|
Name |
Accession |
Description |
Interval |
E-value |
| GDEase |
cd01303 |
Guanine deaminase (GDEase). Guanine deaminase is an aminohydrolase responsible for the ... |
6-411 |
2.71e-133 |
|
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: 389.71 E-value: 2.71e-133
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2700908057 6 LKGTFLDTPA-PDTLRVREGYLLCENGLCAGFS-------------ETAPAGVEVLDYTGKIITPGLVDLHLHAPQYSYC 71
Cdd:cd01303 1 FRGTFIHTKSlPELELVEDALRVVEDGLIVVVDgniiaagaaetlkRAAKPGARVIDSPNQFILPGFIDTHIHAPQYANI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2700908057 72 GTAMDLELLDWLQQYTYPEEAHYADPTYARLGYSYFVRDLKNSATTRACIFATLHTDATLELMHQLRGAGLSAFVGKLGM 151
Cdd:cd01303 81 GSGLGEPLLDWLETYTFPEEAKFADPAYAREVYGRFLDELLRNGTTTACYFATIHPESTEALFEEAAKRGQRAIAGKVCM 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2700908057 152 DRNSPDSYREPSAAAgLAETR----RWLDTcraentlhAGPVRPMITPRFTPSTSDEYMRGLGELAREYN-VPAQSHLSE 226
Cdd:cd01303 161 DRNAPEYYRDTAESS-YRDTKrlieRWHGK--------SGRVKPAITPRFAPSCSEELLAALGKLAKEHPdLHIQTHISE 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2700908057 227 NPGEIAWVAELCPGTKFYGESYSRYGLFGGgvPTVMAHCIYSPDDEAALMKQNRVMIAHCPTSNENVIAGIAPAAHYLRG 306
Cdd:cd01303 232 NLDEIAWVKELFPGARDYLDVYDKYGLLTE--KTVLAHCVHLSEEEFNLLKERGASVAHCPTSNLFLGSGLFDVRKLLDA 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2700908057 307 GWRVGLGSDVAGGQTLDLFTVMATAVQVSKLRWRYIDQSeKPLTMVEALYMATVGGGDFWAdFGEKVGLFEDGYAFDALV 386
Cdd:cd01303 310 GIKVGLGTDVGGGTSFSMLDTLRQAYKVSRLLGYELGGH-AKLSPAEAFYLATLGGAEALG-LDDKIGNFEVGKEFDAVV 387
|
410 420 430
....*....|....*....|....*....|
gi 2700908057 387 LDD--DPL---KNMRAFSAAERLERYAYLG 411
Cdd:cd01303 388 IDPsaTPLladRMFRVESLEEALFKFLYLG 417
|
|
| guan_deamin |
TIGR02967 |
guanine deaminase; This model describes guanine deaminase, which hydrolyzes guanine to ... |
22-411 |
1.29e-106 |
|
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: 320.74 E-value: 1.29e-106
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2700908057 22 REGYLLCENGLCAGFS------ETAPAGVEVLDYTGKIITPGLVDLHLHAPQYSYCGtAMDLELLDWLQQYTYPEEAHYA 95
Cdd:TIGR02967 5 EDGLLVVENGRIVAVGdyaelkETLPAGVEIDDYRGHLIMPGFIDTHIHYPQTEMIA-SYGEQLLEWLEKYTFPTEARFA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2700908057 96 DPTYARLGYSYFVRDLKNSATTRACIFATLHTDATLELMHQLRGAGLSAFVGKLGMDRNSPDSYREpSAAAGLAETRRWL 175
Cdd:TIGR02967 84 DPDHAEEVAEFFLDELLRNGTTTALVFATVHPESVDALFEAALKRGMRMIAGKVLMDRNAPDYLRD-TAESSYDESKALI 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2700908057 176 DTCRAENTLHagpvrPMITPRFTPSTSDEYMRGLGELAREY-NVPAQSHLSENPGEIAWVAELCPGTKFYGESYSRYGLF 254
Cdd:TIGR02967 163 ERWHGKGRLL-----YAVTPRFAPTSSPEQLAAAGELAKEYpDVYVQTHLSENKDEIAWVKELFPEAKDYLDVYDHYGLL 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2700908057 255 GGGvpTVMAHCIYSPDDEAALMKQNRVMIAHCPTSNENVIAGIAPAAHYLRGGWRVGLGSDVAGGQTLDLFTVMATAVQV 334
Cdd:TIGR02967 238 GRR--SVFAHCIHLSDEECQRLAETGAAIAHCPTSNLFLGSGLFNLKKALEHGVRVGLGTDVGGGTSFSMLQTLREAYKV 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2700908057 335 SKLRwryidqsEKPLTMVEALYMATVGGGDFwADFGEKVGLFEDGYAFDALVLDDD--PLKNMRAFSA---AERLERYAY 409
Cdd:TIGR02967 316 SQLQ-------GARLSPFEAFYLATLGGARA-LDLDDRIGNFEPGKEADFVVLDPAatPLLALRFEGAdtlEDKLFKLMY 387
|
..
gi 2700908057 410 LG 411
Cdd:TIGR02967 388 LG 389
|
|
| SsnA |
COG0402 |
Cytosine/adenosine deaminase or related metal-dependent hydrolase [Nucleotide transport and ... |
3-413 |
8.91e-101 |
|
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: 306.37 E-value: 8.91e-101
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2700908057 3 TFTLKGTFLDTPAPDTLRVREGYLLCENGLCAGFSETAPA-----GVEVLDYTGKIITPGLVDLHLHAPQYSYCGTAMDL 77
Cdd:COG0402 1 DLLIRGAWVLTMDPAGGVLEDGAVLVEDGRIAAVGPGAELparypAAEVIDAGGKLVLPGLVNTHTHLPQTLLRGLADDL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2700908057 78 ELLDWLQQYTYPEEAHYaDPTYARLGYSYFVRDLKNSATTRACIFATLHTDATLELMHQLRGAGLSAFVGKLGMDRNSPD 157
Cdd:COG0402 81 PLLDWLEEYIWPLEARL-DPEDVYAGALLALAEMLRSGTTTVADFYYVHPESADALAEAAAEAGIRAVLGRGLMDRGFPD 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2700908057 158 SYREpSAAAGLAETRRWLDTCRAEntlHAGPVRPMITPRFTPSTSDEYMRGLGELAREYNVPAQSHLSENPGEIAWVAEL 237
Cdd:COG0402 160 GLRE-DADEGLADSERLIERWHGA---ADGRIRVALAPHAPYTVSPELLRAAAALARELGLPLHTHLAETRDEVEWVLEL 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2700908057 238 CPGTkfYGESYSRYGLFGGgvPTVMAHCIYSPDDEAALMKQNRVMIAHCPTSNENVIAGIAPAAHYLRGGWRVGLGSDVA 317
Cdd:COG0402 236 YGKR--PVEYLDELGLLGP--RTLLAHCVHLTDEEIALLAETGASVAHCPTSNLKLGSGIAPVPRLLAAGVRVGLGTDGA 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2700908057 318 GGQT-LDLFTVMATAVQVSKLRWRyidqSEKPLTMVEALYMATVGGGDFwADFGEKVGLFEDGYAFDALVLDDDPLknmR 396
Cdd:COG0402 312 ASNNsLDMFEEMRLAALLQRLRGG----DPTALSAREALEMATLGGARA-LGLDDEIGSLEPGKRADLVVLDLDAP---H 383
|
410
....*....|....*..
gi 2700908057 397 AFSAAERLERYAYLGKG 413
Cdd:COG0402 384 LAPLHDPLSALVYAADG 400
|
|
| PRK09228 |
PRK09228 |
guanine deaminase; Provisional |
1-404 |
2.31e-89 |
|
guanine deaminase; Provisional
Pssm-ID: 236419 [Multi-domain] Cd Length: 433 Bit Score: 277.46 E-value: 2.31e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2700908057 1 MNTFTLKGTFLDTPA-------PDTLRVRE-GYLLCENGLCAGF------SETAPAGVEVLDYTGKIITPGLVDLHLHAP 66
Cdd:PRK09228 1 MTTKAYRGRLLHFTAdpaevddEDALRYIEdGLLLVEDGRIVAAgpyaelRAQLPADAEVTDYRGKLILPGFIDTHIHYP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2700908057 67 QYSYCGtAMDLELLDWLQQYTYPEEAHYADPTYARLGYSYFVRDLKNSATTRACIFATLHTDATLELMHQLRGAGLSAFV 146
Cdd:PRK09228 81 QTDMIA-SYGEQLLDWLNTYTFPEERRFADPAYAREVAEFFLDELLRNGTTTALVFGTVHPQSVDALFEAAEARNMRMIA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2700908057 147 GKLGMDRNSPDSYREpSAAAGLAETR----RWLDTCRAentLHAgpvrpmITPRFTPSTSDEYMRGLGELAREY-NVPAQ 221
Cdd:PRK09228 160 GKVLMDRNAPDGLRD-TAESGYDDSKalieRWHGKGRL---LYA------ITPRFAPTSTPEQLEAAGALAREHpDVWIQ 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2700908057 222 SHLSENPGEIAWVAELCPGTKFYGESYSRYGLFGGGvpTVMAHCIYSPDDEAALMKQNRVMIAHCPTSNENVIAGIAPAA 301
Cdd:PRK09228 230 THLSENLDEIAWVKELFPEARDYLDVYERYGLLGPR--AVFAHCIHLEDRERRRLAETGAAIAFCPTSNLFLGSGLFDLK 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2700908057 302 HYLRGGWRVGLGSDVAGGQTLDLFTVMATAVQVSKLRwryidqsEKPLTMVEALYMATVGGgdfwA---DFGEKVGLFED 378
Cdd:PRK09228 308 RADAAGVRVGLGTDVGGGTSFSMLQTMNEAYKVQQLQ-------GYRLSPFQAFYLATLGG----AralGLDDRIGNLAP 376
|
410 420 430
....*....|....*....|....*....|.
gi 2700908057 379 GYAFDALVLD--DDPL---KNMRAFSAAERL 404
Cdd:PRK09228 377 GKEADFVVLDpaATPLlalRTARAESLEELL 407
|
|
| ATZ_TRZ_like |
cd01298 |
TRZ/ATZ family contains enzymes from the atrazine degradation pathway and related hydrolases. ... |
20-388 |
9.01e-57 |
|
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: 192.42 E-value: 9.01e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2700908057 20 RVREGYLLCENGLCAGFSETAPA----GVEVLDYTGKIITPGLVDLHLHAPQYSYCGTAMDLELLDWLQQYTYPEEAHY- 94
Cdd:cd01298 16 VLEDGDVLVEDGRIVAVGPALPLpaypADEVIDAKGKVVMPGLVNTHTHLAMTLLRGLADDLPLMEWLKDLIWPLERLLt 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2700908057 95 ADPTY--ARLGYSYFVRdlknSATTRACIFATLHTDATLELMHQLrgaGLSAFVGKLGMDRNSPDSyrePSAAAGLAETR 172
Cdd:cd01298 96 EEDVYlgALLALAEMIR----SGTTTFADMYFFYPDAVAEAAEEL---GIRAVLGRGIMDLGTEDV---EETEEALAEAE 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2700908057 173 RWLDTCraeNTLHAGPVRPMITPRFTPSTSDEYMRGLGELAREYNVPAQSHLSENPGEIAWVAELcpgtkfYGESYSRY- 251
Cdd:cd01298 166 RLIREW---HGAADGRIRVALAPHAPYTCSDELLREVAELAREYGVPLHIHLAETEDEVEESLEK------YGKRPVEYl 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2700908057 252 ---GLFGggVPTVMAHCIYSPDDEAALMKQNRVMIAHCPTSNENVIAGIAPAAHYLRGGWRVGLGSD-VAGGQTLDLFTV 327
Cdd:cd01298 237 eelGLLG--PDVVLAHCVWLTDEEIELLAETGTGVAHNPASNMKLASGIAPVPEMLEAGVNVGLGTDgAASNNNLDMFEE 314
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2700908057 328 MATAVQVSKLRwryiDQSEKPLTMVEALYMATVGGGDFwadFG-EKVGLFEDGYAFDALVLD 388
Cdd:cd01298 315 MRLAALLQKLA----HGDPTALPAEEALEMATIGGAKA---LGlDEIGSLEVGKKADLILID 369
|
|
| PRK07228 |
PRK07228 |
5'-deoxyadenosine deaminase; |
45-390 |
1.49e-54 |
|
5'-deoxyadenosine deaminase;
Pssm-ID: 180895 [Multi-domain] Cd Length: 445 Bit Score: 187.13 E-value: 1.49e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2700908057 45 EVLDYTGKIITPGLVDLHLHAPQYSYCGTAMDLELLDWLQQYTYP-EEAHYADPTY--ARLGYSYFVRdlknSATTRACI 121
Cdd:PRK07228 45 DHIDATGKVVIPGLIQGHIHLCQTLFRGIADDLELLDWLKDRIWPlEAAHDAESMYysALLGIGELIE----SGTTTIVD 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2700908057 122 FATL-HTDATLELMHQLrgaGLSAFVGKLGMD--RNSPDSYREPSAAAgLAET----RRWLDTcraentlHAGPVRPMIT 194
Cdd:PRK07228 121 MESVhHTDSAFEAAGES---GIRAVLGKVMMDygDDVPEGLQEDTEAS-LAESvrllEKWHGA-------DNGRIRYAFT 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2700908057 195 PRFTPSTSDEYMRGLGELAREYNVPAQSHLSENPGEIAWVAELcpgtkfYGESYSRY----GLFGGGVptVMAHCIYSPD 270
Cdd:PRK07228 190 PRFAVSCTEELLRGVRDLADEYGVRIHTHASENRGEIETVEEE------TGMRNIHYldevGLTGEDL--ILAHCVWLDE 261
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2700908057 271 DEAALMKQNRVMIAHCPTSNENVIAGIAPAAHYLRGGWRVGLGSDVAG-GQTLDLFTVMATAVQVSKLRwryidqSEKPL 349
Cdd:PRK07228 262 EEREILAETGTHVTHCPSSNLKLASGIAPVPDLLERGINVALGADGAPcNNTLDPFTEMRQAALIQKVD------RLGPT 335
|
330 340 350 360
....*....|....*....|....*....|....*....|...
gi 2700908057 350 TM--VEALYMATVGGGDFwADFGEKVGLFEDGYAFDALVLDDD 390
Cdd:PRK07228 336 AMpaRTVFEMATLGGAKA-AGFEDEIGSLEEGKKADLAILDLD 377
|
|
| PRK06038 |
PRK06038 |
N-ethylammeline chlorohydrolase; Provisional |
1-388 |
6.54e-37 |
|
N-ethylammeline chlorohydrolase; Provisional
Pssm-ID: 180363 [Multi-domain] Cd Length: 430 Bit Score: 139.50 E-value: 6.54e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2700908057 1 MNTFTLKGTFLDTPapDTLRVREGYLLCENGLCAGFSETAPAGVE-VLDYTGKIITPGLVDLHLHAPQYSYCGTAMDLEL 79
Cdd:PRK06038 1 MADIIIKNAYVLTM--DAGDLKKGSVVIEDGTITEVSESTPGDADtVIDAKGSVVMPGLVNTHTHAAMTLFRGYADDLPL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2700908057 80 LDWLQQYTYPEEAHY-ADPTYA--RLGYSYFVRdlknSATTRaciFATL--HTDATLELMHQlrgAGLSAFVGKlGMdrn 154
Cdd:PRK06038 79 AEWLNDHIWPAEAKLtAEDVYAgsLLACLEMIK----SGTTS---FADMyfYMDEVAKAVEE---SGLRAALSY-GM--- 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2700908057 155 sPDSYREPSAAAGLAETRRWLDTCRAENTlhaGPVRPMITPRFTPSTSDEYMRGLGELAREYNVPAQSHLSENPGEIAWV 234
Cdd:PRK06038 145 -IDLGDDEKGEAELKEGKRFVKEWHGAAD---GRIKVMYGPHAPYTCSEEFLSKVKKLANKDGVGIHIHVLETEAELNQM 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2700908057 235 AE---LCPGtkfygESYSRYGLFGGGVptVMAHCIYSPDDEAALMKQNRVMIAHCPTSNENVIAGIAPAAHYLRGGWRVG 311
Cdd:PRK06038 221 KEqygMCSV-----NYLDDIGFLGPDV--LAAHCVWLSDGDIEILRERGVNVSHNPVSNMKLASGIAPVPKLLERGVNVS 293
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2700908057 312 LGSD-VAGGQTLDLFTVMATAVQVSKLrwryidQSEKP--LTMVEALYMATVGGGdfwADFGEKVGLFEDGYAFDALVLD 388
Cdd:PRK06038 294 LGTDgCASNNNLDMFEEMKTAALLHKV------NTMDPtaLPARQVLEMATVNGA---KALGINTGMLKEGYLADIIIVD 364
|
|
| Amidohydro_1 |
pfam01979 |
Amidohydrolase family; This family of enzymes are a a large metal dependent hydrolase ... |
53-392 |
2.15e-34 |
|
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: 130.70 E-value: 2.15e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2700908057 53 IITPGLVDLHLHAPQYSYCGTAMDLElldwlqqytypeeahyadptYARLGYSYFVRDLKNSATTRAC---IFATLHTDA 129
Cdd:pfam01979 1 IVLPGLIDAHVHLEMGLLRGIPVPPE--------------------FAYEALRLGITTMLKSGTTTVLdmgATTSTGIEA 60
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2700908057 130 TLELMHQLRgAGLSAFVGKLGMDRNSPDSYREpsaaaglAETRRWLDTCRAENTLHAGPVRPMITPRFTPSTSDEYMRGL 209
Cdd:pfam01979 61 LLEAAEELP-LGLRFLGPGCSLDTDGELEGRK-------ALREKLKAGAEFIKGMADGVVFVGLAPHGAPTFSDDELKAA 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2700908057 210 GELAREYNVPAQSHLSENPGEIAWVAELCPGTK--FYGESYSRYGLFGGGVPTVMAHCIYSPDDEAALMKQ--NRVMIAH 285
Cdd:pfam01979 133 LEEAKKYGLPVAIHALETKGEVEDAIAAFGGGIehGTHLEVAESGGLLDIIKLILAHGVHLSPTEANLLAEhlKGAGVAH 212
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2700908057 286 CPTSNENVIAGIAPAAHYLRGGWRVGLGSDVAG-GQTLDLFTVMATAVQVSKlrwryidQSEKPLTMVEALYMATVGGGD 364
Cdd:pfam01979 213 CPFSNSKLRSGRIALRKALEDGVKVGLGTDGAGsGNSLNMLEELRLALELQF-------DPEGGLSPLEALRMATINPAK 285
|
330 340 350
....*....|....*....|....*....|
gi 2700908057 365 FwadFG--EKVGLFEDGYAFDALVLDDDPL 392
Cdd:pfam01979 286 A---LGldDKVGSIEVGKDADLVVVDLDPL 312
|
|
| PRK08393 |
PRK08393 |
N-ethylammeline chlorohydrolase; Provisional |
45-388 |
3.20e-28 |
|
N-ethylammeline chlorohydrolase; Provisional
Pssm-ID: 181411 [Multi-domain] Cd Length: 424 Bit Score: 115.28 E-value: 3.20e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2700908057 45 EVLDYTGKIITPGLVDLHLHAPQYSYCGTAMDLELLDWLQQYTYPEEAHYAdPTYARLGYSYFVRDLKNSATTracIFAT 124
Cdd:PRK08393 43 TVIDASGSVVSPGFINAHTHSPMVLLRGLADDVPLMEWLQNYIWPRERKLK-RKDIYWGAYLGLLEMIKSGTT---TFVD 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2700908057 125 LH------TDATLElmhqlrgAGLSAFVGKLGMDRNSPDSYREPsaaagLAETRRWLdtcRAENTLHAGPVRPMITPRFT 198
Cdd:PRK08393 119 MYfhmeevAKATLE-------VGLRGYLSYGMVDLGDEEKREKE-----IKETEKLM---EFIEKLNSPRVHFVFGPHAP 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2700908057 199 PSTSDEYMRGLGELAREYNVPAQSHLSENPGEIAWVAELcpgtkfYGES----YSRYGLFGGGVptVMAHCIYSPDDEAA 274
Cdd:PRK08393 184 YTCSLALLKWVREKAREWNKLITIHLSETMDEIKQIREK------YGKSpvvlLDEIGFLNEDV--IAAHGVWLSSRDIR 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2700908057 275 LMKQNRVMIAHCPTSNENVIAGIAPAAHYLRGGWRVGLGSD-VAGGQTLDLFTVMATAVQVSKLRWR--YIDQSEkpltm 351
Cdd:PRK08393 256 ILASAGVTVAHNPASNMKLGSGVMPLRKLLNAGVNVALGTDgAASNNNLDMLREMKLAALLHKVHNLdpTIADAE----- 330
|
330 340 350
....*....|....*....|....*....|....*..
gi 2700908057 352 vEALYMATVGGGdfwADFGEKVGLFEDGYAFDALVLD 388
Cdd:PRK08393 331 -TVFRMATQNGA---KALGLKAGVIKEGYLADIAVID 363
|
|
| PRK09045 |
PRK09045 |
TRZ/ATZ family hydrolase; |
45-388 |
2.59e-27 |
|
TRZ/ATZ family hydrolase;
Pssm-ID: 236366 [Multi-domain] Cd Length: 443 Bit Score: 113.08 E-value: 2.59e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2700908057 45 EVLDYTGKIITPGLVDLHLHAPQYSYCGTAMDLELLDWLQQYTYPEEAHYADPTyarlgysyFVRD---------LKNSA 115
Cdd:PRK09045 55 ETVELPDHVLIPGLINAHTHAAMSLLRGLADDLPLMTWLQDHIWPAEGAWVSEE--------FVRDgtllaiaemLRGGT 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2700908057 116 TTraciFATL--HTDATLELMHQlrgAGLSAFVGKLGMD-----RNSPDSYrepsAAAGLAETRRWLDTcraentlhagp 188
Cdd:PRK09045 127 TC----FNDMyfFPEAAAEAAHQ---AGMRAQIGMPVLDfptawASDADEY----LAKGLELHDQWRHH----------- 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2700908057 189 vrPMITPRFTP----STSDEYMRGLGELAREYNVPAQSHLSENPGEIAwvaelcPGTKFYGES----YSRYGLFGGGvpT 260
Cdd:PRK09045 185 --PLISTAFAPhapyTVSDENLERIRTLAEQLDLPIHIHLHETAQEIA------DSLKQHGQRplarLARLGLLGPR--L 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2700908057 261 VMAHCIYSPDDEAALMKQNRVMIAHCPTSNENVIAGIAPAAHYLRGGWRVGLGSD-VAGGQTLDLFTVMATAVQVSKLrw 339
Cdd:PRK09045 255 IAVHMTQLTDAEIALLAETGCSVVHCPESNLKLASGFCPVAKLLQAGVNVALGTDgAASNNDLDLFGEMRTAALLAKA-- 332
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|...
gi 2700908057 340 ryIDQSEKPLTMVEALYMATVGG----GdfwadFGEKVGLFEDGYAFDALVLD 388
Cdd:PRK09045 333 --VAGDATALPAHTALRMATLNGaralG-----LDDEIGSLEPGKQADLVAVD 378
|
|
| PRK06687 |
PRK06687 |
TRZ/ATZ family protein; |
22-395 |
5.68e-24 |
|
TRZ/ATZ family protein;
Pssm-ID: 180657 [Multi-domain] Cd Length: 419 Bit Score: 103.16 E-value: 5.68e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2700908057 22 REGYLLCENGLCAGFSETAPAGV----EVLDYTGKIITPGLVDLHLHAPQYSYCGTAMDLELLDWLQQYTYPEEahyadp 97
Cdd:PRK06687 20 LDGILAVKDSQIVYVGQDKPAFLeqaeQIIDYQGAWIMPGLVNCHTHSAMTGLRGIRDDSNLHEWLNDYIWPAE------ 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2700908057 98 tyarlgySYFVRDLKNSATTRACIFATLHTDATLELMHQLRGAGLSAF---VGKLGMD-RNSPDSYREP--SAAAGLAET 171
Cdd:PRK06687 94 -------SEFTPDMTTNAVKEALTEMLQSGTTTFNDMYNPNGVDIQQIyqvVKTSKMRcYFSPTLFSSEteTTAETISRT 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2700908057 172 RRWLDTCRAENTLHagpVRPMITPRFTPSTSDEYMRGLGELAREYNVPAQSHLSENPGEIAWVAElcpgtkfygesysRY 251
Cdd:PRK06687 167 RSIIDEILKYKNPN---FKVMVAPHSPYSCSRDLLEASLEMAKELNIPLHVHVAETKEESGIILK-------------RY 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2700908057 252 G------LFGGGV---PTVMAHCIYSPDDEAALMKQNRVMIAHCPTSNENVIAGIAPAAHYLRGGWRVGLGSD-VAGGQT 321
Cdd:PRK06687 231 GkrplafLEELGYldhPSVFAHGVELNEREIERLASSQVAIAHNPISNLKLASGIAPIIQLQKAGVAVGIATDsVASNNN 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2700908057 322 LDLFTVMATAVQVSKLRWRyiDQSEkpLTMVEALYMATVGGGDFWAdFGEKVGLFEDGYAFDALVLDDD------PLKNM 395
Cdd:PRK06687 311 LDMFEEGRTAALLQKMKSG--DASQ--FPIETALKVLTIEGAKALG-MENQIGSLEVGKQADFLVIQPQgkihlqPQENM 385
|
|
| PRK15493 |
PRK15493 |
bifunctional S-methyl-5'-thioadenosine deaminase/S-adenosylhomocysteine deaminase; |
45-414 |
1.95e-23 |
|
bifunctional S-methyl-5'-thioadenosine deaminase/S-adenosylhomocysteine deaminase;
Pssm-ID: 185390 [Multi-domain] Cd Length: 435 Bit Score: 101.67 E-value: 1.95e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2700908057 45 EVLDYTGKIITPGLVDLHLHAPQYSYCGTAMDLELLDWLQQYTYPEEAHYAdPTYA----RLGysyFVRDLKNSATTRAC 120
Cdd:PRK15493 48 EVIDMKGKWVLPGLVNTHTHVVMSLLRGIGDDMLLQPWLETRIWPLESQFT-PELAvastELG---LLEMVKSGTTSFSD 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2700908057 121 IFATLHTDATlELMHQLRGAGLSAFVGKLGMDRNSPDSYREpsaaaGLAETRRWLDTCRAENtlhaGPVRPMITPRFTPS 200
Cdd:PRK15493 124 MFNPIGVDQD-AIMETVSRSGMRAAVSRTLFSFGTKEDEKK-----AIEEAEKYVKRYYNES----GMLTTMVAPHSPYT 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2700908057 201 TSDEYMRGLGELAREYNVPAQSHLSENPGEIAWVAelcpgtKFYGESYSRY----GLFGGgvPTVMAHCIYSPDDEAALM 276
Cdd:PRK15493 194 CSTELLEECARIAVENQTMVHIHLSETEREVRDIE------AQYGKRPVEYaascGLFKR--PTVIAHGVVLNDNERAFL 265
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2700908057 277 KQNRVMIAHCPTSNENVIAGIAPAAHYLRGGWRVGLGSD-VAGGQTLDLFTVMatavQVSKLRWRYIDQSEKPLTMVEAL 355
Cdd:PRK15493 266 AEHDVRVAHNPNSNLKLGSGIANVKAMLEAGIKVGIATDsVASNNNLDMFEEM----RIATLLQKGIHQDATALPVETAL 341
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*....
gi 2700908057 356 YMATVGGGDFWAdfGEKVGLFEDGYAFDALVLddDPLKNMRAFSAAERLERYAYLGKGK 414
Cdd:PRK15493 342 TLATKGAAEVIG--MKQTGSLEVGKCADFITI--DPSNKPHLQPADEVLSHLVYAASGK 396
|
|
| metallo-dependent_hydrolases |
cd01292 |
Superfamily of metallo-dependent hydrolases (also called amidohydrolase superfamily) is a ... |
58-365 |
4.46e-20 |
|
Superfamily of metallo-dependent hydrolases (also called amidohydrolase superfamily) is a large group of proteins that show conservation in their 3-dimensional fold (TIM barrel) and in details of their active site. The vast majority of the members have a conserved metal binding site, involving four histidines and one aspartic acid residue. In the common reaction mechanism, the metal ion (or ions) deprotonate a water molecule for a nucleophilic attack on the substrate. The family includes urease alpha, adenosine deaminase, phosphotriesterase dihydroorotases, allantoinases, hydantoinases, AMP-, adenine and cytosine deaminases, imidazolonepropionase, aryldialkylphosphatase, chlorohydrolases, formylmethanofuran dehydrogenases and others.
Pssm-ID: 238617 [Multi-domain] Cd Length: 275 Bit Score: 89.70 E-value: 4.46e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2700908057 58 LVDLHLHAPQYSYCGTAMDLELldwlqqytypEEAHYADPTYARLGYSYFVRDLKNSATTRACIFATLHTD----ATLEL 133
Cdd:cd01292 1 FIDTHVHLDGSALRGTRLNLEL----------KEAEELSPEDLYEDTLRALEALLAGGVTTVVDMGSTPPPtttkAAIEA 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2700908057 134 MHQ--LRGAGLSAFVGKLGMDRNSPDSYREPsaaaglAETRRWLdtcRAENTLHAGPVRPMITPRFTPSTSDEYMRGLgE 211
Cdd:cd01292 71 VAEaaRASAGIRVVLGLGIPGVPAAVDEDAE------ALLLELL---RRGLELGAVGLKLAGPYTATGLSDESLRRVL-E 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2700908057 212 LAREYNVPAQSHLSENPGEIAWVAELCPgtkfygesysrygLFGGGVPTVMAHCIYSPDDEAALMKQNRVMIAHCPTSNE 291
Cdd:cd01292 141 EARKLGLPVVIHAGELPDPTRALEDLVA-------------LLRLGGRVVIGHVSHLDPELLELLKEAGVSLEVCPLSNY 207
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2700908057 292 ---NVIAGIAPAAHYLRGGWRVGLGSD-VAGGQTLDLFTVMATAVQVSKLrwryidqsekPLTMVEALYMATVGGGDF 365
Cdd:cd01292 208 llgRDGEGAEALRRLLELGIRVTLGTDgPPHPLGTDLLALLRLLLKVLRL----------GLSLEEALRLATINPARA 275
|
|
| PRK08203 |
PRK08203 |
hydroxydechloroatrazine ethylaminohydrolase; Reviewed |
22-362 |
1.42e-18 |
|
hydroxydechloroatrazine ethylaminohydrolase; Reviewed
Pssm-ID: 236184 [Multi-domain] Cd Length: 451 Bit Score: 87.21 E-value: 1.42e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2700908057 22 REGYLLCENG----LCAGfSETAPAGVEVLDYTGKIITPGLVDLHLHAPQYSYCG--TAMDLELLDWLQqytypeeAHYa 95
Cdd:PRK08203 22 ADGGLVVEGGriveVGPG-GALPQPADEVFDARGHVVTPGLVNTHHHFYQTLTRAlpAAQDAELFPWLT-------TLY- 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2700908057 96 dPTYARLGysyfvRDLKNSATTRA--------CIFATLH-----------TDATLELMHQLrgaGLSAFVGKLGMDRNS- 155
Cdd:PRK08203 93 -PVWARLT-----PEMVRVATQTAlaelllsgCTTSSDHhylfpnglrdaLDDQIEAAREI---GMRFHATRGSMSLGEs 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2700908057 156 -----PDSYREpSAAAGLAETRRWLDTcraentLH-AGP---VRPMITPRFTPSTSDEYMRGLGELAREYNVPAQSHLSE 226
Cdd:PRK08203 164 dgglpPDSVVE-DEDAILADSQRLIDR------YHdPGPgamLRIALAPCSPFSVSRELMRESAALARRLGVRLHTHLAE 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2700908057 227 NPGEIAWVAElcpgtKF------YGESYsryGLFGGGVptVMAHCIYSPDDEAALMKQNRVMIAHCPTSNENVIAGIAPA 300
Cdd:PRK08203 237 TLDEEAFCLE-----RFgmrpvdYLEDL---GWLGPDV--WLAHCVHLDDAEIARLARTGTGVAHCPCSNMRLASGIAPV 306
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2700908057 301 AHYLRGGWRVGLGSD-VAGGQTLDLFTVMATAVQVSKLRWRyidqsEKPLTMVEALYMATVGG 362
Cdd:PRK08203 307 RELRAAGVPVGLGVDgSASNDGSNLIGEARQALLLQRLRYG-----PDAMTAREALEWATLGG 364
|
|
| PRK06380 |
PRK06380 |
metal-dependent hydrolase; Provisional |
17-339 |
5.38e-17 |
|
metal-dependent hydrolase; Provisional
Pssm-ID: 180548 [Multi-domain] Cd Length: 418 Bit Score: 82.24 E-value: 5.38e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2700908057 17 DTLRVREGYLLCENGLCAGFSETAPAGVEVLDYTGKIITPGLVDLHLHAPQYSYCGTAMDLELLDWLQQyTYPEEAHYAD 96
Cdd:PRK06380 15 EKREILQGNVYIEGNKIVYVGDVNEEADYIIDATGKVVMPGLINTHAHVGMTASKGLFDDVDLEEFLMK-TFKYDSKRTR 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2700908057 97 P---TYARLGysyfVRDLKNSATTRaciFATLHTDATLeLMHQLRGAGLSAFVGKLGMDRNSPDSYREPsaaaglaetrr 173
Cdd:PRK06380 94 EgiyNSAKLG----MYEMINSGITA---FVDLYYSEDI-IAKAAEELGIRAFLSWAVLDEEITTQKGDP----------- 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2700908057 174 wLDTcrAENTL--HAGP--VRPMITPRFTPSTSDEYMRGLGELAREYNVPAQSHLSENPGEIAwvaelcPGTKFYG---- 245
Cdd:PRK06380 155 -LNN--AENFIreHRNEelVTPSIGVQGIYVANDETYLKAKEIAEKYDTIMHMHLSETRKEVY------DHVKRTGerpv 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2700908057 246 ESYSRYGLFGGGVptVMAHCIYSPDDEAALMKQNRVMIAHCPTSNENV-IAGIAPAAHYLRGGWRVGLGSDVAGG-QTLD 323
Cdd:PRK06380 226 EHLEKIGFLNSKL--IAAHCVWATYHEIKLLSKNGVKVSWNSVSNFKLgTGGSPPIPEMLDNGINVTIGTDSNGSnNSLD 303
|
330
....*....|....*..
gi 2700908057 324 LFTVMA-TAVQVSKLRW 339
Cdd:PRK06380 304 MFEAMKfSALSVKNERW 320
|
|
| Met_dep_hydrolase_D |
cd01312 |
Metallo-dependent hydrolases, subgroup D is part of the superfamily of metallo-dependent ... |
53-422 |
2.99e-16 |
|
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: 79.80 E-value: 2.99e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2700908057 53 IITPGLVDLHLHapqysycgtamdLELLDWLQQYTYPEeahyadptyarlgysyFVRDLKNSATTRACIFATLHTDATLE 132
Cdd:cd01312 28 VLLPGLINAHTH------------LEFSANVAQFTYGR----------------FRAWLLSVINSRDELLKQPWEEAIRQ 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2700908057 133 LMHQLRGAGLSAfVGKLGMDRNSPDSYRE---------------PSAAAGLAETrrWLDTCRAENTLHAGPVRPMITPRF 197
Cdd:cd01312 80 GIRQMLESGTTS-IGAISSDGSLLPALASsglrgvffnevigsnPSAIDFKGET--FLERFKRSKSFESQLFIPAISPHA 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2700908057 198 TPSTSDEYMRGLGELAREYNVPAQSHLSENPGEIAWVAELCPGTKFYGESY-------SRYG------LFGG-GVPTVMA 263
Cdd:cd01312 157 PYSVHPELAQDLIDLAKKLNLPLSTHFLESKEEREWLEESKGWFKHFWESFlklpkpkKLATaidfldMLGGlGTRVSFV 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2700908057 264 HCIYSPDDEAALMKQNRVMIAHCPTSNENVIAGIAPAAHYLRGGWRVGLGSD-VAGGQTLDLFtvmatavqvSKLRWRYI 342
Cdd:cd01312 237 HCVYANLEEAEILASRGASIALCPRSNRLLNGGKLDVSELKKAGIPVSLGTDgLSSNISLSLL---------DELRALLD 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2700908057 343 DQSEKPL--TMVEALYMATVGGGdfwADFGEKVGLFEDGYAFDALVLDddplknMRAFSAAERLERYAYLGKGKLTAKFA 420
Cdd:cd01312 308 LHPEEDLleLASELLLMATLGGA---RALGLNNGEIEAGKRADFAVFE------LPGPGIKEQAPLQFILHAKEVRHLFI 378
|
..
gi 2700908057 421 AG 422
Cdd:cd01312 379 SG 380
|
|
| PRK08204 |
PRK08204 |
hypothetical protein; Provisional |
1-362 |
5.30e-12 |
|
hypothetical protein; Provisional
Pssm-ID: 181288 [Multi-domain] Cd Length: 449 Bit Score: 67.33 E-value: 5.30e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2700908057 1 MNTFTLKGTFLDTPAPDTLRVREGYLLCENGLCAGFSETAPA-GVEVLDYTGKIITPGLVDLHLHAPQYSYCGTAMDLEL 79
Cdd:PRK08204 1 MKRTLIRGGTVLTMDPAIGDLPRGDILIEGDRIAAVAPSIEApDAEVVDARGMIVMPGLVDTHRHTWQSVLRGIGADWTL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2700908057 80 LDWLQQYTYPEEAHY-ADPTYA--RLGysyFVRDLkNSATTracifaTL-----------HTDATLELMHQlrgAGLSAf 145
Cdd:PRK08204 81 QTYFREIHGNLGPMFrPEDVYIanLLG---ALEAL-DAGVT------TLldwshinnspeHADAAIRGLAE---AGIRA- 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2700908057 146 VGKLGMDRNSPDSYRE--PSAAAGLAETR-RWLDtcRAENTLHAG-PVRpmiTPRFTpstSDEYMRGLGELAREYNVPAQ 221
Cdd:PRK08204 147 VFAHGSPGPSPYWPFDsvPHPREDIRRVKkRYFS--SDDGLLTLGlAIR---GPEFS---SWEVARADFRLARELGLPIS 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2700908057 222 SHLS-----ENPGEIAWVAELcpgtkfygesysryGLFGGGvpTVMAHCIYSPDDEAALMKQNRVMIAHCPTSNENVIAG 296
Cdd:PRK08204 219 MHQGfgpwgATPRGVEQLHDA--------------GLLGPD--LNLVHGNDLSDDELKLLADSGGSFSVTPEIEMMMGHG 282
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2700908057 297 IAPAAHYLRGGWRVGLGSDVAGGQTLDLFTVMATAVQVSK-------LRWRYIDQSEKPLTMVEALYMATVGG 362
Cdd:PRK08204 283 YPVTGRLLAHGVRPSLGVDVVTSTGGDMFTQMRFALQAERardnavhLREGGMPPPRLTLTARQVLEWATIEG 355
|
|
| HutI |
COG1228 |
Imidazolonepropionase or related amidohydrolase [Secondary metabolites biosynthesis, transport ... |
21-397 |
4.51e-11 |
|
Imidazolonepropionase or related amidohydrolase [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 440841 [Multi-domain] Cd Length: 386 Bit Score: 64.21 E-value: 4.51e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2700908057 21 VREGYLLCENG----LCAGFSETAPAGVEVLDYTGKIITPGLVDLHLHAPQYSYCGTAMDLELLDWLQQYTYPEEAHYAD 96
Cdd:COG1228 26 IENGTVLVEDGkiaaVGPAADLAVPAGAEVIDATGKTVLPGLIDAHTHLGLGGGRAVEFEAGGGITPTVDLVNPADKRLR 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2700908057 97 pTYARLGYSYfVRDLKNSATT-RACIFATLHTDATLELMHQlRGAGLSAFVGKlgmdrnspdsyrepsAAAGLAETRRWL 175
Cdd:COG1228 106 -RALAAGVTT-VRDLPGGPLGlRDAIIAGESKLLPGPRVLA-AGPALSLTGGA---------------HARGPEEARAAL 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2700908057 176 DTCRAENT----LHAGPVRPMITPrftpstsdEYMRGLGELAREYNVPAQSHlSENPGEIAWVAELcpgtkfygesysry 251
Cdd:COG1228 168 RELLAEGAdyikVFAEGGAPDFSL--------EELRAILEAAHALGLPVAAH-AHQADDIRLAVEA-------------- 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2700908057 252 glfggGVPTVmAHCIYSPDDEAALMKQNRVMIAhCPT------------------SNENVIAGIAPAAHYLRGGWRVGLG 313
Cdd:COG1228 225 -----GVDSI-EHGTYLDDEVADLLAEAGTVVL-VPTlslflallegaaapvaakARKVREAALANARRLHDAGVPVALG 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2700908057 314 SDVAGGQT--LDLFTVMATAVQVSklrwryidqsekpLTMVEALYMATVGGGDFWaDFGEKVGLFEDGYAFDALVLDDDP 391
Cdd:COG1228 298 TDAGVGVPpgRSLHRELALAVEAG-------------LTPEEALRAATINAAKAL-GLDDDVGSLEPGKLADLVLLDGDP 363
|
....*.
gi 2700908057 392 LKNMRA 397
Cdd:COG1228 364 LEDIAY 369
|
|
| PRK07203 |
PRK07203 |
putative aminohydrolase SsnA; |
45-392 |
1.15e-10 |
|
putative aminohydrolase SsnA;
Pssm-ID: 235963 [Multi-domain] Cd Length: 442 Bit Score: 63.03 E-value: 1.15e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2700908057 45 EVLDYTGKIITPGLVDLHLHApqYSYC--GTAMD----------LELLDWLQQYTYPEEAHYADptyarlGYSYFVRDLK 112
Cdd:PRK07203 48 EFIDAKGKLIMPGLINSHNHI--YSGLarGMMANippppdfisiLKNLWWRLDRALTLEDVYYS------ALICSLEAIK 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2700908057 113 NSATTracIF----ATLHTDATLElmhQLRGAGLSafVGKLGM------DRNSpdsyrEPSAAAGLAETRRWLDTCRAEN 182
Cdd:PRK07203 120 NGVTT---VFdhhaSPNYIGGSLF---TIADAAKK--VGLRAMlcyetsDRDG-----EKELQEGVEENIRFIKHIDEAK 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2700908057 183 T--------LHAGpvrpmitprFTpsTSDEYMRGLGELAREYNVPAQSHLSENPgeiawvAELCPGTKFYG----ESYSR 250
Cdd:PRK07203 187 DdmveamfgLHAS---------FT--LSDATLEKCREAVKETGRGYHIHVAEGI------YDVSDSHKKYGkdivERLAD 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2700908057 251 YGLFGGgvPTVMAHCIYSPDDEAALMKQNRVMIAHCPTSNENVIAGIAPAAHYLRGGWRVGLGSDvagGQTLDLFTVMAT 330
Cdd:PRK07203 250 FGLLGE--KTLAAHCIYLSDEEIDLLKETDTFVVHNPESNMGNAVGYNPVLEMIKNGILLGLGTD---GYTSDMFESYKV 324
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2700908057 331 AVQVSKlrwryidQSEKPLTM--VEALYMAtvgggdFWAD-------FGEKVGLFEDGYAFDALVLDDDPL 392
Cdd:PRK07203 325 ANFKHK-------HAGGDPNVgwPESPAML------FENNnkiaeryFGAKFGILEEGAKADLIIVDYNPP 382
|
|
| PRK06151 |
PRK06151 |
N-ethylammeline chlorohydrolase; Provisional |
45-395 |
2.72e-09 |
|
N-ethylammeline chlorohydrolase; Provisional
Pssm-ID: 180428 [Multi-domain] Cd Length: 488 Bit Score: 58.90 E-value: 2.72e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2700908057 45 EVLDYTGKIITPGLVDLHLHAPQYSYC-------GTAM-DLELLDWLQQ-----YTYPEEAHYADPTYARLgysyfvrdL 111
Cdd:PRK06151 46 RVIDAGNALVGPGFIDLDALSDLDTTIlgldngpGWAKgRVWSRDYVEAgrremYTPEELAFQKRYAFAQL--------L 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2700908057 112 KNSATTRACIFATLH-----TDATLELMHQLRGA-GLSAFVG---KLGMDRNSPDSYREP--SAAAGLAETRRWLDTCRA 180
Cdd:PRK06151 118 RNGITTAMPIASLFYrqwaeTYAEFAAAAEAAGRlGLRVYLGpayRSGGSVLEADGSLEVvfDEARGLAGLEEAIAFIKR 197
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2700908057 181 ENTLHAGPVRPMITPRFTPSTSDEYMRGLGELAREYNVPAQSHLSENPGEIAWVAELCPGTKFygESYSRYGLFG----- 255
Cdd:PRK06151 198 VDGAHNGLVRGMLAPDRIETCTVDLLRRTAAAARELGCPVRLHCAQGVLEVETVRRLHGTTPL--EWLADVGLLGprlli 275
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2700908057 256 --GGVPTVMAHCIYSPDDEAALMKQNRVMIAHCPTsnenVIAGIAPA----AHYLRGGWRVGLGSDVAggqTLDLFTVMA 329
Cdd:PRK06151 276 phATYISGSPRLNYSGGDDLALLAEHGVSIVHCPL----VSARHGSAlnsfDRYREAGINLALGTDTF---PPDMVMNMR 348
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2700908057 330 TAVQVSKLrwryidqSEKPLTMVEA--LY-MATVGGGDFwadFGEK-VGLFEDGYAFDALVLD---------DDPLKNM 395
Cdd:PRK06151 349 VGLILGRV-------VEGDLDAASAadLFdAATLGGARA---LGRDdLGRLAPGAKADIVVFDldglhmgpvFDPIRTL 417
|
|
| Met_dep_hydrolase_E |
cd01313 |
Metallo-dependent hydrolases, subgroup D is part of the superfamily of metallo-dependent ... |
166-392 |
1.06e-08 |
|
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: 1.06e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2700908057 166 AGLAETRRWLDTCRAENTLHAGpVRPMITPRFTPSTSDEYMRGLGELAREyNVPAQSHLSENPGEIawvaELCPGTKFYG 245
Cdd:cd01313 170 NGYEDFLGLLEKALRAVKEHAA-ARIGVAPHSLRAVPAEQLAALAALASE-KAPVHIHLAEQPKEV----DDCLAAHGRR 243
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2700908057 246 ESYSRYGLFGGGVPTVMAHCIYSPDDEAALMKQNRVMIAHCPTSNENVIAGIAPAAHYLRGGWRVGLGSDvaGGQTLDLf 325
Cdd:cd01313 244 PVELLLDHGHLDARWCLVHATHLTDNETLLLGRSGAVVGLCPTTEANLGDGIFPAAALLAAGGRIGIGSD--SNARIDL- 320
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2700908057 326 tvmatavqVSKLRW-----RYIDQSEKPLTMV-----EALY-MATVGGGdfwADFGEKVGLFEDGYAFDALVLD-DDPL 392
Cdd:cd01313 321 --------LEELRQleysqRLRDRARNVLATAggssaRALLdAALAGGA---QALGLATGALEAGARADLLSLDlDHPS 388
|
|
| PRK12393 |
PRK12393 |
amidohydrolase; Provisional |
39-315 |
1.51e-08 |
|
amidohydrolase; Provisional
Pssm-ID: 237088 [Multi-domain] Cd Length: 457 Bit Score: 56.61 E-value: 1.51e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2700908057 39 TAPAGVEVLDYTGKIITPGLVDLHLHAPQYSYCG--TAMDLELLDWLQQYTYPEEAHYaDP----TYARLGysyFVRDLK 112
Cdd:PRK12393 42 TPLPGERVIDATDCVVYPGWVNTHHHLFQSLLKGvpAGINQSLTAWLAAVPYRFRARF-DEdlfrLAARIG---LVELLR 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2700908057 113 NSATTRA----CIFATLHTDATLELMHQLRGAGLSAFVGKLGMDRNSPDSYREPSAAAGLAETRRWLDTCRAENTLH-AG 187
Cdd:PRK12393 118 SGCTTVAdhhyLYHPGMPFDTGDILFDEAEALGMRFVLCRGGATQTRGDHPGLPTALRPETLDQMLADVERLVSRYHdAS 197
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2700908057 188 PV---RPMITPRfTP--STSDEYMRGLGELAREYNVPAQSHLSENPGEIAWVAEL--CPGTKFYGEsysrYGLFGGGVpt 260
Cdd:PRK12393 198 PDslrRVVVAPT-TPtfSLPPELLREVARAARGMGLRLHSHLSETVDYVDFCREKygMTPVQFVAE----HDWLGPDV-- 270
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 2700908057 261 VMAHCIYSPDDEAALMKQNRVMIAHCPTSNENVIAGIAPAAHYLRGGWRVGLGSD 315
Cdd:PRK12393 271 WFAHLVKLDAEEIALLAQTGTGIAHCPQSNGRLGSGIAPALAMEAAGVPVSLGVD 325
|
|
| archeal_chlorohydrolases |
cd01305 |
Predicted chlorohydrolases. These metallo-dependent hydrolases from archea are part of the ... |
259-365 |
4.21e-08 |
|
Predicted chlorohydrolases. These metallo-dependent hydrolases from archea are part of the superfamily of metallo-dependent hydrolases, a large group of proteins that show conservation in their 3-dimensional fold (TIM barrel) and in details of their active site. They have a conserved metal binding site, involving four histidines and one aspartic acid residue. In the common reaction mechanism, the metal ion (or ions) deprotonate a water molecule for a nucleophilic attack on the substrate. Some members of this subgroup are predicted to be chlorohyrolases.
Pssm-ID: 238630 [Multi-domain] Cd Length: 263 Bit Score: 53.94 E-value: 4.21e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2700908057 259 PTVMAHCIYSPDDEAALMKQNRVMIAHCPTSNENVIAGIAPAAHYLRGGWRVGLGSDVAGGQTLDLFTVMATAVQVSKLr 338
Cdd:cd01305 165 PDLLVHGTHLTDEDLELVRENGVPVVLCPRSNLYFGVGIPPVAELLKLGIKVLLGTDNVMVNEPDMWAEMEFLAKYSRL- 243
|
90 100
....*....|....*....|....*..
gi 2700908057 339 wryidqsEKPLTMVEALYMATVGGGDF 365
Cdd:cd01305 244 -------QGYLSPLEILRMATVNAAEF 263
|
|
| PRK08418 |
PRK08418 |
metal-dependent hydrolase; |
195-290 |
2.49e-07 |
|
metal-dependent hydrolase;
Pssm-ID: 181419 [Multi-domain] Cd Length: 408 Bit Score: 52.66 E-value: 2.49e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2700908057 195 PRFTP--------STSDEYMRGLGELAREYNVPAQSHLSENPGEIAWVAElcpGTKFYGESYSRY--------------G 252
Cdd:PRK08418 173 KKFIPaiaihspySVHPILAKKALQLAKKENLLVSTHFLESKAEREWLEE---SKGWFKKFFEKFlkepkplytpkeflE 249
|
90 100 110
....*....|....*....|....*....|....*...
gi 2700908057 253 LFGGgVPTVMAHCIYSPDDEAALMKQNRVMIAHCPTSN 290
Cdd:PRK08418 250 LFKG-LRTLFTHCVYASEEELEKIKSKNASITHCPFSN 286
|
|
| NagA |
COG1820 |
N-acetylglucosamine-6-phosphate deacetylase [Carbohydrate transport and metabolism]; |
21-64 |
4.33e-07 |
|
N-acetylglucosamine-6-phosphate deacetylase [Carbohydrate transport and metabolism];
Pssm-ID: 441425 [Multi-domain] Cd Length: 373 Bit Score: 51.64 E-value: 4.33e-07
10 20 30 40
....*....|....*....|....*....|....*....|....
gi 2700908057 21 VREGYLLCENGLCAGFSETAPAGVEVLDYTGKIITPGLVDLHLH 64
Cdd:COG1820 14 LEDGALLIEDGRIAAIGPGAEPDAEVIDLGGGYLAPGFIDLHVH 57
|
|
| PRK07213 |
PRK07213 |
chlorohydrolase; Provisional |
6-394 |
5.27e-07 |
|
chlorohydrolase; Provisional
Pssm-ID: 235969 [Multi-domain] Cd Length: 375 Bit Score: 51.19 E-value: 5.27e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2700908057 6 LKGTFLdtpAPDTLRVREGYLLCENGLCAGFSETAPAGvEVLDYTGKIItPGLVDLHLHAPQYSYCGTAMDLELLDWLQ- 84
Cdd:PRK07213 5 LNGNFL---YGEDFEPKKGNLVIEDGIIKGFTNEVHEG-NVIDAKGLVI-PPLINAHTHIGDSSIKDIGIGKSLDELVKp 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2700908057 85 ----QYTYPEEAHYADPTYA-RLGysyfVRDLKNSATTRACIFatlhTDATLELMHQLRGAGLSAFVGKLGMDRNSPDSY 159
Cdd:PRK07213 80 pnglKHKFLNSCSDKELVEGmKEG----LYDMYNNGIKAFCDF----REGGIKGINLLKKASSDLPIKPIILGRPTEADE 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2700908057 160 REPSAaaglaETRRWLDTCRAentlhagpvrpmitprFTPSTSDEY----MRGLGELAREYNVPAQSHLSENPGEIAWva 235
Cdd:PRK07213 152 NELKK-----EIREILKNSDG----------------IGLSGANEYsdeeLKFICKECKREKKIFSIHAAEHKGSVEY-- 208
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2700908057 236 elcpGTKFYGESYSRYGLFGGGVPTVMAHCIYSPDDEAALMKQNRVMIAHCPTSNENVIAGIAPAAHYLRGGWRVGLGSD 315
Cdd:PRK07213 209 ----SLEKYGMTEIERLINLGFKPDFIVHATHPSNDDLELLKENNIPVVVCPRANASFNVGLPPLNEMLEKGILLGIGTD 284
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2700908057 316 VAGGQTLDLFTVMATAVQVSKlrwryidqsekpLTMVEALYMATVGGGDFWADfgEKVGLFEDGYAFDALVLDDDPLKN 394
Cdd:PRK07213 285 NFMANSPSIFREMEFIYKLYH------------IEPKEILKMATINGAKILGL--INVGLIEEGFKADFTFIKPTNIKF 349
|
|
| PhnM |
COG3454 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate diphosphatase PhnM [Inorganic ion transport ... |
20-62 |
1.68e-05 |
|
Alpha-D-ribose 1-methylphosphonate 5-triphosphate diphosphatase PhnM [Inorganic ion transport and metabolism];
Pssm-ID: 442677 Cd Length: 383 Bit Score: 46.67 E-value: 1.68e-05
10 20 30 40
....*....|....*....|....*....|....*....|...
gi 2700908057 20 RVREGYLLCENGLCAGFSETAPAGVEVLDYTGKIITPGLVDLH 62
Cdd:COG3454 17 EVIDGSVVIEDGRIAAIDEGASAAPGAIDAEGDYLLPGLVDLH 59
|
|
| PRK09237 |
PRK09237 |
amidohydrolase/deacetylase family metallohydrolase; |
39-69 |
1.09e-04 |
|
amidohydrolase/deacetylase family metallohydrolase;
Pssm-ID: 236423 [Multi-domain] Cd Length: 380 Bit Score: 44.07 E-value: 1.09e-04
10 20 30
....*....|....*....|....*....|.
gi 2700908057 39 TAPAGVEVLDYTGKIITPGLVDLHLHAPQYS 69
Cdd:PRK09237 36 DGSQAKKVIDLSGLYVSPGWIDLHVHVYPGS 66
|
|
| pyrC |
PRK09357 |
dihydroorotase; Validated |
26-64 |
1.44e-04 |
|
dihydroorotase; Validated
Pssm-ID: 236479 [Multi-domain] Cd Length: 423 Bit Score: 43.65 E-value: 1.44e-04
10 20 30 40
....*....|....*....|....*....|....*....|
gi 2700908057 26 LLCENGLCAGFSET-APAGVEVLDYTGKIITPGLVDLHLH 64
Cdd:PRK09357 22 VLIDDGKIAAIGENiEAEGAEVIDATGLVVAPGLVDLHVH 61
|
|
| Met_dep_hydrolase_B |
cd01307 |
Metallo-dependent hydrolases, subgroup B is part of the superfamily of metallo-dependent ... |
26-69 |
1.59e-04 |
|
Metallo-dependent hydrolases, subgroup B 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: 238632 [Multi-domain] Cd Length: 338 Bit Score: 43.47 E-value: 1.59e-04
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 2700908057 26 LLCENGLCA--GFSETAPAGVEVLDYTGKIITPGLVDLHLHAPQYS 69
Cdd:cd01307 2 VAIENGKIAavGAALAAPAATQIVDAGGCYVSPGWIDLHVHVYQGG 47
|
|
| Imidazolone-5PH |
cd01296 |
Imidazolonepropionase/imidazolone-5-propionate hydrolase (Imidazolone-5PH) catalyzes the third ... |
40-388 |
1.80e-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: 43.40 E-value: 1.80e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2700908057 40 APAGVEVLDYTGKIITPGLVDLHLHApqySYCGTAMDlELLDWLQQYTYPEEAHyadptyARLGYSYFVRDlknsatTRA 119
Cdd:cd01296 21 GPAAAEEIDAGGRAVTPGLVDCHTHL---VFAGDRVD-EFAARLAGASYEEILA------AGGGILSTVRA------TRA 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2700908057 120 CIFATLHTDATLELMHQLRgAGLSAFVGKLGMDRNSPDSYREPSAAAGLAETRRwLDTCraeNTLHAGPVRPmitPRFTP 199
Cdd:cd01296 85 ASEDELFASALRRLARMLR-HGTTTVEVKSGYGLDLETELKMLRVIRRLKEEGP-VDLV---STFLGAHAVP---PEYKG 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2700908057 200 StsDEYMRG-----LGELAREYNVPAQSHLSE----NPGEIAWV----AELCPGTKFYGESYSRyglfGGGV-------P 259
Cdd:cd01296 157 R--EEYIDLvieevLPAVAEENLADFCDVFCEkgafSLEQSRRIleaaKEAGLPVKIHADELSN----IGGAelaaelgA 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2700908057 260 TVMAHCIYSPDDEAALMKQNRVMIAHCPTSNENVIAGIAPAAHYLRGGWRVGLGSDVAGGQ--TLDLFTVMATAVQVSKl 337
Cdd:cd01296 231 LSADHLEHTSDEGIAALAEAGTVAVLLPGTAFSLRETYPPARKLIDAGVPVALGTDFNPGSspTSSMPLVMHLACRLMR- 309
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....
gi 2700908057 338 rwryidqsekpLTMVEALYMATVGGgdfwA---DFGEKVGLFEDGYAFDALVLD 388
Cdd:cd01296 310 -----------MTPEEALTAATINA----AaalGLGETVGSLEVGKQADLVILD 348
|
|
| PRK09061 |
PRK09061 |
D-glutamate deacylase; Validated |
31-250 |
1.88e-04 |
|
D-glutamate deacylase; Validated
Pssm-ID: 236369 [Multi-domain] Cd Length: 509 Bit Score: 43.53 E-value: 1.88e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2700908057 31 GLCAGFSETAPAGVEVLDYTGKIITPGLVDLHLHA---PQYSYcgTAMD-----LElldwLQQYTYPEEAHYADPTYARL 102
Cdd:PRK09061 46 GKIAAVGTAAIEGDRTIDATGLVVAPGFIDLHAHGqsvAAYRM--QAFDgvttaLE----LEAGVLPVARWYAEQAGEGR 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2700908057 103 GYSYFvrdlknsattraciFATLHTDATLELMHQLRGAGLSAFVGKLgMDRNspdsyREPSAAAGLAETRRWLDtcRAEN 182
Cdd:PRK09061 120 PLNYG--------------ASVGWTPARIAVLTGPQAEGTIADFGKA-LGDP-----RWQERAATPAELAEILE--LLEQ 177
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2700908057 183 TLHAGPVRPMITPRFTPSTSDEYMRGLGELAREYNVPAQSHlsenpgeIAWVAELCPGTKFygESYSR 250
Cdd:PRK09061 178 GLDEGALGIGIGAGYAPGTGHKEYLELARLAARAGVPTYTH-------VRYLSNVDPRSSV--DAYQE 236
|
|
| AllB |
COG0044 |
Dihydroorotase or related cyclic amidohydrolase [Nucleotide transport and metabolism]; ... |
20-64 |
1.94e-04 |
|
Dihydroorotase or related cyclic amidohydrolase [Nucleotide transport and metabolism]; Dihydroorotase or related cyclic amidohydrolase is part of the Pathway/BioSystem: Pyrimidine biosynthesis
Pssm-ID: 439814 [Multi-domain] Cd Length: 439 Bit Score: 43.54 E-value: 1.94e-04
10 20 30 40
....*....|....*....|....*....|....*....|....*..
gi 2700908057 20 RVREGYLLCENGLCAGFSE--TAPAGVEVLDYTGKIITPGLVDLHLH 64
Cdd:COG0044 12 GLERADVLIEDGRIAAIGPdlAAPEAAEVIDATGLLVLPGLIDLHVH 58
|
|
| PRK04250 |
PRK04250 |
dihydroorotase; Provisional |
20-64 |
2.29e-04 |
|
dihydroorotase; Provisional
Pssm-ID: 235265 [Multi-domain] Cd Length: 398 Bit Score: 43.22 E-value: 2.29e-04
10 20 30 40
....*....|....*....|....*....|....*....|....*
gi 2700908057 20 RVREGYLLCENGLCAGFSETAPAGVEVLDYTGKIITPGLVDLHLH 64
Cdd:PRK04250 11 RIVEGGIGIENGRISKISLRDLKGKEVIKVKGGIILPGLIDVHVH 55
|
|
| Met_dep_hydrolase_C |
cd01309 |
Metallo-dependent hydrolases, subgroup C is part of the superfamily of metallo-dependent ... |
35-65 |
2.45e-04 |
|
Metallo-dependent hydrolases, subgroup C 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: 238634 [Multi-domain] Cd Length: 359 Bit Score: 43.07 E-value: 2.45e-04
10 20 30
....*....|....*....|....*....|.
gi 2700908057 35 GFSETAPAGVEVLDYTGKIITPGLVDLHLHA 65
Cdd:cd01309 8 GAEITTPADAEVIDAKGKHVTPGLIDAHSHL 38
|
|
| NagA |
cd00854 |
N-acetylglucosamine-6-phosphate deacetylase, NagA, catalyzes the hydrolysis of the N-acetyl ... |
21-64 |
5.58e-04 |
|
N-acetylglucosamine-6-phosphate deacetylase, NagA, catalyzes the hydrolysis of the N-acetyl group of N-acetyl-glucosamine-6-phosphate (GlcNAc-6-P) to glucosamine 6-phosphate and acetate. This is the first committed step in the biosynthetic pathway to amino-sugar-nucleotides, which is needed for cell wall peptidoglycan and teichoic acid biosynthesis. Deacetylation of N-acetylglucosamine is also important in lipopolysaccharide synthesis and cell wall recycling.
Pssm-ID: 238434 [Multi-domain] Cd Length: 374 Bit Score: 41.80 E-value: 5.58e-04
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 2700908057 21 VREGYLLCENGLCA--GFSETAPAGVEVLDYTGKIITPGLVDLHLH 64
Cdd:cd00854 14 LEDGAVLVEDGKIVaiGPEDELEEADEIIDLKGQYLVPGFIDIHIH 59
|
|
| PRK15446 |
PRK15446 |
phosphonate metabolism protein PhnM; Provisional |
20-62 |
6.72e-04 |
|
phosphonate metabolism protein PhnM; Provisional
Pssm-ID: 237967 [Multi-domain] Cd Length: 383 Bit Score: 41.70 E-value: 6.72e-04
10 20 30 40
....*....|....*....|....*....|....*....|...
gi 2700908057 20 RVREGYLLCENGLCAGFSETAPAGVEVLDYTGKIITPGLVDLH 62
Cdd:PRK15446 16 EVVDGSLLIEDGRIAAIDPGASALPGAIDAEGDYLLPGLVDLH 58
|
|
| COG3964 |
COG3964 |
Predicted amidohydrolase [General function prediction only]; |
40-64 |
7.71e-04 |
|
Predicted amidohydrolase [General function prediction only];
Pssm-ID: 443164 [Multi-domain] Cd Length: 376 Bit Score: 41.31 E-value: 7.71e-04
10 20
....*....|....*....|....*
gi 2700908057 40 APAGVEVLDYTGKIITPGLVDLHLH 64
Cdd:COG3964 38 AAEAKKVIDASGLYVTPGLIDLHTH 62
|
|
| D-HYD |
cd01314 |
D-hydantoinases (D-HYD) also called dihydropyrimidases (DHPase) and related proteins; DHPases ... |
26-64 |
1.47e-03 |
|
D-hydantoinases (D-HYD) also called dihydropyrimidases (DHPase) and related proteins; DHPases are a family of enzymes that catalyze the reversible hydrolytic ring opening of the amide bond in five- or six-membered cyclic diamides, like dihydropyrimidine or hydantoin. The hydrolysis of dihydropyrimidines is the second step of reductive catabolism of pyrimidines in human. The hydrolysis of 5-substituted hydantoins in microorganisms leads to enantiomerically pure N-carbamyl amino acids, which are used for the production of antibiotics, peptide hormones, pyrethroids, and pesticides. HYDs are classified depending on their stereoselectivity. This family also includes collapsin response regulators (CRMPs), cytosolic proteins involved in neuronal differentiation and axonal guidance which have strong homology to DHPases, but lack most of the active site residues.
Pssm-ID: 238639 [Multi-domain] Cd Length: 447 Bit Score: 40.66 E-value: 1.47e-03
10 20 30 40
....*....|....*....|....*....|....*....|.
gi 2700908057 26 LLCENGLCA--GFSETAPAGVEVLDYTGKIITPGLVDLHLH 64
Cdd:cd01314 19 ILIEDGKIVaiGPNLEAPGGVEVIDATGKYVLPGGIDPHTH 59
|
|
| L-HYD_ALN |
cd01315 |
L-Hydantoinases (L-HYDs) and Allantoinase (ALN); L-Hydantoinases are a member of the ... |
21-64 |
4.39e-03 |
|
L-Hydantoinases (L-HYDs) and Allantoinase (ALN); L-Hydantoinases are a member of the dihydropyrimidinase family, which catalyzes the reversible hydrolytic ring opening of dihydropyrimidines and hydantoins (five-membered cyclic diamides used in biotechnology). But L-HYDs differ by having an L-enantio specificity and by lacking activity on possible natural substrates such as dihydropyrimidines. Allantoinase catalyzes the hydrolytic cleavage of the five-member ring of allantoin (5-ureidohydantoin) to form allantoic acid.
Pssm-ID: 238640 [Multi-domain] Cd Length: 447 Bit Score: 39.19 E-value: 4.39e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 2700908057 21 VREGYLLCENGLCA--GFSETAPAGVEVLDYTGKIITPGLVDLHLH 64
Cdd:cd01315 15 VREADIAVKGGKIAaiGPDIANTEAEEVIDAGGLVVMPGLIDTHVH 60
|
|
| Met_dep_hydrolase_A |
cd01299 |
Metallo-dependent hydrolases, subgroup A is part of the superfamily of metallo-dependent ... |
44-397 |
5.83e-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: 38.43 E-value: 5.83e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2700908057 44 VEVLDYTGKIITPGLVDLHLHApqySYCGTAMDLELLDWLQQYTYpEEAHYADpTYARLGYSYfVRDL--KNSATTRACI 121
Cdd:cd01299 1 AQVIDLGGKTLMPGLIDAHTHL---GSDPGDLPLDLALPVEYRTI-RATRQAR-AALRAGFTT-VRDAggADYGLLRDAI 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2700908057 122 fatlhtDATLELMHQLRGAG--LSAFVGKLGMDRNSPDSYREPSAA--AGLAETRRwldtcRAENTLHAGP--------- 188
Cdd:cd01299 75 ------DAGLIPGPRVFASGraLSQTGGHGDPRGLSGLFPAGGLAAvvDGVEEVRA-----AVREQLRRGAdqikimatg 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2700908057 189 -VRPMITPRFTPSTSDEYMRGLGELAREYNVPAQSHLSENPGEIAWVAelcpgtkfygesysryglfgGGVPTVMaHCIY 267
Cdd:cd01299 144 gVLSPGDPPPDTQFSEEELRAIVDEAHKAGLYVAAHAYGAEAIRRAIR--------------------AGVDTIE-HGFL 202
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2700908057 268 SPDDEAALMKQNRVMIAHCPTSNENVI---------------------AGIAPAAHYLRGGWRVGLGSDVaggqtldLFT 326
Cdd:cd01299 203 IDDETIELMKEKGIFLVPTLATYEALAaegaapglpadsaekvalvleAGRDALRRAHKAGVKIAFGTDA-------GFP 275
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2700908057 327 VMATAVQVSKLRWRyidqSEKPLTMVEALYMATVGGgdfWADFG--EKVGLFEDGYAFDALVLDDDPLKNMRA 397
Cdd:cd01299 276 VPPHGWNARELELL----VKAGGTPAEALRAATANA---AELLGlsDELGVIEAGKLADLLVVDGDPLEDIAV 341
|
|
| PRK09229 |
PRK09229 |
N-formimino-L-glutamate deiminase; Validated |
264-315 |
8.56e-03 |
|
N-formimino-L-glutamate deiminase; Validated
Pssm-ID: 236420 [Multi-domain] Cd Length: 456 Bit Score: 38.29 E-value: 8.56e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 2700908057 264 HCIYSPDDEAALMKQNRVMIAHCPTSNENVIAGIAPAAHYLRGGWRVGLGSD 315
Cdd:PRK09229 271 HATHLTDAETARLARSGAVAGLCPTTEANLGDGIFPAVDYLAAGGRFGIGSD 322
|
|
| Amidohydro_3 |
pfam07969 |
Amidohydrolase family; |
45-393 |
9.34e-03 |
|
Amidohydrolase family;
Pssm-ID: 400360 [Multi-domain] Cd Length: 464 Bit Score: 38.28 E-value: 9.34e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2700908057 45 EVLDYTGKIITPGLVDLHLHApqysyCGTAMDLELLDW---LQQYTYPEEAHYADPTYARLGYSYfvrDLKNSATTRACI 121
Cdd:pfam07969 1 EVIDAKGRLVLPGFVDPHTHL-----DGGGLNLRELRLpdvLPNAVVKGQAGRTPKGRWLVGEGW---DEAQFAETRFPY 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2700908057 122 fATLHTDATLE--LMHQLRGAGLSAFVGKLGMDRNSpdsYREPSAAAGLAETRRWLDTCRAENTLHAGPVRPMitprfTP 199
Cdd:pfam07969 73 -ALADLDEVAPdgPVLLRALHTHAAVANSAALDLAG---ITKATEDPPGGEIARDANGEGLTGLLREGAYALP-----PL 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2700908057 200 STSDEYMRGLGELAREYN------VPAQSHLSENPGEIAWVAELCPGTK---------FYGESYSRYG-------LFGGG 257
Cdd:pfam07969 144 LAREAEAAAVAAALAALPgfgitsVDGGGGNVHSLDDYEPLRELTAAEKlkelldapeRLGLPHSIYElrigamkLFADG 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2700908057 258 VP---TVMAHCIYSP--------------------------------DDEAALM--------------KQNRVMIAHCPT 288
Cdd:pfam07969 224 VLgsrTAALTEPYFDapgtgwpdfedealaelvaaarergldvaihaIGDATIDtaldafeavaeklgNQGRVRIEHAQG 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2700908057 289 ------------SNENVIAGIAPAAHY------------------------LRGGWRVGLGSDvAGGQTLDLFTVMATAV 332
Cdd:pfam07969 304 vvpytysqiervAALGGAAGVQPVFDPlwgdwlqdrlgaerargltpvkelLNAGVKVALGSD-APVGPFDPWPRIGAAV 382
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2700908057 333 QVSKLRWRYIDQSEKPLTMVEALYMATVGGgdfWADFGE--KVGLFEDGYAFDALVLDDDPLK 393
Cdd:pfam07969 383 MRQTAGGGEVLGPDEELSLEEALALYTSGP---AKALGLedRKGTLGVGKDADLVVLDDDPLT 442
|
|
| |
