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Conserved domains on  [gi|526271715|gb|AGR76813|]
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metallo-dependent hydrolase, subgroup D [Aliarcobacter butzleri 7h1h]

Protein Classification

metal-dependent hydrolase( domain architecture ID 10793094)

metal-dependent hydrolase similar to Nitratiruptor sp. aminodeoxyfutalosine deaminase that catalyzes the deamination of aminodeoxyfutalosine (AFL) into futalosine (FL), a step in the biosynthesis of menaquinone (MK, vitamin K2)

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PRK08418 PRK08418
metal-dependent hydrolase;
1-407 0e+00

metal-dependent hydrolase;


:

Pssm-ID: 181419 [Multi-domain]  Cd Length: 408  Bit Score: 629.69  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526271715   1 MKAISASYVVTCDENNRIIKDGAVVFDDKLIEIDTLFEIKNKYPNLEIkELEENSILMPGLVNSHIHLEFSANTTTLKYG 80
Cdd:PRK08418   1 MKIIGASYIFTCDENFEILEDGAVVFDDKILEIGDYENLKKKYPNAKI-QFFKNSVLLPAFINPHTHLEFSANKTTLDYG 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526271715  81 NFYSWLNSVIKHREDLINKATNELISTKLNKIKKTGTTTIGAISSYSFDMEACIKSPINTVFFCEVIGSKADMVDTLFAD 160
Cdd:PRK08418  80 DFIPWLGSVINHREDLLEKCKGALIQQAINEMLKSGVGTIGAISSFGIDLEICAKSPLRVVFFNEILGSNASAVDELYQD 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526271715 161 FRSRLNNAKKFASKNFIPAIAIHSPYSVHPFLVREALNVARDENLAVSSHFLESQEEFEWLHKDEGSFLEFFKNFLNQEK 240
Cdd:PRK08418 160 FLARFEESKKFKSKKFIPAIAIHSPYSVHPILAKKALQLAKKENLLVSTHFLESKAEREWLEESKGWFKKFFEKFLKEPK 239

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526271715 241 ATSKPMEFLGLFSKVKNLsFTHCVEASDDDLEKIKDLGASINHCVTSNRLLNNTKLDLDRL--KDIPFTIGTDGLSSNNS 318
Cdd:PRK08418 240 PLYTPKEFLELFKGLRTL-FTHCVYASEEELEKIKSKNASITHCPFSNRLLSNKALDLEKAkkAGINYSIATDGLSSNIS 318

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526271715 319 LSMFDELRNALMAHYDKNVVEFSKTLLKAATFNGSRALGLNKGVLKESFDADMISFKLPNKIEDINDICMQIILHTKFVD 398
Cdd:PRK08418 319 LSLLDELRAALLTHANMPLLELAKILLLSATRYGAKALGLNNGEIKEGKDADLSVFELPEECTKKEQLPLQFILHAKEVK 398


                 ....*....
gi 526271715 399 DVIIGGEYV 407
Cdd:PRK08418 399 KLFIGGKEV 407
 
Name Accession Description Interval E-value
PRK08418 PRK08418
metal-dependent hydrolase;
1-407 0e+00

metal-dependent hydrolase;


Pssm-ID: 181419 [Multi-domain]  Cd Length: 408  Bit Score: 629.69  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526271715   1 MKAISASYVVTCDENNRIIKDGAVVFDDKLIEIDTLFEIKNKYPNLEIkELEENSILMPGLVNSHIHLEFSANTTTLKYG 80
Cdd:PRK08418   1 MKIIGASYIFTCDENFEILEDGAVVFDDKILEIGDYENLKKKYPNAKI-QFFKNSVLLPAFINPHTHLEFSANKTTLDYG 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526271715  81 NFYSWLNSVIKHREDLINKATNELISTKLNKIKKTGTTTIGAISSYSFDMEACIKSPINTVFFCEVIGSKADMVDTLFAD 160
Cdd:PRK08418  80 DFIPWLGSVINHREDLLEKCKGALIQQAINEMLKSGVGTIGAISSFGIDLEICAKSPLRVVFFNEILGSNASAVDELYQD 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526271715 161 FRSRLNNAKKFASKNFIPAIAIHSPYSVHPFLVREALNVARDENLAVSSHFLESQEEFEWLHKDEGSFLEFFKNFLNQEK 240
Cdd:PRK08418 160 FLARFEESKKFKSKKFIPAIAIHSPYSVHPILAKKALQLAKKENLLVSTHFLESKAEREWLEESKGWFKKFFEKFLKEPK 239

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526271715 241 ATSKPMEFLGLFSKVKNLsFTHCVEASDDDLEKIKDLGASINHCVTSNRLLNNTKLDLDRL--KDIPFTIGTDGLSSNNS 318
Cdd:PRK08418 240 PLYTPKEFLELFKGLRTL-FTHCVYASEEELEKIKSKNASITHCPFSNRLLSNKALDLEKAkkAGINYSIATDGLSSNIS 318

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526271715 319 LSMFDELRNALMAHYDKNVVEFSKTLLKAATFNGSRALGLNKGVLKESFDADMISFKLPNKIEDINDICMQIILHTKFVD 398
Cdd:PRK08418 319 LSLLDELRAALLTHANMPLLELAKILLLSATRYGAKALGLNNGEIKEGKDADLSVFELPEECTKKEQLPLQFILHAKEVK 398


                 ....*....
gi 526271715 399 DVIIGGEYV 407
Cdd:PRK08418 399 KLFIGGKEV 407
Met_dep_hydrolase_D cd01312
Metallo-dependent hydrolases, subgroup D is part of the superfamily of metallo-dependent ...
 28-404 6.68e-116

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: 342.89  E-value: 6.68e-116
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526271715  28 DKLIEIDTLFEIKNKYPNLeIKELEENSILMPGLVNSHIHLEFSANTTTLKYGNFYSWLNSVIKHREDLINKATNELIST 107
Cdd:cd01312    1 DKILEVGDYEKLEKRYPGA-KHEFFPNGVLLPGLINAHTHLEFSANVAQFTYGRFRAWLLSVINSRDELLKQPWEEAIRQ 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526271715 108 KLNKIKKTGTTTIGAISSYSFDMEACIKSPINTVFFCEVIGSKADMVDTLFADFRSRLNNAKKFASKNFIPAIAIHSPYS 187
Cdd:cd01312   80 GIRQMLESGTTSIGAISSDGSLLPALASSGLRGVFFNEVIGSNPSAIDFKGETFLERFKRSKSFESQLFIPAISPHAPYS 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526271715 188 VHPFLVREALNVARDENLAVSSHFLESQEEFEWLHKDEGSFLEFFKNFLNQE--KATSKPMEFLGLFSKVK-NLSFTHCV 264
Cdd:cd01312  160 VHPELAQDLIDLAKKLNLPLSTHFLESKEEREWLEESKGWFKHFWESFLKLPkpKKLATAIDFLDMLGGLGtRVSFVHCV 239

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526271715 265 EASDDDLEKIKDLGASINHCVTSNRLLNNTKLDLDRLKD--IPFTIGTDGLSSNNSLSMFDELRNALMAHYDKNVVEFSK 342
Cdd:cd01312  240 YANLEEAEILASRGASIALCPRSNRLLNGGKLDVSELKKagIPVSLGTDGLSSNISLSLLDELRALLDLHPEEDLLELAS 319

                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 526271715 343 TLLKAATFNGSRALGLNKGVLKESFDADMISFKLPnKIEDINDICMQIILHTKFVDDVIIGG 404
Cdd:cd01312  320 ELLLMATLGGARALGLNNGEIEAGKRADFAVFELP-GPGIKEQAPLQFILHAKEVRHLFISG 380
SsnA COG0402
Cytosine/adenosine deaminase or related metal-dependent hydrolase [Nucleotide transport and ...
 3-405 3.31e-71

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: 229.33  E-value: 3.31e-71
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526271715   3 AISASYVVTCDENNRIIKDGAVVFDDKLI-EIDTLFEIKNKYPNLEIKELEeNSILMPGLVNSHIHLEFSANTTTLKYGN 81
Cdd:COG0402    3 LIRGAWVLTMDPAGGVLEDGAVLVEDGRIaAVGPGAELPARYPAAEVIDAG-GKLVLPGLVNTHTHLPQTLLRGLADDLP 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526271715  82 FYSWLNSVI-----KHREDLINKAT----NELIstklnkikKTGTTTIGAISSYSFDM-----EACIKSPINTVFFCEVI 147
Cdd:COG0402   82 LLDWLEEYIwpleaRLDPEDVYAGAllalAEML--------RSGTTTVADFYYVHPESadalaEAAAEAGIRAVLGRGLM 153

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526271715 148 GSKA-----DMVDTLFADFRSRLNNAKKFASKNFIPAIAIHSPYSVHPFLVREALNVARDENLAVSSHFLESQEEFEWLH 222
Cdd:COG0402  154 DRGFpdglrEDADEGLADSERLIERWHGAADGRIRVALAPHAPYTVSPELLRAAAALARELGLPLHTHLAETRDEVEWVL 233

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526271715 223 KDEGsfleffknflnqekatSKPMEFL---GLFSkvKNLSFTHCVEASDDDLEKIKDLGASINHCVTSNRLLNNTKLDLD 299
Cdd:COG0402  234 ELYG----------------KRPVEYLdelGLLG--PRTLLAHCVHLTDEEIALLAETGASVAHCPTSNLKLGSGIAPVP 295

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526271715 300 RLKD--IPFTIGTDGLSSNNSLSMFDELRNALMAH----YDKNVVEfSKTLLKAATFNGSRALGLNK--GVLKESFDADM 371
Cdd:COG0402  296 RLLAagVRVGLGTDGAASNNSLDMFEEMRLAALLQrlrgGDPTALS-AREALEMATLGGARALGLDDeiGSLEPGKRADL 374

                        410       420       430
                 ....*....|....*....|....*....|....*..
gi 526271715 372 ISFKLPN-KIEDINDICMQIIL--HTKFVDDVIIGGE 405
Cdd:COG0402  375 VVLDLDApHLAPLHDPLSALVYaaDGRDVRTVWVAGR 411
Amidohydro_1 pfam01979
Amidohydrolase family; This family of enzymes are a a large metal dependent hydrolase ...
 56-407 4.44e-36

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: 134.94  E-value: 4.44e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526271715   56 ILMPGLVNSHIHLEFSANTTTLKYGNFYSWLnsvikhredlINKATNELIstklnkikKTGTTTI-GAISSYSFDMEACI 134
Cdd:pfam01979   1 IVLPGLIDAHVHLEMGLLRGIPVPPEFAYEA----------LRLGITTML--------KSGTTTVlDMGATTSTGIEALL 62

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526271715  135 KSPINTVFFCEVIGSKADM--------VDTLFADFRSRLNNAKKFASKNFIPAIAIHSPYSVHPFLVREALNVARDENLA 206
Cdd:pfam01979  63 EAAEELPLGLRFLGPGCSLdtdgelegRKALREKLKAGAEFIKGMADGVVFVGLAPHGAPTFSDDELKAALEEAKKYGLP 142

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526271715  207 VSSHFLESQEEFEWLHKDEGSFLEFfknflnqekatSKPMEFLG--LFSKVKNLSFTHCVEASDDDLEKIKD--LGASIN 282
Cdd:pfam01979 143 VAIHALETKGEVEDAIAAFGGGIEH-----------GTHLEVAEsgGLLDIIKLILAHGVHLSPTEANLLAEhlKGAGVA 211

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526271715  283 HCVTSNRLLNNTKLDLDRLKD--IPFTIGTDGLSSNNSLSMFDELRNALMAHYDKNVVEFSKTLLKAATFNGSRALGL-- 358
Cdd:pfam01979 212 HCPFSNSKLRSGRIALRKALEdgVKVGLGTDGAGSGNSLNMLEELRLALELQFDPEGGLSPLEALRMATINPAKALGLdd 291

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*....
gi 526271715  359 NKGVLKESFDADMISFKLpNKIEDINDicmqiILHTKFVDDVIIGGEYV 407
Cdd:pfam01979 292 KVGSIEVGKDADLVVVDL-DPLAAFFG-----LKPDGNVKKVIVKGKIV 334
 
Name Accession Description Interval E-value
PRK08418 PRK08418
metal-dependent hydrolase;
1-407 0e+00

metal-dependent hydrolase;


Pssm-ID: 181419 [Multi-domain]  Cd Length: 408  Bit Score: 629.69  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526271715   1 MKAISASYVVTCDENNRIIKDGAVVFDDKLIEIDTLFEIKNKYPNLEIkELEENSILMPGLVNSHIHLEFSANTTTLKYG 80
Cdd:PRK08418   1 MKIIGASYIFTCDENFEILEDGAVVFDDKILEIGDYENLKKKYPNAKI-QFFKNSVLLPAFINPHTHLEFSANKTTLDYG 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526271715  81 NFYSWLNSVIKHREDLINKATNELISTKLNKIKKTGTTTIGAISSYSFDMEACIKSPINTVFFCEVIGSKADMVDTLFAD 160
Cdd:PRK08418  80 DFIPWLGSVINHREDLLEKCKGALIQQAINEMLKSGVGTIGAISSFGIDLEICAKSPLRVVFFNEILGSNASAVDELYQD 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526271715 161 FRSRLNNAKKFASKNFIPAIAIHSPYSVHPFLVREALNVARDENLAVSSHFLESQEEFEWLHKDEGSFLEFFKNFLNQEK 240
Cdd:PRK08418 160 FLARFEESKKFKSKKFIPAIAIHSPYSVHPILAKKALQLAKKENLLVSTHFLESKAEREWLEESKGWFKKFFEKFLKEPK 239

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526271715 241 ATSKPMEFLGLFSKVKNLsFTHCVEASDDDLEKIKDLGASINHCVTSNRLLNNTKLDLDRL--KDIPFTIGTDGLSSNNS 318
Cdd:PRK08418 240 PLYTPKEFLELFKGLRTL-FTHCVYASEEELEKIKSKNASITHCPFSNRLLSNKALDLEKAkkAGINYSIATDGLSSNIS 318

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526271715 319 LSMFDELRNALMAHYDKNVVEFSKTLLKAATFNGSRALGLNKGVLKESFDADMISFKLPNKIEDINDICMQIILHTKFVD 398
Cdd:PRK08418 319 LSLLDELRAALLTHANMPLLELAKILLLSATRYGAKALGLNNGEIKEGKDADLSVFELPEECTKKEQLPLQFILHAKEVK 398


                 ....*....
gi 526271715 399 DVIIGGEYV 407
Cdd:PRK08418 399 KLFIGGKEV 407
Met_dep_hydrolase_D cd01312
Metallo-dependent hydrolases, subgroup D is part of the superfamily of metallo-dependent ...
 28-404 6.68e-116

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: 342.89  E-value: 6.68e-116
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526271715  28 DKLIEIDTLFEIKNKYPNLeIKELEENSILMPGLVNSHIHLEFSANTTTLKYGNFYSWLNSVIKHREDLINKATNELIST 107
Cdd:cd01312    1 DKILEVGDYEKLEKRYPGA-KHEFFPNGVLLPGLINAHTHLEFSANVAQFTYGRFRAWLLSVINSRDELLKQPWEEAIRQ 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526271715 108 KLNKIKKTGTTTIGAISSYSFDMEACIKSPINTVFFCEVIGSKADMVDTLFADFRSRLNNAKKFASKNFIPAIAIHSPYS 187
Cdd:cd01312   80 GIRQMLESGTTSIGAISSDGSLLPALASSGLRGVFFNEVIGSNPSAIDFKGETFLERFKRSKSFESQLFIPAISPHAPYS 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526271715 188 VHPFLVREALNVARDENLAVSSHFLESQEEFEWLHKDEGSFLEFFKNFLNQE--KATSKPMEFLGLFSKVK-NLSFTHCV 264
Cdd:cd01312  160 VHPELAQDLIDLAKKLNLPLSTHFLESKEEREWLEESKGWFKHFWESFLKLPkpKKLATAIDFLDMLGGLGtRVSFVHCV 239

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526271715 265 EASDDDLEKIKDLGASINHCVTSNRLLNNTKLDLDRLKD--IPFTIGTDGLSSNNSLSMFDELRNALMAHYDKNVVEFSK 342
Cdd:cd01312  240 YANLEEAEILASRGASIALCPRSNRLLNGGKLDVSELKKagIPVSLGTDGLSSNISLSLLDELRALLDLHPEEDLLELAS 319

                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 526271715 343 TLLKAATFNGSRALGLNKGVLKESFDADMISFKLPnKIEDINDICMQIILHTKFVDDVIIGG 404
Cdd:cd01312  320 ELLLMATLGGARALGLNNGEIEAGKRADFAVFELP-GPGIKEQAPLQFILHAKEVRHLFISG 380
SsnA COG0402
Cytosine/adenosine deaminase or related metal-dependent hydrolase [Nucleotide transport and ...
 3-405 3.31e-71

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: 229.33  E-value: 3.31e-71
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526271715   3 AISASYVVTCDENNRIIKDGAVVFDDKLI-EIDTLFEIKNKYPNLEIKELEeNSILMPGLVNSHIHLEFSANTTTLKYGN 81
Cdd:COG0402    3 LIRGAWVLTMDPAGGVLEDGAVLVEDGRIaAVGPGAELPARYPAAEVIDAG-GKLVLPGLVNTHTHLPQTLLRGLADDLP 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526271715  82 FYSWLNSVI-----KHREDLINKAT----NELIstklnkikKTGTTTIGAISSYSFDM-----EACIKSPINTVFFCEVI 147
Cdd:COG0402   82 LLDWLEEYIwpleaRLDPEDVYAGAllalAEML--------RSGTTTVADFYYVHPESadalaEAAAEAGIRAVLGRGLM 153

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526271715 148 GSKA-----DMVDTLFADFRSRLNNAKKFASKNFIPAIAIHSPYSVHPFLVREALNVARDENLAVSSHFLESQEEFEWLH 222
Cdd:COG0402  154 DRGFpdglrEDADEGLADSERLIERWHGAADGRIRVALAPHAPYTVSPELLRAAAALARELGLPLHTHLAETRDEVEWVL 233

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526271715 223 KDEGsfleffknflnqekatSKPMEFL---GLFSkvKNLSFTHCVEASDDDLEKIKDLGASINHCVTSNRLLNNTKLDLD 299
Cdd:COG0402  234 ELYG----------------KRPVEYLdelGLLG--PRTLLAHCVHLTDEEIALLAETGASVAHCPTSNLKLGSGIAPVP 295

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526271715 300 RLKD--IPFTIGTDGLSSNNSLSMFDELRNALMAH----YDKNVVEfSKTLLKAATFNGSRALGLNK--GVLKESFDADM 371
Cdd:COG0402  296 RLLAagVRVGLGTDGAASNNSLDMFEEMRLAALLQrlrgGDPTALS-AREALEMATLGGARALGLDDeiGSLEPGKRADL 374

                        410       420       430
                 ....*....|....*....|....*....|....*..
gi 526271715 372 ISFKLPN-KIEDINDICMQIIL--HTKFVDDVIIGGE 405
Cdd:COG0402  375 VVLDLDApHLAPLHDPLSALVYaaDGRDVRTVWVAGR 411
ATZ_TRZ_like cd01298
TRZ/ATZ family contains enzymes from the atrazine degradation pathway and related hydrolases. ...
 9-407 1.86e-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: 169.69  E-value: 1.86e-48
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526271715   9 VVTCDENnRIIKDGAVVF-DDKLIEIDTLFEIKNkYPNLEIKELEEnSILMPGLVNSHIHLefsanTTTLKYG-----NF 82
Cdd:cd01298    8 IVTTDPR-RVLEDGDVLVeDGRIVAVGPALPLPA-YPADEVIDAKG-KVVMPGLVNTHTHL-----AMTLLRGladdlPL 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526271715  83 YSWLNSVI-----KHREDLINKATN----ELIstklnkikKTGTTTigAISSYSFDM----EACIKSPINTVFFCEVIgs 149
Cdd:cd01298   80 MEWLKDLIwplerLLTEEDVYLGALlalaEMI--------RSGTTT--FADMYFFYPdavaEAAEELGIRAVLGRGIM-- 147

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526271715 150 kaDMVDTLFADFRSRLNNAKKFASK-------NFIPAIAIHSPYSVHPFLVREALNVARDENLAVSSHFLESQEEFEWLH 222
Cdd:cd01298  148 --DLGTEDVEETEEALAEAERLIREwhgaadgRIRVALAPHAPYTCSDELLREVAELAREYGVPLHIHLAETEDEVEESL 225

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526271715 223 KDEGSFleffknflnqekatskPMEFL---GLFSKvkNLSFTHCVEASDDDLEKIKDLGASINHCVTSNRLLNNTKLDLD 299
Cdd:cd01298  226 EKYGKR----------------PVEYLeelGLLGP--DVVLAHCVWLTDEEIELLAETGTGVAHNPASNMKLASGIAPVP 287

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526271715 300 RLKD--IPFTIGTDGLSSNNSLSMFDELRNALM----AHYDKNVVEfSKTLLKAATFNGSRALGLNK-GVLKESFDADMI 372
Cdd:cd01298  288 EMLEagVNVGLGTDGAASNNNLDMFEEMRLAALlqklAHGDPTALP-AEEALEMATIGGAKALGLDEiGSLEVGKKADLI 366

                        410       420       430
                 ....*....|....*....|....*....|....*....
gi 526271715 373 SFKLpNKIE--DINDICMQIILHTK--FVDDVIIGGEYV 407
Cdd:cd01298  367 LIDL-DGPHllPVHDPISHLVYSANggDVDTVIVNGRVV 404
Amidohydro_1 pfam01979
Amidohydrolase family; This family of enzymes are a a large metal dependent hydrolase ...
 56-407 4.44e-36

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: 134.94  E-value: 4.44e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526271715   56 ILMPGLVNSHIHLEFSANTTTLKYGNFYSWLnsvikhredlINKATNELIstklnkikKTGTTTI-GAISSYSFDMEACI 134
Cdd:pfam01979   1 IVLPGLIDAHVHLEMGLLRGIPVPPEFAYEA----------LRLGITTML--------KSGTTTVlDMGATTSTGIEALL 62

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526271715  135 KSPINTVFFCEVIGSKADM--------VDTLFADFRSRLNNAKKFASKNFIPAIAIHSPYSVHPFLVREALNVARDENLA 206
Cdd:pfam01979  63 EAAEELPLGLRFLGPGCSLdtdgelegRKALREKLKAGAEFIKGMADGVVFVGLAPHGAPTFSDDELKAALEEAKKYGLP 142

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526271715  207 VSSHFLESQEEFEWLHKDEGSFLEFfknflnqekatSKPMEFLG--LFSKVKNLSFTHCVEASDDDLEKIKD--LGASIN 282
Cdd:pfam01979 143 VAIHALETKGEVEDAIAAFGGGIEH-----------GTHLEVAEsgGLLDIIKLILAHGVHLSPTEANLLAEhlKGAGVA 211

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526271715  283 HCVTSNRLLNNTKLDLDRLKD--IPFTIGTDGLSSNNSLSMFDELRNALMAHYDKNVVEFSKTLLKAATFNGSRALGL-- 358
Cdd:pfam01979 212 HCPFSNSKLRSGRIALRKALEdgVKVGLGTDGAGSGNSLNMLEELRLALELQFDPEGGLSPLEALRMATINPAKALGLdd 291

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*....
gi 526271715  359 NKGVLKESFDADMISFKLpNKIEDINDicmqiILHTKFVDDVIIGGEYV 407
Cdd:pfam01979 292 KVGSIEVGKDADLVVVDL-DPLAAFFG-----LKPDGNVKKVIVKGKIV 334
PRK06038 PRK06038
N-ethylammeline chlorohydrolase; Provisional
 4-372 1.81e-29

N-ethylammeline chlorohydrolase; Provisional


Pssm-ID: 180363 [Multi-domain]  Cd Length: 430  Bit Score: 118.70  E-value: 1.81e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526271715   4 ISASYVVTCDENNriIKDGAVVFDDKLIEidtlfEIKNKYPNLEIKELE-ENSILMPGLVNSHIHLefsANTTTLKYGN- 81
Cdd:PRK06038   6 IKNAYVLTMDAGD--LKKGSVVIEDGTIT-----EVSESTPGDADTVIDaKGSVVMPGLVNTHTHA---AMTLFRGYADd 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526271715  82 --FYSWLNSVIKHREDLINkATNELISTKLNKIK--KTGTTTIgaiSSYSFDMEACIKSpintvffCEVIGSKA----DM 153
Cdd:PRK06038  76 lpLAEWLNDHIWPAEAKLT-AEDVYAGSLLACLEmiKSGTTSF---ADMYFYMDEVAKA-------VEESGLRAalsyGM 144

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526271715 154 VDtlFADFRSRLNNAKKfaSKNFIP------------AIAIHSPYSVHPFLVREALNVARDENLAVSSHFLESQEEFEWL 221
Cdd:PRK06038 145 ID--LGDDEKGEAELKE--GKRFVKewhgaadgrikvMYGPHAPYTCSEEFLSKVKKLANKDGVGIHIHVLETEAELNQM 220

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526271715 222 HKDEGsfleffknflnqeKATSKPMEFLGLFSKvkNLSFTHCVEASDDDLEKIKDLGASINHCVTSNRLLNNTKLDLDRL 301
Cdd:PRK06038 221 KEQYG-------------MCSVNYLDDIGFLGP--DVLAAHCVWLSDGDIEILRERGVNVSHNPVSNMKLASGIAPVPKL 285

                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 526271715 302 --KDIPFTIGTDGLSSNNSLSMFDELRNALMAHydkNVVEFSKTLLKA------ATFNGSRALGLNKGVLKESFDADMI 372
Cdd:PRK06038 286 leRGVNVSLGTDGCASNNNLDMFEEMKTAALLH---KVNTMDPTALPArqvlemATVNGAKALGINTGMLKEGYLADII 361
PRK06687 PRK06687
TRZ/ATZ family protein;
1-407 1.85e-28

TRZ/ATZ family protein;


Pssm-ID: 180657 [Multi-domain]  Cd Length: 419  Bit Score: 115.49  E-value: 1.85e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526271715   1 MKAISASYVVTCDENNRIIKDGAVVFDDKLI----EIDTLFEIKNKypnlEIKELEeNSILMPGLVNSHIHLEFSANTTT 76
Cdd:PRK06687   1 MKVFQHVNIVTCDQDFHVYLDGILAVKDSQIvyvgQDKPAFLEQAE----QIIDYQ-GAWIMPGLVNCHTHSAMTGLRGI 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526271715  77 LKYGNFYSWLNSVIKHREDLIN-KATNELISTKLNKIKKTGTTTIGAI-SSYSFDM----EACIKSPINTVFFCEVIGSK 150
Cdd:PRK06687  76 RDDSNLHEWLNDYIWPAESEFTpDMTTNAVKEALTEMLQSGTTTFNDMyNPNGVDIqqiyQVVKTSKMRCYFSPTLFSSE 155

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526271715 151 ADMVDTLFADFRSRLNNAKKFASKNFIPAIAIHSPYSVHPFLVREALNVARDENLAVSSHFLESQEEfewlhkdegsfle 230
Cdd:PRK06687 156 TETTAETISRTRSIIDEILKYKNPNFKVMVAPHSPYSCSRDLLEASLEMAKELNIPLHVHVAETKEE------------- 222

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526271715 231 ffkNFLNQEKATSKPMEFLGLFSKVKNLS-FTHCVEASDDDLEKIKDLGASINHCVTSNRLLNNTKLDLDRLKDIPFTIG 309
Cdd:PRK06687 223 ---SGIILKRYGKRPLAFLEELGYLDHPSvFAHGVELNEREIERLASSQVAIAHNPISNLKLASGIAPIIQLQKAGVAVG 299

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526271715 310 --TDGLSSNNSLSMFDELRNA--LMAHYDKNVVEFS-KTLLKAATFNGSRALGLNK--GVLKESFDADMISFKLPNKI-- 380
Cdd:PRK06687 300 iaTDSVASNNNLDMFEEGRTAalLQKMKSGDASQFPiETALKVLTIEGAKALGMENqiGSLEVGKQADFLVIQPQGKIhl 379

                        410       420
                 ....*....|....*....|....*....
gi 526271715 381 EDINDICMQIILHTKF--VDDVIIGGEYV 407
Cdd:PRK06687 380 QPQENMLSHLVYAVKSsdVDDVYIAGEQV 408
PRK08393 PRK08393
N-ethylammeline chlorohydrolase; Provisional
 18-407 2.16e-25

N-ethylammeline chlorohydrolase; Provisional


Pssm-ID: 181411 [Multi-domain]  Cd Length: 424  Bit Score: 106.81  E-value: 2.16e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526271715  18 IIKDGAVVFDD--KLIEIDTLFEiknkypNLEIKELEEN-------------SILMPGLVNSHIH-----LEFSANTTTL 77
Cdd:PRK08393   4 LIKNGYVIYGEnlKVIRADVLIE------GNKIVEVKRNinkpadtvidasgSVVSPGFINAHTHspmvlLRGLADDVPL 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526271715  78 KygnfySWLNSVIKHREdliNKATNELI--STKLNKIK--KTGTTTIgaISSYsFDMEACIKSPINtvffcevIGSKA-- 151
Cdd:PRK08393  78 M-----EWLQNYIWPRE---RKLKRKDIywGAYLGLLEmiKSGTTTF--VDMY-FHMEEVAKATLE-------VGLRGyl 139

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526271715 152 --DMVDTLFADFRSR-LNNAKK---FASK------NFIpaIAIHSPYSVHPFLVREALNVARDENLAVSSHFLESQEEFE 219
Cdd:PRK08393 140 syGMVDLGDEEKREKeIKETEKlmeFIEKlnsprvHFV--FGPHAPYTCSLALLKWVREKAREWNKLITIHLSETMDEIK 217

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526271715 220 WLhkdegsfleffknflnQEKATSKPMEFL---GLFSKvkNLSFTHCVEASDDDLEKIKDLGASINHCVTSNRLLNNTKL 296
Cdd:PRK08393 218 QI----------------REKYGKSPVVLLdeiGFLNE--DVIAAHGVWLSSRDIRILASAGVTVAHNPASNMKLGSGVM 279

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526271715 297 DLDRL--KDIPFTIGTDGLSSNNSLSMFDELRNALM----AHYDKNVVEfSKTLLKAATFNGSRALGLNKGVLKESFDAD 370
Cdd:PRK08393 280 PLRKLlnAGVNVALGTDGAASNNNLDMLREMKLAALlhkvHNLDPTIAD-AETVFRMATQNGAKALGLKAGVIKEGYLAD 358

                        410       420       430       440
                 ....*....|....*....|....*....|....*....|.
gi 526271715 371 M--ISFKLPNkIEDINDICMQIILHTKF--VDDVIIGGEYV 407
Cdd:PRK08393 359 IavIDFNRPH-LRPINNPISHLVYSANGndVETTIVDGKIV 398
GDEase cd01303
Guanine deaminase (GDEase). Guanine deaminase is an aminohydrolase responsible for the ...
 17-372 3.92e-22

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: 97.35  E-value: 3.92e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526271715  17 RIIKDGAVVFDDKLIEI-DTLFEIKNKYPNLEIKELEENSILMPGLVNSHIHLEFSANTttlkyGNFYS-----WLNS-- 88
Cdd:cd01303   22 RVVEDGLIVVVDGNIIAaGAAETLKRAAKPGARVIDSPNQFILPGFIDTHIHAPQYANI-----GSGLGeplldWLETyt 96

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526271715  89 -VIKHR-EDLiNKATNelISTK-LNKIKKTGTTTIGAISSYSFD-----MEACIKSPIntvffcEVIGSKADMvDTLFAD 160
Cdd:cd01303   97 fPEEAKfADP-AYARE--VYGRfLDELLRNGTTTACYFATIHPEstealFEEAAKRGQ------RAIAGKVCM-DRNAPE 166

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526271715 161 FRsrLNNAKKF--ASKNFIPAIAIHSP---YSVHP-F-------LVREALNVARDEN-LAVSSHFLESQEEFEW---LHK 223
Cdd:cd01303  167 YY--RDTAESSyrDTKRLIERWHGKSGrvkPAITPrFapscseeLLAALGKLAKEHPdLHIQTHISENLDEIAWvkeLFP 244

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526271715 224 DEGSFLEFFKNFlnqekatskpmeflGLFSKvkNLSFTHCVEASDDDLEKIKDLGASINHCVTSNRLLNNTKLDLDRLKD 303
Cdd:cd01303  245 GARDYLDVYDKY--------------GLLTE--KTVLAHCVHLSEEEFNLLKERGASVAHCPTSNLFLGSGLFDVRKLLD 308

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526271715 304 --IPFTIGTDgLSSNNSLSMFDELRNALMAHYDKNVVEFSKTLLKA------ATFNGSRALGL-----NKGVLKEsFDAD 370
Cdd:cd01303  309 agIKVGLGTD-VGGGTSFSMLDTLRQAYKVSRLLGYELGGHAKLSPaeafylATLGGAEALGLddkigNFEVGKE-FDAV 386


                 ..
gi 526271715 371 MI 372
Cdd:cd01303  387 VI 388
metallo-dependent_hydrolases cd01292
Superfamily of metallo-dependent hydrolases (also called amidohydrolase superfamily) is a ...
 61-355 1.22e-20

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: 90.86  E-value: 1.22e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526271715  61 LVNSHIHLEFSANTTTLKYGNFYSWLNSVIKHREDLINKATNELIstklnkikKTGTTTIGAISSYSFDM---------- 130
Cdd:cd01292    1 FIDTHVHLDGSALRGTRLNLELKEAEELSPEDLYEDTLRALEALL--------AGGVTTVVDMGSTPPPTttkaaieava 72

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526271715 131 EACIKSPINTVFFCEVIGSKADMVDtlfADFRSRLNNAKKFASKNFIPAIAIHSPYSVHPFLVREALNV---ARDENLAV 207
Cdd:cd01292   73 EAARASAGIRVVLGLGIPGVPAAVD---EDAEALLLELLRRGLELGAVGLKLAGPYTATGLSDESLRRVleeARKLGLPV 149

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526271715 208 SSHFLESqeefewlhKDEGSFLEffknflnqekatskpmEFLGLFSKVKNLSFTHCVEASDDDLEKIKDLGASINHCVTS 287
Cdd:cd01292  150 VIHAGEL--------PDPTRALE----------------DLVALLRLGGRVVIGHVSHLDPELLELLKEAGVSLEVCPLS 205

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 526271715 288 NRLLNNTKLDLDRLK-----DIPFTIGTDGLSSNNSLSMFDELRNALMAHYDKNVVEfskTLLKAATFNGSRA 355
Cdd:cd01292  206 NYLLGRDGEGAEALRrllelGIRVTLGTDGPPHPLGTDLLALLRLLLKVLRLGLSLE---EALRLATINPARA 275
PRK09045 PRK09045
TRZ/ATZ family hydrolase;
4-376 2.02e-20

TRZ/ATZ family hydrolase;


Pssm-ID: 236366 [Multi-domain]  Cd Length: 443  Bit Score: 92.67  E-value: 2.02e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526271715   4 ISASYVVTCDENNRIIKDGAVVFDDKLIeIDTL--FEIKNKYPNLEIKELEENsILMPGLVNSHIHLEFS-----ANTTT 76
Cdd:PRK09045  11 IEARWIVPVEPAGVVLEDHAVAIRDGRI-VAILprAEARARYAAAETVELPDH-VLIPGLINAHTHAAMSllrglADDLP 88

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526271715  77 LkygnfYSWLNSVI-----KH-REDLINKATNELISTKLnkikKTGTTTIGaissysfDM--------EACIKSPINTVF 142
Cdd:PRK09045  89 L-----MTWLQDHIwpaegAWvSEEFVRDGTLLAIAEML----RGGTTCFN-------DMyffpeaaaEAAHQAGMRAQI 152

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526271715 143 FCEVI------GSKADmvD------TLFADFR--SRLNnakkfasknfiPAIAIHSPYSVHPFLVREALNVARDENLAVS 208
Cdd:PRK09045 153 GMPVLdfptawASDAD--EylakglELHDQWRhhPLIS-----------TAFAPHAPYTVSDENLERIRTLAEQLDLPIH 219

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526271715 209 SHFLESQEEFEwlhkdegsfleffknflNQEKATSK-PMEF---LGLFSKvkNLSFTHCVEASDDDLEKIKDLGASINHC 284
Cdd:PRK09045 220 IHLHETAQEIA-----------------DSLKQHGQrPLARlarLGLLGP--RLIAVHMTQLTDAEIALLAETGCSVVHC 280

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526271715 285 VTSNRLLNNTKLDLDRLKD--IPFTIGTDGLSSNNSLSMFDELRNA-LMAhydKNVVEFSKTL-----LKAATFNGSRAL 356
Cdd:PRK09045 281 PESNLKLASGFCPVAKLLQagVNVALGTDGAASNNDLDLFGEMRTAaLLA---KAVAGDATALpahtaLRMATLNGARAL 357

                        410       420
                 ....*....|....*....|..
gi 526271715 357 GLNK--GVLKESFDADMISFKL 376
Cdd:PRK09045 358 GLDDeiGSLEPGKQADLVAVDL 379
PRK06380 PRK06380
metal-dependent hydrolase; Provisional
 3-405 8.71e-18

metal-dependent hydrolase; Provisional


Pssm-ID: 180548 [Multi-domain]  Cd Length: 418  Bit Score: 84.55  E-value: 8.71e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526271715   3 AISASYVVTCDENNRIIKDgavvfdDKLIEIDTLFEIKNKYPNLEIKELEENSILMPGLVNSHIHLEFSANTTTLKYGNF 82
Cdd:PRK06380   4 LIKNAWIVTQNEKREILQG------NVYIEGNKIVYVGDVNEEADYIIDATGKVVMPGLINTHAHVGMTASKGLFDDVDL 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526271715  83 YSWLNSVIKHREDlinKATNELISTKLNKIKKTGTTTIGAISSYSFDMEACIKSpintvffCEVIGSKADMV-DTLFADF 161
Cdd:PRK06380  78 EEFLMKTFKYDSK---RTREGIYNSAKLGMYEMINSGITAFVDLYYSEDIIAKA-------AEELGIRAFLSwAVLDEEI 147

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526271715 162 RSR----LNNAKKF-----ASKNFIPAIAIHSPYSVHPFLVREALNVARDENLAVSSHFLESQEE------------FEW 220
Cdd:PRK06380 148 TTQkgdpLNNAENFirehrNEELVTPSIGVQGIYVANDETYLKAKEIAEKYDTIMHMHLSETRKEvydhvkrtgerpVEH 227

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526271715 221 LHKdegsfleffKNFLNqekatskpmeflglfskvKNLSFTHCVEASDDDLEKIKDLGASINHCVTSN-RLLNNTKLDLD 299
Cdd:PRK06380 228 LEK---------IGFLN------------------SKLIAAHCVWATYHEIKLLSKNGVKVSWNSVSNfKLGTGGSPPIP 280

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526271715 300 RLKD--IPFTIGTDGLSSNNSLSMFDELRNALMAH----YDKNVVEfSKTLLKAATFNGSRALGLNKGVLKESFDADMIS 373
Cdd:PRK06380 281 EMLDngINVTIGTDSNGSNNSLDMFEAMKFSALSVknerWDASIIK-AQEILDFATINAAKALELNAGSIEVGKLADLVI 359

                        410       420       430
                 ....*....|....*....|....*....|....*..
gi 526271715 374 F--KLPNKI-EDINDICMQIILHT--KFVDDVIIGGE 405
Cdd:PRK06380 360 LdaRAPNMIpTRKNNIVSNIVYSLnpLNVDHVIVNGK 396
PRK15493 PRK15493
bifunctional S-methyl-5'-thioadenosine deaminase/S-adenosylhomocysteine deaminase;
9-407 2.82e-17

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


Pssm-ID: 185390 [Multi-domain]  Cd Length: 435  Bit Score: 83.18  E-value: 2.82e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526271715   9 VVTCDENNRIIKDGAVVF-DDKLIEIDTlfeiKNKYPNLEIKELEE--NSILMPGLVNSHIHLEFSANTTTLKYGNFYSW 85
Cdd:PRK15493  10 IVTMNEQNEVIENGYIIVeNDQIIDVNS----GEFASDFEVDEVIDmkGKWVLPGLVNTHTHVVMSLLRGIGDDMLLQPW 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526271715  86 LNSVIKHREdliNKATNELI--STKLNKIK--KTGTTTIGAI-SSYSFDMEACIKSPINTvffceviGSKADMVDTLFA- 159
Cdd:PRK15493  86 LETRIWPLE---SQFTPELAvaSTELGLLEmvKSGTTSFSDMfNPIGVDQDAIMETVSRS-------GMRAAVSRTLFSf 155

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526271715 160 ----DFRSRLNNAKKFASKNF------IPAIAIHSPYSVHPFLVREALNVARDENLAVSSHFLESQEEFEWLHKDEGSfl 229
Cdd:PRK15493 156 gtkeDEKKAIEEAEKYVKRYYnesgmlTTMVAPHSPYTCSTELLEECARIAVENQTMVHIHLSETEREVRDIEAQYGK-- 233

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526271715 230 effknflnqekatsKPMEFL---GLFSKVKNLSftHCVEASDDDLEKIKDLGASINHCVTSNRLLNNTKLDLDRLKD--I 304
Cdd:PRK15493 234 --------------RPVEYAascGLFKRPTVIA--HGVVLNDNERAFLAEHDVRVAHNPNSNLKLGSGIANVKAMLEagI 297

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526271715 305 PFTIGTDGLSSNNSLSMFDELRNALM----AHYDKNVVEFsKTLLKAATFNGSRALGLNK-GVLKESFDADMISFKLPNK 379
Cdd:PRK15493 298 KVGIATDSVASNNNLDMFEEMRIATLlqkgIHQDATALPV-ETALTLATKGAAEVIGMKQtGSLEVGKCADFITIDPSNK 376

                        410       420       430
                 ....*....|....*....|....*....|..
gi 526271715 380 --IEDINDICMQIILHT--KFVDDVIIGGEYV 407
Cdd:PRK15493 377 phLQPADEVLSHLVYAAsgKDISDVIINGKRV 408
PRK07228 PRK07228
5'-deoxyadenosine deaminase;
9-372 1.34e-16

5'-deoxyadenosine deaminase;


Pssm-ID: 180895 [Multi-domain]  Cd Length: 445  Bit Score: 81.20  E-value: 1.34e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526271715   9 VVTCDENnRIIKDGAVVFDDKLIEIDTLFEIKNKYPNLEIKEleeNSILMPGLVNSHIHLefsanTTTLKYG-----NFY 83
Cdd:PRK07228  10 IVTMNAK-REIVDGDVLIEDDRIAAVGDRLDLEDYDDHIDAT---GKVVIPGLIQGHIHL-----CQTLFRGiaddlELL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526271715  84 SWLNSVIKHREDLINKATNElISTKLN--KIKKTGTTTI---GAISSYSFDMEACIKSPINTVFFCEVIGSKADMVDTLF 158
Cdd:PRK07228  81 DWLKDRIWPLEAAHDAESMY-YSALLGigELIESGTTTIvdmESVHHTDSAFEAAGESGIRAVLGKVMMDYGDDVPEGLQ 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526271715 159 ADFRSRLNNA----KKFASKN-------FIPAIAIhspySVHPFLVREALNVARDENLAVSSHFLESQEEFEWLHKDEGs 227
Cdd:PRK07228 160 EDTEASLAESvrllEKWHGADngriryaFTPRFAV----SCTEELLRGVRDLADEYGVRIHTHASENRGEIETVEEETG- 234

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526271715 228 flefFKNFLNQEKatskpmefLGLFSKvkNLSFTHCVEASDDDLEKIKDLGASINHCVTSNRLLNNTKLDLDRLKD--IP 305
Cdd:PRK07228 235 ----MRNIHYLDE--------VGLTGE--DLILAHCVWLDEEEREILAETGTHVTHCPSSNLKLASGIAPVPDLLErgIN 300

                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 526271715 306 FTIGTDGLSSNNSLSMFDELRNALMAH----YDKNVVEfSKTLLKAATFNGSRALGLNK--GVLKESFDADMI 372
Cdd:PRK07228 301 VALGADGAPCNNTLDPFTEMRQAALIQkvdrLGPTAMP-ARTVFEMATLGGAKAAGFEDeiGSLEEGKKADLA 372
PRK07203 PRK07203
putative aminohydrolase SsnA;
1-407 3.09e-13

putative aminohydrolase SsnA;


Pssm-ID: 235963 [Multi-domain]  Cd Length: 442  Bit Score: 70.73  E-value: 3.09e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526271715   1 MKAISASYVVTCDENNRIIKDGAVVFDDKLI-EIDTLFEIKNKYPNLEIKELEeNSILMPGLVNSHIHLefsantttlkY 79
Cdd:PRK07203   1 MLLIGNGTAITRDPAKPVIEDGAIAIEGNVIvEIGTTDELKAKYPDAEFIDAK-GKLIMPGLINSHNHI----------Y 69

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526271715  80 GNFYSWLNSVIKHREDLIN----------KATNE-------LIsTKLNKIkKTGTTTI-------GAISSYSFDM-EACI 134
Cdd:PRK07203  70 SGLARGMMANIPPPPDFISilknlwwrldRALTLedvyysaLI-CSLEAI-KNGVTTVfdhhaspNYIGGSLFTIaDAAK 147

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526271715 135 KSPINTVFFCEVigSKADMVDTLFADFRSRLNNAKKF--ASKNFIPA-IAIHSPYSvhpfLVREALNVARDENLAVSS-- 209
Cdd:PRK07203 148 KVGLRAMLCYET--SDRDGEKELQEGVEENIRFIKHIdeAKDDMVEAmFGLHASFT----LSDATLEKCREAVKETGRgy 221

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526271715 210 --HFLESQEEFEWLHKDEG-SFLEFFKNFlnqekatskpmeflGLFSKvKNLSfTHCVEASDDDLEKIKDLGASINHCVT 286
Cdd:PRK07203 222 hiHVAEGIYDVSDSHKKYGkDIVERLADF--------------GLLGE-KTLA-AHCIYLSDEEIDLLKETDTFVVHNPE 285

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526271715 287 SNrlLNNT-----KLDLDRlKDIPFTIGTDGLSSNnslsMFDELRNALMAHYDKN---VVEFSKTLLKAATFNG---SRA 355
Cdd:PRK07203 286 SN--MGNAvgynpVLEMIK-NGILLGLGTDGYTSD----MFESYKVANFKHKHAGgdpNVGWPESPAMLFENNNkiaERY 358

                        410       420       430       440       450
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 526271715 356 LGLNKGVLKESFDADMI--SFKLPNKIEDiNDICMQII--LHTKFVDDVIIGGEYV 407
Cdd:PRK07203 359 FGAKFGILEEGAKADLIivDYNPPTPLNE-DNINGHILfgMNGGSVDTTIVNGKVV 413
PRK12393 PRK12393
amidohydrolase; Provisional
 185-376 1.31e-11

amidohydrolase; Provisional


Pssm-ID: 237088 [Multi-domain]  Cd Length: 457  Bit Score: 65.86  E-value: 1.31e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526271715 185 PYSVHPFLVREALNVARDENLAVSSHFLESQEefewlhkdegsFLEFFknflnQEKATSKPMEF------LGlfskvKNL 258
Cdd:PRK12393 212 TFSLPPELLREVARAARGMGLRLHSHLSETVD-----------YVDFC-----REKYGMTPVQFvaehdwLG-----PDV 270

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526271715 259 SFTHCVEASDDDLEKIKDLGASINHCVTSNRLLNNTKLDLDRLKD--IPFTIGTDGLSSNNSLSMFDELRNALMAHY--- 333
Cdd:PRK12393 271 WFAHLVKLDAEEIALLAQTGTGIAHCPQSNGRLGSGIAPALAMEAagVPVSLGVDGAASNESADMLSEAHAAWLLHRaeg 350

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*.
gi 526271715 334 --DKNVVEfskTLLKAATFNGSRALGLNK-GVLKESFDADMISFKL 376
Cdd:PRK12393 351 gaDATTVE---DVVHWGTAGGARVLGLDAiGTLAVGQAADLAIYDL 393
PRK07213 PRK07213
chlorohydrolase; Provisional
 254-404 2.24e-09

chlorohydrolase; Provisional


Pssm-ID: 235969 [Multi-domain]  Cd Length: 375  Bit Score: 58.51  E-value: 2.24e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526271715 254 KVKNLSFTHCVEASDDDLEKIKDLGASINHCVTSNRLLNNTKLDLDRL--KDIPFTIGTDGLSSnNSLSMFDELRNALMA 331
Cdd:PRK07213 225 GFKPDFIVHATHPSNDDLELLKENNIPVVVCPRANASFNVGLPPLNEMleKGILLGIGTDNFMA-NSPSIFREMEFIYKL 303

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 526271715 332 HYdknvVEfSKTLLKAATFNGSRALGL-NKGVLKESFDADmISFKLPNKIEDINDICMQIILHT--KFVDDVIIGG 404
Cdd:PRK07213 304 YH----IE-PKEILKMATINGAKILGLiNVGLIEEGFKAD-FTFIKPTNIKFSKNPYASIITRCesGDIVNKILKG 373
PRK08203 PRK08203
hydroxydechloroatrazine ethylaminohydrolase; Reviewed
 179-376 2.21e-08

hydroxydechloroatrazine ethylaminohydrolase; Reviewed


Pssm-ID: 236184 [Multi-domain]  Cd Length: 451  Bit Score: 55.63  E-value: 2.21e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526271715 179 AIAIHSPYSVHPFLVREALNVARDENLAVSSHFLESQEEFEWlhkdegsfleffknflNQEKATSKPMEFLglfSKVKNL 258
Cdd:PRK08203 202 ALAPCSPFSVSRELMRESAALARRLGVRLHTHLAETLDEEAF----------------CLERFGMRPVDYL---EDLGWL 262

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526271715 259 S----FTHCVEASDDDLEKIKDLGASINHCVTSNRLLNN---TKLDLdRLKDIPFTIGTDGLSSNNSLSMFDELRNALM- 330
Cdd:PRK08203 263 GpdvwLAHCVHLDDAEIARLARTGTGVAHCPCSNMRLASgiaPVREL-RAAGVPVGLGVDGSASNDGSNLIGEARQALLl 341

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
gi 526271715 331 --AHYDKNVVEfSKTLLKAATFNGSRALGLNK-GVLKESFDADMISFKL 376
Cdd:PRK08203 342 qrLRYGPDAMT-AREALEWATLGGARVLGRDDiGSLAPGKLADLALFDL 389
HutI COG1228
Imidazolonepropionase or related amidohydrolase [Secondary metabolites biosynthesis, transport ...
 9-407 2.64e-08

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


Pssm-ID: 440841 [Multi-domain]  Cd Length: 386  Bit Score: 55.35  E-value: 2.64e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526271715   9 VVTcDENNRIIKDGAVVFDDKLI-EIDTLFEIKNKyPNLEIKELEeNSILMPGLVNSHIHLEFSANtttlkyGNFYSWLN 87
Cdd:COG1228   17 LVD-GTGGGVIENGTVLVEDGKIaAVGPAADLAVP-AGAEVIDAT-GKTVLPGLIDAHTHLGLGGG------RAVEFEAG 87

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526271715  88 SVIKHREDLINKATNELISTKLNkikktGTTTIGAISSYSFDMEACIKS------PINTVFFCEVI-----GSKADMVDT 156
Cdd:COG1228   88 GGITPTVDLVNPADKRLRRALAA-----GVTTVRDLPGGPLGLRDAIIAgeskllPGPRVLAAGPAlsltgGAHARGPEE 162

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526271715 157 LFADFRsrlNNAKKFASknfipAIAIHSPYSVHPF---LVREALNVARDENLAVSSHflesqeefewLHKDEGSFLeffk 233
Cdd:COG1228  163 ARAALR---ELLAEGAD-----YIKVFAEGGAPDFsleELRAILEAAHALGLPVAAH----------AHQADDIRL---- 220

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526271715 234 nflnqekAtskpMEFlglfsKVKnlSFTHCVEASDDDLEKIKD-----------------LGASINHCVTSNRLLNNTKL 296
Cdd:COG1228  221 -------A----VEA-----GVD--SIEHGTYLDDEVADLLAEagtvvlvptlslflallEGAAAPVAAKARKVREAALA 282

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526271715 297 DLDRLKD--IPFTIGTDGLSSNNS-LSMFDELrnALMAHYDknvveFSKT-LLKAATFNGSRALGLNK--GVLKESFDAD 370
Cdd:COG1228  283 NARRLHDagVPVALGTDAGVGVPPgRSLHREL--ALAVEAG-----LTPEeALRAATINAAKALGLDDdvGSLEPGKLAD 355

                        410       420       430
                 ....*....|....*....|....*....|....*..
gi 526271715 371 MIsfklpnkIEDINDicMQIILHTKFVDDVIIGGEYV 407
Cdd:COG1228  356 LV-------LLDGDP--LEDIAYLEDVRAVMKDGRVV 383
archeal_chlorohydrolases cd01305
Predicted chlorohydrolases. These metallo-dependent hydrolases from archea are part of the ...
 56-353 6.13e-08

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: 53.56  E-value: 6.13e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526271715  56 ILMPGLVNSHIHL------EFSANTTTLKygnFYSWLNSViKHRedLINKATNELIstkLNKIKKTGTTTIGAISSYSFD 129
Cdd:cd01305    1 ILIPALVNAHTHLgdsaikEVGDGLPLDD---LVAPPDGL-KHR--LLAQADDREL---AEAMRKVLRDMRETGIGAFAD 71

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526271715 130 MEAcikspiNTVFFCEVIGSKADMVDTLFADFRSRLNN----AKKFASKNFIpaiAIHSPYSVHPFLVREALnvaRDENL 205
Cdd:cd01305   72 FRE------GGVEGIELLRRALGKLPVPFEVILGRPTEpddpEILLEVADGL---GLSSANDVDLEDILELL---RRRGK 139

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526271715 206 AVSSHFLESQEEfeWLHKDegsfleffknflnQEKATSKPMEFLglfskvknlsfTHCVEASDDDLEKIKDLGASINHCV 285
Cdd:cd01305  140 LFAIHASETRES--VGMTD-------------IERALDLEPDLL-----------VHGTHLTDEDLELVRENGVPVVLCP 193

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526271715 286 TSNRLLNNTKLDLDRLKD--IPFTIGTDGLSSnNSLSMFDELRNAlMAHYDKNVVEFSKTLLKAATFNGS 353
Cdd:cd01305  194 RSNLYFGVGIPPVAELLKlgIKVLLGTDNVMV-NEPDMWAEMEFL-AKYSRLQGYLSPLEILRMATVNAA 261
PRK09228 PRK09228
guanine deaminase; Provisional
 207-372 4.50e-07

guanine deaminase; Provisional


Pssm-ID: 236419 [Multi-domain]  Cd Length: 433  Bit Score: 51.73  E-value: 4.50e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526271715 207 VSSHFLESQEEFEW---LHKDEGSFLEFFKNF-LNQEKATskpmeflglfskvknlsFTHCVEASDDDLEKIKDLGASIN 282
Cdd:PRK09228 228 IQTHLSENLDEIAWvkeLFPEARDYLDVYERYgLLGPRAV-----------------FAHCIHLEDRERRRLAETGAAIA 290

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526271715 283 HCVTSNRLLNNTKLDLDRL--KDIPFTIGTD---GlssnNSLSMFDELrnaLMAHYdknVVEFSKTLLKA------ATFN 351
Cdd:PRK09228 291 FCPTSNLFLGSGLFDLKRAdaAGVRVGLGTDvggG----TSFSMLQTM---NEAYK---VQQLQGYRLSPfqafylATLG 360

                        170       180
                 ....*....|....*....|...
gi 526271715 352 GSRALGLNK--GVLKESFDADMI 372
Cdd:PRK09228 361 GARALGLDDriGNLAPGKEADFV 383
Met_dep_hydrolase_E cd01313
Metallo-dependent hydrolases, subgroup D is part of the superfamily of metallo-dependent ...
 180-405 6.70e-07

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: 50.92  E-value: 6.70e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526271715 180 IAIHSPYSVHPFLVREALNVArDENLAVSSHFLESQEEFEWLHKDEGSfleffknflnqekatsKPMEFLgLFSKVKNLS 259
Cdd:cd01313  196 VAPHSLRAVPAEQLAALAALA-SEKAPVHIHLAEQPKEVDDCLAAHGR----------------RPVELL-LDHGHLDAR 257

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526271715 260 FT--HCVEASDDDLEKIKDLGASINHCVTSNRLLNNTKLDLDRLKDI--PFTIGTDglsSNNSLSMFDELR----NALMA 331
Cdd:cd01313  258 WClvHATHLTDNETLLLGRSGAVVGLCPTTEANLGDGIFPAAALLAAggRIGIGSD---SNARIDLLEELRqleySQRLR 334

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526271715 332 HYDKNVVEFS-----KTLLKAATFNGSRALGLNKGVLKESFDADMISFKL--PNKIEDINDICMQIIL---HTKFVDDVI 401
Cdd:cd01313  335 DRARNVLATAggssaRALLDAALAGGAQALGLATGALEAGARADLLSLDLdhPSLAGALPDTLLDAWVfaaGDREVRDVV 414


                 ....
gi 526271715 402 IGGE 405
Cdd:cd01313  415 VGGR 418
Imidazolone-5PH cd01296
Imidazolonepropionase/imidazolone-5-propionate hydrolase (Imidazolone-5PH) catalyzes the third ...
 24-378 7.49e-07

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: 50.72  E-value: 7.49e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526271715  24 VVFDDKLIEIDTLFEIKNKYPNlEIKELE-ENSILMPGLVNSHIHL--------EFSANTTTLKY-------GNFYSwln 87
Cdd:cd01296    2 AIRDGRIAAVGPAASLPAPGPA-AAEEIDaGGRAVTPGLVDCHTHLvfagdrvdEFAARLAGASYeeilaagGGILS--- 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526271715  88 SVIKHR----EDLINKATnelisTKLNKIKKTGTTTIGAISSYSFDMEACIKspintvffcevigskadMVDTLfadfrS 163
Cdd:cd01296   78 TVRATRaaseDELFASAL-----RRLARMLRHGTTTVEVKSGYGLDLETELK-----------------MLRVI-----R 130

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526271715 164 RLNNAKKFA-SKNFIPAIAIHSPYSVHP----FLVREALNVARDENLAvsshflesqeEFEWLHKDEGSF-LEFFKNFLN 237
Cdd:cd01296  131 RLKEEGPVDlVSTFLGAHAVPPEYKGREeyidLVIEEVLPAVAEENLA----------DFCDVFCEKGAFsLEQSRRILE 200

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526271715 238 QEKATSKPMEF-------LG---LFSKVKNLSFTHCVEASDDDLEKIKDLGASINHCVTSNRLLNNTKLDLDRLKD--IP 305
Cdd:cd01296  201 AAKEAGLPVKIhadelsnIGgaeLAAELGALSADHLEHTSDEGIAALAEAGTVAVLLPGTAFSLRETYPPARKLIDagVP 280

                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 526271715 306 FTIGTDglssNNSLSMFDELRNALMA----HYDKNVVEfsktLLKAATFNGSRALGL--NKGVLKESFDADMISFKLPN 378
Cdd:cd01296  281 VALGTD----FNPGSSPTSSMPLVMHlacrLMRMTPEE----ALTAATINAAAALGLgeTVGSLEVGKQADLVILDAPS 351
PRK06151 PRK06151
N-ethylammeline chlorohydrolase; Provisional
 192-376 3.77e-05

N-ethylammeline chlorohydrolase; Provisional


Pssm-ID: 180428 [Multi-domain]  Cd Length: 488  Bit Score: 45.80  E-value: 3.77e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526271715 192 LVREALNVARDENLAVSSHFLESQEEFEWLHKDEGSfleffknflnqekatsKPMEFL---GLFSKVKNL-------SFT 261
Cdd:PRK06151 222 LLRRTAAAARELGCPVRLHCAQGVLEVETVRRLHGT----------------TPLEWLadvGLLGPRLLIphatyisGSP 285

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526271715 262 HCVEASDDDLEKIKDLGASINHC----VTSNRLLNntklDLDRLKD--IPFTIGTDGLSSnnslsmfDELRNALMAHYDK 335
Cdd:PRK06151 286 RLNYSGGDDLALLAEHGVSIVHCplvsARHGSALN----SFDRYREagINLALGTDTFPP-------DMVMNMRVGLILG 354

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*...
gi 526271715 336 NVVE------FSKTLLKAATFNGSRALGLNK-GVLKESFDADMISFKL 376
Cdd:PRK06151 355 RVVEgdldaaSAADLFDAATLGGARALGRDDlGRLAPGAKADIVVFDL 402
 
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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