|
Name |
Accession |
Description |
Interval |
E-value |
| GDEase |
cd01303 |
Guanine deaminase (GDEase). Guanine deaminase is an aminohydrolase responsible for the ... |
7-446 |
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: 552.27 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1570042588 7 FHGTLIHSRSPADLAILENAVLVLEtDGRIAAIREDLPRGEVPKLLRTlriggDDHANVR-YLRRTEFLIPGFVDTHNHA 85
Cdd:cd01303 1 FRGTFIHTKSLPELELVEDALRVVE-DGLIVVVDGNIIAAGAAETLKR-----AAKPGARvIDSPNQFILPGFIDTHIHA 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1570042588 86 PQYAQRGLGQSMHILDWLEKVTFPNESRFSDPVYARRVYSRCVDGFLRQGITTASYYGSMHAEATKILADLCLEKGQRAF 165
Cdd:cd01303 75 PQYANIGSGLGEPLLDWLETYTFPEEAKFADPAYAREVYGRFLDELLRNGTTTACYFATIHPESTEALFEEAAKRGQRAI 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1570042588 166 VGKCNMNRNAPDYYRDESvESSLRDTEACITHIRGIDPegrLLKHVLTSRFAISCEDALLASLGEIAKRNGDLPIQTHMN 245
Cdd:cd01303 155 AGKVCMDRNAPEYYRDTA-ESSYRDTKRLIERWHGKSG---RVKPAITPRFAPSCSEELLAALGKLAKEHPDLHIQTHIS 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1570042588 246 EAKTEIEFTKTLFPGFANEVDLYAHFGLLTERSILAHCCYMSEYEMGRLKELGCGVAHCPVSNMTVGGGFMaaPVRDFLR 325
Cdd:cd01303 231 ENLDEIAWVKELFPGARDYLDVYDKYGLLTEKTVLAHCVHLSEEEFNLLKERGASVAHCPTSNLFLGSGLF--DVRKLLD 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1570042588 326 RGIKVGLGTDSGGGFSSSILEAMRQALIASNAREVMSqGRDKGLTIPEVFHLATLGGAKVCCLEDKIGSFEIGKEFDALL 405
Cdd:cd01303 309 AGIKVGLGTDVGGGTSFSMLDTLRQAYKVSRLLGYEL-GGHAKLSPAEAFYLATLGGAEALGLDDKIGNFEVGKEFDAVV 387
|
410 420 430 440
....*....|....*....|....*....|....*....|..
gi 1570042588 406 INADSTGVMT-MVEEEDSVRTIFDKFIMTGDDRNINEVYVRG 446
Cdd:cd01303 388 IDPSATPLLAdRMFRVESLEEALFKFLYLGDDRNIREVYVAG 429
|
|
| guan_deamin |
TIGR02967 |
guanine deaminase; This model describes guanine deaminase, which hydrolyzes guanine to ... |
20-446 |
1.62e-137 |
|
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: 400.48 E-value: 1.62e-137
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1570042588 20 LAILENAVLVLEtDGRIAAIredlprGEVPKLLRTLRIGG--DDHanvrylrRTEFLIPGFVDTHNHAPQYAQRGlGQSM 97
Cdd:TIGR02967 1 LEYFEDGLLVVE-NGRIVAV------GDYAELKETLPAGVeiDDY-------RGHLIMPGFIDTHIHYPQTEMIA-SYGE 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1570042588 98 HILDWLEKVTFPNESRFSDPVYARRVYSRCVDGFLRQGITTASYYGSMHAEATKILADLCLEKGQRAFVGKCNMNRNAPD 177
Cdd:TIGR02967 66 QLLEWLEKYTFPTEARFADPDHAEEVAEFFLDELLRNGTTTALVFATVHPESVDALFEAALKRGMRMIAGKVLMDRNAPD 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1570042588 178 YYRDeSVESSLRDTEACITHIRGidpEGRLLkHVLTSRFAISCEDALLASLGEIAKRNGDLPIQTHMNEAKTEIEFTKTL 257
Cdd:TIGR02967 146 YLRD-TAESSYDESKALIERWHG---KGRLL-YAVTPRFAPTSSPEQLAAAGELAKEYPDVYVQTHLSENKDEIAWVKEL 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1570042588 258 FPGFANEVDLYAHFGLLTERSILAHCCYMSEYEMGRLKELGCGVAHCPVSNMTVGGGFMaaPVRDFLRRGIKVGLGTDSG 337
Cdd:TIGR02967 221 FPEAKDYLDVYDHYGLLGRRSVFAHCIHLSDEECQRLAETGAAIAHCPTSNLFLGSGLF--NLKKALEHGVRVGLGTDVG 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1570042588 338 GGFSSSILEAMRQALIASNAREvmsqgrdKGLTIPEVFHLATLGGAKVCCLEDKIGSFEIGKEFDALLINADSTGVMTMV 417
Cdd:TIGR02967 299 GGTSFSMLQTLREAYKVSQLQG-------ARLSPFEAFYLATLGGARALDLDDRIGNFEPGKEADFVVLDPAATPLLALR 371
|
410 420 430
....*....|....*....|....*....|
gi 1570042588 418 -EEEDSVRTIFDKFIMTGDDRNINEVYVRG 446
Cdd:TIGR02967 372 fEGADTLEDKLFKLMYLGDDRNVAETYVAG 401
|
|
| PRK09228 |
PRK09228 |
guanine deaminase; Provisional |
5-452 |
1.05e-110 |
|
guanine deaminase; Provisional
Pssm-ID: 236419 [Multi-domain] Cd Length: 433 Bit Score: 333.31 E-value: 1.05e-110
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1570042588 5 LVFHGTLIHSRSPADLAILENAVLVLEtDGRIAAIredlprGEVPKLLRTLriggDDHANVRYLRrtEFLI-PGFVDTHN 83
Cdd:PRK09228 11 LHFTADPAEVDDEDALRYIEDGLLLVE-DGRIVAA------GPYAELRAQL----PADAEVTDYR--GKLIlPGFIDTHI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1570042588 84 HAPQ------YAQRglgqsmhILDWLEKVTFPNESRFSDPVYARRVYSRCVDGFLRQGITTASYYGSMHAEATKILADLC 157
Cdd:PRK09228 78 HYPQtdmiasYGEQ-------LLDWLNTYTFPEERRFADPAYAREVAEFFLDELLRNGTTTALVFGTVHPQSVDALFEAA 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1570042588 158 LEKGQRAFVGKCNMNRNAPDYYRDeSVESSLRDTEACIT--HIRGidpegRLLkHVLTSRFAISCEDALLASLGEIAKRN 235
Cdd:PRK09228 151 EARNMRMIAGKVLMDRNAPDGLRD-TAESGYDDSKALIErwHGKG-----RLL-YAITPRFAPTSTPEQLEAAGALAREH 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1570042588 236 GDLPIQTHMNEAKTEIEFTKTLFPGFANEVDLYAHFGLLTERSILAHCCYMSEYEMGRLKELGCGVAHCPVSNMTVGGGF 315
Cdd:PRK09228 224 PDVWIQTHLSENLDEIAWVKELFPEARDYLDVYERYGLLGPRAVFAHCIHLEDRERRRLAETGAAIAFCPTSNLFLGSGL 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1570042588 316 MaaPVRDFLRRGIKVGLGTDSGGGFSSSILEAMRQALiasnarEVMsQGRDKGLTIPEVFHLATLGGAKVCCLEDKIGSF 395
Cdd:PRK09228 304 F--DLKRADAAGVRVGLGTDVGGGTSFSMLQTMNEAY------KVQ-QLQGYRLSPFQAFYLATLGGARALGLDDRIGNL 374
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1570042588 396 EIGKEFDALLINADSTGVMTMVEEedSVRTIFDK---FIMTGDDRNINEVYVRGRLVKGG 452
Cdd:PRK09228 375 APGKEADFVVLDPAATPLLALRTA--RAESLEELlfaLMTLGDDRAVAETYVAGRPVYRR 432
|
|
| SsnA |
COG0402 |
Cytosine/adenosine deaminase or related metal-dependent hydrolase [Nucleotide transport and ... |
5-450 |
3.23e-110 |
|
Cytosine/adenosine deaminase or related metal-dependent hydrolase [Nucleotide transport and metabolism, General function prediction only]; Cytosine/adenosine deaminase or related metal-dependent hydrolase is part of the Pathway/BioSystem: Pyrimidine salvage
Pssm-ID: 440171 [Multi-domain] Cd Length: 416 Bit Score: 331.41 E-value: 3.23e-110
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1570042588 5 LVFHGTLIHSRSPADlAILENAVLVLEtDGRIAAIRedlPRGEVPKLLRTLR-IGGDDHAnvrylrrtefLIPGFVDTHN 83
Cdd:COG0402 2 LLIRGAWVLTMDPAG-GVLEDGAVLVE-DGRIAAVG---PGAELPARYPAAEvIDAGGKL----------VLPGLVNTHT 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1570042588 84 HAPQYAQRGLGQSMHILDWLEKVTFPNESRFsDPVYARRVYSRCVDGFLRQGITTASYYGSMHAEATKILADLCLEKGQR 163
Cdd:COG0402 67 HLPQTLLRGLADDLPLLDWLEEYIWPLEARL-DPEDVYAGALLALAEMLRSGTTTVADFYYVHPESADALAEAAAEAGIR 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1570042588 164 AFVGKCNMNRNAPDYYRdESVESSLRDTEACITHIRGidPEGRLLKHVLTSRFAISCEDALLASLGEIAKRNGdLPIQTH 243
Cdd:COG0402 146 AVLGRGLMDRGFPDGLR-EDADEGLADSERLIERWHG--AADGRIRVALAPHAPYTVSPELLRAAAALARELG-LPLHTH 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1570042588 244 MNEAKTEIEFTKTLFPgfANEVDLYAHFGLLTERSILAHCCYMSEYEMGRLKELGCGVAHCPVSNMTVGGGFmaAPVRDF 323
Cdd:COG0402 222 LAETRDEVEWVLELYG--KRPVEYLDELGLLGPRTLLAHCVHLTDEEIALLAETGASVAHCPTSNLKLGSGI--APVPRL 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1570042588 324 LRRGIKVGLGTDSGGGF-SSSILEAMRQALIASNARevmsQGRDKGLTIPEVFHLATLGGAKVCCLEDKIGSFEIGKEFD 402
Cdd:COG0402 298 LAAGVRVGLGTDGAASNnSLDMFEEMRLAALLQRLR----GGDPTALSAREALEMATLGGARALGLDDEIGSLEPGKRAD 373
|
410 420 430 440
....*....|....*....|....*....|....*....|....*...
gi 1570042588 403 ALLINADSTgvmTMVEEEDSVRTIfdkfIMTGDDRNINEVYVRGRLVK 450
Cdd:COG0402 374 LVVLDLDAP---HLAPLHDPLSAL----VYAADGRDVRTVWVAGRVVV 414
|
|
| ATZ_TRZ_like |
cd01298 |
TRZ/ATZ family contains enzymes from the atrazine degradation pathway and related hydrolases. ... |
22-449 |
1.19e-59 |
|
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: 200.51 E-value: 1.19e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1570042588 22 ILENAVLVLEtDGRIAAIREDLPRGEVPKLLRtlrIGGDDHanvrylrrteFLIPGFVDTHNHAPQYAQRGLGQSMHILD 101
Cdd:cd01298 16 VLEDGDVLVE-DGRIVAVGPALPLPAYPADEV---IDAKGK----------VVMPGLVNTHTHLAMTLLRGLADDLPLME 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1570042588 102 WLEKVTFPNESRFSDP-VYARRVYSrCVDgFLRQGITTASyygSMHAEATKILADLCLEKGQRAFVGKCNMNRNAPDYyr 180
Cdd:cd01298 82 WLKDLIWPLERLLTEEdVYLGALLA-LAE-MIRSGTTTFA---DMYFFYPDAVAEAAEELGIRAVLGRGIMDLGTEDV-- 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1570042588 181 dESVESSLRDTEACITHIRGidPEGRLLKHVLTSRFAISCEDALLASLGEIAKRNGdLPIQTHMNEAKTEIEFTKTLF-- 258
Cdd:cd01298 155 -EETEEALAEAERLIREWHG--AADGRIRVALAPHAPYTCSDELLREVAELAREYG-VPLHIHLAETEDEVEESLEKYgk 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1570042588 259 -PgfaneVDLYAHFGLLTERSILAHCCYMSEYEMGRLKELGCGVAHCPVSNMTVGGGFmaAPVRDFLRRGIKVGLGTDSG 337
Cdd:cd01298 231 rP-----VEYLEELGLLGPDVVLAHCVWLTDEEIELLAETGTGVAHNPASNMKLASGI--APVPEMLEAGVNVGLGTDGA 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1570042588 338 G-GFSSSILEAMRQALIASNAREvmsqGRDKGLTIPEVFHLATLGGAKVCCLeDKIGSFEIGKEFDALLINADStgvMTM 416
Cdd:cd01298 304 AsNNNLDMFEEMRLAALLQKLAH----GDPTALPAEEALEMATIGGAKALGL-DEIGSLEVGKKADLILIDLDG---PHL 375
|
410 420 430
....*....|....*....|....*....|...
gi 1570042588 417 VEEEDSVRTIFdkFIMTGDDrnINEVYVRGRLV 449
Cdd:cd01298 376 LPVHDPISHLV--YSANGGD--VDTVIVNGRVV 404
|
|
| PRK07228 |
PRK07228 |
5'-deoxyadenosine deaminase; |
18-411 |
4.63e-49 |
|
5'-deoxyadenosine deaminase;
Pssm-ID: 180895 [Multi-domain] Cd Length: 445 Bit Score: 173.65 E-value: 4.63e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1570042588 18 ADLAILENAVLVleTDGRIAAIREDLPRGEVPkllRTLRIGGDdhanvrylrrteFLIPGFVDTHNHAPQYAQRGLGQSM 97
Cdd:PRK07228 15 AKREIVDGDVLI--EDDRIAAVGDRLDLEDYD---DHIDATGK------------VVIPGLIQGHIHLCQTLFRGIADDL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1570042588 98 HILDWLEKVTFPNESRFSdpvyARRVYSRCVDGFL---RQGITTASYYGSM-HAEATKILAdlcLEKGQRAFVGKCNMN- 172
Cdd:PRK07228 78 ELLDWLKDRIWPLEAAHD----AESMYYSALLGIGeliESGTTTIVDMESVhHTDSAFEAA---GESGIRAVLGKVMMDy 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1570042588 173 -RNAPDYYRdESVESSLRDTEACITHIRGIDpEGRLlKHVLTSRFAISCEDALLASLGEIAKRNGdLPIQTHMNEAKTEI 251
Cdd:PRK07228 151 gDDVPEGLQ-EDTEASLAESVRLLEKWHGAD-NGRI-RYAFTPRFAVSCTEELLRGVRDLADEYG-VRIHTHASENRGEI 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1570042588 252 EFTKTLfPGFANeVDLYAHFGLLTERSILAHCCYMSEYEMGRLKELGCGVAHCPVSNMTVGGGFmaAPVRDFLRRGIKVG 331
Cdd:PRK07228 227 ETVEEE-TGMRN-IHYLDEVGLTGEDLILAHCVWLDEEEREILAETGTHVTHCPSSNLKLASGI--APVPDLLERGINVA 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1570042588 332 LGTDsgGGFSSSILEA---MRQALIASNAREVMSQgrdkGLTIPEVFHLATLGGAKVCCLEDKIGSFEIGKEFDALLINA 408
Cdd:PRK07228 303 LGAD--GAPCNNTLDPfteMRQAALIQKVDRLGPT----AMPARTVFEMATLGGAKAAGFEDEIGSLEEGKKADLAILDL 376
|
...
gi 1570042588 409 DST 411
Cdd:PRK07228 377 DGL 379
|
|
| PRK09045 |
PRK09045 |
TRZ/ATZ family hydrolase; |
10-402 |
8.32e-41 |
|
TRZ/ATZ family hydrolase;
Pssm-ID: 236366 [Multi-domain] Cd Length: 443 Bit Score: 151.22 E-value: 8.32e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1570042588 10 TLIHSR-----SPADlAILENAVLVLEtDGRIAAIredLPRGEVPKLLR-TLRIGGDDHAnvrylrrtefLIPGFVDTHN 83
Cdd:PRK09045 9 LLIEARwivpvEPAG-VVLEDHAVAIR-DGRIVAI---LPRAEARARYAaAETVELPDHV----------LIPGLINAHT 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1570042588 84 HAPQYAQRGLGQSMHILDWLEKVTFPNESRFSDPVYARrvysrcvDG-------FLRQGITTAS--YYgsmHAEATkilA 154
Cdd:PRK09045 74 HAAMSLLRGLADDLPLMTWLQDHIWPAEGAWVSEEFVR-------DGtllaiaeMLRGGTTCFNdmYF---FPEAA---A 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1570042588 155 DLCLEKGQRAFVG------KCNMNRNAPDYYRdesvesslrdteacithiRGIDPEGRLLKHVLTSrFAI------SCED 222
Cdd:PRK09045 141 EAAHQAGMRAQIGmpvldfPTAWASDADEYLA------------------KGLELHDQWRHHPLIS-TAFaphapyTVSD 201
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1570042588 223 ALLASLGEIAKRNgDLPIQTHMNEAKTEIEftktlfpgfaNEVDLY--------AHFGLLTERSILAHCCYMSEYEMGRL 294
Cdd:PRK09045 202 ENLERIRTLAEQL-DLPIHIHLHETAQEIA----------DSLKQHgqrplarlARLGLLGPRLIAVHMTQLTDAEIALL 270
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1570042588 295 KELGCGVAHCPVSNMTVGGGFmaAPVRDFLRRGIKVGLGTDsgGGFSSS---ILEAMRQALIASNArevmSQGRDKGLTI 371
Cdd:PRK09045 271 AETGCSVVHCPESNLKLASGF--CPVAKLLQAGVNVALGTD--GAASNNdldLFGEMRTAALLAKA----VAGDATALPA 342
|
410 420 430
....*....|....*....|....*....|.
gi 1570042588 372 PEVFHLATLGGAKVCCLEDKIGSFEIGKEFD 402
Cdd:PRK09045 343 HTALRMATLNGARALGLDDEIGSLEPGKQAD 373
|
|
| Amidohydro_1 |
pfam01979 |
Amidohydrolase family; This family of enzymes are a a large metal dependent hydrolase ... |
73-449 |
2.04e-37 |
|
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: 139.56 E-value: 2.04e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1570042588 73 FLIPGFVDTHNHAPQYAQRGLGQSMHILDWlekvtfpnesrfsdpvyarrVYSRCVDGFLRQGITTASYYGSMHAEATKI 152
Cdd:pfam01979 1 IVLPGLIDAHVHLEMGLLRGIPVPPEFAYE--------------------ALRLGITTMLKSGTTTVLDMGATTSTGIEA 60
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1570042588 153 LADLCLEK--GQRAFVGKCNMNRNAPDYYRDESVESSLRDTEA-CITHIRGIDPEgrllkhvLTSRFAISCEDALLASLG 229
Cdd:pfam01979 61 LLEAAEELplGLRFLGPGCSLDTDGELEGRKALREKLKAGAEFiKGMADGVVFVG-------LAPHGAPTFSDDELKAAL 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1570042588 230 EIAKRNgDLPIQTHMNEAKTEIEFTKTLFPG---FANEVDLYAHFGLLTE-RSILAHCCYMSEYEMGRLKE--LGCGVAH 303
Cdd:pfam01979 134 EEAKKY-GLPVAIHALETKGEVEDAIAAFGGgieHGTHLEVAESGGLLDIiKLILAHGVHLSPTEANLLAEhlKGAGVAH 212
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1570042588 304 CPVSNMTVGGGFMAapVRDFLRRGIKVGLGTDSGG-GFSSSILEAMRQALIASNAREVmsqgrdkGLTIPEVFHLATLGG 382
Cdd:pfam01979 213 CPFSNSKLRSGRIA--LRKALEDGVKVGLGTDGAGsGNSLNMLEELRLALELQFDPEG-------GLSPLEALRMATINP 283
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1570042588 383 AKVCCLEDKIGSFEIGKEFDALLINADstgvmtmveeedsvrtIFDKFIMTGDDRNINEVYVRGRLV 449
Cdd:pfam01979 284 AKALGLDDKVGSIEVGKDADLVVVDLD----------------PLAAFFGLKPDGNVKKVIVKGKIV 334
|
|
| PRK08393 |
PRK08393 |
N-ethylammeline chlorohydrolase; Provisional |
74-407 |
1.50e-28 |
|
N-ethylammeline chlorohydrolase; Provisional
Pssm-ID: 181411 [Multi-domain] Cd Length: 424 Bit Score: 116.82 E-value: 1.50e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1570042588 74 LIPGFVDTHNHAPQYAQRGLGQSMHILDWLEKVTFPNESRFSdpvyARRVYSRCVDGFL---RQGITT-ASYYGSMHAea 149
Cdd:PRK08393 52 VSPGFINAHTHSPMVLLRGLADDVPLMEWLQNYIWPRERKLK----RKDIYWGAYLGLLemiKSGTTTfVDMYFHMEE-- 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1570042588 150 tkiLADLCLEKGQRAFVGKCNMNRNAPdyyrdESVESSLRDTEACITHIRGIDPEgrLLKHVLTSRFAISCEDALLASLG 229
Cdd:PRK08393 126 ---VAKATLEVGLRGYLSYGMVDLGDE-----EKREKEIKETEKLMEFIEKLNSP--RVHFVFGPHAPYTCSLALLKWVR 195
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1570042588 230 EIAKRNGDLpIQTHMNEAKTEIEFTKTLFPgfANEVDLYAHFGLLTERSILAHCCYMSEYEMGRLKELGCGVAHCPVSNM 309
Cdd:PRK08393 196 EKAREWNKL-ITIHLSETMDEIKQIREKYG--KSPVVLLDEIGFLNEDVIAAHGVWLSSRDIRILASAGVTVAHNPASNM 272
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1570042588 310 TVGGGFMaaPVRDFLRRGIKVGLGTDsgGGFSSSILEAMRQALIASNAREVMSqgRDKGLTIPE-VFHLATLGGAKVCCL 388
Cdd:PRK08393 273 KLGSGVM--PLRKLLNAGVNVALGTD--GAASNNNLDMLREMKLAALLHKVHN--LDPTIADAEtVFRMATQNGAKALGL 346
|
330
....*....|....*....
gi 1570042588 389 edKIGSFEIGKEFDALLIN 407
Cdd:PRK08393 347 --KAGVIKEGYLADIAVID 363
|
|
| PRK08203 |
PRK08203 |
hydroxydechloroatrazine ethylaminohydrolase; Reviewed |
28-402 |
2.85e-28 |
|
hydroxydechloroatrazine ethylaminohydrolase; Reviewed
Pssm-ID: 236184 [Multi-domain] Cd Length: 451 Bit Score: 116.10 E-value: 2.85e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1570042588 28 LVLEtDGRIAAIredLPRGEVPkllrtlriggdDHANVRYLRRTEFLIPGFVDTHNHAPQYAQRGLGQSMH--ILDWLEK 105
Cdd:PRK08203 26 LVVE-GGRIVEV---GPGGALP-----------QPADEVFDARGHVVTPGLVNTHHHFYQTLTRALPAAQDaeLFPWLTT 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1570042588 106 VTfpnesrfsdPVYAR------RVYSR-CVDGFLRQGITTAS--YY----GSMHAEATKILAdlCLEKGQRAFVGKCNMN 172
Cdd:PRK08203 91 LY---------PVWARltpemvRVATQtALAELLLSGCTTSSdhHYlfpnGLRDALDDQIEA--AREIGMRFHATRGSMS 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1570042588 173 RNA------PDYYRdESVESSLRDTEACIT--HIRGidpEGRLLKHVLT--SRFAISCEdaLLASLGEIAKRNGdLPIQT 242
Cdd:PRK08203 160 LGEsdgglpPDSVV-EDEDAILADSQRLIDryHDPG---PGAMLRIALApcSPFSVSRE--LMRESAALARRLG-VRLHT 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1570042588 243 HMNEAKTEIEFTKTLF---PgfaneVDlYAH-FGLLTERSILAHCCYMSEYEMGRLKELGCGVAHCPVSNMTVGGGFmaA 318
Cdd:PRK08203 233 HLAETLDEEAFCLERFgmrP-----VD-YLEdLGWLGPDVWLAHCVHLDDAEIARLARTGTGVAHCPCSNMRLASGI--A 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1570042588 319 PVRDFLRRGIKVGLGTD-SGGGFSSSILEAMRQALIASNARevmsqGRDKGLTIPEVFHLATLGGAKvcCL-EDKIGSFE 396
Cdd:PRK08203 305 PVRELRAAGVPVGLGVDgSASNDGSNLIGEARQALLLQRLR-----YGPDAMTAREALEWATLGGAR--VLgRDDIGSLA 377
|
....*.
gi 1570042588 397 IGKEFD 402
Cdd:PRK08203 378 PGKLAD 383
|
|
| PRK06687 |
PRK06687 |
TRZ/ATZ family protein; |
73-452 |
3.52e-28 |
|
TRZ/ATZ family protein;
Pssm-ID: 180657 [Multi-domain] Cd Length: 419 Bit Score: 115.49 E-value: 3.52e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1570042588 73 FLIPGFVDTHNHAPQYAQRGLGQSMHILDWLEKVTFPNESRFSDPVYARRVYSRCVDgFLRQGITTASYYGSMHAEATKI 152
Cdd:PRK06687 55 WIMPGLVNCHTHSAMTGLRGIRDDSNLHEWLNDYIWPAESEFTPDMTTNAVKEALTE-MLQSGTTTFNDMYNPNGVDIQQ 133
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1570042588 153 LADLCLEKGQRAFVGKCNMNRNApdyyrdESVESSLRDTEACITHIRGIDPEGrlLKHVLTSRFAISCEDALLASLGEIA 232
Cdd:PRK06687 134 IYQVVKTSKMRCYFSPTLFSSET------ETTAETISRTRSIIDEILKYKNPN--FKVMVAPHSPYSCSRDLLEASLEMA 205
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1570042588 233 kRNGDLPIQTHMNEAKTEiefTKTLFPGFANE-VDLYAHFGLLTERSILAHCCYMSEYEMGRLKELGCGVAHCPVSNMTV 311
Cdd:PRK06687 206 -KELNIPLHVHVAETKEE---SGIILKRYGKRpLAFLEELGYLDHPSVFAHGVELNEREIERLASSQVAIAHNPISNLKL 281
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1570042588 312 GGGfmAAPVRDFLRRGIKVGLGTDSGGgfSSSILEAMRQALIASNAREvMSQGRDKGLTIPEVFHLATLGGAKVCCLEDK 391
Cdd:PRK06687 282 ASG--IAPIIQLQKAGVAVGIATDSVA--SNNNLDMFEEGRTAALLQK-MKSGDASQFPIETALKVLTIEGAKALGMENQ 356
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1570042588 392 IGSFEIGKEFDALLINADstGVMTMVEEEDSVRTIFdkFIMTGDDrnINEVYVRGR-LVKGG 452
Cdd:PRK06687 357 IGSLEVGKQADFLVIQPQ--GKIHLQPQENMLSHLV--YAVKSSD--VDDVYIAGEqVVKQG 412
|
|
| PRK08204 |
PRK08204 |
hypothetical protein; Provisional |
29-450 |
2.80e-27 |
|
hypothetical protein; Provisional
Pssm-ID: 181288 [Multi-domain] Cd Length: 449 Bit Score: 113.56 E-value: 2.80e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1570042588 29 VLETDGRIAAIREdlprgevpkllrtlRIGGDDHANVRYlrRTEFLIPGFVDTHNHAPQYAQRGLGQsmhilDWlekvtf 108
Cdd:PRK08204 26 ILIEGDRIAAVAP--------------SIEAPDAEVVDA--RGMIVMPGLVDTHRHTWQSVLRGIGA-----DW------ 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1570042588 109 pnesrfSDPVYARRVYSRCVDGFLRQGITTASYYGSMHAEATKI--LADLClekgqrafvgkcnMNRNAPDYyRDESVE- 185
Cdd:PRK08204 79 ------TLQTYFREIHGNLGPMFRPEDVYIANLLGALEALDAGVttLLDWS-------------HINNSPEH-ADAAIRg 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1570042588 186 -------------SSLRDTEACITHIRgIDPEG--RLLKHVLTSrfaiscEDALL----ASLG------EIAK------R 234
Cdd:PRK08204 139 laeagiravfahgSPGPSPYWPFDSVP-HPREDirRVKKRYFSS------DDGLLtlglAIRGpefsswEVARadfrlaR 211
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1570042588 235 NGDLPIQTHMneakteieftktlfpGFANE------VDLYAHFGLLTERSILAHCCYMSEYEMGRLKELGCGVAHCPVSN 308
Cdd:PRK08204 212 ELGLPISMHQ---------------GFGPWgatprgVEQLHDAGLLGPDLNLVHGNDLSDDELKLLADSGGSFSVTPEIE 276
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1570042588 309 MTVGGGFMaaPVRDFLRRGIKVGLGTDSGGGFSSSILEAMRQALIASNAREVMSQGRDKGLTIPE-------VFHLATLG 381
Cdd:PRK08204 277 MMMGHGYP--VTGRLLAHGVRPSLGVDVVTSTGGDMFTQMRFALQAERARDNAVHLREGGMPPPRltltarqVLEWATIE 354
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1570042588 382 GAKVCCLEDKIGSFEIGKEFDALLINADStgvMTMVEEEDSVRTIfdkfIMTGDDRNINEVYVRGRLVK 450
Cdd:PRK08204 355 GARALGLEDRIGSLTPGKQADLVLIDATD---LNLAPVHDPVGAV----VQSAHPGNVDSVMVAGRAVK 416
|
|
| PRK06038 |
PRK06038 |
N-ethylammeline chlorohydrolase; Provisional |
19-407 |
1.14e-25 |
|
N-ethylammeline chlorohydrolase; Provisional
Pssm-ID: 180363 [Multi-domain] Cd Length: 430 Bit Score: 108.68 E-value: 1.14e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1570042588 19 DLAILENAVLVLEtDGRIAAIREDLPrGEVPKLLrtlriggDDHANVrylrrtefLIPGFVDTHNHAPQYAQRGLGQSMH 98
Cdd:PRK06038 15 DAGDLKKGSVVIE-DGTITEVSESTP-GDADTVI-------DAKGSV--------VMPGLVNTHTHAAMTLFRGYADDLP 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1570042588 99 ILDWLEKVTFPNESRFSDP-VYARRVYSrCVDgFLRQGITT-ASYYGSMHAEATKILadlclEKGQRafvgkCNMNRNAP 176
Cdd:PRK06038 78 LAEWLNDHIWPAEAKLTAEdVYAGSLLA-CLE-MIKSGTTSfADMYFYMDEVAKAVE-----ESGLR-----AALSYGMI 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1570042588 177 DYYRDESVESSLRDTEACITHIRGIdPEGRLlKHVLTSRFAISCEDALLASLGEIAKRNGdLPIQTHMNEAKTEIEFTKT 256
Cdd:PRK06038 146 DLGDDEKGEAELKEGKRFVKEWHGA-ADGRI-KVMYGPHAPYTCSEEFLSKVKKLANKDG-VGIHIHVLETEAELNQMKE 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1570042588 257 LFPgfANEVDLYAHFGLLTERSILAHCCYMSEYEMGRLKELGCGVAHCPVSNMTVGGGFmaAPVRDFLRRGIKVGLGTDs 336
Cdd:PRK06038 223 QYG--MCSVNYLDDIGFLGPDVLAAHCVWLSDGDIEILRERGVNVSHNPVSNMKLASGI--APVPKLLERGVNVSLGTD- 297
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1570042588 337 gGGFSSSILEAMRQALIASNAREVmSQGRDKGLTIPEVFHLATLGGAKVccLEDKIGSFEIGKEFDALLIN 407
Cdd:PRK06038 298 -GCASNNNLDMFEEMKTAALLHKV-NTMDPTALPARQVLEMATVNGAKA--LGINTGMLKEGYLADIIIVD 364
|
|
| PRK06380 |
PRK06380 |
metal-dependent hydrolase; Provisional |
22-452 |
4.55e-24 |
|
metal-dependent hydrolase; Provisional
Pssm-ID: 180548 [Multi-domain] Cd Length: 418 Bit Score: 103.81 E-value: 4.55e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1570042588 22 ILENAVLVLETDGRiaaireDLPRGEVPKLLRTLRIGGDDHANVRYL--RRTEFLIPGFVDTHNHAPQYAQRGLGQSMHI 99
Cdd:PRK06380 4 LIKNAWIVTQNEKR------EILQGNVYIEGNKIVYVGDVNEEADYIidATGKVVMPGLINTHAHVGMTASKGLFDDVDL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1570042588 100 LDWLEKvTFPNESRFSDpvyaRRVYSRCVDG---FLRQGITTAS--YYgsmhaeATKILADLCLEKGQRAFVGKCNMNRn 174
Cdd:PRK06380 78 EEFLMK-TFKYDSKRTR----EGIYNSAKLGmyeMINSGITAFVdlYY------SEDIIAKAAEELGIRAFLSWAVLDE- 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1570042588 175 apDYYRDESveSSLRDTEACITHIRGIdpegRLLKHVLTSRFAISCEDALLASLGEIAKRNGDLpIQTHMNEAKTEI-EF 253
Cdd:PRK06380 146 --EITTQKG--DPLNNAENFIREHRNE----ELVTPSIGVQGIYVANDETYLKAKEIAEKYDTI-MHMHLSETRKEVyDH 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1570042588 254 TKTLFpgfANEVDLYAHFGLLTERSILAHCCYMSEYEMGRLKELGCGVAHCPVSNMTVGGGfMAAPVRDFLRRGIKVGLG 333
Cdd:PRK06380 217 VKRTG---ERPVEHLEKIGFLNSKLIAAHCVWATYHEIKLLSKNGVKVSWNSVSNFKLGTG-GSPPIPEMLDNGINVTIG 292
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1570042588 334 TDSGGGFSS-SILEAMR-QALIASNAREVMSQGRDKgltipEVFHLATLGGAKVccLEDKIGSFEIGKEFDALLINADST 411
Cdd:PRK06380 293 TDSNGSNNSlDMFEAMKfSALSVKNERWDASIIKAQ-----EILDFATINAAKA--LELNAGSIEVGKLADLVILDARAP 365
|
410 420 430 440
....*....|....*....|....*....|....*....|.
gi 1570042588 412 GvMTMVEEEDSVRTIfdkfIMTGDDRNINEVYVRGRLVKGG 452
Cdd:PRK06380 366 N-MIPTRKNNIVSNI----VYSLNPLNVDHVIVNGKILKEN 401
|
|
| PRK15493 |
PRK15493 |
bifunctional S-methyl-5'-thioadenosine deaminase/S-adenosylhomocysteine deaminase; |
22-449 |
9.86e-22 |
|
bifunctional S-methyl-5'-thioadenosine deaminase/S-adenosylhomocysteine deaminase;
Pssm-ID: 185390 [Multi-domain] Cd Length: 435 Bit Score: 97.05 E-value: 9.86e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1570042588 22 ILENAVLVLETDGRIaaireDLPRGEVPKllrtlriggDDHANVRYLRRTEFLIPGFVDTHNHAPQYAQRGLGQSMHILD 101
Cdd:PRK15493 19 VIENGYIIVENDQII-----DVNSGEFAS---------DFEVDEVIDMKGKWVLPGLVNTHTHVVMSLLRGIGDDMLLQP 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1570042588 102 WLEKVTFPNESRFSdPVYARRVYSRCVDGFLRQGITTAS-YYGSMHAEATKILaDLCLEKGQRAFVgkcnmNRNAPDYYR 180
Cdd:PRK15493 85 WLETRIWPLESQFT-PELAVASTELGLLEMVKSGTTSFSdMFNPIGVDQDAIM-ETVSRSGMRAAV-----SRTLFSFGT 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1570042588 181 DESVESSLRDTEaciTHIRGIDPEGRLLKHVLTSRFAISCEDALLASLGEIAKRNGDLpIQTHMNEAKTEIEFTKTLFPg 260
Cdd:PRK15493 158 KEDEKKAIEEAE---KYVKRYYNESGMLTTMVAPHSPYTCSTELLEECARIAVENQTM-VHIHLSETEREVRDIEAQYG- 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1570042588 261 fANEVDLYAHFGLLTERSILAHCCYMSEYEMGRLKELGCGVAHCPVSNMTVGGGFmaAPVRDFLRRGIKVGLGTDSGGgf 340
Cdd:PRK15493 233 -KRPVEYAASCGLFKRPTVIAHGVVLNDNERAFLAEHDVRVAHNPNSNLKLGSGI--ANVKAMLEAGIKVGIATDSVA-- 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1570042588 341 SSSILEAMRQALIASNAREVMSQGRdKGLTIPEVFHLATLGGAKVCCLEdKIGSFEIGKEFDALLINADSTGVMTMVEEe 420
Cdd:PRK15493 308 SNNNLDMFEEMRIATLLQKGIHQDA-TALPVETALTLATKGAAEVIGMK-QTGSLEVGKCADFITIDPSNKPHLQPADE- 384
|
410 420
....*....|....*....|....*....
gi 1570042588 421 dsvrtIFDKFIMTGDDRNINEVYVRGRLV 449
Cdd:PRK15493 385 -----VLSHLVYAASGKDISDVIINGKRV 408
|
|
| PRK12393 |
PRK12393 |
amidohydrolase; Provisional |
32-402 |
2.89e-18 |
|
amidohydrolase; Provisional
Pssm-ID: 237088 [Multi-domain] Cd Length: 457 Bit Score: 86.66 E-value: 2.89e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1570042588 32 TDGRIAAIredlprGEVPKLLRTLRIggDDHANVRYlrrtefliPGFVDTHNHAPQYAQRGLGQSMH--ILDWLEKVTFP 109
Cdd:PRK12393 31 RDGRIAAI------GALTPLPGERVI--DATDCVVY--------PGWVNTHHHLFQSLLKGVPAGINqsLTAWLAAVPYR 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1570042588 110 NESRFsDPVYARrVYSRCvdGF---LRQGITTAS-----YYGSMHAEATKILADLCLEKGQRaFV---GKCNMNRNA--- 175
Cdd:PRK12393 95 FRARF-DEDLFR-LAARI--GLvelLRSGCTTVAdhhylYHPGMPFDTGDILFDEAEALGMR-FVlcrGGATQTRGDhpg 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1570042588 176 -PDYYRDESVESSLRDTEACIThiRGIDPEGRLLKHVL----TSRFAISCEdaLLASLGEIAKRNGdLPIQTHMNEAKTE 250
Cdd:PRK12393 170 lPTALRPETLDQMLADVERLVS--RYHDASPDSLRRVVvaptTPTFSLPPE--LLREVARAARGMG-LRLHSHLSETVDY 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1570042588 251 IEFTKTLF---PgfaneVDLYAHFGLLTERSILAHCCYMSEYEMGRLKELGCGVAHCPVSNMTVGGGFmaAPVRDFLRRG 327
Cdd:PRK12393 245 VDFCREKYgmtP-----VQFVAEHDWLGPDVWFAHLVKLDAEEIALLAQTGTGIAHCPQSNGRLGSGI--APALAMEAAG 317
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1570042588 328 IKVGLGTD-SGGGFSSSILEAMRQALIASNArevmSQGRDkGLTIPEVFHLATLGGAKVCCLeDKIGSFEIGKEFD 402
Cdd:PRK12393 318 VPVSLGVDgAASNESADMLSEAHAAWLLHRA----EGGAD-ATTVEDVVHWGTAGGARVLGL-DAIGTLAVGQAAD 387
|
|
| Met_dep_hydrolase_E |
cd01313 |
Metallo-dependent hydrolases, subgroup D is part of the superfamily of metallo-dependent ... |
24-447 |
2.33e-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: 238638 [Multi-domain] Cd Length: 418 Bit Score: 83.66 E-value: 2.33e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1570042588 24 ENAVLVLETDGRIAAIREDLprgevpkllrtlriggddhANVRYLRRTEFLIPGFVDTHNHAPQYAQRGLGQ-----SMH 98
Cdd:cd01313 9 RNVRIEVDADGRIAAVNPDT-------------------ATEAVALLGGALLPGMPNLHSHAFQRAMAGLTEyrgsaADS 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1570042588 99 ILDWLEkvtfpNESRFSDPVYARRVYSRCVDGF---LRQGITTASYYGSMH---------------------AEATKI-- 152
Cdd:cd01313 70 FWTWRE-----LMYRFAARLTPEQIEAIARQLYiemLLAGITAVGEFHYVHhdpdgtpyadpaelaqrviaaASDAGIgi 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1570042588 153 -LADLCLEK----------GQRAFVgkcnmnrNAPDYYRDEsVESSLRDTEACITHIRGIDPegrllkHVLTsrfAISCE 221
Cdd:cd01313 145 tLLPVLYARagfggpapnpGQRRFI-------NGYEDFLGL-LEKALRAVKEHAAARIGVAP------HSLR---AVPAE 207
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1570042588 222 DalLASLGEIAKRngDLPIQTHMNEAKTEIEftKTLFPGFANEVDLYAHFGLLTERSILAHCCYMSEYEMGRLKELGCGV 301
Cdd:cd01313 208 Q--LAALAALASE--KAPVHIHLAEQPKEVD--DCLAAHGRRPVELLLDHGHLDARWCLVHATHLTDNETLLLGRSGAVV 281
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1570042588 302 AHCPVSNMTVGGGFMAAPvrDFLRRGIKVGLGTDSGGGFssSILEAMRQA----LIASNAREVMSQgrDKGLTIPEVFHL 377
Cdd:cd01313 282 GLCPTTEANLGDGIFPAA--ALLAAGGRIGIGSDSNARI--DLLEELRQLeysqRLRDRARNVLAT--AGGSSARALLDA 355
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1570042588 378 ATLGGAKVccLEDKIGSFEIGKEFDALLINADSTGVmtmveEEDSVRTIFDKFIMTGDDRNINEVYVRGR 447
Cdd:cd01313 356 ALAGGAQA--LGLATGALEAGARADLLSLDLDHPSL-----AGALPDTLLDAWVFAAGDREVRDVVVGGR 418
|
|
| metallo-dependent_hydrolases |
cd01292 |
Superfamily of metallo-dependent hydrolases (also called amidohydrolase superfamily) is a ... |
78-384 |
3.48e-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: 81.23 E-value: 3.48e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1570042588 78 FVDTHNHAPQYAQRGLgqsmhiLDWLEKvtfpNESRFSDPVYARRVYSRCVDGFLRQGITTA-----SYYGSMHAEATKI 152
Cdd:cd01292 1 FIDTHVHLDGSALRGT------RLNLEL----KEAEELSPEDLYEDTLRALEALLAGGVTTVvdmgsTPPPTTTKAAIEA 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1570042588 153 LADLCLE-KGQRAFVGKCNMNRNApdYYRDESVESSLRDTEAcithirgidpEGRLLKHVLTSRFAISCEDALLASLGEI 231
Cdd:cd01292 71 VAEAARAsAGIRVVLGLGIPGVPA--AVDEDAEALLLELLRR----------GLELGAVGLKLAGPYTATGLSDESLRRV 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1570042588 232 AK--RNGDLPIQTHMNEAKTEIEFTKTLfpgfaneVDLYAHFGllteRSILAHCCYMSEYEMGRLKELGCGVAHCPVSNM 309
Cdd:cd01292 139 LEeaRKLGLPVVIHAGELPDPTRALEDL-------VALLRLGG----RVVIGHVSHLDPELLELLKEAGVSLEVCPLSNY 207
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1570042588 310 -TVGGGFMAAPVRDFLRRGIKVGLGTDSGGGFSSSILeamrqaliASNAREVMSQGRDkGLTIPEVFHLATLGGAK 384
Cdd:cd01292 208 lLGRDGEGAEALRRLLELGIRVTLGTDGPPHPLGTDL--------LALLRLLLKVLRL-GLSLEEALRLATINPAR 274
|
|
| Met_dep_hydrolase_D |
cd01312 |
Metallo-dependent hydrolases, subgroup D is part of the superfamily of metallo-dependent ... |
219-402 |
1.63e-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: 80.96 E-value: 1.63e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1570042588 219 SCEDALLASLGEIAKRNGdLPIQTHMNEAKTEIEF-------TKTLFPGF--ANEVDLYA-------HFGLLTERSILAH 282
Cdd:cd01312 159 SVHPELAQDLIDLAKKLN-LPLSTHFLESKEEREWleeskgwFKHFWESFlkLPKPKKLAtaidfldMLGGLGTRVSFVH 237
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1570042588 283 CCYMSEYEMGRLKELGCGVAHCPVSNMTVGGGFmaAPVRDFLRRGIKVGLGTDsggGFSS----SILEAMRQALIASNAR 358
Cdd:cd01312 238 CVYANLEEAEILASRGASIALCPRSNRLLNGGK--LDVSELKKAGIPVSLGTD---GLSSnislSLLDELRALLDLHPEE 312
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1570042588 359 EVMSQGRdkgltipEVFHLATLGGAKVCCLEdkIGSFEIGKEFD 402
Cdd:cd01312 313 DLLELAS-------ELLLMATLGGARALGLN--NGEIEAGKRAD 347
|
|
| PRK06151 |
PRK06151 |
N-ethylammeline chlorohydrolase; Provisional |
132-449 |
8.72e-16 |
|
N-ethylammeline chlorohydrolase; Provisional
Pssm-ID: 180428 [Multi-domain] Cd Length: 488 Bit Score: 79.32 E-value: 8.72e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1570042588 132 LRQGITTASYYGSM-------HAEATKILADLCLEKGQRAFVGKCNMN---------RNAPDYYRDESVeSSLRDTEACI 195
Cdd:PRK06151 117 LRNGITTAMPIASLfyrqwaeTYAEFAAAAEAAGRLGLRVYLGPAYRSggsvleadgSLEVVFDEARGL-AGLEEAIAFI 195
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1570042588 196 THIRGIDpeGRLLKHVLTSRFAISCEDALLASLGEIAkRNGDLPIQTHMNEAKTEIEFTKTLFPGFAneVDLYAHFGLLT 275
Cdd:PRK06151 196 KRVDGAH--NGLVRGMLAPDRIETCTVDLLRRTAAAA-RELGCPVRLHCAQGVLEVETVRRLHGTTP--LEWLADVGLLG 270
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1570042588 276 ERSILAHCCYMSEYE---------MGRLKELGCGVAHCPVsNMTVGGGFMAAPVRdFLRRGIKVGLGTDSgggFSSSILE 346
Cdd:PRK06151 271 PRLLIPHATYISGSPrlnysggddLALLAEHGVSIVHCPL-VSARHGSALNSFDR-YREAGINLALGTDT---FPPDMVM 345
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1570042588 347 AMRQALIASnarEVMSqGRDKGLTIPEVFHLATLGGAKVCCLEDkIGSFEIGKEFDALLINADstgVMTMVEEEDSVRTI 426
Cdd:PRK06151 346 NMRVGLILG---RVVE-GDLDAASAADLFDAATLGGARALGRDD-LGRLAPGAKADIVVFDLD---GLHMGPVFDPIRTL 417
|
330 340
....*....|....*....|...
gi 1570042588 427 fdkfIMTGDDRNINEVYVRGRLV 449
Cdd:PRK06151 418 ----VTGGSGRDVRAVFVDGRVV 436
|
|
| PRK07203 |
PRK07203 |
putative aminohydrolase SsnA; |
265-353 |
1.60e-13 |
|
putative aminohydrolase SsnA;
Pssm-ID: 235963 [Multi-domain] Cd Length: 442 Bit Score: 72.28 E-value: 1.60e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1570042588 265 VDLYAHFGLLTERSILAHCCYMSEYEMGRLKELGCGVAHCPVSNM--TVGggfmAAPVRDFLRRGIKVGLGTDsggGFSS 342
Cdd:PRK07203 244 VERLADFGLLGEKTLAAHCIYLSDEEIDLLKETDTFVVHNPESNMgnAVG----YNPVLEMIKNGILLGLGTD---GYTS 316
|
90
....*....|.
gi 1570042588 343 SILEAMRQALI 353
Cdd:PRK07203 317 DMFESYKVANF 327
|
|
| PRK08418 |
PRK08418 |
metal-dependent hydrolase; |
230-407 |
1.93e-13 |
|
metal-dependent hydrolase;
Pssm-ID: 181419 [Multi-domain] Cd Length: 408 Bit Score: 71.54 E-value: 1.93e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1570042588 230 EIAKRNGdLPIQTHMNEAKTEIE-------FTKTLFPGFANEV-------DLYAHFglLTERSILAHCCYMSEYEMGRLK 295
Cdd:PRK08418 197 QLAKKEN-LLVSTHFLESKAEREwleeskgWFKKFFEKFLKEPkplytpkEFLELF--KGLRTLFTHCVYASEEELEKIK 273
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1570042588 296 ELGCGVAHCPVSNMTVGGGFMaaPVRDFLRRGIKVGLGTDsggGFSS----SILEAMRQALIASNAREVMSQGRdkglti 371
Cdd:PRK08418 274 SKNASITHCPFSNRLLSNKAL--DLEKAKKAGINYSIATD---GLSSnislSLLDELRAALLTHANMPLLELAK------ 342
|
170 180 190
....*....|....*....|....*....|....*.
gi 1570042588 372 pEVFHLATLGGAKVCCLEDkiGSFEIGKEFDALLIN 407
Cdd:PRK08418 343 -ILLLSATRYGAKALGLNN--GEIKEGKDADLSVFE 375
|
|
| HutI |
COG1228 |
Imidazolonepropionase or related amidohydrolase [Secondary metabolites biosynthesis, transport ... |
1-450 |
5.80e-13 |
|
Imidazolonepropionase or related amidohydrolase [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 440841 [Multi-domain] Cd Length: 386 Bit Score: 69.99 E-value: 5.80e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1570042588 1 MKSPLVFHGTLIHSrsPADLAILENAVLVLEtDGRIAAIRedlPRGEVPKLLRTLRIGGDDHanvrylrrteFLIPGFVD 80
Cdd:COG1228 6 QAGTLLITNATLVD--GTGGGVIENGTVLVE-DGKIAAVG---PAADLAVPAGAEVIDATGK----------TVLPGLID 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1570042588 81 THNHAPQYAQRGlgqsmhildwlekVTFPNESRFSDPVYARRVYSRCVDGFLRQGITTA-SYYGSMHAEATKILAdlcle 159
Cdd:COG1228 70 AHTHLGLGGGRA-------------VEFEAGGGITPTVDLVNPADKRLRRALAAGVTTVrDLPGGPLGLRDAIIA----- 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1570042588 160 kGQRAFVgkcnmnrNAPDYYRDE---SVESSLRDT--EACITHIRGIDPEG-RLLKHVLTSRFAISCEDALLASLgEIAK 233
Cdd:COG1228 132 -GESKLL-------PGPRVLAAGpalSLTGGAHARgpEEARAALRELLAEGaDYIKVFAEGGAPDFSLEELRAIL-EAAH 202
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1570042588 234 RNGdLPIQTHMNEAKteieftktlfpgfanEVDLYAHFGLLTersiLAHCCYMSEYEMGRLKELGCgVAHCP-------- 305
Cdd:COG1228 203 ALG-LPVAAHAHQAD---------------DIRLAVEAGVDS----IEHGTYLDDEVADLLAEAGT-VVLVPtlslflal 261
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1570042588 306 --------VSNMTVGGGFMAAPVRDFLRRGIKVGLGTDSGGGFSSSIleamrqaliaSNAREvMSQGRDKGLTIPEVFHL 377
Cdd:COG1228 262 legaaapvAAKARKVREAALANARRLHDAGVPVALGTDAGVGVPPGR----------SLHRE-LALAVEAGLTPEEALRA 330
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1570042588 378 ATLGGAKVCCLEDKIGSFEIGKEFDALLINADSTgvmtmveEEDSVRtifdkfimtgddRNINEVYVRGRLVK 450
Cdd:COG1228 331 ATINAAKALGLDDDVGSLEPGKLADLVLLDGDPL-------EDIAYL------------EDVRAVMKDGRVVD 384
|
|
| Imidazolone-5PH |
cd01296 |
Imidazolonepropionase/imidazolone-5-propionate hydrolase (Imidazolone-5PH) catalyzes the third ... |
282-410 |
2.10e-09 |
|
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: 58.81 E-value: 2.10e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1570042588 282 HCCYMSEYEMGRLKELGCGVAHCPVSNMTVGGGFmaAPVRDFLRRGIKVGLGTDS--GGGFSSSILEAMRQALiasnare 359
Cdd:cd01296 235 HLEHTSDEGIAALAEAGTVAVLLPGTAFSLRETY--PPARKLIDAGVPVALGTDFnpGSSPTSSMPLVMHLAC------- 305
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 1570042588 360 vmsqgRDKGLTIPEVFHLATLGGAKVCCLEDKIGSFEIGKEFDALLINADS 410
Cdd:cd01296 306 -----RLMRMTPEEALTAATINAAAALGLGETVGSLEVGKQADLVILDAPS 351
|
|
| archeal_chlorohydrolases |
cd01305 |
Predicted chlorohydrolases. These metallo-dependent hydrolases from archea are part of the ... |
74-385 |
4.04e-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: 57.41 E-value: 4.04e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1570042588 74 LIPGFVDTHNHAPQYAQRGLGQSMHILDwleKVTFPNEsrfsdpvYARRVYSRCVDGFLRQGITtaSYYGSMHAEATKIL 153
Cdd:cd01305 2 LIPALVNAHTHLGDSAIKEVGDGLPLDD---LVAPPDG-------LKHRLLAQADDRELAEAMR--KVLRDMRETGIGAF 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1570042588 154 ADLcLEKGqrafVGKCNMNRNAPDYYrdesvesslrDTEACITHIRGIDPEGRLLKHVLTSRFAISCE-DALLASLGEIA 232
Cdd:cd01305 70 ADF-REGG----VEGIELLRRALGKL----------PVPFEVILGRPTEPDDPEILLEVADGLGLSSAnDVDLEDILELL 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1570042588 233 KRNGdLPIQTHMNE-----AKTEIEftktlfPGFANEVDLyahfglltersiLAHCCYMSEYEMGRLKELGCGVAHCPVS 307
Cdd:cd01305 135 RRRG-KLFAIHASEtresvGMTDIE------RALDLEPDL------------LVHGTHLTDEDLELVRENGVPVVLCPRS 195
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1570042588 308 NMTVGGGFmaAPVRDFLRRGIKVGLGTDSGGGFSSSILEAMRQALIASNAREVMSQgrdkgltiPEVFHLATLGGAKV 385
Cdd:cd01305 196 NLYFGVGI--PPVAELLKLGIKVLLGTDNVMVNEPDMWAEMEFLAKYSRLQGYLSP--------LEILRMATVNAAEF 263
|
|
| Amidohydro_3 |
pfam07969 |
Amidohydrolase family; |
220-449 |
3.07e-08 |
|
Amidohydrolase family;
Pssm-ID: 400360 [Multi-domain] Cd Length: 464 Bit Score: 55.62 E-value: 3.07e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1570042588 220 CEDALLASLGEIAKRNGdLPIQTHMNEAKTEIEFTKTlfpgFANEVDLYAHFGllteRSILAHCCYM---SEYEMGRLKE 296
Cdd:pfam07969 247 FEDEALAELVAAARERG-LDVAIHAIGDATIDTALDA----FEAVAEKLGNQG----RVRIEHAQGVvpyTYSQIERVAA 317
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1570042588 297 LGCGVAHCPVSNMTVGGGFM----------AAPVRDFLRRGIKVGLGTDSGGGFSSSILeamrqALIASNAREVMSQGR- 365
Cdd:pfam07969 318 LGGAAGVQPVFDPLWGDWLQdrlgaerargLTPVKELLNAGVKVALGSDAPVGPFDPWP-----RIGAAVMRQTAGGGEv 392
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1570042588 366 ---DKGLTIPEVFHLATLGGAKVCCLEDKIGSFEIGKEFDALLINADstgVMTMVEEEDsvrtifdkfimtgDDRNINEV 442
Cdd:pfam07969 393 lgpDEELSLEEALALYTSGPAKALGLEDRKGTLGVGKDADLVVLDDD---PLTVDPPAI-------------ADIRVRLT 456
|
....*..
gi 1570042588 443 YVRGRLV 449
Cdd:pfam07969 457 VVDGRVV 463
|
|
| YtcJ_like |
cd01300 |
YtcJ_like metal dependent amidohydrolases. YtcJ is a Bacillus subtilis ORF of unknown function. ... |
277-399 |
2.86e-07 |
|
YtcJ_like metal dependent amidohydrolases. YtcJ is a Bacillus subtilis ORF of unknown function. The Arabidopsis homolog LAF3 has been identified as a factor required for phytochrome A signalling.
Pssm-ID: 238625 [Multi-domain] Cd Length: 479 Bit Score: 52.70 E-value: 2.86e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1570042588 277 RSILAHCCYMSEYEMGRLKELGCGVA----HCP-----VSNMTVGGGFMAA--PVRDFLRRGIKVGLGTDSGGGFSSSiL 345
Cdd:cd01300 341 RHRIEHAQLVSPDDIPRFAKLGVIASvqpnHLYsdgdaAEDRRLGEERAKRsyPFRSLLDAGVPVALGSDAPVAPPDP-L 419
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 1570042588 346 EAMRQALIASNAREVMSQGRDKGLTIPEVFHLATLGGAKVCCLEDKIGSFEIGK 399
Cdd:cd01300 420 LGIWAAVTRKTPGGGVLGNPEERLSLEEALRAYTIGAAYAIGEEDEKGSLEPGK 473
|
|
| PRK09229 |
PRK09229 |
N-formimino-L-glutamate deiminase; Validated |
24-452 |
9.35e-07 |
|
N-formimino-L-glutamate deiminase; Validated
Pssm-ID: 236420 [Multi-domain] Cd Length: 456 Bit Score: 51.00 E-value: 9.35e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1570042588 24 ENAVLVLETDGRIAAIREDLPRGEVPkllrtlriggddhanvrylRRTEFLIPGFVDTHNHAPQYAQRGLGqsmhildwl 103
Cdd:PRK09229 18 RNVRLTVDADGRIAAVEPGAAPAGAE-------------------RLAGPVLPGMPNLHSHAFQRAMAGLT--------- 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1570042588 104 EKVTFPNES---------RFS---DP----VYARRVYsrcVDgFLRQGITTAS---Y---------YGSMHAEATKILA- 154
Cdd:PRK09229 70 EVRGPPQDSfwswrelmyRFAlrlTPdqleAIARQLY---VE-MLEAGYTSVGefhYlhhdpdgtpYADPAEMALRIVAa 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1570042588 155 ------DLCL---------------EKGQRAFVgkcnmnrnapdyyrdESVESSLRDTEACITHIRGiDPEGRL--LKHV 211
Cdd:PRK09229 146 araagiGLTLlpvlyahsgfggqppNPGQRRFI---------------NDPDGFLRLLEALRRALAA-LPGARLglAPHS 209
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1570042588 212 LtsRfAIScEDALLASLGEIakrNGDLPIqtHMNEAkteiEFTKtlfpgfanEVD-------------LYAHfGLLTERS 278
Cdd:PRK09229 210 L--R-AVT-PDQLAAVLALA---APDGPV--HIHIA----EQTK--------EVDdclawsgarpvewLLDH-APVDARW 267
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1570042588 279 ILAHCCYMSEYEMGRLKELGCGVAHCPVSNMTVGGGFmaAPVRDFLRRGIKVGLGTDSggGFSSSILEAMR-----QALi 353
Cdd:PRK09229 268 CLVHATHLTDAETARLARSGAVAGLCPTTEANLGDGI--FPAVDYLAAGGRFGIGSDS--HVSIDLVEELRlleygQRL- 342
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1570042588 354 ASNAREVMSQGRDkGLTIPEVFHLATLGGAKVCCLedKIGSFEIGKEFDALLINADSTgvmTMVEEEDsvRTIFDKFIMT 433
Cdd:PRK09229 343 RDRRRNVLAAAAQ-PSVGRRLFDAALAGGAQALGR--AIGGLAVGARADLVVLDLDHP---ALAGREG--DALLDRWVFA 414
|
490 500
....*....|....*....|
gi 1570042588 434 GDDRNINEVYVRGR-LVKGG 452
Cdd:PRK09229 415 GGDAAVRDVWVAGRwVVRDG 434
|
|
| Met_dep_hydrolase_A |
cd01299 |
Metallo-dependent hydrolases, subgroup A is part of the superfamily of metallo-dependent ... |
320-409 |
1.91e-06 |
|
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: 49.60 E-value: 1.91e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1570042588 320 VRDFLRRGIKVGLGTDSGGGFsssileamrqALIASNAREV--MSqgrDKGLTIPEVFHLATLGGAKVCCLEDKIGSFEI 397
Cdd:cd01299 256 LRRAHKAGVKIAFGTDAGFPV----------PPHGWNARELelLV---KAGGTPAEALRAATANAAELLGLSDELGVIEA 322
|
90
....*....|..
gi 1570042588 398 GKEFDALLINAD 409
Cdd:cd01299 323 GKLADLLVVDGD 334
|
|
| Bact_CD |
cd01293 |
Bacterial cytosine deaminase and related metal-dependent hydrolases. Cytosine deaminases (CDs) ... |
16-411 |
8.27e-05 |
|
Bacterial cytosine deaminase and related metal-dependent hydrolases. Cytosine deaminases (CDs) catalyze the deamination of cytosine, producing uracil and ammonia. They play an important role in pyrimidine salvage. CDs are present in prokaryotes and fungi, but not mammalian cells. The bacterial enzymes, but not the fungal enzymes, are related to the adenosine deaminases (ADA). The bacterial enzymes are iron dependent and hexameric.
Pssm-ID: 238618 [Multi-domain] Cd Length: 398 Bit Score: 44.55 E-value: 8.27e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1570042588 16 SPADLAIlenavlvleTDGRIAAIRedlPRGEVPkllrtlriGGDDHANVR-YLrrtefLIPGFVDTHNHA-------PQ 87
Cdd:cd01293 13 ALVDIAI---------EDGRIAAIG---PALAVP--------PDAEEVDAKgRL-----VLPAFVDPHIHLdktftggRW 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1570042588 88 YAQRGLGQSMHILDWLEKvtfpNESRFSDPVYARrvysrcvdgfLRQGITTASYYGSM----HAEATKILADLCLEKGQR 163
Cdd:cd01293 68 PNNSGGTLLEAIIAWEER----KLLLTAEDVKER----------AERALELAIAHGTTairtHVDVDPAAGLKALEALLE 133
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170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1570042588 164 A---FVGKCNMNRNA---PDYYRDESVESSLRDT-EACITHIRGIDPegrllkhvLTSRFAIsceDALLASLGEIAKRNG 236
Cdd:cd01293 134 LreeWADLIDLQIVAfpqHGLLSTPGGEELMREAlKMGADVVGGIPP--------AEIDEDG---EESLDTLFELAQEHG 202
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1570042588 237 dLPIQTHMNEAKTEIEFTktlFPGFANEVDlyaHFGLlTERSILAHCC---YMSEYEMGR----LKELGCGVAHCPVSNM 309
Cdd:cd01293 203 -LDIDLHLDETDDPGSRT---LEELAEEAE---RRGM-QGRVTCSHATalgSLPEAEVSRladlLAEAGISVVSLPPINL 274
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1570042588 310 TVGGGFMA-------APVRDFLRRGIKVGLGTDS--------GGGfssSILEAMRQALiasnarEVMSQGRDKGLTIpeV 374
Cdd:cd01293 275 YLQGREDTtpkrrgvTPVKELRAAGVNVALGSDNvrdpwypfGSG---DMLEVANLAA------HIAQLGTPEDLAL--A 343
|
410 420 430
....*....|....*....|....*....|....*..
gi 1570042588 375 FHLATLGGAKVCCLEDkiGSFEIGKEFDALLINADST 411
Cdd:cd01293 344 LDLITGNAARALGLED--YGIKVGCPADLVLLDAEDV 378
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|
| PRK07213 |
PRK07213 |
chlorohydrolase; Provisional |
280-407 |
2.01e-03 |
|
chlorohydrolase; Provisional
Pssm-ID: 235969 [Multi-domain] Cd Length: 375 Bit Score: 40.41 E-value: 2.01e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1570042588 280 LAHCCYMSEYEMGRLKELGCGVAHCPVSNMTVGGGFmaAPVRDFLRRGIKVGLGTDSGGGFSSSILEAMRQALiasnare 359
Cdd:PRK07213 231 IVHATHPSNDDLELLKENNIPVVVCPRANASFNVGL--PPLNEMLEKGILLGIGTDNFMANSPSIFREMEFIY------- 301
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 1570042588 360 vmsqgrdKGLTIP--EVFHLATLGGAKVCCLEDKiGSFEIGKEFDALLIN 407
Cdd:PRK07213 302 -------KLYHIEpkEILKMATINGAKILGLINV-GLIEEGFKADFTFIK 343
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