|
Name |
Accession |
Description |
Interval |
E-value |
| D-HYD |
cd01314 |
D-hydantoinases (D-HYD) also called dihydropyrimidases (DHPase) and related proteins; DHPases ... |
5-457 |
0e+00 |
|
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: 694.35 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71989490 5 LVIKNGTVVNEDGMFKADVLVRNGIIVEVSPNITALPDTEVIDATDRLVIPGGIDPHTHMQMPYMGEVTKDDFLKGTEAA 84
Cdd:cd01314 1 LIIKNGTIVTADGSFKADILIEDGKIVAIGPNLEAPGGVEVIDATGKYVLPGGIDPHTHLELPFMGTVTADDFESGTRAA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71989490 85 VAGGTTMIIDFCCPDhrNGESLIAGYNRWRSWADPKVCCDYGLSVAITMWRPETAEQMAIITspEFGVNSFKFYMAYENT 164
Cdd:cd01314 81 AAGGTTTIIDFAIPN--KGQSLLEAVEKWRGKADGKSVIDYGFHMIITDWTDSVIEELPELV--KKGISSFKVFMAYKGL 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71989490 165 LMVRDDELFRGMQECAKLRALARVHCENGSVIKEKEIDLLAKGVTGPEGHTQSRPEEIEAEATNRACVLAAQANCPVYIV 244
Cdd:cd01314 157 LMVDDEELLDVLKRAKELGALVMVHAENGDVIAELQKKLLAQGKTGPEYHALSRPPEVEAEATARAIRLAELAGAPLYIV 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71989490 245 HVMTKGAASAISHHRAQGSIVFGEPIAAGLALDGSHYYnEDWLHAARYVMSPPLsRDPTTPELLMKLLAAGELHLTGTDN 324
Cdd:cd01314 237 HVSSKEAADEIARARKKGLPVYGETCPQYLLLDDSDYW-KDWFEGAKYVCSPPL-RPKEDQEALWDGLSSGTLQTVGSDH 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71989490 325 CTYDCRQKSLGKGNFTKIPNGINGVEDRMSVVWEKGVHSGIIDPMRYVSITSSTAAKIFNIYPRKGRIAVGSDADIVIFN 404
Cdd:cd01314 315 CPFNFAQKARGKDDFTKIPNGVPGVETRMPLLWSEGVAKGRITLEKFVELTSTNPAKIFGLYPRKGTIAVGSDADLVIWD 394
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|...
gi 71989490 405 PNATRTISKDTHHHNLDFNIFEGINCHGVAEVTISRGRIVWAHGKLQTVPGSG 457
Cdd:cd01314 395 PNAEKTISADTHHHNVDYNIFEGMKVKGWPVVTISRGKVVVEDGELVGEKGSG 447
|
|
| PRK08323 |
PRK08323 |
phenylhydantoinase; Validated |
5-461 |
0e+00 |
|
phenylhydantoinase; Validated
Pssm-ID: 236240 [Multi-domain] Cd Length: 459 Bit Score: 603.32 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71989490 5 LVIKNGTVVNEDGMFKADVLVRNGIIVEVSPNitalPDTEVIDATDRLVIPGGIDPHTHMQMPYMGEVTKDDFLKGTEAA 84
Cdd:PRK08323 3 TLIKNGTVVTADDTYKADVLIEDGKIAAIGAN----LGDEVIDATGKYVMPGGIDPHTHMEMPFGGTVSSDDFETGTRAA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71989490 85 VAGGTTMIIDFCCPDhrNGESLIAGYNRWRSWADPKVCCDYGLSVAITMWRPETAEQMAIItsPEFGVNSFKFYMAYENT 164
Cdd:PRK08323 79 ACGGTTTIIDFALQP--KGQSLREALEAWHGKAAGKAVIDYGFHMIITDWNEVVLDEMPEL--VEEGITSFKLFMAYKGA 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71989490 165 LMVRDDELFRGMQECAKLRALARVHCENGSVIKEKEIDLLAKGVTGPEGHTQSRPEEIEAEATNRACVLAAQANCPVYIV 244
Cdd:PRK08323 155 LMLDDDELLRALQRAAELGALPMVHAENGDAIAYLQAKLLAEGKTGPEYHALSRPPEVEGEATNRAIMLAELAGAPLYIV 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71989490 245 HVMTKGAASAISHHRAQGSIVFGEPIAAGLALDGSHYYNEDWLHAARYVMSPPLsRDPTTPELLMKLLAAGELHLTGTDN 324
Cdd:PRK08323 235 HVSCKEALEAIRRARARGQRVFGETCPQYLLLDESEYDGPDWFEGAKYVMSPPL-RDKEHQDALWRGLQDGDLQVVATDH 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71989490 325 CTYDCRQ-KSLGKGNFTKIPNGINGVEDRMSVVWEKGVHSGIIDPMRYVSITSSTAAKIFNIYPRKGRIAVGSDADIVIF 403
Cdd:PRK08323 314 CPFCFEQkKQLGRGDFTKIPNGTPGVEDRMPLLFSEGVMTGRITLNRFVELTSTNPAKIFGLYPRKGTIAVGADADIVIW 393
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*...
gi 71989490 404 NPNATRTISKDTHHHNLDFNIFEGINCHGVAEVTISRGRIVWAHGKLQTVPGSGKFIP 461
Cdd:PRK08323 394 DPNATKTISASTLHSNVDYNPYEGFEVTGWPVTTLSRGEVVVEDGEFRGKAGHGRFLK 451
|
|
| D-hydantoinase |
TIGR02033 |
D-hydantoinase; This model represents the D-hydantoinase (dihydropyrimidinase) which primarily ... |
5-461 |
0e+00 |
|
D-hydantoinase; This model represents the D-hydantoinase (dihydropyrimidinase) which primarily converts 5,6-dihydrouracil to 3-ureidopropanoate but also acts on dihydrothymine and hydantoin. The enzyme is a metalloenzyme.
Pssm-ID: 273937 [Multi-domain] Cd Length: 454 Bit Score: 569.71 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71989490 5 LVIKNGTVVNEDGMFKADVLVRNGIIVEVSPNITALPDTEVIDATDRLVIPGGIDPHTHMQMPYMGEVTKDDFLKGTEAA 84
Cdd:TIGR02033 1 LLIKGGTVVNADDVFQADVLIEGGKIVAVGDNLIPPDAVEVIDATGKYVLPGGIDVHTHLEMPFGGTTTADDFFTGTKAA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71989490 85 VAGGTTMIIDFCCPDhrNGESLIAGYNRWRSWADPKVCCDYGLSVAITMWRPETAEQMaIITSPEFGVNSFKFYMAYENT 164
Cdd:TIGR02033 81 AAGGTTTIIDFVVPE--KGSSLTEALETWHEKAEGKSVIDYGFHMDITHWNDSVLEEH-IPEVKEEGINSFKVFMAYKNL 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71989490 165 LMVRDDELFRGMQECAKLRALARVHCENGSVIKEKEIDLLAKGVTGPEGHTQSRPEEIEAEATNRACVLAAQANCPVYIV 244
Cdd:TIGR02033 158 LMVDDEELFEILKRLKELGALLQVHAENGDIIAELQARMLAQGITGPEYHALSRPPELEAEAVARAITLAALADAPLYVV 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71989490 245 HVMTKGAASAISHHRAQGSIVFGEPIAAGLALDGSHYyNEDWLHAARYVMSPPLsRDPTTPELLMKLLAAGELHLTGTDN 324
Cdd:TIGR02033 238 HVSTKDAADEIAQARKKGQPVFGETCPQYLVLDDTHY-DKPGFEGAKYVCSPPL-REPEDQDALWSALSSGALQTVGSDH 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71989490 325 CTYDCRQK-SLGKGNFTKIPNGINGVEDRMSVVWEKGVHSGIIDPMRYVSITSSTAAKIFNIYPRKGRIAVGSDADIVIF 403
Cdd:TIGR02033 316 CTFNFAQKkAIGKDDFTKIPNGGPGVEERMSLLFDEGVAKGRITLEKFVEVTSTNPAKIFNLYPRKGTIAVGSDADIVIW 395
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*...
gi 71989490 404 NPNATRTISKDTHHHNLDFNIFEGINCHGVAEVTISRGRIVWAHGKLQTVPGSGKFIP 461
Cdd:TIGR02033 396 DPNRTTVISAETHHSNADYNPFEGFKVRGAPVSVLSRGRVVVEDGQLVGTAGAGRFVK 453
|
|
| PLN02942 |
PLN02942 |
dihydropyrimidinase |
2-487 |
0e+00 |
|
dihydropyrimidinase
Pssm-ID: 178530 Cd Length: 486 Bit Score: 562.54 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71989490 2 SPPLVIKNGTVVNEDGMFKADVLVRNGIIVEVSPNITALPDTEVIDATDRLVIPGGIDPHTHMQMPYMGEVTKDDFLKGT 81
Cdd:PLN02942 4 STKILIKGGTVVNAHHQELADVYVEDGIIVAVAPNLKVPDDVRVIDATGKFVMPGGIDPHTHLAMPFMGTETIDDFFSGQ 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71989490 82 EAAVAGGTTMIIDFCCPdhRNGeSLIAGYNRWRSWADpKVCCDYGLSVAITMWRPETAEQMAIITSpEFGVNSFKFYMAY 161
Cdd:PLN02942 84 AAALAGGTTMHIDFVIP--VNG-NLLAGYEAYEKKAE-KSCMDYGFHMAITKWDDTVSRDMETLVK-EKGINSFKFFMAY 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71989490 162 ENTLMVRDDELFRGMQECAKLRALARVHCENGSVIKEKEIDLLAKGVTGPEGHTQSRPEEIEAEATNRACVLAAQANCPV 241
Cdd:PLN02942 159 KGSLMVTDELLLEGFKRCKSLGALAMVHAENGDAVFEGQKRMIELGITGPEGHALSRPPLLEGEATARAIRLAKFVNTPL 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71989490 242 YIVHVMTKGAASAISHHRAQGSIVFGEPIAAGLALDGSHYYNEDWLHAARYVMSPPLsRDPTTPELLMKLLAAGELHLTG 321
Cdd:PLN02942 239 YVVHVMSIDAMEEIARARKSGQRVIGEPVVSGLVLDDSKLWDPDFTIASKYVMSPPI-RPAGHGKALQAALSSGILQLVG 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71989490 322 TDNCTYDCRQKSLGKGNFTKIPNGINGVEDRMSVVWEKGVHSGIIDPMRYVSITSSTAAKIFNIYPRKGRIAVGSDADIV 401
Cdd:PLN02942 318 TDHCPFNSTQKAFGKDDFRKIPNGVNGIEERMHLVWDTMVESGQISPTDYVRVTSTECAKIFNIYPRKGAILAGSDADII 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71989490 402 IFNPNATRTISKDTHHHNLDFNIFEGINCHGVAEVTISRGRIVWAHGKLQTVPGSGKFIpLLANSPFVFSTHEKREQKIQ 481
Cdd:PLN02942 398 ILNPNSTFTISAKTHHSRIDTNVYEGRRGKGKVEVTISQGRVVWENGELKVVRGSGRYI-EMPPFSYLFDGIQKADAAYL 476
|
....*.
gi 71989490 482 PRIVER 487
Cdd:PLN02942 477 SSLRAP 482
|
|
| AllB |
COG0044 |
Dihydroorotase or related cyclic amidohydrolase [Nucleotide transport and metabolism]; ... |
6-461 |
6.71e-143 |
|
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: 417.19 E-value: 6.71e-143
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71989490 6 VIKNGTVVNEDGMFKADVLVRNGIIVEVSPNITALPDTEVIDATDRLVIPGGIDPHTHMQMPymGEVTKDDFLKGTEAAV 85
Cdd:COG0044 1 LIKNGRVVDPGGLERADVLIEDGRIAAIGPDLAAPEAAEVIDATGLLVLPGLIDLHVHLREP--GLEHKEDIETGTRAAA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71989490 86 AGGTTMIIDFccPDHRNGESLIAGYNRWRSWADPKVCCDYGLSVAITMWRPETAEQMAIITspEFGVNSFKFYMAYEN-T 164
Cdd:COG0044 79 AGGVTTVVDM--PNTNPVTDTPEALEFKLARAEEKALVDVGPHGALTKGLGENLAELGALA--EAGAVAFKVFMGSDDgN 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71989490 165 LMVRDDELFRGMQECAKLRALARVHCENGSVIKEKeidLLAKGVTGPEGHTQSRPEEIEAEATNRACVLAAQANCPVYIV 244
Cdd:COG0044 155 PVLDDGLLRRALEYAAEFGALVAVHAEDPDLIRGG---VMNEGKTSPRLGLKGRPAEAEEEAVARDIALAEETGARLHIV 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71989490 245 HVMTKGAASAISHHRAQGSIVFGEPIAAGLALDGSHYYNEDwlhaARYVMSPPLsRDPTTPELLMKLLAAGELHLTGTDN 324
Cdd:COG0044 232 HVSTAEAVELIREAKARGLPVTAEVCPHHLTLTDEDLERYG----TNFKVNPPL-RTEEDREALWEGLADGTIDVIATDH 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71989490 325 CTYDCRQKslgKGNFTKIPNGINGVEDRMSVVWEKGVHSGIIDPMRYVSITSSTAAKIFNIyPRKGRIAVGSDADIVIFN 404
Cdd:COG0044 307 APHTLEEK---ELPFAEAPNGIPGLETALPLLLTELVHKGRLSLERLVELLSTNPARIFGL-PRKGRIAVGADADLVLFD 382
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*..
gi 71989490 405 PNATRTISKDTHHHNLDFNIFEGINCHGVAEVTISRGRIVWAHGKLQTVPgSGKFIP 461
Cdd:COG0044 383 PDAEWTVTAEDLHSKSKNTPFEGRELTGRVVATIVRGRVVYEDGEVVGEP-RGRFLR 438
|
|
| PRK13404 |
PRK13404 |
dihydropyrimidinase; Provisional |
5-461 |
1.03e-115 |
|
dihydropyrimidinase; Provisional
Pssm-ID: 184033 [Multi-domain] Cd Length: 477 Bit Score: 349.00 E-value: 1.03e-115
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71989490 5 LVIKNGTVVNEDGMFKADVLVRNGIIVEVSPNITalPDTEVIDATDRLVIPGGIDPHTHMQMPY-MGEVTKDDFLKGTEA 83
Cdd:PRK13404 6 LVIRGGTVVTATDTFQADIGIRGGRIAALGEGLG--PGAREIDATGRLVLPGGVDSHCHIDQPSgDGIMMADDFYTGTVS 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71989490 84 AVAGGTTMIIDFCCPdHRnGESLIAGYNRWRSWADPKVCCDYGLSVAITMWRPETAEQM--AIITSpefGVNSFKFYMAY 161
Cdd:PRK13404 84 AAFGGTTTVIPFAAQ-HR-GQSLREAVEDYHRRAAGKAVIDYAFHLIVADPTEEVLTEElpALIAQ---GYTSFKVFMTY 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71989490 162 ENtLMVRDDELFRGMQECAKLRALARVHCENGSVIKEKEIDLLAKGVTGPEGHTQSRPEEIEAEATNRACVLAAQANCPV 241
Cdd:PRK13404 159 DD-LKLDDRQILDVLAVARRHGAMVMVHAENHDMIAWLTKRLLAAGLTAPKYHAISRPMLAEREATHRAIALAELVDVPI 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71989490 242 YIVHVMTKGAASAISHHRAQGSIVFGEPIAAGLALDgSHYYNEDWLHAARYVMSPPLsRDPTTPELLMKLLAAGELHLTG 321
Cdd:PRK13404 238 LIVHVSGREAAEQIRRARGRGLKIFAETCPQYLFLT-AEDLDRPGMEGAKYICSPPP-RDKANQEAIWNGLADGTFEVFS 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71989490 322 TDNCTY--DCRQKSLGKG---NFTKIPNGINGVEDRMSVVWEKGVHSGIIDPMRYVSITSSTAAKIFNIYPRKGRIAVGS 396
Cdd:PRK13404 316 SDHAPFrfDDTDGKLAAGanpSFKAIANGIPGIETRLPLLFSEGVVKGRISLNRFVALTSTNPAKLYGLYPRKGAIAIGA 395
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 71989490 397 DADIVIFNPNATRTISKDTHHHNLDFNIFEGINCHGVAEVTISRGRIVWAHGKLQTVPGSGKFIP 461
Cdd:PRK13404 396 DADIAIWDPDREVTITNADLHHAADYTPYEGMRVTGWPVTVLSRGRVVVEDGELVAERGSGQFLA 460
|
|
| L-HYD_ALN |
cd01315 |
L-Hydantoinases (L-HYDs) and Allantoinase (ALN); L-Hydantoinases are a member of the ... |
5-460 |
6.06e-74 |
|
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: 240.27 E-value: 6.06e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71989490 5 LVIKNGTVVNEDGMFKADVLVRNGIIVEVSPNITALPDTEVIDATDRLVIPGGIDPHTHMQMPymGEVTKDDFLKGTEAA 84
Cdd:cd01315 2 LVIKNGRVVTPDGVREADIAVKGGKIAAIGPDIANTEAEEVIDAGGLVVMPGLIDTHVHINEP--GRTEWEGFETGTKAA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71989490 85 VAGGTTMIIDF---CCPDHRNGESLIAGYNRwrswADPKVCCDYGLSVAITmwrPETAEQmaIITSPEFGVNSFKFYMA- 160
Cdd:cd01315 80 AAGGITTIIDMplnSIPPTTTVENLEAKLEA----AQGKLHVDVGFWGGLV---PGNLDQ--LRPLDEAGVVGFKCFLCp 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71989490 161 --YENTLMVRDDELFRGMQECAKLRALARVHCENGSVIKEKEIDLLAKGVTGPEGHTQSRPEEIEAEATNRACVLAAQAN 238
Cdd:cd01315 151 sgVDEFPAVDDEQLEEAMKELAKTGSVLAVHAENPEITEALQEQAKAKGKRDYRDYLASRPVFTEVEAIQRILLLAKETG 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71989490 239 CPVYIVHVMTKGAASAISHHRAQGSIVFGEPIAAGLALDGshyynEDWLH-AARYVMSPPLsRDPTTPELLMKLLAAGEL 317
Cdd:cd01315 231 CRLHIVHLSSAEAVPLIREARAEGVDVTVETCPHYLTFTA-----EDVPDgGTEFKCAPPI-RDAANQEQLWEALENGDI 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71989490 318 HLTGTDN--CTYDcrQKSLGKGNFTKIPNGINGVEDRMSVVWEKGVHSGIIDPMRYVSITSSTAAKIFNIYPRKGRIAVG 395
Cdd:cd01315 305 DMVVSDHspCTPE--LKLLGKGDFFKAWGGISGLQLGLPVMLTEAVNKRGLSLEDIARLMCENPAKLFGLSHQKGRIAVG 382
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 71989490 396 SDADIVIFNPNATRTISKDT--HHHNLdfNIFEGINCHGVAEVTISRGRIVWAHGKLQTVPgSGKFI 460
Cdd:cd01315 383 YDADFVVWDPEEEFTVDAEDlyYKNKI--SPYVGRTLKGRVHATILRGTVVYQDGEVVGEP-LGQLL 446
|
|
| Cyclic_amidohydrolases |
cd01302 |
Cyclic amidohydrolases, including hydantoinase, dihydropyrimidinase, allantoinase, and ... |
52-432 |
1.18e-66 |
|
Cyclic amidohydrolases, including hydantoinase, dihydropyrimidinase, allantoinase, and dihydroorotase, are involved in the metabolism of pyrimidines and purines, sharing the property of hydrolyzing the cyclic amide bond of each substrate to the corresponding N-carbamyl amino acids. Allantoinases catalyze the degradation of purines, while dihydropyrimidinases and hydantoinases, a microbial counterpart of dihydropyrimidinase, are involved in pyrimidine degradation. Dihydroorotase participates in the de novo synthesis of pyrimidines.
Pssm-ID: 238627 [Multi-domain] Cd Length: 337 Bit Score: 217.64 E-value: 1.18e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71989490 52 LVIPGGIDPHTHMQMPYmGEVTKDDFLKGTEAAVAGGTTMIIDFCcpdhRNGESLIAG--YNRWRSWADPKVCCDYGLSV 129
Cdd:cd01302 2 LVLPGFIDIHVHLRDPG-GTTYKEDFESGSRAAAAGGVTTVIDMP----NTGPPPIDLpaIELKIKLAEESSYVDFSFHA 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71989490 130 AItmWRPETAEQMAiiTSPEFGVNSFKFYMAYENTLM--VRDDELFRGMQECAKLRALARVHCEngsvikekeidllakg 207
Cdd:cd01302 77 GI--GPGDVTDELK--KLFDAGINSLKVFMNYYFGELfdVDDGTLMRTFLEIASRGGPVMVHAE---------------- 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71989490 208 vtgpeghtqsrpeeieaeatnRACVLAAQANCPVYIVHVMTKGAASAISHHRAQGSIVFGEPIAAGLALDGSHYYNEdwl 287
Cdd:cd01302 137 ---------------------RAAQLAEEAGANVHIAHVSSGEALELIKFAKNKGVKVTCEVCPHHLFLDESMLRLN--- 192
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71989490 288 hAARYVMSPPLsRDPTTPELLMKLLAAGELHLTGTDNCTYDCRQKSLGKgNFTKIPNGINGVEDRMSVVWEKGVHSGIId 367
Cdd:cd01302 193 -GAWGKVNPPL-RSKEDREALWEGVKNGKIDTIASDHAPHSKEEKESGK-DIWKAPPGFPGLETRLPILLTEGVKRGLS- 268
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 71989490 368 PMRYVSITSSTAAKIFNIYPrKGRIAVGSDADIVIFNPNATRTISKDTHHHNLDFNIFEGINCHG 432
Cdd:cd01302 269 LETLVEILSENPARIFGLYP-KGTIAVGYDADLVIVDPKKEWKVTAEEIESKADWTPFEGMEVTG 332
|
|
| allantoinase |
TIGR03178 |
allantoinase; This enzyme carries out the first step in the degradation of allantoin, a ... |
5-461 |
2.91e-65 |
|
allantoinase; This enzyme carries out the first step in the degradation of allantoin, a ring-opening hydrolysis. The seed members of this model are all in the vicinity of other genes involved in the processes of xanthine/urate/allantoin catabolism. Although not included in the seed, many eukaryotic homologs of this family are included above the trusted cutoff. Below the noise cutoff are related hydantoinases.
Pssm-ID: 163175 [Multi-domain] Cd Length: 443 Bit Score: 217.25 E-value: 2.91e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71989490 5 LVIKNGTVVNEDGMFKADVLVRNGIIVEVSPNITAlPDTEVIDATDRLVIPGGIDPHTHMQMPymGEVTKDDFLKGTEAA 84
Cdd:TIGR03178 2 LIIRGGRVILPNGEREADVGVKGGKIAAIGPDILG-PAAKIIDAGGLVVFPGVVDTHVHINEP--GRTEWEGFETGTRAA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71989490 85 VAGGTTMIIDF---CCPDHRNGESLIAGynrwRSWADPKVCCDYGLSVAITmwrPETAEQMAIITspEFGVNSFKFYMAY 161
Cdd:TIGR03178 79 AAGGITTYIDMplnSIPATTTRASLEAK----FEAAKGKLAVDVGFWGGLV---PYNLDDLRELD--EAGVVGFKAFLSP 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71989490 162 ---ENTLMVRDDELFRGMQECAKLRALARVHCENGSVIKEKEIDLLAKGVTGPEGHTQSRPEEIEAEATNRACVLAAQAN 238
Cdd:TIGR03178 150 sgdDEFPHVDDWQLYKGMRELARLGQLLLVHAENPAITSALGEEAPPQGGVGADAYLASRPVFAEVEAIRRTLALAKVTG 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71989490 239 CPVYIVHVMTKGAASAISHHRAQGSIVFGEPIaaglaldgSHY---YNEDWLH-AARYVMSPPLsRDPTTPELLMKLLAA 314
Cdd:TIGR03178 230 CRVHVVHLSSAEAVELITEAKQEGLDVTVETC--------PHYltlTAEEVPDgGTLAKCAPPI-RDLANQEGLWEALLN 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71989490 315 GELHLTGTDN--CTYDCRQkslgKGNFTKIPNGINGVEDRMSVVWEKGVHSGIIDPMRYVSITSSTAAKIFNIyPRKGRI 392
Cdd:TIGR03178 301 GLIDCVVSDHspCTPDLKR----AGDFFKAWGGIAGLQSTLDVMFDEAVQKRGLPLEDIARLMATNPAKRFGL-AQKGRI 375
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 71989490 393 AVGSDADIVIFNPNATRTISKDTHHHNLDFNIFEGINCHGVAEVTISRGRIVWAHGKLQTVPgSGKFIP 461
Cdd:TIGR03178 376 APGKDADFVFVDPDESYTLTPDDLYYRHKVSPYVGRTIGGRVRATYLRGQCIYDDEQFIGAP-KGQLLL 443
|
|
| PRK06189 |
PRK06189 |
allantoinase; Provisional |
1-454 |
1.38e-60 |
|
allantoinase; Provisional
Pssm-ID: 235732 [Multi-domain] Cd Length: 451 Bit Score: 205.32 E-value: 1.38e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71989490 1 MSPPLVIKNGTVVNEDGMFKADVLVRNGIIVEVSPNITAlPDTEVIDATDRLVIPGGIDPHTHMQMPymGEVTKDDFLKG 80
Cdd:PRK06189 1 MMYDLIIRGGKVVTPEGVYRADIGIKNGKIAEIAPEISS-PAREIIDADGLYVFPGMIDVHVHFNEP--GRTHWEGFATG 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71989490 81 TEAAVAGGTTMIIDF---CCPDHRNGESLIAGynrwRSWADPKVCCDYGLSVAITMWRPETAEQMAiitspEFGVNSFKF 157
Cdd:PRK06189 78 SAALAAGGCTTYFDMplnSIPPTVTREALDAK----AELARQKSAVDFALWGGLVPGNLEHLRELA-----EAGVIGFKA 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71989490 158 YMAYENTLMVR--DDE-LFRGMQECAKLRALARVHCENGSVIKEKEIDLLAKGVTGPEGHTQSRPEEIEAEATNRACVLA 234
Cdd:PRK06189 149 FMSNSGTDEFRssDDLtLYEGMKEIAALGKILALHAESDALTRHLTTQARQQGKTDVRDYLESRPVVAELEAVQRALLYA 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71989490 235 AQANCPVYIVHVMTKGAASAISHHRAQGSIVFGE--PiaaglaldgsHY--YNEDWLHAARYVM--SPPLsRDPTTPELL 308
Cdd:PRK06189 229 QETGCPLHFVHISSGKAVALIAEAKKRGVDVSVEtcP----------HYllFTEEDFERIGAVAkcAPPL-RSRSQKEEL 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71989490 309 MKLLAAGELHLTGTDN--CTYDCRQKSlgkgNFTKIPNGINGVEDRMSVVWEKGVHSGIIDPMRYVSITSSTAAKIFNIy 386
Cdd:PRK06189 298 WRGLLAGEIDMISSDHspCPPELKEGD----DFFLVWGGISGGQSTLLVMLTEGYIERGIPLETIARLLATNPAKRFGL- 372
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 71989490 387 PRKGRIAVGSDADIVIFNPNATRTISKDTHHHNLDFNIFEGINCHGVAEVTISRGRIVWAHGKLQTVP 454
Cdd:PRK06189 373 PQKGRLEVGADADFVLVDLDETYTLTKEDLFYRHKQSPYEGRTFPGRVVATYLRGQCVYQDGEVFPPP 440
|
|
| PRK02382 |
PRK02382 |
dihydroorotase; Provisional |
5-461 |
1.80e-57 |
|
dihydroorotase; Provisional
Pssm-ID: 179417 [Multi-domain] Cd Length: 443 Bit Score: 196.80 E-value: 1.80e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71989490 5 LVIKNGTVVNEDGMFKADVLVRNGIIVEVSPNITALPDTEVIDATDRLVIPGGIDPHTHMQMPYMGEvtKDDFLKGTEAA 84
Cdd:PRK02382 4 ALLKDGRVYYNNSLQPRDVRIDGGKITAVGKDLDGSSSEEVIDARGMLLLPGGIDVHVHFREPGYTH--KETWYTGSRSA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71989490 85 VAGGTTMIIdfccpDHRN-------GESliagYNRWRSWADPKVCCDYGLSVAIT--------MW-RPETAeqmaiitsp 148
Cdd:PRK02382 82 AAGGVTTVV-----DQPNtdpptvdGES----FDEKAELAARKSIVDFGINGGVTgnwdplesLWeRGVFA--------- 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71989490 149 eFGvnsfKFYMAYENTLMVRDDELFR-GMQECAKLRALARVHCENGSVIKEKEIDLlaKGVTGPEGHTQSRPEEIEAEAT 227
Cdd:PRK02382 144 -LG----EIFMADSTGGMGIDEELFEeALAEAARLGVLATVHAEDEDLFDELAKLL--KGDADADAWSAYRPAAAEAAAV 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71989490 228 NRACVLAAQANCPVYIVHVMTKGAASAIS----------HHraqgsivfgepiaagLALDGSHYynEDWLHAARyvMSPP 297
Cdd:PRK02382 217 ERALEVASETGARIHIAHISTPEGVDAARregitcevtpHH---------------LFLSRRDW--ERLGTFGK--MNPP 277
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71989490 298 LsRDPTTPELLMKLLAAGELHLTGTDNCTYDCRQKSLGkgnFTKIPNGINGVEDRMSVVWEkGVHSGIIDPMRYVSITSS 377
Cdd:PRK02382 278 L-RSEKRREALWERLNDGTIDVVASDHAPHTREEKDAD---IWDAPSGVPGVETMLPLLLA-AVRKNRLPLERVRDVTAA 352
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71989490 378 TAAKIFNIyPRKGRIAVGSDADIVIFNPNATRTISKDTHHHNLDFNIFEGINchGV-AEVTISRGRIVWAHGKLQTVPGS 456
Cdd:PRK02382 353 NPARIFGL-DGKGRIAEGYDADLVLVDPDAAREIRGDDLHSKAGWTPFEGME--GVfPELTMVRGTVVWDGDDINAKRGR 429
|
....*
gi 71989490 457 GKFIP 461
Cdd:PRK02382 430 GEFLR 434
|
|
| pyrC_multi |
TIGR00857 |
dihydroorotase, multifunctional complex type; In contrast to the homodimeric type of ... |
18-444 |
1.82e-47 |
|
dihydroorotase, multifunctional complex type; In contrast to the homodimeric type of dihydroorotase found in E. coli, this class tends to appear in a large, multifunctional complex with aspartate transcarbamoylase. Homologous domains appear in multifunctional proteins of higher eukaryotes. In some species, including Pseudomonas putida and P. aeruginosa, this protein is inactive but is required as a non-catalytic subunit of aspartate transcarbamoylase (ATCase). In these species, a second, active dihydroorotase is also present. The seed for this model does not include any example of the dihydroorotase domain of eukaryotic multidomain pyrimidine synthesis proteins. All proteins described by this model should represent active and inactive dihydroorotase per se and functionally equivalent domains of multifunctional proteins from higher eukaryotes, but exclude related proteins such as allantoinase. [Purines, pyrimidines, nucleosides, and nucleotides, Pyrimidine ribonucleotide biosynthesis]
Pssm-ID: 273302 [Multi-domain] Cd Length: 411 Bit Score: 169.16 E-value: 1.82e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71989490 18 MFKADVLVRNGIIVEVSPNItALPDTEVIDATDRLVIPGGIDPHTHMQMPymGEVTKDDFLKGTEAAVAGGTTMIIDF-- 95
Cdd:TIGR00857 3 ETEVDILVEGGRIKKIGKLR-IPPDAEVIDAKGLLVLPGFIDLHVHLRDP--GEEYKEDIESGSKAAAHGGFTTVADMpn 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71989490 96 CCPDHRNGESLiagYNRWRSwADPKVCCDYGLSVAITMWRP--ETAEQMAIITSPEFGVNSFKFYMAYENTLMVRddelf 173
Cdd:TIGR00857 80 TKPPIDTPETL---EWKLQR-LKKVSLVDVHLYGGVTQGNQgkELTEAYELKEAGAVGRMFTDDGSEVQDILSMR----- 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71989490 174 RGMQECAKLRALARVHCENGSVIKEKEIDllaKGVTGPEGHTQSRPEEIEAEATNRACVLAAQANCPVYIVHVMTKGAAS 253
Cdd:TIGR00857 151 RALEYAAIAGVPIALHAEDPDLIYGGVMH---EGPSAAQLGLPARPPEAEEVAVARLLELAKHAGCPVHICHISTKESLE 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71989490 254 AISHHRAQGSIVFGEPIAAGLALDgshyyNEDWLHAARYV-MSPPLsRDPTTPELLMKLLAAGELHLTGTDNCTYDCRQK 332
Cdd:TIGR00857 228 LIVKAKSQGIKITAEVTPHHLLLS-----EEDVARLDGNGkVNPPL-REKEDRLALIEGLKDGIIDIIATDHAPHTLEEK 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71989490 333 SLgkgNFTKIPNGINGVEDRMSVVWEkGVHSGIIDPMRYVSITSSTAAKIFNIyPRKGRIAVGSDADIVIFNPNATRTIS 412
Cdd:TIGR00857 302 TK---EFAAAPPGIPGLETALPLLLQ-LLVKGLISLKDLIRMLSINPARIFGL-PDKGTLEEGNPADITVFDLKKEWTIN 376
|
410 420 430
....*....|....*....|....*....|..
gi 71989490 413 KDTHHHNLDFNIFEGINCHGVAEVTISRGRIV 444
Cdd:TIGR00857 377 AETFYSKAKNTPFEGMSLKGKPIATILRGKVV 408
|
|
| DHOase_IIa |
cd01317 |
Dihydroorotase (DHOase), subgroup IIa; DHOases catalyze the reversible interconversion of ... |
42-437 |
8.74e-41 |
|
Dihydroorotase (DHOase), subgroup IIa; DHOases catalyze the reversible interconversion of carbamoyl aspartate to dihydroorotate, a key reaction in pyrimidine biosynthesis. This subgroup also contains proteins that lack the active site, like unc-33, a C.elegans protein involved in axon growth.
Pssm-ID: 238642 [Multi-domain] Cd Length: 374 Bit Score: 150.08 E-value: 8.74e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71989490 42 DTEVIDATDRLVIPGGIDPHTHMQMPymGEVTKDDFLKGTEAAVAGGTTMIIdfCCPDHR----NGESLIAGYNRWRSwA 117
Cdd:cd01317 1 DAEVIDAEGKILAPGLVDLHVHLREP--GFEYKETLESGAKAAAAGGFTTVV--CMPNTNpvidNPAVVELLKNRAKD-V 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71989490 118 DPKVCCDYGlsvAITmwRPETAEQMAiitspefGVNSFKFY--MAYENT-LMVRDDELF-RGMQECAKLRALARVHCEN- 192
Cdd:cd01317 76 GIVRVLPIG---ALT--KGLKGEELT-------EIGELLEAgaVGFSDDgKPIQDAELLrRALEYAAMLDLPIIVHPEDp 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71989490 193 ----GSVIKEKEidllakgVTGPEGhTQSRPEEIEAEATNRACVLAAQANCPVYIVHVMTKGAASAISHHRAQGSIVFGE 268
Cdd:cd01317 144 slagGGVMNEGK-------VASRLG-LPGIPPEAETIMVARDLELAEATGARVHFQHLSTARSLELIRKAKAKGLPVTAE 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71989490 269 PIAAGLALDGSHYYNEDwlhaARYVMSPPLsRDPTTPELLMKLLAAGELHLTGTDNC--TYDCRQKSlgkgnFTKIPNGI 346
Cdd:cd01317 216 VTPHHLLLDDEALESYD----TNAKVNPPL-RSEEDREALIEALKDGTIDAIASDHAphTDEEKDLP-----FAEAPPGI 285
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71989490 347 NGVEDRMSVVWEKGVHSGIIDPMRYVSITSSTAAKIFNIYPrkGRIAVGSDADIVIFNPNATRTISKDTHHHNLDFNIFE 426
Cdd:cd01317 286 IGLETALPLLWTLLVKGGLLTLPDLIRALSTNPAKILGLPP--GRLEVGAPADLVLFDPDAEWIVDEETFRSKSKNTPFD 363
|
410
....*....|.
gi 71989490 427 GINCHGVAEVT 437
Cdd:cd01317 364 GQKLKGRVLAT 374
|
|
| PRK08044 |
PRK08044 |
allantoinase AllB; |
1-461 |
4.59e-38 |
|
allantoinase AllB;
Pssm-ID: 169193 [Multi-domain] Cd Length: 449 Bit Score: 144.61 E-value: 4.59e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71989490 1 MSPPLVIKNGTVVNEDGMFKADVLVRNGIIVEVSPNITAlpDTEVIDATDRLVIPGGIDPHTHMQMPymGEVTKDDFLKG 80
Cdd:PRK08044 1 MSFDLIIKNGTVILENEARVVDIAVKGGKIAAIGQDLGD--AKEVMDASGLVVSPGMVDAHTHISEP--GRSHWEGYETG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71989490 81 TEAAVAGGTTMIIDFC---CPDHRNGESLIAGYNRwrswADPKVCCD---YGLSVAITMWRPETAEqmaiitspEFGVNS 154
Cdd:PRK08044 77 TRAAAKGGITTMIEMPlnqLPATVDRASIELKFDA----AKGKLTIDaaqLGGLVSYNLDRLHELD--------EVGVVG 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71989490 155 FKFYMA------YENTLM-VRDDELFRGMQECAKLRALARVHCENGSVIKEKEIDLLAKGVTGPEGHTQSRPEEIEAEAT 227
Cdd:PRK08044 145 FKCFVAtcgdrgIDNDFRdVNDWQFYKGAQKLGELGQPVLVHCENALICDELGEEAKREGRVTAHDYVASRPVFTEVEAI 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71989490 228 NRACVLAAQANCPVYIVHVMTKGAASAISHHRAQGSIVFGEPIAAGLALDgshyyNEDWLHAARYVMSPPLSRDPTTPEL 307
Cdd:PRK08044 225 RRVLYLAKVAGCRLHVCHISSPEGVEEVTRARQEGQDVTCESCPHYFVLD-----TDQFEEIGTLAKCSPPIRDLENQKG 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71989490 308 LMKLLAAGELHLTGTDN--CTYDcrqksLGKGNFTKIPNGINGVEDRMSVVWEKGVHS-GIIDPMrYVSITSSTAAKIFN 384
Cdd:PRK08044 300 MWEKLFNGEIDCLVSDHspCPPE-----MKAGNIMEAWGGIAGLQNCMDVMFDEAVQKrGMSLPM-FGKLMATNAADIFG 373
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 71989490 385 IyPRKGRIAVGSDADIVIFNPNATRTISKDTHHHNLDFNIFEGINCHGVAEVTISRGRIVWAHGKLQTVPGSGKFIP 461
Cdd:PRK08044 374 L-QQKGRIAPGKDADFVFIQPNSSYVLKNEDLEYRHKVSPYVGRTIGARITKTILRGDVIYDIEQGFPVAPKGQFIL 449
|
|
| PRK07575 |
PRK07575 |
dihydroorotase; Provisional |
1-452 |
4.29e-37 |
|
dihydroorotase; Provisional
Pssm-ID: 236055 [Multi-domain] Cd Length: 438 Bit Score: 141.74 E-value: 4.29e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71989490 1 MSPPLVIKNGTVVNEDGMF-KADVLVRNGIIVEVSPNITALPDTEVIDATDRLVIPGGIDPHTHMQMPymGEVTKDDFLK 79
Cdd:PRK07575 1 MMMSLLIRNARILLPSGELlLGDVLVEDGKIVAIAPEISATAVDTVIDAEGLTLLPGVIDPQVHFREP--GLEHKEDLFT 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71989490 80 GTEAAVAGGTTMIIDFccPDHRNGESLIAGYNRWRSWADPKVCCDYGLSVAITmwrPETAEQMaIITSPEFGVnsfKFYM 159
Cdd:PRK07575 79 ASRACAKGGVTSFLEM--PNTKPLTTTQAALDDKLARAAEKCVVNYGFFIGAT---PDNLPEL-LTANPTCGI---KIFM 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71989490 160 -AYENTLMVRDDELFRgmQECAKLRALARVHCENGSVIKEKEIDLlaKGVTGPEGHTQSRPEEIEAEATNRACVLAAQAN 238
Cdd:PRK07575 150 gSSHGPLLVDEEAALE--RIFAEGTRLIAVHAEDQARIRARRAEF--AGISDPADHSQIQDEEAALLATRLALKLSKKYQ 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71989490 239 CPVYIVHVMTkgAASAISHHRAQGSIVFGEPIAAGLALDGSHYYNEDWLHAaryvMSPPLsRDPTTPELLMKLLAAGELH 318
Cdd:PRK07575 226 RRLHILHLST--AIEAELLRQDKPSWVTAEVTPQHLLLNTDAYERIGTLAQ----MNPPL-RSPEDNEALWQALRDGVID 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71989490 319 LTGTDNCTYDCRQKSLGkgnFTKIPNGINGVEDRMSVVWEKgVHSGIIDPMRYVSITSSTAAKIFNIyPRKGRIAVGSDA 398
Cdd:PRK07575 299 FIATDHAPHTLEEKAQP---YPNSPSGMPGVETSLPLMLTA-AMRGKCTVAQVVRWMSTAVARAYGI-PNKGRIAPGYDA 373
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....
gi 71989490 399 DIVIFNPNATRTISKDTHHHNLDFNIFEGINCHGVAEVTISRGRIVWAHGKLQT 452
Cdd:PRK07575 374 DLVLVDLNTYRPVRREELLTKCGWSPFEGWNLTGWPVTTIVGGQIVFDRGQVNT 427
|
|
| pyrC |
PRK09357 |
dihydroorotase; Validated |
5-445 |
6.80e-37 |
|
dihydroorotase; Validated
Pssm-ID: 236479 [Multi-domain] Cd Length: 423 Bit Score: 140.72 E-value: 6.80e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71989490 5 LVIKNGTVVNEDGM-FKADVLVRNGIIVEVSPNItALPDTEVIDATDRLVIPGGIDPHTHMQMPymGEVTKDDFLKGTEA 83
Cdd:PRK09357 3 ILIKNGRVIDPKGLdEVADVLIDDGKIAAIGENI-EAEGAEVIDATGLVVAPGLVDLHVHLREP--GQEDKETIETGSRA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71989490 84 AVAGGTTMIidfCC-------PDHRNGESLIAGYNRWRSWADPKVccdYGlsvAITmwRPETAEQMAiitspEFGvnsfk 156
Cdd:PRK09357 80 AAAGGFTTV---VAmpntkpvIDTPEVVEYVLDRAKEAGLVDVLP---VG---AIT--KGLAGEELT-----EFG----- 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71989490 157 fYMAYENTLMVRDDE--------LFRGMQECAKLRALARVHCE-----NGSVIKEKEI-DLLakGVTGpeghtqsRPEEI 222
Cdd:PRK09357 139 -ALKEAGVVAFSDDGipvqdarlMRRALEYAKALDLLIAQHCEdpsltEGGVMNEGEVsARL--GLPG-------IPAVA 208
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71989490 223 EAEATNRACVLAAQANCPVYIVHVMTKGAASAISHHRAQGSIVFGEPIAAGLALDGSHYYNEDwlhaARYVMSPPLsRDP 302
Cdd:PRK09357 209 EEVMIARDVLLAEATGARVHICHVSTAGSVELIRWAKALGIKVTAEVTPHHLLLTDEDLLTYD----PNYKVNPPL-RTE 283
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71989490 303 TTPELLMKLLAAGELHLTGTD---------NCtydcrqkslgkgNFTKIPNGINGVEDRMSVVWEKGVHSGIIDPMRYVS 373
Cdd:PRK09357 284 EDREALIEGLKDGTIDAIATDhaphareekEC------------EFEAAPFGITGLETALSLLYTTLVKTGLLDLEQLLE 351
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 71989490 374 ITSSTAAKIFNIYPrkGRIAVGSDADIVIFNPNATRTISKDTHHHNLDFNIFEGINCHGVAEVTISRGRIVW 445
Cdd:PRK09357 352 KMTINPARILGLPA--GPLAEGEPADLVIFDPEAEWTVDGEDFASKGKNTPFIGMKLKGKVVYTIVDGKIVY 421
|
|
| DHOase_IIb |
cd01318 |
Dihydroorotase (DHOase), subgroup IIb; DHOases catalyze the reversible interconversion of ... |
50-441 |
1.90e-36 |
|
Dihydroorotase (DHOase), subgroup IIb; DHOases catalyze the reversible interconversion of carbamoyl aspartate to dihydroorotate, a key reaction in pyrimidine biosynthesis. This group contains the archeal members of the DHOase family.
Pssm-ID: 238643 [Multi-domain] Cd Length: 361 Bit Score: 138.24 E-value: 1.90e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71989490 50 DRLVIPGGIDPHTHMQMPymGEVTKDDFLKGTEAAVAGGTTMIIDFccPDHRNGESLIAGYNRWRSWADPKVCCDYGLSV 129
Cdd:cd01318 1 GLLILPGVIDIHVHFREP--GLTYKEDFVSGSRAAAAGGVTTVMDM--PNTKPPTTTAEALYEKLRLAAAKSVVDYGLYF 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71989490 130 AITmwRPETAEQMAiitspEFGVNSFKFYMA-YENTLMVRDDELFRgmqECAKLRALARVHCENGSVIKEKEIDLLakgv 208
Cdd:cd01318 77 GVT--GSEDLEELD-----KAPPAGYKIFMGdSTGDLLDDEETLER---IFAEGSVLVTFHAEDEDRLRENRKELK---- 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71989490 209 tGPEGHTQSRPEEIEAEATNRACVLAAQANCPVYIVHVMTKGAASAIS------------HHraqgsivfgepiaagLAL 276
Cdd:cd01318 143 -GESAHPRIRDAEAAAVATARALKLARRHGARLHICHVSTPEELKLIKkakpgvtvevtpHH---------------LFL 206
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71989490 277 DGSHYYNED-WLHaaryvMSPPLsRDPTTPELLMKLLAAGELHLTGTDNCTYDCRQKSLGkgnFTKIPNGINGVEDRMSV 355
Cdd:cd01318 207 DVEDYDRLGtLGK-----VNPPL-RSREDRKALLQALADGRIDVIASDHAPHTLEEKRKG---YPAAPSGIPGVETALPL 277
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71989490 356 VWEKgVHSGIIDPMRYVSITSSTAAKIFNIyPRKGRIAVGSDADIVIFNPNATRTISKDTHHHNLDFNIFEGINCHGVAE 435
Cdd:cd01318 278 MLTL-VNKGILSLSRVVRLTSHNPARIFGI-KNKGRIAEGYDADLTVVDLKEERTIRAEEFHSKAGWTPFEGFEVTGFPV 355
|
....*.
gi 71989490 436 VTISRG 441
Cdd:cd01318 356 MTIVRG 361
|
|
| PRK09060 |
PRK09060 |
dihydroorotase; Validated |
5-465 |
3.61e-33 |
|
dihydroorotase; Validated
Pssm-ID: 181632 [Multi-domain] Cd Length: 444 Bit Score: 130.81 E-value: 3.61e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71989490 5 LVIKNGTVVNEDGMFKADVLVRNGIIVEVSpNITALPDTEVIDATDRLVIPGGIDPHTHMQMPymGEVTKDDFLKGTEAA 84
Cdd:PRK09060 7 LILKGGTVVNPDGEGRADIGIRDGRIAAIG-DLSGASAGEVIDCRGLHVLPGVIDSQVHFREP--GLEHKEDLETGSRAA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71989490 85 VAGGTTMIIDF--CCPDHRNGESLIA--GYNRWRSWadpkvcCDYGLSVAITmwrPETAEQMAIITSpEFGVNSFKFYM- 159
Cdd:PRK09060 84 VLGGVTAVFEMpnTNPLTTTAEALADklARARHRMH------CDFAFYVGGT---RDNADELAELER-LPGCAGIKVFMg 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71989490 160 AYENTLMVRDDELFRgmqecAKLRALAR---VHCENGSVIKEKEidllAKGVTG-PEGHTQSRPEEIEAEATNRACVLAA 235
Cdd:PRK09060 154 SSTGDLLVEDDEGLR-----RILRNGRRraaFHSEDEYRLRERK----GLRVEGdPSSHPVWRDEEAALLATRRLVRLAR 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71989490 236 QANCPVYIVHVMTKGAASAISHHRAQGSIvfgEPIAAGLALDGSHYYNEDWLHAaryVMSPPLsRDPTTPELLMKLLAAG 315
Cdd:PRK09060 225 ETGRRIHVLHVSTAEEIDFLADHKDVATV---EVTPHHLTLAAPECYERLGTLA---QMNPPI-RDARHRDGLWRGVRQG 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71989490 316 ELHLTGTDNC--TYDCRQKSlgkgnFTKIPNGINGVEDRMSVVWEKgVHSGIIDPMRYVSITSSTAAKIFNIyPRKGRIA 393
Cdd:PRK09060 298 VVDVLGSDHAphTLEEKAKP-----YPASPSGMTGVQTLVPIMLDH-VNAGRLSLERFVDLTSAGPARIFGI-AGKGRIA 370
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 71989490 394 VGSDADIVIFNPNATRTISKDTHHHNLDFNIFEGINCHGVAEVTISRGRIVWAHGKLQTvPGSG---KFIPLLAN 465
Cdd:PRK09060 371 VGYDADFTIVDLKRRETITNEWIASRCGWTPYDGKEVTGWPVGTIVRGQRVMWDGELVG-PPTGepvRFLETLPR 444
|
|
| PLN02795 |
PLN02795 |
allantoinase |
3-464 |
1.27e-31 |
|
allantoinase
Pssm-ID: 178392 [Multi-domain] Cd Length: 505 Bit Score: 127.20 E-value: 1.27e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71989490 3 PPLVIKNGTVVNEDGMFKADVLVRNGIIVEVSPNITA---LPDTEVIDATDRLVIPGGIDPHTHMQMPymGEVTKDDFLK 79
Cdd:PLN02795 44 PHFVLYSKRVVTPAGVIPGAVEVEGGRIVSVTKEEEApksQKKPHVLDYGNAVVMPGLIDVHVHLNEP--GRTEWEGFPT 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71989490 80 GTEAAVAGGTTMIIDFCCPDHRNGESLIAGYNRWRSWADPkvccdygLSVAITMWR---PETAEQMAIITSP-EFGVNSF 155
Cdd:PLN02795 122 GTKAAAAGGITTLVDMPLNSFPSTTSVETLELKIEAAKGK-------LYVDVGFWGglvPENAHNASVLEELlDAGALGL 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71989490 156 KFYM---AYENTLMVRDDELFRGMQECAKLRALARVHCEngsVIKEKEID-LLAKGVTGPEGHTQSRPEEIEAEATNRAC 231
Cdd:PLN02795 195 KSFMcpsGINDFPMTTATHIKAALPVLAKYGRPLLVHAE---VVSPVESDsRLDADPRSYSTYLKSRPPSWEQEAIRQLL 271
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71989490 232 VLA-------AQANCPVYIVHVM-TKGAASAISHHRAQGSIVFGEPIAAGLALDGSHYYNEDwlhaARYVMSPPLsRDPT 303
Cdd:PLN02795 272 EVAkdtrpggVAEGAHVHIVHLSdAESSLELIKEAKAKGDSVTVETCPHYLAFSAEEIPDGD----TRYKCAPPI-RDAA 346
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71989490 304 TPELLMKLLAAGELHLTGTDNCTYDCRQKSLGKGNFTKIPNGINGVEDRMSVVWEKGVHSGI-IDPMryVSITSSTAAKI 382
Cdd:PLN02795 347 NRELLWKALLDGDIDMLSSDHSPSPPDLKLLEEGNFLRAWGGISSLQFVLPATWTAGRAYGLtLEQL--ARWWSERPAKL 424
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71989490 383 FNIyPRKGRIAVGSDADIVIFNPNATRTISKD--THHHNLDFNIFEGINCHGVAEVTISRGRIVWAHGKLQTVP-GSgkf 459
Cdd:PLN02795 425 AGL-DSKGAIAPGKDADIVVWDPEAEFVLDESypIYHKHKSLSPYLGTKLSGKVIATFVRGNLVFLEGKHAKQAcGS--- 500
|
....*
gi 71989490 460 iPLLA 464
Cdd:PLN02795 501 -PILA 504
|
|
| PRK09236 |
PRK09236 |
dihydroorotase; Reviewed |
1-454 |
1.09e-25 |
|
dihydroorotase; Reviewed
Pssm-ID: 181716 Cd Length: 444 Bit Score: 109.19 E-value: 1.09e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71989490 1 MSPpLVIKNGTVVNEDGMFKADVLVRNGIIVEVSPNITALPDTEVIDATDRLVIPGGIDPHTHMQMPymGEVTKDDFLKG 80
Cdd:PRK09236 1 MKR-ILIKNARIVNEGKIFEGDVLIENGRIAKIASSISAKSADTVIDAAGRYLLPGMIDDQVHFREP--GLTHKGDIASE 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71989490 81 TEAAVAGGTTMIIDF--CCPDHRNGESLIAGYNRW--RSWA-------------------DPKVCCdyglsvaitmwrpe 137
Cdd:PRK09236 78 SRAAVAGGITSFMEMpnTNPPTTTLEALEAKYQIAaqRSLAnysfyfgatndnldeikrlDPKRVC-------------- 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71989490 138 taeqmaiitspefGVnsfKFYMAYENTLMVRDDE-----LFRgmqECAKLRAlarVHCENGSVIKEKEIDLLAK--GVTG 210
Cdd:PRK09236 144 -------------GV---KVFMGASTGNMLVDNPetlerIFR---DAPTLIA---THCEDTPTIKANLAKYKEKygDDIP 201
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71989490 211 PEGHTQSRPEEIEAEATNRACVLAAQANCPVYIVHVMTkgaASAISHHRAqGSIVfGEPIAAGLALDGSHYYNEDWLHAA 290
Cdd:PRK09236 202 AEMHPLIRSAEACYKSSSLAVSLAKKHGTRLHVLHIST---AKELSLFEN-GPLA-EKRITAEVCVHHLWFDDSDYARLG 276
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71989490 291 RYVMSPPLSRDPTTPELLMKLLAAGELHLTGTDNCTYDCRQKslgKGNFTKIPNGINGVEDRMSVVWEKgVHSGIIDPMR 370
Cdd:PRK09236 277 NLIKCNPAIKTASDREALRQALADDRIDVIATDHAPHTWEEK---QGPYFQAPSGLPLVQHALPALLEL-VHEGKLSLEK 352
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71989490 371 YVSITSSTAAKIFNIyPRKGRIAVGSDADIVIFNPNATRTISKDthhhnldfNI--------FEGINCHGVAEVTISRGR 442
Cdd:PRK09236 353 VVEKTSHAPAILFDI-KERGFIREGYWADLVLVDLNSPWTVTKE--------NIlykcgwspFEGRTFRSRVATTFVNGQ 423
|
490
....*....|..
gi 71989490 443 IVWAHGKLQTVP 454
Cdd:PRK09236 424 LVYHNGQLVESC 435
|
|
| PRK01211 |
PRK01211 |
dihydroorotase; Provisional |
22-466 |
7.19e-21 |
|
dihydroorotase; Provisional
Pssm-ID: 179247 [Multi-domain] Cd Length: 409 Bit Score: 94.54 E-value: 7.19e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71989490 22 DVLVRNGIIVEVSPNITALPDTEVidatDRLVIPGGIDPHTHMQMPymGEVTKDDFLKGTEAAVAGGTTMIIDFccPDHR 101
Cdd:PRK01211 17 EIEVEDGKIKSIKKDAGNIGKKEL----KGAILPAATDIHVHFRTP--GETEKEDFSTGTLSAIFGGTTFIMDM--PNNN 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71989490 102 NGESLIAGYNRWRSWADPKVCCDYGLsvaitmWRPETAEQMAIITSPEFGvnsFKFYMA---YENTLMVRDDELfrgmQE 178
Cdd:PRK01211 89 IPIKDYNAFSDKLGRVAPKAYVDFSL------YSMETGNNALILDERSIG---LKVYMGgttNTNGTDIEGGEI----KK 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71989490 179 CAKLRALARVHCENGSVIKEKEIDllAKGVtgpEGHTQSRPEEIEAEATNRACVLAAQANCPVYIVHVMTKG--AASAIS 256
Cdd:PRK01211 156 INEANIPVFFHAELSECLRKHQFE--SKNL---RDHDLARPIECEIKAVKYVKNLDLKTKIIAHVSSIDVIGrfLREVTP 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71989490 257 HHraqgsivfgepiaagLALdgshyyNEDWLHAARYVMSPPLsRDPTTPELLMKLLAAGELHLTGTDNCTYDCRQKSlgk 336
Cdd:PRK01211 231 HH---------------LLL------NDDMPLGSYGKVNPPL-RDRWTQERLLEEYISGRFDILSSDHAPHTEEDKQ--- 285
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71989490 337 gNFTKIPNGINGVEDRMSVVWEKgVHSGIIDPMRYVSITSSTAAKIFNIypRKGRIAVGSDADIVIFNPNATRTISKDTH 416
Cdd:PRK01211 286 -EFEYAKSGIIGVETRVPLFLAL-VKKKILPLDVLYKTAIERPASLFGI--KKGKIEEGYDADFMAFDFTNIKKINDKRL 361
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|
gi 71989490 417 HHNLDFNIFEGINCHGVAEVtISRGRIVWAHGKLQTVPgSGKFIPLLANS 466
Cdd:PRK01211 362 HSKCPVSPFNGFDAIFPSHV-IMRGEVVIDNYELISER-TGKFVPKGGES 409
|
|
| HutI |
COG1228 |
Imidazolonepropionase or related amidohydrolase [Secondary metabolites biosynthesis, transport ... |
1-427 |
1.09e-18 |
|
Imidazolonepropionase or related amidohydrolase [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 440841 [Multi-domain] Cd Length: 386 Bit Score: 87.71 E-value: 1.09e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71989490 1 MSPPLVIKNGTVVNEDG---MFKADVLVRNGIIVEVSPN--ITALPDTEVIDATDRLVIPGGIDPHTHMqmpYMGEVTKD 75
Cdd:COG1228 6 QAGTLLITNATLVDGTGggvIENGTVLVEDGKIAAVGPAadLAVPAGAEVIDATGKTVLPGLIDAHTHL---GLGGGRAV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71989490 76 DFLKGT----------------EAAVAGGTTMIIDFCCPDHRNGESLIAGYNRWRsWADPKVCCDYGLSV--AITMWRPE 137
Cdd:COG1228 83 EFEAGGgitptvdlvnpadkrlRRALAAGVTTVRDLPGGPLGLRDAIIAGESKLL-PGPRVLAAGPALSLtgGAHARGPE 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71989490 138 TAEQMAiitsPEF---GVNSFKFYMAYENTLMvRDDELFRGMQECAKLRALARVHCEngsvikekeidllakgvtgpegh 214
Cdd:COG1228 162 EARAAL----RELlaeGADYIKVFAEGGAPDF-SLEELRAILEAAHALGLPVAAHAH----------------------- 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71989490 215 tqsRPEEIEaeatnracvLAAQANCPVyIVHV--MTKGAASAIshhRAQGSIVFGePiAAGLALDGSHYYNEDWLHAARY 292
Cdd:COG1228 214 ---QADDIR---------LAVEAGVDS-IEHGtyLDDEVADLL---AEAGTVVLV-P-TLSLFLALLEGAAAPVAAKARK 275
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71989490 293 VMspplsrdPTTPELLMKLLAAGELHLTGTDnctydcrqkslgkGNFTKIPNGingvedRMSVVWEKGVHSGiIDPMR-Y 371
Cdd:COG1228 276 VR-------EAALANARRLHDAGVPVALGTD-------------AGVGVPPGR------SLHRELALAVEAG-LTPEEaL 328
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*.
gi 71989490 372 VSITsSTAAKIFNIYPRKGRIAVGSDADIVIFNPNATRTISkdtHHHNLDFNIFEG 427
Cdd:COG1228 329 RAAT-INAAKALGLDDDVGSLEPGKLADLVLLDGDPLEDIA---YLEDVRAVMKDG 380
|
|
| D-aminoacylase |
cd01297 |
D-aminoacylases (N-acyl-D-Amino acid amidohydrolases) catalyze the hydrolysis of ... |
5-455 |
4.44e-18 |
|
D-aminoacylases (N-acyl-D-Amino acid amidohydrolases) catalyze the hydrolysis of N-acyl-D-amino acids to produce the corresponding D-amino acids, which are used as intermediates in the synthesis of pesticides, bioactive peptides, and antibiotics.
Pssm-ID: 238622 [Multi-domain] Cd Length: 415 Bit Score: 86.20 E-value: 4.44e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71989490 5 LVIKNGTVVneDGM----FKADVLVRNGIIVEVSPNiTALPDTEVIDATDRLVIPGGIDPHTHmqmpYMGEVTKDDFLkg 80
Cdd:cd01297 2 LVIRNGTVV--DGTgappFTADVGIRDGRIAAIGPI-LSTSAREVIDAAGLVVAPGFIDVHTH----YDGQVFWDPDL-- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71989490 81 TEAAVAGGTTMIIDFC------------CPDHRNGESLIAGYN----RWRSWAD-----------PKVCCDYG---LSVA 130
Cdd:cd01297 73 RPSSRQGVTTVVLGNCgvspapanpddlARLIMLMEGLVALGEglpwGWATFAEyldalearppaVNVAALVGhaaLRRA 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71989490 131 ITMWRPETA-----EQMAIITSPE-----FGVNSFKFYMayentlmvrdDELFRGMQEcakLRALARVHCENGSVIkeke 200
Cdd:cd01297 153 VMGLDAREAteeelAKMRELLREAleagaLGISTGLAYA----------PRLYAGTAE---LVALARVAARYGGVY---- 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71989490 201 idllakgVTGPEGHTQSRPEEIEaeatnRACVLAAQANCPVYIVHVmtkGAASAISHHRAQGSI-VFGEPIAAGLALdgs 279
Cdd:cd01297 216 -------QTHVRYEGDSILEALD-----ELLRLGRETGRPVHISHL---KSAGAPNWGKIDRLLaLIEAARAEGLQV--- 277
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71989490 280 hyynedWLHAARYvmsPPLSRDPTTPELLMKL-------LAAGELHLTgtdncTYDCRQKSLGKgnftkipnginGVEDR 352
Cdd:cd01297 278 ------TADVYPY---GAGSEDDVRRIMAHPVvmggsdgGALGKPHPR-----SYGDFTRVLGH-----------YVRER 332
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71989490 353 MSVVWEKGVHSgiidpMryvsitSSTAAKIFNIYPRkGRIAVGSDADIVIFNPNATRTISKDTHHHNLDfnifEGInchg 432
Cdd:cd01297 333 KLLSLEEAVRK-----M------TGLPARVFGLADR-GRIAPGYRADIVVFDPDTLADRATFTRPNQPA----EGI---- 392
|
490 500
....*....|....*....|....
gi 71989490 433 vaEVTISRGRIVWAHGKLQTV-PG 455
Cdd:cd01297 393 --EAVLVNGVPVVRDGAFTGArPG 414
|
|
| PRK04250 |
PRK04250 |
dihydroorotase; Provisional |
6-444 |
7.71e-15 |
|
dihydroorotase; Provisional
Pssm-ID: 235265 [Multi-domain] Cd Length: 398 Bit Score: 75.96 E-value: 7.71e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71989490 6 VIKNGTVVnedgmfKADVLVRNGIIVEVSpnITALPDTEVIDATDRLVIPGGIDPHTHMQmpYMGEVTKDDFLKGTEAAV 85
Cdd:PRK04250 6 FLLKGRIV------EGGIGIENGRISKIS--LRDLKGKEVIKVKGGIILPGLIDVHVHLR--DFEESYKETIESGTKAAL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71989490 86 AGGTTMIIDFccPDHRNGESLIAGYNRWRSWADPKVCCDYGLSVAITMWRPETAEQMAIItspefgvnsfkfymaYENTL 165
Cdd:PRK04250 76 HGGITLVFDM--PNTKPPIMDEKTYEKRMRIAEKKSYADYALNFLIAGNCEKAEEIKADF---------------YKIFM 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71989490 166 MVRDDELFRGMQEC--AKLRALARVHCENGSVIKEKeidllakgvtgPEghtqsRPEEIEAEATNRACVLAAQANCPVYI 243
Cdd:PRK04250 139 GASTGGIFSENFEVdyACAPGIVSVHAEDPELIREF-----------PE-----RPPEAEVVAIERALEAGKKLKKPLHI 202
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71989490 244 VHVMTKGAASAISHHRAQGSIVFGEPiaaglaldgSH--YYNEDWLHAARYVMSPPLsRDPTTPELLMKLLAagELHLTG 321
Cdd:PRK04250 203 CHISTKDGLKLILKSNLPWVSFEVTP---------HHlfLTRKDYERNPLLKVYPPL-RSEEDRKALWENFS--KIPIIA 270
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71989490 322 TDNCTYDCRQKSLGKGnftkipnGINGVEDRMSVVWEkGVHSGIIDPMRYVSITSSTAAKIFNIyPRKGrIAVGSDADIV 401
Cdd:PRK04250 271 SDHAPHTLEDKEAGAA-------GIPGLETEVPLLLD-AANKGMISLFDIVEKMHDNPARIFGI-KNYG-IEEGNYANFA 340
|
410 420 430 440
....*....|....*....|....*....|....*....|...
gi 71989490 402 IFNPNATRTISKDTHHHNLDFNIFEGINCHGVAEVTISRGRIV 444
Cdd:PRK04250 341 VFDMKKEWTIKAEELYTKAGWTPYEGFKLKGKVIMTILRGEVV 383
|
|
| COG3653 |
COG3653 |
N-acyl-D-aspartate/D-glutamate deacylase [Secondary metabolites biosynthesis, transport and ... |
5-93 |
1.47e-14 |
|
N-acyl-D-aspartate/D-glutamate deacylase [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 442870 [Multi-domain] Cd Length: 528 Bit Score: 75.98 E-value: 1.47e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71989490 5 LVIKNGTVVneDGM----FKADVLVRNGIIVEVSPNITAlPDTEVIDATDRLVIPGGIDPHTHmqmpYMGEVTKDDFLkg 80
Cdd:COG3653 4 LLIRGGTVV--DGTgappFRADVAIKGGRIVAVGDLAAA-EAARVIDATGLVVAPGFIDIHTH----YDLQLLWDPRL-- 74
|
90
....*....|....
gi 71989490 81 tEAAVAGG-TTMII 93
Cdd:COG3653 75 -EPSLRQGvTTVVM 87
|
|
| Amidohydro_1 |
pfam01979 |
Amidohydrolase family; This family of enzymes are a a large metal dependent hydrolase ... |
52-444 |
1.48e-13 |
|
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: 71.76 E-value: 1.48e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71989490 52 LVIPGGIDPHTHMQMPYM------GEVTKDDFLKGTEAAVAGGTTMIIDF----CCPDH---RNGESLIAGYNRWRSWAD 118
Cdd:pfam01979 1 IVLPGLIDAHVHLEMGLLrgipvpPEFAYEALRLGITTMLKSGTTTVLDMgattSTGIEallEAAEELPLGLRFLGPGCS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71989490 119 PKVccDYGLSVAITMWRPETAEQMAI-ITSPEFGVNSFKFYMAYENTlmvrDDELFRGMQECAKLRALARVHCENGSviK 197
Cdd:pfam01979 81 LDT--DGELEGRKALREKLKAGAEFIkGMADGVVFVGLAPHGAPTFS----DDELKAALEEAKKYGLPVAIHALETK--G 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71989490 198 EKEIDLLAKGVTGPEGHTQSRPEEIEAeatNRACVLAAQANcpvyiVHVMTKGAASAISHHRAQGsivfgepiaaglald 277
Cdd:pfam01979 153 EVEDAIAAFGGGIEHGTHLEVAESGGL---LDIIKLILAHG-----VHLSPTEANLLAEHLKGAG--------------- 209
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71989490 278 gshyynedwlhaaryVMSPPLSRDPTTPEL--LMKLLAAGELHLTGTDNCtydcrqksLGKGNFTKIPNGINGVEDRmsv 355
Cdd:pfam01979 210 ---------------VAHCPFSNSKLRSGRiaLRKALEDGVKVGLGTDGA--------GSGNSLNMLEELRLALELQ--- 263
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71989490 356 vwekGVHSGIIDPMRYVSITSSTAAKIFNIYPRKGRIAVGSDADIVIFNPNATrtiskdthhhnldfNIFEGINCHGVAE 435
Cdd:pfam01979 264 ----FDPEGGLSPLEALRMATINPAKALGLDDKVGSIEVGKDADLVVVDLDPL--------------AAFFGLKPDGNVK 325
|
....*....
gi 71989490 436 VTISRGRIV 444
Cdd:pfam01979 326 KVIVKGKIV 334
|
|
| COG3964 |
COG3964 |
Predicted amidohydrolase [General function prediction only]; |
4-94 |
7.58e-13 |
|
Predicted amidohydrolase [General function prediction only];
Pssm-ID: 443164 [Multi-domain] Cd Length: 376 Bit Score: 69.81 E-value: 7.58e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71989490 4 PLVIKNGTVVNE----DGmfKADVLVRNGIIVEVSPNITALPDTEVIDATDRLVIPGGIDPHTHMqmpymgevtkddFLK 79
Cdd:COG3964 1 DLLIKGGRVIDPangiDG--VMDIAIKDGKIAAVAKDIDAAEAKKVIDASGLYVTPGLIDLHTHV------------FPG 66
|
90 100
....*....|....*....|..
gi 71989490 80 GT-------EAAVAGGTTMIID 94
Cdd:COG3964 67 GTdygvdpdGVGVRSGVTTVVD 88
|
|
| PRK08204 |
PRK08204 |
hypothetical protein; Provisional |
6-100 |
3.02e-12 |
|
hypothetical protein; Provisional
Pssm-ID: 181288 [Multi-domain] Cd Length: 449 Bit Score: 68.49 E-value: 3.02e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71989490 6 VIKNGTVVNEDGMF----KADVLVRNGIIVEVSPNITAlPDTEVIDATDRLVIPGGIDPHTHM-QMP---YMGEVTKDDF 77
Cdd:PRK08204 5 LIRGGTVLTMDPAIgdlpRGDILIEGDRIAAVAPSIEA-PDAEVVDARGMIVMPGLVDTHRHTwQSVlrgIGADWTLQTY 83
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 71989490 78 LK---------------------GTEAAVAGGTTMIIDFC----CPDH 100
Cdd:PRK08204 84 FReihgnlgpmfrpedvyianllGALEALDAGVTTLLDWShinnSPEH 131
|
|
| SsnA |
COG0402 |
Cytosine/adenosine deaminase or related metal-dependent hydrolase [Nucleotide transport and ... |
5-96 |
6.60e-12 |
|
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: 67.16 E-value: 6.60e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71989490 5 LVIKNGTVVNEDGMF----KADVLVRNGIIVEVSPNITA---LPDTEVIDATDRLVIPGGIDPHTHMQM----------- 66
Cdd:COG0402 2 LLIRGAWVLTMDPAGgvleDGAVLVEDGRIAAVGPGAELparYPAAEVIDAGGKLVLPGLVNTHTHLPQtllrgladdlp 81
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 71989490 67 ----------PYMGEVTKDDFLKGTEAAVA----GGTTMIIDFC 96
Cdd:COG0402 82 lldwleeyiwPLEARLDPEDVYAGALLALAemlrSGTTTVADFY 125
|
|
| NagA |
cd00854 |
N-acetylglucosamine-6-phosphate deacetylase, NagA, catalyzes the hydrolysis of the N-acetyl ... |
5-63 |
2.73e-11 |
|
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: 64.91 E-value: 2.73e-11
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 71989490 5 LVIKNGTVVNEDGMFKADVLVRNGIIVEVSPNITALPDTEVIDATDRLVIPGGIDPHTH 63
Cdd:cd00854 1 LIIKNARILTPGGLEDGAVLVEDGKIVAIGPEDELEEADEIIDLKGQYLVPGFIDIHIH 59
|
|
| pyrC |
PRK00369 |
dihydroorotase; Provisional |
50-459 |
5.15e-11 |
|
dihydroorotase; Provisional
Pssm-ID: 234738 [Multi-domain] Cd Length: 392 Bit Score: 64.40 E-value: 5.15e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71989490 50 DRLVIPGGIDPHTHM---QMPYmgevtKDDFLKGTEAAVAGGTTMIIDF--CCPDHRNGESLIAGYNRWRSWADpkvcCD 124
Cdd:PRK00369 42 GTLILPGAIDLHVHLrglKLSY-----KEDVASGTSEAAYGGVTLVADMpnTIPPLNTPEAITEKLAELEYYSR----VD 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71989490 125 YGLSVAItmwrPETAEQMAiitspEFGVNSFKFYMayENtlMVRDDELFRgmqeCAKLRALARVHcengsvikekeidll 204
Cdd:PRK00369 113 YFVYSGV----TKDPEKVD-----KLPIAGYKIFP--ED--LEREETFRV----LLKSRKLKILH--------------- 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71989490 205 akgvtgPEGHTQSRPEEIEAeatnRACVLAAQAncpVYIVHvmtkGAASA-ISHHRAQGSIVFGEPIaaGLALDGS-HYY 282
Cdd:PRK00369 161 ------PEVPLALKSNRKLR----RNCWYEIAA---LYYVK----DYQNVhITHASNPRTVRLAKEL--GFTVDITpHHL 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71989490 283 NEDWLHAARYVMSPPLsRDPTTPELLMKLLAagELHLTGTDNCTYDCRQKSLgkgNFTKIPNGINGVEDRMSVVWEKgVH 362
Cdd:PRK00369 222 LVNGEKDCLTKVNPPI-RDINERLWLLQALS--EVDAIASDHAPHSSFEKLQ---PYEVCPPGIAALSFTPPFIYTL-VS 294
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71989490 363 SGIIDPMRYVSITSSTAAKIFNIypRKGRIAVGSDADIVIFNPNATR---TISKDTHHHNLDFNIFEGInchgvaEVTIS 439
Cdd:PRK00369 295 KGILSIDRAVELISTNPARILGI--PYGEIKEGYRANFTVIQFEDWRystKYSKVIETPLDGFELKASV------YATIV 366
|
410 420
....*....|....*....|
gi 71989490 440 RGRIVWAHGKLQTVPGSGKF 459
Cdd:PRK00369 367 QGKLAYLEGEVFPVKGINPF 386
|
|
| PRK07369 |
PRK07369 |
dihydroorotase; Provisional |
21-417 |
6.69e-11 |
|
dihydroorotase; Provisional
Pssm-ID: 236002 [Multi-domain] Cd Length: 418 Bit Score: 64.24 E-value: 6.69e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71989490 21 ADVLVRNGIIVEVSPNITALP-DTEVIDATDRLVIPGGIDPHTHMQMPymGEVTKDDFLKGTEAAVAGGTT--MIIDFCC 97
Cdd:PRK07369 22 ADVLIEDGKIQAIEPHIDPIPpDTQIIDASGLILGPGLVDLYSHSGEP--GFEERETLASLAAAAAAGGFTrvAILPDTF 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71989490 98 PDHRNGESL------IAGYN--RWRSWAdpkvccdyglsvAITmwRPETAEQMAIITS-PEFGVNSFKFYMAYENTLMVR 168
Cdd:PRK07369 100 PPLDNPATLarlqqqAQQIPpvQLHFWG------------ALT--LGGQGKQLTELAElAAAGVVGFTDGQPLENLALLR 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71989490 169 ddelfrgmqecaklRALARVHCENGSV-IKEKEIDLLAKGVTgPEGHTQSR----PEEIEAEATNRACVL--AAQANCPV 241
Cdd:PRK07369 166 --------------RLLEYLKPLGKPVaLWPCDRSLAGNGVM-REGLLALRlglpGDPASAETTALAALLelVAAIGTPV 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71989490 242 YIVHVMTKGAASAISHHRAQGSivfgePIAAGLAldgshyynedWLH-------AARY----VMSPPLSRdPTTPELLMK 310
Cdd:PRK07369 231 HLMRISTARSVELIAQAKARGL-----PITASTT----------WMHllldteaLASYdpnlRLDPPLGN-PSDRQALIE 294
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71989490 311 LLAAGELHLTGTDNCTYDCRQKSLGkgnFTKIPNGINGVEDRMSVVWEKGVHSGIIDPMRYVSITSSTAAKIFNIYPRkg 390
Cdd:PRK07369 295 GVRTGVIDAIAIDHAPYTYEEKTVA---FAEAPPGAIGLELALPLLWQNLVETGELSALQLWQALSTNPARCLGQEPP-- 369
|
410 420
....*....|....*....|....*..
gi 71989490 391 RIAVGSDADIVIFNPNATRTISKDTHH 417
Cdd:PRK07369 370 SLAPGQPAELILFDPQKTWTVSAQTLH 396
|
|
| PRK09237 |
PRK09237 |
amidohydrolase/deacetylase family metallohydrolase; |
5-94 |
1.56e-10 |
|
amidohydrolase/deacetylase family metallohydrolase;
Pssm-ID: 236423 [Multi-domain] Cd Length: 380 Bit Score: 62.56 E-value: 1.56e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71989490 5 LVIKNGTVV----NEDGMFkaDVLVRNGIIVEVSPNITALPDTEVIDATDRLVIPGGIDPHTHMqmpYMGevTKDDFLKG 80
Cdd:PRK09237 1 LLLRGGRVIdpanGIDGVI--DIAIEDGKIAAVAGDIDGSQAKKVIDLSGLYVSPGWIDLHVHV---YPG--STPYGDEP 73
|
90
....*....|....
gi 71989490 81 TEAAVAGGTTMIID 94
Cdd:PRK09237 74 DEVGVRSGVTTVVD 87
|
|
| PRK08417 |
PRK08417 |
metal-dependent hydrolase; |
274-444 |
1.67e-10 |
|
metal-dependent hydrolase;
Pssm-ID: 236262 [Multi-domain] Cd Length: 386 Bit Score: 62.80 E-value: 1.67e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71989490 274 LALDGSHYynEDWLHAARyvMSPPLsRDPTTPELLMKLLAAGELH-LTGTDNCTYDCRqKSLGkgnFTKIPNGINGVEDR 352
Cdd:PRK08417 231 LILDDSAC--ENFNTAAK--LNPPL-RSKEDRLALLEALKEGKIDfLTSLHSAKSNSK-KDLA---FDEAAFGIDSICEY 301
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71989490 353 MSVVWEKGVHSGIIDPMRYVSITSSTAAKIFNIypRKGRIAVGSDADIVIFNPNaTRTISKDthhhnlDFNIFEGINCHG 432
Cdd:PRK08417 302 FSLCYTYLVKEGIITWSELSRFTSYNPAQFLGL--NSGEIEVGKEADLVLFDPN-ESTIIDD------NFSLYSGDELYG 372
|
170
....*....|..
gi 71989490 433 VAEVTISRGRIV 444
Cdd:PRK08417 373 KIEAVIIKGKLY 384
|
|
| PRK08393 |
PRK08393 |
N-ethylammeline chlorohydrolase; Provisional |
5-66 |
2.17e-10 |
|
N-ethylammeline chlorohydrolase; Provisional
Pssm-ID: 181411 [Multi-domain] Cd Length: 424 Bit Score: 62.51 E-value: 2.17e-10
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 71989490 5 LVIKNGTVVNEDGM--FKADVLVRNGIIVEVSPNITALPDTeVIDATDRLVIPGGIDPHTHMQM 66
Cdd:PRK08393 3 ILIKNGYVIYGENLkvIRADVLIEGNKIVEVKRNINKPADT-VIDASGSVVSPGFINAHTHSPM 65
|
|
| FwdA |
COG1229 |
Formylmethanofuran dehydrogenase subunit A [Energy production and conversion]; |
5-63 |
3.50e-10 |
|
Formylmethanofuran dehydrogenase subunit A [Energy production and conversion];
Pssm-ID: 440842 Cd Length: 554 Bit Score: 62.13 E-value: 3.50e-10
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 71989490 5 LVIKNGTV---VNE-DGMfKADVLVRNGIIVE-VSPNitalPDTEVIDATDRLVIPGGIDPHTH 63
Cdd:COG1229 3 LIIKNGRVydpANGiDGE-VMDIAIKDGKIVEePSDP----KDAKVIDASGKVVMAGGVDIHTH 61
|
|
| ATZ_TRZ_like |
cd01298 |
TRZ/ATZ family contains enzymes from the atrazine degradation pathway and related hydrolases. ... |
5-94 |
6.87e-10 |
|
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: 60.68 E-value: 6.87e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71989490 5 LVIKNGTVV---NEDGMFKADVLVRNGIIVEVSPNITA--LPDTEVIDATDRLVIPGGIDPHTHMQM------------- 66
Cdd:cd01298 1 ILIRNGTIVttdPRRVLEDGDVLVEDGRIVAVGPALPLpaYPADEVIDAKGKVVMPGLVNTHTHLAMtllrgladdlplm 80
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 71989490 67 --------PYMGEVTKDDFLKGTEAAVA----GGTTMIID 94
Cdd:cd01298 81 ewlkdliwPLERLLTEEDVYLGALLALAemirSGTTTFAD 120
|
|
| NagA |
COG1820 |
N-acetylglucosamine-6-phosphate deacetylase [Carbohydrate transport and metabolism]; |
6-63 |
8.55e-10 |
|
N-acetylglucosamine-6-phosphate deacetylase [Carbohydrate transport and metabolism];
Pssm-ID: 441425 [Multi-domain] Cd Length: 373 Bit Score: 60.50 E-value: 8.55e-10
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 71989490 6 VIKNGTVVNEDGMFK-ADVLVRNGIIVEVSPniTALPDTEVIDATDRLVIPGGIDPHTH 63
Cdd:COG1820 1 AITNARIFTGDGVLEdGALLIEDGRIAAIGP--GAEPDAEVIDLGGGYLAPGFIDLHVH 57
|
|
| AdeC |
COG1001 |
Adenine deaminase [Nucleotide transport and metabolism]; |
5-94 |
1.48e-09 |
|
Adenine deaminase [Nucleotide transport and metabolism];
Pssm-ID: 440625 [Multi-domain] Cd Length: 559 Bit Score: 60.11 E-value: 1.48e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71989490 5 LVIKNGTVVN----EdgMFKADVLVRNGIIVEVSPNItaLPDTEVIDATDRLVIPGGIDPHTHM--QMpymgeVTKDDFl 78
Cdd:COG1001 7 LVIKNGRLVNvftgE--ILEGDIAIAGGRIAGVGDYI--GEATEVIDAAGRYLVPGFIDGHVHIesSM-----VTPAEF- 76
|
90
....*....|....*..
gi 71989490 79 kgTEAAVAGGTT-MIID 94
Cdd:COG1001 77 --ARAVLPHGTTtVIAD 91
|
|
| PRK15446 |
PRK15446 |
phosphonate metabolism protein PhnM; Provisional |
2-62 |
2.11e-09 |
|
phosphonate metabolism protein PhnM; Provisional
Pssm-ID: 237967 [Multi-domain] Cd Length: 383 Bit Score: 59.04 E-value: 2.11e-09
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 71989490 2 SPPLVIKNGTVVNEDGMFKADVLVRNGIIVEVSPNITALPDTevIDATDRLVIPGGIDPHT 62
Cdd:PRK15446 1 MMEMILSNARLVLPDEVVDGSLLIEDGRIAAIDPGASALPGA--IDAEGDYLLPGLVDLHT 59
|
|
| PRK07572 |
PRK07572 |
cytosine deaminase; Validated |
5-64 |
2.78e-09 |
|
cytosine deaminase; Validated
Pssm-ID: 181039 Cd Length: 426 Bit Score: 58.88 E-value: 2.78e-09
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 71989490 5 LVIKNGTVvnEDGMFKADVLVRNGIIVEVSPNITAlPDTEVIDATDRLVIPGGIDPHTHM 64
Cdd:PRK07572 4 LIVRNANL--PDGRTGIDIGIAGGRIAAVEPGLQA-EAAEEIDAAGRLVSPPFVDPHFHM 60
|
|
| PRK09059 |
PRK09059 |
dihydroorotase; Validated |
1-447 |
1.33e-08 |
|
dihydroorotase; Validated
Pssm-ID: 181631 [Multi-domain] Cd Length: 429 Bit Score: 56.97 E-value: 1.33e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71989490 1 MSPPLVIKNGTVV----NEDGMfkADVLVRNGIIVEVSPNITA--LPD-TEVIDATDRLVIPGGIDPHTHMQMPymGEVT 73
Cdd:PRK09059 1 MMRPILLANARIIdpsrGLDEI--GTVLIEDGVIVAAGKGAGNqgAPEgAEIVDCAGKAVAPGLVDARVFVGEP--GAEH 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71989490 74 KDDFLKGTEAAVAGGTTMIIdfCCPDhrngesliagynrwrswADPkVCCDYGLSVAITMWRPETA----EQMAIITS-- 147
Cdd:PRK09059 77 RETIASASRAAAAGGVTSII--MMPD-----------------TDP-VIDDVALVEFVKRTARDTAivniHPAAAITKgl 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71989490 148 -----PEFGVNSFKFYMAY-ENTLMVRDDELFRgmqecaklRAL--ARvhcENGSVI--KEKEIDLLAKGVTGpEGHTQS 217
Cdd:PRK09059 137 ageemTEFGLLRAAGAVAFtDGRRSVANTQVMR--------RALtyAR---DFDAVIvhETRDPDLGGNGVMN-EGLFAS 204
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71989490 218 R------PEEIEAEATNRACVLAAQANCPVYIVHVMTKGAASAISHHRAQgsivfGEPIAAGLALDgsHY-YNEDWLHAA 290
Cdd:PRK09059 205 WlglsgiPREAEVIPLERDLRLAALTRGRYHAAQISCAESAEALRRAKDR-----GLKVTAGVSIN--HLsLNENDIGEY 277
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71989490 291 R--YVMSPPLsRDPTTPELLMKLLAAGELHLTGTDNCTYDCRQKSLgkgNFTKIPNGINGVEDRMSVVWeKGVHSGIIDP 368
Cdd:PRK09059 278 RtfFKLSPPL-RTEDDRVAMVEAVASGTIDIIVSSHDPQDVDTKRL---PFSEAAAGAIGLETLLAAAL-RLYHNGEVPL 352
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 71989490 369 MRYVSITSSTAAKIFNIypRKGRIAVGSDADIVIFNPNATRTISKDTHHHNLDFNIFEGINCHGVAEVTISRGRIVWAH 447
Cdd:PRK09059 353 LRLIEALSTRPAEIFGL--PAGTLKPGAPADIIVIDLDEPWVVDPEDLKSRSKNTPFEEARFQGRVVRTIVAGKTVYEL 429
|
|
| FMDH_A |
cd01304 |
Formylmethanofuran dehydrogenase (FMDH) subunit A; Methanogenic bacteria and archea derive ... |
7-63 |
1.57e-08 |
|
Formylmethanofuran dehydrogenase (FMDH) subunit A; Methanogenic bacteria and archea derive the energy for autotrophic growth from methanogenesis, the reduction of CO2 with molecular hydrogen as the electron donor. FMDH catalyzes the first step in methanogenesis, the formyl-methanofuran synthesis. In this step, CO2 is bound to methanofuran and subsequently reduced to the formyl state with electrons derived from hydrogen.
Pssm-ID: 238629 [Multi-domain] Cd Length: 541 Bit Score: 57.04 E-value: 1.57e-08
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 71989490 7 IKNGTVV---NEDGMFKADVLVRNGIIVEVSpniTALPDTEVIDATDRLVIPGGIDPHTH 63
Cdd:cd01304 1 IKNGTVYdplNGINGEKMDIFIRDGKIVESS---SGAKPAKVIDASGKVVMAGGVDMHSH 57
|
|
| Urease_alpha |
cd00375 |
Urease alpha-subunit; Urease is a nickel-dependent metalloenzyme that catalyzes the hydrolysis ... |
5-92 |
1.84e-08 |
|
Urease alpha-subunit; Urease is a nickel-dependent metalloenzyme that catalyzes the hydrolysis of urea to form ammonia and carbon dioxide. Nickel-dependent ureases are found in bacteria, fungi and plants. Their primary role is to allow the use of external and internally generated urea as a nitrogen source. The enzyme consists of 3 subunits, alpha, beta and gamma, which can be fused and present on a single protein chain and which in turn forms multimers, mainly trimers. The large alpha subunit is the catalytic domain containing an active site with a bi-nickel center complexed by a carbamylated lysine. The beta and gamma subunits play a role in subunit association to form the higher order trimers.
Pssm-ID: 238221 [Multi-domain] Cd Length: 567 Bit Score: 56.57 E-value: 1.84e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71989490 5 LVIKNGTVVNEDGMFKADVLVRNGIIVE------------VSPNITALPDTEVIDATDRLVIPGGIDPHTHMQMPYMGEv 72
Cdd:cd00375 67 LVITNALIIDYTGIYKADIGIKDGRIVAigkagnpdimdgVTPNMIVGPSTEVIAGEGKIVTAGGIDTHVHFICPQQIE- 145
|
90 100
....*....|....*....|
gi 71989490 73 tkddflkgtEAAVAGGTTMI 92
Cdd:cd00375 146 ---------EALASGITTMI 156
|
|
| YtcJ |
COG1574 |
Predicted amidohydrolase YtcJ [General function prediction only]; |
2-64 |
3.91e-08 |
|
Predicted amidohydrolase YtcJ [General function prediction only];
Pssm-ID: 441182 [Multi-domain] Cd Length: 535 Bit Score: 55.58 E-value: 3.91e-08
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 71989490 2 SPPLVIKNGTV--VNEDGMFKADVLVRNGIIVEVSPN--ITAL--PDTEVIDATDRLVIPGGIDPHTHM 64
Cdd:COG1574 7 AADLLLTNGRIytMDPAQPVAEAVAVRDGRIVAVGSDaeVRALagPATEVIDLGGKTVLPGFIDAHVHL 75
|
|
| ureC |
PRK13207 |
urease subunit alpha; Reviewed |
5-92 |
1.53e-07 |
|
urease subunit alpha; Reviewed
Pssm-ID: 237305 [Multi-domain] Cd Length: 568 Bit Score: 53.64 E-value: 1.53e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71989490 5 LVIKNGTVVNEDGMFKADVLVRNGIIV--------EVSPNITAL--PDTEVIDATDRLVIPGGIDPHTHMQMPYMGEvtk 74
Cdd:PRK13207 69 TVITNALILDHWGIVKADIGIKDGRIVaigkagnpDIQDGVDIIigPGTEVIAGEGLIVTAGGIDTHIHFICPQQIE--- 145
|
90
....*....|....*...
gi 71989490 75 ddflkgtEAAVAGGTTMI 92
Cdd:PRK13207 146 -------EALASGVTTMI 156
|
|
| ureC |
PRK13206 |
urease subunit alpha; Reviewed |
2-92 |
1.85e-07 |
|
urease subunit alpha; Reviewed
Pssm-ID: 237304 [Multi-domain] Cd Length: 573 Bit Score: 53.56 E-value: 1.85e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71989490 2 SPPLVIKNGTVVNEDGMFKADVLVRNGIIVE------------VSPNITALPDTEVIDATDRLVIPGGIDPHTHMQMPYM 69
Cdd:PRK13206 70 APDTVITGAVILDHWGIVKADVGIRDGRIVAigkagnpdimdgVHPDLVIGPSTEIIAGNGRILTAGAIDCHVHFICPQI 149
|
90 100
....*....|....*....|...
gi 71989490 70 GEvtkddflkgtEAAVAGGTTMI 92
Cdd:PRK13206 150 VD----------EALAAGITTLI 162
|
|
| PRK07228 |
PRK07228 |
5'-deoxyadenosine deaminase; |
5-63 |
3.08e-07 |
|
5'-deoxyadenosine deaminase;
Pssm-ID: 180895 [Multi-domain] Cd Length: 445 Bit Score: 52.69 E-value: 3.08e-07
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 71989490 5 LVIKNGTVV---NEDGMFKADVLVRNGIIVEVSPNITALPDTEVIDATDRLVIPGGIDPHTH 63
Cdd:PRK07228 3 ILIKNAGIVtmnAKREIVDGDVLIEDDRIAAVGDRLDLEDYDDHIDATGKVVIPGLIQGHIH 64
|
|
| Amidohydro_3 |
pfam07969 |
Amidohydrolase family; |
44-444 |
4.68e-07 |
|
Amidohydrolase family;
Pssm-ID: 400360 [Multi-domain] Cd Length: 464 Bit Score: 52.15 E-value: 4.68e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71989490 44 EVIDATDRLVIPGGIDPHTH-------MQMPYMGEVTKDDFLKGTEA--------------------AVAGGTTMIIDFC 96
Cdd:pfam07969 1 EVIDAKGRLVLPGFVDPHTHldggglnLRELRLPDVLPNAVVKGQAGrtpkgrwlvgegwdeaqfaeTRFPYALADLDEV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71989490 97 CPDH-------------RN-----------------GESLIAGYNRWRSWAdpkvccdYGLSVAITMWRPETAEQMAIIT 146
Cdd:pfam07969 81 APDGpvllralhthaavANsaaldlagitkatedppGGEIARDANGEGLTG-------LLREGAYALPPLLAREAEAAAV 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71989490 147 S---PEFGVNSFKFYMAYENTLMVRDD-ELFRGMQECAKLRALARVHCENGSVIKEKE-----IDLLAKGVTG------- 210
Cdd:pfam07969 154 AaalAALPGFGITSVDGGGGNVHSLDDyEPLRELTAAEKLKELLDAPERLGLPHSIYElrigaMKLFADGVLGsrtaalt 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71989490 211 -PEGHTQSRPEEIEAEAT-NRACVLAAQANCPVYIvHVMTKGAASA-------------------ISHhrAQGSIVFG-- 267
Cdd:pfam07969 234 ePYFDAPGTGWPDFEDEAlAELVAAARERGLDVAI-HAIGDATIDTaldafeavaeklgnqgrvrIEH--AQGVVPYTys 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71989490 268 --EPIAA-GLALDGSHYYNEDWLHAARYVMSPPlSRDPTTPelLMKLLAAGELHLTGTD-NCTYDCRQKSLGkGNFTKIP 343
Cdd:pfam07969 311 qiERVAAlGGAAGVQPVFDPLWGDWLQDRLGAE-RARGLTP--VKELLNAGVKVALGSDaPVGPFDPWPRIG-AAVMRQT 386
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71989490 344 NGingvedRMSVVWEKGVHSgiidpmRY--VSITSSTAAKIFNIYPRKGRIAVGSDADIVIFNPNATRTisKDTHHHNLd 421
Cdd:pfam07969 387 AG------GGEVLGPDEELS------LEeaLALYTSGPAKALGLEDRKGTLGVGKDADLVVLDDDPLTV--DPPAIADI- 451
|
490 500
....*....|....*....|...
gi 71989490 422 fnifeginchgVAEVTISRGRIV 444
Cdd:pfam07969 452 -----------RVRLTVVDGRVV 463
|
|
| PRK06038 |
PRK06038 |
N-ethylammeline chlorohydrolase; Provisional |
5-66 |
4.74e-07 |
|
N-ethylammeline chlorohydrolase; Provisional
Pssm-ID: 180363 [Multi-domain] Cd Length: 430 Bit Score: 52.06 E-value: 4.74e-07
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 71989490 5 LVIKNGTVVNED--GMFKADVLVRNGIIVEVSPNITALPDTeVIDATDRLVIPGGIDPHTHMQM 66
Cdd:PRK06038 4 IIIKNAYVLTMDagDLKKGSVVIEDGTITEVSESTPGDADT-VIDAKGSVVMPGLVNTHTHAAM 66
|
|
| Bact_CD |
cd01293 |
Bacterial cytosine deaminase and related metal-dependent hydrolases. Cytosine deaminases (CDs) ... |
21-64 |
4.80e-07 |
|
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: 51.86 E-value: 4.80e-07
10 20 30 40
....*....|....*....|....*....|....*....|....
gi 71989490 21 ADVLVRNGIIVEVSPNITALPDTEVIDATDRLVIPGGIDPHTHM 64
Cdd:cd01293 15 VDIAIEDGRIAAIGPALAVPPDAEEVDAKGRLVLPAFVDPHIHL 58
|
|
| PLN02303 |
PLN02303 |
urease |
6-92 |
4.83e-07 |
|
urease
Pssm-ID: 215172 [Multi-domain] Cd Length: 837 Bit Score: 52.44 E-value: 4.83e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71989490 6 VIKNGTVVNEDGMFKADVLVRNGIIV------------EVSPNITALPDTEVIDATDRLVIPGGIDPHTHMQMPYMgevt 73
Cdd:PLN02303 337 VITNAVIIDYTGIYKADIGIKDGLIVgigkagnpdvmdGVTSNMIVGVNTEVIAGEGMIVTAGGIDCHVHFICPQL---- 412
|
90
....*....|....*....
gi 71989490 74 kddflkGTEAAVAGGTTMI 92
Cdd:PLN02303 413 ------ATEAIASGITTLV 425
|
|
| Met_dep_hydrolase_C |
cd01309 |
Metallo-dependent hydrolases, subgroup C is part of the superfamily of metallo-dependent ... |
27-63 |
5.09e-07 |
|
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: 51.54 E-value: 5.09e-07
10 20 30
....*....|....*....|....*....|....*..
gi 71989490 27 NGIIVEVSPNITALPDTEVIDATDRLVIPGGIDPHTH 63
Cdd:cd01309 1 DGKIVAVGAEITTPADAEVIDAKGKHVTPGLIDAHSH 37
|
|
| YtcJ_like |
cd01300 |
YtcJ_like metal dependent amidohydrolases. YtcJ is a Bacillus subtilis ORF of unknown function. ... |
22-64 |
6.26e-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: 51.93 E-value: 6.26e-07
10 20 30 40
....*....|....*....|....*....|....*....|....*..
gi 71989490 22 DVLVRNGIIVEVSPNITAL----PDTEVIDATDRLVIPGGIDPHTHM 64
Cdd:cd01300 1 AVAVRDGRIVAVGSDAEAKalkgPATEVIDLKGKTVLPGFIDSHSHL 47
|
|
| PRK05985 |
PRK05985 |
cytosine deaminase; Provisional |
21-63 |
1.38e-06 |
|
cytosine deaminase; Provisional
Pssm-ID: 180337 [Multi-domain] Cd Length: 391 Bit Score: 50.32 E-value: 1.38e-06
10 20 30 40
....*....|....*....|....*....|....*....|...
gi 71989490 21 ADVLVRNGIIVEVSPNITALPDTEVIDATDRLVIPGGIDPHTH 63
Cdd:PRK05985 17 VDILIRDGRIAAIGPALAAPPGAEVEDGGGALALPGLVDGHIH 59
|
|
| Imidazolone-5PH |
cd01296 |
Imidazolonepropionase/imidazolone-5-propionate hydrolase (Imidazolone-5PH) catalyzes the third ... |
23-63 |
2.23e-06 |
|
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: 49.56 E-value: 2.23e-06
10 20 30 40
....*....|....*....|....*....|....*....|....*
gi 71989490 23 VLVRNGIIVEVSP----NITALPDTEVIDATDRLVIPGGIDPHTH 63
Cdd:cd01296 1 IAIRDGRIAAVGPaaslPAPGPAAAEEIDAGGRAVTPGLVDCHTH 45
|
|
| PRK07203 |
PRK07203 |
putative aminohydrolase SsnA; |
5-63 |
2.99e-06 |
|
putative aminohydrolase SsnA;
Pssm-ID: 235963 [Multi-domain] Cd Length: 442 Bit Score: 49.55 E-value: 2.99e-06
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 71989490 5 LVIKNGTVVNEDG----MFKADVLVRNGIIVEVSPN---ITALPDTEVIDATDRLVIPGGIDPHTH 63
Cdd:PRK07203 2 LLIGNGTAITRDPakpvIEDGAIAIEGNVIVEIGTTdelKAKYPDAEFIDAKGKLIMPGLINSHNH 67
|
|
| metallo-dependent_hydrolases |
cd01292 |
Superfamily of metallo-dependent hydrolases (also called amidohydrolase superfamily) is a ... |
58-194 |
3.67e-06 |
|
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: 48.48 E-value: 3.67e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71989490 58 IDPHTHMQMPYMGEV----------------TKDDFLKGTEAAVAGGTTMIIDFCCPDHRNGE----SLIAGYNRWRSWA 117
Cdd:cd01292 2 IDTHVHLDGSALRGTrlnlelkeaeelspedLYEDTLRALEALLAGGVTTVVDMGSTPPPTTTkaaiEAVAEAARASAGI 81
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 71989490 118 DpKVCCDYGLSVAITMWRPETAEQMA-IITSPEFGVNSFKFYMAYENTLmVRDDELFRGMQECAKLRALARVHCENGS 194
Cdd:cd01292 82 R-VVLGLGIPGVPAAVDEDAEALLLElLRRGLELGAVGLKLAGPYTATG-LSDESLRRVLEEARKLGLPVVIHAGELP 157
|
|
| Met_dep_hydrolase_B |
cd01307 |
Metallo-dependent hydrolases, subgroup B is part of the superfamily of metallo-dependent ... |
22-94 |
5.73e-06 |
|
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: 48.48 E-value: 5.73e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 71989490 22 DVLVRNGIIVEVSPNITALPDTEVIDATDRLVIPGGIDPHTHMqMPYMGEVtkddFLKGTEAAVAGGTTMIID 94
Cdd:cd01307 1 DVAIENGKIAAVGAALAAPAATQIVDAGGCYVSPGWIDLHVHV-YQGGTRY----GDRPDMIGVKSGVTTVVD 68
|
|
| ureC |
PRK13308 |
urease subunit alpha; Reviewed |
5-102 |
6.28e-06 |
|
urease subunit alpha; Reviewed
Pssm-ID: 183965 [Multi-domain] Cd Length: 569 Bit Score: 48.55 E-value: 6.28e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71989490 5 LVIKNGTVVNE-DGMFKADVLVRNGIIV------------EVSPNITALPDTEVIDATDRLVIPGGIDPHTHMQMPYMge 71
Cdd:PRK13308 70 FVLCNVTVIDPvLGIVKGDIGIRDGRIVgigkagnpdimdGVDPRLVVGPGTDVRPAEGLIATPGAIDVHVHFDSAQL-- 147
|
90 100 110
....*....|....*....|....*....|....*....
gi 71989490 72 vtkddflkgTEAAVAGG-TTMI-------IDFCCPDHRN 102
Cdd:PRK13308 148 ---------VDHALASGiTTMLggglgptVGIDSGGPFN 177
|
|
| PRK09061 |
PRK09061 |
D-glutamate deacylase; Validated |
5-405 |
1.03e-05 |
|
D-glutamate deacylase; Validated
Pssm-ID: 236369 [Multi-domain] Cd Length: 509 Bit Score: 47.77 E-value: 1.03e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71989490 5 LVIKNGTVVNEDGMFKA--DVLVRNGIIVEVSPNitALPDTEVIDATDRLVIPGGIDPHTHMQMPymgevtKDDFLKgte 82
Cdd:PRK09061 21 LVIRNGRVVDPETGLDAvrDVGIKGGKIAAVGTA--AIEGDRTIDATGLVVAPGFIDLHAHGQSV------AAYRMQ--- 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71989490 83 aAVAGGTTMI-----IDfccP-----DHRNGESLIAGYNRWRSWADPKVCCDYGLSVAITM-----WRPETAEQMAIITS 147
Cdd:PRK09061 90 -AFDGVTTALeleagVL---PvarwyAEQAGEGRPLNYGASVGWTPARIAVLTGPQAEGTIadfgkALGDPRWQERAATP 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71989490 148 PEfgvnsfkfymaYENTLMVRDDELFRGMQECAKLRALArvhceNGSVIKE-KEIDLLAKGVTGPEgHTQSRP-----EE 221
Cdd:PRK09061 166 AE-----------LAEILELLEQGLDEGALGIGIGAGYA-----PGTGHKEyLELARLAARAGVPT-YTHVRYlsnvdPR 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71989490 222 IEAEATNRACVLAAQANCPVYIVHVMTKG------AASAISHHRAQGSIVFGE--PIAAGLALDGSHYYNEDWLHA---- 289
Cdd:PRK09061 229 SSVDAYQELIAAAAETGAHMHICHVNSTSlrdidrCLALVEKAQAQGLDVTTEayPYGAGSTVVGAAFFDPGWLERmglg 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71989490 290 -------------------ARYVMSPP--------LSRDPTTPELLMK--------LLAAGELHLTGTDNCTYDCRQKSL 334
Cdd:PRK09061 309 ygslqwvetgerlltreelAKLRANDPgglvlihfLDEDNPRDRALLDrsvlfpgaAIASDAMPWTWSDGTVYEGDAWPL 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71989490 335 GKGNFTKiPNGiNG---------VEDRMSVVWEKGVHSGIIDPMRYVSiTSSTAAKifniypRKGRIAVGSDADIVIFNP 405
Cdd:PRK09061 389 PEDAVSH-PRS-AGtfarflreyVRERKALSLLEAIRKCTLMPAQILE-DSVPAMR------RKGRLQAGADADIVVFDP 459
|
|
| PRK07583 |
PRK07583 |
cytosine deaminase; |
3-64 |
1.14e-05 |
|
cytosine deaminase;
Pssm-ID: 236062 Cd Length: 438 Bit Score: 47.67 E-value: 1.14e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 71989490 3 PPLVIKNGT--VVNEDGMFKADVLVRNGIIVEVSPNITALPDTEVIDATDRLVIPGGIDPHTHM 64
Cdd:PRK07583 21 PAALLEGGVppGDTLEGLVLVDIEIADGKIAAILPAGGAPDELPAVDLKGRMVWPCFVDMHTHL 84
|
|
| PRK12393 |
PRK12393 |
amidohydrolase; Provisional |
21-64 |
1.33e-05 |
|
amidohydrolase; Provisional
Pssm-ID: 237088 [Multi-domain] Cd Length: 457 Bit Score: 47.37 E-value: 1.33e-05
10 20 30 40
....*....|....*....|....*....|....*....|....
gi 71989490 21 ADVLVRNGIIVEVSPnITALPDTEVIDATDRLVIPGGIDPHTHM 64
Cdd:PRK12393 26 PDIRIRDGRIAAIGA-LTPLPGERVIDATDCVVYPGWVNTHHHL 68
|
|
| ureB |
PRK13985 |
urease subunit alpha; |
5-89 |
1.37e-05 |
|
urease subunit alpha;
Pssm-ID: 184438 [Multi-domain] Cd Length: 568 Bit Score: 47.58 E-value: 1.37e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71989490 5 LVIKNGTVVNEDGMFKADVLVRNGIIV------------EVSPNITALPDTEVIDATDRLVIPGGIDPHTHMQMPymgEV 72
Cdd:PRK13985 67 LIITNALIIDYTGIYKADIGIKDGKIAgigkggnkdmqdGVKNNLSVGPATEALAGEGLIVTAGGIDTHIHFISP---QQ 143
|
90
....*....|....*..
gi 71989490 73 TKDDFLKGTEAAVAGGT 89
Cdd:PRK13985 144 IPTAFASGVTTMIGGGT 160
|
|
| PRK08203 |
PRK08203 |
hydroxydechloroatrazine ethylaminohydrolase; Reviewed |
3-64 |
2.46e-05 |
|
hydroxydechloroatrazine ethylaminohydrolase; Reviewed
Pssm-ID: 236184 [Multi-domain] Cd Length: 451 Bit Score: 46.77 E-value: 2.46e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 71989490 3 PPLVIKNG-TVVNEDGMFKAD----VLVRNGIIVEVSPNiTALPDT--EVIDATDRLVIPGGIDPHTHM 64
Cdd:PRK08203 1 TTLWIKNPlAIVTMDAARREIadggLVVEGGRIVEVGPG-GALPQPadEVFDARGHVVTPGLVNTHHHF 68
|
|
| PRK09230 |
PRK09230 |
cytosine deaminase; Provisional |
2-64 |
2.73e-05 |
|
cytosine deaminase; Provisional
Pssm-ID: 181713 Cd Length: 426 Bit Score: 46.62 E-value: 2.73e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 71989490 2 SPPLVIKNGTVVNEDGMFkaDVLVRNGIIVEVSPNITA-LPDTEVIDATDRLVIPGGIDPHTHM 64
Cdd:PRK09230 3 NALMTIKNARLPGKEGLW--QITIEDGKISAIEPQSEAsLEAGEVLDAEGGLAIPPFIEPHIHL 64
|
|
| CAD_DHOase |
cd01316 |
The eukaryotic CAD protein is a trifunctional enzyme of carbamoylphosphate ... |
54-143 |
3.69e-05 |
|
The eukaryotic CAD protein is a trifunctional enzyme of carbamoylphosphate synthetase-aspartate transcarbamoylase-dihydroorotase, which catalyzes the first three steps of de novo pyrimidine nucleotide biosynthesis. Dihydroorotase (DHOase) catalyzes the third step, the reversible interconversion of carbamoyl aspartate to dihydroorotate.
Pssm-ID: 238641 [Multi-domain] Cd Length: 344 Bit Score: 45.90 E-value: 3.69e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71989490 54 IPGGIDPHTHMQMPymGEVTKDDFLKGTEAAVAGGTTMI--IDFCCPDHRNGESLIAGynrwRSWADPKVCCDYGLSVAI 131
Cdd:cd01316 5 LPGLIDVHVHLREP--GATHKEDFASGTKAALAGGFTMVraMPNTNPSIVDVASLKLV----QSLAQAKARCDYAFSIGA 78
|
90
....*....|..
gi 71989490 132 TMWRPETAEQMA 143
Cdd:cd01316 79 TSTNAATVGELA 90
|
|
| PRK06380 |
PRK06380 |
metal-dependent hydrolase; Provisional |
1-81 |
8.53e-05 |
|
metal-dependent hydrolase; Provisional
Pssm-ID: 180548 [Multi-domain] Cd Length: 418 Bit Score: 44.87 E-value: 8.53e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71989490 1 MSppLVIKNGTVVNEDG---MFKADVLVRNGIIVEVSpniTALPDTE-VIDATDRLVIPGGIDPHTHMQMPYM----GEV 72
Cdd:PRK06380 1 MS--ILIKNAWIVTQNEkreILQGNVYIEGNKIVYVG---DVNEEADyIIDATGKVVMPGLINTHAHVGMTASkglfDDV 75
|
....*....
gi 71989490 73 TKDDFLKGT 81
Cdd:PRK06380 76 DLEEFLMKT 84
|
|
| Isoaspartyl-dipeptidase |
cd01308 |
Isoaspartyl dipeptidase hydrolyzes the beta-L-isoaspartyl linkages in dipeptides, as part of ... |
5-64 |
1.03e-04 |
|
Isoaspartyl dipeptidase hydrolyzes the beta-L-isoaspartyl linkages in dipeptides, as part of the degradative pathway to eliminate proteins with beta-L-isoaspartyl peptide bonds, bonds whereby the beta-group of an aspartate forms the peptide link with the amino group of the following amino acid. Formation of this bond is a spontaneous nonenzymatic reaction in nature and can profoundly effect the function of the protein. Isoaspartyl dipeptidase is an octameric enzyme that contains a binuclear zinc center in the active site of each subunit and shows a strong preference of hydrolyzing Asp-Leu dipeptides.
Pssm-ID: 238633 [Multi-domain] Cd Length: 387 Bit Score: 44.69 E-value: 1.03e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 71989490 5 LVIKNGTVVNEDGMFKADVLVRNGIIVEVSPNI--TALPDTEVIDATDRLVIPGGIDPHTHM 64
Cdd:cd01308 2 TLIKNAEVYAPEYLGKKDILIAGGKILAIEDQLnlPGYENVTVVDLHGKILVPGFIDQHVHI 63
|
|
| PRK12394 |
PRK12394 |
metallo-dependent hydrolase; |
1-94 |
2.62e-04 |
|
metallo-dependent hydrolase;
Pssm-ID: 183497 [Multi-domain] Cd Length: 379 Bit Score: 43.21 E-value: 2.62e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71989490 1 MSPPLVIKNGTVVN--EDGMFKADVLVRNGIIVEVSpNITALPDTEVIDATDRLVIPGGIDPHTHMqmpymgevtkddFL 78
Cdd:PRK12394 1 MKNDILITNGHIIDpaRNINEINNLRIINDIIVDAD-KYPVASETRIIHADGCIVTPGLIDYHAHV------------FY 67
|
90 100
....*....|....*....|...
gi 71989490 79 KGTEAAVAG-------GTTMIID 94
Cdd:PRK12394 68 DGTEGGVRPdmymppnGVTTVVD 90
|
|
| ureC |
PRK13309 |
urease subunit alpha; Reviewed |
5-109 |
4.19e-04 |
|
urease subunit alpha; Reviewed
Pssm-ID: 183966 [Multi-domain] Cd Length: 572 Bit Score: 42.94 E-value: 4.19e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71989490 5 LVIKNGTVVNE-DGMFKADVLVRNGIIVE------------VSPNITALPDTEVIDATDRLVIPGGIDPHTHMQMPymge 71
Cdd:PRK13309 70 LVITNVTIVDArLGVIKADVGIRDGKIVGigksgnpstmdgVTQGMVVGVSTDAISGEHLILTAAGIDTHIHLISP---- 145
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 71989490 72 vtkddflKGTEAAVAGG-TTMIIDFCCP-DHRNGESLIAG 109
Cdd:PRK13309 146 -------QQAYHALSNGvTTFFGGGIGPtDGTNGTTVTPG 178
|
|
| PRK09045 |
PRK09045 |
TRZ/ATZ family hydrolase; |
23-100 |
4.41e-04 |
|
TRZ/ATZ family hydrolase;
Pssm-ID: 236366 [Multi-domain] Cd Length: 443 Bit Score: 42.59 E-value: 4.41e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71989490 23 VLVRNGIIVEVSPNITAL---PDTEVIDATDRLVIPGGIDPHTHMQM----------PYM-----------GEVTKDDFL 78
Cdd:PRK09045 31 VAIRDGRIVAILPRAEARaryAAAETVELPDHVLIPGLINAHTHAAMsllrgladdlPLMtwlqdhiwpaeGAWVSEEFV 110
|
90 100
....*....|....*....|....*..
gi 71989490 79 K-GTEAAVA----GGTTmiidfCCPDH 100
Cdd:PRK09045 111 RdGTLLAIAemlrGGTT-----CFNDM 132
|
|
| PRK09228 |
PRK09228 |
guanine deaminase; Provisional |
15-63 |
1.49e-03 |
|
guanine deaminase; Provisional
Pssm-ID: 236419 [Multi-domain] Cd Length: 433 Bit Score: 40.94 E-value: 1.49e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 71989490 15 EDGMfkadVLVRNGIIVEVSP----NITALPDTEVIDATDRLVIPGGIDPHTH 63
Cdd:PRK09228 30 EDGL----LLVEDGRIVAAGPyaelRAQLPADAEVTDYRGKLILPGFIDTHIH 78
|
|
| |
