|
Name |
Accession |
Description |
Interval |
E-value |
| D-HYD |
cd01314 |
D-hydantoinases (D-HYD) also called dihydropyrimidases (DHPase) and related proteins; DHPases ... |
7-460 |
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: 731.33 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958791289 7 LLIRGGRVVNDDFSQVADVLVEDGVVRALGRDLLPPGdtsrGLRILDAAGKLVLPGGIDTHTHMQFPFMGSQSVDDFHQG 86
Cdd:cd01314 1 LIIKNGTIVTADGSFKADILIEDGKIVAIGPNLEAPG----GVEVIDATGKYVLPGGIDPHTHLELPFMGTVTADDFESG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958791289 87 TKAALAGGTTMIIDFAIPQKGSSLIEAFETWRNWADPKVCCDYSLHVAVTWWSDKVKEEMKTLAqDKGVNSFKMFMAYKD 166
Cdd:cd01314 77 TRAAAAGGTTTIIDFAIPNKGQSLLEAVEKWRGKADGKSVIDYGFHMIITDWTDSVIEELPELV-KKGISSFKVFMAYKG 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958791289 167 LYMVQDQQMYAAFSQCKEIGAIAQVHAENGDLIAEGAKKMLALGITGPEGHELCRPEAVEAEATLRAITIASAVNCPLYI 246
Cdd:cd01314 156 LLMVDDEELLDVLKRAKELGALVMVHAENGDVIAELQKKLLAQGKTGPEYHALSRPPEVEAEATARAIRLAELAGAPLYI 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958791289 247 VHVMSKSAAKVIADAKREGKVVYGEPIAAGLGTDGTQYWnKEWRHAAHHVMGPPLRPDpSTPGFLMNLLANGDLTTTGSD 326
Cdd:cd01314 236 VHVSSKEAADEIARARKKGLPVYGETCPQYLLLDDSDYW-KDWFEGAKYVCSPPLRPK-EDQEALWDGLSSGTLQTVGSD 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958791289 327 NCTFNTCQKALGKDDFTKIPNGVNGVEDRMSVIWEKGVHSGKMDENRFVAVTSTNAAKIFNLYPKKGRIAVGSDADIVIW 406
Cdd:cd01314 314 HCPFNFAQKARGKDDFTKIPNGVPGVETRMPLLWSEGVAKGRITLEKFVELTSTNPAKIFGLYPRKGTIAVGSDADLVIW 393
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....
gi 1958791289 407 DPEATRTISAKTHHQAVNFNIFEGMVCHGVPLVTISRGRVVYEAGVFDVTAGHG 460
Cdd:cd01314 394 DPNAEKTISADTHHHNVDYNIFEGMKVKGWPVVTISRGKVVVEDGELVGEKGSG 447
|
|
| D-hydantoinase |
TIGR02033 |
D-hydantoinase; This model represents the D-hydantoinase (dihydropyrimidinase) which primarily ... |
7-465 |
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: 640.97 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958791289 7 LLIRGGRVVNDDFSQVADVLVEDGVVRALGRDLLPPGdtsrGLRILDAAGKLVLPGGIDTHTHMQFPFMGSQSVDDFHQG 86
Cdd:TIGR02033 1 LLIKGGTVVNADDVFQADVLIEGGKIVAVGDNLIPPD----AVEVIDATGKYVLPGGIDVHTHLEMPFGGTTTADDFFTG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958791289 87 TKAALAGGTTMIIDFAIPQKGSSLIEAFETWRNWADPKVCCDYSLHVAVTWWSDKVKEEMKTLAQDKGVNSFKMFMAYKD 166
Cdd:TIGR02033 77 TKAAAAGGTTTIIDFVVPEKGSSLTEALETWHEKAEGKSVIDYGFHMDITHWNDSVLEEHIPEVKEEGINSFKVFMAYKN 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958791289 167 LYMVQDQQMYAAFSQCKEIGAIAQVHAENGDLIAEGAKKMLALGITGPEGHELCRPEAVEAEATLRAITIASAVNCPLYI 246
Cdd:TIGR02033 157 LLMVDDEELFEILKRLKELGALLQVHAENGDIIAELQARMLAQGITGPEYHALSRPPELEAEAVARAITLAALADAPLYV 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958791289 247 VHVMSKSAAKVIADAKREGKVVYGEPIAAGLGTDGTQYWnKEWRHAAHHVMGPPLRpDPSTPGFLMNLLANGDLTTTGSD 326
Cdd:TIGR02033 237 VHVSTKDAADEIAQARKKGQPVFGETCPQYLVLDDTHYD-KPGFEGAKYVCSPPLR-EPEDQDALWSALSSGALQTVGSD 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958791289 327 NCTFNTCQK-ALGKDDFTKIPNGVNGVEDRMSVIWEKGVHSGKMDENRFVAVTSTNAAKIFNLYPKKGRIAVGSDADIVI 405
Cdd:TIGR02033 315 HCTFNFAQKkAIGKDDFTKIPNGGPGVEERMSLLFDEGVAKGRITLEKFVEVTSTNPAKIFNLYPRKGTIAVGSDADIVI 394
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958791289 406 WDPEATRTISAKTHHQAVNFNIFEGMVCHGVPLVTISRGRVVYEAGVFDVTAGHGKFIPR 465
Cdd:TIGR02033 395 WDPNRTTVISAETHHSNADYNPFEGFKVRGAPVSVLSRGRVVVEDGQLVGTAGAGRFVKR 454
|
|
| PRK08323 |
PRK08323 |
phenylhydantoinase; Validated |
6-468 |
0e+00 |
|
phenylhydantoinase; Validated
Pssm-ID: 236240 [Multi-domain] Cd Length: 459 Bit Score: 637.60 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958791289 6 RLLIRGGRVVNDDFSQVADVLVEDGVVRALGRDllppgdtsRGLRILDAAGKLVLPGGIDTHTHMQFPFMGSQSVDDFHQ 85
Cdd:PRK08323 2 STLIKNGTVVTADDTYKADVLIEDGKIAAIGAN--------LGDEVIDATGKYVMPGGIDPHTHMEMPFGGTVSSDDFET 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958791289 86 GTKAALAGGTTMIIDFAIPQKGSSLIEAFETWRNWADPKVCCDYSLHVAVTWWSDKVKEEMKTLAqDKGVNSFKMFMAYK 165
Cdd:PRK08323 74 GTRAAACGGTTTIIDFALQPKGQSLREALEAWHGKAAGKAVIDYGFHMIITDWNEVVLDEMPELV-EEGITSFKLFMAYK 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958791289 166 DLYMVQDQQMYAAFSQCKEIGAIAQVHAENGDLIAEGAKKMLALGITGPEGHELCRPEAVEAEATLRAITIASAVNCPLY 245
Cdd:PRK08323 153 GALMLDDDELLRALQRAAELGALPMVHAENGDAIAYLQAKLLAEGKTGPEYHALSRPPEVEGEATNRAIMLAELAGAPLY 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958791289 246 IVHVMSKSAAKVIADAKREGKVVYGEPIAAGLGTDGTQYWNKEWRHAAHHVMGPPLRPDPSTpGFLMNLLANGDLTTTGS 325
Cdd:PRK08323 233 IVHVSCKEALEAIRRARARGQRVFGETCPQYLLLDESEYDGPDWFEGAKYVMSPPLRDKEHQ-DALWRGLQDGDLQVVAT 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958791289 326 DNCTFNTCQKA-LGKDDFTKIPNGVNGVEDRMSVIWEKGVHSGKMDENRFVAVTSTNAAKIFNLYPKKGRIAVGSDADIV 404
Cdd:PRK08323 312 DHCPFCFEQKKqLGRGDFTKIPNGTPGVEDRMPLLFSEGVMTGRITLNRFVELTSTNPAKIFGLYPRKGTIAVGADADIV 391
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1958791289 405 IWDPEATRTISAKTHHQAVNFNIFEGMVCHGVPLVTISRGRVVYEAGVFDVTAGHGKFIPRQPF 468
Cdd:PRK08323 392 IWDPNATKTISASTLHSNVDYNPYEGFEVTGWPVTTLSRGEVVVEDGEFRGKAGHGRFLKRKPF 455
|
|
| PLN02942 |
PLN02942 |
dihydropyrimidinase |
1-491 |
0e+00 |
|
dihydropyrimidinase
Pssm-ID: 178530 Cd Length: 486 Bit Score: 623.40 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958791289 1 MAPQERLLIRGGRVVNDDFSQVADVLVEDGVVRALGRDLlppgDTSRGLRILDAAGKLVLPGGIDTHTHMQFPFMGSQSV 80
Cdd:PLN02942 1 GASSTKILIKGGTVVNAHHQELADVYVEDGIIVAVAPNL----KVPDDVRVIDATGKFVMPGGIDPHTHLAMPFMGTETI 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958791289 81 DDFHQGTKAALAGGTTMIIDFAIPQKGSsLIEAFETWRNWADpKVCCDYSLHVAVTWWSDKVKEEMKTLAQDKGVNSFKM 160
Cdd:PLN02942 77 DDFFSGQAAALAGGTTMHIDFVIPVNGN-LLAGYEAYEKKAE-KSCMDYGFHMAITKWDDTVSRDMETLVKEKGINSFKF 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958791289 161 FMAYKDLYMVQDQQMYAAFSQCKEIGAIAQVHAENGDLIAEGAKKMLALGITGPEGHELCRPEAVEAEATLRAITIASAV 240
Cdd:PLN02942 155 FMAYKGSLMVTDELLLEGFKRCKSLGALAMVHAENGDAVFEGQKRMIELGITGPEGHALSRPPLLEGEATARAIRLAKFV 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958791289 241 NCPLYIVHVMSKSAAKVIADAKREGKVVYGEPIAAGLGTDGTQYWNKEWRHAAHHVMGPPLRPdPSTPGFLMNLLANGDL 320
Cdd:PLN02942 235 NTPLYVVHVMSIDAMEEIARARKSGQRVIGEPVVSGLVLDDSKLWDPDFTIASKYVMSPPIRP-AGHGKALQAALSSGIL 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958791289 321 TTTGSDNCTFNTCQKALGKDDFTKIPNGVNGVEDRMSVIWEKGVHSGKMDENRFVAVTSTNAAKIFNLYPKKGRIAVGSD 400
Cdd:PLN02942 314 QLVGTDHCPFNSTQKAFGKDDFRKIPNGVNGIEERMHLVWDTMVESGQISPTDYVRVTSTECAKIFNIYPRKGAILAGSD 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958791289 401 ADIVIWDPEATRTISAKTHHQAVNFNIFEGMVCHGVPLVTISRGRVVYEAGVFDVTAGHGKFIPRQPFAeFIYKRVKQRD 480
Cdd:PLN02942 394 ADIIILNPNSTFTISAKTHHSRIDTNVYEGRRGKGKVEVTISQGRVVWENGELKVVRGSGRYIEMPPFS-YLFDGIQKAD 472
|
490
....*....|....
gi 1958791289 481 QTCTP---IPVKRA 491
Cdd:PLN02942 473 AAYLSslrAPVKRT 486
|
|
| AllB |
COG0044 |
Dihydroorotase or related cyclic amidohydrolase [Nucleotide transport and metabolism]; ... |
8-465 |
3.48e-145 |
|
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: 424.12 E-value: 3.48e-145
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958791289 8 LIRGGRVVNDDFSQVADVLVEDGVVRALGRDLLPPGDTsrglRILDAAGKLVLPGGIDTHTHMQFPFMGSQsvDDFHQGT 87
Cdd:COG0044 1 LIKNGRVVDPGGLERADVLIEDGRIAAIGPDLAAPEAA----EVIDATGLLVLPGLIDLHVHLREPGLEHK--EDIETGT 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958791289 88 KAALAGGTTMIIDFAIPQKGSSLIEAFETWRNWADPKVCCDYSLHVAVTWWSDKVKEEMKTLAqDKGVNSFKMFMAYKDL 167
Cdd:COG0044 75 RAAAAGGVTTVVDMPNTNPVTDTPEALEFKLARAEEKALVDVGPHGALTKGLGENLAELGALA-EAGAVAFKVFMGSDDG 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958791289 168 YMVQD-QQMYAAFSQCKEIGAIAQVHAENGDLIAEGAKkmlALGITGPEGHELCRPEAVEAEATLRAITIASAVNCPLYI 246
Cdd:COG0044 154 NPVLDdGLLRRALEYAAEFGALVAVHAEDPDLIRGGVM---NEGKTSPRLGLKGRPAEAEEEAVARDIALAEETGARLHI 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958791289 247 VHVMSKSAAKVIADAKREGKVVYGE--P-----IAAGLGTDGTQYwnkewrhaahhVMGPPLRpDPSTPGFLMNLLANGD 319
Cdd:COG0044 231 VHVSTAEAVELIREAKARGLPVTAEvcPhhltlTDEDLERYGTNF-----------KVNPPLR-TEEDREALWEGLADGT 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958791289 320 LTTTGSDNCTFNTCQKAlgkDDFTKIPNGVNGVEDRMSVIWEKGVHSGKMDENRFVAVTSTNAAKIFNLyPKKGRIAVGS 399
Cdd:COG0044 299 IDVIATDHAPHTLEEKE---LPFAEAPNGIPGLETALPLLLTELVHKGRLSLERLVELLSTNPARIFGL-PRKGRIAVGA 374
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1958791289 400 DADIVIWDPEATRTISAKTHHQAVNFNIFEGMVCHGVPLVTISRGRVVYEAGVFdVTAGHGKFIPR 465
Cdd:COG0044 375 DADLVLFDPDAEWTVTAEDLHSKSKNTPFEGRELTGRVVATIVRGRVVYEDGEV-VGEPRGRFLRR 439
|
|
| PRK13404 |
PRK13404 |
dihydropyrimidinase; Provisional |
3-465 |
1.43e-132 |
|
dihydropyrimidinase; Provisional
Pssm-ID: 184033 [Multi-domain] Cd Length: 477 Bit Score: 393.29 E-value: 1.43e-132
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958791289 3 PQERLLIRGGRVVNDDFSQVADVLVEDGVVRALGRDLLPpgdtsrGLRILDAAGKLVLPGGIDTHTHM-QFPFMGSQSVD 81
Cdd:PRK13404 2 MAFDLVIRGGTVVTATDTFQADIGIRGGRIAALGEGLGP------GAREIDATGRLVLPGGVDSHCHIdQPSGDGIMMAD 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958791289 82 DFHQGTKAALAGGTTMIIDFAIPQKGSSLIEAFETWRNWADPKVCCDYSLHVAVTWWSDKV-KEEMKTLAQDkGVNSFKM 160
Cdd:PRK13404 76 DFYTGTVSAAFGGTTTVIPFAAQHRGQSLREAVEDYHRRAAGKAVIDYAFHLIVADPTEEVlTEELPALIAQ-GYTSFKV 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958791289 161 FMAYKDLyMVQDQQMYAAFSQCKEIGAIAQVHAENGDLIAEGAKKMLALGITGPEGHELCRPEAVEAEATLRAITIASAV 240
Cdd:PRK13404 155 FMTYDDL-KLDDRQILDVLAVARRHGAMVMVHAENHDMIAWLTKRLLAAGLTAPKYHAISRPMLAEREATHRAIALAELV 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958791289 241 NCPLYIVHVMSKSAAKVIADAKREGKVVYGEP-------IAAGLGTDGTqywnkewrHAAHHVMGPPLRpDPSTPGFLMN 313
Cdd:PRK13404 234 DVPILIVHVSGREAAEQIRRARGRGLKIFAETcpqylflTAEDLDRPGM--------EGAKYICSPPPR-DKANQEAIWN 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958791289 314 LLANGDLTTTGSDNCTFN---TCQKALGKDD--FTKIPNGVNGVEDRMSVIWEKGVHSGKMDENRFVAVTSTNAAKIFNL 388
Cdd:PRK13404 305 GLADGTFEVFSSDHAPFRfddTDGKLAAGANpsFKAIANGIPGIETRLPLLFSEGVVKGRISLNRFVALTSTNPAKLYGL 384
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1958791289 389 YPKKGRIAVGSDADIVIWDPEATRTISAKTHHQAVNFNIFEGMVCHGVPLVTISRGRVVYEAGVFDVTAGHGKFIPR 465
Cdd:PRK13404 385 YPRKGAIAIGADADIAIWDPDREVTITNADLHHAADYTPYEGMRVTGWPVTVLSRGRVVVEDGELVAERGSGQFLAR 461
|
|
| L-HYD_ALN |
cd01315 |
L-Hydantoinases (L-HYDs) and Allantoinase (ALN); L-Hydantoinases are a member of the ... |
7-463 |
2.66e-76 |
|
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: 247.20 E-value: 2.66e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958791289 7 LLIRGGRVVNDDFSQVADVLVEDGVVRALGRDLLPPGdtsrGLRILDAAGKLVLPGGIDTHTHMQFPfmGSQSVDDFHQG 86
Cdd:cd01315 2 LVIKNGRVVTPDGVREADIAVKGGKIAAIGPDIANTE----AEEVIDAGGLVVMPGLIDTHVHINEP--GRTEWEGFETG 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958791289 87 TKAALAGGTTMIIDF---AIPQkgSSLIEAFETWRNWADPKvccdysLHVAVTWWSDKVK---EEMKTLAqDKGVNSFKM 160
Cdd:cd01315 76 TKAAAAGGITTIIDMplnSIPP--TTTVENLEAKLEAAQGK------LHVDVGFWGGLVPgnlDQLRPLD-EAGVVGFKC 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958791289 161 FMA---YKDLYMVQDQQMYAAFSQCKEIGAIAQVHAENGDLIAEGAKKMLALGITGPEGHELCRPEAVEAEATLRAITIA 237
Cdd:cd01315 147 FLCpsgVDEFPAVDDEQLEEAMKELAKTGSVLAVHAENPEITEALQEQAKAKGKRDYRDYLASRPVFTEVEAIQRILLLA 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958791289 238 SAVNCPLYIVHVMSKSAAKVIADAKREGKVVYGEPIAAGLGTDGTQYwnkEWRHAAHHVmGPPLRpDPSTPGFLMNLLAN 317
Cdd:cd01315 227 KETGCRLHIVHLSSAEAVPLIREARAEGVDVTVETCPHYLTFTAEDV---PDGGTEFKC-APPIR-DAANQEQLWEALEN 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958791289 318 GDLTTTGSDN--CTFNtcQKALGKDDFTKIPNGVNGVEDRMSVIWEKGVHSGKMDENRFVAVTSTNAAKIFNLYPKKGRI 395
Cdd:cd01315 302 GDIDMVVSDHspCTPE--LKLLGKGDFFKAWGGISGLQLGLPVMLTEAVNKRGLSLEDIARLMCENPAKLFGLSHQKGRI 379
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1958791289 396 AVGSDADIVIWDPEATRTISA---KTHHQAvnfNIFEGMVCHGVPLVTISRGRVVYEAGVFdVTAGHGKFI 463
Cdd:cd01315 380 AVGYDADFVVWDPEEEFTVDAedlYYKNKI---SPYVGRTLKGRVHATILRGTVVYQDGEV-VGEPLGQLL 446
|
|
| Cyclic_amidohydrolases |
cd01302 |
Cyclic amidohydrolases, including hydantoinase, dihydropyrimidinase, allantoinase, and ... |
57-440 |
1.46e-70 |
|
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: 228.82 E-value: 1.46e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958791289 57 KLVLPGGIDTHTHMQFPFMGSQSvDDFHQGTKAALAGGTTMIIDFAIPQKGSSLIEAFETWRNWADPKVCCDYSLHVAVt 136
Cdd:cd01302 1 LLVLPGFIDIHVHLRDPGGTTYK-EDFESGSRAAAAGGVTTVIDMPNTGPPPIDLPAIELKIKLAEESSYVDFSFHAGI- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958791289 137 wWSDKVKEEMKtLAQDKGVNSFKMFMAYK--DLYMVQDQQMYAAFSQCKEIGAIAQVHAEngdliaegakkmlalgitgp 214
Cdd:cd01302 79 -GPGDVTDELK-KLFDAGINSLKVFMNYYfgELFDVDDGTLMRTFLEIASRGGPVMVHAE-------------------- 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958791289 215 eghelcrpeaveaeatlRAITIASAVNCPLYIVHVMSKSAAKVIADAKREGKVVYGEPiaaglgtdGTQYWN---KEWRH 291
Cdd:cd01302 137 -----------------RAAQLAEEAGANVHIAHVSSGEALELIKFAKNKGVKVTCEV--------CPHHLFldeSMLRL 191
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958791289 292 AAHH-VMGPPLRPdPSTPGFLMNLLANGDLTTTGSDNCTFNTCQKALGKDdFTKIPNGVNGVEDRMSVIWEKGVHSGkMD 370
Cdd:cd01302 192 NGAWgKVNPPLRS-KEDREALWEGVKNGKIDTIASDHAPHSKEEKESGKD-IWKAPPGFPGLETRLPILLTEGVKRG-LS 268
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958791289 371 ENRFVAVTSTNAAKIFNLYPKKgRIAVGSDADIVIWDPEATRTISAKTHHQAVNFNIFEGMVCHGVPLVT 440
Cdd:cd01302 269 LETLVEILSENPARIFGLYPKG-TIAVGYDADLVIVDPKKEWKVTAEEIESKADWTPFEGMEVTGKPVST 337
|
|
| PRK02382 |
PRK02382 |
dihydroorotase; Provisional |
7-464 |
4.58e-60 |
|
dihydroorotase; Provisional
Pssm-ID: 179417 [Multi-domain] Cd Length: 443 Bit Score: 204.50 E-value: 4.58e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958791289 7 LLIRGGRVVNDDFSQVADVLVEDGVVRALGRDLlppgDTSRGLRILDAAGKLVLPGGIDTHTHmqFPFMGSQSVDDFHQG 86
Cdd:PRK02382 4 ALLKDGRVYYNNSLQPRDVRIDGGKITAVGKDL----DGSSSEEVIDARGMLLLPGGIDVHVH--FREPGYTHKETWYTG 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958791289 87 TKAALAGGTTMIIDfaIPQKGSSLI--EAFETWRNWADPKVCCDYSLHVAVTWWSDKVKEEMktlaqDKGVNSF-KMFMA 163
Cdd:PRK02382 78 SRSAAAGGVTTVVD--QPNTDPPTVdgESFDEKAELAARKSIVDFGINGGVTGNWDPLESLW-----ERGVFALgEIFMA 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958791289 164 YKDLYMVQDQQMYA-AFSQCKEIGAIAQVHAENGDLIAEGAKkmLALGITGPEGHELCRPEAVEAEATLRAITIASAVNC 242
Cdd:PRK02382 151 DSTGGMGIDEELFEeALAEAARLGVLATVHAEDEDLFDELAK--LLKGDADADAWSAYRPAAAEAAAVERALEVASETGA 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958791289 243 PLYIVHVmskSAAKVIADAKREGKVVYGEPIAAGLGTDgtqywnkEW-RHAAHHVMGPPLRPDPSTPGfLMNLLANGDLT 321
Cdd:PRK02382 229 RIHIAHI---STPEGVDAARREGITCEVTPHHLFLSRR-------DWeRLGTFGKMNPPLRSEKRREA-LWERLNDGTID 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958791289 322 TTGSDNCTFNTCQKALgkdDFTKIPNGVNGVEDRMSVIWEkGVHSGKMDENRFVAVTSTNAAKIFNLyPKKGRIAVGSDA 401
Cdd:PRK02382 298 VVASDHAPHTREEKDA---DIWDAPSGVPGVETMLPLLLA-AVRKNRLPLERVRDVTAANPARIFGL-DGKGRIAEGYDA 372
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1958791289 402 DIVIWDPEATRTISAKTHHQAVNFNIFEGMVchGV-PLVTISRGRVVYEAGVFDVTAGHGKFIP 464
Cdd:PRK02382 373 DLVLVDPDAAREIRGDDLHSKAGWTPFEGME--GVfPELTMVRGTVVWDGDDINAKRGRGEFLR 434
|
|
| PRK06189 |
PRK06189 |
allantoinase; Provisional |
7-467 |
3.27e-54 |
|
allantoinase; Provisional
Pssm-ID: 235732 [Multi-domain] Cd Length: 451 Bit Score: 189.14 E-value: 3.27e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958791289 7 LLIRGGRVVNDDFSQVADVLVEDGVVRALGRDLLPPGDtsrglRILDAAGKLVLPGGIDTHTHMQFPfmGSQSVDDFHQG 86
Cdd:PRK06189 5 LIIRGGKVVTPEGVYRADIGIKNGKIAEIAPEISSPAR-----EIIDADGLYVFPGMIDVHVHFNEP--GRTHWEGFATG 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958791289 87 TKAALAGGTTMIIDFAIPQKGSSLI-EAFETWRNWADPKVCCDYSLhvavtwWSDKV---KEEMKTLAqDKGVNSFKMFM 162
Cdd:PRK06189 78 SAALAAGGCTTYFDMPLNSIPPTVTrEALDAKAELARQKSAVDFAL------WGGLVpgnLEHLRELA-EAGVIGFKAFM 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958791289 163 AY---KDLYMVQDQQMYAAFSQCKEIGAIAQVHAENGDLIAEGAKKMLALGITGPEGHELCRPEAVEAEATLRAITIASA 239
Cdd:PRK06189 151 SNsgtDEFRSSDDLTLYEGMKEIAALGKILALHAESDALTRHLTTQARQQGKTDVRDYLESRPVVAELEAVQRALLYAQE 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958791289 240 VNCPLYIVHVMSKSAAKVIADAKREGKVVYGEPIAAGLGTDGTQYwnkeWRHAAHHVMGPPLRpDPSTPGFLMNLLANGD 319
Cdd:PRK06189 231 TGCPLHFVHISSGKAVALIAEAKKRGVDVSVETCPHYLLFTEEDF----ERIGAVAKCAPPLR-SRSQKEELWRGLLAGE 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958791289 320 LTTTGSDNctfNTCQKALGK-DDFTKIPNGVNGVEDRMSVIWEKGVHSGKMDENRFVAVTSTNAAKIFNLyPKKGRIAVG 398
Cdd:PRK06189 306 IDMISSDH---SPCPPELKEgDDFFLVWGGISGGQSTLLVMLTEGYIERGIPLETIARLLATNPAKRFGL-PQKGRLEVG 381
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1958791289 399 SDADIVIWDPEATRTISAKTHHQAVNFNIFEGMVCHGVPLVTISRGRVVYEAGVFDVTAgHGKFIPRQP 467
Cdd:PRK06189 382 ADADFVLVDLDETYTLTKEDLFYRHKQSPYEGRTFPGRVVATYLRGQCVYQDGEVFPPP-RGQLLRPSV 449
|
|
| pyrC_multi |
TIGR00857 |
dihydroorotase, multifunctional complex type; In contrast to the homodimeric type of ... |
23-450 |
1.39e-52 |
|
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: 183.80 E-value: 1.39e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958791289 23 ADVLVEDGVVRALGRDLLPPGDTsrglrILDAAGKLVLPGGIDTHTHMQFPfmGSQSVDDFHQGTKAALAGGTTMIIDFA 102
Cdd:TIGR00857 6 VDILVEGGRIKKIGKLRIPPDAE-----VIDAKGLLVLPGFIDLHVHLRDP--GEEYKEDIESGSKAAAHGGFTTVADMP 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958791289 103 IPQKGSSLIEAFETWRNWADPKVCCDYSLHVAVTWwSDKVKEEMKtlaqdkgvnSFKMFMA------YKDlYMVQDQQ-- 174
Cdd:TIGR00857 79 NTKPPIDTPETLEWKLQRLKKVSLVDVHLYGGVTQ-GNQGKELTE---------AYELKEAgavgrmFTD-DGSEVQDil 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958791289 175 -MYAAFSQCKEIGAIAQVHAENGDLIAEGAKKmlaLGITGPEGHELCRPEAVEAEATLRAITIASAVNCPLYIVHVMSKS 253
Cdd:TIGR00857 148 sMRRALEYAAIAGVPIALHAEDPDLIYGGVMH---EGPSAAQLGLPARPPEAEEVAVARLLELAKHAGCPVHICHISTKE 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958791289 254 AAKVIADAKREGKVVYGE--P--------IAAGLGTdgtqyWNKewrhaahhvMGPPLRPdPSTPGFLMNLLANGDLTTT 323
Cdd:TIGR00857 225 SLELIVKAKSQGIKITAEvtPhhlllseeDVARLDG-----NGK---------VNPPLRE-KEDRLALIEGLKDGIIDII 289
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958791289 324 GSDNCTFNTCQKALGkddFTKIPNGVNGVEDRMSVIWEkGVHSGKMDENRFVAVTSTNAAKIFNLyPKKGRIAVGSDADI 403
Cdd:TIGR00857 290 ATDHAPHTLEEKTKE---FAAAPPGIPGLETALPLLLQ-LLVKGLISLKDLIRMLSINPARIFGL-PDKGTLEEGNPADI 364
|
410 420 430 440
....*....|....*....|....*....|....*....|....*..
gi 1958791289 404 VIWDPEATRTISAKTHHQAVNFNIFEGMVCHGVPLVTISRGRVVYEA 450
Cdd:TIGR00857 365 TVFDLKKEWTINAETFYSKAKNTPFEGMSLKGKPIATILRGKVVYED 411
|
|
| pyrC |
PRK09357 |
dihydroorotase; Validated |
6-450 |
4.62e-41 |
|
dihydroorotase; Validated
Pssm-ID: 236479 [Multi-domain] Cd Length: 423 Bit Score: 152.66 E-value: 4.62e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958791289 6 RLLIRGGRVVN-DDFSQVADVLVEDGVVRALGRDLLPPGDTsrglrILDAAGKLVLPGGIDTHTHMQFPfmGSQSVDDFH 84
Cdd:PRK09357 2 MILIKNGRVIDpKGLDEVADVLIDDGKIAAIGENIEAEGAE-----VIDATGLVVAPGLVDLHVHLREP--GQEDKETIE 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958791289 85 QGTKAALAGG---------TTMIIDfaipqkgsSLIEAFETWRNWADPKVCcdyslHV----AVTWWSD-KVKEEMKTLA 150
Cdd:PRK09357 75 TGSRAAAAGGfttvvampnTKPVID--------TPEVVEYVLDRAKEAGLV-----DVlpvgAITKGLAgEELTEFGALK 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958791289 151 qDKGVnsfkmFMAYKDLYMVQDQQ-MYAAFSQCKEIG-AIAQvHAENGDLIAEGA----KKMLALGITGpeghelcRPEA 224
Cdd:PRK09357 142 -EAGV-----VAFSDDGIPVQDARlMRRALEYAKALDlLIAQ-HCEDPSLTEGGVmnegEVSARLGLPG-------IPAV 207
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958791289 225 VEAEATLRAITIASAVNCPLYIVHVMSKSAAKVIADAKREGKVVYGE--PiaaglgtdgtqywnkewrhaaHHV------ 296
Cdd:PRK09357 208 AEEVMIARDVLLAEATGARVHICHVSTAGSVELIRWAKALGIKVTAEvtP---------------------HHLlltded 266
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958791289 297 ---------MGPPLRpDPSTPGFLMNLLANGDLTTTGSD---------NCtfntcqkalgkdDFTKIPNGVNGVEDRMSV 358
Cdd:PRK09357 267 lltydpnykVNPPLR-TEEDREALIEGLKDGTIDAIATDhaphareekEC------------EFEAAPFGITGLETALSL 333
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958791289 359 IWEKGVHSGKMDENRFVAVTSTNAAKIFNLypKKGRIAVGSDADIVIWDPEATRTISAKTHHQAVNFNIFEGMVCHGVPL 438
Cdd:PRK09357 334 LYTTLVKTGLLDLEQLLEKMTINPARILGL--PAGPLAEGEPADLVIFDPEAEWTVDGEDFASKGKNTPFIGMKLKGKVV 411
|
490
....*....|..
gi 1958791289 439 VTISRGRVVYEA 450
Cdd:PRK09357 412 YTIVDGKIVYQD 423
|
|
| PRK08044 |
PRK08044 |
allantoinase AllB; |
7-464 |
2.97e-39 |
|
allantoinase AllB;
Pssm-ID: 169193 [Multi-domain] Cd Length: 449 Bit Score: 148.47 E-value: 2.97e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958791289 7 LLIRGGRVVNDDFSQVADVLVEDGVVRALGRDLlppgdtSRGLRILDAAGKLVLPGGIDTHTHMQFPfmGSQSVDDFHQG 86
Cdd:PRK08044 5 LIIKNGTVILENEARVVDIAVKGGKIAAIGQDL------GDAKEVMDASGLVVSPGMVDAHTHISEP--GRSHWEGYETG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958791289 87 TKAALAGGTTMIIDFAIPQKGSSLIEA-FETWRNWADPKVCCDY-SLHVAVTWWSDKVKEemktlAQDKGVNSFKMFMAY 164
Cdd:PRK08044 77 TRAAAKGGITTMIEMPLNQLPATVDRAsIELKFDAAKGKLTIDAaQLGGLVSYNLDRLHE-----LDEVGVVGFKCFVAT 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958791289 165 -------KDLYMVQDQQMYAAFSQCKEIGAIAQVHAENG---DLIAEGAKKMlalGITGPEGHELCRPEAVEAEATLRAI 234
Cdd:PRK08044 152 cgdrgidNDFRDVNDWQFYKGAQKLGELGQPVLVHCENAlicDELGEEAKRE---GRVTAHDYVASRPVFTEVEAIRRVL 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958791289 235 TIASAVNCPLYIVHVMSKSAAKVIADAKREGKVVYGEPIAAGLGTDGTQYwnKEWRHAAHhvMGPPLRpDPSTPGFLMNL 314
Cdd:PRK08044 229 YLAKVAGCRLHVCHISSPEGVEEVTRARQEGQDVTCESCPHYFVLDTDQF--EEIGTLAK--CSPPIR-DLENQKGMWEK 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958791289 315 LANGDLTTTGSDNctfNTCQKALGKDDFTKIPNGVNGVEDRMSVIWEKGVHSGKMDENRFVAVTSTNAAKIFNLyPKKGR 394
Cdd:PRK08044 304 LFNGEIDCLVSDH---SPCPPEMKAGNIMEAWGGIAGLQNCMDVMFDEAVQKRGMSLPMFGKLMATNAADIFGL-QQKGR 379
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1958791289 395 IAVGSDADIVIWDPEATRTISAKTHHQAVNFNIFEGMVCHGVPLVTISRGRVVY--EAGVfdVTAGHGKFIP 464
Cdd:PRK08044 380 IAPGKDADFVFIQPNSSYVLKNEDLEYRHKVSPYVGRTIGARITKTILRGDVIYdiEQGF--PVAPKGQFIL 449
|
|
| DHOase_IIb |
cd01318 |
Dihydroorotase (DHOase), subgroup IIb; DHOases catalyze the reversible interconversion of ... |
56-444 |
1.16e-38 |
|
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: 144.78 E-value: 1.16e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958791289 56 GKLVLPGGIDTHTHMQFPfmGSQSVDDFHQGTKAALAGGTTMIIDFAIPQKGSSLIEAFETWRNWADPKVCCDYSLHVAV 135
Cdd:cd01318 1 GLLILPGVIDIHVHFREP--GLTYKEDFVSGSRAAAAGGVTTVMDMPNTKPPTTTAEALYEKLRLAAAKSVVDYGLYFGV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958791289 136 TwwSDKVKEEMKTLaqdkGVNSFKMFMA--YKDLyMVQDQQMYAAFSQCKEIGAiaqVHAENGDLIAEGAKKMLALGItg 213
Cdd:cd01318 79 T--GSEDLEELDKA----PPAGYKIFMGdsTGDL-LDDEETLERIFAEGSVLVT---FHAEDEDRLRENRKELKGESA-- 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958791289 214 pegHELCRPEAVEAEATLRAITIASAVNCPLYIVHVMSKSAAKVIADAKREGKV-------VYGEPIAAGLGTdgtqyWN 286
Cdd:cd01318 147 ---HPRIRDAEAAAVATARALKLARRHGARLHICHVSTPEELKLIKKAKPGVTVevtphhlFLDVEDYDRLGT-----LG 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958791289 287 KewrhaahhvMGPPLRPDPSTPGfLMNLLANGDLTTTGSDNCTFNTCQKALGkddFTKIPNGVNGVEDRMSVIWEKgVHS 366
Cdd:cd01318 219 K---------VNPPLRSREDRKA-LLQALADGRIDVIASDHAPHTLEEKRKG---YPAAPSGIPGVETALPLMLTL-VNK 284
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1958791289 367 GKMDENRFVAVTSTNAAKIFNLyPKKGRIAVGSDADIVIWDPEATRTISAKTHHQAVNFNIFEGMVCHGVPLVTISRG 444
Cdd:cd01318 285 GILSLSRVVRLTSHNPARIFGI-KNKGRIAEGYDADLTVVDLKEERTIRAEEFHSKAGWTPFEGFEVTGFPVMTIVRG 361
|
|
| DHOase_IIa |
cd01317 |
Dihydroorotase (DHOase), subgroup IIa; DHOases catalyze the reversible interconversion of ... |
48-440 |
3.24e-35 |
|
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: 135.44 E-value: 3.24e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958791289 48 GLRILDAAGKLVLPGGIDTHTHMQFPfmGSQSVDDFHQGTKAALAGGTTMII-----DFAIPQKgssliEAFETWRNWAD 122
Cdd:cd01317 1 DAEVIDAEGKILAPGLVDLHVHLREP--GFEYKETLESGAKAAAAGGFTTVVcmpntNPVIDNP-----AVVELLKNRAK 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958791289 123 PkvccdySLHVAVTWWS-----DKVKE--EMKTLAqDKGVNSFKmfmayKDLYMVQDQQ-MYAAFSQCKEIGAIAQVHAE 194
Cdd:cd01317 74 D------VGIVRVLPIGaltkgLKGEEltEIGELL-EAGAVGFS-----DDGKPIQDAElLRRALEYAAMLDLPIIVHPE 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958791289 195 NGDLIAEGA----KKMLALGITGpeghelcRPEAVEAEATLRAITIASAVNCPLYIVHVMSKSAAKVIADAKREGkvvyg 270
Cdd:cd01317 142 DPSLAGGGVmnegKVASRLGLPG-------IPPEAETIMVARDLELAEATGARVHFQHLSTARSLELIRKAKAKG----- 209
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958791289 271 EPIAAG------------LGTDGTqywnkewrhaAHHVMgPPLRpDPSTPGFLMNLLANGDLTTTGSDNCTFNTCQKALG 338
Cdd:cd01317 210 LPVTAEvtphhlllddeaLESYDT----------NAKVN-PPLR-SEEDREALIEALKDGTIDAIASDHAPHTDEEKDLP 277
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958791289 339 KDDftkIPNGVNGVEDRMSVIWEKGVHSGKMDENRFVAVTSTNAAKIFNLYPkkGRIAVGSDADIVIWDPEATRTISAKT 418
Cdd:cd01317 278 FAE---APPGIIGLETALPLLWTLLVKGGLLTLPDLIRALSTNPAKILGLPP--GRLEVGAPADLVLFDPDAEWIVDEET 352
|
410 420
....*....|....*....|..
gi 1958791289 419 HHQAVNFNIFEGMVCHGVPLVT 440
Cdd:cd01317 353 FRSKSKNTPFDGQKLKGRVLAT 374
|
|
| PLN02795 |
PLN02795 |
allantoinase |
12-451 |
8.82e-35 |
|
allantoinase
Pssm-ID: 178392 [Multi-domain] Cd Length: 505 Bit Score: 136.83 E-value: 8.82e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958791289 12 GRVVNDDFSQVADVLVEDGVVRALGRDLLPPGDTSRGlRILDAAGKLVLPGGIDTHTHMQFPfmGSQSVDDFHQGTKAAL 91
Cdd:PLN02795 51 KRVVTPAGVIPGAVEVEGGRIVSVTKEEEAPKSQKKP-HVLDYGNAVVMPGLIDVHVHLNEP--GRTEWEGFPTGTKAAA 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958791289 92 AGGTTMIIDF---AIPQKGSSliEAFETWRNWADPKvccdysLHVAVTWWSDKVKE------EMKTLAqDKGVNSFKMFM 162
Cdd:PLN02795 128 AGGITTLVDMplnSFPSTTSV--ETLELKIEAAKGK------LYVDVGFWGGLVPEnahnasVLEELL-DAGALGLKSFM 198
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958791289 163 ---AYKDLYMVQDQQMYAAFSQCKEIGAIAQVHAENGDLIAEGAkkMLALGITGPEGHELCRPEAVEAEATLRAITIAS- 238
Cdd:PLN02795 199 cpsGINDFPMTTATHIKAALPVLAKYGRPLLVHAEVVSPVESDS--RLDADPRSYSTYLKSRPPSWEQEAIRQLLEVAKd 276
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958791289 239 ------AVNCPLYIVHVM-SKSAAKVIADAKREGKVVYGEPIAAGLGTDGTQYWNKEWRHAAhhvmGPPLRpDPSTPGFL 311
Cdd:PLN02795 277 trpggvAEGAHVHIVHLSdAESSLELIKEAKAKGDSVTVETCPHYLAFSAEEIPDGDTRYKC----APPIR-DAANRELL 351
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958791289 312 MNLLANGDLTTTGSDNCTFNTCQKALGKDDFTKIPNGVNGVEDRMSVIWEKGVHSGkMDENRFVAVTSTNAAKIFNLyPK 391
Cdd:PLN02795 352 WKALLDGDIDMLSSDHSPSPPDLKLLEEGNFLRAWGGISSLQFVLPATWTAGRAYG-LTLEQLARWWSERPAKLAGL-DS 429
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1958791289 392 KGRIAVGSDADIVIWDPEATRTI--SAKTHHQAVNFNIFEGMVCHGVPLVTISRGRVVYEAG 451
Cdd:PLN02795 430 KGAIAPGKDADIVVWDPEAEFVLdeSYPIYHKHKSLSPYLGTKLSGKVIATFVRGNLVFLEG 491
|
|
| PRK09060 |
PRK09060 |
dihydroorotase; Validated |
7-447 |
5.82e-34 |
|
dihydroorotase; Validated
Pssm-ID: 181632 [Multi-domain] Cd Length: 444 Bit Score: 133.51 E-value: 5.82e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958791289 7 LLIRGGRVVNDDFSQVADVLVEDGVVRALGRdllpPGDTSRGlRILDAAGKLVLPGGIDTHTHMQFPfmGSQSVDDFHQG 86
Cdd:PRK09060 7 LILKGGTVVNPDGEGRADIGIRDGRIAAIGD----LSGASAG-EVIDCRGLHVLPGVIDSQVHFREP--GLEHKEDLETG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958791289 87 TKAALAGGTTMIidFAIPQKGSSLI--EAFETWRNWADPKVCCDYSLHVAVTwwSDKVkEEMKTLAQDKGVNSFKMFM-- 162
Cdd:PRK09060 80 SRAAVLGGVTAV--FEMPNTNPLTTtaEALADKLARARHRMHCDFAFYVGGT--RDNA-DELAELERLPGCAGIKVFMgs 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958791289 163 AYKDLyMVQDQQMYAAFsqCKEIGAIAQVHAENGDLIAEgaKKMLAlgITG-PEGHELCRPEAVEAEATLRAITIASAVN 241
Cdd:PRK09060 155 STGDL-LVEDDEGLRRI--LRNGRRRAAFHSEDEYRLRE--RKGLR--VEGdPSSHPVWRDEEAALLATRRLVRLARETG 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958791289 242 CPLYIVHVMSKSAAKVIADAKREGKV--------VYGEPIAAGLGTdgtqywnkewrhaaHHVMGPPLRpDPSTPGFLMN 313
Cdd:PRK09060 228 RRIHVLHVSTAEEIDFLADHKDVATVevtphhltLAAPECYERLGT--------------LAQMNPPIR-DARHRDGLWR 292
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958791289 314 LLANGDLTTTGSDNCTFNTCQKALgkdDFTKIPNGVNGVEDRMSVIWEKgVHSGKMDENRFVAVTSTNAAKIFNLyPKKG 393
Cdd:PRK09060 293 GVRQGVVDVLGSDHAPHTLEEKAK---PYPASPSGMTGVQTLVPIMLDH-VNAGRLSLERFVDLTSAGPARIFGI-AGKG 367
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....
gi 1958791289 394 RIAVGSDADIVIWDPEATRTISAKTHHQAVNFNIFEGMVCHGVPLVTISRGRVV 447
Cdd:PRK09060 368 RIAVGYDADFTIVDLKRRETITNEWIASRCGWTPYDGKEVTGWPVGTIVRGQRV 421
|
|
| PRK07575 |
PRK07575 |
dihydroorotase; Provisional |
3-461 |
3.44e-30 |
|
dihydroorotase; Provisional
Pssm-ID: 236055 [Multi-domain] Cd Length: 438 Bit Score: 122.48 E-value: 3.44e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958791289 3 PQERLLIRGGRVVNDDFS-QVADVLVEDGVVRALGRDLLPPGDTsrglRILDAAGKLVLPGGIDTHTHMQFPfmGSQSVD 81
Cdd:PRK07575 1 MMMSLLIRNARILLPSGElLLGDVLVEDGKIVAIAPEISATAVD----TVIDAEGLTLLPGVIDPQVHFREP--GLEHKE 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958791289 82 DFHQGTKAALAGGTTMIIDFAIPQKGSSLIEAFETWRNWADPKVCCDYSLHVAVTwwSDKVKEemktLAQDKGVNSFKMF 161
Cdd:PRK07575 75 DLFTASRACAKGGVTSFLEMPNTKPLTTTQAALDDKLARAAEKCVVNYGFFIGAT--PDNLPE----LLTANPTCGIKIF 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958791289 162 M--AYKDLYMVQDQQMYAAFSQCKEIgaIAqVHAENGDLIAEgAKKMLAlGITGPEGHELCRPEAVEAEATLRAITIASA 239
Cdd:PRK07575 149 MgsSHGPLLVDEEAALERIFAEGTRL--IA-VHAEDQARIRA-RRAEFA-GISDPADHSQIQDEEAALLATRLALKLSKK 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958791289 240 VNCPLYIVHVMSKSAAKVIADAKREGKVVYGEPIAAGLGTDGTQywnkewRHAAHHVMGPPLRpDPSTPGFLMNLLANGD 319
Cdd:PRK07575 224 YQRRLHILHLSTAIEAELLRQDKPSWVTAEVTPQHLLLNTDAYE------RIGTLAQMNPPLR-SPEDNEALWQALRDGV 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958791289 320 LTTTGSDNCTFNTCQKALGkddFTKIPNGVNGVEDRMSVIWEKgVHSGKMDENRFVAVTSTNAAKIFNLyPKKGRIAVGS 399
Cdd:PRK07575 297 IDFIATDHAPHTLEEKAQP---YPNSPSGMPGVETSLPLMLTA-AMRGKCTVAQVVRWMSTAVARAYGI-PNKGRIAPGY 371
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1958791289 400 DADIVIWDPEATRTISAKTHHQAVNFNIFEGMVCHGVPLVTISRGRVVYEAGVFDvTAGHGK 461
Cdd:PRK07575 372 DADLVLVDLNTYRPVRREELLTKCGWSPFEGWNLTGWPVTTIVGGQIVFDRGQVN-TEVRGQ 432
|
|
| PRK04250 |
PRK04250 |
dihydroorotase; Provisional |
12-451 |
1.21e-24 |
|
dihydroorotase; Provisional
Pssm-ID: 235265 [Multi-domain] Cd Length: 398 Bit Score: 105.62 E-value: 1.21e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958791289 12 GRVVNddfsqvADVLVEDGVVRALGRDLLppgdtsRGLRILDAAGKLVLPGGIDTHTHMQfpfmgsqsvdDFHQ------ 85
Cdd:PRK04250 10 GRIVE------GGIGIENGRISKISLRDL------KGKEVIKVKGGIILPGLIDVHVHLR----------DFEEsyketi 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958791289 86 --GTKAALAGGTTMIIDfaIPQKGSSLI--EAFETWRNWADPKVCCDYSLHVAVTWWSDKVKEEMKTLaqdkgvnsFKMF 161
Cdd:PRK04250 68 esGTKAALHGGITLVFD--MPNTKPPIMdeKTYEKRMRIAEKKSYADYALNFLIAGNCEKAEEIKADF--------YKIF 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958791289 162 M--AYKDLYMVQDQQMYaafsqcKEIGAIAQVHAENGDLIAEGakkmlalgitgPEghelcRPEAVEAEATLRAITIASA 239
Cdd:PRK04250 138 MgaSTGGIFSENFEVDY------ACAPGIVSVHAEDPELIREF-----------PE-----RPPEAEVVAIERALEAGKK 195
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958791289 240 VNCPLYIVHVMSKSAAKVIadAKREGKVVYGEPIAAGLgtdgtQYWNKEWRHAAHHVMGPPLRpDPSTPGFLMNLLANGD 319
Cdd:PRK04250 196 LKKPLHICHISTKDGLKLI--LKSNLPWVSFEVTPHHL-----FLTRKDYERNPLLKVYPPLR-SEEDRKALWENFSKIP 267
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958791289 320 LttTGSDNCTFNTCQKALGKddftkipNGVNGVEDRMSVIWEkGVHSGKMDENRFVAVTSTNAAKIFNLypkKGR-IAVG 398
Cdd:PRK04250 268 I--IASDHAPHTLEDKEAGA-------AGIPGLETEVPLLLD-AANKGMISLFDIVEKMHDNPARIFGI---KNYgIEEG 334
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|...
gi 1958791289 399 SDADIVIWDPEATRTISAKTHHQAVNFNIFEGMVCHGVPLVTISRGRVVYEAG 451
Cdd:PRK04250 335 NYANFAVFDMKKEWTIKAEELYTKAGWTPYEGFKLKGKVIMTILRGEVVMEDD 387
|
|
| Amidohydro_1 |
pfam01979 |
Amidohydrolase family; This family of enzymes are a a large metal dependent hydrolase ... |
58-447 |
3.53e-23 |
|
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: 100.27 E-value: 3.53e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958791289 58 LVLPGGIDTHTHMQFPFM------GSQSVDDFHQGTKAALAGGTTMIIDFAI--PQKGSSLIEAFEtwRNWADPKVC--- 126
Cdd:pfam01979 1 IVLPGLIDAHVHLEMGLLrgipvpPEFAYEALRLGITTMLKSGTTTVLDMGAttSTGIEALLEAAE--ELPLGLRFLgpg 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958791289 127 ----CDYSLHVAVTWWsDKVKEEMKTLAQDKGVNSFKMFMAYKDlYMVQDQQMYAAFSQCKEIGAIAQVHAENGDLIAEG 202
Cdd:pfam01979 79 csldTDGELEGRKALR-EKLKAGAEFIKGMADGVVFVGLAPHGA-PTFSDDELKAALEEAKKYGLPVAIHALETKGEVED 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958791289 203 AKKmlALGITGPEGHELcrpEAVEAEATLRAITIASAVNcplyiVHVMSKSAAKVIADAKREGkvVYGEPIAAGLGTDGT 282
Cdd:pfam01979 157 AIA--AFGGGIEHGTHL---EVAESGGLLDIIKLILAHG-----VHLSPTEANLLAEHLKGAG--VAHCPFSNSKLRSGR 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958791289 283 qywnkewrhaahhvmgPPLRPdpstpgflmnLLANGDLTTTGSDNCtfntcqkaLGKDDFTKIPNGVNGVEDRmsviwek 362
Cdd:pfam01979 225 ----------------IALRK----------ALEDGVKVGLGTDGA--------GSGNSLNMLEELRLALELQ------- 263
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958791289 363 GVHSGKMDENRFVAVTSTNAAKIFNLYPKKGRIAVGSDADIVIWDPEATrtisakthhqavnfNIFEGMVCHGVPLVTIS 442
Cdd:pfam01979 264 FDPEGGLSPLEALRMATINPAKALGLDDKVGSIEVGKDADLVVVDLDPL--------------AAFFGLKPDGNVKKVIV 329
|
....*
gi 1958791289 443 RGRVV 447
Cdd:pfam01979 330 KGKIV 334
|
|
| PRK01211 |
PRK01211 |
dihydroorotase; Provisional |
16-465 |
1.01e-21 |
|
dihydroorotase; Provisional
Pssm-ID: 179247 [Multi-domain] Cd Length: 409 Bit Score: 97.24 E-value: 1.01e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958791289 16 NDDFSQVAdVLVEDGVVRALGRDLLPPGDTSrglriLDAAgklVLPGGIDTHTHMQFPfmGSQSVDDFHQGTKAALAGGT 95
Cdd:PRK01211 10 KGKFDYLE-IEVEDGKIKSIKKDAGNIGKKE-----LKGA---ILPAATDIHVHFRTP--GETEKEDFSTGTLSAIFGGT 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958791289 96 TMIIDFA---IPQKGsslIEAFETWRNWADPKVCCDYSLHVAVTWWSDKVKEEMKTlaqdkgvnSFKMFMA---YKDLYM 169
Cdd:PRK01211 79 TFIMDMPnnnIPIKD---YNAFSDKLGRVAPKAYVDFSLYSMETGNNALILDERSI--------GLKVYMGgttNTNGTD 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958791289 170 VQDQQMyaafSQCKEIGAIAQVHAENGDLIAEGAKKMLALgitgpEGHELCRPEAVEAEAT--LRAITIASAVncplyIV 247
Cdd:PRK01211 148 IEGGEI----KKINEANIPVFFHAELSECLRKHQFESKNL-----RDHDLARPIECEIKAVkyVKNLDLKTKI-----IA 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958791289 248 HVmskSAAKVIADAKREgkvvygepiaaglGTDGTQYWNKEWRHAAHHVMGPPLRpDPSTPGFLMNLLANGDLTTTGSDN 327
Cdd:PRK01211 214 HV---SSIDVIGRFLRE-------------VTPHHLLLNDDMPLGSYGKVNPPLR-DRWTQERLLEEYISGRFDILSSDH 276
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958791289 328 CTFNTCQKAlgkdDFTKIPNGVNGVEDRMSVIWEKgVHSGKMDENRFVAVTSTNAAKIFNLypKKGRIAVGSDADIVIWD 407
Cdd:PRK01211 277 APHTEEDKQ----EFEYAKSGIIGVETRVPLFLAL-VKKKILPLDVLYKTAIERPASLFGI--KKGKIEEGYDADFMAFD 349
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1958791289 408 PEATRTISAKTHHQAVNFNIFEGMVCHgVPLVTISRGRVV---YEagvfDVTAGHGKFIPR 465
Cdd:PRK01211 350 FTNIKKINDKRLHSKCPVSPFNGFDAI-FPSHVIMRGEVVidnYE----LISERTGKFVPK 405
|
|
| PRK09236 |
PRK09236 |
dihydroorotase; Reviewed |
6-459 |
2.88e-15 |
|
dihydroorotase; Reviewed
Pssm-ID: 181716 Cd Length: 444 Bit Score: 77.99 E-value: 2.88e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958791289 6 RLLIRGGRVVNDDFSQVADVLVEDGVVRALGRDLlppgDTSRGLRILDAAGKLVLPGGIDTHTHMQFPfmGSQSVDDFHQ 85
Cdd:PRK09236 3 RILIKNARIVNEGKIFEGDVLIENGRIAKIASSI----SAKSADTVIDAAGRYLLPGMIDDQVHFREP--GLTHKGDIAS 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958791289 86 GTKAALAGGTTMIIDF--AIPQkgSSLIEAFETWRNWADPKVCCDYSLHVAVTwwSDKVkEEMKTLaqDK----GVnsfK 159
Cdd:PRK09236 77 ESRAAVAGGITSFMEMpnTNPP--TTTLEALEAKYQIAAQRSLANYSFYFGAT--NDNL-DEIKRL--DPkrvcGV---K 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958791289 160 MFMAYKDLYM-VQDQQMYAA-FSQCKEIgaIAqVHAENGDLIAEGAKKMLAL---GITgPEGHELCRPEAVEAEATLRAI 234
Cdd:PRK09236 147 VFMGASTGNMlVDNPETLERiFRDAPTL--IA-THCEDTPTIKANLAKYKEKygdDIP-AEMHPLIRSAEACYKSSSLAV 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958791289 235 TIASAVNCPLYIVHVmskSAAKVIA---DAKREGKVVYGEPIAAGLGTDGTQY--------WN-----KEWRHAahhvmg 298
Cdd:PRK09236 223 SLAKKHGTRLHVLHI---STAKELSlfeNGPLAEKRITAEVCVHHLWFDDSDYarlgnlikCNpaiktASDREA------ 293
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958791289 299 pplrpdpstpgfLMNLLANGDLTTTGSDNCTFNTCQKALGkddFTKIPNGVNGVEDRMSVIWEKgVHSGKMDENRFVAVT 378
Cdd:PRK09236 294 ------------LRQALADDRIDVIATDHAPHTWEEKQGP---YFQAPSGLPLVQHALPALLEL-VHEGKLSLEKVVEKT 357
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958791289 379 STNAAKIFNLyPKKGRIAVGSDADIVIWDPEATRTISAKTHHQAVNFNIFEGMVCHGVPLVTISRGRVVYEAG-VFDVTA 457
Cdd:PRK09236 358 SHAPAILFDI-KERGFIREGYWADLVLVDLNSPWTVTKENILYKCGWSPFEGRTFRSRVATTFVNGQLVYHNGqLVESCR 436
|
..
gi 1958791289 458 GH 459
Cdd:PRK09236 437 GQ 438
|
|
| HutI |
COG1228 |
Imidazolonepropionase or related amidohydrolase [Secondary metabolites biosynthesis, transport ... |
2-432 |
3.52e-15 |
|
Imidazolonepropionase or related amidohydrolase [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 440841 [Multi-domain] Cd Length: 386 Bit Score: 77.31 E-value: 3.52e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958791289 2 APQERLLIRGGRVVNDDFSQV---ADVLVEDGVVRALGR--DLLPPGDTsrglRILDAAGKLVLPGGIDTHTHMQFPFMG 76
Cdd:COG1228 5 AQAGTLLITNATLVDGTGGGVienGTVLVEDGKIAAVGPaaDLAVPAGA----EVIDATGKTVLPGLIDAHTHLGLGGGR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958791289 77 SQS----------VDDFHQGTK---AALAGGTTMIIDfaipQKGSSL-----IEAFETWRNWADPKVCCDYSLHV---AV 135
Cdd:COG1228 81 AVEfeagggitptVDLVNPADKrlrRALAAGVTTVRD----LPGGPLglrdaIIAGESKLLPGPRVLAAGPALSLtggAH 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958791289 136 TWWSDKVKEEMKTLAQDkGVNSFKMFMAYKDLYMVQDqQMYAAFSQCKEIGAIAQVHAENgdliAEGAKKMLALGITGpe 215
Cdd:COG1228 157 ARGPEEARAALRELLAE-GADYIKVFAEGGAPDFSLE-ELRAILEAAHALGLPVAAHAHQ----ADDIRLAVEAGVDS-- 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958791289 216 ghelcrpeaveaeatlraitiasavncplyIVHVMSKSAAkVIADAKREGKVVYGePiAAGLGTDGTQYWNKEWRHAAHH 295
Cdd:COG1228 229 ------------------------------IEHGTYLDDE-VADLLAEAGTVVLV-P-TLSLFLALLEGAAAPVAAKARK 275
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958791289 296 VMGPPLRPdpstpgfLMNLLANGDLTTTGSDNctfntcqkalgkddftkipNGVNGVEDRMSVIWEKGVHSGkMDENR-F 374
Cdd:COG1228 276 VREAALAN-------ARRLHDAGVPVALGTDA-------------------GVGVPPGRSLHRELALAVEAG-LTPEEaL 328
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*...
gi 1958791289 375 VAVTStNAAKIFNLYPKKGRIAVGSDADIVIWDPEATRTISAkthHQAVNFNIFEGMV 432
Cdd:COG1228 329 RAATI-NAAKALGLDDDVGSLEPGKLADLVLLDGDPLEDIAY---LEDVRAVMKDGRV 382
|
|
| D-aminoacylase |
cd01297 |
D-aminoacylases (N-acyl-D-Amino acid amidohydrolases) catalyze the hydrolysis of ... |
7-458 |
2.57e-14 |
|
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: 74.64 E-value: 2.57e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958791289 7 LLIRGGRVV----NDDFSqvADVLVEDGVVRALGRDLLPPGDtsrglRILDAAGKLVLPGGIDTHTHMQFPFMGSQSVdd 82
Cdd:cd01297 2 LVIRNGTVVdgtgAPPFT--ADVGIRDGRIAAIGPILSTSAR-----EVIDAAGLVVAPGFIDVHTHYDGQVFWDPDL-- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958791289 83 fhqgTKAALAGGTTMII----------DFAIPQKGSSLIEAF--------ETWRNWAD-----------PKVCCDY---S 130
Cdd:cd01297 73 ----RPSSRQGVTTVVLgncgvspapaNPDDLARLIMLMEGLvalgeglpWGWATFAEyldalearppaVNVAALVghaA 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958791289 131 LHVAVTWWSDKVK-----EEMKTLAqDKGVNS----FKMFMAYKDLYMVQDQQMYAAFSQCKEIGAIAQVHAEN-GDLIA 200
Cdd:cd01297 149 LRRAVMGLDAREAteeelAKMRELL-REALEAgalgISTGLAYAPRLYAGTAELVALARVAARYGGVYQTHVRYeGDSIL 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958791289 201 EGAKKMLALGitgpeghelcrpeaveaEATLRAITIASAVNCPLYIVHVMSKSAAkVIADAKREGKVVYGE--PIAAGLG 278
Cdd:cd01297 228 EALDELLRLG-----------------RETGRPVHISHLKSAGAPNWGKIDRLLA-LIEAARAEGLQVTADvyPYGAGSE 289
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958791289 279 TDgtqywnKEWRHAAHHVM-----GPPLRPDPSTpgflmnllangdltttgsdNCTFNtcqKALGKddftkipngvnGVE 353
Cdd:cd01297 290 DD------VRRIMAHPVVMggsdgGALGKPHPRS-------------------YGDFT---RVLGH-----------YVR 330
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958791289 354 DRMSVIWEKGVHsgKMdenrfvavtSTNAAKIFNLYpKKGRIAVGSDADIVIWDPEatrTISAKTHHQAVNFNifegmvC 433
Cdd:cd01297 331 ERKLLSLEEAVR--KM---------TGLPARVFGLA-DRGRIAPGYRADIVVFDPD---TLADRATFTRPNQP------A 389
|
490 500
....*....|....*....|....*.
gi 1958791289 434 HGVPLVTISrGRVVYEAGVF-DVTAG 458
Cdd:cd01297 390 EGIEAVLVN-GVPVVRDGAFtGARPG 414
|
|
| PRK09059 |
PRK09059 |
dihydroorotase; Validated |
7-450 |
9.76e-12 |
|
dihydroorotase; Validated
Pssm-ID: 181631 [Multi-domain] Cd Length: 429 Bit Score: 66.98 E-value: 9.76e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958791289 7 LLIRGGRVVND--DFSQVADVLVEDGVVRALGRDLLPPGdTSRGLRILDAAGKLVLPGGIDTHTHMQFPfmGSQSVDDFH 84
Cdd:PRK09059 5 ILLANARIIDPsrGLDEIGTVLIEDGVIVAAGKGAGNQG-APEGAEIVDCAGKAVAPGLVDARVFVGEP--GAEHRETIA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958791289 85 QGTKAALAGGTTMII-----DFAIPQkgSSLIE-AFETWRNWADPKVccdyslHVAVTWWSDKVKEEMKT--LAQDKGVN 156
Cdd:PRK09059 82 SASRAAAAGGVTSIImmpdtDPVIDD--VALVEfVKRTARDTAIVNI------HPAAAITKGLAGEEMTEfgLLRAAGAV 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958791289 157 SFkmfmaYKDLYMVQDQQ-MYAAFSQCKEIGAIAQVHAENGDLIAEGA--KKMLA--LGITG-PeghelCRPEAVEAEAT 230
Cdd:PRK09059 154 AF-----TDGRRSVANTQvMRRALTYARDFDAVIVHETRDPDLGGNGVmnEGLFAswLGLSGiP-----REAEVIPLERD 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958791289 231 LR--AITI----ASAVNCPLyivhvmsksAAKVIADAKREgkvvyGEPIAAGLGTDGTQYwNK----EWRhaAHHVMGPP 300
Cdd:PRK09059 224 LRlaALTRgryhAAQISCAE---------SAEALRRAKDR-----GLKVTAGVSINHLSL-NEndigEYR--TFFKLSPP 286
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958791289 301 LRPDPSTPGfLMNLLANGDLTTTGSDNCTFNTCQKALgkdDFTKIPNGVNGVEDRMSVIWeKGVHSGKMDENRFVAVTST 380
Cdd:PRK09059 287 LRTEDDRVA-MVEAVASGTIDIIVSSHDPQDVDTKRL---PFSEAAAGAIGLETLLAAAL-RLYHNGEVPLLRLIEALST 361
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958791289 381 NAAKIFNLypKKGRIAVGSDADIVIWDPEATRTISAKTHHQAVNFNIFEGMVCHGVPLVTISRGRVVYEA 450
Cdd:PRK09059 362 RPAEIFGL--PAGTLKPGAPADIIVIDLDEPWVVDPEDLKSRSKNTPFEEARFQGRVVRTIVAGKTVYEL 429
|
|
| PRK09237 |
PRK09237 |
amidohydrolase/deacetylase family metallohydrolase; |
7-69 |
2.00e-11 |
|
amidohydrolase/deacetylase family metallohydrolase;
Pssm-ID: 236423 [Multi-domain] Cd Length: 380 Bit Score: 65.64 E-value: 2.00e-11
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1958791289 7 LLIRGGRVVN--DDFSQVADVLVEDGVVRALGRDLlppgDTSRGLRILDAAGKLVLPGGIDTHTH 69
Cdd:PRK09237 1 LLLRGGRVIDpaNGIDGVIDIAIEDGKIAAVAGDI----DGSQAKKVIDLSGLYVSPGWIDLHVH 61
|
|
| SsnA |
COG0402 |
Cytosine/adenosine deaminase or related metal-dependent hydrolase [Nucleotide transport and ... |
6-115 |
3.76e-11 |
|
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: 64.85 E-value: 3.76e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958791289 6 RLLIRGGRVVNDDFSQV----ADVLVEDGVVRALGRDLlPPGDTSRGLRILDAAGKLVLPGGIDTHTHM----------- 70
Cdd:COG0402 1 DLLIRGAWVLTMDPAGGvledGAVLVEDGRIAAVGPGA-ELPARYPAAEVIDAGGKLVLPGLVNTHTHLpqtllrgladd 79
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1958791289 71 ----------QFPFMGSQSVDDFHQGTKAA----LAGGTTMIIDFAIPQKGSS--LIEAFE 115
Cdd:COG0402 80 lplldwleeyIWPLEARLDPEDVYAGALLAlaemLRSGTTTVADFYYVHPESAdaLAEAAA 140
|
|
| CAD_DHOase |
cd01316 |
The eukaryotic CAD protein is a trifunctional enzyme of carbamoylphosphate ... |
60-460 |
4.34e-11 |
|
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: 64.39 E-value: 4.34e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958791289 60 LPGGIDTHTHMQFPfmGSQSVDDFHQGTKAALAGGTTMIIdfAIPQKGSSLI--EAFETWRNWADPKVCCDYSLHVAVTw 137
Cdd:cd01316 5 LPGLIDVHVHLREP--GATHKEDFASGTKAALAGGFTMVR--AMPNTNPSIVdvASLKLVQSLAQAKARCDYAFSIGAT- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958791289 138 wsdkvKEEMKTLAQ--DKGVNS----FKMFMAYKDLYMVQDQQMYAAFSQCKEIGAiaqvHAENGDLIAegakkmlalgi 211
Cdd:cd01316 80 -----STNAATVGElaSEAVGLkfylNETFSTLILDKITAWASHFNAWPSTKPIVT----HAKSQTLAA----------- 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958791289 212 tgpeghelcrpeaveaeatlrAITIASAVNCPLYIVHVMSKSAAKVIADAKREGKVVYGE--PIAAGLGTDGTQYWNKEW 289
Cdd:cd01316 140 ---------------------VLLLASLHNRSIHICHVSSKEEINLIRLAKARGLKVTCEvsPHHLFLSQDDLPRGQYEV 198
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958791289 290 RhaahhvmgpPLRPDPSTPGFLMNLLANGDLTTTGSdnctfntCQKALGKDDFTKIPNGVNGVEDRMSVIWeKGVHSGKM 369
Cdd:cd01316 199 R---------PFLPTREDQEALWENLDYIDCFATDH-------APHTLAEKTGNKPPPGFPGVETSLPLLL-TAVHEGRL 261
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958791289 370 DENRFVAVTSTNAAKIFNLYPKkgriavgSDADIVIwDPEATRTISAKTHHQAVNFNIFEGMVCHGVPLVTISRGRVVYE 449
Cdd:cd01316 262 TIEDIVDRLHTNPKRIFNLPPQ-------SDTYVEV-DLDEEWTIPKNPLQSKKGWTPFEGKKVKGKVQRVVLRGETAFI 333
|
410
....*....|.
gi 1958791289 450 AGVFDVTAGHG 460
Cdd:cd01316 334 DGEIVAPPGFG 344
|
|
| PRK07369 |
PRK07369 |
dihydroorotase; Provisional |
4-420 |
5.29e-11 |
|
dihydroorotase; Provisional
Pssm-ID: 236002 [Multi-domain] Cd Length: 418 Bit Score: 64.62 E-value: 5.29e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958791289 4 QERLLIRGGRVVnDDFSQ---VADVLVEDGVVRALGRDLLP-PGDTsrglRILDAAGKLVLPGGIDTHTHMQFPfmGSQS 79
Cdd:PRK07369 1 MSNELLQQVRVL-DPVSNtdrIADVLIEDGKIQAIEPHIDPiPPDT----QIIDASGLILGPGLVDLYSHSGEP--GFEE 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958791289 80 VDDFHQGTKAALAGGTT---MIIDFAIPQKGSSLIEAFETWRNWADPkvccdyslhVAVTWW---SDKVKEEMKT----L 149
Cdd:PRK07369 74 RETLASLAAAAAAGGFTrvaILPDTFPPLDNPATLARLQQQAQQIPP---------VQLHFWgalTLGGQGKQLTelaeL 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958791289 150 AQdKGVNSFKMFMAYKDLYMVQDQQMYA-------AFSQCKeigaiAQVHAeNGdLIAEGAKKmLALGITGpeghelcRP 222
Cdd:PRK07369 145 AA-AGVVGFTDGQPLENLALLRRLLEYLkplgkpvALWPCD-----RSLAG-NG-VMREGLLA-LRLGLPG-------DP 208
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958791289 223 EAVEAEATLRAITIASAVNCPlyiVHVMSKSAAK---VIADAKREGKvvygePIAAG-------LGTDGTQYWNKEWRha 292
Cdd:PRK07369 209 ASAETTALAALLELVAAIGTP---VHLMRISTARsveLIAQAKARGL-----PITASttwmhllLDTEALASYDPNLR-- 278
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958791289 293 ahhvMGPPLrPDPSTPGFLMNLLANGDLTTTGSDNCTFNTCQKALGkddFTKIPNGVNGVEDRMSVIWEKGVHSGKMDEN 372
Cdd:PRK07369 279 ----LDPPL-GNPSDRQALIEGVRTGVIDAIAIDHAPYTYEEKTVA---FAEAPPGAIGLELALPLLWQNLVETGELSAL 350
|
410 420 430 440
....*....|....*....|....*....|....*....|....*...
gi 1958791289 373 RFVAVTSTNAAKIFNLYPKkgRIAVGSDADIVIWDPEATRTISAKTHH 420
Cdd:PRK07369 351 QLWQALSTNPARCLGQEPP--SLAPGQPAELILFDPQKTWTVSAQTLH 396
|
|
| ATZ_TRZ_like |
cd01298 |
TRZ/ATZ family contains enzymes from the atrazine degradation pathway and related hydrolases. ... |
7-100 |
6.29e-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: 61.06 E-value: 6.29e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958791289 7 LLIRGGRVVNDDFSQV---ADVLVEDGVVRALGRDLLPPGDTsrGLRILDAAGKLVLPGGIDTHTHMQ------------ 71
Cdd:cd01298 1 ILIRNGTIVTTDPRRVledGDVLVEDGRIVAVGPALPLPAYP--ADEVIDAKGKVVMPGLVNTHTHLAmtllrgladdlp 78
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 1958791289 72 ---------FPFMGSQSVDDFHQGTKAALA----GGTTMIID 100
Cdd:cd01298 79 lmewlkdliWPLERLLTEEDVYLGALLALAemirSGTTTFAD 120
|
|
| pyrC |
PRK00369 |
dihydroorotase; Provisional |
56-457 |
5.51e-09 |
|
dihydroorotase; Provisional
Pssm-ID: 234738 [Multi-domain] Cd Length: 392 Bit Score: 58.23 E-value: 5.51e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958791289 56 GKLVLPGGIDTHTHMQfpfmGSQSV--DDFHQGTKAALAGGTTMIIDFAIPQKGSSLIEAFETWRNWADPKVCCDYSLHV 133
Cdd:PRK00369 42 GTLILPGAIDLHVHLR----GLKLSykEDVASGTSEAAYGGVTLVADMPNTIPPLNTPEAITEKLAELEYYSRVDYFVYS 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958791289 134 AVTwwsdKVKEEMKTLaqdkGVNSFKMFMAykdlymvqdqqmyaafsqckeigaiaqvhaengDLIAEGAKKMLA----L 209
Cdd:PRK00369 118 GVT----KDPEKVDKL----PIAGYKIFPE---------------------------------DLEREETFRVLLksrkL 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958791289 210 GITGPEGHELCRPEaveaEATLRAI--TIASavncpLYIVHvmskSAAKV-IADAKREGKVVygepIAAGLG--TDGTqy 284
Cdd:PRK00369 157 KILHPEVPLALKSN----RKLRRNCwyEIAA-----LYYVK----DYQNVhITHASNPRTVR----LAKELGftVDIT-- 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958791289 285 wnkewrhaAHHVM-----------GPPLRpDPSTPGFLMNLLANGDltTTGSDNCTFNTCQKalgKDDFTKIPNGVNGVE 353
Cdd:PRK00369 218 --------PHHLLvngekdcltkvNPPIR-DINERLWLLQALSEVD--AIASDHAPHSSFEK---LQPYEVCPPGIAALS 283
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958791289 354 DRMSVIWEKgVHSGKMDENRFVAVTSTNAAKIFNLypKKGRIAVGSDADIVIWDPEATR--TISAKTHHQAVnfNIFEGM 431
Cdd:PRK00369 284 FTPPFIYTL-VSKGILSIDRAVELISTNPARILGI--PYGEIKEGYRANFTVIQFEDWRysTKYSKVIETPL--DGFELK 358
|
410 420
....*....|....*....|....*..
gi 1958791289 432 VChgvPLVTISRGRVVYEAG-VFDVTA 457
Cdd:PRK00369 359 AS---VYATIVQGKLAYLEGeVFPVKG 382
|
|
| Met_dep_hydrolase_B |
cd01307 |
Metallo-dependent hydrolases, subgroup B is part of the superfamily of metallo-dependent ... |
24-407 |
8.15e-09 |
|
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: 57.34 E-value: 8.15e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958791289 24 DVLVEDGVVRALGRDLLPPGDTsrglRILDAAGKLVLPGGIDTHTHMqFPFMGSQSVDDFHQGTKAalagGTTMIIDfai 103
Cdd:cd01307 1 DVAIENGKIAAVGAALAAPAAT----QIVDAGGCYVSPGWIDLHVHV-YQGGTRYGDRPDMIGVKS----GVTTVVD--- 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958791289 104 pqKGSSLIEAFETWRnwadpkvccdyslhvavtwwsdkvkeemKTLAQDKGVNSFkmfmAYKDLYMV-QDQQMYAAFSQC 182
Cdd:cd01307 69 --AGSAGADNIDGFR----------------------------YTVIERSATRVY----AFLNISRVgLVAQDELPDPDN 114
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958791289 183 KEIGAIAQVHAENGDLIAeGAKKMLALGITGPEGHELCRpeaveaeatlRAITIASAVNCPLYiVHVMSKSAA-KVIADA 261
Cdd:cd01307 115 IDEDAVVAAAREYPDVIV-GLKARASKSVVGEWGIKPLE----------LAKKIAKEADLPLM-VHIGSPPPIlDEVVPL 182
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958791289 262 KREGKVVygepiaaglgtdgtqywnkewRHAAHHVMGPPLRPDPSTPGFLMNLLANG---DLtTTGSDNCTFNTCQKA-- 336
Cdd:cd01307 183 LRRGDVL---------------------THCFNGKPNGIVDEEGEVLPLVRRARERGvifDV-GHGTASFSFRVARAAia 240
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1958791289 337 -------LGKDDFTKipNGVNGVEDRMSVIWEKGVHSGKMDENRFVAVTsTNAAKIFNLyPKKGRIAVGSDADIVIWD 407
Cdd:cd01307 241 agllpdtISSDIHGR--NRTNGPVYALATTLSKLLALGMPLEEVIEAVT-ANPARMLGL-AEIGTLAVGYDADLTVFD 314
|
|
| PRK08204 |
PRK08204 |
hypothetical protein; Provisional |
5-69 |
1.96e-08 |
|
hypothetical protein; Provisional
Pssm-ID: 181288 [Multi-domain] Cd Length: 449 Bit Score: 56.55 E-value: 1.96e-08
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1958791289 5 ERLLIRGGRVVNDD----FSQVADVLVEDGVVRALGRDLLPPGDtsrglRILDAAGKLVLPGGIDTHTH 69
Cdd:PRK08204 2 KRTLIRGGTVLTMDpaigDLPRGDILIEGDRIAAVAPSIEAPDA-----EVVDARGMIVMPGLVDTHRH 65
|
|
| NagA |
COG1820 |
N-acetylglucosamine-6-phosphate deacetylase [Carbohydrate transport and metabolism]; |
8-96 |
3.03e-08 |
|
N-acetylglucosamine-6-phosphate deacetylase [Carbohydrate transport and metabolism];
Pssm-ID: 441425 [Multi-domain] Cd Length: 373 Bit Score: 55.49 E-value: 3.03e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958791289 8 LIRGGRVVNDD-FSQVADVLVEDGVVRALGRDLLPPGDtsrglrILDAAGKLVLPGGIDTHTH--MQFPFMgSQSVDDFH 84
Cdd:COG1820 1 AITNARIFTGDgVLEDGALLIEDGRIAAIGPGAEPDAE------VIDLGGGYLAPGFIDLHVHggGGVDFM-DGTPEALR 73
|
90
....*....|..
gi 1958791289 85 QGTKAALAGGTT 96
Cdd:COG1820 74 TIARAHARHGTT 85
|
|
| metallo-dependent_hydrolases |
cd01292 |
Superfamily of metallo-dependent hydrolases (also called amidohydrolase superfamily) is a ... |
64-214 |
3.92e-08 |
|
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: 54.65 E-value: 3.92e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958791289 64 IDTHTHMQFP----------------FMGSQSVDDFHQGTKAALAGGTTMIIDFAIPQKGSSLIEAFETWRNWADP---- 123
Cdd:cd01292 2 IDTHVHLDGSalrgtrlnlelkeaeeLSPEDLYEDTLRALEALLAGGVTTVVDMGSTPPPTTTKAAIEAVAEAARAsagi 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958791289 124 -KVCCDYSLHVAVTWWSDKVKEEMKTLAQ--DKGVNSFKMFMAYKDlYMVQDQQMYAAFSQCKEIGAIAQVHAENGDLIA 200
Cdd:cd01292 82 rVVLGLGIPGVPAAVDEDAEALLLELLRRglELGAVGLKLAGPYTA-TGLSDESLRRVLEEARKLGLPVVIHAGELPDPT 160
|
170
....*....|....
gi 1958791289 201 EGAKKMLALGITGP 214
Cdd:cd01292 161 RALEDLVALLRLGG 174
|
|
| PRK09061 |
PRK09061 |
D-glutamate deacylase; Validated |
6-468 |
5.63e-08 |
|
D-glutamate deacylase; Validated
Pssm-ID: 236369 [Multi-domain] Cd Length: 509 Bit Score: 55.09 E-value: 5.63e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958791289 6 RLLIRGGRVVNDD--FSQVADVLVEDGVVRALGRDLLppgdtsRGLRILDAAGKLVLPGGIDTHTHMQfpfmgSQSVDDF 83
Cdd:PRK09061 20 DLVIRNGRVVDPEtgLDAVRDVGIKGGKIAAVGTAAI------EGDRTIDATGLVVAPGFIDLHAHGQ-----SVAAYRM 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958791289 84 HqgtkaALAGGTTMiIDFAIpqkGSSLIEAFetWRNWADPKVCCDYSlhVAVTWWSDKVKeEMKTLAQDKGVNSFKMFMA 163
Cdd:PRK09061 89 Q-----AFDGVTTA-LELEA---GVLPVARW--YAEQAGEGRPLNYG--ASVGWTPARIA-VLTGPQAEGTIADFGKALG 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958791289 164 YKdlymvqDQQMYAAFSQckEIGAIAQVhAENGdlIAEGAkkmLALGI-------TGP-EGHELCRPEA----------- 224
Cdd:PRK09061 155 DP------RWQERAATPA--ELAEILEL-LEQG--LDEGA---LGIGIgagyapgTGHkEYLELARLAAragvptythvr 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958791289 225 --------VEAEATLRAITIASAVNCPLYIVHVMSKS------AAKVIADAKREGKVVYGE--PIAAG---LGTD----- 280
Cdd:PRK09061 221 ylsnvdprSSVDAYQELIAAAAETGAHMHICHVNSTSlrdidrCLALVEKAQAQGLDVTTEayPYGAGstvVGAAffdpg 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958791289 281 -----GTQYWNKEWRHAAHHVM--------------GPPL-----RPDPSTPGFLMNLLANGD-------LTTTGSDNCT 329
Cdd:PRK09061 301 wlermGLGYGSLQWVETGERLLtreelaklrandpgGLVLihfldEDNPRDRALLDRSVLFPGaaiasdaMPWTWSDGTV 380
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958791289 330 FNTCQKALGKDDFTKiPNGvNG---------VEDRMSVIWEKGVHsgKMdenrfvavtSTNAAKIFNLY----PKKGRIA 396
Cdd:PRK09061 381 YEGDAWPLPEDAVSH-PRS-AGtfarflreyVRERKALSLLEAIR--KC---------TLMPAQILEDSvpamRRKGRLQ 447
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1958791289 397 VGSDADIVIWDPEatrTISAKTHHQAVNfnifegMVCHGVPLVTISrGRVVYEAGVFDVTAGHGKFIpRQPF 468
Cdd:PRK09061 448 AGADADIVVFDPE---TITDRATFEDPN------RPSEGVRHVLVN-GVPVVSNGELVRDARPGRPV-RRPV 508
|
|
| YtcJ |
COG1574 |
Predicted amidohydrolase YtcJ [General function prediction only]; |
7-70 |
7.58e-08 |
|
Predicted amidohydrolase YtcJ [General function prediction only];
Pssm-ID: 441182 [Multi-domain] Cd Length: 535 Bit Score: 54.80 E-value: 7.58e-08
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1958791289 7 LLIRGGRV--VNDDFSQVADVLVEDGVVRALG-----RDLLPPGDtsrglRILDAAGKLVLPGGIDTHTHM 70
Cdd:COG1574 10 LLLTNGRIytMDPAQPVAEAVAVRDGRIVAVGsdaevRALAGPAT-----EVIDLGGKTVLPGFIDAHVHL 75
|
|
| NagA |
cd00854 |
N-acetylglucosamine-6-phosphate deacetylase, NagA, catalyzes the hydrolysis of the N-acetyl ... |
7-408 |
1.10e-07 |
|
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: 54.12 E-value: 1.10e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958791289 7 LLIRGGRVVNDDFSQVADVLVEDGVVRALGrdllPPGDTSRGLRILDAAGKLVLPGGIDTHTHmqfpfmGSQSVdDFHQG 86
Cdd:cd00854 1 LIIKNARILTPGGLEDGAVLVEDGKIVAIG----PEDELEEADEIIDLKGQYLVPGFIDIHIH------GGGGA-DFMDG 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958791289 87 TKAALAG--------GTTMIIDFAIPQKGSSLIEAFETWRNWADPKVCCDY-SLHVAVTWWSdkvkEEMKTlAQDKGVns 157
Cdd:cd00854 70 TAEALKTiaealakhGTTSFLPTTVTAPPEEIAKALAAIAEAIAEGQGAEIlGIHLEGPFIS----PEKKG-AHPPEY-- 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958791289 158 fkMFMAYKDLYmvqdQQMYAAFSQCKEIGAIAQVHAENGDLIaegaKKMLALGITGPEGH-----ELCRpEAVEAEATL- 231
Cdd:cd00854 143 --LRAPDPEEL----KKWLEAAGGLIKLVTLAPELDGALELI----RYLVERGIIVSIGHsdatyEQAV-AAFEAGATHv 211
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958791289 232 ------------RAITIASAVNCPLYI--------VHVmSKSAAKVIADAKREGKVVYgepI-----AAGLGtDGtqywn 286
Cdd:cd00854 212 thlfnamsplhhREPGVVGAALSDDDVyaeliadgIHV-HPAAVRLAYRAKGADKIVL---VtdamaAAGLP-DG----- 281
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958791289 287 kewrhaaHHVMGPplRPDPSTPGflMNLLANGdlTTTGSDnCTFNTCQKALGKddFTKIPngvngVED--RMSviwekgv 364
Cdd:cd00854 282 -------EYELGG--QTVTVKDG--VARLADG--TLAGST-LTMDQAVRNMVK--WGGCP-----LEEavRMA------- 333
|
410 420 430 440
....*....|....*....|....*....|....*....|....
gi 1958791289 365 hsgkmdenrfvavtSTNAAKIFNLYPKKGRIAVGSDADIVIWDP 408
Cdd:cd00854 334 --------------SLNPAKLLGLDDRKGSLKPGKDADLVVLDD 363
|
|
| PRK08393 |
PRK08393 |
N-ethylammeline chlorohydrolase; Provisional |
7-69 |
1.17e-07 |
|
N-ethylammeline chlorohydrolase; Provisional
Pssm-ID: 181411 [Multi-domain] Cd Length: 424 Bit Score: 54.04 E-value: 1.17e-07
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1958791289 7 LLIRGGRVV-NDDFSQV-ADVLVEDGVVRALGRDLLPPGDTsrglrILDAAGKLVLPGGIDTHTH 69
Cdd:PRK08393 3 ILIKNGYVIyGENLKVIrADVLIEGNKIVEVKRNINKPADT-----VIDASGSVVSPGFINAHTH 62
|
|
| FwdA |
COG1229 |
Formylmethanofuran dehydrogenase subunit A [Energy production and conversion]; |
7-69 |
2.79e-07 |
|
Formylmethanofuran dehydrogenase subunit A [Energy production and conversion];
Pssm-ID: 440842 Cd Length: 554 Bit Score: 53.27 E-value: 2.79e-07
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1958791289 7 LLIRGGRV------VNDDfsqVADVLVEDGVVRAlgrdllPPGDtSRGLRILDAAGKLVLPGGIDTHTH 69
Cdd:COG1229 3 LIIKNGRVydpangIDGE---VMDIAIKDGKIVE------EPSD-PKDAKVIDASGKVVMAGGVDIHTH 61
|
|
| Imidazolone-5PH |
cd01296 |
Imidazolonepropionase/imidazolone-5-propionate hydrolase (Imidazolone-5PH) catalyzes the third ... |
25-99 |
3.19e-07 |
|
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: 52.65 E-value: 3.19e-07
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1958791289 25 VLVEDGVVRALGRDLLPPGDTSRGLRILDAAGKLVLPGGIDTHTHMQFpfmGSQSVDDFhqgtKAALAGGTTMII 99
Cdd:cd01296 1 IAIRDGRIAAVGPAASLPAPGPAAAEEIDAGGRAVTPGLVDCHTHLVF---AGDRVDEF----AARLAGASYEEI 68
|
|
| PRK08417 |
PRK08417 |
metal-dependent hydrolase; |
299-449 |
9.19e-07 |
|
metal-dependent hydrolase;
Pssm-ID: 236262 [Multi-domain] Cd Length: 386 Bit Score: 51.24 E-value: 9.19e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958791289 299 PPLRpDPSTPGFLMNLLANGDLTTTGSDNC-TFNTcqkalgKDD--FTKIPNGVNGVEDRMSVIWEKGVHSGKMDENRFV 375
Cdd:PRK08417 249 PPLR-SKEDRLALLEALKEGKIDFLTSLHSaKSNS------KKDlaFDEAAFGIDSICEYFSLCYTYLVKEGIITWSELS 321
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1958791289 376 AVTSTNAAKIFNLypKKGRIAVGSDADIVIWDPEaTRTISAKthhqavNFNIFEGMVCHGVPLVTISRGRVVYE 449
Cdd:PRK08417 322 RFTSYNPAQFLGL--NSGEIEVGKEADLVLFDPN-ESTIIDD------NFSLYSGDELYGKIEAVIIKGKLYLE 386
|
|
| PRK15446 |
PRK15446 |
phosphonate metabolism protein PhnM; Provisional |
6-97 |
1.81e-06 |
|
phosphonate metabolism protein PhnM; Provisional
Pssm-ID: 237967 [Multi-domain] Cd Length: 383 Bit Score: 50.18 E-value: 1.81e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958791289 6 RLLIRGGRVVNDDFSQVADVLVEDGVVRALGrdllppGDTSRGLRILDAAGKLVLPGGIDTHT-----HMQ------FPF 74
Cdd:PRK15446 3 EMILSNARLVLPDEVVDGSLLIEDGRIAAID------PGASALPGAIDAEGDYLLPGLVDLHTdnlekHLAprpgvdWPA 76
|
90 100
....*....|....*....|....
gi 1958791289 75 MGS-QSVDdfhqgTKAALAGGTTM 97
Cdd:PRK15446 77 DAAlAAHD-----AQLAAAGITTV 95
|
|
| NagA |
COG1820 |
N-acetylglucosamine-6-phosphate deacetylase [Carbohydrate transport and metabolism]; |
375-409 |
4.02e-06 |
|
N-acetylglucosamine-6-phosphate deacetylase [Carbohydrate transport and metabolism];
Pssm-ID: 441425 [Multi-domain] Cd Length: 373 Bit Score: 48.94 E-value: 4.02e-06
10 20 30
....*....|....*....|....*....|....*
gi 1958791289 375 VAVTSTNAAKIFNLYPKKGRIAVGSDADIVIWDPE 409
Cdd:COG1820 328 VRMASLNPARALGLDDRKGSIAPGKDADLVVLDDD 362
|
|
| PRK08203 |
PRK08203 |
hydroxydechloroatrazine ethylaminohydrolase; Reviewed |
6-70 |
4.62e-06 |
|
hydroxydechloroatrazine ethylaminohydrolase; Reviewed
Pssm-ID: 236184 [Multi-domain] Cd Length: 451 Bit Score: 49.08 E-value: 4.62e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958791289 6 RLLIRGGRVV---NDDFSQVAD--VLVEDGVVRALGRDLLPPGDTSRglrILDAAGKLVLPGGIDTHTHM 70
Cdd:PRK08203 2 TLWIKNPLAIvtmDAARREIADggLVVEGGRIVEVGPGGALPQPADE---VFDARGHVVTPGLVNTHHHF 68
|
|
| COG3653 |
COG3653 |
N-acyl-D-aspartate/D-glutamate deacylase [Secondary metabolites biosynthesis, transport and ... |
7-458 |
5.50e-06 |
|
N-acyl-D-aspartate/D-glutamate deacylase [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 442870 [Multi-domain] Cd Length: 528 Bit Score: 49.02 E-value: 5.50e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958791289 7 LLIRGGRVVndDFS----QVADVLVEDGVVRALGRDLLPPGDtsrglRILDAAGKLVLPGGIDTHTHMQFPFMGSQSVDD 82
Cdd:COG3653 4 LLIRGGTVV--DGTgappFRADVAIKGGRIVAVGDLAAAEAA-----RVIDATGLVVAPGFIDIHTHYDLQLLWDPRLEP 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958791289 83 F-HQGTkaalaggTTMII-------DFAIPQKGSSLIEAFETWRnwadpkvccDYSLHVAVTWWSdkVKEEMKTL-AQDK 153
Cdd:COG3653 77 SlRQGV-------TTVVMgncgvsfAPVRPEDRDRLIDLMEGVE---------GIPEGLDWDWES--FGEYLDALeRRGL 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958791289 154 GVNsFKMFMAYKDL--Y----------------MVQ--DQQM------------YA--AFSQCKEIGAIAQVHAENGDLI 199
Cdd:COG3653 139 GVN-VASLVGHGTLraYvmglddrpptpeelarMRAllREAMeagalglstgliYVpgTYASTDELVALAKVVAEYGGVY 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958791289 200 AegakkmlalGITGPEGHELCrpEAVEAeatlrAITIASAVNCPLYIVHV---------MSKSAAKVIADAKREG-KV-- 267
Cdd:COG3653 218 Q---------SHMRDEGDGLL--EAVDE-----LIRIGREAGVPVHISHLkaagkpnwgKADEVLALIEAARAEGlDVta 281
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958791289 268 -VYGEPI------------AAGLGTDGT--------------------QYWNKEWRHAAHHVMGPPLRPDPSTPG----- 309
Cdd:COG3653 282 dVYPYPAgstglgallppwAAAGGLDERlarlrdpatrariraeieegLPDNLLGRGGWDNILISDSPPNEPLVGkslae 361
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958791289 310 -----------FLMNLLANGDL----------------------TTTGSDNC--------TFNTCQKALGKddftkipng 348
Cdd:COG3653 362 iaaergvdpadAALDLLLEEDGrvlivyfimseedvrellrhpwVMIGSDGGlggkahprAYGTFPRVLGH--------- 432
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958791289 349 vnGVEDR--MSViwEKGVHsgKMdenrfvavTStNAAKIFNLyPKKGRIAVGSDADIVIWDPEatrTISAK-THHQAVNF 425
Cdd:COG3653 433 --YVRERgvLSL--EEAVR--KL--------TS-LPADRLGL-KDRGLLRPGYRADLVVFDPA---TLADRaTFDLPAQR 493
|
570 580 590
....*....|....*....|....*....|....
gi 1958791289 426 NifEGMVChgvplvTISRGRVVYEAGVF-DVTAG 458
Cdd:COG3653 494 A--DGIRA------VIVNGVVVVEDGKPtGARPG 519
|
|
| Amidohydro_3 |
pfam07969 |
Amidohydrolase family; |
50-448 |
1.00e-05 |
|
Amidohydrolase family;
Pssm-ID: 400360 [Multi-domain] Cd Length: 464 Bit Score: 47.91 E-value: 1.00e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958791289 50 RILDAAGKLVLPGGIDTHTHM--QFPFMGSQSVDDFHQGTKAALAGGTTMIID-----------FAIPQKGSSL------ 110
Cdd:pfam07969 1 EVIDAKGRLVLPGFVDPHTHLdgGGLNLRELRLPDVLPNAVVKGQAGRTPKGRwlvgegwdeaqFAETRFPYALadldev 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958791289 111 ----------IEAFETWRN------WADPKVCCD-----------------YSLHVAVTWWSDKVKEEMKTLAQD--KGV 155
Cdd:pfam07969 81 apdgpvllraLHTHAAVANsaaldlAGITKATEDppggeiardangegltgLLREGAYALPPLLAREAEAAAVAAalAAL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958791289 156 NSFKMFMAYKDLYMVQDQQMYAAFSQCKEIGAIAQVHAE--------NGDLIAEGAKKMLALGITG--------PEGHEL 219
Cdd:pfam07969 161 PGFGITSVDGGGGNVHSLDDYEPLRELTAAEKLKELLDAperlglphSIYELRIGAMKLFADGVLGsrtaaltePYFDAP 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958791289 220 CRPEAVEAEATL-RAITIASAVNCPLYIvH------VMS--KSAAKVIADAKREGKVV-------------YGEPIAAGL 277
Cdd:pfam07969 241 GTGWPDFEDEALaELVAAARERGLDVAI-HaigdatIDTalDAFEAVAEKLGNQGRVRiehaqgvvpytysQIERVAALG 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958791289 278 GTDGTQY-WNKEWRHAAHHVMGPPlRPDPSTPgfLMNLLANGDLTTTGSDN--CTFntcqkalgkDDFTKIPNGVNG-VE 353
Cdd:pfam07969 320 GAAGVQPvFDPLWGDWLQDRLGAE-RARGLTP--VKELLNAGVKVALGSDApvGPF---------DPWPRIGAAVMRqTA 387
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958791289 354 DRMSVIWEkgvhSGKMDENRFVAVTSTNAAKIFNLYPKKGRIAVGSDADIVIWDPEATRTISAKTHHQAVnfnifegmvc 433
Cdd:pfam07969 388 GGGEVLGP----DEELSLEEALALYTSGPAKALGLEDRKGTLGVGKDADLVVLDDDPLTVDPPAIADIRV---------- 453
|
490
....*....|....*
gi 1958791289 434 hgvpLVTISRGRVVY 448
Cdd:pfam07969 454 ----RLTVVDGRVVY 464
|
|
| Bact_CD |
cd01293 |
Bacterial cytosine deaminase and related metal-dependent hydrolases. Cytosine deaminases (CDs) ... |
8-122 |
1.54e-05 |
|
Bacterial cytosine deaminase and related metal-dependent hydrolases. Cytosine deaminases (CDs) catalyze the deamination of cytosine, producing uracil and ammonia. They play an important role in pyrimidine salvage. CDs are present in prokaryotes and fungi, but not mammalian cells. The bacterial enzymes, but not the fungal enzymes, are related to the adenosine deaminases (ADA). The bacterial enzymes are iron dependent and hexameric.
Pssm-ID: 238618 [Multi-domain] Cd Length: 398 Bit Score: 47.24 E-value: 1.54e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958791289 8 LIRGGRVVNDDFSQVaDVLVEDGVVRALGRDLLPPGDTSRglriLDAAGKLVLPGGIDTHTHMQFPFMG----------- 76
Cdd:cd01293 1 LLRNARLADGGTALV-DIAIEDGRIAAIGPALAVPPDAEE----VDAKGRLVLPAFVDPHIHLDKTFTGgrwpnnsggtl 75
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1958791289 77 ------------SQSVDDFHQ----GTKAALAGGTTMI-----IDFAIPQKG-SSLIEAFETWRNWAD 122
Cdd:cd01293 76 leaiiaweerklLLTAEDVKEraerALELAIAHGTTAIrthvdVDPAAGLKAlEALLELREEWADLID 143
|
|
| AdeC |
COG1001 |
Adenine deaminase [Nucleotide transport and metabolism]; |
7-100 |
1.55e-05 |
|
Adenine deaminase [Nucleotide transport and metabolism];
Pssm-ID: 440625 [Multi-domain] Cd Length: 559 Bit Score: 47.40 E-value: 1.55e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958791289 7 LLIRGGRVVNddfsqV-------ADVLVEDGVVRALGRDLLPpgdtsrGLRILDAAGKLVLPGGIDTHTHMQFPFMgsqS 79
Cdd:COG1001 7 LVIKNGRLVN-----VftgeileGDIAIAGGRIAGVGDYIGE------ATEVIDAAGRYLVPGFIDGHVHIESSMV---T 72
|
90 100
....*....|....*....|..
gi 1958791289 80 VDDFhqgTKAALAGGTT-MIID 100
Cdd:COG1001 73 PAEF---ARAVLPHGTTtVIAD 91
|
|
| PRK07627 |
PRK07627 |
dihydroorotase; Provisional |
6-450 |
1.60e-05 |
|
dihydroorotase; Provisional
Pssm-ID: 181059 [Multi-domain] Cd Length: 425 Bit Score: 47.36 E-value: 1.60e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958791289 6 RLLIRGGRVVN--DDFSQVADVLVEDGVVRALGRDllPPGDTSRglRILDAAGKLVLPGGIDTHTHMQFPfmGSQSVDDF 83
Cdd:PRK07627 2 KIHIKGGRLIDpaAGTDRQADLYVAAGKIAAIGQA--PAGFNAD--KTIDASGLIVCPGLVDLSARLREP--GYEYKATL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958791289 84 HQGTKAALAGGTTMII---DFAIPQKGSSLIEAFE-TWRNWADPKVccdYSLHVAVTWWSDKVKEEMKTLAqDKGVNSFk 159
Cdd:PRK07627 76 ESEMAAAVAGGVTSLVcppDTDPVLDEPGLVEMLKfRARNLNQAHV---YPLGALTVGLKGEVLTEMVELT-EAGCVGF- 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958791289 160 mfmAYKDLYMVQDQQMYAAFSQCKEIGAIAQVHAE-----NGDLIAEGAkkmLA--LGITGPeghelcrPEAVEAEATLR 232
Cdd:PRK07627 151 ---SQANVPVVDTQVLLRALQYASTFGFTVWLRPLdaflgRGGVAASGA---VAsrLGLSGV-------PVAAETIALHT 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958791289 233 AITIASAVNCPLYIVHVMSKSAAKVIADAKREGKvvygePIAAGLGTDGTQ-------YWNKEWRhaahhvMGPPLRPDP 305
Cdd:PRK07627 218 IFELMRVTGARVHLARLSSAAGVALVRAAKAEGL-----PVTCDVGVNHVHlidvdigYFDSQFR------LDPPLRSQR 286
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958791289 306 STPGfLMNLLANGDLTTTGSDNCTFNTCQKALgkdDFTKIPNGVNGVEDRMSVIWeKGVHSGKMDENRFVAVTSTNAAKI 385
Cdd:PRK07627 287 DREA-IRAALADGTIDAICSDHTPVDDDEKLL---PFAEATPGATGLELLLPLTL-KWADEAKVPLARALARITSAPARV 361
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1958791289 386 FNLypKKGRIAVGSDADIVIWDPEATRTISAKT-HHQAVNfNIFEGMVCHGVPLVTISRGRVVYEA 450
Cdd:PRK07627 362 LGL--PAGRLAEGAPADLCVFDPDAHWRVEPRAlKSQGKN-TPFLGYELPGRVRATLVAGQVAFER 424
|
|
| PRK07583 |
PRK07583 |
cytosine deaminase; |
23-122 |
1.87e-05 |
|
cytosine deaminase;
Pssm-ID: 236062 Cd Length: 438 Bit Score: 47.29 E-value: 1.87e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958791289 23 ADVLVEDGVVRALgrdlLPPGDTSRGLRILDAAGKLVLPGGIDTHTHM-------QFP-----FMGSQ-----------S 79
Cdd:PRK07583 41 VDIEIADGKIAAI----LPAGGAPDELPAVDLKGRMVWPCFVDMHTHLdkghiwpRSPnpdgtFPGALdavtadreahwS 116
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 1958791289 80 VDDFHQ----GTKAALAGGTTMI---IDFAIPQKGSSLiEAFETWRN-WAD 122
Cdd:PRK07583 117 AEDLYRrmefGLRCAYAHGTSAIrthLDSFAPQAAISW-EVFAELREaWAG 166
|
|
| PRK05985 |
PRK05985 |
cytosine deaminase; Provisional |
7-76 |
2.55e-05 |
|
cytosine deaminase; Provisional
Pssm-ID: 180337 [Multi-domain] Cd Length: 391 Bit Score: 46.46 E-value: 2.55e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958791289 7 LLIRGGRvvnDDFSQVADVLVEDGVVRALGRDLLPPgdtsRGLRILDAAGKLVLPGGIDTHTHMQFPFMG 76
Cdd:PRK05985 4 LLFRNVR---PAGGAAVDILIRDGRIAAIGPALAAP----PGAEVEDGGGALALPGLVDGHIHLDKTFWG 66
|
|
| PRK07228 |
PRK07228 |
5'-deoxyadenosine deaminase; |
6-69 |
2.67e-05 |
|
5'-deoxyadenosine deaminase;
Pssm-ID: 180895 [Multi-domain] Cd Length: 445 Bit Score: 46.53 E-value: 2.67e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1958791289 6 RLLIRGGRVVNDDFSQV---ADVLVEDGVVRALGRDLLPPGDTsrglRILDAAGKLVLPGGIDTHTH 69
Cdd:PRK07228 2 TILIKNAGIVTMNAKREivdGDVLIEDDRIAAVGDRLDLEDYD----DHIDATGKVVIPGLIQGHIH 64
|
|
| PRK09228 |
PRK09228 |
guanine deaminase; Provisional |
25-73 |
2.80e-05 |
|
guanine deaminase; Provisional
Pssm-ID: 236419 [Multi-domain] Cd Length: 433 Bit Score: 46.34 E-value: 2.80e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 1958791289 25 VLVEDGVVRALG-----RDLLPPGdtsrgLRILDAAGKLVLPGGIDTHTHmqFP 73
Cdd:PRK09228 34 LLVEDGRIVAAGpyaelRAQLPAD-----AEVTDYRGKLILPGFIDTHIH--YP 80
|
|
| YtcJ_like |
cd01300 |
YtcJ_like metal dependent amidohydrolases. YtcJ is a Bacillus subtilis ORF of unknown function. ... |
24-70 |
3.32e-04 |
|
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: 43.07 E-value: 3.32e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 1958791289 24 DVLVEDGVVRALGRD----LLPPGDTsrglRILDAAGKLVLPGGIDTHTHM 70
Cdd:cd01300 1 AVAVRDGRIVAVGSDaeakALKGPAT----EVIDLKGKTVLPGFIDSHSHL 47
|
|
| FMDH_A |
cd01304 |
Formylmethanofuran dehydrogenase (FMDH) subunit A; Methanogenic bacteria and archea derive ... |
9-69 |
7.94e-04 |
|
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: 42.02 E-value: 7.94e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1958791289 9 IRGGRVV---NDDFSQVADVLVEDGVVRAlgrdllPPGDTSRGlRILDAAGKLVLPGGIDTHTH 69
Cdd:cd01304 1 IKNGTVYdplNGINGEKMDIFIRDGKIVE------SSSGAKPA-KVIDASGKVVMAGGVDMHSH 57
|
|
| GDEase |
cd01303 |
Guanine deaminase (GDEase). Guanine deaminase is an aminohydrolase responsible for the ... |
27-77 |
9.01e-04 |
|
Guanine deaminase (GDEase). Guanine deaminase is an aminohydrolase responsible for the conversion of guanine to xanthine and ammonia, the first step to utilize guanine as a nitrogen source. This reaction also removes the guanine base from the pool and therefore can play a role in the regulation of cellular GTP and the guanylate nucleotide pool.
Pssm-ID: 238628 [Multi-domain] Cd Length: 429 Bit Score: 41.88 E-value: 9.01e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 1958791289 27 VEDGVVRALGRDLLPPGDTSR-------GLRILDAAGKLVLPGGIDTHTHM-QFPFMGS 77
Cdd:cd01303 24 VEDGLIVVVDGNIIAAGAAETlkraakpGARVIDSPNQFILPGFIDTHIHApQYANIGS 82
|
|
| PRK07572 |
PRK07572 |
cytosine deaminase; Validated |
7-70 |
1.45e-03 |
|
cytosine deaminase; Validated
Pssm-ID: 181039 Cd Length: 426 Bit Score: 41.16 E-value: 1.45e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1958791289 7 LLIRGGRVvnDDFSQVADVLVEDGVVRALGrdllpPGDTSRGLRILDAAGKLVLPGGIDTHTHM 70
Cdd:PRK07572 4 LIVRNANL--PDGRTGIDIGIAGGRIAAVE-----PGLQAEAAEEIDAAGRLVSPPFVDPHFHM 60
|
|
| PRK07203 |
PRK07203 |
putative aminohydrolase SsnA; |
7-69 |
1.75e-03 |
|
putative aminohydrolase SsnA;
Pssm-ID: 235963 [Multi-domain] Cd Length: 442 Bit Score: 40.69 E-value: 1.75e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1958791289 7 LLIRGGRVVNDD----FSQVADVLVEDGVVRALG-RDLLppGDTSRGLRILDAAGKLVLPGGIDTHTH 69
Cdd:PRK07203 2 LLIGNGTAITRDpakpVIEDGAIAIEGNVIVEIGtTDEL--KAKYPDAEFIDAKGKLIMPGLINSHNH 67
|
|
| PRK06038 |
PRK06038 |
N-ethylammeline chlorohydrolase; Provisional |
5-69 |
1.87e-03 |
|
N-ethylammeline chlorohydrolase; Provisional
Pssm-ID: 180363 [Multi-domain] Cd Length: 430 Bit Score: 40.89 E-value: 1.87e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1958791289 5 ERLLIRGGRVVNDDFSQV--ADVLVEDGVVRALGRDLLPPGDTsrglrILDAAGKLVLPGGIDTHTH 69
Cdd:PRK06038 2 ADIIIKNAYVLTMDAGDLkkGSVVIEDGTITEVSESTPGDADT-----VIDAKGSVVMPGLVNTHTH 63
|
|
| Isoaspartyl-dipeptidase |
cd01308 |
Isoaspartyl dipeptidase hydrolyzes the beta-L-isoaspartyl linkages in dipeptides, as part of ... |
377-409 |
1.91e-03 |
|
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: 40.45 E-value: 1.91e-03
10 20 30
....*....|....*....|....*....|...
gi 1958791289 377 VTSTNAAKIFNLYpKKGRIAVGSDADIVIWDPE 409
Cdd:cd01308 330 VITSNVARILKLR-KKGEIQPGFDADLVILDKD 361
|
|
| ureC |
PRK13206 |
urease subunit alpha; Reviewed |
12-99 |
2.04e-03 |
|
urease subunit alpha; Reviewed
Pssm-ID: 237304 [Multi-domain] Cd Length: 573 Bit Score: 40.85 E-value: 2.04e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958791289 12 GRVVNDDFSQV-ADVLVEDGVVRALGRDLLPpgDTSRGL----------RILDAAGKLVLPGGIDTHTHmqfpFMGSQSV 80
Cdd:PRK13206 77 GAVILDHWGIVkADVGIRDGRIVAIGKAGNP--DIMDGVhpdlvigpstEIIAGNGRILTAGAIDCHVH----FICPQIV 150
|
90
....*....|....*....
gi 1958791289 81 DDfhqgtkaALAGGTTMII 99
Cdd:PRK13206 151 DE-------ALAAGITTLI 162
|
|
| Met_dep_hydrolase_C |
cd01309 |
Metallo-dependent hydrolases, subgroup C is part of the superfamily of metallo-dependent ... |
29-69 |
2.33e-03 |
|
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: 40.37 E-value: 2.33e-03
10 20 30 40
....*....|....*....|....*....|....*....|.
gi 1958791289 29 DGVVRALGRDLLPPGDTsrglRILDAAGKLVLPGGIDTHTH 69
Cdd:cd01309 1 DGKIVAVGAEITTPADA----EVIDAKGKHVTPGLIDAHSH 37
|
|
| Urease_alpha |
cd00375 |
Urease alpha-subunit; Urease is a nickel-dependent metalloenzyme that catalyzes the hydrolysis ... |
23-99 |
4.09e-03 |
|
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: 39.62 E-value: 4.09e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958791289 23 ADVLVEDGVVRALGR----DLLPpGDTSR-----GLRILDAAGKLVLPGGIDTHTHMQFPfmgsqsvddfhQGTKAALAG 93
Cdd:cd00375 83 ADIGIKDGRIVAIGKagnpDIMD-GVTPNmivgpSTEVIAGEGKIVTAGGIDTHVHFICP-----------QQIEEALAS 150
|
....*.
gi 1958791289 94 GTTMII 99
Cdd:cd00375 151 GITTMI 156
|
|
| ureC |
PRK13207 |
urease subunit alpha; Reviewed |
23-98 |
4.26e-03 |
|
urease subunit alpha; Reviewed
Pssm-ID: 237305 [Multi-domain] Cd Length: 568 Bit Score: 39.78 E-value: 4.26e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958791289 23 ADVLVEDGVVRALGR----DLLPPGD--TSRGLRILDAAGKLVLPGGIDTHTHmqfpFMGSQSVDdfhqgtkAALAGG-T 95
Cdd:PRK13207 85 ADIGIKDGRIVAIGKagnpDIQDGVDiiIGPGTEVIAGEGLIVTAGGIDTHIH----FICPQQIE-------EALASGvT 153
|
...
gi 1958791289 96 TMI 98
Cdd:PRK13207 154 TMI 156
|
|
| Met_dep_hydrolase_C |
cd01309 |
Metallo-dependent hydrolases, subgroup C is part of the superfamily of metallo-dependent ... |
376-407 |
5.90e-03 |
|
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: 38.83 E-value: 5.90e-03
10 20 30
....*....|....*....|....*....|..
gi 1958791289 376 AVTStNAAKIFNLYPKKGRIAVGSDADIVIWD 407
Cdd:cd01309 308 AITI-NPAKILGIEDRVGSLEPGKDADLVVWN 338
|
|
| |
