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Conserved domains on  [gi|767958781|ref|XP_011517519|]
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guanine deaminase isoform X3 [Homo sapiens]

Protein Classification

guanine deaminase( domain architecture ID 10101379)

guanine deaminase catalyzes the deamination of guanine to yield xanthine

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
GDEase cd01303
Guanine deaminase (GDEase). Guanine deaminase is an aminohydrolase responsible for the ...
 13-482 0e+00

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


:

Pssm-ID: 238628 [Multi-domain]  Cd Length: 429  Bit Score: 624.69  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958781  13 FRGTFVHSTWTCPMEvLRDHLLGVSDSGKIVFLEEASQQEKLAKEW--CFKPCEIRELSHHEFFMPGLVDTHIHASQYSF 90
Cdd:cd01303    1 FRGTFIHTKSLPELE-LVEDALRVVEDGLIVVVDGNIIAAGAAETLkrAAKPGARVIDSPNQFILPGFIDTHIHAPQYAN 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958781  91 AGSSIDLPLLEWLTKYTFPAEHRFQNIDFAEEVYTRVVtlellmsvlvkktlffhkggnmeckqpsqghvannrqnRRTL 170
Cdd:cd01303   80 IGSGLGEPLLDWLETYTFPEEAKFADPAYAREVYGRFL--------------------------------------DELL 121

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958781 171 KNGTTTACYFATIHTDSSLLLADITDKFGQRAFVGKVCMDLNDtfPEYK-ETTEESIKETERFVSEMLQKnYSRVKPIVT 249
Cdd:cd01303  122 RNGTTTACYFATIHPESTEALFEEAAKRGQRAIAGKVCMDRNA--PEYYrDTAESSYRDTKRLIERWHGK-SGRVKPAIT 198

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958781 250 PRFSLSCSETLMGELGNIAKT-RDLHIQSHISENRDEVEAVKNLYPSYKNYTSVYDKNNLLTNKTVMAHGCYLSAEELNV 328
Cdd:cd01303  199 PRFAPSCSEELLAALGKLAKEhPDLHIQTHISENLDEIAWVKELFPGARDYLDVYDKYGLLTEKTVLAHCVHLSEEEFNL 278

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958781 329 FHERGASIAHCPNSNLSLSSGFLNVLEVLKHEVKIGLGTDVAGGYSYSMLDAIRRAVMVSNILLINKVNEKSLTLKEVFR 408
Cdd:cd01303  279 LKERGASVAHCPTSNLFLGSGLFDVRKLLDAGIKVGLGTDVGGGTSFSMLDTLRQAYKVSRLLGYELGGHAKLSPAEAFY 358

                        410       420       430       440       450       460       470
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 767958781 409 LATLGGSQALGLDGEIGNFEVGKEFDAILINPKASDSPIDLfygDFFGDISEAVIQKFLYLGDDRNIEEVYVGG 482
Cdd:cd01303  359 LATLGGAEALGLDDKIGNFEVGKEFDAVVIDPSATPLLADR---MFRVESLEEALFKFLYLGDDRNIREVYVAG 429
 
Name Accession Description Interval E-value
GDEase cd01303
Guanine deaminase (GDEase). Guanine deaminase is an aminohydrolase responsible for the ...
 13-482 0e+00

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


Pssm-ID: 238628 [Multi-domain]  Cd Length: 429  Bit Score: 624.69  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958781  13 FRGTFVHSTWTCPMEvLRDHLLGVSDSGKIVFLEEASQQEKLAKEW--CFKPCEIRELSHHEFFMPGLVDTHIHASQYSF 90
Cdd:cd01303    1 FRGTFIHTKSLPELE-LVEDALRVVEDGLIVVVDGNIIAAGAAETLkrAAKPGARVIDSPNQFILPGFIDTHIHAPQYAN 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958781  91 AGSSIDLPLLEWLTKYTFPAEHRFQNIDFAEEVYTRVVtlellmsvlvkktlffhkggnmeckqpsqghvannrqnRRTL 170
Cdd:cd01303   80 IGSGLGEPLLDWLETYTFPEEAKFADPAYAREVYGRFL--------------------------------------DELL 121

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958781 171 KNGTTTACYFATIHTDSSLLLADITDKFGQRAFVGKVCMDLNDtfPEYK-ETTEESIKETERFVSEMLQKnYSRVKPIVT 249
Cdd:cd01303  122 RNGTTTACYFATIHPESTEALFEEAAKRGQRAIAGKVCMDRNA--PEYYrDTAESSYRDTKRLIERWHGK-SGRVKPAIT 198

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958781 250 PRFSLSCSETLMGELGNIAKT-RDLHIQSHISENRDEVEAVKNLYPSYKNYTSVYDKNNLLTNKTVMAHGCYLSAEELNV 328
Cdd:cd01303  199 PRFAPSCSEELLAALGKLAKEhPDLHIQTHISENLDEIAWVKELFPGARDYLDVYDKYGLLTEKTVLAHCVHLSEEEFNL 278

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958781 329 FHERGASIAHCPNSNLSLSSGFLNVLEVLKHEVKIGLGTDVAGGYSYSMLDAIRRAVMVSNILLINKVNEKSLTLKEVFR 408
Cdd:cd01303  279 LKERGASVAHCPTSNLFLGSGLFDVRKLLDAGIKVGLGTDVGGGTSFSMLDTLRQAYKVSRLLGYELGGHAKLSPAEAFY 358

                        410       420       430       440       450       460       470
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 767958781 409 LATLGGSQALGLDGEIGNFEVGKEFDAILINPKASDSPIDLfygDFFGDISEAVIQKFLYLGDDRNIEEVYVGG 482
Cdd:cd01303  359 LATLGGAEALGLDDKIGNFEVGKEFDAVVIDPSATPLLADR---MFRVESLEEALFKFLYLGDDRNIREVYVAG 429
guan_deamin TIGR02967
guanine deaminase; This model describes guanine deaminase, which hydrolyzes guanine to ...
 26-482 0e+00

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


Pssm-ID: 132012 [Multi-domain]  Cd Length: 401  Bit Score: 558.41  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958781   26 MEVLRDHLLGVSDsGKIVFLEEASQQeklaKEWCFKPCEIRELSHHeFFMPGLVDTHIHASQYSFAGSsIDLPLLEWLTK 105
Cdd:TIGR02967   1 LEYFEDGLLVVEN-GRIVAVGDYAEL----KETLPAGVEIDDYRGH-LIMPGFIDTHIHYPQTEMIAS-YGEQLLEWLEK 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958781  106 YTFPAEHRFQNIDFAEEVYTRVVtlellmsvlvkktlffhkggnmeckqpsqghvannrqnRRTLKNGTTTACYFATIHT 185
Cdd:TIGR02967  74 YTFPTEARFADPDHAEEVAEFFL--------------------------------------DELLRNGTTTALVFATVHP 115

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958781  186 DSSLLLADITDKFGQRAFVGKVCMDLNdtFPEY-KETTEESIKETERFVSEMLQKNysRVKPIVTPRFSLSCSETLMGEL 264
Cdd:TIGR02967 116 ESVDALFEAALKRGMRMIAGKVLMDRN--APDYlRDTAESSYDESKALIERWHGKG--RLLYAVTPRFAPTSSPEQLAAA 191

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958781  265 GNIAKTR-DLHIQSHISENRDEVEAVKNLYPSYKNYTSVYDKNNLLTNKTVMAHGCYLSAEELNVFHERGASIAHCPNSN 343
Cdd:TIGR02967 192 GELAKEYpDVYVQTHLSENKDEIAWVKELFPEAKDYLDVYDHYGLLGRRSVFAHCIHLSDEECQRLAETGAAIAHCPTSN 271

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958781  344 LSLSSGFLNVLEVLKHEVKIGLGTDVAGGYSYSMLDAIRRAVMVSNILlinkvnEKSLTLKEVFRLATLGGSQALGLDGE 423
Cdd:TIGR02967 272 LFLGSGLFNLKKALEHGVRVGLGTDVGGGTSFSMLQTLREAYKVSQLQ------GARLSPFEAFYLATLGGARALDLDDR 345

                         410       420       430       440       450
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 767958781  424 IGNFEVGKEFDAILINPKASDSPIDLFYGdffGDISEAVIQKFLYLGDDRNIEEVYVGG 482
Cdd:TIGR02967 346 IGNFEPGKEADFVVLDPAATPLLALRFEG---ADTLEDKLFKLMYLGDDRNVAETYVAG 401
SsnA COG0402
Cytosine/adenosine deaminase or related metal-dependent hydrolase [Nucleotide transport and ...
 16-486 3.37e-113

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: 340.65  E-value: 3.37e-113
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958781  16 TFVHSTWTCPM----EVLRDHLLGVSDsGKIVFLEEASQQEKLakewcFKPCEIRELSHHeFFMPGLVDTHIHASQYSFA 91
Cdd:COG0402    2 LLIRGAWVLTMdpagGVLEDGAVLVED-GRIAAVGPGAELPAR-----YPAAEVIDAGGK-LVLPGLVNTHTHLPQTLLR 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958781  92 GSSIDLPLLEWLTKYTFPAEHRFQnidfAEEVY--TRVVTLELLmsvlvkktlffhkggnmeckqpsqghvannrqnrrt 169
Cdd:COG0402   75 GLADDLPLLDWLEEYIWPLEARLD----PEDVYagALLALAEML------------------------------------ 114

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958781 170 lKNGTTTACYFATIHTDSSLLLADITDKFGQRAFVGKVCMDLNdtFPE-YKETTEESIKETERFVSEMLQKNYSRVKPIV 248
Cdd:COG0402  115 -RSGTTTVADFYYVHPESADALAEAAAEAGIRAVLGRGLMDRG--FPDgLREDADEGLADSERLIERWHGAADGRIRVAL 191

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958781 249 TPRFSLSCSETLMGELGNIAKTRDLHIQSHISENRDEVEAVKNLYPsyKNYTSVYDKNNLLTNKTVMAHGCYLSAEELNV 328
Cdd:COG0402  192 APHAPYTVSPELLRAAAALARELGLPLHTHLAETRDEVEWVLELYG--KRPVEYLDELGLLGPRTLLAHCVHLTDEEIAL 269

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958781 329 FHERGASIAHCPNSNLSLSSGFLNVLEVLKHEVKIGLGTDVAGG-YSYSMLDAIRRAVMVSNILlinKVNEKSLTLKEVF 407
Cdd:COG0402  270 LAETGASVAHCPTSNLKLGSGIAPVPRLLAAGVRVGLGTDGAASnNSLDMFEEMRLAALLQRLR---GGDPTALSAREAL 346

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958781 408 RLATLGGSQALGLDGEIGNFEVGKEFDAILINPKASD-SPIDlfygdffgdiseAVIQKFLYLGDDRNIEEVYVGGKQVV 486
Cdd:COG0402  347 EMATLGGARALGLDDEIGSLEPGKRADLVVLDLDAPHlAPLH------------DPLSALVYAADGRDVRTVWVAGRVVV 414
PRK09228 PRK09228
guanine deaminase; Provisional
 11-485 1.08e-97

guanine deaminase; Provisional


Pssm-ID: 236419 [Multi-domain]  Cd Length: 433  Bit Score: 301.34  E-value: 1.08e-97
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958781  11 HIFRGTFVHST---WTCP----MEVLRDHLLGVSDsGKIVFLEEASQ-QEKLAKEwcfkpCEIRELSHHeFFMPGLVDTH 82
Cdd:PRK09228   4 KAYRGRLLHFTadpAEVDdedaLRYIEDGLLLVED-GRIVAAGPYAElRAQLPAD-----AEVTDYRGK-LILPGFIDTH 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958781  83 IHASQYSFAGSsidlP---LLEWLTKYTFPAEHRFQNIDFAEEVYTRVVTlELLmsvlvkktlffhkggnmeckqpsqgh 159
Cdd:PRK09228  77 IHYPQTDMIAS----YgeqLLDWLNTYTFPEERRFADPAYAREVAEFFLD-ELL-------------------------- 125

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958781 160 vannrqnrrtlKNGTTTACYFATIHTDSsllladiTDKF-------GQRAFVGKVCMDLNdtFPEY-KETTEESIKETER 231
Cdd:PRK09228 126 -----------RNGTTTALVFGTVHPQS-------VDALfeaaearNMRMIAGKVLMDRN--APDGlRDTAESGYDDSKA 185

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958781 232 fvseMLQK--NYSRVKPIVTPRFSLSCSETLMGELGNIAKTR-DLHIQSHISENRDEVEAVKNLYPSYKNYTSVYDKNNL 308
Cdd:PRK09228 186 ----LIERwhGKGRLLYAITPRFAPTSTPEQLEAAGALAREHpDVWIQTHLSENLDEIAWVKELFPEARDYLDVYERYGL 261

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958781 309 LTNKTVMAHGCYLSAEELNVFHERGASIAHCPNSNLSLSSGFLNVLEVLKHEVKIGLGTDVAGGYSYSMLDAIRRAVMVS 388
Cdd:PRK09228 262 LGPRAVFAHCIHLEDRERRRLAETGAAIAFCPTSNLFLGSGLFDLKRADAAGVRVGLGTDVGGGTSFSMLQTMNEAYKVQ 341

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958781 389 nillinKVNEKSLTLKEVFRLATLGGSQALGLDGEIGNFEVGKEFDAILINPKA----------SDSPIDLFYGdffgdi 458
Cdd:PRK09228 342 ------QLQGYRLSPFQAFYLATLGGARALGLDDRIGNLAPGKEADFVVLDPAAtpllalrtarAESLEELLFA------ 409

                        490       500
                 ....*....|....*....|....*..
gi 767958781 459 seaviqkFLYLGDDRNIEEVYVGGKQV 485
Cdd:PRK09228 410 -------LMTLGDDRAVAETYVAGRPV 429
Amidohydro_1 pfam01979
Amidohydrolase family; This family of enzymes are a a large metal dependent hydrolase ...
 75-485 6.18e-49

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: 171.15  E-value: 6.18e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958781   75 MPGLVDTHIHASQYSFAGSSIDLpllewltkytfpaehrfqniDFAEEVYTRVVTlellmsvlvkktlffhkggnmeckq 154
Cdd:pfam01979   3 LPGLIDAHVHLEMGLLRGIPVPP--------------------EFAYEALRLGIT------------------------- 37

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958781  155 psqghvannrqnrRTLKNGTTTACYFATIHTDSSLLLADITDK--FGQRAFVGKVCMDLNDTFPEYKETTEESIKETErf 232
Cdd:pfam01979  38 -------------TMLKSGTTTVLDMGATTSTGIEALLEAAEElpLGLRFLGPGCSLDTDGELEGRKALREKLKAGAE-- 102

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958781  233 vsEMLQKNYSRVKPIVTPRFSLSCSETLMGELGNIAKTRDLHIQSHISENRDEVEAVKNLYPS---YKNYTSVYDKNNLL 309
Cdd:pfam01979 103 --FIKGMADGVVFVGLAPHGAPTFSDDELKAALEEAKKYGLPVAIHALETKGEVEDAIAAFGGgieHGTHLEVAESGGLL 180

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958781  310 -TNKTVMAHGCYLSAEELNVFHER--GASIAHCPNSNLSLSSGFLNVLEVLKHEVKIGLGTDVAG-GYSYSMLDAIRRAV 385
Cdd:pfam01979 181 dIIKLILAHGVHLSPTEANLLAEHlkGAGVAHCPFSNSKLRSGRIALRKALEDGVKVGLGTDGAGsGNSLNMLEELRLAL 260

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958781  386 mvsnilLINKVNEKSLTLKEVFRLATLGGSQALGLDGEIGNFEVGKEFDAILINPKasdspidlfygdffgdiseaVIQK 465
Cdd:pfam01979 261 ------ELQFDPEGGLSPLEALRMATINPAKALGLDDKVGSIEVGKDADLVVVDLD--------------------PLAA 314

                         410       420
                  ....*....|....*....|
gi 767958781  466 FLYLGDDRNIEEVYVGGKQV 485
Cdd:pfam01979 315 FFGLKPDGNVKKVIVKGKIV 334
 
Name Accession Description Interval E-value
GDEase cd01303
Guanine deaminase (GDEase). Guanine deaminase is an aminohydrolase responsible for the ...
 13-482 0e+00

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


Pssm-ID: 238628 [Multi-domain]  Cd Length: 429  Bit Score: 624.69  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958781  13 FRGTFVHSTWTCPMEvLRDHLLGVSDSGKIVFLEEASQQEKLAKEW--CFKPCEIRELSHHEFFMPGLVDTHIHASQYSF 90
Cdd:cd01303    1 FRGTFIHTKSLPELE-LVEDALRVVEDGLIVVVDGNIIAAGAAETLkrAAKPGARVIDSPNQFILPGFIDTHIHAPQYAN 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958781  91 AGSSIDLPLLEWLTKYTFPAEHRFQNIDFAEEVYTRVVtlellmsvlvkktlffhkggnmeckqpsqghvannrqnRRTL 170
Cdd:cd01303   80 IGSGLGEPLLDWLETYTFPEEAKFADPAYAREVYGRFL--------------------------------------DELL 121

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958781 171 KNGTTTACYFATIHTDSSLLLADITDKFGQRAFVGKVCMDLNDtfPEYK-ETTEESIKETERFVSEMLQKnYSRVKPIVT 249
Cdd:cd01303  122 RNGTTTACYFATIHPESTEALFEEAAKRGQRAIAGKVCMDRNA--PEYYrDTAESSYRDTKRLIERWHGK-SGRVKPAIT 198

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958781 250 PRFSLSCSETLMGELGNIAKT-RDLHIQSHISENRDEVEAVKNLYPSYKNYTSVYDKNNLLTNKTVMAHGCYLSAEELNV 328
Cdd:cd01303  199 PRFAPSCSEELLAALGKLAKEhPDLHIQTHISENLDEIAWVKELFPGARDYLDVYDKYGLLTEKTVLAHCVHLSEEEFNL 278

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958781 329 FHERGASIAHCPNSNLSLSSGFLNVLEVLKHEVKIGLGTDVAGGYSYSMLDAIRRAVMVSNILLINKVNEKSLTLKEVFR 408
Cdd:cd01303  279 LKERGASVAHCPTSNLFLGSGLFDVRKLLDAGIKVGLGTDVGGGTSFSMLDTLRQAYKVSRLLGYELGGHAKLSPAEAFY 358

                        410       420       430       440       450       460       470
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 767958781 409 LATLGGSQALGLDGEIGNFEVGKEFDAILINPKASDSPIDLfygDFFGDISEAVIQKFLYLGDDRNIEEVYVGG 482
Cdd:cd01303  359 LATLGGAEALGLDDKIGNFEVGKEFDAVVIDPSATPLLADR---MFRVESLEEALFKFLYLGDDRNIREVYVAG 429
guan_deamin TIGR02967
guanine deaminase; This model describes guanine deaminase, which hydrolyzes guanine to ...
 26-482 0e+00

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


Pssm-ID: 132012 [Multi-domain]  Cd Length: 401  Bit Score: 558.41  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958781   26 MEVLRDHLLGVSDsGKIVFLEEASQQeklaKEWCFKPCEIRELSHHeFFMPGLVDTHIHASQYSFAGSsIDLPLLEWLTK 105
Cdd:TIGR02967   1 LEYFEDGLLVVEN-GRIVAVGDYAEL----KETLPAGVEIDDYRGH-LIMPGFIDTHIHYPQTEMIAS-YGEQLLEWLEK 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958781  106 YTFPAEHRFQNIDFAEEVYTRVVtlellmsvlvkktlffhkggnmeckqpsqghvannrqnRRTLKNGTTTACYFATIHT 185
Cdd:TIGR02967  74 YTFPTEARFADPDHAEEVAEFFL--------------------------------------DELLRNGTTTALVFATVHP 115

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958781  186 DSSLLLADITDKFGQRAFVGKVCMDLNdtFPEY-KETTEESIKETERFVSEMLQKNysRVKPIVTPRFSLSCSETLMGEL 264
Cdd:TIGR02967 116 ESVDALFEAALKRGMRMIAGKVLMDRN--APDYlRDTAESSYDESKALIERWHGKG--RLLYAVTPRFAPTSSPEQLAAA 191

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958781  265 GNIAKTR-DLHIQSHISENRDEVEAVKNLYPSYKNYTSVYDKNNLLTNKTVMAHGCYLSAEELNVFHERGASIAHCPNSN 343
Cdd:TIGR02967 192 GELAKEYpDVYVQTHLSENKDEIAWVKELFPEAKDYLDVYDHYGLLGRRSVFAHCIHLSDEECQRLAETGAAIAHCPTSN 271

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958781  344 LSLSSGFLNVLEVLKHEVKIGLGTDVAGGYSYSMLDAIRRAVMVSNILlinkvnEKSLTLKEVFRLATLGGSQALGLDGE 423
Cdd:TIGR02967 272 LFLGSGLFNLKKALEHGVRVGLGTDVGGGTSFSMLQTLREAYKVSQLQ------GARLSPFEAFYLATLGGARALDLDDR 345

                         410       420       430       440       450
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 767958781  424 IGNFEVGKEFDAILINPKASDSPIDLFYGdffGDISEAVIQKFLYLGDDRNIEEVYVGG 482
Cdd:TIGR02967 346 IGNFEPGKEADFVVLDPAATPLLALRFEG---ADTLEDKLFKLMYLGDDRNVAETYVAG 401
SsnA COG0402
Cytosine/adenosine deaminase or related metal-dependent hydrolase [Nucleotide transport and ...
 16-486 3.37e-113

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: 340.65  E-value: 3.37e-113
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958781  16 TFVHSTWTCPM----EVLRDHLLGVSDsGKIVFLEEASQQEKLakewcFKPCEIRELSHHeFFMPGLVDTHIHASQYSFA 91
Cdd:COG0402    2 LLIRGAWVLTMdpagGVLEDGAVLVED-GRIAAVGPGAELPAR-----YPAAEVIDAGGK-LVLPGLVNTHTHLPQTLLR 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958781  92 GSSIDLPLLEWLTKYTFPAEHRFQnidfAEEVY--TRVVTLELLmsvlvkktlffhkggnmeckqpsqghvannrqnrrt 169
Cdd:COG0402   75 GLADDLPLLDWLEEYIWPLEARLD----PEDVYagALLALAEML------------------------------------ 114

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958781 170 lKNGTTTACYFATIHTDSSLLLADITDKFGQRAFVGKVCMDLNdtFPE-YKETTEESIKETERFVSEMLQKNYSRVKPIV 248
Cdd:COG0402  115 -RSGTTTVADFYYVHPESADALAEAAAEAGIRAVLGRGLMDRG--FPDgLREDADEGLADSERLIERWHGAADGRIRVAL 191

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958781 249 TPRFSLSCSETLMGELGNIAKTRDLHIQSHISENRDEVEAVKNLYPsyKNYTSVYDKNNLLTNKTVMAHGCYLSAEELNV 328
Cdd:COG0402  192 APHAPYTVSPELLRAAAALARELGLPLHTHLAETRDEVEWVLELYG--KRPVEYLDELGLLGPRTLLAHCVHLTDEEIAL 269

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958781 329 FHERGASIAHCPNSNLSLSSGFLNVLEVLKHEVKIGLGTDVAGG-YSYSMLDAIRRAVMVSNILlinKVNEKSLTLKEVF 407
Cdd:COG0402  270 LAETGASVAHCPTSNLKLGSGIAPVPRLLAAGVRVGLGTDGAASnNSLDMFEEMRLAALLQRLR---GGDPTALSAREAL 346

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958781 408 RLATLGGSQALGLDGEIGNFEVGKEFDAILINPKASD-SPIDlfygdffgdiseAVIQKFLYLGDDRNIEEVYVGGKQVV 486
Cdd:COG0402  347 EMATLGGARALGLDDEIGSLEPGKRADLVVLDLDAPHlAPLH------------DPLSALVYAADGRDVRTVWVAGRVVV 414
PRK09228 PRK09228
guanine deaminase; Provisional
 11-485 1.08e-97

guanine deaminase; Provisional


Pssm-ID: 236419 [Multi-domain]  Cd Length: 433  Bit Score: 301.34  E-value: 1.08e-97
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958781  11 HIFRGTFVHST---WTCP----MEVLRDHLLGVSDsGKIVFLEEASQ-QEKLAKEwcfkpCEIRELSHHeFFMPGLVDTH 82
Cdd:PRK09228   4 KAYRGRLLHFTadpAEVDdedaLRYIEDGLLLVED-GRIVAAGPYAElRAQLPAD-----AEVTDYRGK-LILPGFIDTH 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958781  83 IHASQYSFAGSsidlP---LLEWLTKYTFPAEHRFQNIDFAEEVYTRVVTlELLmsvlvkktlffhkggnmeckqpsqgh 159
Cdd:PRK09228  77 IHYPQTDMIAS----YgeqLLDWLNTYTFPEERRFADPAYAREVAEFFLD-ELL-------------------------- 125

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958781 160 vannrqnrrtlKNGTTTACYFATIHTDSsllladiTDKF-------GQRAFVGKVCMDLNdtFPEY-KETTEESIKETER 231
Cdd:PRK09228 126 -----------RNGTTTALVFGTVHPQS-------VDALfeaaearNMRMIAGKVLMDRN--APDGlRDTAESGYDDSKA 185

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958781 232 fvseMLQK--NYSRVKPIVTPRFSLSCSETLMGELGNIAKTR-DLHIQSHISENRDEVEAVKNLYPSYKNYTSVYDKNNL 308
Cdd:PRK09228 186 ----LIERwhGKGRLLYAITPRFAPTSTPEQLEAAGALAREHpDVWIQTHLSENLDEIAWVKELFPEARDYLDVYERYGL 261

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958781 309 LTNKTVMAHGCYLSAEELNVFHERGASIAHCPNSNLSLSSGFLNVLEVLKHEVKIGLGTDVAGGYSYSMLDAIRRAVMVS 388
Cdd:PRK09228 262 LGPRAVFAHCIHLEDRERRRLAETGAAIAFCPTSNLFLGSGLFDLKRADAAGVRVGLGTDVGGGTSFSMLQTMNEAYKVQ 341

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958781 389 nillinKVNEKSLTLKEVFRLATLGGSQALGLDGEIGNFEVGKEFDAILINPKA----------SDSPIDLFYGdffgdi 458
Cdd:PRK09228 342 ------QLQGYRLSPFQAFYLATLGGARALGLDDRIGNLAPGKEADFVVLDPAAtpllalrtarAESLEELLFA------ 409

                        490       500
                 ....*....|....*....|....*..
gi 767958781 459 seaviqkFLYLGDDRNIEEVYVGGKQV 485
Cdd:PRK09228 410 -------LMTLGDDRAVAETYVAGRPV 429
ATZ_TRZ_like cd01298
TRZ/ATZ family contains enzymes from the atrazine degradation pathway and related hydrolases. ...
 23-486 1.22e-67

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: 222.85  E-value: 1.22e-67
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958781  23 TCPMEVLRDHLLGVSDsGKIVFLEEASQQEKLAKEwcfkpcEIRELSHHeFFMPGLVDTHIHASQYSFAGSSIDLPLLEW 102
Cdd:cd01298   11 TDPRRVLEDGDVLVED-GRIVAVGPALPLPAYPAD------EVIDAKGK-VVMPGLVNTHTHLAMTLLRGLADDLPLMEW 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958781 103 LTKYTFPAEHRFQnidfAEEVY--TRVVTLELLmsvlvkktlffhkggnmeckqpsqghvannrqnrrtlKNGTTTAC-- 178
Cdd:cd01298   83 LKDLIWPLERLLT----EEDVYlgALLALAEMI-------------------------------------RSGTTTFAdm 121

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958781 179 YFatIHTDSsllLADITDKFGQRAFVGKVCMDLNDtfpEYKETTEESIKETERFVSEMLQKNYSRVKPIVTPRFSLSCSE 258
Cdd:cd01298  122 YF--FYPDA---VAEAAEELGIRAVLGRGIMDLGT---EDVEETEEALAEAERLIREWHGAADGRIRVALAPHAPYTCSD 193

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958781 259 TLMGELGNIAKTRDLHIQSHISENRDEVEAVKNLYpsykNYTSV-Y-DKNNLLTNKTVMAHGCYLSAEELNVFHERGASI 336
Cdd:cd01298  194 ELLREVAELAREYGVPLHIHLAETEDEVEESLEKY----GKRPVeYlEELGLLGPDVVLAHCVWLTDEEIELLAETGTGV 269

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958781 337 AHCPNSNLSLSSGFLNVLEVLKHEVKIGLGTD-VAGGYSYSMLDAIRRAvmvsniLLINKV---NEKSLTLKEVFRLATL 412
Cdd:cd01298  270 AHNPASNMKLASGIAPVPEMLEAGVNVGLGTDgAASNNNLDMFEEMRLA------ALLQKLahgDPTALPAEEALEMATI 343

                        410       420       430       440       450       460       470
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 767958781 413 GGSQALGLDgEIGNFEVGKEFDAILINPkasDSPidlfygDFFG---DISEAViqkflYLGDDRNIEEVYVGGKQVV 486
Cdd:cd01298  344 GGAKALGLD-EIGSLEVGKKADLILIDL---DGP------HLLPvhdPISHLV-----YSANGGDVDTVIVNGRVVM 405
PRK07228 PRK07228
5'-deoxyadenosine deaminase;
75-439 1.24e-57

5'-deoxyadenosine deaminase;


Pssm-ID: 180895 [Multi-domain]  Cd Length: 445  Bit Score: 197.14  E-value: 1.24e-57
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958781  75 MPGLVDTHIHASQYSFAGSSIDLPLLEWLTKYTFPAE--HRfqnidfAEEVYTrvvtlellmSVLVkktlffhkgGNMEC 152
Cdd:PRK07228  55 IPGLIQGHIHLCQTLFRGIADDLELLDWLKDRIWPLEaaHD------AESMYY---------SALL---------GIGEL 110

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958781 153 kqpsqghvannrqnrrtLKNGTTTACYFATI-HTDSSL-LLADItdkfGQRAFVGKVCMDLNDTFPE-YKETTEESIKET 229
Cdd:PRK07228 111 -----------------IESGTTTIVDMESVhHTDSAFeAAGES----GIRAVLGKVMMDYGDDVPEgLQEDTEASLAES 169

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958781 230 ERFVSEMLQKNYSRVKPIVTPRFSLSCSETLMGELGNIAKTRDLHIQSHISENRDEVEAVKNlYPSYKNYTsVYDKNNLL 309
Cdd:PRK07228 170 VRLLEKWHGADNGRIRYAFTPRFAVSCTEELLRGVRDLADEYGVRIHTHASENRGEIETVEE-ETGMRNIH-YLDEVGLT 247

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958781 310 TNKTVMAHGCYLSAEELNVFHERGASIAHCPNSNLSLSSGFLNVLEVLKHEVKIGLGTDvaGGYSYSMLDA---IRRAVm 386
Cdd:PRK07228 248 GEDLILAHCVWLDEEEREILAETGTHVTHCPSSNLKLASGIAPVPDLLERGINVALGAD--GAPCNNTLDPfteMRQAA- 324

                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 767958781 387 vsnilLINKVNE---KSLTLKEVFRLATLGGSQALGLDGEIGNFEVGKEFDAILIN 439
Cdd:PRK07228 325 -----LIQKVDRlgpTAMPARTVFEMATLGGAKAAGFEDEIGSLEEGKKADLAILD 375
Amidohydro_1 pfam01979
Amidohydrolase family; This family of enzymes are a a large metal dependent hydrolase ...
 75-485 6.18e-49

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: 171.15  E-value: 6.18e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958781   75 MPGLVDTHIHASQYSFAGSSIDLpllewltkytfpaehrfqniDFAEEVYTRVVTlellmsvlvkktlffhkggnmeckq 154
Cdd:pfam01979   3 LPGLIDAHVHLEMGLLRGIPVPP--------------------EFAYEALRLGIT------------------------- 37

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958781  155 psqghvannrqnrRTLKNGTTTACYFATIHTDSSLLLADITDK--FGQRAFVGKVCMDLNDTFPEYKETTEESIKETErf 232
Cdd:pfam01979  38 -------------TMLKSGTTTVLDMGATTSTGIEALLEAAEElpLGLRFLGPGCSLDTDGELEGRKALREKLKAGAE-- 102

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958781  233 vsEMLQKNYSRVKPIVTPRFSLSCSETLMGELGNIAKTRDLHIQSHISENRDEVEAVKNLYPS---YKNYTSVYDKNNLL 309
Cdd:pfam01979 103 --FIKGMADGVVFVGLAPHGAPTFSDDELKAALEEAKKYGLPVAIHALETKGEVEDAIAAFGGgieHGTHLEVAESGGLL 180

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958781  310 -TNKTVMAHGCYLSAEELNVFHER--GASIAHCPNSNLSLSSGFLNVLEVLKHEVKIGLGTDVAG-GYSYSMLDAIRRAV 385
Cdd:pfam01979 181 dIIKLILAHGVHLSPTEANLLAEHlkGAGVAHCPFSNSKLRSGRIALRKALEDGVKVGLGTDGAGsGNSLNMLEELRLAL 260

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958781  386 mvsnilLINKVNEKSLTLKEVFRLATLGGSQALGLDGEIGNFEVGKEFDAILINPKasdspidlfygdffgdiseaVIQK 465
Cdd:pfam01979 261 ------ELQFDPEGGLSPLEALRMATINPAKALGLDDKVGSIEVGKDADLVVVDLD--------------------PLAA 314

                         410       420
                  ....*....|....*....|
gi 767958781  466 FLYLGDDRNIEEVYVGGKQV 485
Cdd:pfam01979 315 FFGLKPDGNVKKVIVKGKIV 334
PRK09045 PRK09045
TRZ/ATZ family hydrolase;
16-486 9.33e-46

TRZ/ATZ family hydrolase;


Pssm-ID: 236366 [Multi-domain]  Cd Length: 443  Bit Score: 165.47  E-value: 9.33e-46
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958781  16 TFVHSTWTCPME----VLRDHLLGVSDsGKIVFLeeASQQEKLAKewcFKPCEIRELSHHeFFMPGLVDTHIHASQYSFA 91
Cdd:PRK09045   9 LLIEARWIVPVEpagvVLEDHAVAIRD-GRIVAI--LPRAEARAR---YAAAETVELPDH-VLIPGLINAHTHAAMSLLR 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958781  92 GSSIDLPLLEWLTKYTFPAEHRFQNIDFaeeVY--TRVVTLELLmsvlvkktlffhkggnmeckqpsqghvannrqnrrt 169
Cdd:PRK09045  82 GLADDLPLMTWLQDHIWPAEGAWVSEEF---VRdgTLLAIAEML------------------------------------ 122

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958781 170 lKNGTTTA--CYFatiHTDSsllLADITDKFGQRAFVGKVCMDlndtFP-EYKETTEESI----KETERFvsemlqKNYS 242
Cdd:PRK09045 123 -RGGTTCFndMYF---FPEA---AAEAAHQAGMRAQIGMPVLD----FPtAWASDADEYLakglELHDQW------RHHP 185

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958781 243 RVKPIVTPRFSLSCSETLMGELGNIAKTRDLHIQSHISENRDEVEAvknlypSYKNY----TSVYDKNNLLTNKTVMAHG 318
Cdd:PRK09045 186 LISTAFAPHAPYTVSDENLERIRTLAEQLDLPIHIHLHETAQEIAD------SLKQHgqrpLARLARLGLLGPRLIAVHM 259

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958781 319 CYLSAEELNVFHERGASIAHCPNSNLSLSSGFLNVLEVLKHEVKIGLGTD-VAGGYSYSMLDAIRRAVMVSnillinKV- 396
Cdd:PRK09045 260 TQLTDAEIALLAETGCSVVHCPESNLKLASGFCPVAKLLQAGVNVALGTDgAASNNDLDLFGEMRTAALLA------KAv 333

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958781 397 --NEKSLTLKEVFRLATLGGSQALGLDGEIGNFEVGKEFDAILINPKASDS-PIdlfygdfFGDISEAViqkflYLGDDR 473
Cdd:PRK09045 334 agDATALPAHTALRMATLNGARALGLDDEIGSLEPGKQADLVAVDLSGLETqPV-------YDPVSQLV-----YAAGRE 401

                        490
                 ....*....|...
gi 767958781 474 NIEEVYVGGKQVV 486
Cdd:PRK09045 402 QVSHVWVAGKQLL 414
PRK08393 PRK08393
N-ethylammeline chlorohydrolase; Provisional
 71-486 2.17e-42

N-ethylammeline chlorohydrolase; Provisional


Pssm-ID: 181411 [Multi-domain]  Cd Length: 424  Bit Score: 155.73  E-value: 2.17e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958781  71 HEFFMPGLVDTHIHASQYSFAGSSIDLPLLEWLTKYTFPAEHRFQNidfaEEVY--TRVVTLELLmsvlvkktlffhkgg 148
Cdd:PRK08393  49 GSVVSPGFINAHTHSPMVLLRGLADDVPLMEWLQNYIWPRERKLKR----KDIYwgAYLGLLEMI--------------- 109

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958781 149 nmeckqpsqghvannrqnrrtlKNGTTT--ACYFatiHTDSsllLADITDKFGQRAFVGKVCMDLNDtfpeyKETTEESI 226
Cdd:PRK08393 110 ----------------------KSGTTTfvDMYF---HMEE---VAKATLEVGLRGYLSYGMVDLGD-----EEKREKEI 156

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958781 227 KETERFVSEMLQKNYSRVKPIVTPRFSLSCSETLMGELGNIAKTRDLHIQSHISENRDEVEAVKNLYPsyKNYTSVYDKN 306
Cdd:PRK08393 157 KETEKLMEFIEKLNSPRVHFVFGPHAPYTCSLALLKWVREKAREWNKLITIHLSETMDEIKQIREKYG--KSPVVLLDEI 234

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958781 307 NLLTNKTVMAHGCYLSAEELNVFHERGASIAHCPNSNLSLSSGFLNVLEVLKHEVKIGLGTDvaGGYSYSMLDAIRRAVM 386
Cdd:PRK08393 235 GFLNEDVIAAHGVWLSSRDIRILASAGVTVAHNPASNMKLGSGVMPLRKLLNAGVNVALGTD--GAASNNNLDMLREMKL 312

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958781 387 VSnilLINKVNEKSLTL---KEVFRLATLGGSQALGLDGeiGNFEVGKEFDAILIN-PKASDSPIDlfygdffgdiseAV 462
Cdd:PRK08393 313 AA---LLHKVHNLDPTIadaETVFRMATQNGAKALGLKA--GVIKEGYLADIAVIDfNRPHLRPIN------------NP 375

                        410       420
                 ....*....|....*....|....
gi 767958781 463 IQKFLYLGDDRNIEEVYVGGKQVV 486
Cdd:PRK08393 376 ISHLVYSANGNDVETTIVDGKIVM 399
PRK06038 PRK06038
N-ethylammeline chlorohydrolase; Provisional
 70-441 2.94e-40

N-ethylammeline chlorohydrolase; Provisional


Pssm-ID: 180363 [Multi-domain]  Cd Length: 430  Bit Score: 150.29  E-value: 2.94e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958781  70 HHEFFMPGLVDTHIHASQYSFAGSSIDLPLLEWLTKYTFPAEHRFQnidfAEEVY--TRVVTLELLmsvlvkktlffhkg 147
Cdd:PRK06038  49 KGSVVMPGLVNTHTHAAMTLFRGYADDLPLAEWLNDHIWPAEAKLT----AEDVYagSLLACLEMI-------------- 110

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958781 148 gnmeckqpsqghvannrqnrrtlKNGTTTacyFAT--IHTDSSlllADITDKFGQRAFVGKVCMDLNDTfpeykETTEES 225
Cdd:PRK06038 111 -----------------------KSGTTS---FADmyFYMDEV---AKAVEESGLRAALSYGMIDLGDD-----EKGEAE 156

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958781 226 IKETERFVSEMLQKNYSRVKPIVTPRFSLSCSETLMGELGNIAKTRDLHIQSHISENRDEVEAVKNLYpsykNYTSVY-- 303
Cdd:PRK06038 157 LKEGKRFVKEWHGAADGRIKVMYGPHAPYTCSEEFLSKVKKLANKDGVGIHIHVLETEAELNQMKEQY----GMCSVNyl 232

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958781 304 DKNNLLTNKTVMAHGCYLSAEELNVFHERGASIAHCPNSNLSLSSGFLNVLEVLKHEVKIGLGTD-VAGGYSYSMLDAIR 382
Cdd:PRK06038 233 DDIGFLGPDVLAAHCVWLSDGDIEILRERGVNVSHNPVSNMKLASGIAPVPKLLERGVNVSLGTDgCASNNNLDMFEEMK 312

                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 767958781 383 RAVMVSNillINKVNEKSLTLKEVFRLATLGGSQALGLdgEIGNFEVGKEFDAILINPK 441
Cdd:PRK06038 313 TAALLHK---VNTMDPTALPARQVLEMATVNGAKALGI--NTGMLKEGYLADIIIVDMN 366
PRK06687 PRK06687
TRZ/ATZ family protein;
23-486 1.79e-38

TRZ/ATZ family protein;


Pssm-ID: 180657 [Multi-domain]  Cd Length: 419  Bit Score: 145.15  E-value: 1.79e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958781  23 TC--PMEVLRDHLLGVSDSgKIV--------FLEEASQQEKLAKEWcfkpceirelshhefFMPGLVDTHIHASQYSFAG 92
Cdd:PRK06687  11 TCdqDFHVYLDGILAVKDS-QIVyvgqdkpaFLEQAEQIIDYQGAW---------------IMPGLVNCHTHSAMTGLRG 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958781  93 SSIDLPLLEWLTKYTFPAEHrfqniDFAEEVYTRVVTLELLMSVLVKKTLFfhkggnMECKQPSQGHVANNRQNRRTLKn 172
Cdd:PRK06687  75 IRDDSNLHEWLNDYIWPAES-----EFTPDMTTNAVKEALTEMLQSGTTTF------NDMYNPNGVDIQQIYQVVKTSK- 142

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958781 173 gttTACYFATIhtdssllladitdkfgqrafvgkvcmdlndTFPEYKETTEESIKETERFVSEMLQKNYSRVKPIVTPRF 252
Cdd:PRK06687 143 ---MRCYFSPT------------------------------LFSSETETTAETISRTRSIIDEILKYKNPNFKVMVAPHS 189

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958781 253 SLSCSETLMGELGNIAKTRDLHIQSHISENRDEVEAVKNLYPsyKNYTSVYDKNNLLTNKTVMAHGCYLSAEELNVFHER 332
Cdd:PRK06687 190 PYSCSRDLLEASLEMAKELNIPLHVHVAETKEESGIILKRYG--KRPLAFLEELGYLDHPSVFAHGVELNEREIERLASS 267

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958781 333 GASIAHCPNSNLSLSSGFLNVLEVLKHEVKIGLGTD-VAGGYSYSMLDAIRRAVMVSNillINKVNEKSLTLKEVFRLAT 411
Cdd:PRK06687 268 QVAIAHNPISNLKLASGIAPIIQLQKAGVAVGIATDsVASNNNLDMFEEGRTAALLQK---MKSGDASQFPIETALKVLT 344

                        410       420       430       440       450       460       470
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 767958781 412 LGGSQALGLDGEIGNFEVGKEFDAILINPKASdspIDLFygdffgdISEAVIQKFLYLGDDRNIEEVYVGGKQVV 486
Cdd:PRK06687 345 IEGAKALGMENQIGSLEVGKQADFLVIQPQGK---IHLQ-------PQENMLSHLVYAVKSSDVDDVYIAGEQVV 409
PRK15493 PRK15493
bifunctional S-methyl-5'-thioadenosine deaminase/S-adenosylhomocysteine deaminase;
72-486 1.81e-29

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


Pssm-ID: 185390 [Multi-domain]  Cd Length: 435  Bit Score: 120.16  E-value: 1.81e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958781  72 EFFMPGLVDTHIHASQYSFAGSSIDLPLLEWLTKYTFPAEHRFqnidfAEEVYTRVVTLELLMSVlvkktlffhkggnme 151
Cdd:PRK15493  55 KWVLPGLVNTHTHVVMSLLRGIGDDMLLQPWLETRIWPLESQF-----TPELAVASTELGLLEMV--------------- 114

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958781 152 ckqpsqghvannrqnrrtlKNGTTT-ACYFATIHTDSSLLLADITDKfGQRAFVGKVCMDLNDtfpeyKETTEESIKETE 230
Cdd:PRK15493 115 -------------------KSGTTSfSDMFNPIGVDQDAIMETVSRS-GMRAAVSRTLFSFGT-----KEDEKKAIEEAE 169

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958781 231 RFVSEMLQKNySRVKPIVTPRFSLSCSETLMGELGNIAKTRDLHIQSHISENRDEVEAVKNLYPsyKNYTSVYDKNNLLT 310
Cdd:PRK15493 170 KYVKRYYNES-GMLTTMVAPHSPYTCSTELLEECARIAVENQTMVHIHLSETEREVRDIEAQYG--KRPVEYAASCGLFK 246

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958781 311 NKTVMAHGCYLSAEELNVFHERGASIAHCPNSNLSLSSGFLNVLEVLKHEVKIGLGTD-VAGGYSYSMLDAIRRAVMVSN 389
Cdd:PRK15493 247 RPTVIAHGVVLNDNERAFLAEHDVRVAHNPNSNLKLGSGIANVKAMLEAGIKVGIATDsVASNNNLDMFEEMRIATLLQK 326

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958781 390 ILlinKVNEKSLTLKEVFRLATLGGSQALGLDgEIGNFEVGKEFDAILINP--KASDSPidlfygdffgdiSEAVIQKFL 467
Cdd:PRK15493 327 GI---HQDATALPVETALTLATKGAAEVIGMK-QTGSLEVGKCADFITIDPsnKPHLQP------------ADEVLSHLV 390

                        410
                 ....*....|....*....
gi 767958781 468 YLGDDRNIEEVYVGGKQVV 486
Cdd:PRK15493 391 YAASGKDISDVIINGKRVV 409
PRK06380 PRK06380
metal-dependent hydrolase; Provisional
 75-483 2.94e-21

metal-dependent hydrolase; Provisional


Pssm-ID: 180548 [Multi-domain]  Cd Length: 418  Bit Score: 95.72  E-value: 2.94e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958781  75 MPGLVDTHIHASQYSFAGSSIDLPLLEWLTKyTFPAEHRFQNidfaEEVYtrvvtlellmsvlvkktlffhKGGNMECKQ 154
Cdd:PRK06380  53 MPGLINTHAHVGMTASKGLFDDVDLEEFLMK-TFKYDSKRTR----EGIY---------------------NSAKLGMYE 106

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958781 155 psqghvannrqnrrTLKNGTTTacyFATIHTDSSLLlADITDKFGQRAFVGKVCMDlndtfPEYKETTEESIKETERFVS 234
Cdd:PRK06380 107 --------------MINSGITA---FVDLYYSEDII-AKAAEELGIRAFLSWAVLD-----EEITTQKGDPLNNAENFIR 163

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958781 235 EMLQKNYsrVKPIVTPRFSLSCSETLMGELGNIAKTRDLHIQSHISENRDEVeavknlYPSYKNY----TSVYDKNNLLT 310
Cdd:PRK06380 164 EHRNEEL--VTPSIGVQGIYVANDETYLKAKEIAEKYDTIMHMHLSETRKEV------YDHVKRTgerpVEHLEKIGFLN 235

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958781 311 NKTVMAHGCYLSAEELNVFHERGASIAHCPNSNLSLSS-GFLNVLEVLKHEVKIGLGTDVAGgySYSMLDAIrRAVMVSN 389
Cdd:PRK06380 236 SKLIAAHCVWATYHEIKLLSKNGVKVSWNSVSNFKLGTgGSPPIPEMLDNGINVTIGTDSNG--SNNSLDMF-EAMKFSA 312

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958781 390 ILLINKVNEKSLT-LKEVFRLATLGGSQALGLDGeiGNFEVGKEFDAILINPKASdSPIDLFYGDFFGDIseaviqkfLY 468
Cdd:PRK06380 313 LSVKNERWDASIIkAQEILDFATINAAKALELNA--GSIEVGKLADLVILDARAP-NMIPTRKNNIVSNI--------VY 381

                        410
                 ....*....|....*
gi 767958781 469 LGDDRNIEEVYVGGK 483
Cdd:PRK06380 382 SLNPLNVDHVIVNGK 396
PRK08203 PRK08203
hydroxydechloroatrazine ethylaminohydrolase; Reviewed
 220-434 4.49e-21

hydroxydechloroatrazine ethylaminohydrolase; Reviewed


Pssm-ID: 236184 [Multi-domain]  Cd Length: 451  Bit Score: 95.69  E-value: 4.49e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958781 220 ETTEESIKETERFVSEMLQKN-YSRVKPIVTPRFSLSCSETLMGELGNIAKTRDLHIQSHISENRDEVEAVKNLYpsykN 298
Cdd:PRK08203 174 EDEDAILADSQRLIDRYHDPGpGAMLRIALAPCSPFSVSRELMRESAALARRLGVRLHTHLAETLDEEAFCLERF----G 249

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958781 299 YTSV-Y-DKNNLLTNKTVMAHGCYLSAEELNVFHERGASIAHCPNSNLSLSSGFLNVLEVLKHEVKIGLGTD-VAGGYSY 375
Cdd:PRK08203 250 MRPVdYlEDLGWLGPDVWLAHCVHLDDAEIARLARTGTGVAHCPCSNMRLASGIAPVRELRAAGVPVGLGVDgSASNDGS 329

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 767958781 376 SMLDAIRRAvmvsniLLINKV--NEKSLTLKEVFRLATLGGSQALGLDgEIGNFEVGKEFD 434
Cdd:PRK08203 330 NLIGEARQA------LLLQRLryGPDAMTAREALEWATLGGARVLGRD-DIGSLAPGKLAD 383
PRK12393 PRK12393
amidohydrolase; Provisional
 76-486 4.05e-20

amidohydrolase; Provisional


Pssm-ID: 237088 [Multi-domain]  Cd Length: 457  Bit Score: 92.82  E-value: 4.05e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958781  76 PGLVDTHIHASQYSFAG--SSIDLPLLEWL--TKYTFPA---EHRFQnidfaeeVYTRVVTLELLMSvlvkktlffhkgg 148
Cdd:PRK12393  59 PGWVNTHHHLFQSLLKGvpAGINQSLTAWLaaVPYRFRArfdEDLFR-------LAARIGLVELLRS------------- 118

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958781 149 nmeckqpsqghvannrqnrrtlknGTTTAC-----YFATIHTDSSLLLADITDKFGQRaFV---GKVCMDLNDTfPEYK- 219
Cdd:PRK12393 119 ------------------------GCTTVAdhhylYHPGMPFDTGDILFDEAEALGMR-FVlcrGGATQTRGDH-PGLPt 172

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958781 220 ----ETTEESIKETERFVSEMLQKNYSRVKPIV----TPRFSLScsETLMGELGNIAKTRDLHIQSHISENRDEVEAVKN 291
Cdd:PRK12393 173 alrpETLDQMLADVERLVSRYHDASPDSLRRVVvaptTPTFSLP--PELLREVARAARGMGLRLHSHLSETVDYVDFCRE 250

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958781 292 LYpsykNYTSVY--DKNNLLTNKTVMAHGCYLSAEELNVFHERGASIAHCPNSNLSLSSGFLNVLEVLKHEVKIGLGTD- 368
Cdd:PRK12393 251 KY----GMTPVQfvAEHDWLGPDVWFAHLVKLDAEEIALLAQTGTGIAHCPQSNGRLGSGIAPALAMEAAGVPVSLGVDg 326

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958781 369 VAGGYSYSMLDAIRRAVMVSNILlinkVNEKSLTLKEVFRLATLGGSQALGLDgEIGNFEVGKEFDAILINpkaSDSPid 448
Cdd:PRK12393 327 AASNESADMLSEAHAAWLLHRAE----GGADATTVEDVVHWGTAGGARVLGLD-AIGTLAVGQAADLAIYD---LDDP-- 396

                        410       420       430
                 ....*....|....*....|....*....|....*...
gi 767958781 449 LFYGdfFGDISEAVIQKflylGDDRNIEEVYVGGKQVV 486
Cdd:PRK12393 397 RFFG--LHDPAIAPVAC----GGPAPVKALLVNGRPVV 428
PRK08418 PRK08418
metal-dependent hydrolase;
266-486 2.58e-19

metal-dependent hydrolase;


Pssm-ID: 181419 [Multi-domain]  Cd Length: 408  Bit Score: 90.03  E-value: 2.58e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958781 266 NIAKTRDLHIQSHISENRDEVEAVKNLYPSYKNY--------TSVYDKNNLL----TNKTVMAHGCYLSAEELNVFHERG 333
Cdd:PRK08418 197 QLAKKENLLVSTHFLESKAEREWLEESKGWFKKFfekflkepKPLYTPKEFLelfkGLRTLFTHCVYASEEELEKIKSKN 276

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958781 334 ASIAHCPNSNLSLSSGFLNVLEVLKHEVKIGLGTD-VAGGYSYSMLDAIRRAVMVSNillinkvNEKSLTL-KEVFRLAT 411
Cdd:PRK08418 277 ASITHCPFSNRLLSNKALDLEKAKKAGINYSIATDgLSSNISLSLLDELRAALLTHA-------NMPLLELaKILLLSAT 349

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 767958781 412 LGGSQALGLD-GEIgnfEVGKEFDAILINpkasdspidlfYGDFFGDISEAVIQKFLYlgdDRNIEEVYVGGKQVV 486
Cdd:PRK08418 350 RYGAKALGLNnGEI---KEGKDADLSVFE-----------LPEECTKKEQLPLQFILH---AKEVKKLFIGGKEVK 408
PRK08204 PRK08204
hypothetical protein; Provisional
 247-483 1.07e-18

hypothetical protein; Provisional


Pssm-ID: 181288 [Multi-domain]  Cd Length: 449  Bit Score: 88.52  E-value: 1.07e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958781 247 IVTPRFSlsCSETLMGELGnIAKTRDLHIQSHISenrdeveavknLYPSYKNYTSV--YDKNNLLTNKTVMAHGCYLSAE 324
Cdd:PRK08204 192 IRGPEFS--SWEVARADFR-LARELGLPISMHQG-----------FGPWGATPRGVeqLHDAGLLGPDLNLVHGNDLSDD 257

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958781 325 ELNVFHERGASIAHCPNSNLSLSSGFLNVLEVLKHEVKIGLGTDVAGGYSYSMLDAIR------RAVMVSNILLINKV-- 396
Cdd:PRK08204 258 ELKLLADSGGSFSVTPEIEMMMGHGYPVTGRLLAHGVRPSLGVDVVTSTGGDMFTQMRfalqaeRARDNAVHLREGGMpp 337

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958781 397 NEKSLTLKEVFRLATLGGSQALGLDGEIGNFEVGKEFDAILINPKAsdspIDLFYgdfFGDISEAVIQkflyLGDDRNIE 476
Cdd:PRK08204 338 PRLTLTARQVLEWATIEGARALGLEDRIGSLTPGKQADLVLIDATD----LNLAP---VHDPVGAVVQ----SAHPGNVD 406


                 ....*..
gi 767958781 477 EVYVGGK 483
Cdd:PRK08204 407 SVMVAGR 413
Met_dep_hydrolase_D cd01312
Metallo-dependent hydrolases, subgroup D is part of the superfamily of metallo-dependent ...
 167-434 2.12e-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: 83.65  E-value: 2.12e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958781 167 RRTLKNGTTTAcyfATIHTDSSLLLADITDKFGQRAFVGKVCMDlNDTFPEYKETTEESIKETERFVSemlqknySRVKP 246
Cdd:cd01312   82 RQMLESGTTSI---GAISSDGSLLPALASSGLRGVFFNEVIGSN-PSAIDFKGETFLERFKRSKSFES-------QLFIP 150

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958781 247 IVTPRFSLSCSETLMGELGNIAKTRDLHIQSHISENRDEVEAV-------KNLYPSY---KNYTSVYDKNNL------LT 310
Cdd:cd01312  151 AISPHAPYSVHPELAQDLIDLAKKLNLPLSTHFLESKEEREWLeeskgwfKHFWESFlklPKPKKLATAIDFldmlggLG 230

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958781 311 NKTVMAHGCYLSAEELNVFHERGASIAHCPNSNLSLSSGFLNVLEVLKHEVKIGLGTD-VAGGYSYSMLDAIRravmvSN 389
Cdd:cd01312  231 TRVSFVHCVYANLEEAEILASRGASIALCPRSNRLLNGGKLDVSELKKAGIPVSLGTDgLSSNISLSLLDELR-----AL 305

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*
gi 767958781 390 ILLINKVNEKSLTlKEVFRLATLGGSQALGLdgEIGNFEVGKEFD 434
Cdd:cd01312  306 LDLHPEEDLLELA-SELLLMATLGGARALGL--NNGEIEAGKRAD 347
PRK07203 PRK07203
putative aminohydrolase SsnA;
75-391 2.27e-16

putative aminohydrolase SsnA;


Pssm-ID: 235963 [Multi-domain]  Cd Length: 442  Bit Score: 81.14  E-value: 2.27e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958781  75 MPGLVDTHIHAsqYS-FA-GSSIDLP----LLEWLTKYTFpaehrfqNIDfaeevytRVVTLE-LLMSVLVkkTLffhkg 147
Cdd:PRK07203  58 MPGLINSHNHI--YSgLArGMMANIPpppdFISILKNLWW-------RLD-------RALTLEdVYYSALI--CS----- 114

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958781 148 gnMECkqpsqghvannrqnrrtLKNGTTT-----ACYFATihTDSSLLLADITDKFGQRafvGKVCMDLNDTFPEykETT 222
Cdd:PRK07203 115 --LEA-----------------IKNGVTTvfdhhASPNYI--GGSLFTIADAAKKVGLR---AMLCYETSDRDGE--KEL 168

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958781 223 EESIKETERFVSEMLQKNYSRVKPIVTPRFSLSCS-ETL------MGELGniaktRDLHIqsHISENRDEVEAVKNLYps 295
Cdd:PRK07203 169 QEGVEENIRFIKHIDEAKDDMVEAMFGLHASFTLSdATLekcreaVKETG-----RGYHI--HVAEGIYDVSDSHKKY-- 239

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958781 296 YKNYTSVYDKNNLLTNKTVMAHGCYLSAEELNVFHERGASIAHCPNSNLSLSSGFLNVLEVLKHEVKIGLGTDvagGYSY 375
Cdd:PRK07203 240 GKDIVERLADFGLLGEKTLAAHCIYLSDEEIDLLKETDTFVVHNPESNMGNAVGYNPVLEMIKNGILLGLGTD---GYTS 316

                        330
                 ....*....|....*.
gi 767958781 376 SMLDAIRravmVSNIL 391
Cdd:PRK07203 317 DMFESYK----VANFK 328
metallo-dependent_hydrolases cd01292
Superfamily of metallo-dependent hydrolases (also called amidohydrolase superfamily) is a ...
 167-417 1.16e-14

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: 74.29  E-value: 1.16e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958781 167 RRTLKNGTTTAC-----YFATIHTDSSLLLAD-ITDKFGQRAFVGKVCMDLNdtfPEYKETTEESIKETERFVsemlqkn 240
Cdd:cd01292   42 EALLAGGVTTVVdmgstPPPTTTKAAIEAVAEaARASAGIRVVLGLGIPGVP---AAVDEDAEALLLELLRRG------- 111

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958781 241 YSRVKPIVTPRFSLSCSETLMGELGNI---AKTRDLHIQSHISENRDEVEAVKNLYpsyknytsvydKNNLLTNKTVMAH 317
Cdd:cd01292  112 LELGAVGLKLAGPYTATGLSDESLRRVleeARKLGLPVVIHAGELPDPTRALEDLV-----------ALLRLGGRVVIGH 180

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958781 318 GCYLSAEELNVFHERGASIAHCPNSNLSLSS---GFLNVLEVLKHEVKIGLGTDVAGGYSYSMLDAIRRAVMVSNILLin 394
Cdd:cd01292  181 VSHLDPELLELLKEAGVSLEVCPLSNYLLGRdgeGAEALRRLLELGIRVTLGTDGPPHPLGTDLLALLRLLLKVLRLG-- 258

                        250       260
                 ....*....|....*....|...
gi 767958781 395 kvneksLTLKEVFRLATLGGSQA 417
Cdd:cd01292  259 ------LSLEEALRLATINPARA 275
PRK06151 PRK06151
N-ethylammeline chlorohydrolase; Provisional
 226-486 3.40e-13

N-ethylammeline chlorohydrolase; Provisional


Pssm-ID: 180428 [Multi-domain]  Cd Length: 488  Bit Score: 71.61  E-value: 3.40e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958781 226 IKETERFVSEMLQKNYSRVKPIVTPRFSLSCSETLMGELGNIAKTRDLHIQSHISENRDEVEAVKNLYpsykNYTS--VY 303
Cdd:PRK06151 188 LEEAIAFIKRVDGAHNGLVRGMLAPDRIETCTVDLLRRTAAAARELGCPVRLHCAQGVLEVETVRRLH----GTTPleWL 263

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958781 304 DKNNLLTNKTVMAHGCYLS---------AEELNVFHERGASIAHCPnSNLSLSSGFLNVLEVLKHE-VKIGLGTDVAggy 373
Cdd:PRK06151 264 ADVGLLGPRLLIPHATYISgsprlnysgGDDLALLAEHGVSIVHCP-LVSARHGSALNSFDRYREAgINLALGTDTF--- 339

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958781 374 sysmldairRAVMVSNI---LLINKVNEKSLT---LKEVFRLATLGGSQALGLDgEIGNFEVGKEFDAILINPKasdspi 447
Cdd:PRK06151 340 ---------PPDMVMNMrvgLILGRVVEGDLDaasAADLFDAATLGGARALGRD-DLGRLAPGAKADIVVFDLD------ 403

                        250       260       270
                 ....*....|....*....|....*....|....*....
gi 767958781 448 DLFYGDFFGDISEAVIQkflylGDDRNIEEVYVGGKQVV 486
Cdd:PRK06151 404 GLHMGPVFDPIRTLVTG-----GSGRDVRAVFVDGRVVM 437
archeal_chlorohydrolases cd01305
Predicted chlorohydrolases. These metallo-dependent hydrolases from archea are part of the ...
 267-415 4.81e-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: 63.19  E-value: 4.81e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958781 267 IAKTRDLHIQSHISENRD-----EVEAVKNLYPsyknytsvydknNLLTnktvmaHGCYLSAEELNVFHERGASIAHCPN 341
Cdd:cd01305  133 LLRRRGKLFAIHASETREsvgmtDIERALDLEP------------DLLV------HGTHLTDEDLELVRENGVPVVLCPR 194

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 767958781 342 SNLSLSSGFLNVLEVLKHEVKIGLGTDVAGGYSYSMLDAIRRAVMVSNILlinkvneKSLTLKEVFRLATLGGS 415
Cdd:cd01305  195 SNLYFGVGIPPVAELLKLGIKVLLGTDNVMVNEPDMWAEMEFLAKYSRLQ-------GYLSPLEILRMATVNAA 261
PRK07213 PRK07213
chlorohydrolase; Provisional
 278-442 9.25e-11

chlorohydrolase; Provisional


Pssm-ID: 235969 [Multi-domain]  Cd Length: 375  Bit Score: 63.52  E-value: 9.25e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958781 278 HISENRDEVEAVKNLYpsykNYTSVYDKNNLLTNKTVMAHGCYLSAEELNVFHERGASIAHCPNSNLSLSSGFLNVLEVL 357
Cdd:PRK07213 198 HAAEHKGSVEYSLEKY----GMTEIERLINLGFKPDFIVHATHPSNDDLELLKENNIPVVVCPRANASFNVGLPPLNEML 273

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958781 358 KHEVKIGLGTDVAGGYSYSM---LDAIRRAVmvsnillinkvnekSLTLKEVFRLATLGGSQALGLDgEIGNFEVGKEFD 434
Cdd:PRK07213 274 EKGILLGIGTDNFMANSPSIfreMEFIYKLY--------------HIEPKEILKMATINGAKILGLI-NVGLIEEGFKAD 338


                 ....*...
gi 767958781 435 AILINPKA 442
Cdd:PRK07213 339 FTFIKPTN 346
Met_dep_hydrolase_E cd01313
Metallo-dependent hydrolases, subgroup D is part of the superfamily of metallo-dependent ...
 273-483 5.80e-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: 5.80e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958781 273 LHIqsHISENRDEVEAVknLYPSYKNYTSVYDKNNLLTNKTVMAHGCYLSAEELNVFHERGASIAHCPNSNLSLSSGFLN 352
Cdd:cd01313  222 VHI--HLAEQPKEVDDC--LAAHGRRPVELLLDHGHLDARWCLVHATHLTDNETLLLGRSGAVVGLCPTTEANLGDGIFP 297

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958781 353 VLEVLKHEVKIGLGTDVAGG-----------YSYSMLDAiRRAVMVSnillinkvnEKSLTLKEVFRLATLGGSQALGLD 421
Cdd:cd01313  298 AAALLAAGGRIGIGSDSNARidlleelrqleYSQRLRDR-ARNVLAT---------AGGSSARALLDAALAGGAQALGLA 367

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 767958781 422 geIGNFEVGKEFDAILInpkASDSPidlfygDFFGDISEAVIQKFLYLGDDRNIEEVYVGGK 483
Cdd:cd01313  368 --TGALEAGARADLLSL---DLDHP------SLAGALPDTLLDAWVFAAGDREVRDVVVGGR 418
HutI COG1228
Imidazolonepropionase or related amidohydrolase [Secondary metabolites biosynthesis, transport ...
 313-486 3.89e-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: 3.89e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958781 313 TVMAHGCYLSAEELNVFHERGASIAhCPNSNLSLSSGFL------------------NVLEVLKHEVKIGLGTDVAGGYS 374
Cdd:COG1228  227 DSIEHGTYLDDEVADLLAEAGTVVL-VPTLSLFLALLEGaaapvaakarkvreaalaNARRLHDAGVPVALGTDAGVGVP 305

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958781 375 --YSMLDAIRRAVMVSnillinkvneksLTLKEVFRLATLGGSQALGLDGEIGNFEVGKEFDAILINpkasdspidlfyG 452
Cdd:COG1228  306 pgRSLHRELALAVEAG------------LTPEEALRAATINAAKALGLDDDVGSLEPGKLADLVLLD------------G 361

                        170       180       190
                 ....*....|....*....|....*....|....
gi 767958781 453 DFFGDISeaviqkflYLgddRNIEEVYVGGKQVV 486
Cdd:COG1228  362 DPLEDIA--------YL---EDVRAVMKDGRVVD 384
Amidohydro_3 pfam07969
Amidohydrolase family;
315-486 1.73e-05

Amidohydrolase family;


Pssm-ID: 400360 [Multi-domain]  Cd Length: 464  Bit Score: 47.14  E-value: 1.73e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958781  315 MAHGC---YLSAEELNVFHERGASIAHCPNSNLSLS------------SGFLNVLEVLKHEVKIGLGTDVAGGySYSMLD 379
Cdd:pfam07969 298 IEHAQgvvPYTYSQIERVAALGGAAGVQPVFDPLWGdwlqdrlgaeraRGLTPVKELLNAGVKVALGSDAPVG-PFDPWP 376

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958781  380 AIRRAVM-----VSNILLInkvnEKSLTLKEVFRLATLGGSQALGLDGEIGNFEVGKEFDAILINpkasdspIDLFygdf 454
Cdd:pfam07969 377 RIGAAVMrqtagGGEVLGP----DEELSLEEALALYTSGPAKALGLEDRKGTLGVGKDADLVVLD-------DDPL---- 441

                         170       180       190
                  ....*....|....*....|....*....|..
gi 767958781  455 fgDISEAVIqkflylgDDRNIEEVYVGGKQVV 486
Cdd:pfam07969 442 --TVDPPAI-------ADIRVRLTVVDGRVVY 464
PRK09229 PRK09229
N-formimino-L-glutamate deiminase; Validated
 273-486 7.91e-05

N-formimino-L-glutamate deiminase; Validated


Pssm-ID: 236420 [Multi-domain]  Cd Length: 456  Bit Score: 44.84  E-value: 7.91e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958781 273 LHIqsHISENRDEVEAVKNLY---PsyknyTSVYDKNNLLTNKTVMAHGCYLSAEELNVFHERGASIAHCPNSNLSLSSG 349
Cdd:PRK09229 231 VHI--HIAEQTKEVDDCLAWSgarP-----VEWLLDHAPVDARWCLVHATHLTDAETARLARSGAVAGLCPTTEANLGDG 303

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958781 350 FLNVLEVLKHEVKIGLGTDvaggySYSMLDAI---------------RRAVMVSNillinkvnEKSLTLKEVFRLATLGG 414
Cdd:PRK09229 304 IFPAVDYLAAGGRFGIGSD-----SHVSIDLVeelrlleygqrlrdrRRNVLAAA--------AQPSVGRRLFDAALAGG 370

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 767958781 415 SQALGLDgeIGNFEVGKEFDAILINPkasDSPidlfygDFFGDISEAVIQKFLYLGDDRNIEEVYVGGKQVV 486
Cdd:PRK09229 371 AQALGRA--IGGLAVGARADLVVLDL---DHP------ALAGREGDALLDRWVFAGGDAAVRDVWVAGRWVV 431
Imidazolone-5PH cd01296
Imidazolonepropionase/imidazolone-5-propionate hydrolase (Imidazolone-5PH) catalyzes the third ...
 315-465 1.14e-04

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


Pssm-ID: 238621 [Multi-domain]  Cd Length: 371  Bit Score: 44.17  E-value: 1.14e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958781 315 MAHGCYLSAEELNVFHERGASIAHCPNSNLSLSSGFLNVLEVLKHEVKIGLGTDVAGGySY---SMLDAIRRAVmvsnIL 391
Cdd:cd01296  233 ADHLEHTSDEGIAALAEAGTVAVLLPGTAFSLRETYPPARKLIDAGVPVALGTDFNPG-SSptsSMPLVMHLAC----RL 307

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 767958781 392 LinkvnekSLTLKEVFRLATLGGSQALGLDGEIGNFEVGKEFDAILINpkaSDSPIDLFYgdFFG-DISEAVIQK 465
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 ...
 344-439 2.01e-03

Metallo-dependent hydrolases, subgroup A is part of the superfamily of metallo-dependent hydrolases, a large group of proteins that show conservation in their 3-dimensional fold (TIM barrel) and in details of their active site. The vast majority of the members have a conserved metal binding site, involving four histidines and one aspartic acid residue. In the common reaction mechanism, the metal ion (or ions) deprotonate a water molecule for a nucleophilic attack on the substrate. The function of this subgroup is unknown.


Pssm-ID: 238624 [Multi-domain]  Cd Length: 342  Bit Score: 40.35  E-value: 2.01e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767958781 344 LSLSSGFLNVLEVLKHEVKIGLGTD-----VAGGYSYSMLdairrAVMVsnillinkvnEKSLTLKEVFRLATLGGSQAL 418
Cdd:cd01299  247 LVLEAGRDALRRAHKAGVKIAFGTDagfpvPPHGWNAREL-----ELLV----------KAGGTPAEALRAATANAAELL 311

                         90       100
                 ....*....|....*....|.
gi 767958781 419 GLDGEIGNFEVGKEFDAILIN 439
Cdd:cd01299  312 GLSDELGVIEAGKLADLLVVD 332
 
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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