAVKSLYPSYKNYTDVYDKNNLLTNKTVMAHGCYLSEEELNIFSERGASIAHCPNSNLSLSSGL 238
Cdd:cd01303   221 pDLHIQTHISENLDEIAWVKELFPGARDYLDVYDKYGLLTEKTVLAHCVHLSEEEFNLLKERGASVAHCPTSNLFLGSGL 300

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039757181 239 LNVLEVLKHKVKIGLGTDVAGGYSYSMLDAIRRAVMVSNVLLINKVNEKNLTLKEVFRLATLGGSQALGLDSEIGNFEVG 318
Cdd:cd01303   301 FDVRKLLDAGIKVGLGTDVGGGTSFSMLDTLRQAYKVSRLLGYELGGHAKLSPAEAFYLATLGGAEALGLDDKIGNFEVG 380

                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1039757181 319 KEFDALLINPRASDSPIDLfygDFVGDISEAVIQKFLYLGDDRNIEEVYVGG 370
Cdd:cd01303   381 KEFDAVVIDPSATPLLADR---MFRVESLEEALFKFLYLGDDRNIREVYVAG 429
 
Name Accession Description Interval E-value
GDEase cd01303
Guanine deaminase (GDEase). Guanine deaminase is an aminohydrolase responsible for the ...
 1-370 0e+00

Guanine deaminase (GDEase). Guanine deaminase is an aminohydrolase responsible for the conversion of guanine to xanthine and ammonia, the first step to utilize guanine as a nitrogen source. This reaction also removes the guanine base from the pool and therefore can play a role in the regulation of cellular GTP and the guanylate nucleotide pool.


Pssm-ID: 238628 [Multi-domain]  Cd Length: 429  Bit Score: 561.51  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039757181   1 MPGLVDTHIHAPQYAFAGSNVDLPLLEWLNKYTFPTEQRFRSTDVAEEVYTRVVRRTLKNGTTTACYFGTIHTDSSLILA 80
Cdd:cd01303    64 LPGFIDTHIHAPQYANIGSGLGEPLLDWLETYTFPEEAKFADPAYAREVYGRFLDELLRNGTTTACYFATIHPESTEALF 143

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039757181  81 EITDKFGQRAFVGKVCMDLNDtvPEYK-ETTEESVKETERFVSEMLQKnYPRVKPIVTPRFTLSCTETLMSELGNIAKTH 159
Cdd:cd01303   144 EEAAKRGQRAIAGKVCMDRNA--PEYYrDTAESSYRDTKRLIERWHGK-SGRVKPAITPRFAPSCSEELLAALGKLAKEH 220

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039757181 160 -DLYIQSHISENREEIEAVKSLYPSYKNYTDVYDKNNLLTNKTVMAHGCYLSEEELNIFSERGASIAHCPNSNLSLSSGL 238
Cdd:cd01303   221 pDLHIQTHISENLDEIAWVKELFPGARDYLDVYDKYGLLTEKTVLAHCVHLSEEEFNLLKERGASVAHCPTSNLFLGSGL 300

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039757181 239 LNVLEVLKHKVKIGLGTDVAGGYSYSMLDAIRRAVMVSNVLLINKVNEKNLTLKEVFRLATLGGSQALGLDSEIGNFEVG 318
Cdd:cd01303   301 FDVRKLLDAGIKVGLGTDVGGGTSFSMLDTLRQAYKVSRLLGYELGGHAKLSPAEAFYLATLGGAEALGLDDKIGNFEVG 380

                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1039757181 319 KEFDALLINPRASDSPIDLfygDFVGDISEAVIQKFLYLGDDRNIEEVYVGG 370
Cdd:cd01303   381 KEFDAVVIDPSATPLLADR---MFRVESLEEALFKFLYLGDDRNIREVYVAG 429
guan_deamin TIGR02967
guanine deaminase; This model describes guanine deaminase, which hydrolyzes guanine to ...
 1-370 5.48e-179

guanine deaminase; This model describes guanine deaminase, which hydrolyzes guanine to xanthine and ammonia. Xanthine can then be converted to urate by xanthine dehydrogenase, and urate subsequently degraded. In some bacteria, the guanine deaminase gene is found near the xdhABC genes for xanthine dehydrogenase. Non-homologous forms of guanine deaminase also exist, as well as distantly related forms outside the scope of this model. [Purines, pyrimidines, nucleosides, and nucleotides, Other]


Pssm-ID: 132012 [Multi-domain]  Cd Length: 401  Bit Score: 502.94  E-value: 5.48e-179
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039757181   1 MPGLVDTHIHAPQYAFAGSnVDLPLLEWLNKYTFPTEQRFRSTDVAEEVYTRVVRRTLKNGTTTACYFGTIHTDSSLILA 80
Cdd:TIGR02967  44 MPGFIDTHIHYPQTEMIAS-YGEQLLEWLEKYTFPTEARFADPDHAEEVAEFFLDELLRNGTTTALVFATVHPESVDALF 122

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039757181  81 EITDKFGQRAFVGKVCMDLNdtVPEY-KETTEESVKETERFVSEMLQKNypRVKPIVTPRFTLSCTETLMSELGNIAKTH 159
Cdd:TIGR02967 123 EAALKRGMRMIAGKVLMDRN--APDYlRDTAESSYDESKALIERWHGKG--RLLYAVTPRFAPTSSPEQLAAAGELAKEY 198

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039757181 160 -DLYIQSHISENREEIEAVKSLYPSYKNYTDVYDKNNLLTNKTVMAHGCYLSEEELNIFSERGASIAHCPNSNLSLSSGL 238
Cdd:TIGR02967 199 pDVYVQTHLSENKDEIAWVKELFPEAKDYLDVYDHYGLLGRRSVFAHCIHLSDEECQRLAETGAAIAHCPTSNLFLGSGL 278

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039757181 239 LNVLEVLKHKVKIGLGTDVAGGYSYSMLDAIRRAVMVSNVLlinkvnEKNLTLKEVFRLATLGGSQALGLDSEIGNFEVG 318
Cdd:TIGR02967 279 FNLKKALEHGVRVGLGTDVGGGTSFSMLQTLREAYKVSQLQ------GARLSPFEAFYLATLGGARALDLDDRIGNFEPG 352

                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1039757181 319 KEFDALLINPRASDSPIDLFYGdfvGDISEAVIQKFLYLGDDRNIEEVYVGG 370
Cdd:TIGR02967 353 KEADFVVLDPAATPLLALRFEG---ADTLEDKLFKLMYLGDDRNVAETYVAG 401
SsnA COG0402
Cytosine/adenosine deaminase or related metal-dependent hydrolase [Nucleotide transport and ...
 1-374 3.97e-109

Cytosine/adenosine deaminase or related metal-dependent hydrolase [Nucleotide transport and metabolism, General function prediction only]; Cytosine/adenosine deaminase or related metal-dependent hydrolase is part of the Pathway/BioSystem: Pyrimidine salvage


Pssm-ID: 440171 [Multi-domain]  Cd Length: 416  Bit Score: 326.01  E-value: 3.97e-109
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039757181   1 MPGLVDTHIHAPQYAFAGSNVDLPLLEWLNKYTFPTEQRFrSTDVAEEVYTRVVRRTLKNGTTTACYFGTIHTDSSLILA 80
Cdd:COG0402    58 LPGLVNTHTHLPQTLLRGLADDLPLLDWLEEYIWPLEARL-DPEDVYAGALLALAEMLRSGTTTVADFYYVHPESADALA 136

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039757181  81 EITDKFGQRAFVGKVCMDLNdTVPEYKETTEESVKETERFVSEMLQKNYPRVKPIVTPRFTLSCTETLMSELGNIAKTHD 160
Cdd:COG0402   137 EAAAEAGIRAVLGRGLMDRG-FPDGLREDADEGLADSERLIERWHGAADGRIRVALAPHAPYTVSPELLRAAAALARELG 215

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039757181 161 LYIQSHISENREEIEAVKSLYPsyKNYTDVYDKNNLLTNKTVMAHGCYLSEEELNIFSERGASIAHCPNSNLSLSSGLLN 240
Cdd:COG0402   216 LPLHTHLAETRDEVEWVLELYG--KRPVEYLDELGLLGPRTLLAHCVHLTDEEIALLAETGASVAHCPTSNLKLGSGIAP 293

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039757181 241 VLEVLKHKVKIGLGTDVAGG-YSYSMLDAIRRAvmvsnvLLINKVNEKN---LTLKEVFRLATLGGSQALGLDSEIGNFE 316
Cdd:COG0402   294 VPRLLAAGVRVGLGTDGAASnNSLDMFEEMRLA------ALLQRLRGGDptaLSAREALEMATLGGARALGLDDEIGSLE 367

                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1039757181 317 VGKEFDALLINPRASD-SPIDlfygdfvgdiseAVIQKFLYLGDDRNIEEVYVGGKQVV 374
Cdd:COG0402   368 PGKRADLVVLDLDAPHlAPLH------------DPLSALVYAADGRDVRTVWVAGRVVV 414
PRK09228 PRK09228
guanine deaminase; Provisional
 1-373 1.03e-102

guanine deaminase; Provisional


Pssm-ID: 236419 [Multi-domain]  Cd Length: 433  Bit Score: 310.20  E-value: 1.03e-102
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039757181   1 MPGLVDTHIHAPQYAFAGSNVDlPLLEWLNKYTFPTEQRFRSTDVAEEVYTRVVRRTLKNGTTTACYFGTIHTDSSLILA 80
Cdd:PRK09228   69 LPGFIDTHIHYPQTDMIASYGE-QLLDWLNTYTFPEERRFADPAYAREVAEFFLDELLRNGTTTALVFGTVHPQSVDALF 147

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039757181  81 EITDKFGQRAFVGKVCMDLNdtVPEY-KETTEESVKETERFVSEMLQKNypRVKPIVTPRFTLSCTETLMSELGNIAKTH 159
Cdd:PRK09228  148 EAAEARNMRMIAGKVLMDRN--APDGlRDTAESGYDDSKALIERWHGKG--RLLYAITPRFAPTSTPEQLEAAGALAREH 223

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039757181 160 -DLYIQSHISENREEIEAVKSLYPSYKNYTDVYDKNNLLTNKTVMAHGCYLSEEELNIFSERGASIAHCPNSNLSLSSGL 238
Cdd:PRK09228  224 pDVWIQTHLSENLDEIAWVKELFPEARDYLDVYERYGLLGPRAVFAHCIHLEDRERRRLAETGAAIAFCPTSNLFLGSGL 303

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039757181 239 LNVLEVLKHKVKIGLGTDVAGGYSYSMLDAIRRAVMVSnvllinKVNEKNLTLKEVFRLATLGGSQALGLDSEIGNFEVG 318
Cdd:PRK09228  304 FDLKRADAAGVRVGLGTDVGGGTSFSMLQTMNEAYKVQ------QLQGYRLSPFQAFYLATLGGARALGLDDRIGNLAPG 377

                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1039757181 319 KEFDALLINPRASdSPIDLFYgDFVGDISEAVIQKFLyLGDDRNIEEVYVGGKQV 373
Cdd:PRK09228  378 KEADFVVLDPAAT-PLLALRT-ARAESLEELLFALMT-LGDDRAVAETYVAGRPV 429
Amidohydro_1 pfam01979
Amidohydrolase family; This family of enzymes are a a large metal dependent hydrolase ...
 1-373 3.12e-53

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: 179.62  E-value: 3.12e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039757181   1 MPGLVDTHIHAPQYAFAGSNVDLpllewlnkytfpteqrfrstDVAEEVYTRVVRRTLKNGTTTACYFGTIHTDSSLILA 80
Cdd:pfam01979   3 LPGLIDAHVHLEMGLLRGIPVPP--------------------EFAYEALRLGITTMLKSGTTTVLDMGATTSTGIEALL 62

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039757181  81 EITDK--FGQRAFVGKVCMDLNDTVPEYKETTEESVKETErfvsEMLQKNYPRVKPIVTPRFTLSCTETLMSELGNIAKT 158
Cdd:pfam01979  63 EAAEElpLGLRFLGPGCSLDTDGELEGRKALREKLKAGAE----FIKGMADGVVFVGLAPHGAPTFSDDELKAALEEAKK 138

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039757181 159 HDLYIQSHISENREEIEAVKSLYPS---YKNYTDVYDKNNLL-TNKTVMAHGCYLSEEELNIFSER--GASIAHCPNSNL 232
Cdd:pfam01979 139 YGLPVAIHALETKGEVEDAIAAFGGgieHGTHLEVAESGGLLdIIKLILAHGVHLSPTEANLLAEHlkGAGVAHCPFSNS 218

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039757181 233 SLSSGLLNVLEVLKHKVKIGLGTDVAG-GYSYSMLDAIRRAVmvsnvlLINKVNEKNLTLKEVFRLATLGGSQALGLDSE 311
Cdd:pfam01979 219 KLRSGRIALRKALEDGVKVGLGTDGAGsGNSLNMLEELRLAL------ELQFDPEGGLSPLEALRMATINPAKALGLDDK 292

                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1039757181 312 IGNFEVGKEFDALLINPRasdspidlfygdfvgdiseaVIQKFLYLGDDRNIEEVYVGGKQV 373
Cdd:pfam01979 293 VGSIEVGKDADLVVVDLD--------------------PLAAFFGLKPDGNVKKVIVKGKIV 334
 
Name Accession Description Interval E-value
GDEase cd01303
Guanine deaminase (GDEase). Guanine deaminase is an aminohydrolase responsible for the ...
 1-370 0e+00

Guanine deaminase (GDEase). Guanine deaminase is an aminohydrolase responsible for the conversion of guanine to xanthine and ammonia, the first step to utilize guanine as a nitrogen source. This reaction also removes the guanine base from the pool and therefore can play a role in the regulation of cellular GTP and the guanylate nucleotide pool.


Pssm-ID: 238628 [Multi-domain]  Cd Length: 429  Bit Score: 561.51  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039757181   1 MPGLVDTHIHAPQYAFAGSNVDLPLLEWLNKYTFPTEQRFRSTDVAEEVYTRVVRRTLKNGTTTACYFGTIHTDSSLILA 80
Cdd:cd01303    64 LPGFIDTHIHAPQYANIGSGLGEPLLDWLETYTFPEEAKFADPAYAREVYGRFLDELLRNGTTTACYFATIHPESTEALF 143

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039757181  81 EITDKFGQRAFVGKVCMDLNDtvPEYK-ETTEESVKETERFVSEMLQKnYPRVKPIVTPRFTLSCTETLMSELGNIAKTH 159
Cdd:cd01303   144 EEAAKRGQRAIAGKVCMDRNA--PEYYrDTAESSYRDTKRLIERWHGK-SGRVKPAITPRFAPSCSEELLAALGKLAKEH 220

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039757181 160 -DLYIQSHISENREEIEAVKSLYPSYKNYTDVYDKNNLLTNKTVMAHGCYLSEEELNIFSERGASIAHCPNSNLSLSSGL 238
Cdd:cd01303   221 pDLHIQTHISENLDEIAWVKELFPGARDYLDVYDKYGLLTEKTVLAHCVHLSEEEFNLLKERGASVAHCPTSNLFLGSGL 300

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039757181 239 LNVLEVLKHKVKIGLGTDVAGGYSYSMLDAIRRAVMVSNVLLINKVNEKNLTLKEVFRLATLGGSQALGLDSEIGNFEVG 318
Cdd:cd01303   301 FDVRKLLDAGIKVGLGTDVGGGTSFSMLDTLRQAYKVSRLLGYELGGHAKLSPAEAFYLATLGGAEALGLDDKIGNFEVG 380

                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1039757181 319 KEFDALLINPRASDSPIDLfygDFVGDISEAVIQKFLYLGDDRNIEEVYVGG 370
Cdd:cd01303   381 KEFDAVVIDPSATPLLADR---MFRVESLEEALFKFLYLGDDRNIREVYVAG 429
guan_deamin TIGR02967
guanine deaminase; This model describes guanine deaminase, which hydrolyzes guanine to ...
 1-370 5.48e-179

guanine deaminase; This model describes guanine deaminase, which hydrolyzes guanine to xanthine and ammonia. Xanthine can then be converted to urate by xanthine dehydrogenase, and urate subsequently degraded. In some bacteria, the guanine deaminase gene is found near the xdhABC genes for xanthine dehydrogenase. Non-homologous forms of guanine deaminase also exist, as well as distantly related forms outside the scope of this model. [Purines, pyrimidines, nucleosides, and nucleotides, Other]


Pssm-ID: 132012 [Multi-domain]  Cd Length: 401  Bit Score: 502.94  E-value: 5.48e-179
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039757181   1 MPGLVDTHIHAPQYAFAGSnVDLPLLEWLNKYTFPTEQRFRSTDVAEEVYTRVVRRTLKNGTTTACYFGTIHTDSSLILA 80
Cdd:TIGR02967  44 MPGFIDTHIHYPQTEMIAS-YGEQLLEWLEKYTFPTEARFADPDHAEEVAEFFLDELLRNGTTTALVFATVHPESVDALF 122

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039757181  81 EITDKFGQRAFVGKVCMDLNdtVPEY-KETTEESVKETERFVSEMLQKNypRVKPIVTPRFTLSCTETLMSELGNIAKTH 159
Cdd:TIGR02967 123 EAALKRGMRMIAGKVLMDRN--APDYlRDTAESSYDESKALIERWHGKG--RLLYAVTPRFAPTSSPEQLAAAGELAKEY 198

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039757181 160 -DLYIQSHISENREEIEAVKSLYPSYKNYTDVYDKNNLLTNKTVMAHGCYLSEEELNIFSERGASIAHCPNSNLSLSSGL 238
Cdd:TIGR02967 199 pDVYVQTHLSENKDEIAWVKELFPEAKDYLDVYDHYGLLGRRSVFAHCIHLSDEECQRLAETGAAIAHCPTSNLFLGSGL 278

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039757181 239 LNVLEVLKHKVKIGLGTDVAGGYSYSMLDAIRRAVMVSNVLlinkvnEKNLTLKEVFRLATLGGSQALGLDSEIGNFEVG 318
Cdd:TIGR02967 279 FNLKKALEHGVRVGLGTDVGGGTSFSMLQTLREAYKVSQLQ------GARLSPFEAFYLATLGGARALDLDDRIGNFEPG 352

                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1039757181 319 KEFDALLINPRASDSPIDLFYGdfvGDISEAVIQKFLYLGDDRNIEEVYVGG 370
Cdd:TIGR02967 353 KEADFVVLDPAATPLLALRFEG---ADTLEDKLFKLMYLGDDRNVAETYVAG 401
SsnA COG0402
Cytosine/adenosine deaminase or related metal-dependent hydrolase [Nucleotide transport and ...
 1-374 3.97e-109

Cytosine/adenosine deaminase or related metal-dependent hydrolase [Nucleotide transport and metabolism, General function prediction only]; Cytosine/adenosine deaminase or related metal-dependent hydrolase is part of the Pathway/BioSystem: Pyrimidine salvage


Pssm-ID: 440171 [Multi-domain]  Cd Length: 416  Bit Score: 326.01  E-value: 3.97e-109
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039757181   1 MPGLVDTHIHAPQYAFAGSNVDLPLLEWLNKYTFPTEQRFrSTDVAEEVYTRVVRRTLKNGTTTACYFGTIHTDSSLILA 80
Cdd:COG0402    58 LPGLVNTHTHLPQTLLRGLADDLPLLDWLEEYIWPLEARL-DPEDVYAGALLALAEMLRSGTTTVADFYYVHPESADALA 136

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039757181  81 EITDKFGQRAFVGKVCMDLNdTVPEYKETTEESVKETERFVSEMLQKNYPRVKPIVTPRFTLSCTETLMSELGNIAKTHD 160
Cdd:COG0402   137 EAAAEAGIRAVLGRGLMDRG-FPDGLREDADEGLADSERLIERWHGAADGRIRVALAPHAPYTVSPELLRAAAALARELG 215

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039757181 161 LYIQSHISENREEIEAVKSLYPsyKNYTDVYDKNNLLTNKTVMAHGCYLSEEELNIFSERGASIAHCPNSNLSLSSGLLN 240
Cdd:COG0402   216 LPLHTHLAETRDEVEWVLELYG--KRPVEYLDELGLLGPRTLLAHCVHLTDEEIALLAETGASVAHCPTSNLKLGSGIAP 293

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039757181 241 VLEVLKHKVKIGLGTDVAGG-YSYSMLDAIRRAvmvsnvLLINKVNEKN---LTLKEVFRLATLGGSQALGLDSEIGNFE 316
Cdd:COG0402   294 VPRLLAAGVRVGLGTDGAASnNSLDMFEEMRLA------ALLQRLRGGDptaLSAREALEMATLGGARALGLDDEIGSLE 367

                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1039757181 317 VGKEFDALLINPRASD-SPIDlfygdfvgdiseAVIQKFLYLGDDRNIEEVYVGGKQVV 374
Cdd:COG0402   368 PGKRADLVVLDLDAPHlAPLH------------DPLSALVYAADGRDVRTVWVAGRVVV 414
PRK09228 PRK09228
guanine deaminase; Provisional
 1-373 1.03e-102

guanine deaminase; Provisional


Pssm-ID: 236419 [Multi-domain]  Cd Length: 433  Bit Score: 310.20  E-value: 1.03e-102
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039757181   1 MPGLVDTHIHAPQYAFAGSNVDlPLLEWLNKYTFPTEQRFRSTDVAEEVYTRVVRRTLKNGTTTACYFGTIHTDSSLILA 80
Cdd:PRK09228   69 LPGFIDTHIHYPQTDMIASYGE-QLLDWLNTYTFPEERRFADPAYAREVAEFFLDELLRNGTTTALVFGTVHPQSVDALF 147

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039757181  81 EITDKFGQRAFVGKVCMDLNdtVPEY-KETTEESVKETERFVSEMLQKNypRVKPIVTPRFTLSCTETLMSELGNIAKTH 159
Cdd:PRK09228  148 EAAEARNMRMIAGKVLMDRN--APDGlRDTAESGYDDSKALIERWHGKG--RLLYAITPRFAPTSTPEQLEAAGALAREH 223

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039757181 160 -DLYIQSHISENREEIEAVKSLYPSYKNYTDVYDKNNLLTNKTVMAHGCYLSEEELNIFSERGASIAHCPNSNLSLSSGL 238
Cdd:PRK09228  224 pDVWIQTHLSENLDEIAWVKELFPEARDYLDVYERYGLLGPRAVFAHCIHLEDRERRRLAETGAAIAFCPTSNLFLGSGL 303

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039757181 239 LNVLEVLKHKVKIGLGTDVAGGYSYSMLDAIRRAVMVSnvllinKVNEKNLTLKEVFRLATLGGSQALGLDSEIGNFEVG 318
Cdd:PRK09228  304 FDLKRADAAGVRVGLGTDVGGGTSFSMLQTMNEAYKVQ------QLQGYRLSPFQAFYLATLGGARALGLDDRIGNLAPG 377

                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1039757181 319 KEFDALLINPRASdSPIDLFYgDFVGDISEAVIQKFLyLGDDRNIEEVYVGGKQV 373
Cdd:PRK09228  378 KEADFVVLDPAAT-PLLALRT-ARAESLEELLFALMT-LGDDRAVAETYVAGRPV 429
ATZ_TRZ_like cd01298
TRZ/ATZ family contains enzymes from the atrazine degradation pathway and related hydrolases. ...
 1-374 1.43e-64

TRZ/ATZ family contains enzymes from the atrazine degradation pathway and related hydrolases. Atrazine, a chlorinated herbizide, can be catabolized by a variety of different bacteria. The first three steps of the atrazine dehalogenation pathway are catalyzed by atrazine chlorohydrolase (AtzA), hydroxyatrazine ethylaminohydrolase (AtzB), and N-isopropylammelide N-isopropylaminohydrolase (AtzC). All three enzymes belong to the superfamily of metal dependent hydrolases. AtzA and AtzB, beside other related enzymes are represented in this CD.


Pssm-ID: 238623 [Multi-domain]  Cd Length: 411  Bit Score: 211.29  E-value: 1.43e-64
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039757181   1 MPGLVDTHIHAPQYAFAGSNVDLPLLEWLNKYTFPTEQRFRstdvAEEVY--TRV-VRRTLKNGTTTACYFGTIHTDssl 77
Cdd:cd01298    55 MPGLVNTHTHLAMTLLRGLADDLPLMEWLKDLIWPLERLLT----EEDVYlgALLaLAEMIRSGTTTFADMYFFYPD--- 127

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039757181  78 ILAEITDKFGQRAFVGKVCMDLNDTVPEykeTTEESVKETERFVSEMLQKNYPRVKPIVTPRFTLSCTETLMSELGNIAK 157
Cdd:cd01298   128 AVAEAAEELGIRAVLGRGIMDLGTEDVE---ETEEALAEAERLIREWHGAADGRIRVALAPHAPYTCSDELLREVAELAR 204

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039757181 158 THDLYIQSHISENREEIEAVKSLY---PsyknyTDVYDKNNLLTNKTVMAHGCYLSEEELNIFSERGASIAHCPNSNLSL 234
Cdd:cd01298   205 EYGVPLHIHLAETEDEVEESLEKYgkrP-----VEYLEELGLLGPDVVLAHCVWLTDEEIELLAETGTGVAHNPASNMKL 279

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039757181 235 SSGLLNVLEVLKHKVKIGLGTD-VAGGYSYSMLDAIRRAvmvsnvLLINKV---NEKNLTLKEVFRLATLGGSQALGLDs 310
Cdd:cd01298   280 ASGIAPVPEMLEAGVNVGLGTDgAASNNNLDMFEEMRLA------ALLQKLahgDPTALPAEEALEMATIGGAKALGLD- 352

                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1039757181 311 EIGNFEVGKEFDALLINPRASD-SPIDlfygdfvGDISEAViqkflYLGDDRNIEEVYVGGKQVV 374
Cdd:cd01298   353 EIGSLEVGKKADLILIDLDGPHlLPVH-------DPISHLV-----YSANGGDVDTVIVNGRVVM 405
PRK07228 PRK07228
5'-deoxyadenosine deaminase;
1-327 1.65e-57

5'-deoxyadenosine deaminase;


Pssm-ID: 180895 [Multi-domain]  Cd Length: 445  Bit Score: 193.68  E-value: 1.65e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039757181   1 MPGLVDTHIHAPQYAFAGSNVDLPLLEWLNKYTFPTEQrfrSTDvAEEVYTRV---VRRTLKNGTTTACYFGTI-HTDSS 76
Cdd:PRK07228   55 IPGLIQGHIHLCQTLFRGIADDLELLDWLKDRIWPLEA---AHD-AESMYYSAllgIGELIESGTTTIVDMESVhHTDSA 130

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039757181  77 LilaEITDKFGQRAFVGKVCMDLNDTVPE-YKETTEESVKETERFVSEMLQKNYPRVKPIVTPRFTLSCTETLMSELGNI 155
Cdd:PRK07228  131 F---EAAGESGIRAVLGKVMMDYGDDVPEgLQEDTEASLAESVRLLEKWHGADNGRIRYAFTPRFAVSCTEELLRGVRDL 207

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039757181 156 AKTHDLYIQSHISENREEIEAVKSlYPSYKNYTdVYDKNNLLTNKTVMAHGCYLSEEELNIFSERGASIAHCPNSNLSLS 235
Cdd:PRK07228  208 ADEYGVRIHTHASENRGEIETVEE-ETGMRNIH-YLDEVGLTGEDLILAHCVWLDEEEREILAETGTHVTHCPSSNLKLA 285

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039757181 236 SGLLNVLEVLKHKVKIGLGTDvaGGYSYSMLDA---IRRAVmvsnvlLINKVNEKN---LTLKEVFRLATLGGSQALGLD 309
Cdd:PRK07228  286 SGIAPVPDLLERGINVALGAD--GAPCNNTLDPfteMRQAA------LIQKVDRLGptaMPARTVFEMATLGGAKAAGFE 357

                         330
                  ....*....|....*...
gi 1039757181 310 SEIGNFEVGKEFDALLIN 327
Cdd:PRK07228  358 DEIGSLEEGKKADLAILD 375
Amidohydro_1 pfam01979
Amidohydrolase family; This family of enzymes are a a large metal dependent hydrolase ...
 1-373 3.12e-53

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: 179.62  E-value: 3.12e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039757181   1 MPGLVDTHIHAPQYAFAGSNVDLpllewlnkytfpteqrfrstDVAEEVYTRVVRRTLKNGTTTACYFGTIHTDSSLILA 80
Cdd:pfam01979   3 LPGLIDAHVHLEMGLLRGIPVPP--------------------EFAYEALRLGITTMLKSGTTTVLDMGATTSTGIEALL 62

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039757181  81 EITDK--FGQRAFVGKVCMDLNDTVPEYKETTEESVKETErfvsEMLQKNYPRVKPIVTPRFTLSCTETLMSELGNIAKT 158
Cdd:pfam01979  63 EAAEElpLGLRFLGPGCSLDTDGELEGRKALREKLKAGAE----FIKGMADGVVFVGLAPHGAPTFSDDELKAALEEAKK 138

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039757181 159 HDLYIQSHISENREEIEAVKSLYPS---YKNYTDVYDKNNLL-TNKTVMAHGCYLSEEELNIFSER--GASIAHCPNSNL 232
Cdd:pfam01979 139 YGLPVAIHALETKGEVEDAIAAFGGgieHGTHLEVAESGGLLdIIKLILAHGVHLSPTEANLLAEHlkGAGVAHCPFSNS 218

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039757181 233 SLSSGLLNVLEVLKHKVKIGLGTDVAG-GYSYSMLDAIRRAVmvsnvlLINKVNEKNLTLKEVFRLATLGGSQALGLDSE 311
Cdd:pfam01979 219 KLRSGRIALRKALEDGVKVGLGTDGAGsGNSLNMLEELRLAL------ELQFDPEGGLSPLEALRMATINPAKALGLDDK 292

                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1039757181 312 IGNFEVGKEFDALLINPRasdspidlfygdfvgdiseaVIQKFLYLGDDRNIEEVYVGGKQV 373
Cdd:pfam01979 293 VGSIEVGKDADLVVVDLD--------------------PLAAFFGLKPDGNVKKVIVKGKIV 334
PRK08393 PRK08393
N-ethylammeline chlorohydrolase; Provisional
 2-312 1.65e-46

N-ethylammeline chlorohydrolase; Provisional


Pssm-ID: 181411 [Multi-domain]  Cd Length: 424  Bit Score: 164.20  E-value: 1.65e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039757181   2 PGLVDTHIHAPQYAFAGSNVDLPLLEWLNKYTFPTEQRFRSTDVAEEVYTRVVRrTLKNGTTT--ACYFgtiHTDSsliL 79
Cdd:PRK08393   54 PGFINAHTHSPMVLLRGLADDVPLMEWLQNYIWPRERKLKRKDIYWGAYLGLLE-MIKSGTTTfvDMYF---HMEE---V 126

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039757181  80 AEITDKFGQRAFVGKVCMDLNDtvpeyKETTEESVKETERFVSEMLQKNYPRVKPIVTPRFTLSCTETLMSELGNIAKTH 159
Cdd:PRK08393  127 AKATLEVGLRGYLSYGMVDLGD-----EEKREKEIKETEKLMEFIEKLNSPRVHFVFGPHAPYTCSLALLKWVREKAREW 201

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039757181 160 DLYIQSHISENREEIEAVKSLYPsyKNYTDVYDKNNLLTNKTVMAHGCYLSEEELNIFSERGASIAHCPNSNLSLSSGLL 239
Cdd:PRK08393  202 NKLITIHLSETMDEIKQIREKYG--KSPVVLLDEIGFLNEDVIAAHGVWLSSRDIRILASAGVTVAHNPASNMKLGSGVM 279

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1039757181 240 NVLEVLKHKVKIGLGTDvaGGYSYSMLDAIRRAVMVSnvlLINKVNEKNLTL---KEVFRLATLGGSQALGLDSEI 312
Cdd:PRK08393  280 PLRKLLNAGVNVALGTD--GAASNNNLDMLREMKLAA---LLHKVHNLDPTIadaETVFRMATQNGAKALGLKAGV 350
PRK06038 PRK06038
N-ethylammeline chlorohydrolase; Provisional
 1-329 2.99e-38

N-ethylammeline chlorohydrolase; Provisional


Pssm-ID: 180363 [Multi-domain]  Cd Length: 430  Bit Score: 142.20  E-value: 2.99e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039757181   1 MPGLVDTHIHAPQYAFAGSNVDLPLLEWLNKYTFPTEQRFRstdvAEEVYTRVVRRTL---KNGTTT--ACYFGTIHTds 75
Cdd:PRK06038   54 MPGLVNTHTHAAMTLFRGYADDLPLAEWLNDHIWPAEAKLT----AEDVYAGSLLACLemiKSGTTSfaDMYFYMDEV-- 127

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039757181  76 slilAEITDKFGQRAFVGKVCMDLNDTvpeykETTEESVKETERFVSEMLQKNYPRVKPIVTPRFTLSCTETLMSELGNI 155
Cdd:PRK06038  128 ----AKAVEESGLRAALSYGMIDLGDD-----EKGEAELKEGKRFVKEWHGAADGRIKVMYGPHAPYTCSEEFLSKVKKL 198

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039757181 156 AKTHDLYIQSHISENREEIEAVKSLYPsyKNYTDVYDKNNLLTNKTVMAHGCYLSEEELNIFSERGASIAHCPNSNLSLS 235
Cdd:PRK06038  199 ANKDGVGIHIHVLETEAELNQMKEQYG--MCSVNYLDDIGFLGPDVLAAHCVWLSDGDIEILRERGVNVSHNPVSNMKLA 276

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039757181 236 SGLLNVLEVLKHKVKIGLGTD-VAGGYSYSMLDAIRRAVmvsnvlLINKVNEKNLTL---KEVFRLATLGGSQALGLDSe 311
Cdd:PRK06038  277 SGIAPVPKLLERGVNVSLGTDgCASNNNLDMFEEMKTAA------LLHKVNTMDPTAlpaRQVLEMATVNGAKALGINT- 349

                         330
                  ....*....|....*...
gi 1039757181 312 iGNFEVGKEFDALLINPR 329
Cdd:PRK06038  350 -GMLKEGYLADIIIVDMN 366
PRK06687 PRK06687
TRZ/ATZ family protein;
1-374 6.58e-37

TRZ/ATZ family protein;


Pssm-ID: 180657 [Multi-domain]  Cd Length: 419  Bit Score: 138.21  E-value: 6.58e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039757181   1 MPGLVDTHIHAPQYAFAGSNVDLPLLEWLNKYTFPTEQRFrSTDVAEEVYTRVVRRTLKNGTTTacyFGTIHTDSSLILA 80
Cdd:PRK06687   57 MPGLVNCHTHSAMTGLRGIRDDSNLHEWLNDYIWPAESEF-TPDMTTNAVKEALTEMLQSGTTT---FNDMYNPNGVDIQ 132

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039757181  81 EITDKFGQRafvGKVCMDLNDTVPEYKETTEESVKETERFVSEMLQKNYPRVKPIVTPRFTLSCTETLMSELGNIAKTHD 160
Cdd:PRK06687  133 QIYQVVKTS---KMRCYFSPTLFSSETETTAETISRTRSIIDEILKYKNPNFKVMVAPHSPYSCSRDLLEASLEMAKELN 209

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039757181 161 LYIQSHISENREEIEAVKSLYPsyKNYTDVYDKNNLLTNKTVMAHGCYLSEEELNIFSERGASIAHCPNSNLSLSSGLLN 240
Cdd:PRK06687  210 IPLHVHVAETKEESGIILKRYG--KRPLAFLEELGYLDHPSVFAHGVELNEREIERLASSQVAIAHNPISNLKLASGIAP 287

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039757181 241 VLEVLKHKVKIGLGTD-VAGGYSYSMLDAIRRAVMVSNvllINKVNEKNLTLKEVFRLATLGGSQALGLDSEIGNFEVGK 319
Cdd:PRK06687  288 IIQLQKAGVAVGIATDsVASNNNLDMFEEGRTAALLQK---MKSGDASQFPIETALKVLTIEGAKALGMENQIGSLEVGK 364

                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1039757181 320 EFDALLINPRASdspIDLFygdfvgdISEAVIQKFLYLGDDRNIEEVYVGGKQVV 374
Cdd:PRK06687  365 QADFLVIQPQGK---IHLQ-------PQENMLSHLVYAVKSSDVDDVYIAGEQVV 409
PRK09045 PRK09045
TRZ/ATZ family hydrolase;
1-322 4.23e-30

TRZ/ATZ family hydrolase;


Pssm-ID: 236366 [Multi-domain]  Cd Length: 443  Bit Score: 120.02  E-value: 4.23e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039757181   1 MPGLVDTHIHAPQYAFAGSNVDLPLLEWLNKYTFPTEQRFRSTD---------VAEevytrvvrrTLKNGTTTA--CYFg 69
Cdd:PRK09045   65 IPGLINAHTHAAMSLLRGLADDLPLMTWLQDHIWPAEGAWVSEEfvrdgtllaIAE---------MLRGGTTCFndMYF- 134

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039757181  70 tiHTDsslILAEITDKFGQRAFVGKVCMDlndtVP-EYKETTEES----VKETERFvsemlqKNYPRVKPIVTPR--FTL 142
Cdd:PRK09045  135 --FPE---AAAEAAHQAGMRAQIGMPVLD----FPtAWASDADEYlakgLELHDQW------RHHPLISTAFAPHapYTV 199

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039757181 143 ScTETLmSELGNIAKTHDLYIQSHISENREEIEAvkslypSYKNY----TDVYDKNNLLTNKTVMAHGCYLSEEELNIFS 218
Cdd:PRK09045  200 S-DENL-ERIRTLAEQLDLPIHIHLHETAQEIAD------SLKQHgqrpLARLARLGLLGPRLIAVHMTQLTDAEIALLA 271

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039757181 219 ERGASIAHCPNSNLSLSSGLLNVLEVLKHKVKIGLGTD-VAGGYSYSMLDAIRRAVMVSnvllinkvneKNLTL------ 291
Cdd:PRK09045  272 ETGCSVVHCPESNLKLASGFCPVAKLLQAGVNVALGTDgAASNNDLDLFGEMRTAALLA----------KAVAGdatalp 341

                         330       340       350
                  ....*....|....*....|....*....|..
gi 1039757181 292 -KEVFRLATLGGSQALGLDSEIGNFEVGKEFD 322
Cdd:PRK09045  342 aHTALRMATLNGARALGLDDEIGSLEPGKQAD 373
PRK15493 PRK15493
bifunctional S-methyl-5'-thioadenosine deaminase/S-adenosylhomocysteine deaminase;
1-374 9.51e-28

bifunctional S-methyl-5'-thioadenosine deaminase/S-adenosylhomocysteine deaminase;


Pssm-ID: 185390 [Multi-domain]  Cd Length: 435  Bit Score: 113.23  E-value: 9.51e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039757181   1 MPGLVDTHIHAPQYAFAGSNVDLPLLEWLNKYTFPTEQRFrSTDVAEEVYTRVVRRTLKNGTTT-ACYFGTIHTDSSLIL 79
Cdd:PRK15493   58 LPGLVNTHTHVVMSLLRGIGDDMLLQPWLETRIWPLESQF-TPELAVASTELGLLEMVKSGTTSfSDMFNPIGVDQDAIM 136

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039757181  80 aEITDKFGQRAFVGKVCMDLNDtvpeyKETTEESVKETERFVSEMLQKNyPRVKPIVTPRFTLSCTETLMSELGNIAKTH 159
Cdd:PRK15493  137 -ETVSRSGMRAAVSRTLFSFGT-----KEDEKKAIEEAEKYVKRYYNES-GMLTTMVAPHSPYTCSTELLEECARIAVEN 209

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039757181 160 DLYIQSHISENREEIEAVKSLYPsyKNYTDVYDKNNLLTNKTVMAHGCYLSEEELNIFSERGASIAHCPNSNLSLSSGLL 239
Cdd:PRK15493  210 QTMVHIHLSETEREVRDIEAQYG--KRPVEYAASCGLFKRPTVIAHGVVLNDNERAFLAEHDVRVAHNPNSNLKLGSGIA 287

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039757181 240 NVLEVLKHKVKIGLGTD-VAGGYSYSMLDAIRRAVMVSNVLlinKVNEKNLTLKEVFRLATLGGSQALGLdSEIGNFEVG 318
Cdd:PRK15493  288 NVKAMLEAGIKVGIATDsVASNNNLDMFEEMRIATLLQKGI---HQDATALPVETALTLATKGAAEVIGM-KQTGSLEVG 363

                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1039757181 319 KEFDALLINPraSDSPidlfygdfVGDISEAVIQKFLYLGDDRNIEEVYVGGKQVV 374
Cdd:PRK15493  364 KCADFITIDP--SNKP--------HLQPADEVLSHLVYAASGKDISDVIINGKRVV 409
PRK06380 PRK06380
metal-dependent hydrolase; Provisional
 1-371 6.45e-24

metal-dependent hydrolase; Provisional


Pssm-ID: 180548 [Multi-domain]  Cd Length: 418  Bit Score: 102.27  E-value: 6.45e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039757181   1 MPGLVDTHIHAPQYAFAGSNVDLPLLEWLNKyTFpteqRFRSTDVAEEVYTRV---VRRTLKNGTTTacyFGTIHTDSSL 77
Cdd:PRK06380   53 MPGLINTHAHVGMTASKGLFDDVDLEEFLMK-TF----KYDSKRTREGIYNSAklgMYEMINSGITA---FVDLYYSEDI 124

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039757181  78 IlAEITDKFGQRAFVGKVCMDlndtvPEYKETTEESVKETERFVSEMLQKNYprVKPIVTPRFTLSCTETLMSELGNIAK 157
Cdd:PRK06380  125 I-AKAAEELGIRAFLSWAVLD-----EEITTQKGDPLNNAENFIREHRNEEL--VTPSIGVQGIYVANDETYLKAKEIAE 196

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039757181 158 THDLYIQSHISENREEIeavkslYPSYKNY----TDVYDKNNLLTNKTVMAHGCYLSEEELNIFSERGASIAHCPNSNLS 233
Cdd:PRK06380  197 KYDTIMHMHLSETRKEV------YDHVKRTgerpVEHLEKIGFLNSKLIAAHCVWATYHEIKLLSKNGVKVSWNSVSNFK 270

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039757181 234 LSSGLLNVL-EVLKHKVKIGLGTDVAGG-YSYSMLDAIR-RAVMVSNvlliNKVNEKNLTLKEVFRLATLGGSQALGLDS 310
Cdd:PRK06380  271 LGTGGSPPIpEMLDNGINVTIGTDSNGSnNSLDMFEAMKfSALSVKN----ERWDASIIKAQEILDFATINAAKALELNA 346

                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1039757181 311 eiGNFEVGKEFDALLINPRASdSPIDLFYGDFVGDIseaviqkfLYLGDDRNIEEVYVGGK 371
Cdd:PRK06380  347 --GSIEVGKLADLVILDARAP-NMIPTRKNNIVSNI--------VYSLNPLNVDHVIVNGK 396
PRK08203 PRK08203
hydroxydechloroatrazine ethylaminohydrolase; Reviewed
 1-374 1.27e-19

hydroxydechloroatrazine ethylaminohydrolase; Reviewed


Pssm-ID: 236184 [Multi-domain]  Cd Length: 451  Bit Score: 89.91  E-value: 1.27e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039757181   1 MPGLVDTHIHAPQY---AFAGSnVDLPLLEWLnKYTFPTEQRFrsTDVAEEVYTRV-VRRTLKNGTTTAC---Y-FGTIH 72
Cdd:PRK08203   58 TPGLVNTHHHFYQTltrALPAA-QDAELFPWL-TTLYPVWARL--TPEMVRVATQTaLAELLLSGCTTSSdhhYlFPNGL 133

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039757181  73 TDSSLILAEITDKFGQRAFVGKVCMDLN--------DTVpeyKETTEESVKETERFVSE--------MLQknyprvkpI- 135
Cdd:PRK08203  134 RDALDDQIEAAREIGMRFHATRGSMSLGesdgglppDSV---VEDEDAILADSQRLIDRyhdpgpgaMLR--------Ia 202

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039757181 136 VTPRFTLSCTETLMSELGNIAKTHDLYIQSHISENREEIEAVKSLY---PsyknyTDVYDKNNLLTNKTVMAHGCYLSEE 212
Cdd:PRK08203  203 LAPCSPFSVSRELMRESAALARRLGVRLHTHLAETLDEEAFCLERFgmrP-----VDYLEDLGWLGPDVWLAHCVHLDDA 277

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039757181 213 ELNIFSERGASIAHCPNSNLSLSSGLLNVLEVLKHKVKIGLGTD-VAGGYSYSMLDAIRRAvmvsnvLLINKV--NEKNL 289
Cdd:PRK08203  278 EIARLARTGTGVAHCPCSNMRLASGIAPVRELRAAGVPVGLGVDgSASNDGSNLIGEARQA------LLLQRLryGPDAM 351

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039757181 290 TLKEVFRLATLGGSQALGLDsEIGNFEVGKEFD-AL--LINPRASDSpidlfygdfvGDISEAviqkfLYLGDDRNIEEV 366
Cdd:PRK08203  352 TAREALEWATLGGARVLGRD-DIGSLAPGKLADlALfdLDELRFAGA----------HDPVAA-----LVLCGPPRADRV 415


                  ....*...
gi 1039757181 367 YVGGKQVV 374
Cdd:PRK08203  416 MVGGRWVV 423
PRK08204 PRK08204
hypothetical protein; Provisional
 1-371 8.89e-19

hypothetical protein; Provisional


Pssm-ID: 181288 [Multi-domain]  Cd Length: 449  Bit Score: 87.37  E-value: 8.89e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039757181   1 MPGLVDTHIHAPQYAFAGSNVDLPLLEWLNKYTFPTEQRFRSTDVaeEVYTRV-VRRTLKNGTTTACYFGTI-----HTD 74
Cdd:PRK08204   56 MPGLVDTHRHTWQSVLRGIGADWTLQTYFREIHGNLGPMFRPEDV--YIANLLgALEALDAGVTTLLDWSHInnspeHAD 133

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039757181  75 SSLI-LAEItdkfGQRA--FVGKVcmdlNDTVPEYKETTEESVKETERFVSEMLQKNYPRVK---PIVTPRFtlSCTETL 148
Cdd:PRK08204  134 AAIRgLAEA----GIRAvfAHGSP----GPSPYWPFDSVPHPREDIRRVKKRYFSSDDGLLTlglAIRGPEF--SSWEVA 203

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039757181 149 MSELGnIAKTHDLYIQSHISenreeieavksLYPSYKNYTDV--YDKNNLLTNKTVMAHGCYLSEEELNIFSERGASIAH 226
Cdd:PRK08204  204 RADFR-LARELGLPISMHQG-----------FGPWGATPRGVeqLHDAGLLGPDLNLVHGNDLSDDELKLLADSGGSFSV 271

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039757181 227 CPNSNLSLSSGLLNVLEVLKHKVKIGLGTDVAGGYSYSMLDAIR------RAVMVSNVLLINKV--NEKNLTLKEVFRLA 298
Cdd:PRK08204  272 TPEIEMMMGHGYPVTGRLLAHGVRPSLGVDVVTSTGGDMFTQMRfalqaeRARDNAVHLREGGMppPRLTLTARQVLEWA 351

                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1039757181 299 TLGGSQALGLDSEIGNFEVGKEFDALLINPRAsdspIDLFYgdfVGDISEAVIQkflyLGDDRNIEEVYVGGK 371
Cdd:PRK08204  352 TIEGARALGLEDRIGSLTPGKQADLVLIDATD----LNLAP---VHDPVGAVVQ----SAHPGNVDSVMVAGR 413
PRK08418 PRK08418
metal-dependent hydrolase;
1-374 2.82e-17

metal-dependent hydrolase;


Pssm-ID: 181419 [Multi-domain]  Cd Length: 408  Bit Score: 82.71  E-value: 2.82e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039757181   1 MPGLVDTHIHapqYAFAGSNVDL---PLLEWLNKYTFPTEQRFRSTDvaEEVYTRVVRRTLKNGTTTacyFGTIhtDSSL 77
Cdd:PRK08418   57 LPAFINPHTH---LEFSANKTTLdygDFIPWLGSVINHREDLLEKCK--GALIQQAINEMLKSGVGT---IGAI--SSFG 126

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039757181  78 ILAEITDKFGQRA-FVGKVCMDLNDTVPEYKETTEESVKETERFVSEMLqknyprvKPIVTPRFTLSCTETLMSELGNIA 156
Cdd:PRK08418  127 IDLEICAKSPLRVvFFNEILGSNASAVDELYQDFLARFEESKKFKSKKF-------IPAIAIHSPYSVHPILAKKALQLA 199

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039757181 157 KTHDLYIQSHISENREEIEAV-------KSLYPSY-KNYTDVYDKNNLL----TNKTVMAHGCYLSEEELNIFSERGASI 224
Cdd:PRK08418  200 KKENLLVSTHFLESKAEREWLeeskgwfKKFFEKFlKEPKPLYTPKEFLelfkGLRTLFTHCVYASEEELEKIKSKNASI 279

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039757181 225 AHCPNSNLSLSSGLLNVLEVLKHKVKIGLGTD-VAGGYSYSMLDAIRRAVMVSNvllinkvNEKNLTL-KEVFRLATLGG 302
Cdd:PRK08418  280 THCPFSNRLLSNKALDLEKAKKAGINYSIATDgLSSNISLSLLDELRAALLTHA-------NMPLLELaKILLLSATRYG 352

                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1039757181 303 SQALGLDSeiGNFEVGKEFDALLINprasdspidlfYGDFVGDISEAVIQKFLYlgdDRNIEEVYVGGKQVV 374
Cdd:PRK08418  353 AKALGLNN--GEIKEGKDADLSVFE-----------LPEECTKKEQLPLQFILH---AKEVKKLFIGGKEVK 408
metallo-dependent_hydrolases cd01292
Superfamily of metallo-dependent hydrolases (also called amidohydrolase superfamily) is a ...
 4-305 3.94e-17

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: 80.46  E-value: 3.94e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039757181   4 LVDTHIHAPQYAFAGSNVDLPLLEWLNKYTFPTEQRFRstdvaeevytRVVRRTLKNGTTTACYFGTIHTDS------SL 77
Cdd:cd01292     1 FIDTHVHLDGSALRGTRLNLELKEAEELSPEDLYEDTL----------RALEALLAGGVTTVVDMGSTPPPTttkaaiEA 70

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039757181  78 ILAEITDKFGQRAFVGKVCMDlndtvpEYKETTEESVKETERFVSEMLQKNYPRVKPIVTPRFTLSCTETLMSELGnIAK 157
Cdd:cd01292    71 VAEAARASAGIRVVLGLGIPG------VPAAVDEDAEALLLELLRRGLELGAVGLKLAGPYTATGLSDESLRRVLE-EAR 143

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039757181 158 THDLYIQSHISENREEIEAVKSLYpsyknytdvydKNNLLTNKTVMAHGCYLSEEELNIFSERGASIAHCPNSNLSLSSG 237
Cdd:cd01292   144 KLGLPVVIHAGELPDPTRALEDLV-----------ALLRLGGRVVIGHVSHLDPELLELLKEAGVSLEVCPLSNYLLGRD 212

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1039757181 238 LLN---VLEVLKHKVKIGLGTDVAGGYSYSMLDAIRRAVMVSNVLlinkvnekNLTLKEVFRLATLGGSQA 305
Cdd:cd01292   213 GEGaeaLRRLLELGIRVTLGTDGPPHPLGTDLLALLRLLLKVLRL--------GLSLEEALRLATINPARA 275
Met_dep_hydrolase_D cd01312
Metallo-dependent hydrolases, subgroup D is part of the superfamily of metallo-dependent ...
 1-322 5.67e-17

Metallo-dependent hydrolases, subgroup D is part of the superfamily of metallo-dependent hydrolases, 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 function of this subgroup is unknown.


Pssm-ID: 238637 [Multi-domain]  Cd Length: 381  Bit Score: 81.34  E-value: 5.67e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039757181   1 MPGLVDTHIHapqYAFAGSNVDL---PLLEWLNkyTFPTEQRFRSTDVAEEVYTRVVRRTLKNGTTTAcyfGTIHTDssL 77
Cdd:cd01312    30 LPGLINAHTH---LEFSANVAQFtygRFRAWLL--SVINSRDELLKQPWEEAIRQGIRQMLESGTTSI---GAISSD--G 99

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039757181  78 ILAEITDKFGQRAFVGKVCMDLNDTVPEYKETTEEsvketERFVSEMLQKNyPRVKPIVTPRFTLSCTETLMSELGNIAK 157
Cdd:cd01312   100 SLLPALASSGLRGVFFNEVIGSNPSAIDFKGETFL-----ERFKRSKSFES-QLFIPAISPHAPYSVHPELAQDLIDLAK 173

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039757181 158 THDLYIQSHISENREEIEavksLYPSYKNYTDVYDKNNL--------------------LTNKTVMAHGCYLSEEELNIF 217
Cdd:cd01312   174 KLNLPLSTHFLESKEERE----WLEESKGWFKHFWESFLklpkpkklataidfldmlggLGTRVSFVHCVYANLEEAEIL 249

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039757181 218 SERGASIAHCPNSNLSLSSGLLNVLEVLKHKVKIGLGTD-VAGGYSYSMLDAIRravmvSNVLLINKVNEKNLTlKEVFR 296
Cdd:cd01312   250 ASRGASIALCPRSNRLLNGGKLDVSELKKAGIPVSLGTDgLSSNISLSLLDELR-----ALLDLHPEEDLLELA-SELLL 323

                         330       340
                  ....*....|....*....|....*.
gi 1039757181 297 LATLGGSQALGLdsEIGNFEVGKEFD 322
Cdd:cd01312   324 MATLGGARALGL--NNGEIEAGKRAD 347
PRK12393 PRK12393
amidohydrolase; Provisional
 2-374 2.57e-14

amidohydrolase; Provisional


Pssm-ID: 237088 [Multi-domain]  Cd Length: 457  Bit Score: 73.95  E-value: 2.57e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039757181   2 PGLVDTHIHAPQYAFAG--SNVDLPLLEWLNKYTFP-----TEQRFRstdvaeeVYTRV-VRRTLKNGTTTAC-----YF 68
Cdd:PRK12393   59 PGWVNTHHHLFQSLLKGvpAGINQSLTAWLAAVPYRfrarfDEDLFR-------LAARIgLVELLRSGCTTVAdhhylYH 131

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039757181  69 GTIHTDSSLILAEITDKFGQRaFVgkVC---------MDLNDTVPEYKETTEESVKETERFVSEMLQKNYPRVKPIV--- 136
Cdd:PRK12393  132 PGMPFDTGDILFDEAEALGMR-FV--LCrggatqtrgDHPGLPTALRPETLDQMLADVERLVSRYHDASPDSLRRVVvap 208

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039757181 137 -TPRFTLscTETLMSELGNIAKTHDLYIQSHISENREEIEAVKSLYPsyKNYTDVYDKNNLLTNKTVMAHGCYLSEEELN 215
Cdd:PRK12393  209 tTPTFSL--PPELLREVARAARGMGLRLHSHLSETVDYVDFCREKYG--MTPVQFVAEHDWLGPDVWFAHLVKLDAEEIA 284

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039757181 216 IFSERGASIAHCPNSNLSLSSGLLNVLEVLKHKVKIGLGTD-VAGGYSYSMLDAIRRAVMVSNVLlinkVNEKNLTLKEV 294
Cdd:PRK12393  285 LLAQTGTGIAHCPQSNGRLGSGIAPALAMEAAGVPVSLGVDgAASNESADMLSEAHAAWLLHRAE----GGADATTVEDV 360

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039757181 295 FRLATLGGSQALGLDsEIGNFEVGKEFD-AL--LINPRasdspidlFYGdfVGDISEAVIQKflylGDDRNIEEVYVGGK 371
Cdd:PRK12393  361 VHWGTAGGARVLGLD-AIGTLAVGQAADlAIydLDDPR--------FFG--LHDPAIAPVAC----GGPAPVKALLVNGR 425


                  ...
gi 1039757181 372 QVV 374
Cdd:PRK12393  426 PVV 428
PRK06151 PRK06151
N-ethylammeline chlorohydrolase; Provisional
 1-374 2.58e-13

N-ethylammeline chlorohydrolase; Provisional


Pssm-ID: 180428 [Multi-domain]  Cd Length: 488  Bit Score: 70.84  E-value: 2.58e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039757181   1 MPGLVDTHIHapqyafagSNVDLPLL------EWLNKYTFP---TEQRFRSTDVAEEV---YTRVVRRTLKNGTTTACYF 68
Cdd:PRK06151   56 GPGFIDLDAL--------SDLDTTILgldngpGWAKGRVWSrdyVEAGRREMYTPEELafqKRYAFAQLLRNGITTAMPI 127

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039757181  69 GTI-------HTDSSLILAEITDKFGQRAFVGKVCM--------DLNDTVPEYKETTEESVKETERFVSEMLQKNYPRVK 133
Cdd:PRK06151  128 ASLfyrqwaeTYAEFAAAAEAAGRLGLRVYLGPAYRsggsvleaDGSLEVVFDEARGLAGLEEAIAFIKRVDGAHNGLVR 207

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039757181 134 PIVTPRFTLSCTETLMSELGNIAKTHDLYIQSHISENREEIEAVKSLYPsyKNYTDVYDKNNLLTNKTVMAHGCYLSE-- 211
Cdd:PRK06151  208 GMLAPDRIETCTVDLLRRTAAAARELGCPVRLHCAQGVLEVETVRRLHG--TTPLEWLADVGLLGPRLLIPHATYISGsp 285

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039757181 212 -------EELNIFSERGASIAHCPNSNLSLSSGLLNVLEVLKHKVKIGLGTDVAggysysmldairRAVMVSNV---LLI 281
Cdd:PRK06151  286 rlnysggDDLALLAEHGVSIVHCPLVSARHGSALNSFDRYREAGINLALGTDTF------------PPDMVMNMrvgLIL 353

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039757181 282 NKVNEKNLT---LKEVFRLATLGGSQALGLDsEIGNFEVGKEFDALLINPRasdspiDLFYGDFVGDISEAVIQkflylG 358
Cdd:PRK06151  354 GRVVEGDLDaasAADLFDAATLGGARALGRD-DLGRLAPGAKADIVVFDLD------GLHMGPVFDPIRTLVTG-----G 421

                         410
                  ....*....|....*.
gi 1039757181 359 DDRNIEEVYVGGKQVV 374
Cdd:PRK06151  422 SGRDVRAVFVDGRVVM 437
PRK07203 PRK07203
putative aminohydrolase SsnA;
1-279 2.82e-12

putative aminohydrolase SsnA;


Pssm-ID: 235963 [Multi-domain]  Cd Length: 442  Bit Score: 67.65  E-value: 2.82e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039757181   1 MPGLVDTHIHApqY-AFA-GSNVDLP----LLEWLNKYTFpteqRFRSTDVAEEVYTRVVRRTL---KNGTTTA----CY 67
Cdd:PRK07203   58 MPGLINSHNHI--YsGLArGMMANIPpppdFISILKNLWW----RLDRALTLEDVYYSALICSLeaiKNGVTTVfdhhAS 131

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039757181  68 FGTIhTDSSLILAEITDKFGQRafvGKVCMDLNDTVPEykETTEESVKETERFVSEMLQKNYPRVKPIVT--PRFTLScT 145
Cdd:PRK07203  132 PNYI-GGSLFTIADAAKKVGLR---AMLCYETSDRDGE--KELQEGVEENIRFIKHIDEAKDDMVEAMFGlhASFTLS-D 204

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039757181 146 ETLmSELGNIAKTHDLYIQSHISENREEIEAvkSLYPSYKNYTDVYDKNNLLTNKTVMAHGCYLSEEELNIFSERGASIA 225
Cdd:PRK07203  205 ATL-EKCREAVKETGRGYHIHVAEGIYDVSD--SHKKYGKDIVERLADFGLLGEKTLAAHCIYLSDEEIDLLKETDTFVV 281

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1039757181 226 HCPNSNLSLSSGLLNVLEVLKHKVKIGLGTDvagGYSYSMLDAIRravmVSNVL 279
Cdd:PRK07203  282 HNPESNMGNAVGYNPVLEMIKNGILLGLGTD---GYTSDMFESYK----VANFK 328
HutI COG1228
Imidazolonepropionase or related amidohydrolase [Secondary metabolites biosynthesis, transport ...
 1-374 1.03e-10

Imidazolonepropionase or related amidohydrolase [Secondary metabolites biosynthesis, transport and catabolism];


Pssm-ID: 440841 [Multi-domain]  Cd Length: 386  Bit Score: 62.67  E-value: 1.03e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039757181   1 MPGLVDTHIHapqYAFAGSNVDlpllewlnkyTFPTEQRFRSTDVAEEVYTRVVRRTLKNGTTTACyfgtIHTDSSLILA 80
Cdd:COG1228    64 LPGLIDAHTH---LGLGGGRAV----------EFEAGGGITPTVDLVNPADKRLRRALAAGVTTVR----DLPGGPLGLR 126

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039757181  81 EITDK------FGQRAFVGKVCMDLNDTVPEYketteeSVKETERFVSEMLQKNYPRVKPIVT---PRFTLSCTETLMSE 151
Cdd:COG1228   127 DAIIAgeskllPGPRVLAAGPALSLTGGAHAR------GPEEARAALRELLAEGADYIKVFAEggaPDFSLEELRAILEA 200

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039757181 152 lgniAKTHDLYIQSHISENREEIEAVKSlypsyknytdvydknnlltNKTVMAHGCYLSEEELNIFSERGASI------- 224
Cdd:COG1228   201 ----AHALGLPVAAHAHQADDIRLAVEA-------------------GVDSIEHGTYLDDEVADLLAEAGTVVlvptlsl 257

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039757181 225 --AHCPNSNLSLSSGLLNVLEV--------LKHKVKIGLGTDVAGGYS--YSMLDAIRRAVMVsnvllinkvnekNLTLK 292
Cdd:COG1228   258 flALLEGAAAPVAAKARKVREAalanarrlHDAGVPVALGTDAGVGVPpgRSLHRELALAVEA------------GLTPE 325

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039757181 293 EVFRLATLGGSQALGLDSEIGNFEVGKEFDALLINprasdspidlfyGDFVGDISeaviqkflYLgddRNIEEVYVGGKQ 372
Cdd:COG1228   326 EALRAATINAAKALGLDDDVGSLEPGKLADLVLLD------------GDPLEDIA--------YL---EDVRAVMKDGRV 382


                  ..
gi 1039757181 373 VV 374
Cdd:COG1228   383 VD 384
archeal_chlorohydrolases cd01305
Predicted chlorohydrolases. These metallo-dependent hydrolases from archea are part of the ...
 1-303 2.00e-09

Predicted chlorohydrolases. These metallo-dependent hydrolases from archea are part of the superfamily of metallo-dependent hydrolases, a large group of proteins that show conservation in their 3-dimensional fold (TIM barrel) and in details of their active site. They 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. Some members of this subgroup are predicted to be chlorohyrolases.


Pssm-ID: 238630 [Multi-domain]  Cd Length: 263  Bit Score: 57.80  E-value: 2.00e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039757181   1 MPGLVDTHIHAPQYAFAGSNVDLPLLE---WLN--KYTFPTEQRFRSTDVAEEvytRVVRRTLKNGTTTACYFGTIHTDS 75
Cdd:cd01305     3 IPALVNAHTHLGDSAIKEVGDGLPLDDlvaPPDglKHRLLAQADDRELAEAMR---KVLRDMRETGIGAFADFREGGVEG 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039757181  76 SLILAEITDKFgqrAFVGKVCMDlNDTVPEYKETTEEsvketerfVSEMLQKNYPRvkpivtprftlsctETLMSELGNI 155
Cdd:cd01305    80 IELLRRALGKL---PVPFEVILG-RPTEPDDPEILLE--------VADGLGLSSAN--------------DVDLEDILEL 133

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039757181 156 AKTHDLYIQSHISENRE-----EIEAVKSLYPsyknytdvydknNLLTnktvmaHGCYLSEEELNIFSERGASIAHCPNS 230
Cdd:cd01305   134 LRRRGKLFAIHASETREsvgmtDIERALDLEP------------DLLV------HGTHLTDEDLELVRENGVPVVLCPRS 195

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1039757181 231 NLSLSSGLLNVLEVLKHKVKIGLGTDVAGGYSYSMLDAIRRAVMVSNVLliNKVNEknltlKEVFRLATLGGS 303
Cdd:cd01305   196 NLYFGVGIPPVAELLKLGIKVLLGTDNVMVNEPDMWAEMEFLAKYSRLQ--GYLSP-----LEILRMATVNAA 261
Met_dep_hydrolase_E cd01313
Metallo-dependent hydrolases, subgroup D is part of the superfamily of metallo-dependent ...
 166-371 7.47e-09

Metallo-dependent hydrolases, subgroup D is part of the superfamily of metallo-dependent hydrolases, 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 function of this subgroup is unknown.


Pssm-ID: 238638 [Multi-domain]  Cd Length: 418  Bit Score: 57.08  E-value: 7.47e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039757181 166 HISENREEIEAVksLYPSYKNYTDVYDKNNLLTNKTVMAHGCYLSEEELNIFSERGASIAHCPNSNLSLSSGLLNVLEVL 245
Cdd:cd01313   225 HLAEQPKEVDDC--LAAHGRRPVELLLDHGHLDARWCLVHATHLTDNETLLLGRSGAVVGLCPTTEANLGDGIFPAAALL 302

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039757181 246 KHKVKIGLGTDVAGG-----------YSYSMLDAIRravmvsNVLlinkVNEKNLTLKEVFRLATLGGSQALGLDSeiGN 314
Cdd:cd01313   303 AAGGRIGIGSDSNARidlleelrqleYSQRLRDRAR------NVL----ATAGGSSARALLDAALAGGAQALGLAT--GA 370

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1039757181 315 FEVGKEFDALLInprASDSPidlfygDFVGDISEAVIQKFLYLGDDRNIEEVYVGGK 371
Cdd:cd01313   371 LEAGARADLLSL---DLDHP------SLAGALPDTLLDAWVFAAGDREVRDVVVGGR 418
Amidohydro_3 pfam07969
Amidohydrolase family;
241-374 6.91e-06

Amidohydrolase family;


Pssm-ID: 400360 [Multi-domain]  Cd Length: 464  Bit Score: 47.91  E-value: 6.91e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039757181 241 VLEVLKHKVKIGLGTDVAGGySYSMLDAIRRAVM-----VSNVLLINKVneknLTLKEVFRLATLGGSQALGLDSEIGNF 315
Cdd:pfam07969 351 VKELLNAGVKVALGSDAPVG-PFDPWPRIGAAVMrqtagGGEVLGPDEE----LSLEEALALYTSGPAKALGLEDRKGTL 425

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1039757181 316 EVGKEFDALLINprasdspIDLFygdfvgDISEAVIqkflylgDDRNIEEVYVGGKQVV 374
Cdd:pfam07969 426 GVGKDADLVVLD-------DDPL------TVDPPAI-------ADIRVRLTVVDGRVVY 464
PRK07213 PRK07213
chlorohydrolase; Provisional
 166-330 1.03e-05

chlorohydrolase; Provisional


Pssm-ID: 235969 [Multi-domain]  Cd Length: 375  Bit Score: 46.95  E-value: 1.03e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039757181 166 HISENREEIEAVKSLYpsykNYTDVYDKNNLLTNKTVMAHGCYLSEEELNIFSERGASIAHCPNSNLSLSSGLLNVLEVL 245
Cdd:PRK07213  198 HAAEHKGSVEYSLEKY----GMTEIERLINLGFKPDFIVHATHPSNDDLELLKENNIPVVVCPRANASFNVGLPPLNEML 273

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039757181 246 KHKVKIGLGTDVAGGYSYSM---LDAIRRAVmvsnvllinkvnekNLTLKEVFRLATLGGSQALGLDsEIGNFEVGKEFD 322
Cdd:PRK07213  274 EKGILLGIGTDNFMANSPSIfreMEFIYKLY--------------HIEPKEILKMATINGAKILGLI-NVGLIEEGFKAD 338


                  ....*...
gi 1039757181 323 ALLINPRA 330
Cdd:PRK07213  339 FTFIKPTN 346
Imidazolone-5PH cd01296
Imidazolonepropionase/imidazolone-5-propionate hydrolase (Imidazolone-5PH) catalyzes the third ...
 203-353 5.25e-04

Imidazolonepropionase/imidazolone-5-propionate hydrolase (Imidazolone-5PH) catalyzes the third step in the histidine degradation pathway, the hydrolysis of (S)-3-(5-oxo-4,5-dihydro-3H-imidazol-4-yl)propanoate to N-formimidoyl-L-glutamate. In bacteria, the enzyme is part of histidine utilization (hut) operon.


Pssm-ID: 238621 [Multi-domain]  Cd Length: 371  Bit Score: 41.86  E-value: 5.25e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039757181 203 MAHGCYLSEEELNIFSERGASIAHCPNSNLSLSSGLLNVLEVLKHKVKIGLGTDVAGGySY---SMLDAIRRAVmvsnvl 279
Cdd:cd01296   233 ADHLEHTSDEGIAALAEAGTVAVLLPGTAFSLRETYPPARKLIDAGVPVALGTDFNPG-SSptsSMPLVMHLAC------ 305

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1039757181 280 linkVNEKnLTLKEVFRLATLGGSQALGLDSEIGNFEVGKEFDALLINpraSDSPIDLFYgDFVGDISEAVIQK 353
Cdd:cd01296   306 ----RLMR-MTPEEALTAATINAAAALGLGETVGSLEVGKQADLVILD---APSYEHLAY-RFGVNLVEYVIKN 370
nagA PRK11170
N-acetylglucosamine-6-phosphate deacetylase; Provisional
 259-319 3.04e-03

N-acetylglucosamine-6-phosphate deacetylase; Provisional


Pssm-ID: 183010  Cd Length: 382  Bit Score: 39.19  E-value: 3.04e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1039757181 259 GGYSYSMLDAIRravmvsnvlliNKVNEKNLTLKEVFRLATLGGSQALGLDSEIGNFEVGK 319
Cdd:PRK11170  307 SGSALTMIEAVR-----------NLVEHVGIALDEALRMATLYPARAIGVDKRLGSIEAGK 356
Met_dep_hydrolase_A cd01299
Metallo-dependent hydrolases, subgroup A is part of the superfamily of metallo-dependent ...
 246-330 3.84e-03

Metallo-dependent hydrolases, subgroup A is part of the superfamily of metallo-dependent hydrolases, 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 function of this subgroup is unknown.


Pssm-ID: 238624 [Multi-domain]  Cd Length: 342  Bit Score: 38.81  E-value: 3.84e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039757181 246 KHKVKIGLGTD-----VAGGYSYSMLdairrAVMVsnvllinkvnEKNLTLKEVFRLATLGGSQALGLDSEIGNFEVGKE 320
Cdd:cd01299   261 KAGVKIAFGTDagfpvPPHGWNAREL-----ELLV----------KAGGTPAEALRAATANAAELLGLSDELGVIEAGKL 325

                          90
                  ....*....|..
gi 1039757181 321 FDALLI--NPRA 330
Cdd:cd01299   326 ADLLVVdgDPLE 337
PRK09229 PRK09229
N-formimino-L-glutamate deiminase; Validated
 295-374 7.46e-03

N-formimino-L-glutamate deiminase; Validated


Pssm-ID: 236420 [Multi-domain]  Cd Length: 456  Bit Score: 38.29  E-value: 7.46e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039757181 295 FRLATLGGSQALGLDseIGNFEVGKEFDALLINPrasDSPidlfygDFVGDISEAVIQKFLYLGDDRNIEEVYVGGKQVV 374
Cdd:PRK09229  363 FDAALAGGAQALGRA--IGGLAVGARADLVVLDL---DHP------ALAGREGDALLDRWVFAGGDAAVRDVWVAGRWVV 431
 
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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