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Conserved domains on  [gi|1034671998|ref|XP_016870829|]
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guanine deaminase isoform X13 [Homo sapiens]

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 ...
 1-274 3.27e-146

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: 417.45  E-value: 3.27e-146
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034671998   1 MDLNDtfPEYK-ETTEESIKETERFVSEMLQKnYSRVKPIVTPRFSLSCSETLMGELGNIAKT-RDLHIQSHISENRDEV 78
Cdd:cd01303   160 MDRNA--PEYYrDTAESSYRDTKRLIERWHGK-SGRVKPAITPRFAPSCSEELLAALGKLAKEhPDLHIQTHISENLDEI 236

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034671998  79 EAVKNLYPSYKNYTSVYDKNNLLTNKTVMAHGCYLSAEELNVFHERGASIAHCPNSNLSLSSGFLNVLEVLKHEVKIGLG 158
Cdd:cd01303   237 AWVKELFPGARDYLDVYDKYGLLTEKTVLAHCVHLSEEEFNLLKERGASVAHCPTSNLFLGSGLFDVRKLLDAGIKVGLG 316

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034671998 159 TDVAGGYSYSMLDAIRRAVMVSNILLINKVNEKSLTLKEVFRLATLGGSQALGLDGEIGNFEVGKEFDAILINPKASDSP 238
Cdd:cd01303   317 TDVGGGTSFSMLDTLRQAYKVSRLLGYELGGHAKLSPAEAFYLATLGGAEALGLDDKIGNFEVGKEFDAVVIDPSATPLL 396

                         250       260       270
                  ....*....|....*....|....*....|....*.
gi 1034671998 239 IDLfygDFFGDISEAVIQKFLYLGDDRNIEEVYVGG 274
Cdd:cd01303   397 ADR---MFRVESLEEALFKFLYLGDDRNIREVYVAG 429
 
Name Accession Description Interval E-value
GDEase cd01303
Guanine deaminase (GDEase). Guanine deaminase is an aminohydrolase responsible for the ...
 1-274 3.27e-146

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: 417.45  E-value: 3.27e-146
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034671998   1 MDLNDtfPEYK-ETTEESIKETERFVSEMLQKnYSRVKPIVTPRFSLSCSETLMGELGNIAKT-RDLHIQSHISENRDEV 78
Cdd:cd01303   160 MDRNA--PEYYrDTAESSYRDTKRLIERWHGK-SGRVKPAITPRFAPSCSEELLAALGKLAKEhPDLHIQTHISENLDEI 236

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034671998  79 EAVKNLYPSYKNYTSVYDKNNLLTNKTVMAHGCYLSAEELNVFHERGASIAHCPNSNLSLSSGFLNVLEVLKHEVKIGLG 158
Cdd:cd01303   237 AWVKELFPGARDYLDVYDKYGLLTEKTVLAHCVHLSEEEFNLLKERGASVAHCPTSNLFLGSGLFDVRKLLDAGIKVGLG 316

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034671998 159 TDVAGGYSYSMLDAIRRAVMVSNILLINKVNEKSLTLKEVFRLATLGGSQALGLDGEIGNFEVGKEFDAILINPKASDSP 238
Cdd:cd01303   317 TDVGGGTSFSMLDTLRQAYKVSRLLGYELGGHAKLSPAEAFYLATLGGAEALGLDDKIGNFEVGKEFDAVVIDPSATPLL 396

                         250       260       270
                  ....*....|....*....|....*....|....*.
gi 1034671998 239 IDLfygDFFGDISEAVIQKFLYLGDDRNIEEVYVGG 274
Cdd:cd01303   397 ADR---MFRVESLEEALFKFLYLGDDRNIREVYVAG 429
SsnA COG0402
Cytosine/adenosine deaminase or related metal-dependent hydrolase [Nucleotide transport and ...
 1-278 6.87e-78

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: 242.81  E-value: 6.87e-78
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034671998   1 MDLNdtFPE-YKETTEESIKETERFVSEMLQKNYSRVKPIVTPRFSLSCSETLMGELGNIAKTRDLHIQSHISENRDEVE 79
Cdd:COG0402   153 MDRG--FPDgLREDADEGLADSERLIERWHGAADGRIRVALAPHAPYTVSPELLRAAAALARELGLPLHTHLAETRDEVE 230

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034671998  80 AVKNLYPsyKNYTSVYDKNNLLTNKTVMAHGCYLSAEELNVFHERGASIAHCPNSNLSLSSGFLNVLEVLKHEVKIGLGT 159
Cdd:COG0402   231 WVLELYG--KRPVEYLDELGLLGPRTLLAHCVHLTDEEIALLAETGASVAHCPTSNLKLGSGIAPVPRLLAAGVRVGLGT 308

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034671998 160 DVAGG-YSYSMLDAIRRAVMVSNILlinKVNEKSLTLKEVFRLATLGGSQALGLDGEIGNFEVGKEFDAILINPKASD-S 237
Cdd:COG0402   309 DGAASnNSLDMFEEMRLAALLQRLR---GGDPTALSAREALEMATLGGARALGLDDEIGSLEPGKRADLVVLDLDAPHlA 385

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|.
gi 1034671998 238 PIDlfygdffgdiseAVIQKFLYLGDDRNIEEVYVGGKQVV 278
Cdd:COG0402   386 PLH------------DPLSALVYAADGRDVRTVWVAGRVVV 414
PRK09228 PRK09228
guanine deaminase; Provisional
 1-277 3.40e-72

guanine deaminase; Provisional


Pssm-ID: 236419 [Multi-domain]  Cd Length: 433  Bit Score: 228.54  E-value: 3.40e-72
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034671998   1 MDLNdtFPEY-KETTEESIKETERfvseMLQK--NYSRVKPIVTPRFSLSCSETLMGELGNIAKTR-DLHIQSHISENRD 76
Cdd:PRK09228  164 MDRN--APDGlRDTAESGYDDSKA----LIERwhGKGRLLYAITPRFAPTSTPEQLEAAGALAREHpDVWIQTHLSENLD 237

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034671998  77 EVEAVKNLYPSYKNYTSVYDKNNLLTNKTVMAHGCYLSAEELNVFHERGASIAHCPNSNLSLSSGFLNVLEVLKHEVKIG 156
Cdd:PRK09228  238 EIAWVKELFPEARDYLDVYERYGLLGPRAVFAHCIHLEDRERRRLAETGAAIAFCPTSNLFLGSGLFDLKRADAAGVRVG 317

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034671998 157 LGTDVAGGYSYSMLDAIRRAVMVSnillinKVNEKSLTLKEVFRLATLGGSQALGLDGEIGNFEVGKEFDAILINPKA-- 234
Cdd:PRK09228  318 LGTDVGGGTSFSMLQTMNEAYKVQ------QLQGYRLSPFQAFYLATLGGARALGLDDRIGNLAPGKEADFVVLDPAAtp 391

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1034671998 235 --------SDSPIDLFYGdffgdiseaviqkFLYLGDDRNIEEVYVGGKQV 277
Cdd:PRK09228  392 llalrtarAESLEELLFA-------------LMTLGDDRAVAETYVAGRPV 429
Amidohydro_1 pfam01979
Amidohydrolase family; This family of enzymes are a a large metal dependent hydrolase ...
 7-277 7.55e-41

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: 144.57  E-value: 7.55e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034671998   7 FPEYKETTEESIKETERFVSEM---LQKNYSRVKPIVTPRFSLSCSETLMGELGNIAKTRDLHIQSHISENRDEVEAVKN 83
Cdd:pfam01979  80 SLDTDGELEGRKALREKLKAGAefiKGMADGVVFVGLAPHGAPTFSDDELKAALEEAKKYGLPVAIHALETKGEVEDAIA 159

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034671998  84 LYPS---YKNYTSVYDKNNLL-TNKTVMAHGCYLSAEELNVFHER--GASIAHCPNSNLSLSSGFLNVLEVLKHEVKIGL 157
Cdd:pfam01979 160 AFGGgieHGTHLEVAESGGLLdIIKLILAHGVHLSPTEANLLAEHlkGAGVAHCPFSNSKLRSGRIALRKALEDGVKVGL 239

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034671998 158 GTDVAG-GYSYSMLDAIRRAVmvsnilLINKVNEKSLTLKEVFRLATLGGSQALGLDGEIGNFEVGKEFDAILINPKasd 236
Cdd:pfam01979 240 GTDGAGsGNSLNMLEELRLAL------ELQFDPEGGLSPLEALRMATINPAKALGLDDKVGSIEVGKDADLVVVDLD--- 310

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|.
gi 1034671998 237 spidlfygdffgdiseaVIQKFLYLGDDRNIEEVYVGGKQV 277
Cdd:pfam01979 311 -----------------PLAAFFGLKPDGNVKKVIVKGKIV 334
 
Name Accession Description Interval E-value
GDEase cd01303
Guanine deaminase (GDEase). Guanine deaminase is an aminohydrolase responsible for the ...
 1-274 3.27e-146

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: 417.45  E-value: 3.27e-146
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034671998   1 MDLNDtfPEYK-ETTEESIKETERFVSEMLQKnYSRVKPIVTPRFSLSCSETLMGELGNIAKT-RDLHIQSHISENRDEV 78
Cdd:cd01303   160 MDRNA--PEYYrDTAESSYRDTKRLIERWHGK-SGRVKPAITPRFAPSCSEELLAALGKLAKEhPDLHIQTHISENLDEI 236

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034671998  79 EAVKNLYPSYKNYTSVYDKNNLLTNKTVMAHGCYLSAEELNVFHERGASIAHCPNSNLSLSSGFLNVLEVLKHEVKIGLG 158
Cdd:cd01303   237 AWVKELFPGARDYLDVYDKYGLLTEKTVLAHCVHLSEEEFNLLKERGASVAHCPTSNLFLGSGLFDVRKLLDAGIKVGLG 316

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034671998 159 TDVAGGYSYSMLDAIRRAVMVSNILLINKVNEKSLTLKEVFRLATLGGSQALGLDGEIGNFEVGKEFDAILINPKASDSP 238
Cdd:cd01303   317 TDVGGGTSFSMLDTLRQAYKVSRLLGYELGGHAKLSPAEAFYLATLGGAEALGLDDKIGNFEVGKEFDAVVIDPSATPLL 396

                         250       260       270
                  ....*....|....*....|....*....|....*.
gi 1034671998 239 IDLfygDFFGDISEAVIQKFLYLGDDRNIEEVYVGG 274
Cdd:cd01303   397 ADR---MFRVESLEEALFKFLYLGDDRNIREVYVAG 429
SsnA COG0402
Cytosine/adenosine deaminase or related metal-dependent hydrolase [Nucleotide transport and ...
 1-278 6.87e-78

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: 242.81  E-value: 6.87e-78
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034671998   1 MDLNdtFPE-YKETTEESIKETERFVSEMLQKNYSRVKPIVTPRFSLSCSETLMGELGNIAKTRDLHIQSHISENRDEVE 79
Cdd:COG0402   153 MDRG--FPDgLREDADEGLADSERLIERWHGAADGRIRVALAPHAPYTVSPELLRAAAALARELGLPLHTHLAETRDEVE 230

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034671998  80 AVKNLYPsyKNYTSVYDKNNLLTNKTVMAHGCYLSAEELNVFHERGASIAHCPNSNLSLSSGFLNVLEVLKHEVKIGLGT 159
Cdd:COG0402   231 WVLELYG--KRPVEYLDELGLLGPRTLLAHCVHLTDEEIALLAETGASVAHCPTSNLKLGSGIAPVPRLLAAGVRVGLGT 308

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034671998 160 DVAGG-YSYSMLDAIRRAVMVSNILlinKVNEKSLTLKEVFRLATLGGSQALGLDGEIGNFEVGKEFDAILINPKASD-S 237
Cdd:COG0402   309 DGAASnNSLDMFEEMRLAALLQRLR---GGDPTALSAREALEMATLGGARALGLDDEIGSLEPGKRADLVVLDLDAPHlA 385

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|.
gi 1034671998 238 PIDlfygdffgdiseAVIQKFLYLGDDRNIEEVYVGGKQVV 278
Cdd:COG0402   386 PLH------------DPLSALVYAADGRDVRTVWVAGRVVV 414
PRK09228 PRK09228
guanine deaminase; Provisional
 1-277 3.40e-72

guanine deaminase; Provisional


Pssm-ID: 236419 [Multi-domain]  Cd Length: 433  Bit Score: 228.54  E-value: 3.40e-72
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034671998   1 MDLNdtFPEY-KETTEESIKETERfvseMLQK--NYSRVKPIVTPRFSLSCSETLMGELGNIAKTR-DLHIQSHISENRD 76
Cdd:PRK09228  164 MDRN--APDGlRDTAESGYDDSKA----LIERwhGKGRLLYAITPRFAPTSTPEQLEAAGALAREHpDVWIQTHLSENLD 237

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034671998  77 EVEAVKNLYPSYKNYTSVYDKNNLLTNKTVMAHGCYLSAEELNVFHERGASIAHCPNSNLSLSSGFLNVLEVLKHEVKIG 156
Cdd:PRK09228  238 EIAWVKELFPEARDYLDVYERYGLLGPRAVFAHCIHLEDRERRRLAETGAAIAFCPTSNLFLGSGLFDLKRADAAGVRVG 317

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034671998 157 LGTDVAGGYSYSMLDAIRRAVMVSnillinKVNEKSLTLKEVFRLATLGGSQALGLDGEIGNFEVGKEFDAILINPKA-- 234
Cdd:PRK09228  318 LGTDVGGGTSFSMLQTMNEAYKVQ------QLQGYRLSPFQAFYLATLGGARALGLDDRIGNLAPGKEADFVVLDPAAtp 391

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1034671998 235 --------SDSPIDLFYGdffgdiseaviqkFLYLGDDRNIEEVYVGGKQV 277
Cdd:PRK09228  392 llalrtarAESLEELLFA-------------LMTLGDDRAVAETYVAGRPV 429
ATZ_TRZ_like cd01298
TRZ/ATZ family contains enzymes from the atrazine degradation pathway and related hydrolases. ...
 1-278 1.02e-48

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: 166.99  E-value: 1.02e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034671998   1 MDLNDtfpEYKETTEESIKETERFVSEMLQKNYSRVKPIVTPRFSLSCSETLMGELGNIAKTRDLHIQSHISENRDEVEA 80
Cdd:cd01298   147 MDLGT---EDVEETEEALAEAERLIREWHGAADGRIRVALAPHAPYTCSDELLREVAELAREYGVPLHIHLAETEDEVEE 223

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034671998  81 VKNLYpsykNYTSV-Y-DKNNLLTNKTVMAHGCYLSAEELNVFHERGASIAHCPNSNLSLSSGFLNVLEVLKHEVKIGLG 158
Cdd:cd01298   224 SLEKY----GKRPVeYlEELGLLGPDVVLAHCVWLTDEEIELLAETGTGVAHNPASNMKLASGIAPVPEMLEAGVNVGLG 299

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034671998 159 TD-VAGGYSYSMLDAIRRAvmvsniLLINKV---NEKSLTLKEVFRLATLGGSQALGLDgEIGNFEVGKEFDAILINPka 234
Cdd:cd01298   300 TDgAASNNNLDMFEEMRLA------ALLQKLahgDPTALPAEEALEMATIGGAKALGLD-EIGSLEVGKKADLILIDL-- 370

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*..
gi 1034671998 235 sDSPidlfygDFFG---DISEAViqkflYLGDDRNIEEVYVGGKQVV 278
Cdd:cd01298   371 -DGP------HLLPvhdPISHLV-----YSANGGDVDTVIVNGRVVM 405
PRK07228 PRK07228
5'-deoxyadenosine deaminase;
1-231 1.47e-43

5'-deoxyadenosine deaminase;


Pssm-ID: 180895 [Multi-domain]  Cd Length: 445  Bit Score: 154.39  E-value: 1.47e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034671998   1 MDLNDTFPE-YKETTEESIKETERFVSEMLQKNYSRVKPIVTPRFSLSCSETLMGELGNIAKTRDLHIQSHISENRDEVE 79
Cdd:PRK07228  148 MDYGDDVPEgLQEDTEASLAESVRLLEKWHGADNGRIRYAFTPRFAVSCTEELLRGVRDLADEYGVRIHTHASENRGEIE 227

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034671998  80 AVKNlYPSYKNYTsVYDKNNLLTNKTVMAHGCYLSAEELNVFHERGASIAHCPNSNLSLSSGFLNVLEVLKHEVKIGLGT 159
Cdd:PRK07228  228 TVEE-ETGMRNIH-YLDEVGLTGEDLILAHCVWLDEEEREILAETGTHVTHCPSSNLKLASGIAPVPDLLERGINVALGA 305

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1034671998 160 DvaGGYSYSMLDA---IRRAVmvsnilLINKVNE---KSLTLKEVFRLATLGGSQALGLDGEIGNFEVGKEFDAILIN 231
Cdd:PRK07228  306 D--GAPCNNTLDPfteMRQAA------LIQKVDRlgpTAMPARTVFEMATLGGAKAAGFEDEIGSLEEGKKADLAILD 375
Amidohydro_1 pfam01979
Amidohydrolase family; This family of enzymes are a a large metal dependent hydrolase ...
 7-277 7.55e-41

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: 144.57  E-value: 7.55e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034671998   7 FPEYKETTEESIKETERFVSEM---LQKNYSRVKPIVTPRFSLSCSETLMGELGNIAKTRDLHIQSHISENRDEVEAVKN 83
Cdd:pfam01979  80 SLDTDGELEGRKALREKLKAGAefiKGMADGVVFVGLAPHGAPTFSDDELKAALEEAKKYGLPVAIHALETKGEVEDAIA 159

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034671998  84 LYPS---YKNYTSVYDKNNLL-TNKTVMAHGCYLSAEELNVFHER--GASIAHCPNSNLSLSSGFLNVLEVLKHEVKIGL 157
Cdd:pfam01979 160 AFGGgieHGTHLEVAESGGLLdIIKLILAHGVHLSPTEANLLAEHlkGAGVAHCPFSNSKLRSGRIALRKALEDGVKVGL 239

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034671998 158 GTDVAG-GYSYSMLDAIRRAVmvsnilLINKVNEKSLTLKEVFRLATLGGSQALGLDGEIGNFEVGKEFDAILINPKasd 236
Cdd:pfam01979 240 GTDGAGsGNSLNMLEELRLAL------ELQFDPEGGLSPLEALRMATINPAKALGLDDKVGSIEVGKDADLVVVDLD--- 310

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|.
gi 1034671998 237 spidlfygdffgdiseaVIQKFLYLGDDRNIEEVYVGGKQV 277
Cdd:pfam01979 311 -----------------PLAAFFGLKPDGNVKKVIVKGKIV 334
PRK08393 PRK08393
N-ethylammeline chlorohydrolase; Provisional
 1-278 4.54e-32

N-ethylammeline chlorohydrolase; Provisional


Pssm-ID: 181411 [Multi-domain]  Cd Length: 424  Bit Score: 122.99  E-value: 4.54e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034671998   1 MDLNDtfpeyKETTEESIKETERFVSEMLQKNYSRVKPIVTPRFSLSCSETLMGELGNIAKTRDLHIQSHISENRDEVEA 80
Cdd:PRK08393  144 VDLGD-----EEKREKEIKETEKLMEFIEKLNSPRVHFVFGPHAPYTCSLALLKWVREKAREWNKLITIHLSETMDEIKQ 218

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034671998  81 VKNLYPsyKNYTSVYDKNNLLTNKTVMAHGCYLSAEELNVFHERGASIAHCPNSNLSLSSGFLNVLEVLKHEVKIGLGTD 160
Cdd:PRK08393  219 IREKYG--KSPVVLLDEIGFLNEDVIAAHGVWLSSRDIRILASAGVTVAHNPASNMKLGSGVMPLRKLLNAGVNVALGTD 296

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034671998 161 vaGGYSYSMLDAIRRAVMVSnilLINKVNEKSLTL---KEVFRLATLGGSQALGLDGeiGNFEVGKEFDAILIN-PKASD 236
Cdd:PRK08393  297 --GAASNNNLDMLREMKLAA---LLHKVHNLDPTIadaETVFRMATQNGAKALGLKA--GVIKEGYLADIAVIDfNRPHL 369

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|..
gi 1034671998 237 SPIDlfygdffgdiseAVIQKFLYLGDDRNIEEVYVGGKQVV 278
Cdd:PRK08393  370 RPIN------------NPISHLVYSANGNDVETTIVDGKIVM 399
PRK06687 PRK06687
TRZ/ATZ family protein;
7-278 1.95e-31

TRZ/ATZ family protein;


Pssm-ID: 180657 [Multi-domain]  Cd Length: 419  Bit Score: 121.27  E-value: 1.95e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034671998   7 FPEYKETTEESIKETERFVSEMLQKNYSRVKPIVTPRFSLSCSETLMGELGNIAKTRDLHIQSHISENRDEVEAVKNLYP 86
Cdd:PRK06687  152 FSSETETTAETISRTRSIIDEILKYKNPNFKVMVAPHSPYSCSRDLLEASLEMAKELNIPLHVHVAETKEESGIILKRYG 231

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034671998  87 syKNYTSVYDKNNLLTNKTVMAHGCYLSAEELNVFHERGASIAHCPNSNLSLSSGFLNVLEVLKHEVKIGLGTD-VAGGY 165
Cdd:PRK06687  232 --KRPLAFLEELGYLDHPSVFAHGVELNEREIERLASSQVAIAHNPISNLKLASGIAPIIQLQKAGVAVGIATDsVASNN 309

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034671998 166 SYSMLDAIRRAVMVSNillINKVNEKSLTLKEVFRLATLGGSQALGLDGEIGNFEVGKEFDAILINPKASdspIDLFygd 245
Cdd:PRK06687  310 NLDMFEEGRTAALLQK---MKSGDASQFPIETALKVLTIEGAKALGMENQIGSLEVGKQADFLVIQPQGK---IHLQ--- 380

                         250       260       270
                  ....*....|....*....|....*....|...
gi 1034671998 246 ffgdISEAVIQKFLYLGDDRNIEEVYVGGKQVV 278
Cdd:PRK06687  381 ----PQENMLSHLVYAVKSSDVDDVYIAGEQVV 409
PRK06038 PRK06038
N-ethylammeline chlorohydrolase; Provisional
 12-233 4.45e-27

N-ethylammeline chlorohydrolase; Provisional


Pssm-ID: 180363 [Multi-domain]  Cd Length: 430  Bit Score: 109.45  E-value: 4.45e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034671998  12 ETTEESIKETERFVSEMLQKNYSRVKPIVTPRFSLSCSETLMGELGNIAKTRDLHIQSHISENRDEVEAVKNLYpsykNY 91
Cdd:PRK06038  151 EKGEAELKEGKRFVKEWHGAADGRIKVMYGPHAPYTCSEEFLSKVKKLANKDGVGIHIHVLETEAELNQMKEQY----GM 226

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034671998  92 TSVY--DKNNLLTNKTVMAHGCYLSAEELNVFHERGASIAHCPNSNLSLSSGFLNVLEVLKHEVKIGLGTD-VAGGYSYS 168
Cdd:PRK06038  227 CSVNylDDIGFLGPDVLAAHCVWLSDGDIEILRERGVNVSHNPVSNMKLASGIAPVPKLLERGVNVSLGTDgCASNNNLD 306

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1034671998 169 MLDAIRRAVMVSNillINKVNEKSLTLKEVFRLATLGGSQALGLdgEIGNFEVGKEFDAILINPK 233
Cdd:PRK06038  307 MFEEMKTAALLHK---VNTMDPTALPARQVLEMATVNGAKALGI--NTGMLKEGYLADIIIVDMN 366
PRK15493 PRK15493
bifunctional S-methyl-5'-thioadenosine deaminase/S-adenosylhomocysteine deaminase;
11-278 2.08e-25

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


Pssm-ID: 185390 [Multi-domain]  Cd Length: 435  Bit Score: 104.75  E-value: 2.08e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034671998  11 KETTEESIKETERFVSEMLQKNySRVKPIVTPRFSLSCSETLMGELGNIAKTRDLHIQSHISENRDEVEAVKNLYPsyKN 90
Cdd:PRK15493  158 KEDEKKAIEEAEKYVKRYYNES-GMLTTMVAPHSPYTCSTELLEECARIAVENQTMVHIHLSETEREVRDIEAQYG--KR 234

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034671998  91 YTSVYDKNNLLTNKTVMAHGCYLSAEELNVFHERGASIAHCPNSNLSLSSGFLNVLEVLKHEVKIGLGTD-VAGGYSYSM 169
Cdd:PRK15493  235 PVEYAASCGLFKRPTVIAHGVVLNDNERAFLAEHDVRVAHNPNSNLKLGSGIANVKAMLEAGIKVGIATDsVASNNNLDM 314

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034671998 170 LDAIRRAVMVSNILlinKVNEKSLTLKEVFRLATLGGSQALGLDgEIGNFEVGKEFDAILINP--KASDSPidlfygdff 247
Cdd:PRK15493  315 FEEMRIATLLQKGI---HQDATALPVETALTLATKGAAEVIGMK-QTGSLEVGKCADFITIDPsnKPHLQP--------- 381

                         250       260       270
                  ....*....|....*....|....*....|.
gi 1034671998 248 gdiSEAVIQKFLYLGDDRNIEEVYVGGKQVV 278
Cdd:PRK15493  382 ---ADEVLSHLVYAASGKDISDVIINGKRVV 409
PRK09045 PRK09045
TRZ/ATZ family hydrolase;
59-278 2.09e-25

TRZ/ATZ family hydrolase;


Pssm-ID: 236366 [Multi-domain]  Cd Length: 443  Bit Score: 104.99  E-value: 2.09e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034671998  59 IAKTRDLHIQSHISENRDEVEAvknlypSYKNY----TSVYDKNNLLTNKTVMAHGCYLSAEELNVFHERGASIAHCPNS 134
Cdd:PRK09045  210 LAEQLDLPIHIHLHETAQEIAD------SLKQHgqrpLARLARLGLLGPRLIAVHMTQLTDAEIALLAETGCSVVHCPES 283

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034671998 135 NLSLSSGFLNVLEVLKHEVKIGLGTD-VAGGYSYSMLDAIRRAVMVSnillinKV---NEKSLTLKEVFRLATLGGSQAL 210
Cdd:PRK09045  284 NLKLASGFCPVAKLLQAGVNVALGTDgAASNNDLDLFGEMRTAALLA------KAvagDATALPAHTALRMATLNGARAL 357

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1034671998 211 GLDGEIGNFEVGKEFDAILINPKASDS-PIdlfygdfFGDISEAViqkflYLGDDRNIEEVYVGGKQVV 278
Cdd:PRK09045  358 GLDDEIGSLEPGKQADLVAVDLSGLETqPV-------YDPVSQLV-----YAAGREQVSHVWVAGKQLL 414
PRK08203 PRK08203
hydroxydechloroatrazine ethylaminohydrolase; Reviewed
 12-226 4.11e-22

hydroxydechloroatrazine ethylaminohydrolase; Reviewed


Pssm-ID: 236184 [Multi-domain]  Cd Length: 451  Bit Score: 95.69  E-value: 4.11e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034671998  12 ETTEESIKETERFVSEMLQKN-YSRVKPIVTPRFSLSCSETLMGELGNIAKTRDLHIQSHISENRDEVEAVKNLYpsykN 90
Cdd:PRK08203  174 EDEDAILADSQRLIDRYHDPGpGAMLRIALAPCSPFSVSRELMRESAALARRLGVRLHTHLAETLDEEAFCLERF----G 249

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034671998  91 YTSV-Y-DKNNLLTNKTVMAHGCYLSAEELNVFHERGASIAHCPNSNLSLSSGFLNVLEVLKHEVKIGLGTD-VAGGYSY 167
Cdd:PRK08203  250 MRPVdYlEDLGWLGPDVWLAHCVHLDDAEIARLARTGTGVAHCPCSNMRLASGIAPVRELRAAGVPVGLGVDgSASNDGS 329

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1034671998 168 SMLDAIRRAvmvsniLLINKV--NEKSLTLKEVFRLATLGGSQALGLDgEIGNFEVGKEFD 226
Cdd:PRK08203  330 NLIGEARQA------LLLQRLryGPDAMTAREALEWATLGGARVLGRD-DIGSLAPGKLAD 383
PRK08418 PRK08418
metal-dependent hydrolase;
58-278 6.39e-20

metal-dependent hydrolase;


Pssm-ID: 181419 [Multi-domain]  Cd Length: 408  Bit Score: 88.87  E-value: 6.39e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034671998  58 NIAKTRDLHIQSHISENRDEVEAVKNLYPSYKNY--------TSVYDKNNLL----TNKTVMAHGCYLSAEELNVFHERG 125
Cdd:PRK08418  197 QLAKKENLLVSTHFLESKAEREWLEESKGWFKKFfekflkepKPLYTPKEFLelfkGLRTLFTHCVYASEEELEKIKSKN 276

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034671998 126 ASIAHCPNSNLSLSSGFLNVLEVLKHEVKIGLGTD-VAGGYSYSMLDAIRRAVMVSNillinkvNEKSLTL-KEVFRLAT 203
Cdd:PRK08418  277 ASITHCPFSNRLLSNKALDLEKAKKAGINYSIATDgLSSNISLSLLDELRAALLTHA-------NMPLLELaKILLLSAT 349

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1034671998 204 LGGSQALGLD-GEIgnfEVGKEFDAILINpkasdspidlfYGDFFGDISEAVIQKFLYlgdDRNIEEVYVGGKQVV 278
Cdd:PRK08418  350 RYGAKALGLNnGEI---KEGKDADLSVFE-----------LPEECTKKEQLPLQFILH---AKEVKKLFIGGKEVK 408
PRK08204 PRK08204
hypothetical protein; Provisional
 39-275 1.32e-19

hypothetical protein; Provisional


Pssm-ID: 181288 [Multi-domain]  Cd Length: 449  Bit Score: 88.52  E-value: 1.32e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034671998  39 IVTPRFSlsCSETLMGELGnIAKTRDLHIQSHISenrdeveavknLYPSYKNYTSV--YDKNNLLTNKTVMAHGCYLSAE 116
Cdd:PRK08204  192 IRGPEFS--SWEVARADFR-LARELGLPISMHQG-----------FGPWGATPRGVeqLHDAGLLGPDLNLVHGNDLSDD 257

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034671998 117 ELNVFHERGASIAHCPNSNLSLSSGFLNVLEVLKHEVKIGLGTDVAGGYSYSMLDAIR------RAVMVSNILLINKV-- 188
Cdd:PRK08204  258 ELKLLADSGGSFSVTPEIEMMMGHGYPVTGRLLAHGVRPSLGVDVVTSTGGDMFTQMRfalqaeRARDNAVHLREGGMpp 337

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034671998 189 NEKSLTLKEVFRLATLGGSQALGLDGEIGNFEVGKEFDAILINPKAsdspIDLFYgdfFGDISEAVIQkflyLGDDRNIE 268
Cdd:PRK08204  338 PRLTLTARQVLEWATIEGARALGLEDRIGSLTPGKQADLVLIDATD----LNLAP---VHDPVGAVVQ----SAHPGNVD 406


                  ....*..
gi 1034671998 269 EVYVGGK 275
Cdd:PRK08204  407 SVMVAGR 413
PRK06380 PRK06380
metal-dependent hydrolase; Provisional
 13-275 1.03e-17

metal-dependent hydrolase; Provisional


Pssm-ID: 180548 [Multi-domain]  Cd Length: 418  Bit Score: 82.62  E-value: 1.03e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034671998  13 TTEES--IKETERFVSEMLQKNYsrVKPIVTPRFSLSCSETLMGELGNIAKTRDLHIQSHISENRDEVeavknlYPSYKN 90
Cdd:PRK06380  148 TTQKGdpLNNAENFIREHRNEEL--VTPSIGVQGIYVANDETYLKAKEIAEKYDTIMHMHLSETRKEV------YDHVKR 219

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034671998  91 Y----TSVYDKNNLLTNKTVMAHGCYLSAEELNVFHERGASIAHCPNSNLSLSS-GFLNVLEVLKHEVKIGLGTDVAGgy 165
Cdd:PRK06380  220 TgerpVEHLEKIGFLNSKLIAAHCVWATYHEIKLLSKNGVKVSWNSVSNFKLGTgGSPPIPEMLDNGINVTIGTDSNG-- 297

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034671998 166 SYSMLDAIrRAVMVSNILLINKVNEKSLT-LKEVFRLATLGGSQALGLDGeiGNFEVGKEFDAILINPKASdSPIDLFYG 244
Cdd:PRK06380  298 SNNSLDMF-EAMKFSALSVKNERWDASIIkAQEILDFATINAAKALELNA--GSIEVGKLADLVILDARAP-NMIPTRKN 373

                         250       260       270
                  ....*....|....*....|....*....|.
gi 1034671998 245 DFFGDIseaviqkfLYLGDDRNIEEVYVGGK 275
Cdd:PRK06380  374 NIVSNI--------VYSLNPLNVDHVIVNGK 396
Met_dep_hydrolase_D cd01312
Metallo-dependent hydrolases, subgroup D is part of the superfamily of metallo-dependent ...
 20-226 1.90e-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: 81.73  E-value: 1.90e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034671998  20 ETERFVSEMLQKNySRVKPIVTPRFSLSCSETLMGELGNIAKTRDLHIQSHISENRDEVEAV-------KNLYPSY---K 89
Cdd:cd01312   133 FLERFKRSKSFES-QLFIPAISPHAPYSVHPELAQDLIDLAKKLNLPLSTHFLESKEEREWLeeskgwfKHFWESFlklP 211

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034671998  90 NYTSVYDKNNL------LTNKTVMAHGCYLSAEELNVFHERGASIAHCPNSNLSLSSGFLNVLEVLKHEVKIGLGTD-VA 162
Cdd:cd01312   212 KPKKLATAIDFldmlggLGTRVSFVHCVYANLEEAEILASRGASIALCPRSNRLLNGGKLDVSELKKAGIPVSLGTDgLS 291

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1034671998 163 GGYSYSMLDAIRravmvSNILLINKVNEKSLTlKEVFRLATLGGSQALGLdgEIGNFEVGKEFD 226
Cdd:cd01312   292 SNISLSLLDELR-----ALLDLHPEEDLLELA-SELLLMATLGGARALGL--NNGEIEAGKRAD 347
PRK12393 PRK12393
amidohydrolase; Provisional
 12-278 4.76e-16

amidohydrolase; Provisional


Pssm-ID: 237088 [Multi-domain]  Cd Length: 457  Bit Score: 77.80  E-value: 4.76e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034671998  12 ETTEESIKETERFVSEMLQKNYSRVKPIV----TPRFSLScsETLMGELGNIAKTRDLHIQSHISENRDEVEAVKNLYps 87
Cdd:PRK12393  177 ETLDQMLADVERLVSRYHDASPDSLRRVVvaptTPTFSLP--PELLREVARAARGMGLRLHSHLSETVDYVDFCREKY-- 252

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034671998  88 ykNYTSVY--DKNNLLTNKTVMAHGCYLSAEELNVFHERGASIAHCPNSNLSLSSGFLNVLEVLKHEVKIGLGTD-VAGG 164
Cdd:PRK12393  253 --GMTPVQfvAEHDWLGPDVWFAHLVKLDAEEIALLAQTGTGIAHCPQSNGRLGSGIAPALAMEAAGVPVSLGVDgAASN 330

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034671998 165 YSYSMLDAIRRAVMVSNILlinkVNEKSLTLKEVFRLATLGGSQALGLDgEIGNFEVGKEFDAILINpkaSDSPidLFYG 244
Cdd:PRK12393  331 ESADMLSEAHAAWLLHRAE----GGADATTVEDVVHWGTAGGARVLGLD-AIGTLAVGQAADLAIYD---LDDP--RFFG 400

                         250       260       270
                  ....*....|....*....|....*....|....
gi 1034671998 245 dfFGDISEAVIQKflylGDDRNIEEVYVGGKQVV 278
Cdd:PRK12393  401 --LHDPAIAPVAC----GGPAPVKALLVNGRPVV 428
PRK07203 PRK07203
putative aminohydrolase SsnA;
11-183 1.14e-14

putative aminohydrolase SsnA;


Pssm-ID: 235963 [Multi-domain]  Cd Length: 442  Bit Score: 73.82  E-value: 1.14e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034671998  11 KETTEESIKETERFVSEMLQKNYSRVKPIVTPRFSLSCS-ETL------MGELGniaktRDLHIqsHISENRDEVEAVKN 83
Cdd:PRK07203  165 EKELQEGVEENIRFIKHIDEAKDDMVEAMFGLHASFTLSdATLekcreaVKETG-----RGYHI--HVAEGIYDVSDSHK 237

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034671998  84 LYpsYKNYTSVYDKNNLLTNKTVMAHGCYLSAEELNVFHERGASIAHCPNSNLSLSSGFLNVLEVLKHEVKIGLGTDvag 163
Cdd:PRK07203  238 KY--GKDIVERLADFGLLGEKTLAAHCIYLSDEEIDLLKETDTFVVHNPESNMGNAVGYNPVLEMIKNGILLGLGTD--- 312

                         170       180
                  ....*....|....*....|
gi 1034671998 164 GYSYSMLDAIRravmVSNIL 183
Cdd:PRK07203  313 GYTSDMFESYK----VANFK 328
PRK06151 PRK06151
N-ethylammeline chlorohydrolase; Provisional
 18-278 7.15e-14

N-ethylammeline chlorohydrolase; Provisional


Pssm-ID: 180428 [Multi-domain]  Cd Length: 488  Bit Score: 71.61  E-value: 7.15e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034671998  18 IKETERFVSEMLQKNYSRVKPIVTPRFSLSCSETLMGELGNIAKTRDLHIQSHISENRDEVEAVKNLYpsykNYTS--VY 95
Cdd:PRK06151  188 LEEAIAFIKRVDGAHNGLVRGMLAPDRIETCTVDLLRRTAAAARELGCPVRLHCAQGVLEVETVRRLH----GTTPleWL 263

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034671998  96 DKNNLLTNKTVMAHGCYLS---------AEELNVFHERGASIAHCPnSNLSLSSGFLNVLEVLKHE-VKIGLGTDVAggy 165
Cdd:PRK06151  264 ADVGLLGPRLLIPHATYISgsprlnysgGDDLALLAEHGVSIVHCP-LVSARHGSALNSFDRYREAgINLALGTDTF--- 339

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034671998 166 sysmldairRAVMVSNI---LLINKVNEKSLT---LKEVFRLATLGGSQALGLDgEIGNFEVGKEFDAILINPKasdspi 239
Cdd:PRK06151  340 ---------PPDMVMNMrvgLILGRVVEGDLDaasAADLFDAATLGGARALGRD-DLGRLAPGAKADIVVFDLD------ 403

                         250       260       270
                  ....*....|....*....|....*....|....*....
gi 1034671998 240 DLFYGDFFGDISEAVIQkflylGDDRNIEEVYVGGKQVV 278
Cdd:PRK06151  404 GLHMGPVFDPIRTLVTG-----GSGRDVRAVFVDGRVVM 437
metallo-dependent_hydrolases cd01292
Superfamily of metallo-dependent hydrolases (also called amidohydrolase superfamily) is a ...
 60-209 4.09e-12

Superfamily of metallo-dependent hydrolases (also called amidohydrolase superfamily) is a large group of proteins that show conservation in their 3-dimensional fold (TIM barrel) and in details of their active site. The vast majority of the members have a conserved metal binding site, involving four histidines and one aspartic acid residue. In the common reaction mechanism, the metal ion (or ions) deprotonate a water molecule for a nucleophilic attack on the substrate. The family includes urease alpha, adenosine deaminase, phosphotriesterase dihydroorotases, allantoinases, hydantoinases, AMP-, adenine and cytosine deaminases, imidazolonepropionase, aryldialkylphosphatase, chlorohydrolases, formylmethanofuran dehydrogenases and others.


Pssm-ID: 238617 [Multi-domain]  Cd Length: 275  Bit Score: 65.05  E-value: 4.09e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034671998  60 AKTRDLHIQSHISENRDEVEAVKNLYpsyknytsvydKNNLLTNKTVMAHGCYLSAEELNVFHERGASIAHCPNSNLSLS 139
Cdd:cd01292   142 ARKLGLPVVIHAGELPDPTRALEDLV-----------ALLRLGGRVVIGHVSHLDPELLELLKEAGVSLEVCPLSNYLLG 210

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1034671998 140 S---GFLNVLEVLKHEVKIGLGTDVAGGYSYSMLDAIRRAVMVSNILLinkvneksLTLKEVFRLATLGGSQA 209
Cdd:cd01292   211 RdgeGAEALRRLLELGIRVTLGTDGPPHPLGTDLLALLRLLLKVLRLG--------LSLEEALRLATINPARA 275
archeal_chlorohydrolases cd01305
Predicted chlorohydrolases. These metallo-dependent hydrolases from archea are part of the ...
 59-207 6.41e-11

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: 61.65  E-value: 6.41e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034671998  59 IAKTRDLHIQSHISENRD-----EVEAVKNLYPsyknytsvydknNLLTnktvmaHGCYLSAEELNVFHERGASIAHCPN 133
Cdd:cd01305   133 LLRRRGKLFAIHASETREsvgmtDIERALDLEP------------DLLV------HGTHLTDEDLELVRENGVPVVLCPR 194

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1034671998 134 SNLSLSSGFLNVLEVLKHEVKIGLGTDVAGGYSYSMLDAIRRAVMVSNILlinkvneKSLTLKEVFRLATLGGS 207
Cdd:cd01305   195 SNLYFGVGIPPVAELLKLGIKVLLGTDNVMVNEPDMWAEMEFLAKYSRLQ-------GYLSPLEILRMATVNAA 261
Met_dep_hydrolase_E cd01313
Metallo-dependent hydrolases, subgroup D is part of the superfamily of metallo-dependent ...
 65-275 1.76e-10

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: 61.32  E-value: 1.76e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034671998  65 LHIqsHISENRDEVEAVknLYPSYKNYTSVYDKNNLLTNKTVMAHGCYLSAEELNVFHERGASIAHCPNSNLSLSSGFLN 144
Cdd:cd01313   222 VHI--HLAEQPKEVDDC--LAAHGRRPVELLLDHGHLDARWCLVHATHLTDNETLLLGRSGAVVGLCPTTEANLGDGIFP 297

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034671998 145 VLEVLKHEVKIGLGTDVAGG-----------YSYSMLDAiRRAVMVSnillinkvnEKSLTLKEVFRLATLGGSQALGLD 213
Cdd:cd01313   298 AAALLAAGGRIGIGSDSNARidlleelrqleYSQRLRDR-ARNVLAT---------AGGSSARALLDAALAGGAQALGLA 367

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1034671998 214 geIGNFEVGKEFDAILInpkASDSPidlfygDFFGDISEAVIQKFLYLGDDRNIEEVYVGGK 275
Cdd:cd01313   368 --TGALEAGARADLLSL---DLDHP------SLAGALPDTLLDAWVFAAGDREVRDVVVGGR 418
PRK07213 PRK07213
chlorohydrolase; Provisional
 70-234 2.10e-10

chlorohydrolase; Provisional


Pssm-ID: 235969 [Multi-domain]  Cd Length: 375  Bit Score: 60.82  E-value: 2.10e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034671998  70 HISENRDEVEAVKNLYpsykNYTSVYDKNNLLTNKTVMAHGCYLSAEELNVFHERGASIAHCPNSNLSLSSGFLNVLEVL 149
Cdd:PRK07213  198 HAAEHKGSVEYSLEKY----GMTEIERLINLGFKPDFIVHATHPSNDDLELLKENNIPVVVCPRANASFNVGLPPLNEML 273

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034671998 150 KHEVKIGLGTDVAGGYSYSM---LDAIRRAVmvsnillinkvnekSLTLKEVFRLATLGGSQALGLDgEIGNFEVGKEFD 226
Cdd:PRK07213  274 EKGILLGIGTDNFMANSPSIfreMEFIYKLY--------------HIEPKEILKMATINGAKILGLI-NVGLIEEGFKAD 338


                  ....*...
gi 1034671998 227 AILINPKA 234
Cdd:PRK07213  339 FTFIKPTN 346
HutI COG1228
Imidazolonepropionase or related amidohydrolase [Secondary metabolites biosynthesis, transport ...
 105-278 1.47e-07

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


Pssm-ID: 440841 [Multi-domain]  Cd Length: 386  Bit Score: 52.27  E-value: 1.47e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034671998 105 TVMAHGCYLSAEELNVFHERGASIAhCPNSNLSLSSGFL------------------NVLEVLKHEVKIGLGTDVAGGYS 166
Cdd:COG1228   227 DSIEHGTYLDDEVADLLAEAGTVVL-VPTLSLFLALLEGaaapvaakarkvreaalaNARRLHDAGVPVALGTDAGVGVP 305

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034671998 167 --YSMLDAIRRAVMVSnillinkvneksLTLKEVFRLATLGGSQALGLDGEIGNFEVGKEFDAILINpkasdspidlfyG 244
Cdd:COG1228   306 pgRSLHRELALAVEAG------------LTPEEALRAATINAAKALGLDDDVGSLEPGKLADLVLLD------------G 361

                         170       180       190
                  ....*....|....*....|....*....|....
gi 1034671998 245 DFFGDISeaviqkflYLgddRNIEEVYVGGKQVV 278
Cdd:COG1228   362 DPLEDIA--------YL---EDVRAVMKDGRVVD 384
Amidohydro_3 pfam07969
Amidohydrolase family;
107-278 6.98e-06

Amidohydrolase family;


Pssm-ID: 400360 [Multi-domain]  Cd Length: 464  Bit Score: 47.14  E-value: 6.98e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034671998 107 MAHGC---YLSAEELNVFHERGASIAHCPNSNLSLS------------SGFLNVLEVLKHEVKIGLGTDVAGGySYSMLD 171
Cdd:pfam07969 298 IEHAQgvvPYTYSQIERVAALGGAAGVQPVFDPLWGdwlqdrlgaeraRGLTPVKELLNAGVKVALGSDAPVG-PFDPWP 376

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034671998 172 AIRRAVM-----VSNILLInkvnEKSLTLKEVFRLATLGGSQALGLDGEIGNFEVGKEFDAILINpkasdspIDLFygdf 246
Cdd:pfam07969 377 RIGAAVMrqtagGGEVLGP----DEELSLEEALALYTSGPAKALGLEDRKGTLGVGKDADLVVLD-------DDPL---- 441

                         170       180       190
                  ....*....|....*....|....*....|..
gi 1034671998 247 fgDISEAVIqkflylgDDRNIEEVYVGGKQVV 278
Cdd:pfam07969 442 --TVDPPAI-------ADIRVRLTVVDGRVVY 464
PRK09229 PRK09229
N-formimino-L-glutamate deiminase; Validated
 65-278 3.31e-05

N-formimino-L-glutamate deiminase; Validated


Pssm-ID: 236420 [Multi-domain]  Cd Length: 456  Bit Score: 44.84  E-value: 3.31e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034671998  65 LHIqsHISENRDEVEAVKNLY---PsyknyTSVYDKNNLLTNKTVMAHGCYLSAEELNVFHERGASIAHCPNSNLSLSSG 141
Cdd:PRK09229  231 VHI--HIAEQTKEVDDCLAWSgarP-----VEWLLDHAPVDARWCLVHATHLTDAETARLARSGAVAGLCPTTEANLGDG 303

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034671998 142 FLNVLEVLKHEVKIGLGTDvaggySYSMLDAI---------------RRAVMVSNillinkvnEKSLTLKEVFRLATLGG 206
Cdd:PRK09229  304 IFPAVDYLAAGGRFGIGSD-----SHVSIDLVeelrlleygqrlrdrRRNVLAAA--------AQPSVGRRLFDAALAGG 370

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1034671998 207 SQALGLDgeIGNFEVGKEFDAILINPkasDSPidlfygDFFGDISEAVIQKFLYLGDDRNIEEVYVGGKQVV 278
Cdd:PRK09229  371 AQALGRA--IGGLAVGARADLVVLDL---DHP------ALAGREGDALLDRWVFAGGDAAVRDVWVAGRWVV 431
Imidazolone-5PH cd01296
Imidazolonepropionase/imidazolone-5-propionate hydrolase (Imidazolone-5PH) catalyzes the third ...
 107-257 4.96e-05

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: 44.17  E-value: 4.96e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034671998 107 MAHGCYLSAEELNVFHERGASIAHCPNSNLSLSSGFLNVLEVLKHEVKIGLGTDVAGGySY---SMLDAIRRAVmvsnIL 183
Cdd:cd01296   233 ADHLEHTSDEGIAALAEAGTVAVLLPGTAFSLRETYPPARKLIDAGVPVALGTDFNPG-SSptsSMPLVMHLAC----RL 307

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1034671998 184 LinkvnekSLTLKEVFRLATLGGSQALGLDGEIGNFEVGKEFDAILINpkaSDSPIDLFYgdFFG-DISEAVIQK 257
Cdd:cd01296   308 M-------RMTPEEALTAATINAAAALGLGETVGSLEVGKQADLVILD---APSYEHLAY--RFGvNLVEYVIKN 370
Met_dep_hydrolase_A cd01299
Metallo-dependent hydrolases, subgroup A is part of the superfamily of metallo-dependent ...
 136-231 9.30e-04

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: 40.35  E-value: 9.30e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034671998 136 LSLSSGFLNVLEVLKHEVKIGLGTD-----VAGGYSYSMLdairrAVMVsnillinkvnEKSLTLKEVFRLATLGGSQAL 210
Cdd:cd01299   247 LVLEAGRDALRRAHKAGVKIAFGTDagfpvPPHGWNAREL-----ELLV----------KAGGTPAEALRAATANAAELL 311

                          90       100
                  ....*....|....*....|.
gi 1034671998 211 GLDGEIGNFEVGKEFDAILIN 231
Cdd:cd01299   312 GLSDELGVIEAGKLADLLVVD 332
nagA PRK11170
N-acetylglucosamine-6-phosphate deacetylase; Provisional
 163-223 5.72e-03

N-acetylglucosamine-6-phosphate deacetylase; Provisional


Pssm-ID: 183010  Cd Length: 382  Bit Score: 38.03  E-value: 5.72e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1034671998 163 GGYSYSMLDAIRravmvsnilliNKVNEKSLTLKEVFRLATLGGSQALGLDGEIGNFEVGK 223
Cdd:PRK11170  307 SGSALTMIEAVR-----------NLVEHVGIALDEALRMATLYPARAIGVDKRLGSIEAGK 356
 
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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