|
Name |
Accession |
Description |
Interval |
E-value |
| GDEase |
cd01303 |
Guanine deaminase (GDEase). Guanine deaminase is an aminohydrolase responsible for the ... |
2-402 |
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: 578.08 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006403 2 FLEESSQQEKLAKEW--CFKPCEIRELSHHEFFMPGLVDTHIHAPQYAFAGSNVDLPLLEWLNKYTFPTEQRFRSTDVAE 79
Cdd:cd01303 31 VVDGNIIAAGAAETLkrAAKPGARVIDSPNQFILPGFIDTHIHAPQYANIGSGLGEPLLDWLETYTFPEEAKFADPAYAR 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006403 80 EVYTRVVRRTLKNGTTTACYFGTIHTDSSLILAEITDKFGQRAFVGKVCMDLNDtvPEYK-ETTEESVKETERFVSEMLQ 158
Cdd:cd01303 111 EVYGRFLDELLRNGTTTACYFATIHPESTEALFEEAAKRGQRAIAGKVCMDRNA--PEYYrDTAESSYRDTKRLIERWHG 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006403 159 KnYPRVKPIVTPRFTLSCTETLMSELGNIAKTH-DLYIQSHISENREEIEAVKSLYPSYKNYTDVYDKNNLLTNKTVMAH 237
Cdd:cd01303 189 K-SGRVKPAITPRFAPSCSEELLAALGKLAKEHpDLHIQTHISENLDEIAWVKELFPGARDYLDVYDKYGLLTEKTVLAH 267
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006403 238 GCYLSEEELNIFSERGASIAHCPNSNLSLSSGLLNVLEVLKHKVKIGLGTDVAGGYSYSMLDAIRRAVMVSNVLLINKVN 317
Cdd:cd01303 268 CVHLSEEEFNLLKERGASVAHCPTSNLFLGSGLFDVRKLLDAGIKVGLGTDVGGGTSFSMLDTLRQAYKVSRLLGYELGG 347
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006403 318 EKNLTLKEVFRLATLGGSQALGLDSEIGNFEVGKEFDALLINPRASDSPIDLfygDFVGDISEAVIQKFLYLGDDRNIEE 397
Cdd:cd01303 348 HAKLSPAEAFYLATLGGAEALGLDDKIGNFEVGKEFDAVVIDPSATPLLADR---MFRVESLEEALFKFLYLGDDRNIRE 424
|
....*
gi 569006403 398 VYVGG 402
Cdd:cd01303 425 VYVAG 429
|
|
| guan_deamin |
TIGR02967 |
guanine deaminase; This model describes guanine deaminase, which hydrolyzes guanine to ... |
14-402 |
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: 519.50 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006403 14 KEWCFKPCEIRELSHHeFFMPGLVDTHIHAPQYAFAGSnVDLPLLEWLNKYTFPTEQRFRSTDVAEEVYTRVVRRTLKNG 93
Cdd:TIGR02967 26 KETLPAGVEIDDYRGH-LIMPGFIDTHIHYPQTEMIAS-YGEQLLEWLEKYTFPTEARFADPDHAEEVAEFFLDELLRNG 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006403 94 TTTACYFGTIHTDSSLILAEITDKFGQRAFVGKVCMDLNdtVPEY-KETTEESVKETERFVSEMLQKNypRVKPIVTPRF 172
Cdd:TIGR02967 104 TTTALVFATVHPESVDALFEAALKRGMRMIAGKVLMDRN--APDYlRDTAESSYDESKALIERWHGKG--RLLYAVTPRF 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006403 173 TLSCTETLMSELGNIAKTH-DLYIQSHISENREEIEAVKSLYPSYKNYTDVYDKNNLLTNKTVMAHGCYLSEEELNIFSE 251
Cdd:TIGR02967 180 APTSSPEQLAAAGELAKEYpDVYVQTHLSENKDEIAWVKELFPEAKDYLDVYDHYGLLGRRSVFAHCIHLSDEECQRLAE 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006403 252 RGASIAHCPNSNLSLSSGLLNVLEVLKHKVKIGLGTDVAGGYSYSMLDAIRRAVMVSNVLlinkvnEKNLTLKEVFRLAT 331
Cdd:TIGR02967 260 TGAAIAHCPTSNLFLGSGLFNLKKALEHGVRVGLGTDVGGGTSFSMLQTLREAYKVSQLQ------GARLSPFEAFYLAT 333
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 569006403 332 LGGSQALGLDSEIGNFEVGKEFDALLINPRASDSPIDLFYGdfvGDISEAVIQKFLYLGDDRNIEEVYVGG 402
Cdd:TIGR02967 334 LGGARALDLDDRIGNFEPGKEADFVVLDPAATPLLALRFEG---ADTLEDKLFKLMYLGDDRNVAETYVAG 401
|
|
| SsnA |
COG0402 |
Cytosine/adenosine deaminase or related metal-dependent hydrolase [Nucleotide transport and ... |
22-406 |
8.18e-109 |
|
Cytosine/adenosine deaminase or related metal-dependent hydrolase [Nucleotide transport and metabolism, General function prediction only]; Cytosine/adenosine deaminase or related metal-dependent hydrolase is part of the Pathway/BioSystem: Pyrimidine salvage
Pssm-ID: 440171 [Multi-domain] Cd Length: 416 Bit Score: 326.40 E-value: 8.18e-109
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006403 22 EIRELSHHeFFMPGLVDTHIHAPQYAFAGSNVDLPLLEWLNKYTFPTEQRFrSTDVAEEVYTRVVRRTLKNGTTTACYFG 101
Cdd:COG0402 48 EVIDAGGK-LVLPGLVNTHTHLPQTLLRGLADDLPLLDWLEEYIWPLEARL-DPEDVYAGALLALAEMLRSGTTTVADFY 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006403 102 TIHTDSSLILAEITDKFGQRAFVGKVCMDLNdTVPEYKETTEESVKETERFVSEMLQKNYPRVKPIVTPRFTLSCTETLM 181
Cdd:COG0402 126 YVHPESADALAEAAAEAGIRAVLGRGLMDRG-FPDGLREDADEGLADSERLIERWHGAADGRIRVALAPHAPYTVSPELL 204
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006403 182 SELGNIAKTHDLYIQSHISENREEIEAVKSLYPsyKNYTDVYDKNNLLTNKTVMAHGCYLSEEELNIFSERGASIAHCPN 261
Cdd:COG0402 205 RAAAALARELGLPLHTHLAETRDEVEWVLELYG--KRPVEYLDELGLLGPRTLLAHCVHLTDEEIALLAETGASVAHCPT 282
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006403 262 SNLSLSSGLLNVLEVLKHKVKIGLGTDVAGG-YSYSMLDAIRRAvmvsnvLLINKVNEKN---LTLKEVFRLATLGGSQA 337
Cdd:COG0402 283 SNLKLGSGIAPVPRLLAAGVRVGLGTDGAASnNSLDMFEEMRLA------ALLQRLRGGDptaLSAREALEMATLGGARA 356
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006403 338 LGLDSEIGNFEVGKEFDALLINPRASD-SPIDlfygdfvgdiseAVIQKFLYLGDDRNIEEVYVGGKQVV 406
Cdd:COG0402 357 LGLDDEIGSLEPGKRADLVVLDLDAPHlAPLH------------DPLSALVYAADGRDVRTVWVAGRVVV 414
|
|
| PRK09228 |
PRK09228 |
guanine deaminase; Provisional |
22-405 |
2.58e-102 |
|
guanine deaminase; Provisional
Pssm-ID: 236419 [Multi-domain] Cd Length: 433 Bit Score: 310.20 E-value: 2.58e-102
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006403 22 EIRELSHHeFFMPGLVDTHIHAPQYAFAGSNVDlPLLEWLNKYTFPTEQRFRSTDVAEEVYTRVVRRTLKNGTTTACYFG 101
Cdd:PRK09228 59 EVTDYRGK-LILPGFIDTHIHYPQTDMIASYGE-QLLDWLNTYTFPEERRFADPAYAREVAEFFLDELLRNGTTTALVFG 136
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006403 102 TIHTDSSLILAEITDKFGQRAFVGKVCMDLNdtVPEY-KETTEESVKETERFVSEMLQKNypRVKPIVTPRFTLSCTETL 180
Cdd:PRK09228 137 TVHPQSVDALFEAAEARNMRMIAGKVLMDRN--APDGlRDTAESGYDDSKALIERWHGKG--RLLYAITPRFAPTSTPEQ 212
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006403 181 MSELGNIAKTH-DLYIQSHISENREEIEAVKSLYPSYKNYTDVYDKNNLLTNKTVMAHGCYLSEEELNIFSERGASIAHC 259
Cdd:PRK09228 213 LEAAGALAREHpDVWIQTHLSENLDEIAWVKELFPEARDYLDVYERYGLLGPRAVFAHCIHLEDRERRRLAETGAAIAFC 292
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006403 260 PNSNLSLSSGLLNVLEVLKHKVKIGLGTDVAGGYSYSMLDAIRRAVMVSnvllinKVNEKNLTLKEVFRLATLGGSQALG 339
Cdd:PRK09228 293 PTSNLFLGSGLFDLKRADAAGVRVGLGTDVGGGTSFSMLQTMNEAYKVQ------QLQGYRLSPFQAFYLATLGGARALG 366
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 569006403 340 LDSEIGNFEVGKEFDALLINPRASdSPIDLFYgDFVGDISEAVIQKFLyLGDDRNIEEVYVGGKQV 405
Cdd:PRK09228 367 LDDRIGNLAPGKEADFVVLDPAAT-PLLALRT-ARAESLEELLFALMT-LGDDRAVAETYVAGRPV 429
|
|
| ATZ_TRZ_like |
cd01298 |
TRZ/ATZ family contains enzymes from the atrazine degradation pathway and related hydrolases. ... |
33-406 |
3.68e-64 |
|
TRZ/ATZ family contains enzymes from the atrazine degradation pathway and related hydrolases. Atrazine, a chlorinated herbizide, can be catabolized by a variety of different bacteria. The first three steps of the atrazine dehalogenation pathway are catalyzed by atrazine chlorohydrolase (AtzA), hydroxyatrazine ethylaminohydrolase (AtzB), and N-isopropylammelide N-isopropylaminohydrolase (AtzC). All three enzymes belong to the superfamily of metal dependent hydrolases. AtzA and AtzB, beside other related enzymes are represented in this CD.
Pssm-ID: 238623 [Multi-domain] Cd Length: 411 Bit Score: 211.29 E-value: 3.68e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006403 33 MPGLVDTHIHAPQYAFAGSNVDLPLLEWLNKYTFPTEQRFRstdvAEEVY--TRV-VRRTLKNGTTTACYFGTIHTDssl 109
Cdd:cd01298 55 MPGLVNTHTHLAMTLLRGLADDLPLMEWLKDLIWPLERLLT----EEDVYlgALLaLAEMIRSGTTTFADMYFFYPD--- 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006403 110 ILAEITDKFGQRAFVGKVCMDLNDTVPEykeTTEESVKETERFVSEMLQKNYPRVKPIVTPRFTLSCTETLMSELGNIAK 189
Cdd:cd01298 128 AVAEAAEELGIRAVLGRGIMDLGTEDVE---ETEEALAEAERLIREWHGAADGRIRVALAPHAPYTCSDELLREVAELAR 204
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006403 190 THDLYIQSHISENREEIEAVKSLY---PsyknyTDVYDKNNLLTNKTVMAHGCYLSEEELNIFSERGASIAHCPNSNLSL 266
Cdd:cd01298 205 EYGVPLHIHLAETEDEVEESLEKYgkrP-----VEYLEELGLLGPDVVLAHCVWLTDEEIELLAETGTGVAHNPASNMKL 279
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006403 267 SSGLLNVLEVLKHKVKIGLGTD-VAGGYSYSMLDAIRRAvmvsnvLLINKV---NEKNLTLKEVFRLATLGGSQALGLDs 342
Cdd:cd01298 280 ASGIAPVPEMLEAGVNVGLGTDgAASNNNLDMFEEMRLA------ALLQKLahgDPTALPAEEALEMATIGGAKALGLD- 352
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 569006403 343 EIGNFEVGKEFDALLINPRASD-SPIDlfygdfvGDISEAViqkflYLGDDRNIEEVYVGGKQVV 406
Cdd:cd01298 353 EIGSLEVGKKADLILIDLDGPHlLPVH-------DPISHLV-----YSANGGDVDTVIVNGRVVM 405
|
|
| PRK07228 |
PRK07228 |
5'-deoxyadenosine deaminase; |
33-359 |
4.05e-57 |
|
5'-deoxyadenosine deaminase;
Pssm-ID: 180895 [Multi-domain] Cd Length: 445 Bit Score: 193.68 E-value: 4.05e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006403 33 MPGLVDTHIHAPQYAFAGSNVDLPLLEWLNKYTFPTEQrfrSTDvAEEVYTRV---VRRTLKNGTTTACYFGTI-HTDSS 108
Cdd:PRK07228 55 IPGLIQGHIHLCQTLFRGIADDLELLDWLKDRIWPLEA---AHD-AESMYYSAllgIGELIESGTTTIVDMESVhHTDSA 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006403 109 LilaEITDKFGQRAFVGKVCMDLNDTVPE-YKETTEESVKETERFVSEMLQKNYPRVKPIVTPRFTLSCTETLMSELGNI 187
Cdd:PRK07228 131 F---EAAGESGIRAVLGKVMMDYGDDVPEgLQEDTEASLAESVRLLEKWHGADNGRIRYAFTPRFAVSCTEELLRGVRDL 207
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006403 188 AKTHDLYIQSHISENREEIEAVKSlYPSYKNYTdVYDKNNLLTNKTVMAHGCYLSEEELNIFSERGASIAHCPNSNLSLS 267
Cdd:PRK07228 208 ADEYGVRIHTHASENRGEIETVEE-ETGMRNIH-YLDEVGLTGEDLILAHCVWLDEEEREILAETGTHVTHCPSSNLKLA 285
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006403 268 SGLLNVLEVLKHKVKIGLGTDvaGGYSYSMLDA---IRRAVmvsnvlLINKVNEKN---LTLKEVFRLATLGGSQALGLD 341
Cdd:PRK07228 286 SGIAPVPDLLERGINVALGAD--GAPCNNTLDPfteMRQAA------LIQKVDRLGptaMPARTVFEMATLGGAKAAGFE 357
|
330
....*....|....*...
gi 569006403 342 SEIGNFEVGKEFDALLIN 359
Cdd:PRK07228 358 DEIGSLEEGKKADLAILD 375
|
|
| Amidohydro_1 |
pfam01979 |
Amidohydrolase family; This family of enzymes are a a large metal dependent hydrolase ... |
33-405 |
1.72e-53 |
|
Amidohydrolase family; This family of enzymes are a a large metal dependent hydrolase superfamily. The family includes Adenine deaminase EC:3.5.4.2 that hydrolyses adenine to form hypoxanthine and ammonia. Adenine deaminases reaction is important for adenine utilization as a purine and also as a nitrogen source. This family also includes dihydroorotase and N-acetylglucosamine-6-phosphate deacetylases, EC:3.5.1.25 These enzymes catalyze the reaction N-acetyl-D-glucosamine 6-phosphate + H2O <=> D-glucosamine 6-phosphate + acetate. This family includes the catalytic domain of urease alpha subunit. Dihydroorotases (EC:3.5.2.3) are also included.
Pssm-ID: 460401 [Multi-domain] Cd Length: 334 Bit Score: 181.16 E-value: 1.72e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006403 33 MPGLVDTHIHAPQYAFAGSNVDLpllewlnkytfpteqrfrstDVAEEVYTRVVRRTLKNGTTTACYFGTIHTDSSLILA 112
Cdd:pfam01979 3 LPGLIDAHVHLEMGLLRGIPVPP--------------------EFAYEALRLGITTMLKSGTTTVLDMGATTSTGIEALL 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006403 113 EITDK--FGQRAFVGKVCMDLNDTVPEYKETTEESVKETErfvsEMLQKNYPRVKPIVTPRFTLSCTETLMSELGNIAKT 190
Cdd:pfam01979 63 EAAEElpLGLRFLGPGCSLDTDGELEGRKALREKLKAGAE----FIKGMADGVVFVGLAPHGAPTFSDDELKAALEEAKK 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006403 191 HDLYIQSHISENREEIEAVKSLYPS---YKNYTDVYDKNNLL-TNKTVMAHGCYLSEEELNIFSER--GASIAHCPNSNL 264
Cdd:pfam01979 139 YGLPVAIHALETKGEVEDAIAAFGGgieHGTHLEVAESGGLLdIIKLILAHGVHLSPTEANLLAEHlkGAGVAHCPFSNS 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006403 265 SLSSGLLNVLEVLKHKVKIGLGTDVAG-GYSYSMLDAIRRAVmvsnvlLINKVNEKNLTLKEVFRLATLGGSQALGLDSE 343
Cdd:pfam01979 219 KLRSGRIALRKALEDGVKVGLGTDGAGsGNSLNMLEELRLAL------ELQFDPEGGLSPLEALRMATINPAKALGLDDK 292
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 569006403 344 IGNFEVGKEFDALLINPRasdspidlfygdfvgdiseaVIQKFLYLGDDRNIEEVYVGGKQV 405
Cdd:pfam01979 293 VGSIEVGKDADLVVVDLD--------------------PLAAFFGLKPDGNVKKVIVKGKIV 334
|
|
| PRK08393 |
PRK08393 |
N-ethylammeline chlorohydrolase; Provisional |
29-344 |
1.26e-46 |
|
N-ethylammeline chlorohydrolase; Provisional
Pssm-ID: 181411 [Multi-domain] Cd Length: 424 Bit Score: 165.36 E-value: 1.26e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006403 29 HEFFMPGLVDTHIHAPQYAFAGSNVDLPLLEWLNKYTFPTEQRFRSTDVAEEVYTRVVRrTLKNGTTT--ACYFgtiHTD 106
Cdd:PRK08393 49 GSVVSPGFINAHTHSPMVLLRGLADDVPLMEWLQNYIWPRERKLKRKDIYWGAYLGLLE-MIKSGTTTfvDMYF---HME 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006403 107 SsliLAEITDKFGQRAFVGKVCMDLNDtvpeyKETTEESVKETERFVSEMLQKNYPRVKPIVTPRFTLSCTETLMSELGN 186
Cdd:PRK08393 125 E---VAKATLEVGLRGYLSYGMVDLGD-----EEKREKEIKETEKLMEFIEKLNSPRVHFVFGPHAPYTCSLALLKWVRE 196
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006403 187 IAKTHDLYIQSHISENREEIEAVKSLYPsyKNYTDVYDKNNLLTNKTVMAHGCYLSEEELNIFSERGASIAHCPNSNLSL 266
Cdd:PRK08393 197 KAREWNKLITIHLSETMDEIKQIREKYG--KSPVVLLDEIGFLNEDVIAAHGVWLSSRDIRILASAGVTVAHNPASNMKL 274
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006403 267 SSGLLNVLEVLKHKVKIGLGTDvaGGYSYSMLDAIRRAVMVSnvlLINKVNEKNLTL---KEVFRLATLGGSQALGLDSE 343
Cdd:PRK08393 275 GSGVMPLRKLLNAGVNVALGTD--GAASNNNLDMLREMKLAA---LLHKVHNLDPTIadaETVFRMATQNGAKALGLKAG 349
|
.
gi 569006403 344 I 344
Cdd:PRK08393 350 V 350
|
|
| PRK06038 |
PRK06038 |
N-ethylammeline chlorohydrolase; Provisional |
28-361 |
1.26e-38 |
|
N-ethylammeline chlorohydrolase; Provisional
Pssm-ID: 180363 [Multi-domain] Cd Length: 430 Bit Score: 144.12 E-value: 1.26e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006403 28 HHEFFMPGLVDTHIHAPQYAFAGSNVDLPLLEWLNKYTFPTEQRFRstdvAEEVYTRVVRRTL---KNGTTT--ACYFGT 102
Cdd:PRK06038 49 KGSVVMPGLVNTHTHAAMTLFRGYADDLPLAEWLNDHIWPAEAKLT----AEDVYAGSLLACLemiKSGTTSfaDMYFYM 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006403 103 IHTdsslilAEITDKFGQRAFVGKVCMDLNDTvpeykETTEESVKETERFVSEMLQKNYPRVKPIVTPRFTLSCTETLMS 182
Cdd:PRK06038 125 DEV------AKAVEESGLRAALSYGMIDLGDD-----EKGEAELKEGKRFVKEWHGAADGRIKVMYGPHAPYTCSEEFLS 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006403 183 ELGNIAKTHDLYIQSHISENREEIEAVKSLYPsyKNYTDVYDKNNLLTNKTVMAHGCYLSEEELNIFSERGASIAHCPNS 262
Cdd:PRK06038 194 KVKKLANKDGVGIHIHVLETEAELNQMKEQYG--MCSVNYLDDIGFLGPDVLAAHCVWLSDGDIEILRERGVNVSHNPVS 271
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006403 263 NLSLSSGLLNVLEVLKHKVKIGLGTD-VAGGYSYSMLDAIRRAVmvsnvlLINKVNEKNLTL---KEVFRLATLGGSQAL 338
Cdd:PRK06038 272 NMKLASGIAPVPKLLERGVNVSLGTDgCASNNNLDMFEEMKTAA------LLHKVNTMDPTAlpaRQVLEMATVNGAKAL 345
|
330 340
....*....|....*....|...
gi 569006403 339 GLDSeiGNFEVGKEFDALLINPR 361
Cdd:PRK06038 346 GINT--GMLKEGYLADIIIVDMN 366
|
|
| PRK06687 |
PRK06687 |
TRZ/ATZ family protein; |
31-406 |
1.23e-36 |
|
TRZ/ATZ family protein;
Pssm-ID: 180657 [Multi-domain] Cd Length: 419 Bit Score: 138.21 E-value: 1.23e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006403 31 FFMPGLVDTHIHAPQYAFAGSNVDLPLLEWLNKYTFPTEQRFrSTDVAEEVYTRVVRRTLKNGTTTacyFGTIHTDSSLI 110
Cdd:PRK06687 55 WIMPGLVNCHTHSAMTGLRGIRDDSNLHEWLNDYIWPAESEF-TPDMTTNAVKEALTEMLQSGTTT---FNDMYNPNGVD 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006403 111 LAEITDKFGQRafvGKVCMDLNDTVPEYKETTEESVKETERFVSEMLQKNYPRVKPIVTPRFTLSCTETLMSELGNIAKT 190
Cdd:PRK06687 131 IQQIYQVVKTS---KMRCYFSPTLFSSETETTAETISRTRSIIDEILKYKNPNFKVMVAPHSPYSCSRDLLEASLEMAKE 207
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006403 191 HDLYIQSHISENREEIEAVKSLYPsyKNYTDVYDKNNLLTNKTVMAHGCYLSEEELNIFSERGASIAHCPNSNLSLSSGL 270
Cdd:PRK06687 208 LNIPLHVHVAETKEESGIILKRYG--KRPLAFLEELGYLDHPSVFAHGVELNEREIERLASSQVAIAHNPISNLKLASGI 285
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006403 271 LNVLEVLKHKVKIGLGTD-VAGGYSYSMLDAIRRAVMVSNvllINKVNEKNLTLKEVFRLATLGGSQALGLDSEIGNFEV 349
Cdd:PRK06687 286 APIIQLQKAGVAVGIATDsVASNNNLDMFEEGRTAALLQK---MKSGDASQFPIETALKVLTIEGAKALGMENQIGSLEV 362
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*..
gi 569006403 350 GKEFDALLINPRASdspIDLFygdfvgdISEAVIQKFLYLGDDRNIEEVYVGGKQVV 406
Cdd:PRK06687 363 GKQADFLVIQPQGK---IHLQ-------PQENMLSHLVYAVKSSDVDDVYIAGEQVV 409
|
|
| PRK09045 |
PRK09045 |
TRZ/ATZ family hydrolase; |
18-354 |
2.95e-32 |
|
TRZ/ATZ family hydrolase;
Pssm-ID: 236366 [Multi-domain] Cd Length: 443 Bit Score: 126.56 E-value: 2.95e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006403 18 FKPCEIRELSHHeFFMPGLVDTHIHAPQYAFAGSNVDLPLLEWLNKYTFPTEQRFRSTD---------VAEevytrvvrr 88
Cdd:PRK09045 51 YAAAETVELPDH-VLIPGLINAHTHAAMSLLRGLADDLPLMTWLQDHIWPAEGAWVSEEfvrdgtllaIAE--------- 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006403 89 TLKNGTTTA--CYFgtiHTDsslILAEITDKFGQRAFVGKVCMDlndtVP-EYKETTEES----VKETERFvsemlqKNY 161
Cdd:PRK09045 121 MLRGGTTCFndMYF---FPE---AAAEAAHQAGMRAQIGMPVLD----FPtAWASDADEYlakgLELHDQW------RHH 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006403 162 PRVKPIVTPR--FTLScTETLmSELGNIAKTHDLYIQSHISENREEIEAvkslypSYKNY----TDVYDKNNLLTNKTVM 235
Cdd:PRK09045 185 PLISTAFAPHapYTVS-DENL-ERIRTLAEQLDLPIHIHLHETAQEIAD------SLKQHgqrpLARLARLGLLGPRLIA 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006403 236 AHGCYLSEEELNIFSERGASIAHCPNSNLSLSSGLLNVLEVLKHKVKIGLGTD-VAGGYSYSMLDAIRRAVMVSnvllin 314
Cdd:PRK09045 257 VHMTQLTDAEIALLAETGCSVVHCPESNLKLASGFCPVAKLLQAGVNVALGTDgAASNNDLDLFGEMRTAALLA------ 330
|
330 340 350 360
....*....|....*....|....*....|....*....|....*..
gi 569006403 315 kvneKNLTL-------KEVFRLATLGGSQALGLDSEIGNFEVGKEFD 354
Cdd:PRK09045 331 ----KAVAGdatalpaHTALRMATLNGARALGLDDEIGSLEPGKQAD 373
|
|
| PRK15493 |
PRK15493 |
bifunctional S-methyl-5'-thioadenosine deaminase/S-adenosylhomocysteine deaminase; |
30-406 |
1.10e-27 |
|
bifunctional S-methyl-5'-thioadenosine deaminase/S-adenosylhomocysteine deaminase;
Pssm-ID: 185390 [Multi-domain] Cd Length: 435 Bit Score: 113.61 E-value: 1.10e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006403 30 EFFMPGLVDTHIHAPQYAFAGSNVDLPLLEWLNKYTFPTEQRFrSTDVAEEVYTRVVRRTLKNGTTT-ACYFGTIHTDSS 108
Cdd:PRK15493 55 KWVLPGLVNTHTHVVMSLLRGIGDDMLLQPWLETRIWPLESQF-TPELAVASTELGLLEMVKSGTTSfSDMFNPIGVDQD 133
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006403 109 LILaEITDKFGQRAFVGKVCMDLNDtvpeyKETTEESVKETERFVSEMLQKNyPRVKPIVTPRFTLSCTETLMSELGNIA 188
Cdd:PRK15493 134 AIM-ETVSRSGMRAAVSRTLFSFGT-----KEDEKKAIEEAEKYVKRYYNES-GMLTTMVAPHSPYTCSTELLEECARIA 206
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006403 189 KTHDLYIQSHISENREEIEAVKSLYPsyKNYTDVYDKNNLLTNKTVMAHGCYLSEEELNIFSERGASIAHCPNSNLSLSS 268
Cdd:PRK15493 207 VENQTMVHIHLSETEREVRDIEAQYG--KRPVEYAASCGLFKRPTVIAHGVVLNDNERAFLAEHDVRVAHNPNSNLKLGS 284
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006403 269 GLLNVLEVLKHKVKIGLGTD-VAGGYSYSMLDAIRRAVMVSNVLlinKVNEKNLTLKEVFRLATLGGSQALGLdSEIGNF 347
Cdd:PRK15493 285 GIANVKAMLEAGIKVGIATDsVASNNNLDMFEEMRIATLLQKGI---HQDATALPVETALTLATKGAAEVIGM-KQTGSL 360
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*....
gi 569006403 348 EVGKEFDALLINPraSDSPidlfygdfVGDISEAVIQKFLYLGDDRNIEEVYVGGKQVV 406
Cdd:PRK15493 361 EVGKCADFITIDP--SNKP--------HLQPADEVLSHLVYAASGKDISDVIINGKRVV 409
|
|
| PRK06380 |
PRK06380 |
metal-dependent hydrolase; Provisional |
33-403 |
2.90e-24 |
|
metal-dependent hydrolase; Provisional
Pssm-ID: 180548 [Multi-domain] Cd Length: 418 Bit Score: 103.81 E-value: 2.90e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006403 33 MPGLVDTHIHAPQYAFAGSNVDLPLLEWLNKyTFpteqRFRSTDVAEEVYTRV---VRRTLKNGTTTacyFGTIHTDSSL 109
Cdd:PRK06380 53 MPGLINTHAHVGMTASKGLFDDVDLEEFLMK-TF----KYDSKRTREGIYNSAklgMYEMINSGITA---FVDLYYSEDI 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006403 110 IlAEITDKFGQRAFVGKVCMDlndtvPEYKETTEESVKETERFVSEMLQKNYprVKPIVTPRFTLSCTETLMSELGNIAK 189
Cdd:PRK06380 125 I-AKAAEELGIRAFLSWAVLD-----EEITTQKGDPLNNAENFIREHRNEEL--VTPSIGVQGIYVANDETYLKAKEIAE 196
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006403 190 THDLYIQSHISENREEIeavkslYPSYKNY----TDVYDKNNLLTNKTVMAHGCYLSEEELNIFSERGASIAHCPNSNLS 265
Cdd:PRK06380 197 KYDTIMHMHLSETRKEV------YDHVKRTgerpVEHLEKIGFLNSKLIAAHCVWATYHEIKLLSKNGVKVSWNSVSNFK 270
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006403 266 LSSGLLNVL-EVLKHKVKIGLGTDVAGG-YSYSMLDAIR-RAVMVSNvlliNKVNEKNLTLKEVFRLATLGGSQALGLDS 342
Cdd:PRK06380 271 LGTGGSPPIpEMLDNGINVTIGTDSNGSnNSLDMFEAMKfSALSVKN----ERWDASIIKAQEILDFATINAAKALELNA 346
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 569006403 343 eiGNFEVGKEFDALLINPRASdSPIDLFYGDFVGDIseaviqkfLYLGDDRNIEEVYVGGK 403
Cdd:PRK06380 347 --GSIEVGKLADLVILDARAP-NMIPTRKNNIVSNI--------VYSLNPLNVDHVIVNGK 396
|
|
| PRK08203 |
PRK08203 |
hydroxydechloroatrazine ethylaminohydrolase; Reviewed |
33-406 |
1.89e-19 |
|
hydroxydechloroatrazine ethylaminohydrolase; Reviewed
Pssm-ID: 236184 [Multi-domain] Cd Length: 451 Bit Score: 89.91 E-value: 1.89e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006403 33 MPGLVDTHIHAPQY---AFAGSnVDLPLLEWLnKYTFPTEQRFrsTDVAEEVYTRV-VRRTLKNGTTTAC---Y-FGTIH 104
Cdd:PRK08203 58 TPGLVNTHHHFYQTltrALPAA-QDAELFPWL-TTLYPVWARL--TPEMVRVATQTaLAELLLSGCTTSSdhhYlFPNGL 133
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006403 105 TDSSLILAEITDKFGQRAFVGKVCMDLN--------DTVpeyKETTEESVKETERFVSE--------MLQknyprvkpI- 167
Cdd:PRK08203 134 RDALDDQIEAAREIGMRFHATRGSMSLGesdgglppDSV---VEDEDAILADSQRLIDRyhdpgpgaMLR--------Ia 202
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006403 168 VTPRFTLSCTETLMSELGNIAKTHDLYIQSHISENREEIEAVKSLY---PsyknyTDVYDKNNLLTNKTVMAHGCYLSEE 244
Cdd:PRK08203 203 LAPCSPFSVSRELMRESAALARRLGVRLHTHLAETLDEEAFCLERFgmrP-----VDYLEDLGWLGPDVWLAHCVHLDDA 277
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006403 245 ELNIFSERGASIAHCPNSNLSLSSGLLNVLEVLKHKVKIGLGTD-VAGGYSYSMLDAIRRAvmvsnvLLINKV--NEKNL 321
Cdd:PRK08203 278 EIARLARTGTGVAHCPCSNMRLASGIAPVRELRAAGVPVGLGVDgSASNDGSNLIGEARQA------LLLQRLryGPDAM 351
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006403 322 TLKEVFRLATLGGSQALGLDsEIGNFEVGKEFD-AL--LINPRASDSpidlfygdfvGDISEAviqkfLYLGDDRNIEEV 398
Cdd:PRK08203 352 TAREALEWATLGGARVLGRD-DIGSLAPGKLADlALfdLDELRFAGA----------HDPVAA-----LVLCGPPRADRV 415
|
....*...
gi 569006403 399 YVGGKQVV 406
Cdd:PRK08203 416 MVGGRWVV 423
|
|
| PRK08204 |
PRK08204 |
hypothetical protein; Provisional |
33-403 |
1.26e-18 |
|
hypothetical protein; Provisional
Pssm-ID: 181288 [Multi-domain] Cd Length: 449 Bit Score: 87.37 E-value: 1.26e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006403 33 MPGLVDTHIHAPQYAFAGSNVDLPLLEWLNKYTFPTEQRFRSTDVaeEVYTRV-VRRTLKNGTTTACYFGTI-----HTD 106
Cdd:PRK08204 56 MPGLVDTHRHTWQSVLRGIGADWTLQTYFREIHGNLGPMFRPEDV--YIANLLgALEALDAGVTTLLDWSHInnspeHAD 133
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006403 107 SSLI-LAEItdkfGQRA--FVGKVcmdlNDTVPEYKETTEESVKETERFVSEMLQKNYPRVK---PIVTPRFtlSCTETL 180
Cdd:PRK08204 134 AAIRgLAEA----GIRAvfAHGSP----GPSPYWPFDSVPHPREDIRRVKKRYFSSDDGLLTlglAIRGPEF--SSWEVA 203
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006403 181 MSELGnIAKTHDLYIQSHISenreeieavksLYPSYKNYTDV--YDKNNLLTNKTVMAHGCYLSEEELNIFSERGASIAH 258
Cdd:PRK08204 204 RADFR-LARELGLPISMHQG-----------FGPWGATPRGVeqLHDAGLLGPDLNLVHGNDLSDDELKLLADSGGSFSV 271
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006403 259 CPNSNLSLSSGLLNVLEVLKHKVKIGLGTDVAGGYSYSMLDAIR------RAVMVSNVLLINKV--NEKNLTLKEVFRLA 330
Cdd:PRK08204 272 TPEIEMMMGHGYPVTGRLLAHGVRPSLGVDVVTSTGGDMFTQMRfalqaeRARDNAVHLREGGMppPRLTLTARQVLEWA 351
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 569006403 331 TLGGSQALGLDSEIGNFEVGKEFDALLINPRAsdspIDLFYgdfVGDISEAVIQkflyLGDDRNIEEVYVGGK 403
Cdd:PRK08204 352 TIEGARALGLEDRIGSLTPGKQADLVLIDATD----LNLAP---VHDPVGAVVQ----SAHPGNVDSVMVAGR 413
|
|
| Met_dep_hydrolase_D |
cd01312 |
Metallo-dependent hydrolases, subgroup D is part of the superfamily of metallo-dependent ... |
29-354 |
1.13e-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: 84.04 E-value: 1.13e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006403 29 HEFF-----MPGLVDTHIHapqYAFAGSNVDL---PLLEWLNkyTFPTEQRFRSTDVAEEVYTRVVRRTLKNGTTTAcyf 100
Cdd:cd01312 21 HEFFpngvlLPGLINAHTH---LEFSANVAQFtygRFRAWLL--SVINSRDELLKQPWEEAIRQGIRQMLESGTTSI--- 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006403 101 GTIHTDssLILAEITDKFGQRAFVGKVCMDLNDTVPEYKETTEEsvketERFVSEMLQKNyPRVKPIVTPRFTLSCTETL 180
Cdd:cd01312 93 GAISSD--GSLLPALASSGLRGVFFNEVIGSNPSAIDFKGETFL-----ERFKRSKSFES-QLFIPAISPHAPYSVHPEL 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006403 181 MSELGNIAKTHDLYIQSHISENREEIEavksLYPSYKNYTDVYDKNNL--------------------LTNKTVMAHGCY 240
Cdd:cd01312 165 AQDLIDLAKKLNLPLSTHFLESKEERE----WLEESKGWFKHFWESFLklpkpkklataidfldmlggLGTRVSFVHCVY 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006403 241 LSEEELNIFSERGASIAHCPNSNLSLSSGLLNVLEVLKHKVKIGLGTD-VAGGYSYSMLDAIRravmvSNVLLINKVNEK 319
Cdd:cd01312 241 ANLEEAEILASRGASIALCPRSNRLLNGGKLDVSELKKAGIPVSLGTDgLSSNISLSLLDELR-----ALLDLHPEEDLL 315
|
330 340 350
....*....|....*....|....*....|....*
gi 569006403 320 NLTlKEVFRLATLGGSQALGLdsEIGNFEVGKEFD 354
Cdd:cd01312 316 ELA-SELLLMATLGGARALGL--NNGEIEAGKRAD 347
|
|
| metallo-dependent_hydrolases |
cd01292 |
Superfamily of metallo-dependent hydrolases (also called amidohydrolase superfamily) is a ... |
36-337 |
5.40e-17 |
|
Superfamily of metallo-dependent hydrolases (also called amidohydrolase superfamily) is a large group of proteins that show conservation in their 3-dimensional fold (TIM barrel) and in details of their active site. The vast majority of the members have a conserved metal binding site, involving four histidines and one aspartic acid residue. In the common reaction mechanism, the metal ion (or ions) deprotonate a water molecule for a nucleophilic attack on the substrate. The family includes urease alpha, adenosine deaminase, phosphotriesterase dihydroorotases, allantoinases, hydantoinases, AMP-, adenine and cytosine deaminases, imidazolonepropionase, aryldialkylphosphatase, chlorohydrolases, formylmethanofuran dehydrogenases and others.
Pssm-ID: 238617 [Multi-domain] Cd Length: 275 Bit Score: 80.46 E-value: 5.40e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006403 36 LVDTHIHAPQYAFAGSNVDLPLLEWLNKYTFPTEQRFRstdvaeevytRVVRRTLKNGTTTACYFGTIHTDS------SL 109
Cdd:cd01292 1 FIDTHVHLDGSALRGTRLNLELKEAEELSPEDLYEDTL----------RALEALLAGGVTTVVDMGSTPPPTttkaaiEA 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006403 110 ILAEITDKFGQRAFVGKVCMDlndtvpEYKETTEESVKETERFVSEMLQKNYPRVKPIVTPRFTLSCTETLMSELGnIAK 189
Cdd:cd01292 71 VAEAARASAGIRVVLGLGIPG------VPAAVDEDAEALLLELLRRGLELGAVGLKLAGPYTATGLSDESLRRVLE-EAR 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006403 190 THDLYIQSHISENREEIEAVKSLYpsyknytdvydKNNLLTNKTVMAHGCYLSEEELNIFSERGASIAHCPNSNLSLSSG 269
Cdd:cd01292 144 KLGLPVVIHAGELPDPTRALEDLV-----------ALLRLGGRVVIGHVSHLDPELLELLKEAGVSLEVCPLSNYLLGRD 212
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 569006403 270 LLN---VLEVLKHKVKIGLGTDVAGGYSYSMLDAIRRAVMVSNVLlinkvnekNLTLKEVFRLATLGGSQA 337
Cdd:cd01292 213 GEGaeaLRRLLELGIRVTLGTDGPPHPLGTDLLALLRLLLKVLRL--------GLSLEEALRLATINPARA 275
|
|
| PRK08418 |
PRK08418 |
metal-dependent hydrolase; |
33-406 |
1.36e-16 |
|
metal-dependent hydrolase;
Pssm-ID: 181419 [Multi-domain] Cd Length: 408 Bit Score: 80.78 E-value: 1.36e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006403 33 MPGLVDTHIHapqYAFAGSNVDL---PLLEWLNKYTFPTEQRFRSTDvaEEVYTRVVRRTLKNGTTTacyFGTIhtDSSL 109
Cdd:PRK08418 57 LPAFINPHTH---LEFSANKTTLdygDFIPWLGSVINHREDLLEKCK--GALIQQAINEMLKSGVGT---IGAI--SSFG 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006403 110 ILAEITDKFGQRA-FVGKVCMDLNDTVPEYKETTEESVKETERFVSEMLqknyprvKPIVTPRFTLSCTETLMSELGNIA 188
Cdd:PRK08418 127 IDLEICAKSPLRVvFFNEILGSNASAVDELYQDFLARFEESKKFKSKKF-------IPAIAIHSPYSVHPILAKKALQLA 199
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006403 189 KTHDLYIQSHISENREEIEAV-------KSLYPSY-KNYTDVYDKNNLL----TNKTVMAHGCYLSEEELNIFSERGASI 256
Cdd:PRK08418 200 KKENLLVSTHFLESKAEREWLeeskgwfKKFFEKFlKEPKPLYTPKEFLelfkGLRTLFTHCVYASEEELEKIKSKNASI 279
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006403 257 AHCPNSNLSLSSGLLNVLEVLKHKVKIGLGTD-VAGGYSYSMLDAIRRAVMVSNvllinkvNEKNLTL-KEVFRLATLGG 334
Cdd:PRK08418 280 THCPFSNRLLSNKALDLEKAKKAGINYSIATDgLSSNISLSLLDELRAALLTHA-------NMPLLELaKILLLSATRYG 352
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 569006403 335 SQALGLDSeiGNFEVGKEFDALLINprasdspidlfYGDFVGDISEAVIQKFLYlgdDRNIEEVYVGGKQVV 406
Cdd:PRK08418 353 AKALGLNN--GEIKEGKDADLSVFE-----------LPEECTKKEQLPLQFILH---AKEVKKLFIGGKEVK 408
|
|
| PRK12393 |
PRK12393 |
amidohydrolase; Provisional |
34-406 |
3.65e-14 |
|
amidohydrolase; Provisional
Pssm-ID: 237088 [Multi-domain] Cd Length: 457 Bit Score: 73.95 E-value: 3.65e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006403 34 PGLVDTHIHAPQYAFAG--SNVDLPLLEWLNKYTFP-----TEQRFRstdvaeeVYTRV-VRRTLKNGTTTAC-----YF 100
Cdd:PRK12393 59 PGWVNTHHHLFQSLLKGvpAGINQSLTAWLAAVPYRfrarfDEDLFR-------LAARIgLVELLRSGCTTVAdhhylYH 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006403 101 GTIHTDSSLILAEITDKFGQRaFVgkVC---------MDLNDTVPEYKETTEESVKETERFVSEMLQKNYPRVKPIV--- 168
Cdd:PRK12393 132 PGMPFDTGDILFDEAEALGMR-FV--LCrggatqtrgDHPGLPTALRPETLDQMLADVERLVSRYHDASPDSLRRVVvap 208
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006403 169 -TPRFTLscTETLMSELGNIAKTHDLYIQSHISENREEIEAVKSLYPsyKNYTDVYDKNNLLTNKTVMAHGCYLSEEELN 247
Cdd:PRK12393 209 tTPTFSL--PPELLREVARAARGMGLRLHSHLSETVDYVDFCREKYG--MTPVQFVAEHDWLGPDVWFAHLVKLDAEEIA 284
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006403 248 IFSERGASIAHCPNSNLSLSSGLLNVLEVLKHKVKIGLGTD-VAGGYSYSMLDAIRRAVMVSNVLlinkVNEKNLTLKEV 326
Cdd:PRK12393 285 LLAQTGTGIAHCPQSNGRLGSGIAPALAMEAAGVPVSLGVDgAASNESADMLSEAHAAWLLHRAE----GGADATTVEDV 360
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006403 327 FRLATLGGSQALGLDsEIGNFEVGKEFD-AL--LINPRasdspidlFYGdfVGDISEAVIQKflylGDDRNIEEVYVGGK 403
Cdd:PRK12393 361 VHWGTAGGARVLGLD-AIGTLAVGQAADlAIydLDDPR--------FFG--LHDPAIAPVAC----GGPAPVKALLVNGR 425
|
...
gi 569006403 404 QVV 406
Cdd:PRK12393 426 PVV 428
|
|
| PRK06151 |
PRK06151 |
N-ethylammeline chlorohydrolase; Provisional |
33-406 |
3.53e-13 |
|
N-ethylammeline chlorohydrolase; Provisional
Pssm-ID: 180428 [Multi-domain] Cd Length: 488 Bit Score: 70.84 E-value: 3.53e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006403 33 MPGLVDTHIHapqyafagSNVDLPLL------EWLNKYTFP---TEQRFRSTDVAEEV---YTRVVRRTLKNGTTTACYF 100
Cdd:PRK06151 56 GPGFIDLDAL--------SDLDTTILgldngpGWAKGRVWSrdyVEAGRREMYTPEELafqKRYAFAQLLRNGITTAMPI 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006403 101 GTI-------HTDSSLILAEITDKFGQRAFVGKVCM--------DLNDTVPEYKETTEESVKETERFVSEMLQKNYPRVK 165
Cdd:PRK06151 128 ASLfyrqwaeTYAEFAAAAEAAGRLGLRVYLGPAYRsggsvleaDGSLEVVFDEARGLAGLEEAIAFIKRVDGAHNGLVR 207
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006403 166 PIVTPRFTLSCTETLMSELGNIAKTHDLYIQSHISENREEIEAVKSLYPsyKNYTDVYDKNNLLTNKTVMAHGCYLSE-- 243
Cdd:PRK06151 208 GMLAPDRIETCTVDLLRRTAAAARELGCPVRLHCAQGVLEVETVRRLHG--TTPLEWLADVGLLGPRLLIPHATYISGsp 285
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006403 244 -------EELNIFSERGASIAHCPNSNLSLSSGLLNVLEVLKHKVKIGLGTDVAggysysmldairRAVMVSNV---LLI 313
Cdd:PRK06151 286 rlnysggDDLALLAEHGVSIVHCPLVSARHGSALNSFDRYREAGINLALGTDTF------------PPDMVMNMrvgLIL 353
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006403 314 NKVNEKNLT---LKEVFRLATLGGSQALGLDsEIGNFEVGKEFDALLINPRasdspiDLFYGDFVGDISEAVIQkflylG 390
Cdd:PRK06151 354 GRVVEGDLDaasAADLFDAATLGGARALGRD-DLGRLAPGAKADIVVFDLD------GLHMGPVFDPIRTLVTG-----G 421
|
410
....*....|....*.
gi 569006403 391 DDRNIEEVYVGGKQVV 406
Cdd:PRK06151 422 SGRDVRAVFVDGRVVM 437
|
|
| PRK07203 |
PRK07203 |
putative aminohydrolase SsnA; |
33-311 |
2.96e-12 |
|
putative aminohydrolase SsnA;
Pssm-ID: 235963 [Multi-domain] Cd Length: 442 Bit Score: 68.04 E-value: 2.96e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006403 33 MPGLVDTHIHApqY-AFA-GSNVDLP----LLEWLNKYTFpteqRFRSTDVAEEVYTRVVRRTL---KNGTTTA----CY 99
Cdd:PRK07203 58 MPGLINSHNHI--YsGLArGMMANIPpppdFISILKNLWW----RLDRALTLEDVYYSALICSLeaiKNGVTTVfdhhAS 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006403 100 FGTIhTDSSLILAEITDKFGQRafvGKVCMDLNDTVPEykETTEESVKETERFVSEMLQKNYPRVKPIVT--PRFTLScT 177
Cdd:PRK07203 132 PNYI-GGSLFTIADAAKKVGLR---AMLCYETSDRDGE--KELQEGVEENIRFIKHIDEAKDDMVEAMFGlhASFTLS-D 204
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006403 178 ETLmSELGNIAKTHDLYIQSHISENREEIEAvkSLYPSYKNYTDVYDKNNLLTNKTVMAHGCYLSEEELNIFSERGASIA 257
Cdd:PRK07203 205 ATL-EKCREAVKETGRGYHIHVAEGIYDVSD--SHKKYGKDIVERLADFGLLGEKTLAAHCIYLSDEEIDLLKETDTFVV 281
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 569006403 258 HCPNSNLSLSSGLLNVLEVLKHKVKIGLGTDvagGYSYSMLDAIRravmVSNVL 311
Cdd:PRK07203 282 HNPESNMGNAVGYNPVLEMIKNGILLGLGTD---GYTSDMFESYK----VANFK 328
|
|
| HutI |
COG1228 |
Imidazolonepropionase or related amidohydrolase [Secondary metabolites biosynthesis, transport ... |
33-406 |
1.23e-10 |
|
Imidazolonepropionase or related amidohydrolase [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 440841 [Multi-domain] Cd Length: 386 Bit Score: 62.67 E-value: 1.23e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006403 33 MPGLVDTHIHapqYAFAGSNVDlpllewlnkyTFPTEQRFRSTDVAEEVYTRVVRRTLKNGTTTACyfgtIHTDSSLILA 112
Cdd:COG1228 64 LPGLIDAHTH---LGLGGGRAV----------EFEAGGGITPTVDLVNPADKRLRRALAAGVTTVR----DLPGGPLGLR 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006403 113 EITDK------FGQRAFVGKVCMDLNDTVPEYketteeSVKETERFVSEMLQKNYPRVKPIVT---PRFTLSCTETLMSE 183
Cdd:COG1228 127 DAIIAgeskllPGPRVLAAGPALSLTGGAHAR------GPEEARAALRELLAEGADYIKVFAEggaPDFSLEELRAILEA 200
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006403 184 lgniAKTHDLYIQSHISENREEIEAVKSlypsyknytdvydknnlltNKTVMAHGCYLSEEELNIFSERGASI------- 256
Cdd:COG1228 201 ----AHALGLPVAAHAHQADDIRLAVEA-------------------GVDSIEHGTYLDDEVADLLAEAGTVVlvptlsl 257
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006403 257 --AHCPNSNLSLSSGLLNVLEV--------LKHKVKIGLGTDVAGGYS--YSMLDAIRRAVMVsnvllinkvnekNLTLK 324
Cdd:COG1228 258 flALLEGAAAPVAAKARKVREAalanarrlHDAGVPVALGTDAGVGVPpgRSLHRELALAVEA------------GLTPE 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006403 325 EVFRLATLGGSQALGLDSEIGNFEVGKEFDALLINprasdspidlfyGDFVGDISeaviqkflYLgddRNIEEVYVGGKQ 404
Cdd:COG1228 326 EALRAATINAAKALGLDDDVGSLEPGKLADLVLLD------------GDPLEDIA--------YL---EDVRAVMKDGRV 382
|
..
gi 569006403 405 VV 406
Cdd:COG1228 383 VD 384
|
|
| archeal_chlorohydrolases |
cd01305 |
Predicted chlorohydrolases. These metallo-dependent hydrolases from archea are part of the ... |
33-335 |
1.64e-09 |
|
Predicted chlorohydrolases. These metallo-dependent hydrolases from archea are part of the superfamily of metallo-dependent hydrolases, a large group of proteins that show conservation in their 3-dimensional fold (TIM barrel) and in details of their active site. They have a conserved metal binding site, involving four histidines and one aspartic acid residue. In the common reaction mechanism, the metal ion (or ions) deprotonate a water molecule for a nucleophilic attack on the substrate. Some members of this subgroup are predicted to be chlorohyrolases.
Pssm-ID: 238630 [Multi-domain] Cd Length: 263 Bit Score: 58.18 E-value: 1.64e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006403 33 MPGLVDTHIHAPQYAFAGSNVDLPLLE---WLN--KYTFPTEQRFRSTDVAEEvytRVVRRTLKNGTTTACYFGTIHTDS 107
Cdd:cd01305 3 IPALVNAHTHLGDSAIKEVGDGLPLDDlvaPPDglKHRLLAQADDRELAEAMR---KVLRDMRETGIGAFADFREGGVEG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006403 108 SLILAEITDKFgqrAFVGKVCMDlNDTVPEYKETTEEsvketerfVSEMLQKNYPRvkpivtprftlsctETLMSELGNI 187
Cdd:cd01305 80 IELLRRALGKL---PVPFEVILG-RPTEPDDPEILLE--------VADGLGLSSAN--------------DVDLEDILEL 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006403 188 AKTHDLYIQSHISENRE-----EIEAVKSLYPsyknytdvydknNLLTnktvmaHGCYLSEEELNIFSERGASIAHCPNS 262
Cdd:cd01305 134 LRRRGKLFAIHASETREsvgmtDIERALDLEP------------DLLV------HGTHLTDEDLELVRENGVPVVLCPRS 195
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 569006403 263 NLSLSSGLLNVLEVLKHKVKIGLGTDVAGGYSYSMLDAIRRAVMVSNVLliNKVNEknltlKEVFRLATLGGS 335
Cdd:cd01305 196 NLYFGVGIPPVAELLKLGIKVLLGTDNVMVNEPDMWAEMEFLAKYSRLQ--GYLSP-----LEILRMATVNAA 261
|
|
| Met_dep_hydrolase_E |
cd01313 |
Metallo-dependent hydrolases, subgroup D is part of the superfamily of metallo-dependent ... |
198-403 |
9.94e-09 |
|
Metallo-dependent hydrolases, subgroup D is part of the superfamily of metallo-dependent hydrolases, a large group of proteins that show conservation in their 3-dimensional fold (TIM barrel) and in details of their active site. The vast majority of the members have a conserved metal binding site, involving four histidines and one aspartic acid residue. In the common reaction mechanism, the metal ion (or ions) deprotonate a water molecule for a nucleophilic attack on the substrate. The function of this subgroup is unknown.
Pssm-ID: 238638 [Multi-domain] Cd Length: 418 Bit Score: 56.70 E-value: 9.94e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006403 198 HISENREEIEAVksLYPSYKNYTDVYDKNNLLTNKTVMAHGCYLSEEELNIFSERGASIAHCPNSNLSLSSGLLNVLEVL 277
Cdd:cd01313 225 HLAEQPKEVDDC--LAAHGRRPVELLLDHGHLDARWCLVHATHLTDNETLLLGRSGAVVGLCPTTEANLGDGIFPAAALL 302
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006403 278 KHKVKIGLGTDVAGG-----------YSYSMLDAIRravmvsNVLlinkVNEKNLTLKEVFRLATLGGSQALGLDSeiGN 346
Cdd:cd01313 303 AAGGRIGIGSDSNARidlleelrqleYSQRLRDRAR------NVL----ATAGGSSARALLDAALAGGAQALGLAT--GA 370
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 569006403 347 FEVGKEFDALLInprASDSPidlfygDFVGDISEAVIQKFLYLGDDRNIEEVYVGGK 403
Cdd:cd01313 371 LEAGARADLLSL---DLDHP------SLAGALPDTLLDAWVFAAGDREVRDVVVGGR 418
|
|
| Amidohydro_3 |
pfam07969 |
Amidohydrolase family; |
273-406 |
7.99e-06 |
|
Amidohydrolase family;
Pssm-ID: 400360 [Multi-domain] Cd Length: 464 Bit Score: 47.91 E-value: 7.99e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006403 273 VLEVLKHKVKIGLGTDVAGGySYSMLDAIRRAVM-----VSNVLLINKVneknLTLKEVFRLATLGGSQALGLDSEIGNF 347
Cdd:pfam07969 351 VKELLNAGVKVALGSDAPVG-PFDPWPRIGAAVMrqtagGGEVLGPDEE----LSLEEALALYTSGPAKALGLEDRKGTL 425
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 569006403 348 EVGKEFDALLINprasdspIDLFygdfvgDISEAVIqkflylgDDRNIEEVYVGGKQVV 406
Cdd:pfam07969 426 GVGKDADLVVLD-------DDPL------TVDPPAI-------ADIRVRLTVVDGRVVY 464
|
|
| PRK07213 |
PRK07213 |
chlorohydrolase; Provisional |
198-362 |
1.15e-05 |
|
chlorohydrolase; Provisional
Pssm-ID: 235969 [Multi-domain] Cd Length: 375 Bit Score: 46.95 E-value: 1.15e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006403 198 HISENREEIEAVKSLYpsykNYTDVYDKNNLLTNKTVMAHGCYLSEEELNIFSERGASIAHCPNSNLSLSSGLLNVLEVL 277
Cdd:PRK07213 198 HAAEHKGSVEYSLEKY----GMTEIERLINLGFKPDFIVHATHPSNDDLELLKENNIPVVVCPRANASFNVGLPPLNEML 273
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006403 278 KHKVKIGLGTDVAGGYSYSM---LDAIRRAVmvsnvllinkvnekNLTLKEVFRLATLGGSQALGLDsEIGNFEVGKEFD 354
Cdd:PRK07213 274 EKGILLGIGTDNFMANSPSIfreMEFIYKLY--------------HIEPKEILKMATINGAKILGLI-NVGLIEEGFKAD 338
|
....*...
gi 569006403 355 ALLINPRA 362
Cdd:PRK07213 339 FTFIKPTN 346
|
|
| Imidazolone-5PH |
cd01296 |
Imidazolonepropionase/imidazolone-5-propionate hydrolase (Imidazolone-5PH) catalyzes the third ... |
235-385 |
6.02e-04 |
|
Imidazolonepropionase/imidazolone-5-propionate hydrolase (Imidazolone-5PH) catalyzes the third step in the histidine degradation pathway, the hydrolysis of (S)-3-(5-oxo-4,5-dihydro-3H-imidazol-4-yl)propanoate to N-formimidoyl-L-glutamate. In bacteria, the enzyme is part of histidine utilization (hut) operon.
Pssm-ID: 238621 [Multi-domain] Cd Length: 371 Bit Score: 41.86 E-value: 6.02e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006403 235 MAHGCYLSEEELNIFSERGASIAHCPNSNLSLSSGLLNVLEVLKHKVKIGLGTDVAGGySY---SMLDAIRRAVmvsnvl 311
Cdd:cd01296 233 ADHLEHTSDEGIAALAEAGTVAVLLPGTAFSLRETYPPARKLIDAGVPVALGTDFNPG-SSptsSMPLVMHLAC------ 305
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 569006403 312 linkVNEKnLTLKEVFRLATLGGSQALGLDSEIGNFEVGKEFDALLINpraSDSPIDLFYgDFVGDISEAVIQK 385
Cdd:cd01296 306 ----RLMR-MTPEEALTAATINAAAALGLGETVGSLEVGKQADLVILD---APSYEHLAY-RFGVNLVEYVIKN 370
|
|
| nagA |
PRK11170 |
N-acetylglucosamine-6-phosphate deacetylase; Provisional |
291-351 |
2.78e-03 |
|
N-acetylglucosamine-6-phosphate deacetylase; Provisional
Pssm-ID: 183010 Cd Length: 382 Bit Score: 39.57 E-value: 2.78e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 569006403 291 GGYSYSMLDAIRravmvsnvlliNKVNEKNLTLKEVFRLATLGGSQALGLDSEIGNFEVGK 351
Cdd:PRK11170 307 SGSALTMIEAVR-----------NLVEHVGIALDEALRMATLYPARAIGVDKRLGSIEAGK 356
|
|
| Met_dep_hydrolase_A |
cd01299 |
Metallo-dependent hydrolases, subgroup A is part of the superfamily of metallo-dependent ... |
278-362 |
4.34e-03 |
|
Metallo-dependent hydrolases, subgroup A is part of the superfamily of metallo-dependent hydrolases, a large group of proteins that show conservation in their 3-dimensional fold (TIM barrel) and in details of their active site. The vast majority of the members have a conserved metal binding site, involving four histidines and one aspartic acid residue. In the common reaction mechanism, the metal ion (or ions) deprotonate a water molecule for a nucleophilic attack on the substrate. The function of this subgroup is unknown.
Pssm-ID: 238624 [Multi-domain] Cd Length: 342 Bit Score: 38.81 E-value: 4.34e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006403 278 KHKVKIGLGTD-----VAGGYSYSMLdairrAVMVsnvllinkvnEKNLTLKEVFRLATLGGSQALGLDSEIGNFEVGKE 352
Cdd:cd01299 261 KAGVKIAFGTDagfpvPPHGWNAREL-----ELLV----------KAGGTPAEALRAATANAAELLGLSDELGVIEAGKL 325
|
90
....*....|..
gi 569006403 353 FDALLI--NPRA 362
Cdd:cd01299 326 ADLLVVdgDPLE 337
|
|
| PRK09229 |
PRK09229 |
N-formimino-L-glutamate deiminase; Validated |
327-406 |
8.44e-03 |
|
N-formimino-L-glutamate deiminase; Validated
Pssm-ID: 236420 [Multi-domain] Cd Length: 456 Bit Score: 38.29 E-value: 8.44e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569006403 327 FRLATLGGSQALGLDseIGNFEVGKEFDALLINPrasDSPidlfygDFVGDISEAVIQKFLYLGDDRNIEEVYVGGKQVV 406
Cdd:PRK09229 363 FDAALAGGAQALGRA--IGGLAVGARADLVVLDL---DHP------ALAGREGDALLDRWVFAGGDAAVRDVWVAGRWVV 431
|
|
| |
