|
Name |
Accession |
Description |
Interval |
E-value |
| PRK09230 |
PRK09230 |
cytosine deaminase; Provisional |
1-421 |
0e+00 |
|
cytosine deaminase; Provisional
Pssm-ID: 181713 Cd Length: 426 Bit Score: 934.12 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1341381309 1 MLIRNVRLAGREGMWQILCQGGVIRAIEPMSTQLLSVRE-LDGEQGLVIPPFIEPHIHLDTTQTAGEPSWNFSGTLFEGI 79
Cdd:PRK09230 6 MTIKNARLPGKEGLWQITIEDGKISAIEPQSEASLEAGEvLDAEGGLAIPPFIEPHIHLDTTQTAGEPNWNQSGTLFEGI 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1341381309 80 ERWAERKALLTHEDVKQRAIQTLKWQIANGIQFVRTHVDVSDPNLVALKAMLEVREEMKEWVELQIVAFPQEGILSYPNG 159
Cdd:PRK09230 86 ERWAERKALLTHEDVKQRAWQTLKWQIANGIQHVRTHVDVSDPTLTALKAMLEVKEEVAPWVDLQIVAFPQEGILSYPNG 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1341381309 160 KALLEEALKLGADVIGAIPHFEFTREYGVESLHYVFDLAEKYQVLVDVHCDEIDDEQSRFIETLATLAYERGIGHRVTAS 239
Cdd:PRK09230 166 EALLEEALRLGADVVGAIPHFEFTREYGVESLHKAFALAQKYDRLIDVHCDEIDDEQSRFVETVAALAHREGMGARVTAS 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1341381309 240 HTTAMHSYNGAYASRLFRLLRMADINFVANPLVNIHLQGRFDSYPKRRGITRVKEMLEANINVCFGHDDVFDPWYPMGTA 319
Cdd:PRK09230 246 HTTAMHSYNGAYTSRLFRLLKMSGINFVANPLVNIHLQGRFDTYPKRRGITRVKEMLEAGINVCFGHDDVFDPWYPLGTA 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1341381309 320 NMLQVLHMGLHVCQIMGYEQINDSLKLIGSHSARTLNVQDrYGIEVGKPANLLILPAENGFDAVRRQVPVRYSIRHGRVI 399
Cdd:PRK09230 326 NMLQVLHMGLHVCQLMGYGQINDGLNLITTHSARTLNLQD-YGIEVGNPANLIILPAENGFDAVRRQVPVRYSIRHGKVI 404
|
410 420
....*....|....*....|..
gi 1341381309 400 ADTRPAETTLHLVNAESVDFRR 421
Cdd:PRK09230 405 AETQPAQTTIYLEQPEAVDFKR 426
|
|
| Bact_CD |
cd01293 |
Bacterial cytosine deaminase and related metal-dependent hydrolases. Cytosine deaminases (CDs) ... |
2-399 |
0e+00 |
|
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: 517.57 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1341381309 2 LIRNVRL-AGREGMWQILCQGGVIRAIEPMSTQLLSVRELDGEQGLVIPPFIEPHIHLDTTQTAGEPSWNFSGTLFEGIE 80
Cdd:cd01293 1 LLRNARLaDGGTALVDIAIEDGRIAAIGPALAVPPDAEEVDAKGRLVLPAFVDPHIHLDKTFTGGRWPNNSGGTLLEAII 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1341381309 81 RWAERKALLTHEDVKQRAIQTLKWQIANGIQFVRTHVDVSDP-NLVALKAMLEVREEMKEWVELQIVAFPQEGILSYPNG 159
Cdd:cd01293 81 AWEERKLLLTAEDVKERAERALELAIAHGTTAIRTHVDVDPAaGLKALEALLELREEWADLIDLQIVAFPQHGLLSTPGG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1341381309 160 KALLEEALKLGADVIGAIPHFEfTREYGVESLHYVFDLAEKYQVLVDVHCDEIDDEQSRFIETLATLAYERGIGHRVTAS 239
Cdd:cd01293 161 EELMREALKMGADVVGGIPPAE-IDEDGEESLDTLFELAQEHGLDIDLHLDETDDPGSRTLEELAEEAERRGMQGRVTCS 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1341381309 240 HTTAMHSYNGAYASRLFRLLRMADINFVANPLVNIHLQGRFDSYPKRRGITRVKEMLEANINVCFGHDDVFDPWYPMGTA 319
Cdd:cd01293 240 HATALGSLPEAEVSRLADLLAEAGISVVSLPPINLYLQGREDTTPKRRGVTPVKELRAAGVNVALGSDNVRDPWYPFGSG 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1341381309 320 NMLQVLHMGLHVCQIMGYEQINDSLKLIGSHSARTLNVQDrYGIEVGKPANLLILPAENGFDAVRRQVPVRYSIRHGRVI 399
Cdd:cd01293 320 DMLEVANLAAHIAQLGTPEDLALALDLITGNAARALGLED-YGIKVGCPADLVLLDAEDVAEAVARQPPRRVVIRKGRVV 398
|
|
| PRK07572 |
PRK07572 |
cytosine deaminase; Validated |
1-421 |
2.36e-168 |
|
cytosine deaminase; Validated
Pssm-ID: 181039 Cd Length: 426 Bit Score: 478.74 E-value: 2.36e-168
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1341381309 1 MLIRNVRL-AGREGMwQILCQGGVIRAIEPmSTQLLSVRELDGEQGLVIPPFIEPHIHLDTTQTAGEPSWNFSGTLFEGI 79
Cdd:PRK07572 4 LIVRNANLpDGRTGI-DIGIAGGRIAAVEP-GLQAEAAEEIDAAGRLVSPPFVDPHFHMDATLSYGLPRVNASGTLLEGI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1341381309 80 ERWAERKALLTHEDVKQRAIQTLKWQIANGIQFVRTHVDVSDPNLVALKAMLEVREEMKEWVELQIVAFPQEGILSYPNG 159
Cdd:PRK07572 82 ALWGELKPLLTQEALVERALRYCDWAVARGLLAIRSHVDVCDPRLLAVEALLEVRERVAPYLDLQLVAFPQDGVLRSPGA 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1341381309 160 KALLEEALKLGADVIGAIPHFEFTREYGVESLHYVFDLAEKYQVLVDVHCDEIDDEQSRFIETLATLAYERGIGHRVTAS 239
Cdd:PRK07572 162 VDNLERALDMGVDVVGGIPHFERTMADGAESVRLLCEIAAERGLRVDMHCDESDDPLSRHIETLAAETQRLGLQGRVAGS 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1341381309 240 HTTAMHSYNGAYASRLFRLLRMADINFVANPLVNIHLQGRFDSYPKRRGITRVKEMLEANINVCFGHDDVFDPWYPMGTA 319
Cdd:PRK07572 242 HLTSMHSMDNYYVSKLIPLMAEAGVNAIANPLINITLQGRHDTYPKRRGMTRVPELMAAGINVAFGHDCVMDPWYSLGSG 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1341381309 320 NMLQVLHMGLHVCQIMGYEQINDSLKLIGSHSARTLNVQDrYGIEVGKPANLLILPAENGFDAVRRQVPVRYSIRHGRVI 399
Cdd:PRK07572 322 DMLEVAHMGLHVAQMTGQDAMRACFDAVTVNPARIMGLEG-YGLEPGCNADLVLLQARDPIEAIRLRAARLAVIRRGKVI 400
|
410 420
....*....|....*....|...
gi 1341381309 400 ADTRPAETTLHLVN-AESVDFRR 421
Cdd:PRK07572 401 ARTPPRVARLSLPGrPATVDFRL 423
|
|
| PRK05985 |
PRK05985 |
cytosine deaminase; Provisional |
1-400 |
2.24e-60 |
|
cytosine deaminase; Provisional
Pssm-ID: 180337 [Multi-domain] Cd Length: 391 Bit Score: 200.93 E-value: 2.24e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1341381309 1 MLIRNVRLAGREGMwQILCQGGVIRAIEPMSTQLLSVRELDGEQGLVIPPFIEPHIHLDTTqTAGEPsW---NFSGTLFE 77
Cdd:PRK05985 4 LLFRNVRPAGGAAV-DILIRDGRIAAIGPALAAPPGAEVEDGGGALALPGLVDGHIHLDKT-FWGDP-WypnEPGPSLRE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1341381309 78 GIERWAERKALLTHeDVKQRAIQTLKWQIANGIQFVRTHVDVsDPN--LVALKAMLEVREEMKEWVELQIVAFPQEGILS 155
Cdd:PRK05985 81 RIANERRRRAASGH-PAAERALALARAAAAAGTTAMRSHVDV-DPDagLRHLEAVLAARETLRGLIDIQIVAFPQSGVLS 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1341381309 156 YPNGKALLEEALKLGADVIGAIPHFEFTREyGVESLHYVFDLAEKYQVLVDVHCDEIDDEQSRFIETLATLAYERGIGHR 235
Cdd:PRK05985 159 RPGTAELLDAALRAGADVVGGLDPAGIDGD-PEGQLDIVFGLAERHGVGIDIHLHEPGELGAFQLERIAARTRALGMQGR 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1341381309 236 VTASHTTAMHSYNGAYASRLFRLLRMADINFVANPlvnihlqgrfdsyPKRRGITRVKEMLEANINVCFGHDDVFDPWYP 315
Cdd:PRK05985 238 VAVSHAFCLGDLPEREVDRLAERLAEAGVAIMTNA-------------PGSVPVPPVAALRAAGVTVFGGNDGIRDTWWP 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1341381309 316 MGTANMLQVLHMglhvcqiMGYEQ---INDSLKL---IGSHS-ARTLNVQDrYGIEVGKPANLLILPAENGFDAVrRQVP 388
Cdd:PRK05985 305 YGNGDMLERAML-------IGYRSgfrTDDELAAaldCVTHGgARALGLED-YGLAVGARADFVLVDAETVAEAV-VAVP 375
|
410
....*....|...
gi 1341381309 389 VRYSI-RHGRVIA 400
Cdd:PRK05985 376 VRRLVvRGGRIVA 388
|
|
| Amidohydro_3 |
pfam07969 |
Amidohydrolase family; |
38-400 |
1.41e-52 |
|
Amidohydrolase family;
Pssm-ID: 400360 [Multi-domain] Cd Length: 464 Bit Score: 182.35 E-value: 1.41e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1341381309 38 RELDGEQGLVIPPFIEPHIHLD------TTQTAGEPSWN-----FSGTLFEGIERWAE-RKALLTHEDVKQRAIQTLKWQ 105
Cdd:pfam07969 1 EVIDAKGRLVLPGFVDPHTHLDggglnlRELRLPDVLPNavvkgQAGRTPKGRWLVGEgWDEAQFAETRFPYALADLDEV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1341381309 106 IANGIQFVR---THVDVSDPNLVA------------------------LKAMLE----------VREEMKEWVELQIVAF 148
Cdd:pfam07969 81 APDGPVLLRalhTHAAVANSAALDlagitkatedppggeiardangegLTGLLRegayalppllAREAEAAAVAAALAAL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1341381309 149 PQEGILSYP--------------------------------------NGKALLEEALKLGADVIGAIPHFEFTREY---- 186
Cdd:pfam07969 161 PGFGITSVDggggnvhslddyeplreltaaeklkelldaperlglphSIYELRIGAMKLFADGVLGSRTAALTEPYfdap 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1341381309 187 -------GVESLHYVFDLAEKYQVLVDVHCDEIDDEQSrFIETLATLAYERGIGHRVTASHTTAMHSYNGAYASRLFRLL 259
Cdd:pfam07969 241 gtgwpdfEDEALAELVAAARERGLDVAIHAIGDATIDT-ALDAFEAVAEKLGNQGRVRIEHAQGVVPYTYSQIERVAALG 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1341381309 260 RMADINFVANPLVNIHLQGRFDsYPKRRGITRVKEMLEANINVCFGHD---DVFDPWYPMGTANMLQVLhMGLHVCQIMG 336
Cdd:pfam07969 320 GAAGVQPVFDPLWGDWLQDRLG-AERARGLTPVKELLNAGVKVALGSDapvGPFDPWPRIGAAVMRQTA-GGGEVLGPDE 397
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1341381309 337 YEQINDSLKLIGSHSARTLNVQDRYG-IEVGKPANLLILPAeNGFD---AVRRQVPVRYSIRHGRVIA 400
Cdd:pfam07969 398 ELSLEEALALYTSGPAKALGLEDRKGtLGVGKDADLVVLDD-DPLTvdpPAIADIRVRLTVVDGRVVY 464
|
|
| PRK06846 |
PRK06846 |
putative deaminase; Validated |
1-400 |
2.55e-45 |
|
putative deaminase; Validated
Pssm-ID: 235873 [Multi-domain] Cd Length: 410 Bit Score: 161.72 E-value: 2.55e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1341381309 1 MLIRNVRL------------AGREGMWQILCQGGVIRAIEPMSTQLLS-VRELDGEQGLVIPPFIEPHIHLDTTQTAGEp 67
Cdd:PRK06846 6 YWLTNVRLetgfdyengvivQTETALCTLEIQDGKIVAIRPNKQVPDAtLPTYDANGLLMLPAFREMHIHLDKTYYGGP- 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1341381309 68 sWNFS---GTLFEGI--ERWAERKALLThedVKQRAIQTLKWQIANGIQFVRTHVDVsDP--NLVALKAMLEVREEMKEW 140
Cdd:PRK06846 85 -WKACrpaKTIQDRIelEQKELPELLPT---TQERAEKLIELLQSKGATHIRSHCNI-DPviGLKNLENLQAALERYKDG 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1341381309 141 VELQIVAFPQEGILsYPNGKALLEEALKLGADVIGAI-PHfefTREYGVE-SLHYVFDLAEKYQVLVDVHCDEIDDEQSR 218
Cdd:PRK06846 160 FTYEIVAFPQHGLL-RSNSEPLMREAMKMGAHLVGGVdPA---SVDGAIEkSLDTMFQIAVDFNKGVDIHLHDTGPLGVA 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1341381309 219 FIETLATLAYERGIGHRVTASHTTAMHSYNGAYASRLFRLLRMADINFVAnplvnihlqgrfdSYPKRRGITRVKEMLEA 298
Cdd:PRK06846 236 TIKYLVETTEEAQWKGKVTISHAFALGDLNEEEVEELAERLAAQGISITS-------------TVPIGRLHMPIPLLHDK 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1341381309 299 NINVCFGHDDVFDPWYPMGTANMLQVLHMglhVCQIMGY---EQINDSLKLIgSHSARTLNVQ-DRYGIEVGKPANLLIL 374
Cdd:PRK06846 303 GVKVSLGTDSVIDHWSPFGTGDMLEKANL---LAELYRWsdeRSLSRSLALA-TGGVLPLNDEgERVWPKVGDEASFVLV 378
|
410 420
....*....|....*....|....*.
gi 1341381309 375 PAENGFDAVRRQVPVRYSIRHGRVIA 400
Cdd:PRK06846 379 DASCSAEAVARQSPRTAVFHKGQLVA 404
|
|
| PRK07583 |
PRK07583 |
cytosine deaminase; |
17-404 |
2.16e-39 |
|
cytosine deaminase;
Pssm-ID: 236062 Cd Length: 438 Bit Score: 146.28 E-value: 2.16e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1341381309 17 ILCQGGVIRAIEPMSTQLLSVRELDGEQGLVIPPFIEPHIHLD---TTQTAGEPSWNFSGTLFEGIerwAERKALLTHED 93
Cdd:PRK07583 43 IEIADGKIAAILPAGGAPDELPAVDLKGRMVWPCFVDMHTHLDkghIWPRSPNPDGTFPGALDAVT---ADREAHWSAED 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1341381309 94 VKQRAIQTLKWQIANGIQFVRTHVDVSDPNL-VALKAMLEVREEMKEWVELQIVA-FPQEGILSyPNGKALLEEALKLGA 171
Cdd:PRK07583 120 LYRRMEFGLRCAYAHGTSAIRTHLDSFAPQAaISWEVFAELREAWAGRIALQAVSlVPLDAYLT-DAGERLADLVAEAGG 198
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1341381309 172 dVIGAI----PHFEftreygvESLHYVFDLAEKYQVLVDVHCDEIDDEQSRFIETLATLAYERGIGHRVTASHTTAMHSY 247
Cdd:PRK07583 199 -LLGGVtymnPDLD-------AQLDRLFRLARERGLDLDLHVDETGDPASRTLKAVAEAALRNGFEGKVTCGHCCSLAVQ 270
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1341381309 248 NGAYASRLFRLLRMADINFVANPLVNIHLQGRFDSY-PKRRGITRVKEMLEANINVCFGHDDVFDPWYPMGTANMLQVLH 326
Cdd:PRK07583 271 PEEQAQATIALVAEAGIAIVSLPMCNLYLQDRQPGRtPRWRGVTLVHELKAAGIPVAVASDNCRDPFYAYGDHDMLEVFR 350
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1341381309 327 MGLHVCQI-MGYEqinDSLKLIGSHSARTLNVQDRYGIEVGKPANLLILPAENGFDAVRRQVPVRYSIRHGRVIADTRP 404
Cdd:PRK07583 351 EAVRILHLdHPYD---DWPAAVTTTPADIMGLPDLGRIAVGAPADLVLFKARSFSELLSRPQSDRIVLRAGKPIDTTLP 426
|
|
| metallo-dependent_hydrolases |
cd01292 |
Superfamily of metallo-dependent hydrolases (also called amidohydrolase superfamily) is a ... |
51-353 |
2.76e-28 |
|
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: 112.43 E-value: 2.76e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1341381309 51 FIEPHIHLDTTQTAGEPSWNfsgtlfegierWAERKALLTHEDVKQRAIQTLKWQIANGIQFVRTHVDVSDPNLvALKAM 130
Cdd:cd01292 1 FIDTHVHLDGSALRGTRLNL-----------ELKEAEELSPEDLYEDTLRALEALLAGGVTTVVDMGSTPPPTT-TKAAI 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1341381309 131 LEVREEMKEWVELQIVAFPqeGILSYPN---------GKALLEEALKLGADVIGAIPHfEFTREYGVESLHYVFDLAEKY 201
Cdd:cd01292 69 EAVAEAARASAGIRVVLGL--GIPGVPAavdedaealLLELLRRGLELGAVGLKLAGP-YTATGLSDESLRRVLEEARKL 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1341381309 202 QVLVDVHCDEIDDEqSRFIETLATLAyerGIGHRVTASHTTAMHSyngayasRLFRLLRMADINFVANPLVNIHLQgrfd 281
Cdd:cd01292 146 GLPVVIHAGELPDP-TRALEDLVALL---RLGGRVVIGHVSHLDP-------ELLELLKEAGVSLEVCPLSNYLLG---- 210
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1341381309 282 syPKRRGITRVKEMLEANINVCFGHDDVFDPwypmGTANMLQVLHMGLHVCQIMGyeQINDSLKLIGSHSAR 353
Cdd:cd01292 211 --RDGEGAEALRRLLELGIRVTLGTDGPPHP----LGTDLLALLRLLLKVLRLGL--SLEEALRLATINPAR 274
|
|
| PRK06886 |
PRK06886 |
hypothetical protein; Validated |
84-342 |
7.46e-27 |
|
hypothetical protein; Validated
Pssm-ID: 180740 Cd Length: 329 Bit Score: 109.54 E-value: 7.46e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1341381309 84 ERKALLTHEDVKQRAIQTLKWQIANGIQFVRTHVDVsDP--NLVALKAMLEVREEMKEWVELQIVAFPQEGILSyPNGKA 161
Cdd:PRK06886 57 EVKRNSTVEDYYARFSQAIELMISQGVTAFGTFVDI-DPicEDRAIIAAHKAREVYKHDIILKFANQTLKGVIE-PTAKK 134
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1341381309 162 LLEEALKLgADVIGAIPH-FEFTREYGVESLHYVFDLAEKYQVLVDVHCDEIDDEQSRFIETLATLAYERGIGHRVTASH 240
Cdd:PRK06886 135 WFDIGSEM-VDMIGGLPYrDELDYGRGLEAMDILLDTAKSLGKMVHVHVDQFNTPKEKETEQLCDKTIEHGMQGRVVAIH 213
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1341381309 241 TTAMHSYNGAYASRLFRLLRMADINFVANPLVNIHLQGRFDSYPKRRGITRVKEMLEANINVCFGHDDVFDPWYPMGTAN 320
Cdd:PRK06886 214 GISIGAHSKEYRYRLYQKMREADMMVIACPMAWIDSNRKEDLMPFHNALTPADEMIPEGITVALGTDNICDYMVPLCEGD 293
|
250 260
....*....|....*....|..
gi 1341381309 321 MLQVLHMGLHVCQIMGYEQIND 342
Cdd:PRK06886 294 MWQELSLLAAGCRFYDLDEMVN 315
|
|
| SsnA |
COG0402 |
Cytosine/adenosine deaminase or related metal-dependent hydrolase [Nucleotide transport and ... |
17-377 |
3.54e-15 |
|
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: 76.79 E-value: 3.54e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1341381309 17 ILCQGGVIRAIEPMST---QLLSVRELDGEQGLVIPPFIEPHIHLDTTQTAGE-PSWNFSGTLFEGIERwAERKalLTHE 92
Cdd:COG0402 24 VLVEDGRIAAVGPGAElpaRYPAAEVIDAGGKLVLPGLVNTHTHLPQTLLRGLaDDLPLLDWLEEYIWP-LEAR--LDPE 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1341381309 93 DVKQRAIQTLKWQIANGIqfvrTHV-DVSDPNLVALKAMLEVREEMKewveLQIVAFPqeGILSYPNGKALLEEALKLGA 171
Cdd:COG0402 101 DVYAGALLALAEMLRSGT----TTVaDFYYVHPESADALAEAAAEAG----IRAVLGR--GLMDRGFPDGLREDADEGLA 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1341381309 172 DVIGAI----------------PHFEFTreygV--ESLHYVFDLAEKYQVLVDVHC----DEIDDEQSRFIETLATLAYE 229
Cdd:COG0402 171 DSERLIerwhgaadgrirvalaPHAPYT----VspELLRAAAALARELGLPLHTHLaetrDEVEWVLELYGKRPVEYLDE 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1341381309 230 RGI-GHRVTASHTTAMHSyngayasRLFRLLRMADINFVANPLVNIHLqgrfdsypkRRGITRVKEMLEANINVCFGHD- 307
Cdd:COG0402 247 LGLlGPRTLLAHCVHLTD-------EEIALLAETGASVAHCPTSNLKL---------GSGIAPVPRLLAAGVRVGLGTDg 310
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1341381309 308 ----DVFDPWYPMGTANMLQVLHMGLHvcQIMGYEQIndsLKLIGSHSARTLNVQDRYG-IEVGKPANLLILPAE 377
Cdd:COG0402 311 aasnNSLDMFEEMRLAALLQRLRGGDP--TALSAREA---LEMATLGGARALGLDDEIGsLEPGKRADLVVLDLD 380
|
|
| HutI |
COG1228 |
Imidazolonepropionase or related amidohydrolase [Secondary metabolites biosynthesis, transport ... |
1-402 |
1.56e-13 |
|
Imidazolonepropionase or related amidohydrolase [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 440841 [Multi-domain] Cd Length: 386 Bit Score: 71.53 E-value: 1.56e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1341381309 1 MLIRNVRLA-GREGM----WQILCQGGVIRAIEPMSTQLL--SVRELDGEQGLVIPPFIEPHIHLDttqtagepswnFSG 73
Cdd:COG1228 10 LLITNATLVdGTGGGvienGTVLVEDGKIAAVGPAADLAVpaGAEVIDATGKTVLPGLIDAHTHLG-----------LGG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1341381309 74 tlfEGIERWAERKALLTHEDVKQRAIQTLKWQIANGIQFVRTHVDvsdpNLVALKAMLEvREEMKEWVELQIvaFPQEGI 153
Cdd:COG1228 79 ---GRAVEFEAGGGITPTVDLVNPADKRLRRALAAGVTTVRDLPG----GPLGLRDAII-AGESKLLPGPRV--LAAGPA 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1341381309 154 LSYPNG---------KALLEEALKLGADVI-----GAIPHFEftreygVESLHYVFDLAEKYQVLVDVHCDEIDDeqsrf 219
Cdd:COG1228 149 LSLTGGahargpeeaRAALRELLAEGADYIkvfaeGGAPDFS------LEELRAILEAAHALGLPVAAHAHQADD----- 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1341381309 220 ietlATLAYERGI-----GHRVTASHTTAMHSYNGAYASRLFrllrmadinFVANPLVNIHLQGRFDSYPKRRGITR--V 292
Cdd:COG1228 218 ----IRLAVEAGVdsiehGTYLDDEVADLLAEAGTVVLVPTL---------SLFLALLEGAAAPVAAKARKVREAALanA 284
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1341381309 293 KEMLEANINVCFGHDDVFdpWYPMGTANMLQVLHMGLHVcqiMGYEQIndsLKLIGSHSARTLNVQDRYG-IEVGKPANL 371
Cdd:COG1228 285 RRLHDAGVPVALGTDAGV--GVPPGRSLHRELALAVEAG---LTPEEA---LRAATINAAKALGLDDDVGsLEPGKLADL 356
|
410 420 430
....*....|....*....|....*....|.
gi 1341381309 372 LILPAeNGFDAVRRQVPVRYSIRHGRVIADT 402
Cdd:COG1228 357 VLLDG-DPLEDIAYLEDVRAVMKDGRVVDRS 386
|
|
| Amidohydro_1 |
pfam01979 |
Amidohydrolase family; This family of enzymes are a a large metal dependent hydrolase ... |
46-399 |
8.74e-11 |
|
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: 62.90 E-value: 8.74e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1341381309 46 LVIPPFIEPHIHLdttqtagEPSWNFSGTLFEGIERWAERKALLTHedvkqraiqtlkwqIANGIQFVRTHVDVSDPNLV 125
Cdd:pfam01979 1 IVLPGLIDAHVHL-------EMGLLRGIPVPPEFAYEALRLGITTM--------------LKSGTTTVLDMGATTSTGIE 59
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1341381309 126 AL-KAMLEVREEMKEWVELQIVAFPQEGILSYPNGKALLEEALKLGADVIGAI-----PHFEFTreYGVESLHYVFDLAE 199
Cdd:pfam01979 60 ALlEAAEELPLGLRFLGPGCSLDTDGELEGRKALREKLKAGAEFIKGMADGVVfvglaPHGAPT--FSDDELKAALEEAK 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1341381309 200 KYQVLVDVHCDEIDDEQSRFIEtlatlAYERGIGHrvtASHTTAMHSYN-----------GAY--ASRLFRLLRMADINF 266
Cdd:pfam01979 138 KYGLPVAIHALETKGEVEDAIA-----AFGGGIEH---GTHLEVAESGGlldiiklilahGVHlsPTEANLLAEHLKGAG 209
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1341381309 267 VANPLVNIHLqgrfdsypKRRGITRVKEMLEANINVCFGHDDVFDpwypMGTANMLQVL-HMGLHVCQIMGYEQINDSLK 345
Cdd:pfam01979 210 VAHCPFSNSK--------LRSGRIALRKALEDGVKVGLGTDGAGS----GNSLNMLEELrLALELQFDPEGGLSPLEALR 277
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*..
gi 1341381309 346 LIGSHSARTLNVQDRYG-IEVGKPANLLI--LPAENGFDAVRRQVPVRYSIRHGRVI 399
Cdd:pfam01979 278 MATINPAKALGLDDKVGsIEVGKDADLVVvdLDPLAAFFGLKPDGNVKKVIVKGKIV 334
|
|
| Imidazolone-5PH |
cd01296 |
Imidazolonepropionase/imidazolone-5-propionate hydrolase (Imidazolone-5PH) catalyzes the third ... |
17-378 |
1.22e-08 |
|
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: 56.50 E-value: 1.22e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1341381309 17 ILCQGGVIRAIEPMSTQLLS----VRELDGEQGLVIPPFIEPHIHL----DTTQtagEPSWNFSGTLFE-------GIER 81
Cdd:cd01296 1 IAIRDGRIAAVGPAASLPAPgpaaAEEIDAGGRAVTPGLVDCHTHLvfagDRVD---EFAARLAGASYEeilaaggGILS 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1341381309 82 --WAERKAllTHEDVKQRAIQTLKWQIANGIQFVRT----HVDVSDPnlvalKAMLEVREEMKEWVELQIVA-FpqEGIL 154
Cdd:cd01296 78 tvRATRAA--SEDELFASALRRLARMLRHGTTTVEVksgyGLDLETE-----LKMLRVIRRLKEEGPVDLVStF--LGAH 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1341381309 155 SYPNGKALLEEALKLGADVIgaIPHFEftreygveslhyvfdlAEKYQVLVDVHCDEI--DDEQSRfieTLATLAYERGI 232
Cdd:cd01296 149 AVPPEYKGREEYIDLVIEEV--LPAVA----------------EENLADFCDVFCEKGafSLEQSR---RILEAAKEAGL 207
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1341381309 233 GHRVTASHTTAMH------SYNGAYASRLFRL-----LRMADINFVAN--PLVNIHLQgrfDSYPkrrgitRVKEMLEAN 299
Cdd:cd01296 208 PVKIHADELSNIGgaelaaELGALSADHLEHTsdegiAALAEAGTVAVllPGTAFSLR---ETYP------PARKLIDAG 278
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1341381309 300 INVCFGHDdvFDPwYPMGTANMLQVLHMGlhvCQIMGYeQINDSLKLIGSHSARTLNVQDRYG-IEVGKPANLLILPAEN 378
Cdd:cd01296 279 VPVALGTD--FNP-GSSPTSSMPLVMHLA---CRLMRM-TPEEALTAATINAAAALGLGETVGsLEVGKQADLVILDAPS 351
|
|
| ATZ_TRZ_like |
cd01298 |
TRZ/ATZ family contains enzymes from the atrazine degradation pathway and related hydrolases. ... |
1-374 |
6.22e-08 |
|
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: 54.52 E-value: 6.22e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1341381309 1 MLIRNVRL-----AGREGMWQILCQGGVIRAIEPMSTQLL--SVRELDGEQGLVIPPFIEPHIHLDTTQTAGEPS-WNFS 72
Cdd:cd01298 1 ILIRNGTIvttdpRRVLEDGDVLVEDGRIVAVGPALPLPAypADEVIDAKGKVVMPGLVNTHTHLAMTLLRGLADdLPLM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1341381309 73 GTLFEGIERWAerkALLTHEDVKQRAIQTLKWQIANGIQfvrTHVD--VSDPNLVAlkamlevreemKEWVELQIVAFPQ 150
Cdd:cd01298 81 EWLKDLIWPLE---RLLTEEDVYLGALLALAEMIRSGTT---TFADmyFFYPDAVA-----------EAAEELGIRAVLG 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1341381309 151 EGILSYPNGKA-LLEEALKLGADVIGAI-------------PHFEFTreYGVESLHYVFDLAEKYQVLVDVHCDEIDDEQ 216
Cdd:cd01298 144 RGIMDLGTEDVeETEEALAEAERLIREWhgaadgrirvalaPHAPYT--CSDELLREVAELAREYGVPLHIHLAETEDEV 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1341381309 217 SRFIET--LATLAY--ERGI-GHRVTASHttamhsynGAYAS-RLFRLLRMADINFVANPLVNIHLQGrfdsypkrrGIT 290
Cdd:cd01298 222 EESLEKygKRPVEYleELGLlGPDVVLAH--------CVWLTdEEIELLAETGTGVAHNPASNMKLAS---------GIA 284
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1341381309 291 RVKEMLEANINVCFGHD--------DVFDpwyPMGTANMLQ--------------VLHMGlhvcQIMGYEQINdsLKLIG 348
Cdd:cd01298 285 PVPEMLEAGVNVGLGTDgaasnnnlDMFE---EMRLAALLQklahgdptalpaeeALEMA----TIGGAKALG--LDEIG 355
|
410 420
....*....|....*....|....*.
gi 1341381309 349 ShsartlnvqdrygIEVGKPANLLIL 374
Cdd:cd01298 356 S-------------LEVGKKADLILI 368
|
|
| D-HYD |
cd01314 |
D-hydantoinases (D-HYD) also called dihydropyrimidases (DHPase) and related proteins; DHPases ... |
1-221 |
2.54e-04 |
|
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: 42.97 E-value: 2.54e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1341381309 1 MLIRNVRLAGREGMWQ--ILCQGGVIRAIEPMSTQLLSVRELDGEQGLVIPPFIEPHIHLDT----TQTA-----GEPSW 69
Cdd:cd01314 1 LIIKNGTIVTADGSFKadILIEDGKIVAIGPNLEAPGGVEVIDATGKYVLPGGIDPHTHLELpfmgTVTAddfesGTRAA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1341381309 70 NFSGT--------------LFEGIERW---AERKALlthedvkqraiqtlkwqIANGIqfvrtHVDVSDPNlvalkamLE 132
Cdd:cd01314 81 AAGGTttiidfaipnkgqsLLEAVEKWrgkADGKSV-----------------IDYGF-----HMIITDWT-------DS 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1341381309 133 VREEMKEWVELQIVAFpqEGILSYPNgkalleeaLKLGADvigaiphfeftreygvESLHYVFDLAEKYQVLVDVHC--- 209
Cdd:cd01314 132 VIEELPELVKKGISSF--KVFMAYKG--------LLMVDD----------------EELLDVLKRAKELGALVMVHAeng 185
|
250
....*....|..
gi 1341381309 210 DEIDDEQSRFIE 221
Cdd:cd01314 186 DVIAELQKKLLA 197
|
|
| PRK06380 |
PRK06380 |
metal-dependent hydrolase; Provisional |
40-376 |
3.95e-04 |
|
metal-dependent hydrolase; Provisional
Pssm-ID: 180548 [Multi-domain] Cd Length: 418 Bit Score: 42.56 E-value: 3.95e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1341381309 40 LDGEQGLVIPPFIEPHIHLDTTQTAGEpswnFSGT-LFEGIERWAERKALLTHEDVKQRAIQTLKWQIANGIQfvrTHVD 118
Cdd:PRK06380 45 IDATGKVVMPGLINTHAHVGMTASKGL----FDDVdLEEFLMKTFKYDSKRTREGIYNSAKLGMYEMINSGIT---AFVD 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1341381309 119 V-SDPNLVALKA-MLEVREEMKeWVELQIVAFPQEGilsypngkalleEALKLGADVIGAIPHFEF-TREYGV------- 188
Cdd:PRK06380 118 LyYSEDIIAKAAeELGIRAFLS-WAVLDEEITTQKG------------DPLNNAENFIREHRNEELvTPSIGVqgiyvan 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1341381309 189 -ESLHYVFDLAEKYQVLVDVHCDEIDDEQSRFIETLAtlayERGIGH---------RVTASHTTAMhSYNGAyasrlfRL 258
Cdd:PRK06380 185 dETYLKAKEIAEKYDTIMHMHLSETRKEVYDHVKRTG----ERPVEHlekigflnsKLIAAHCVWA-TYHEI------KL 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1341381309 259 LRMADINFVANPLVNIHLqgrfdsypKRRGITRVKEMLEANINVCFGHDDvfdpwypMGTANMLQVLH-MGLHVCQIMGY 337
Cdd:PRK06380 254 LSKNGVKVSWNSVSNFKL--------GTGGSPPIPEMLDNGINVTIGTDS-------NGSNNSLDMFEaMKFSALSVKNE 318
|
330 340 350 360
....*....|....*....|....*....|....*....|....*
gi 1341381309 338 E------QINDSLKLIGSHSARTLNVqDRYGIEVGKPANLLILPA 376
Cdd:PRK06380 319 RwdasiiKAQEILDFATINAAKALEL-NAGSIEVGKLADLVILDA 362
|
|
| PRK08323 |
PRK08323 |
phenylhydantoinase; Validated |
1-59 |
4.31e-03 |
|
phenylhydantoinase; Validated
Pssm-ID: 236240 [Multi-domain] Cd Length: 459 Bit Score: 39.00 E-value: 4.31e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1341381309 1 MLIRNVRLAGREGMWQ--ILCQGGVIRAIEPMStqllSVRELDGEQGLVIPPFIEPHIHLD 59
Cdd:PRK08323 3 TLIKNGTVVTADDTYKadVLIEDGKIAAIGANL----GDEVIDATGKYVMPGGIDPHTHME 59
|
|
| pyrC |
PRK09357 |
dihydroorotase; Validated |
1-58 |
7.34e-03 |
|
dihydroorotase; Validated
Pssm-ID: 236479 [Multi-domain] Cd Length: 423 Bit Score: 38.25 E-value: 7.34e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1341381309 1 MLIRNVRLAGREGMWQ---ILCQGGVIRAIEPmSTQLLSVRELDGEQGLVIPPFIEPHIHL 58
Cdd:PRK09357 3 ILIKNGRVIDPKGLDEvadVLIDDGKIAAIGE-NIEAEGAEVIDATGLVVAPGLVDLHVHL 62
|
|
| |
