|
Name |
Accession |
Description |
Interval |
E-value |
| GDEase |
cd01303 |
Guanine deaminase (GDEase). Guanine deaminase is an aminohydrolase responsible for the ... |
1-408 |
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: 575.38 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217382246 1 MPGLVDTHIHASQYSFAGSSIDLPLLEWLTKYTFPAEHRFQNIDFAEEVYTRVVtlellmsvlvkktlffhkggnmeckq 80
Cdd:cd01303 64 LPGFIDTHIHAPQYANIGSGLGEPLLDWLETYTFPEEAKFADPAYAREVYGRFL-------------------------- 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217382246 81 psqghvannrqnRRTLKNGTTTACYFATIHTDSSLLLADITDKFGQRAFVGKVCMDLNDtfPEYK-ETTEESIKETERFV 159
Cdd:cd01303 118 ------------DELLRNGTTTACYFATIHPESTEALFEEAAKRGQRAIAGKVCMDRNA--PEYYrDTAESSYRDTKRLI 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217382246 160 SEMLQKnYSRVKPIVTPRFSLSCSETLMGELGNIAKT-RDLHIQSHISENRDEVEAVKNLYPSYKNYTSVYDKNNLLTNK 238
Cdd:cd01303 184 ERWHGK-SGRVKPAITPRFAPSCSEELLAALGKLAKEhPDLHIQTHISENLDEIAWVKELFPGARDYLDVYDKYGLLTEK 262
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217382246 239 TVMAHGCYLSAEELNVFHERGASIAHCPNSNLSLSSGFLNVLEVLKHEVKIGLGTDVAGGYSYSMLDAIRRAVMVSNILL 318
Cdd:cd01303 263 TVLAHCVHLSEEEFNLLKERGASVAHCPTSNLFLGSGLFDVRKLLDAGIKVGLGTDVGGGTSFSMLDTLRQAYKVSRLLG 342
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217382246 319 INKVNEKSLTLKEVFRLATLGGSQALGLDGEIGNFEVGKEFDAILINPKASDSPIDLfygDFFGDISEAVIQKFLYLGDD 398
Cdd:cd01303 343 YELGGHAKLSPAEAFYLATLGGAEALGLDDKIGNFEVGKEFDAVVIDPSATPLLADR---MFRVESLEEALFKFLYLGDD 419
|
410
....*....|
gi 2217382246 399 RNIEEVYVGG 408
Cdd:cd01303 420 RNIREVYVAG 429
|
|
| guan_deamin |
TIGR02967 |
guanine deaminase; This model describes guanine deaminase, which hydrolyzes guanine to ... |
1-408 |
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: 522.97 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217382246 1 MPGLVDTHIHASQYSFAGSsIDLPLLEWLTKYTFPAEHRFQNIDFAEEVYTRVVtlellmsvlvkktlffhkggnmeckq 80
Cdd:TIGR02967 44 MPGFIDTHIHYPQTEMIAS-YGEQLLEWLEKYTFPTEARFADPDHAEEVAEFFL-------------------------- 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217382246 81 psqghvannrqnRRTLKNGTTTACYFATIHTDSSLLLADITDKFGQRAFVGKVCMDLNdtFPEY-KETTEESIKETERFV 159
Cdd:TIGR02967 97 ------------DELLRNGTTTALVFATVHPESVDALFEAALKRGMRMIAGKVLMDRN--APDYlRDTAESSYDESKALI 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217382246 160 SEMLQKNysRVKPIVTPRFSLSCSETLMGELGNIAKTR-DLHIQSHISENRDEVEAVKNLYPSYKNYTSVYDKNNLLTNK 238
Cdd:TIGR02967 163 ERWHGKG--RLLYAVTPRFAPTSSPEQLAAAGELAKEYpDVYVQTHLSENKDEIAWVKELFPEAKDYLDVYDHYGLLGRR 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217382246 239 TVMAHGCYLSAEELNVFHERGASIAHCPNSNLSLSSGFLNVLEVLKHEVKIGLGTDVAGGYSYSMLDAIRRAVMVSNILl 318
Cdd:TIGR02967 241 SVFAHCIHLSDEECQRLAETGAAIAHCPTSNLFLGSGLFNLKKALEHGVRVGLGTDVGGGTSFSMLQTLREAYKVSQLQ- 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217382246 319 inkvnEKSLTLKEVFRLATLGGSQALGLDGEIGNFEVGKEFDAILINPKASDSPIDLFYGdffGDISEAVIQKFLYLGDD 398
Cdd:TIGR02967 320 -----GARLSPFEAFYLATLGGARALDLDDRIGNFEPGKEADFVVLDPAATPLLALRFEG---ADTLEDKLFKLMYLGDD 391
|
410
....*....|
gi 2217382246 399 RNIEEVYVGG 408
Cdd:TIGR02967 392 RNVAETYVAG 401
|
|
| SsnA |
COG0402 |
Cytosine/adenosine deaminase or related metal-dependent hydrolase [Nucleotide transport and ... |
1-412 |
6.45e-110 |
|
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: 329.87 E-value: 6.45e-110
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217382246 1 MPGLVDTHIHASQYSFAGSSIDLPLLEWLTKYTFPAEHRFQnidfAEEVY--TRVVTLELLmsvlvkktlffhkggnmec 78
Cdd:COG0402 58 LPGLVNTHTHLPQTLLRGLADDLPLLDWLEEYIWPLEARLD----PEDVYagALLALAEML------------------- 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217382246 79 kqpsqghvannrqnrrtlKNGTTTACYFATIHTDSSLLLADITDKFGQRAFVGKVCMDLNdtFPE-YKETTEESIKETER 157
Cdd:COG0402 115 ------------------RSGTTTVADFYYVHPESADALAEAAAEAGIRAVLGRGLMDRG--FPDgLREDADEGLADSER 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217382246 158 FVSEMLQKNYSRVKPIVTPRFSLSCSETLMGELGNIAKTRDLHIQSHISENRDEVEAVKNLYPsyKNYTSVYDKNNLLTN 237
Cdd:COG0402 175 LIERWHGAADGRIRVALAPHAPYTVSPELLRAAAALARELGLPLHTHLAETRDEVEWVLELYG--KRPVEYLDELGLLGP 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217382246 238 KTVMAHGCYLSAEELNVFHERGASIAHCPNSNLSLSSGFLNVLEVLKHEVKIGLGTDVAGG-YSYSMLDAIRRAVMVSNI 316
Cdd:COG0402 253 RTLLAHCVHLTDEEIALLAETGASVAHCPTSNLKLGSGIAPVPRLLAAGVRVGLGTDGAASnNSLDMFEEMRLAALLQRL 332
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217382246 317 LlinKVNEKSLTLKEVFRLATLGGSQALGLDGEIGNFEVGKEFDAILINPKASD-SPIDlfygdffgdiseAVIQKFLYL 395
Cdd:COG0402 333 R---GGDPTALSAREALEMATLGGARALGLDDEIGSLEPGKRADLVVLDLDAPHlAPLH------------DPLSALVYA 397
|
410
....*....|....*..
gi 2217382246 396 GDDRNIEEVYVGGKQVV 412
Cdd:COG0402 398 ADGRDVRTVWVAGRVVV 414
|
|
| PRK09228 |
PRK09228 |
guanine deaminase; Provisional |
1-411 |
2.30e-97 |
|
guanine deaminase; Provisional
Pssm-ID: 236419 [Multi-domain] Cd Length: 433 Bit Score: 298.26 E-value: 2.30e-97
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217382246 1 MPGLVDTHIHASQYSFAGSsidlP---LLEWLTKYTFPAEHRFQNIDFAEEVYTRVVTlELLmsvlvkktlffhkggnme 77
Cdd:PRK09228 69 LPGFIDTHIHYPQTDMIAS----YgeqLLDWLNTYTFPEERRFADPAYAREVAEFFLD-ELL------------------ 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217382246 78 ckqpsqghvannrqnrrtlKNGTTTACYFATIHTDSsllladiTDKF-------GQRAFVGKVCMDLNdtFPEY-KETTE 149
Cdd:PRK09228 126 -------------------RNGTTTALVFGTVHPQS-------VDALfeaaearNMRMIAGKVLMDRN--APDGlRDTAE 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217382246 150 ESIKETERfvseMLQK--NYSRVKPIVTPRFSLSCSETLMGELGNIAKTR-DLHIQSHISENRDEVEAVKNLYPSYKNYT 226
Cdd:PRK09228 178 SGYDDSKA----LIERwhGKGRLLYAITPRFAPTSTPEQLEAAGALAREHpDVWIQTHLSENLDEIAWVKELFPEARDYL 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217382246 227 SVYDKNNLLTNKTVMAHGCYLSAEELNVFHERGASIAHCPNSNLSLSSGFLNVLEVLKHEVKIGLGTDVAGGYSYSMLDA 306
Cdd:PRK09228 254 DVYERYGLLGPRAVFAHCIHLEDRERRRLAETGAAIAFCPTSNLFLGSGLFDLKRADAAGVRVGLGTDVGGGTSFSMLQT 333
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217382246 307 IRRAVMVSnillinKVNEKSLTLKEVFRLATLGGSQALGLDGEIGNFEVGKEFDAILINPKA----------SDSPIDLF 376
Cdd:PRK09228 334 MNEAYKVQ------QLQGYRLSPFQAFYLATLGGARALGLDDRIGNLAPGKEADFVVLDPAAtpllalrtarAESLEELL 407
|
410 420 430
....*....|....*....|....*....|....*
gi 2217382246 377 YGdffgdiseaviqkFLYLGDDRNIEEVYVGGKQV 411
Cdd:PRK09228 408 FA-------------LMTLGDDRAVAETYVAGRPV 429
|
|
| ATZ_TRZ_like |
cd01298 |
TRZ/ATZ family contains enzymes from the atrazine degradation pathway and related hydrolases. ... |
1-412 |
3.82e-68 |
|
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: 222.08 E-value: 3.82e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217382246 1 MPGLVDTHIHASQYSFAGSSIDLPLLEWLTKYTFPAEHRFQnidfAEEVY--TRVVTLELLmsvlvkktlffhkggnmec 78
Cdd:cd01298 55 MPGLVNTHTHLAMTLLRGLADDLPLMEWLKDLIWPLERLLT----EEDVYlgALLALAEMI------------------- 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217382246 79 kqpsqghvannrqnrrtlKNGTTTAC--YFatIHTDSsllLADITDKFGQRAFVGKVCMDLNDtfpEYKETTEESIKETE 156
Cdd:cd01298 112 ------------------RSGTTTFAdmYF--FYPDA---VAEAAEELGIRAVLGRGIMDLGT---EDVEETEEALAEAE 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217382246 157 RFVSEMLQKNYSRVKPIVTPRFSLSCSETLMGELGNIAKTRDLHIQSHISENRDEVEAVKNLYpsykNYTSV-Y-DKNNL 234
Cdd:cd01298 166 RLIREWHGAADGRIRVALAPHAPYTCSDELLREVAELAREYGVPLHIHLAETEDEVEESLEKY----GKRPVeYlEELGL 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217382246 235 LTNKTVMAHGCYLSAEELNVFHERGASIAHCPNSNLSLSSGFLNVLEVLKHEVKIGLGTD-VAGGYSYSMLDAIRRAvmv 313
Cdd:cd01298 242 LGPDVVLAHCVWLTDEEIELLAETGTGVAHNPASNMKLASGIAPVPEMLEAGVNVGLGTDgAASNNNLDMFEEMRLA--- 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217382246 314 sniLLINKV---NEKSLTLKEVFRLATLGGSQALGLDgEIGNFEVGKEFDAILINPkasDSPidlfygDFFG---DISEA 387
Cdd:cd01298 319 ---ALLQKLahgDPTALPAEEALEMATIGGAKALGLD-EIGSLEVGKKADLILIDL---DGP------HLLPvhdPISHL 385
|
410 420
....*....|....*....|....*
gi 2217382246 388 ViqkflYLGDDRNIEEVYVGGKQVV 412
Cdd:cd01298 386 V-----YSANGGDVDTVIVNGRVVM 405
|
|
| PRK07228 |
PRK07228 |
5'-deoxyadenosine deaminase; |
1-365 |
3.06e-58 |
|
5'-deoxyadenosine deaminase;
Pssm-ID: 180895 [Multi-domain] Cd Length: 445 Bit Score: 197.14 E-value: 3.06e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217382246 1 MPGLVDTHIHASQYSFAGSSIDLPLLEWLTKYTFPAE--HRfqnidfAEEVYTrvvtlellmSVLVkktlffhkgGNMEC 78
Cdd:PRK07228 55 IPGLIQGHIHLCQTLFRGIADDLELLDWLKDRIWPLEaaHD------AESMYY---------SALL---------GIGEL 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217382246 79 kqpsqghvannrqnrrtLKNGTTTACYFATI-HTDSSL-LLADItdkfGQRAFVGKVCMDLNDTFPE-YKETTEESIKET 155
Cdd:PRK07228 111 -----------------IESGTTTIVDMESVhHTDSAFeAAGES----GIRAVLGKVMMDYGDDVPEgLQEDTEASLAES 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217382246 156 ERFVSEMLQKNYSRVKPIVTPRFSLSCSETLMGELGNIAKTRDLHIQSHISENRDEVEAVKNlYPSYKNYTsVYDKNNLL 235
Cdd:PRK07228 170 VRLLEKWHGADNGRIRYAFTPRFAVSCTEELLRGVRDLADEYGVRIHTHASENRGEIETVEE-ETGMRNIH-YLDEVGLT 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217382246 236 TNKTVMAHGCYLSAEELNVFHERGASIAHCPNSNLSLSSGFLNVLEVLKHEVKIGLGTDvaGGYSYSMLDA---IRRAVm 312
Cdd:PRK07228 248 GEDLILAHCVWLDEEEREILAETGTHVTHCPSSNLKLASGIAPVPDLLERGINVALGAD--GAPCNNTLDPfteMRQAA- 324
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*.
gi 2217382246 313 vsnilLINKVNE---KSLTLKEVFRLATLGGSQALGLDGEIGNFEVGKEFDAILIN 365
Cdd:PRK07228 325 -----LIQKVDRlgpTAMPARTVFEMATLGGAKAAGFEDEIGSLEEGKKADLAILD 375
|
|
| Amidohydro_1 |
pfam01979 |
Amidohydrolase family; This family of enzymes are a a large metal dependent hydrolase ... |
1-411 |
1.59e-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: 1.59e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217382246 1 MPGLVDTHIHASQYSFAGSSIDLpllewltkytfpaehrfqniDFAEEVYTRVVTlellmsvlvkktlffhkggnmeckq 80
Cdd:pfam01979 3 LPGLIDAHVHLEMGLLRGIPVPP--------------------EFAYEALRLGIT------------------------- 37
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217382246 81 psqghvannrqnrRTLKNGTTTACYFATIHTDSSLLLADITDK--FGQRAFVGKVCMDLNDTFPEYKETTEESIKETErf 158
Cdd:pfam01979 38 -------------TMLKSGTTTVLDMGATTSTGIEALLEAAEElpLGLRFLGPGCSLDTDGELEGRKALREKLKAGAE-- 102
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217382246 159 vsEMLQKNYSRVKPIVTPRFSLSCSETLMGELGNIAKTRDLHIQSHISENRDEVEAVKNLYPS---YKNYTSVYDKNNLL 235
Cdd:pfam01979 103 --FIKGMADGVVFVGLAPHGAPTFSDDELKAALEEAKKYGLPVAIHALETKGEVEDAIAAFGGgieHGTHLEVAESGGLL 180
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217382246 236 -TNKTVMAHGCYLSAEELNVFHER--GASIAHCPNSNLSLSSGFLNVLEVLKHEVKIGLGTDVAG-GYSYSMLDAIRRAV 311
Cdd:pfam01979 181 dIIKLILAHGVHLSPTEANLLAEHlkGAGVAHCPFSNSKLRSGRIALRKALEDGVKVGLGTDGAGsGNSLNMLEELRLAL 260
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217382246 312 mvsnilLINKVNEKSLTLKEVFRLATLGGSQALGLDGEIGNFEVGKEFDAILINPKasdspidlfygdffgdiseaVIQK 391
Cdd:pfam01979 261 ------ELQFDPEGGLSPLEALRMATINPAKALGLDDKVGSIEVGKDADLVVVDLD--------------------PLAA 314
|
410 420
....*....|....*....|
gi 2217382246 392 FLYLGDDRNIEEVYVGGKQV 411
Cdd:pfam01979 315 FFGLKPDGNVKKVIVKGKIV 334
|
|
| PRK08393 |
PRK08393 |
N-ethylammeline chlorohydrolase; Provisional |
2-412 |
1.66e-42 |
|
N-ethylammeline chlorohydrolase; Provisional
Pssm-ID: 181411 [Multi-domain] Cd Length: 424 Bit Score: 154.96 E-value: 1.66e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217382246 2 PGLVDTHIHASQYSFAGSSIDLPLLEWLTKYTFPAEHRFQNidfaEEVY--TRVVTLELLmsvlvkktlffhkggnmeck 79
Cdd:PRK08393 54 PGFINAHTHSPMVLLRGLADDVPLMEWLQNYIWPRERKLKR----KDIYwgAYLGLLEMI-------------------- 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217382246 80 qpsqghvannrqnrrtlKNGTTTAC--YFatiHTDSsllLADITDKFGQRAFVGKVCMDLNDtfpeyKETTEESIKETER 157
Cdd:PRK08393 110 -----------------KSGTTTFVdmYF---HMEE---VAKATLEVGLRGYLSYGMVDLGD-----EEKREKEIKETEK 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217382246 158 FVSEMLQKNYSRVKPIVTPRFSLSCSETLMGELGNIAKTRDLHIQSHISENRDEVEAVKNLYPsyKNYTSVYDKNNLLTN 237
Cdd:PRK08393 162 LMEFIEKLNSPRVHFVFGPHAPYTCSLALLKWVREKAREWNKLITIHLSETMDEIKQIREKYG--KSPVVLLDEIGFLNE 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217382246 238 KTVMAHGCYLSAEELNVFHERGASIAHCPNSNLSLSSGFLNVLEVLKHEVKIGLGTDvaGGYSYSMLDAIRRAVMVSnil 317
Cdd:PRK08393 240 DVIAAHGVWLSSRDIRILASAGVTVAHNPASNMKLGSGVMPLRKLLNAGVNVALGTD--GAASNNNLDMLREMKLAA--- 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217382246 318 LINKVNEKSLTL---KEVFRLATLGGSQALGLDGeiGNFEVGKEFDAILIN-PKASDSPIDlfygdffgdiseAVIQKFL 393
Cdd:PRK08393 315 LLHKVHNLDPTIadaETVFRMATQNGAKALGLKA--GVIKEGYLADIAVIDfNRPHLRPIN------------NPISHLV 380
|
410
....*....|....*....
gi 2217382246 394 YLGDDRNIEEVYVGGKQVV 412
Cdd:PRK08393 381 YSANGNDVETTIVDGKIVM 399
|
|
| PRK06038 |
PRK06038 |
N-ethylammeline chlorohydrolase; Provisional |
1-367 |
2.61e-40 |
|
N-ethylammeline chlorohydrolase; Provisional
Pssm-ID: 180363 [Multi-domain] Cd Length: 430 Bit Score: 149.13 E-value: 2.61e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217382246 1 MPGLVDTHIHASQYSFAGSSIDLPLLEWLTKYTFPAEHRFQnidfAEEVY--TRVVTLELLmsvlvkktlffhkggnmec 78
Cdd:PRK06038 54 MPGLVNTHTHAAMTLFRGYADDLPLAEWLNDHIWPAEAKLT----AEDVYagSLLACLEMI------------------- 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217382246 79 kqpsqghvannrqnrrtlKNGTTTacyFAT--IHTDSSlllADITDKFGQRAFVGKVCMDLNDTfpeykETTEESIKETE 156
Cdd:PRK06038 111 ------------------KSGTTS---FADmyFYMDEV---AKAVEESGLRAALSYGMIDLGDD-----EKGEAELKEGK 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217382246 157 RFVSEMLQKNYSRVKPIVTPRFSLSCSETLMGELGNIAKTRDLHIQSHISENRDEVEAVKNLYpsykNYTSVY--DKNNL 234
Cdd:PRK06038 162 RFVKEWHGAADGRIKVMYGPHAPYTCSEEFLSKVKKLANKDGVGIHIHVLETEAELNQMKEQY----GMCSVNylDDIGF 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217382246 235 LTNKTVMAHGCYLSAEELNVFHERGASIAHCPNSNLSLSSGFLNVLEVLKHEVKIGLGTD-VAGGYSYSMLDAIRRAVMV 313
Cdd:PRK06038 238 LGPDVLAAHCVWLSDGDIEILRERGVNVSHNPVSNMKLASGIAPVPKLLERGVNVSLGTDgCASNNNLDMFEEMKTAALL 317
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....
gi 2217382246 314 SNillINKVNEKSLTLKEVFRLATLGGSQALGLdgEIGNFEVGKEFDAILINPK 367
Cdd:PRK06038 318 HK---VNTMDPTALPARQVLEMATVNGAKALGI--NTGMLKEGYLADIIIVDMN 366
|
|
| PRK06687 |
PRK06687 |
TRZ/ATZ family protein; |
1-412 |
1.58e-37 |
|
TRZ/ATZ family protein;
Pssm-ID: 180657 [Multi-domain] Cd Length: 419 Bit Score: 141.30 E-value: 1.58e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217382246 1 MPGLVDTHIHASQYSFAGSSIDLPLLEWLTKYTFPAEHrfqniDFAEEVYTRVVTLELLMSVLVKKTLFfhkggnMECKQ 80
Cdd:PRK06687 57 MPGLVNCHTHSAMTGLRGIRDDSNLHEWLNDYIWPAES-----EFTPDMTTNAVKEALTEMLQSGTTTF------NDMYN 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217382246 81 PSQGHVANNRQNRRTLKngttTACYFATIhtdssllladitdkfgqrafvgkvcmdlndTFPEYKETTEESIKETERFVS 160
Cdd:PRK06687 126 PNGVDIQQIYQVVKTSK----MRCYFSPT------------------------------LFSSETETTAETISRTRSIID 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217382246 161 EMLQKNYSRVKPIVTPRFSLSCSETLMGELGNIAKTRDLHIQSHISENRDEVEAVKNLYPsyKNYTSVYDKNNLLTNKTV 240
Cdd:PRK06687 172 EILKYKNPNFKVMVAPHSPYSCSRDLLEASLEMAKELNIPLHVHVAETKEESGIILKRYG--KRPLAFLEELGYLDHPSV 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217382246 241 MAHGCYLSAEELNVFHERGASIAHCPNSNLSLSSGFLNVLEVLKHEVKIGLGTD-VAGGYSYSMLDAIRRAVMVSNillI 319
Cdd:PRK06687 250 FAHGVELNEREIERLASSQVAIAHNPISNLKLASGIAPIIQLQKAGVAVGIATDsVASNNNLDMFEEGRTAALLQK---M 326
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217382246 320 NKVNEKSLTLKEVFRLATLGGSQALGLDGEIGNFEVGKEFDAILINPKASdspIDLFygdffgdISEAVIQKFLYLGDDR 399
Cdd:PRK06687 327 KSGDASQFPIETALKVLTIEGAKALGMENQIGSLEVGKQADFLVIQPQGK---IHLQ-------PQENMLSHLVYAVKSS 396
|
410
....*....|...
gi 2217382246 400 NIEEVYVGGKQVV 412
Cdd:PRK06687 397 DVDDVYIAGEQVV 409
|
|
| PRK09045 |
PRK09045 |
TRZ/ATZ family hydrolase; |
1-412 |
3.37e-36 |
|
TRZ/ATZ family hydrolase;
Pssm-ID: 236366 [Multi-domain] Cd Length: 443 Bit Score: 138.12 E-value: 3.37e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217382246 1 MPGLVDTHIHASQYSFAGSSIDLPLLEWLTKYTFPAEHRFQNIDFaeeVY--TRVVTLELLmsvlvkktlffhkggnmec 78
Cdd:PRK09045 65 IPGLINAHTHAAMSLLRGLADDLPLMTWLQDHIWPAEGAWVSEEF---VRdgTLLAIAEML------------------- 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217382246 79 kqpsqghvannrqnrrtlKNGTTTA--CYFatiHTDSsllLADITDKFGQRAFVGKVCMDlndtFP-EYKETTEESI--- 152
Cdd:PRK09045 123 ------------------RGGTTCFndMYF---FPEA---AAEAAHQAGMRAQIGMPVLD----FPtAWASDADEYLakg 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217382246 153 -KETERFvsemlqKNYSRVKPIVTPRFSLSCSETLMGELGNIAKTRDLHIQSHISENRDEVEAvknlypSYKNY----TS 227
Cdd:PRK09045 175 lELHDQW------RHHPLISTAFAPHAPYTVSDENLERIRTLAEQLDLPIHIHLHETAQEIAD------SLKQHgqrpLA 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217382246 228 VYDKNNLLTNKTVMAHGCYLSAEELNVFHERGASIAHCPNSNLSLSSGFLNVLEVLKHEVKIGLGTD-VAGGYSYSMLDA 306
Cdd:PRK09045 243 RLARLGLLGPRLIAVHMTQLTDAEIALLAETGCSVVHCPESNLKLASGFCPVAKLLQAGVNVALGTDgAASNNDLDLFGE 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217382246 307 IRRAVMVSnillinKV---NEKSLTLKEVFRLATLGGSQALGLDGEIGNFEVGKEFDAILINPKASDS-PIdlfygdfFG 382
Cdd:PRK09045 323 MRTAALLA------KAvagDATALPAHTALRMATLNGARALGLDDEIGSLEPGKQADLVAVDLSGLETqPV-------YD 389
|
410 420 430
....*....|....*....|....*....|
gi 2217382246 383 DISEAViqkflYLGDDRNIEEVYVGGKQVV 412
Cdd:PRK09045 390 PVSQLV-----YAAGREQVSHVWVAGKQLL 414
|
|
| PRK15493 |
PRK15493 |
bifunctional S-methyl-5'-thioadenosine deaminase/S-adenosylhomocysteine deaminase; |
1-412 |
1.95e-29 |
|
bifunctional S-methyl-5'-thioadenosine deaminase/S-adenosylhomocysteine deaminase;
Pssm-ID: 185390 [Multi-domain] Cd Length: 435 Bit Score: 119.01 E-value: 1.95e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217382246 1 MPGLVDTHIHASQYSFAGSSIDLPLLEWLTKYTFPAEHRFqnidfAEEVYTRVVTLELLMSVlvkktlffhkggnmeckq 80
Cdd:PRK15493 58 LPGLVNTHTHVVMSLLRGIGDDMLLQPWLETRIWPLESQF-----TPELAVASTELGLLEMV------------------ 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217382246 81 psqghvannrqnrrtlKNGTTT-ACYFATIHTDSSLLLADITDKfGQRAFVGKVCMDLNDtfpeyKETTEESIKETERFV 159
Cdd:PRK15493 115 ----------------KSGTTSfSDMFNPIGVDQDAIMETVSRS-GMRAAVSRTLFSFGT-----KEDEKKAIEEAEKYV 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217382246 160 SEMLQKNySRVKPIVTPRFSLSCSETLMGELGNIAKTRDLHIQSHISENRDEVEAVKNLYPsyKNYTSVYDKNNLLTNKT 239
Cdd:PRK15493 173 KRYYNES-GMLTTMVAPHSPYTCSTELLEECARIAVENQTMVHIHLSETEREVRDIEAQYG--KRPVEYAASCGLFKRPT 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217382246 240 VMAHGCYLSAEELNVFHERGASIAHCPNSNLSLSSGFLNVLEVLKHEVKIGLGTD-VAGGYSYSMLDAIRRAVMVSNILl 318
Cdd:PRK15493 250 VIAHGVVLNDNERAFLAEHDVRVAHNPNSNLKLGSGIANVKAMLEAGIKVGIATDsVASNNNLDMFEEMRIATLLQKGI- 328
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217382246 319 inKVNEKSLTLKEVFRLATLGGSQALGLDgEIGNFEVGKEFDAILINP--KASDSPidlfygdffgdiSEAVIQKFLYLG 396
Cdd:PRK15493 329 --HQDATALPVETALTLATKGAAEVIGMK-QTGSLEVGKCADFITIDPsnKPHLQP------------ADEVLSHLVYAA 393
|
410
....*....|....*.
gi 2217382246 397 DDRNIEEVYVGGKQVV 412
Cdd:PRK15493 394 SGKDISDVIINGKRVV 409
|
|
| PRK08203 |
PRK08203 |
hydroxydechloroatrazine ethylaminohydrolase; Reviewed |
146-360 |
2.81e-21 |
|
hydroxydechloroatrazine ethylaminohydrolase; Reviewed
Pssm-ID: 236184 [Multi-domain] Cd Length: 451 Bit Score: 95.69 E-value: 2.81e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217382246 146 ETTEESIKETERFVSEMLQKN-YSRVKPIVTPRFSLSCSETLMGELGNIAKTRDLHIQSHISENRDEVEAVKNLYpsykN 224
Cdd:PRK08203 174 EDEDAILADSQRLIDRYHDPGpGAMLRIALAPCSPFSVSRELMRESAALARRLGVRLHTHLAETLDEEAFCLERF----G 249
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217382246 225 YTSV-Y-DKNNLLTNKTVMAHGCYLSAEELNVFHERGASIAHCPNSNLSLSSGFLNVLEVLKHEVKIGLGTD-VAGGYSY 301
Cdd:PRK08203 250 MRPVdYlEDLGWLGPDVWLAHCVHLDDAEIARLARTGTGVAHCPCSNMRLASGIAPVRELRAAGVPVGLGVDgSASNDGS 329
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2217382246 302 SMLDAIRRAvmvsniLLINKV--NEKSLTLKEVFRLATLGGSQALGLDgEIGNFEVGKEFD 360
Cdd:PRK08203 330 NLIGEARQA------LLLQRLryGPDAMTAREALEWATLGGARVLGRD-DIGSLAPGKLAD 383
|
|
| PRK06380 |
PRK06380 |
metal-dependent hydrolase; Provisional |
1-409 |
8.59e-21 |
|
metal-dependent hydrolase; Provisional
Pssm-ID: 180548 [Multi-domain] Cd Length: 418 Bit Score: 93.79 E-value: 8.59e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217382246 1 MPGLVDTHIHASQYSFAGSSIDLPLLEWLTKyTFPAEHRFQNidfaEEVYtrvvtlellmsvlvkktlffhKGGNMECKQ 80
Cdd:PRK06380 53 MPGLINTHAHVGMTASKGLFDDVDLEEFLMK-TFKYDSKRTR----EGIY---------------------NSAKLGMYE 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217382246 81 psqghvannrqnrrTLKNGTTTacyFATIHTDSSLLlADITDKFGQRAFVGKVCMDlndtfPEYKETTEESIKETERFVS 160
Cdd:PRK06380 107 --------------MINSGITA---FVDLYYSEDII-AKAAEELGIRAFLSWAVLD-----EEITTQKGDPLNNAENFIR 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217382246 161 EMLQKNYsrVKPIVTPRFSLSCSETLMGELGNIAKTRDLHIQSHISENRDEVeavknlYPSYKNY----TSVYDKNNLLT 236
Cdd:PRK06380 164 EHRNEEL--VTPSIGVQGIYVANDETYLKAKEIAEKYDTIMHMHLSETRKEV------YDHVKRTgerpVEHLEKIGFLN 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217382246 237 NKTVMAHGCYLSAEELNVFHERGASIAHCPNSNLSLSS-GFLNVLEVLKHEVKIGLGTDVAGgySYSMLDAIrRAVMVSN 315
Cdd:PRK06380 236 SKLIAAHCVWATYHEIKLLSKNGVKVSWNSVSNFKLGTgGSPPIPEMLDNGINVTIGTDSNG--SNNSLDMF-EAMKFSA 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217382246 316 ILLINKVNEKSLT-LKEVFRLATLGGSQALGLDGeiGNFEVGKEFDAILINPKASdSPIDLFYGDFFGDIseaviqkfLY 394
Cdd:PRK06380 313 LSVKNERWDASIIkAQEILDFATINAAKALELNA--GSIEVGKLADLVILDARAP-NMIPTRKNNIVSNI--------VY 381
|
410
....*....|....*
gi 2217382246 395 LGDDRNIEEVYVGGK 409
Cdd:PRK06380 382 SLNPLNVDHVIVNGK 396
|
|
| PRK12393 |
PRK12393 |
amidohydrolase; Provisional |
2-412 |
2.61e-20 |
|
amidohydrolase; Provisional
Pssm-ID: 237088 [Multi-domain] Cd Length: 457 Bit Score: 92.82 E-value: 2.61e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217382246 2 PGLVDTHIHASQYSFAG--SSIDLPLLEWL--TKYTFPA---EHRFQnidfaeeVYTRVVTLELLMSvlvkktlffhkgg 74
Cdd:PRK12393 59 PGWVNTHHHLFQSLLKGvpAGINQSLTAWLaaVPYRFRArfdEDLFR-------LAARIGLVELLRS------------- 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217382246 75 nmeckqpsqghvannrqnrrtlknGTTTAC-----YFATIHTDSSLLLADITDKFGQRaFV---GKVCMDLNDTfPEYK- 145
Cdd:PRK12393 119 ------------------------GCTTVAdhhylYHPGMPFDTGDILFDEAEALGMR-FVlcrGGATQTRGDH-PGLPt 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217382246 146 ----ETTEESIKETERFVSEMLQKNYSRVKPIV----TPRFSLScsETLMGELGNIAKTRDLHIQSHISENRDEVEAVKN 217
Cdd:PRK12393 173 alrpETLDQMLADVERLVSRYHDASPDSLRRVVvaptTPTFSLP--PELLREVARAARGMGLRLHSHLSETVDYVDFCRE 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217382246 218 LYpsykNYTSVY--DKNNLLTNKTVMAHGCYLSAEELNVFHERGASIAHCPNSNLSLSSGFLNVLEVLKHEVKIGLGTD- 294
Cdd:PRK12393 251 KY----GMTPVQfvAEHDWLGPDVWFAHLVKLDAEEIALLAQTGTGIAHCPQSNGRLGSGIAPALAMEAAGVPVSLGVDg 326
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217382246 295 VAGGYSYSMLDAIRRAVMVSNILlinkVNEKSLTLKEVFRLATLGGSQALGLDgEIGNFEVGKEFDAILINpkaSDSPid 374
Cdd:PRK12393 327 AASNESADMLSEAHAAWLLHRAE----GGADATTVEDVVHWGTAGGARVLGLD-AIGTLAVGQAADLAIYD---LDDP-- 396
|
410 420 430
....*....|....*....|....*....|....*...
gi 2217382246 375 LFYGdfFGDISEAVIQKflylGDDRNIEEVYVGGKQVV 412
Cdd:PRK12393 397 RFFG--LHDPAIAPVAC----GGPAPVKALLVNGRPVV 428
|
|
| PRK08418 |
PRK08418 |
metal-dependent hydrolase; |
192-412 |
1.74e-19 |
|
metal-dependent hydrolase;
Pssm-ID: 181419 [Multi-domain] Cd Length: 408 Bit Score: 90.03 E-value: 1.74e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217382246 192 NIAKTRDLHIQSHISENRDEVEAVKNLYPSYKNY--------TSVYDKNNLL----TNKTVMAHGCYLSAEELNVFHERG 259
Cdd:PRK08418 197 QLAKKENLLVSTHFLESKAEREWLEESKGWFKKFfekflkepKPLYTPKEFLelfkGLRTLFTHCVYASEEELEKIKSKN 276
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217382246 260 ASIAHCPNSNLSLSSGFLNVLEVLKHEVKIGLGTD-VAGGYSYSMLDAIRRAVMVSNillinkvNEKSLTL-KEVFRLAT 337
Cdd:PRK08418 277 ASITHCPFSNRLLSNKALDLEKAKKAGINYSIATDgLSSNISLSLLDELRAALLTHA-------NMPLLELaKILLLSAT 349
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2217382246 338 LGGSQALGLD-GEIgnfEVGKEFDAILINpkasdspidlfYGDFFGDISEAVIQKFLYlgdDRNIEEVYVGGKQVV 412
Cdd:PRK08418 350 RYGAKALGLNnGEI---KEGKDADLSVFE-----------LPEECTKKEQLPLQFILH---AKEVKKLFIGGKEVK 408
|
|
| PRK08204 |
PRK08204 |
hypothetical protein; Provisional |
173-409 |
7.21e-19 |
|
hypothetical protein; Provisional
Pssm-ID: 181288 [Multi-domain] Cd Length: 449 Bit Score: 88.52 E-value: 7.21e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217382246 173 IVTPRFSlsCSETLMGELGnIAKTRDLHIQSHISenrdeveavknLYPSYKNYTSV--YDKNNLLTNKTVMAHGCYLSAE 250
Cdd:PRK08204 192 IRGPEFS--SWEVARADFR-LARELGLPISMHQG-----------FGPWGATPRGVeqLHDAGLLGPDLNLVHGNDLSDD 257
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217382246 251 ELNVFHERGASIAHCPNSNLSLSSGFLNVLEVLKHEVKIGLGTDVAGGYSYSMLDAIR------RAVMVSNILLINKV-- 322
Cdd:PRK08204 258 ELKLLADSGGSFSVTPEIEMMMGHGYPVTGRLLAHGVRPSLGVDVVTSTGGDMFTQMRfalqaeRARDNAVHLREGGMpp 337
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217382246 323 NEKSLTLKEVFRLATLGGSQALGLDGEIGNFEVGKEFDAILINPKAsdspIDLFYgdfFGDISEAVIQkflyLGDDRNIE 402
Cdd:PRK08204 338 PRLTLTARQVLEWATIEGARALGLEDRIGSLTPGKQADLVLIDATD----LNLAP---VHDPVGAVVQ----SAHPGNVD 406
|
....*..
gi 2217382246 403 EVYVGGK 409
Cdd:PRK08204 407 SVMVAGR 413
|
|
| Met_dep_hydrolase_D |
cd01312 |
Metallo-dependent hydrolases, subgroup D is part of the superfamily of metallo-dependent ... |
93-360 |
1.59e-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: 1.59e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217382246 93 RRTLKNGTTTAcyfATIHTDSSLLLADITDKFGQRAFVGKVCMDlNDTFPEYKETTEESIKETERFVSemlqknySRVKP 172
Cdd:cd01312 82 RQMLESGTTSI---GAISSDGSLLPALASSGLRGVFFNEVIGSN-PSAIDFKGETFLERFKRSKSFES-------QLFIP 150
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217382246 173 IVTPRFSLSCSETLMGELGNIAKTRDLHIQSHISENRDEVEAV-------KNLYPSY---KNYTSVYDKNNL------LT 236
Cdd:cd01312 151 AISPHAPYSVHPELAQDLIDLAKKLNLPLSTHFLESKEEREWLeeskgwfKHFWESFlklPKPKKLATAIDFldmlggLG 230
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217382246 237 NKTVMAHGCYLSAEELNVFHERGASIAHCPNSNLSLSSGFLNVLEVLKHEVKIGLGTD-VAGGYSYSMLDAIRravmvSN 315
Cdd:cd01312 231 TRVSFVHCVYANLEEAEILASRGASIALCPRSNRLLNGGKLDVSELKKAGIPVSLGTDgLSSNISLSLLDELR-----AL 305
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 2217382246 316 ILLINKVNEKSLTlKEVFRLATLGGSQALGLdgEIGNFEVGKEFD 360
Cdd:cd01312 306 LDLHPEEDLLELA-SELLLMATLGGARALGL--NNGEIEAGKRAD 347
|
|
| PRK07203 |
PRK07203 |
putative aminohydrolase SsnA; |
1-317 |
1.66e-16 |
|
putative aminohydrolase SsnA;
Pssm-ID: 235963 [Multi-domain] Cd Length: 442 Bit Score: 81.14 E-value: 1.66e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217382246 1 MPGLVDTHIHAsqYS-FA-GSSIDLP----LLEWLTKYTFpaehrfqNIDfaeevytRVVTLE-LLMSVLVkkTLffhkg 73
Cdd:PRK07203 58 MPGLINSHNHI--YSgLArGMMANIPpppdFISILKNLWW-------RLD-------RALTLEdVYYSALI--CS----- 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217382246 74 gnMECkqpsqghvannrqnrrtLKNGTTT-----ACYFATihTDSSLLLADITDKFGQRafvGKVCMDLNDTFPEykETT 148
Cdd:PRK07203 115 --LEA-----------------IKNGVTTvfdhhASPNYI--GGSLFTIADAAKKVGLR---AMLCYETSDRDGE--KEL 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217382246 149 EESIKETERFVSEMLQKNYSRVKPIVTPRFSLSCS-ETL------MGELGniaktRDLHIqsHISENRDEVEAVKNLYps 221
Cdd:PRK07203 169 QEGVEENIRFIKHIDEAKDDMVEAMFGLHASFTLSdATLekcreaVKETG-----RGYHI--HVAEGIYDVSDSHKKY-- 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217382246 222 YKNYTSVYDKNNLLTNKTVMAHGCYLSAEELNVFHERGASIAHCPNSNLSLSSGFLNVLEVLKHEVKIGLGTDvagGYSY 301
Cdd:PRK07203 240 GKDIVERLADFGLLGEKTLAAHCIYLSDEEIDLLKETDTFVVHNPESNMGNAVGYNPVLEMIKNGILLGLGTD---GYTS 316
|
330
....*....|....*.
gi 2217382246 302 SMLDAIRravmVSNIL 317
Cdd:PRK07203 317 DMFESYK----VANFK 328
|
|
| metallo-dependent_hydrolases |
cd01292 |
Superfamily of metallo-dependent hydrolases (also called amidohydrolase superfamily) is a ... |
93-343 |
9.24e-15 |
|
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: 9.24e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217382246 93 RRTLKNGTTTAC-----YFATIHTDSSLLLAD-ITDKFGQRAFVGKVCMDLNdtfPEYKETTEESIKETERFVsemlqkn 166
Cdd:cd01292 42 EALLAGGVTTVVdmgstPPPTTTKAAIEAVAEaARASAGIRVVLGLGIPGVP---AAVDEDAEALLLELLRRG------- 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217382246 167 YSRVKPIVTPRFSLSCSETLMGELGNI---AKTRDLHIQSHISENRDEVEAVKNLYpsyknytsvydKNNLLTNKTVMAH 243
Cdd:cd01292 112 LELGAVGLKLAGPYTATGLSDESLRRVleeARKLGLPVVIHAGELPDPTRALEDLV-----------ALLRLGGRVVIGH 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217382246 244 GCYLSAEELNVFHERGASIAHCPNSNLSLSS---GFLNVLEVLKHEVKIGLGTDVAGGYSYSMLDAIRRAVMVSNILLin 320
Cdd:cd01292 181 VSHLDPELLELLKEAGVSLEVCPLSNYLLGRdgeGAEALRRLLELGIRVTLGTDGPPHPLGTDLLALLRLLLKVLRLG-- 258
|
250 260
....*....|....*....|...
gi 2217382246 321 kvneksLTLKEVFRLATLGGSQA 343
Cdd:cd01292 259 ------LSLEEALRLATINPARA 275
|
|
| PRK06151 |
PRK06151 |
N-ethylammeline chlorohydrolase; Provisional |
152-412 |
2.52e-13 |
|
N-ethylammeline chlorohydrolase; Provisional
Pssm-ID: 180428 [Multi-domain] Cd Length: 488 Bit Score: 71.61 E-value: 2.52e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217382246 152 IKETERFVSEMLQKNYSRVKPIVTPRFSLSCSETLMGELGNIAKTRDLHIQSHISENRDEVEAVKNLYpsykNYTS--VY 229
Cdd:PRK06151 188 LEEAIAFIKRVDGAHNGLVRGMLAPDRIETCTVDLLRRTAAAARELGCPVRLHCAQGVLEVETVRRLH----GTTPleWL 263
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217382246 230 DKNNLLTNKTVMAHGCYLS---------AEELNVFHERGASIAHCPnSNLSLSSGFLNVLEVLKHE-VKIGLGTDVAggy 299
Cdd:PRK06151 264 ADVGLLGPRLLIPHATYISgsprlnysgGDDLALLAEHGVSIVHCP-LVSARHGSALNSFDRYREAgINLALGTDTF--- 339
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217382246 300 sysmldairRAVMVSNI---LLINKVNEKSLT---LKEVFRLATLGGSQALGLDgEIGNFEVGKEFDAILINPKasdspi 373
Cdd:PRK06151 340 ---------PPDMVMNMrvgLILGRVVEGDLDaasAADLFDAATLGGARALGRD-DLGRLAPGAKADIVVFDLD------ 403
|
250 260 270
....*....|....*....|....*....|....*....
gi 2217382246 374 DLFYGDFFGDISEAVIQkflylGDDRNIEEVYVGGKQVV 412
Cdd:PRK06151 404 GLHMGPVFDPIRTLVTG-----GSGRDVRAVFVDGRVVM 437
|
|
| archeal_chlorohydrolases |
cd01305 |
Predicted chlorohydrolases. These metallo-dependent hydrolases from archea are part of the ... |
193-341 |
5.37e-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: 62.80 E-value: 5.37e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217382246 193 IAKTRDLHIQSHISENRD-----EVEAVKNLYPsyknytsvydknNLLTnktvmaHGCYLSAEELNVFHERGASIAHCPN 267
Cdd:cd01305 133 LLRRRGKLFAIHASETREsvgmtDIERALDLEP------------DLLV------HGTHLTDEDLELVRENGVPVVLCPR 194
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2217382246 268 SNLSLSSGFLNVLEVLKHEVKIGLGTDVAGGYSYSMLDAIRRAVMVSNILlinkvneKSLTLKEVFRLATLGGS 341
Cdd:cd01305 195 SNLYFGVGIPPVAELLKLGIKVLLGTDNVMVNEPDMWAEMEFLAKYSRLQ-------GYLSPLEILRMATVNAA 261
|
|
| PRK07213 |
PRK07213 |
chlorohydrolase; Provisional |
204-368 |
1.25e-10 |
|
chlorohydrolase; Provisional
Pssm-ID: 235969 [Multi-domain] Cd Length: 375 Bit Score: 62.75 E-value: 1.25e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217382246 204 HISENRDEVEAVKNLYpsykNYTSVYDKNNLLTNKTVMAHGCYLSAEELNVFHERGASIAHCPNSNLSLSSGFLNVLEVL 283
Cdd:PRK07213 198 HAAEHKGSVEYSLEKY----GMTEIERLINLGFKPDFIVHATHPSNDDLELLKENNIPVVVCPRANASFNVGLPPLNEML 273
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217382246 284 KHEVKIGLGTDVAGGYSYSM---LDAIRRAVmvsnillinkvnekSLTLKEVFRLATLGGSQALGLDgEIGNFEVGKEFD 360
Cdd:PRK07213 274 EKGILLGIGTDNFMANSPSIfreMEFIYKLY--------------HIEPKEILKMATINGAKILGLI-NVGLIEEGFKAD 338
|
....*...
gi 2217382246 361 AILINPKA 368
Cdd:PRK07213 339 FTFIKPTN 346
|
|
| Met_dep_hydrolase_E |
cd01313 |
Metallo-dependent hydrolases, subgroup D is part of the superfamily of metallo-dependent ... |
199-409 |
4.57e-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: 4.57e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217382246 199 LHIqsHISENRDEVEAVknLYPSYKNYTSVYDKNNLLTNKTVMAHGCYLSAEELNVFHERGASIAHCPNSNLSLSSGFLN 278
Cdd:cd01313 222 VHI--HLAEQPKEVDDC--LAAHGRRPVELLLDHGHLDARWCLVHATHLTDNETLLLGRSGAVVGLCPTTEANLGDGIFP 297
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217382246 279 VLEVLKHEVKIGLGTDVAGG-----------YSYSMLDAiRRAVMVSnillinkvnEKSLTLKEVFRLATLGGSQALGLD 347
Cdd:cd01313 298 AAALLAAGGRIGIGSDSNARidlleelrqleYSQRLRDR-ARNVLAT---------AGGSSARALLDAALAGGAQALGLA 367
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2217382246 348 geIGNFEVGKEFDAILInpkASDSPidlfygDFFGDISEAVIQKFLYLGDDRNIEEVYVGGK 409
Cdd:cd01313 368 --TGALEAGARADLLSL---DLDHP------SLAGALPDTLLDAWVFAAGDREVRDVVVGGR 418
|
|
| HutI |
COG1228 |
Imidazolonepropionase or related amidohydrolase [Secondary metabolites biosynthesis, transport ... |
239-412 |
3.16e-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: 3.16e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217382246 239 TVMAHGCYLSAEELNVFHERGASIAhCPNSNLSLSSGFL------------------NVLEVLKHEVKIGLGTDVAGGYS 300
Cdd:COG1228 227 DSIEHGTYLDDEVADLLAEAGTVVL-VPTLSLFLALLEGaaapvaakarkvreaalaNARRLHDAGVPVALGTDAGVGVP 305
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217382246 301 --YSMLDAIRRAVMVSnillinkvneksLTLKEVFRLATLGGSQALGLDGEIGNFEVGKEFDAILINpkasdspidlfyG 378
Cdd:COG1228 306 pgRSLHRELALAVEAG------------LTPEEALRAATINAAKALGLDDDVGSLEPGKLADLVLLD------------G 361
|
170 180 190
....*....|....*....|....*....|....
gi 2217382246 379 DFFGDISeaviqkflYLgddRNIEEVYVGGKQVV 412
Cdd:COG1228 362 DPLEDIA--------YL---EDVRAVMKDGRVVD 384
|
|
| Amidohydro_3 |
pfam07969 |
Amidohydrolase family; |
241-412 |
1.42e-05 |
|
Amidohydrolase family;
Pssm-ID: 400360 [Multi-domain] Cd Length: 464 Bit Score: 47.14 E-value: 1.42e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217382246 241 MAHGC---YLSAEELNVFHERGASIAHCPNSNLSLS------------SGFLNVLEVLKHEVKIGLGTDVAGGySYSMLD 305
Cdd:pfam07969 298 IEHAQgvvPYTYSQIERVAALGGAAGVQPVFDPLWGdwlqdrlgaeraRGLTPVKELLNAGVKVALGSDAPVG-PFDPWP 376
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217382246 306 AIRRAVM-----VSNILLInkvnEKSLTLKEVFRLATLGGSQALGLDGEIGNFEVGKEFDAILINpkasdspIDLFygdf 380
Cdd:pfam07969 377 RIGAAVMrqtagGGEVLGP----DEELSLEEALALYTSGPAKALGLEDRKGTLGVGKDADLVVLD-------DDPL---- 441
|
170 180 190
....*....|....*....|....*....|..
gi 2217382246 381 fgDISEAVIqkflylgDDRNIEEVYVGGKQVV 412
Cdd:pfam07969 442 --TVDPPAI-------ADIRVRLTVVDGRVVY 464
|
|
| PRK09229 |
PRK09229 |
N-formimino-L-glutamate deiminase; Validated |
199-412 |
6.53e-05 |
|
N-formimino-L-glutamate deiminase; Validated
Pssm-ID: 236420 [Multi-domain] Cd Length: 456 Bit Score: 44.84 E-value: 6.53e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217382246 199 LHIqsHISENRDEVEAVKNLY---PsyknyTSVYDKNNLLTNKTVMAHGCYLSAEELNVFHERGASIAHCPNSNLSLSSG 275
Cdd:PRK09229 231 VHI--HIAEQTKEVDDCLAWSgarP-----VEWLLDHAPVDARWCLVHATHLTDAETARLARSGAVAGLCPTTEANLGDG 303
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217382246 276 FLNVLEVLKHEVKIGLGTDvaggySYSMLDAI---------------RRAVMVSNillinkvnEKSLTLKEVFRLATLGG 340
Cdd:PRK09229 304 IFPAVDYLAAGGRFGIGSD-----SHVSIDLVeelrlleygqrlrdrRRNVLAAA--------AQPSVGRRLFDAALAGG 370
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2217382246 341 SQALGLDgeIGNFEVGKEFDAILINPkasDSPidlfygDFFGDISEAVIQKFLYLGDDRNIEEVYVGGKQVV 412
Cdd:PRK09229 371 AQALGRA--IGGLAVGARADLVVLDL---DHP------ALAGREGDALLDRWVFAGGDAAVRDVWVAGRWVV 431
|
|
| Imidazolone-5PH |
cd01296 |
Imidazolonepropionase/imidazolone-5-propionate hydrolase (Imidazolone-5PH) catalyzes the third ... |
241-391 |
9.51e-05 |
|
Imidazolonepropionase/imidazolone-5-propionate hydrolase (Imidazolone-5PH) catalyzes the third step in the histidine degradation pathway, the hydrolysis of (S)-3-(5-oxo-4,5-dihydro-3H-imidazol-4-yl)propanoate to N-formimidoyl-L-glutamate. In bacteria, the enzyme is part of histidine utilization (hut) operon.
Pssm-ID: 238621 [Multi-domain] Cd Length: 371 Bit Score: 44.17 E-value: 9.51e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217382246 241 MAHGCYLSAEELNVFHERGASIAHCPNSNLSLSSGFLNVLEVLKHEVKIGLGTDVAGGySY---SMLDAIRRAVmvsnIL 317
Cdd:cd01296 233 ADHLEHTSDEGIAALAEAGTVAVLLPGTAFSLRETYPPARKLIDAGVPVALGTDFNPG-SSptsSMPLVMHLAC----RL 307
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2217382246 318 LinkvnekSLTLKEVFRLATLGGSQALGLDGEIGNFEVGKEFDAILINpkaSDSPIDLFYgdFFG-DISEAVIQK 391
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 ... |
270-365 |
1.69e-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: 1.69e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217382246 270 LSLSSGFLNVLEVLKHEVKIGLGTD-----VAGGYSYSMLdairrAVMVsnillinkvnEKSLTLKEVFRLATLGGSQAL 344
Cdd:cd01299 247 LVLEAGRDALRRAHKAGVKIAFGTDagfpvPPHGWNAREL-----ELLV----------KAGGTPAEALRAATANAAELL 311
|
90 100
....*....|....*....|.
gi 2217382246 345 GLDGEIGNFEVGKEFDAILIN 365
Cdd:cd01299 312 GLSDELGVIEAGKLADLLVVD 332
|
|
| nagA |
PRK11170 |
N-acetylglucosamine-6-phosphate deacetylase; Provisional |
297-357 |
9.51e-03 |
|
N-acetylglucosamine-6-phosphate deacetylase; Provisional
Pssm-ID: 183010 Cd Length: 382 Bit Score: 38.03 E-value: 9.51e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2217382246 297 GGYSYSMLDAIRravmvsnilliNKVNEKSLTLKEVFRLATLGGSQALGLDGEIGNFEVGK 357
Cdd:PRK11170 307 SGSALTMIEAVR-----------NLVEHVGIALDEALRMATLYPARAIGVDKRLGSIEAGK 356
|
|
| |
