|
Name |
Accession |
Description |
Interval |
E-value |
| D-HYD |
cd01314 |
D-hydantoinases (D-HYD) also called dihydropyrimidases (DHPase) and related proteins; DHPases ... |
1-403 |
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: 637.72 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034565965 1 MVLPGGVDVHTRLQMPVLGMTPADDFCQGTKAALAGGTTMILDHVFPDTGVSLLAAYEQWRERADSAACCDYSLHVDITR 80
Cdd:cd01314 48 YVLPGGIDPHTHLELPFMGTVTADDFESGTRAAAAGGTTTIIDFAIPNKGQSLLEAVEKWRGKADGKSVIDYGFHMIITD 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034565965 81 WHESIKEELEALVKeKGVNSFLVFMAYKDRCQCSDSQMYEIFSIIRDLGALAQVHAENGDIVEEEQKRLLELGITGPEGH 160
Cdd:cd01314 128 WTDSVIEELPELVK-KGISSFKVFMAYKGLLMVDDEELLDVLKRAKELGALVMVHAENGDVIAELQKKLLAQGKTGPEYH 206
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034565965 161 VLSHPEEVEAEAVYRAVTIAKQANCPLYVTKVMSKGAADAIAQAKRRGVVVFGEPITASLGTDGSHYWsKNWAKAAAFVT 240
Cdd:cd01314 207 ALSRPPEVEAEATARAIRLAELAGAPLYIVHVSSKEAADEIARARKKGLPVYGETCPQYLLLDDSDYW-KDWFEGAKYVC 285
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034565965 241 SPPVNPDpTTADHLTCLLSSGDLQVTGSAHCTFTTAQKAVGKDNFALIPEGTNGIEERMSMVWEKCVASGKMDENEFVAV 320
Cdd:cd01314 286 SPPLRPK-EDQEALWDGLSSGTLQTVGSDHCPFNFAQKARGKDDFTKIPNGVPGVETRMPLLWSEGVAKGRITLEKFVEL 364
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034565965 321 TSTNAAKIFNFYPRKGRVAVGSDADLVIWNPKATKIISAKTHNLNVEYNIFEGVECRGAPAVVISQGRVALEDGKMFVTP 400
Cdd:cd01314 365 TSTNPAKIFGLYPRKGTIAVGSDADLVIWDPNAEKTISADTHHHNVDYNIFEGMKVKGWPVVTISRGKVVVEDGELVGEK 444
|
...
gi 1034565965 401 GAG 403
Cdd:cd01314 445 GSG 447
|
|
| D-hydantoinase |
TIGR02033 |
D-hydantoinase; This model represents the D-hydantoinase (dihydropyrimidinase) which primarily ... |
1-408 |
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: 585.50 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034565965 1 MVLPGGVDVHTRLQMPVLGMTPADDFCQGTKAALAGGTTMILDHVFPDTGVSLLAAYEQWRERADSAACCDYSLHVDITR 80
Cdd:TIGR02033 48 YVLPGGIDVHTHLEMPFGGTTTADDFFTGTKAAAAGGTTTIIDFVVPEKGSSLTEALETWHEKAEGKSVIDYGFHMDITH 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034565965 81 WHESIKEELEALVKEKGVNSFLVFMAYKDRCQCSDSQMYEIFSIIRDLGALAQVHAENGDIVEEEQKRLLELGITGPEGH 160
Cdd:TIGR02033 128 WNDSVLEEHIPEVKEEGINSFKVFMAYKNLLMVDDEELFEILKRLKELGALLQVHAENGDIIAELQARMLAQGITGPEYH 207
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034565965 161 VLSHPEEVEAEAVYRAVTIAKQANCPLYVTKVMSKGAADAIAQAKRRGVVVFGEPITASLGTDGSHYWsKNWAKAAAFVT 240
Cdd:TIGR02033 208 ALSRPPELEAEAVARAITLAALADAPLYVVHVSTKDAADEIAQARKKGQPVFGETCPQYLVLDDTHYD-KPGFEGAKYVC 286
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034565965 241 SPPVNpDPTTADHLTCLLSSGDLQVTGSAHCTFTTAQK-AVGKDNFALIPEGTNGIEERMSMVWEKCVASGKMDENEFVA 319
Cdd:TIGR02033 287 SPPLR-EPEDQDALWSALSSGALQTVGSDHCTFNFAQKkAIGKDDFTKIPNGGPGVEERMSLLFDEGVAKGRITLEKFVE 365
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034565965 320 VTSTNAAKIFNFYPRKGRVAVGSDADLVIWNPKATKIISAKTHNLNVEYNIFEGVECRGAPAVVISQGRVALEDGKMFVT 399
Cdd:TIGR02033 366 VTSTNPAKIFNLYPRKGTIAVGSDADIVIWDPNRTTVISAETHHSNADYNPFEGFKVRGAPVSVLSRGRVVVEDGQLVGT 445
|
....*....
gi 1034565965 400 PGAGRFVPR 408
Cdd:TIGR02033 446 AGAGRFVKR 454
|
|
| PRK08323 |
PRK08323 |
phenylhydantoinase; Validated |
2-412 |
8.63e-180 |
|
phenylhydantoinase; Validated
Pssm-ID: 236240 [Multi-domain] Cd Length: 459 Bit Score: 512.41 E-value: 8.63e-180
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034565965 2 VLPGGVDVHTRLQMPVLGMTPADDFCQGTKAALAGGTTMILDHVFPDTGVSLLAAYEQWRERADSAACCDYSLHVDITRW 81
Cdd:PRK08323 47 VMPGGIDPHTHMEMPFGGTVSSDDFETGTRAAACGGTTTIIDFALQPKGQSLREALEAWHGKAAGKAVIDYGFHMIITDW 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034565965 82 HESIKEELEALVKEkGVNSFLVFMAYKDRCQCSDSQMYEIFSIIRDLGALAQVHAENGDIVEEEQKRLLELGITGPEGHV 161
Cdd:PRK08323 127 NEVVLDEMPELVEE-GITSFKLFMAYKGALMLDDDELLRALQRAAELGALPMVHAENGDAIAYLQAKLLAEGKTGPEYHA 205
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034565965 162 LSHPEEVEAEAVYRAVTIAKQANCPLYVTKVMSKGAADAIAQAKRRGVVVFGEPITASLGTDGSHYWSKNWAKAAAFVTS 241
Cdd:PRK08323 206 LSRPPEVEGEATNRAIMLAELAGAPLYIVHVSCKEALEAIRRARARGQRVFGETCPQYLLLDESEYDGPDWFEGAKYVMS 285
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034565965 242 PPVNPdPTTADHLTCLLSSGDLQVTGSAHCTFTTAQKA-VGKDNFALIPEGTNGIEERMSMVWEKCVASGKMDENEFVAV 320
Cdd:PRK08323 286 PPLRD-KEHQDALWRGLQDGDLQVVATDHCPFCFEQKKqLGRGDFTKIPNGTPGVEDRMPLLFSEGVMTGRITLNRFVEL 364
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034565965 321 TSTNAAKIFNFYPRKGRVAVGSDADLVIWNPKATKIISAKTHNLNVEYNIFEGVECRGAPAVVISQGRVALEDGKMFVTP 400
Cdd:PRK08323 365 TSTNPAKIFGLYPRKGTIAVGADADIVIWDPNATKTISASTLHSNVDYNPYEGFEVTGWPVTTLSRGEVVVEDGEFRGKA 444
|
410
....*....|..
gi 1034565965 401 GAGRFVPRKTFP 412
Cdd:PRK08323 445 GHGRFLKRKPFQ 456
|
|
| PLN02942 |
PLN02942 |
dihydropyrimidinase |
2-423 |
3.54e-171 |
|
dihydropyrimidinase
Pssm-ID: 178530 Cd Length: 486 Bit Score: 491.67 E-value: 3.54e-171
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034565965 2 VLPGGVDVHTRLQMPVLGMTPADDFCQGTKAALAGGTTMILDHVFPDTGvSLLAAYEQWRERADSAaCCDYSLHVDITRW 81
Cdd:PLN02942 55 VMPGGIDPHTHLAMPFMGTETIDDFFSGQAAALAGGTTMHIDFVIPVNG-NLLAGYEAYEKKAEKS-CMDYGFHMAITKW 132
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034565965 82 HESIKEELEALVKEKGVNSFLVFMAYKDRCQCSDSQMYEIFSIIRDLGALAQVHAENGDIVEEEQKRLLELGITGPEGHV 161
Cdd:PLN02942 133 DDTVSRDMETLVKEKGINSFKFFMAYKGSLMVTDELLLEGFKRCKSLGALAMVHAENGDAVFEGQKRMIELGITGPEGHA 212
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034565965 162 LSHPEEVEAEAVYRAVTIAKQANCPLYVTKVMSKGAADAIAQAKRRGVVVFGEPITASLGTDGSHYWSKNWAKAAAFVTS 241
Cdd:PLN02942 213 LSRPPLLEGEATARAIRLAKFVNTPLYVVHVMSIDAMEEIARARKSGQRVIGEPVVSGLVLDDSKLWDPDFTIASKYVMS 292
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034565965 242 PPVNPdpttADH---LTCLLSSGDLQVTGSAHCTFTTAQKAVGKDNFALIPEGTNGIEERMSMVWEKCVASGKMDENEFV 318
Cdd:PLN02942 293 PPIRP----AGHgkaLQAALSSGILQLVGTDHCPFNSTQKAFGKDDFRKIPNGVNGIEERMHLVWDTMVESGQISPTDYV 368
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034565965 319 AVTSTNAAKIFNFYPRKGRVAVGSDADLVIWNPKATKIISAKTHNLNVEYNIFEGVECRGAPAVVISQGRVALEDGKMFV 398
Cdd:PLN02942 369 RVTSTECAKIFNIYPRKGAILAGSDADIIILNPNSTFTISAKTHHSRIDTNVYEGRRGKGKVEVTISQGRVVWENGELKV 448
|
410 420
....*....|....*....|....*
gi 1034565965 399 TPGAGRFVPRKTFPdFVYKRIKARN 423
Cdd:PLN02942 449 VRGSGRYIEMPPFS-YLFDGIQKAD 472
|
|
| AllB |
COG0044 |
Dihydroorotase or related cyclic amidohydrolase [Nucleotide transport and metabolism]; ... |
2-408 |
2.70e-106 |
|
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: 324.35 E-value: 2.70e-106
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034565965 2 VLPGGVDVHTRLQMPvlGMTPADDFCQGTKAALAGGTTMILDhvFPDT--GVSLLAAYEQWRERADSAACCDYSLHVDIT 79
Cdd:COG0044 48 VLPGLIDLHVHLREP--GLEHKEDIETGTRAAAAGGVTTVVD--MPNTnpVTDTPEALEFKLARAEEKALVDVGPHGALT 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034565965 80 RWHESIKEELEALVkEKGVNSFLVFMAYKD-RCQCSDSQMYEIFSIIRDLGALAQVHAENGDIVEEeqkRLLELGITGPE 158
Cdd:COG0044 124 KGLGENLAELGALA-EAGAVAFKVFMGSDDgNPVLDDGLLRRALEYAAEFGALVAVHAEDPDLIRG---GVMNEGKTSPR 199
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034565965 159 GHVLSHPEEVEAEAVYRAVTIAKQANCPLYVTKVMSKGAADAIAQAKRRGVVVFGE--P----ITAS-LGTDGSHYwskn 231
Cdd:COG0044 200 LGLKGRPAEAEEEAVARDIALAEETGARLHIVHVSTAEAVELIREAKARGLPVTAEvcPhhltLTDEdLERYGTNF---- 275
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034565965 232 wakaaafVTSPPVNpdpTTADHLTCL--LSSGDLQVTGSAHCTFTTAQKAvgkDNFALIPEGTNGIEERMSMVWEKCVAS 309
Cdd:COG0044 276 -------KVNPPLR---TEEDREALWegLADGTIDVIATDHAPHTLEEKE---LPFAEAPNGIPGLETALPLLLTELVHK 342
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034565965 310 GKMDENEFVAVTSTNAAKIFNFyPRKGRVAVGSDADLVIWNPKATKIISAKTHNLNVEYNIFEGVECRGAPAVVISQGRV 389
Cdd:COG0044 343 GRLSLERLVELLSTNPARIFGL-PRKGRIAVGADADLVLFDPDAEWTVTAEDLHSKSKNTPFEGRELTGRVVATIVRGRV 421
|
410
....*....|....*....
gi 1034565965 390 ALEDGKmFVTPGAGRFVPR 408
Cdd:COG0044 422 VYEDGE-VVGEPRGRFLRR 439
|
|
| PRK13404 |
PRK13404 |
dihydropyrimidinase; Provisional |
1-408 |
9.13e-101 |
|
dihydropyrimidinase; Provisional
Pssm-ID: 184033 [Multi-domain] Cd Length: 477 Bit Score: 311.25 E-value: 9.13e-101
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034565965 1 MVLPGGVDVHTRLQMPV-LGMTPADDFCQGTKAALAGGTTMILDHVFPDTGVSLLAAYEQWRERADSAACCDYSLHV--- 76
Cdd:PRK13404 51 LVLPGGVDSHCHIDQPSgDGIMMADDFYTGTVSAAFGGTTTVIPFAAQHRGQSLREAVEDYHRRAAGKAVIDYAFHLiva 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034565965 77 DITRwhESIKEELEALVKEkGVNSFLVFMAYkDRCQCSDSQMYEIFSIIRDLGALAQVHAENGDIVEEEQKRLLELGITG 156
Cdd:PRK13404 131 DPTE--EVLTEELPALIAQ-GYTSFKVFMTY-DDLKLDDRQILDVLAVARRHGAMVMVHAENHDMIAWLTKRLLAAGLTA 206
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034565965 157 PEGHVLSHPEEVEAEAVYRAVTIAKQANCPLYVTKVMSKGAADAIAQAKRRGVVVFGEP------ITAS-LGTDGSHyws 229
Cdd:PRK13404 207 PKYHAISRPMLAEREATHRAIALAELVDVPILIVHVSGREAAEQIRRARGRGLKIFAETcpqylfLTAEdLDRPGME--- 283
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034565965 230 knwakAAAFVTSPPvnpdPTTADHLTCL---LSSGDLQVTGSAHCTF---TTAQKAVGKDN--FALIPEGTNGIEERMSM 301
Cdd:PRK13404 284 -----GAKYICSPP----PRDKANQEAIwngLADGTFEVFSSDHAPFrfdDTDGKLAAGANpsFKAIANGIPGIETRLPL 354
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034565965 302 VWEKCVASGKMDENEFVAVTSTNAAKIFNFYPRKGRVAVGSDADLVIWNPKATKIISAKTHNLNVEYNIFEGVECRGAPA 381
Cdd:PRK13404 355 LFSEGVVKGRISLNRFVALTSTNPAKLYGLYPRKGAIAIGADADIAIWDPDREVTITNADLHHAADYTPYEGMRVTGWPV 434
|
410 420
....*....|....*....|....*..
gi 1034565965 382 VVISQGRVALEDGKMFVTPGAGRFVPR 408
Cdd:PRK13404 435 TVLSRGRVVVEDGELVAERGSGQFLAR 461
|
|
| Cyclic_amidohydrolases |
cd01302 |
Cyclic amidohydrolases, including hydantoinase, dihydropyrimidinase, allantoinase, and ... |
2-380 |
5.72e-56 |
|
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: 190.30 E-value: 5.72e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034565965 2 VLPGGVDVHTRLQMPVLGMTpADDFCQGTKAALAGGTTMILDHVFPDTGVSLLAAYEQWRERADSAACCDYSLHVDITRw 81
Cdd:cd01302 3 VLPGFIDIHVHLRDPGGTTY-KEDFESGSRAAAAGGVTTVIDMPNTGPPPIDLPAIELKIKLAEESSYVDFSFHAGIGP- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034565965 82 hESIKEELEaLVKEKGVNSFLVFMAYK--DRCQCSDSQMYEIFSIIRDLGALAQVHAEngdiveeeqkrllelgitgpeg 159
Cdd:cd01302 81 -GDVTDELK-KLFDAGINSLKVFMNYYfgELFDVDDGTLMRTFLEIASRGGPVMVHAE---------------------- 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034565965 160 hvlshpeeveaeavyRAVTIAKQANCPLYVTKVMSKGAADAIAQAKRRGVVVFGEPITASLGTDGShYWSKNWAKaaaFV 239
Cdd:cd01302 137 ---------------RAAQLAEEAGANVHIAHVSSGEALELIKFAKNKGVKVTCEVCPHHLFLDES-MLRLNGAW---GK 197
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034565965 240 TSPPVNPdPTTADHLTCLLSSGDLQVTGSAHCTFTTAQKAVGKDnFALIPEGTNGIEERMSMVWEKcVASGKMDENEFVA 319
Cdd:cd01302 198 VNPPLRS-KEDREALWEGVKNGKIDTIASDHAPHSKEEKESGKD-IWKAPPGFPGLETRLPILLTE-GVKRGLSLETLVE 274
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1034565965 320 VTSTNAAKIFNFYPrKGRVAVGSDADLVIWNPKATKIISAKTHNLNVEYNIFEGVECRGAP 380
Cdd:cd01302 275 ILSENPARIFGLYP-KGTIAVGYDADLVIVDPKKEWKVTAEEIESKADWTPFEGMEVTGKP 334
|
|
| L-HYD_ALN |
cd01315 |
L-Hydantoinases (L-HYDs) and Allantoinase (ALN); L-Hydantoinases are a member of the ... |
1-406 |
1.59e-48 |
|
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: 173.24 E-value: 1.59e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034565965 1 MVLPGGVDVHTRLQMPvlGMTPADDFCQGTKAALAGGTTMILD---HVFPDT--GVSLLAAYEQWRERadsaaccdysLH 75
Cdd:cd01315 49 VVMPGLIDTHVHINEP--GRTEWEGFETGTKAAAAGGITTIIDmplNSIPPTttVENLEAKLEAAQGK----------LH 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034565965 76 VDITRWHESIK---EELEALVkEKGVNSFLVFMA---YKDRCQCSDSQMYEIFSIIRDLGALAQVHAENGDIVEEEQKRL 149
Cdd:cd01315 117 VDVGFWGGLVPgnlDQLRPLD-EAGVVGFKCFLCpsgVDEFPAVDDEQLEEAMKELAKTGSVLAVHAENPEITEALQEQA 195
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034565965 150 LELGITGPEGHVLSHPEEVEAEAVYRAVTIAKQANCPLYVTKVMSKGAADAIAQAKRRGVVVFGEPITaslgtdgsHYWS 229
Cdd:cd01315 196 KAKGKRDYRDYLASRPVFTEVEAIQRILLLAKETGCRLHIVHLSSAEAVPLIREARAEGVDVTVETCP--------HYLT 267
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034565965 230 -------KNwakAAAFVTSPPVNpDPTTADHLTCLLSSGDLQVTGSAHCTFTTAQKAVGKDNFALIPEGTNGIEERMSMV 302
Cdd:cd01315 268 ftaedvpDG---GTEFKCAPPIR-DAANQEQLWEALENGDIDMVVSDHSPCTPELKLLGKGDFFKAWGGISGLQLGLPVM 343
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034565965 303 WEKCVASGKMDENEFVAVTSTNAAKIFNFYPRKGRVAVGSDADLVIWNPKATKIISA---KTHNlnvEYNIFEGVECRGA 379
Cdd:cd01315 344 LTEAVNKRGLSLEDIARLMCENPAKLFGLSHQKGRIAVGYDADFVVWDPEEEFTVDAedlYYKN---KISPYVGRTLKGR 420
|
410 420
....*....|....*....|....*..
gi 1034565965 380 PAVVISQGRVALEDGKMFVTPgAGRFV 406
Cdd:cd01315 421 VHATILRGTVVYQDGEVVGEP-LGQLL 446
|
|
| pyrC_multi |
TIGR00857 |
dihydroorotase, multifunctional complex type; In contrast to the homodimeric type of ... |
1-393 |
4.19e-37 |
|
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: 141.43 E-value: 4.19e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034565965 1 MVLPGGVDVHTRLQMPvlGMTPADDFCQGTKAALAGGTTMILDhvFPDTGVSLLAAYE-QWR-ERADSAACCDYSLHVDI 78
Cdd:TIGR00857 36 LVLPGFIDLHVHLRDP--GEEYKEDIESGSKAAAHGGFTTVAD--MPNTKPPIDTPETlEWKlQRLKKVSLVDVHLYGGV 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034565965 79 TRwHESIKEELEAlvkekgvnSFLVFMA-----YKDRCQC--SDSQMYEIFSIIRDLGALAQVHAENGDIVEEEQKRLLE 151
Cdd:TIGR00857 112 TQ-GNQGKELTEA--------YELKEAGavgrmFTDDGSEvqDILSMRRALEYAAIAGVPIALHAEDPDLIYGGVMHEGP 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034565965 152 LgitGPEGHVLSHPEEVEAEAVYRAVTIAKQANCPLYVTKVMSKGAADAIAQAKRRGVvvfgePITAS------LGTDGS 225
Cdd:TIGR00857 183 S---AAQLGLPARPPEAEEVAVARLLELAKHAGCPVHICHISTKESLELIVKAKSQGI-----KITAEvtphhlLLSEED 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034565965 226 HYWSKNWAKaaafvTSPPVNPdPTTADHLTCLLSSGDLQVTGSAHCTFTTAQKAVgkdNFALIPEGTNGIEERMSMVWEK 305
Cdd:TIGR00857 255 VARLDGNGK-----VNPPLRE-KEDRLALIEGLKDGIIDIIATDHAPHTLEEKTK---EFAAAPPGIPGLETALPLLLQL 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034565965 306 CVAsGKMDENEFVAVTSTNAAKIFNFyPRKGRVAVGSDADLVIWNPKATKIISAKTHNLNVEYNIFEGVECRGAPAVVIS 385
Cdd:TIGR00857 326 LVK-GLISLKDLIRMLSINPARIFGL-PDKGTLEEGNPADITVFDLKKEWTINAETFYSKAKNTPFEGMSLKGKPIATIL 403
|
....*...
gi 1034565965 386 QGRVALED 393
Cdd:TIGR00857 404 RGKVVYED 411
|
|
| PRK02382 |
PRK02382 |
dihydroorotase; Provisional |
2-409 |
2.91e-33 |
|
dihydroorotase; Provisional
Pssm-ID: 179417 [Multi-domain] Cd Length: 443 Bit Score: 131.31 E-value: 2.91e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034565965 2 VLPGGVDVHTRLQMPvlGMTPADDFCQGTKAALAGGTTMILDHVFPDTGVSLLAAYEQWRERADSAACCDYSLHVDITRW 81
Cdd:PRK02382 52 LLPGGIDVHVHFREP--GYTHKETWYTGSRSAAAGGVTTVVDQPNTDPPTVDGESFDEKAELAARKSIVDFGINGGVTGN 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034565965 82 HESIKEELEalvkeKGVNSF-LVFMAYKDRCQCSDSQMY-EIFSIIRDLGALAQVHAENGDIVEEeQKRLLElGITGPEG 159
Cdd:PRK02382 130 WDPLESLWE-----RGVFALgEIFMADSTGGMGIDEELFeEALAEAARLGVLATVHAEDEDLFDE-LAKLLK-GDADADA 202
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034565965 160 HVLSHPEEVEAEAVYRAVTIAKQANCPLYVTKVMSkgaADAIAQAKRRGVVVFGEPITASLGTDgshywskNWAKAAAFV 239
Cdd:PRK02382 203 WSAYRPAAAEAAAVERALEVASETGARIHIAHIST---PEGVDAARREGITCEVTPHHLFLSRR-------DWERLGTFG 272
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034565965 240 -TSPPVNPDPTTaDHLTCLLSSGDLQVTGSAHCTFTTAQKAVG-KDnfalIPEGTNGIEERMSMVWEKcVASGKMDENEF 317
Cdd:PRK02382 273 kMNPPLRSEKRR-EALWERLNDGTIDVVASDHAPHTREEKDADiWD----APSGVPGVETMLPLLLAA-VRKNRLPLERV 346
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034565965 318 VAVTSTNAAKIFNFyPRKGRVAVGSDADLVIWNPKATKIISAKTHNLNVEYNIFEGVEcrGA-PAVVISQGRVALEDGKM 396
Cdd:PRK02382 347 RDVTAANPARIFGL-DGKGRIAEGYDADLVLVDPDAAREIRGDDLHSKAGWTPFEGME--GVfPELTMVRGTVVWDGDDI 423
|
410
....*....|...
gi 1034565965 397 FVTPGAGRFVPRK 409
Cdd:PRK02382 424 NAKRGRGEFLRGR 436
|
|
| DHOase_IIb |
cd01318 |
Dihydroorotase (DHOase), subgroup IIb; DHOases catalyze the reversible interconversion of ... |
2-387 |
1.75e-32 |
|
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: 127.45 E-value: 1.75e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034565965 2 VLPGGVDVHTRLQMPvlGMTPADDFCQGTKAALAGGTTMILDhvFPDTG--VSLLAAYEQWRERADSAACCDYSLHVDIT 79
Cdd:cd01318 4 ILPGVIDIHVHFREP--GLTYKEDFVSGSRAAAAGGVTTVMD--MPNTKppTTTAEALYEKLRLAAAKSVVDYGLYFGVT 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034565965 80 RwhESIKEELEALvkekGVNSFLVFMAYkdrcqcSDSQMYE----IFSIIRDLGALAQVHAENGDIVEEEQKRLLELGIt 155
Cdd:cd01318 80 G--SEDLEELDKA----PPAGYKIFMGD------STGDLLDdeetLERIFAEGSVLVTFHAEDEDRLRENRKELKGESA- 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034565965 156 gpegHVLSHPEEVEAEAVYRAVTIAKQANCPLYVTKVMSKGAADAIAQAKRRGVV-------VFGEPITASLGTdgshyw 228
Cdd:cd01318 147 ----HPRIRDAEAAAVATARALKLARRHGARLHICHVSTPEELKLIKKAKPGVTVevtphhlFLDVEDYDRLGT------ 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034565965 229 sknWAKaaafvtsppVNP---DPTTADHLTCLLSSGDLQVTGSAHCTFTTAQKAVGKDNfalIPEGTNGIEERMS-MVWe 304
Cdd:cd01318 217 ---LGK---------VNPplrSREDRKALLQALADGRIDVIASDHAPHTLEEKRKGYPA---APSGIPGVETALPlMLT- 280
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034565965 305 kCVASGKMDENEFVAVTSTNAAKIFNFyPRKGRVAVGSDADLVIWNPKATKIISAKTHNLNVEYNIFEGVECRGAPAVVI 384
Cdd:cd01318 281 -LVNKGILSLSRVVRLTSHNPARIFGI-KNKGRIAEGYDADLTVVDLKEERTIRAEEFHSKAGWTPFEGFEVTGFPVMTI 358
|
...
gi 1034565965 385 SQG 387
Cdd:cd01318 359 VRG 361
|
|
| PRK06189 |
PRK06189 |
allantoinase; Provisional |
2-406 |
2.22e-32 |
|
allantoinase; Provisional
Pssm-ID: 235732 [Multi-domain] Cd Length: 451 Bit Score: 129.05 E-value: 2.22e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034565965 2 VLPGGVDVHTRLQMPvlGMTPADDFCQGTKAALAGGTTMILDHVFPDTGVSLLA-AYEQWRERADSAACCDYSLHVDITR 80
Cdd:PRK06189 52 VFPGMIDVHVHFNEP--GRTHWEGFATGSAALAAGGCTTYFDMPLNSIPPTVTReALDAKAELARQKSAVDFALWGGLVP 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034565965 81 WHesiKEELEALVkEKGVNSFLVFMAYK--DRCQ-CSDSQMYEIFSIIRDLGALAQVHAENGDIVEEEQKRLLELGITGP 157
Cdd:PRK06189 130 GN---LEHLRELA-EAGVIGFKAFMSNSgtDEFRsSDDLTLYEGMKEIAALGKILALHAESDALTRHLTTQARQQGKTDV 205
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034565965 158 EGHVLSHPEEVEAEAVYRAVTIAKQANCPLYVTKVMSKGAADAIAQAKRRGVVV----------FGEPITASLGTdgshy 227
Cdd:PRK06189 206 RDYLESRPVVAELEAVQRALLYAQETGCPLHFVHISSGKAVALIAEAKKRGVDVsvetcphyllFTEEDFERIGA----- 280
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034565965 228 wsknWAKAAafvtsPPVNpDPTTADHLTCLLSSGDLQVTGSAHCTFTTAQKAvgKDNFALIPEGTNGIEERMSMVWEKCV 307
Cdd:PRK06189 281 ----VAKCA-----PPLR-SRSQKEELWRGLLAGEIDMISSDHSPCPPELKE--GDDFFLVWGGISGGQSTLLVMLTEGY 348
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034565965 308 ASGKMDENEFVAVTSTNAAKIFNFyPRKGRVAVGSDADLVIWNPKATKIISAKTHNLNVEYNIFEGVECRGAPAVVISQG 387
Cdd:PRK06189 349 IERGIPLETIARLLATNPAKRFGL-PQKGRLEVGADADFVLVDLDETYTLTKEDLFYRHKQSPYEGRTFPGRVVATYLRG 427
|
410
....*....|....*....
gi 1034565965 388 RVALEDGKmFVTPGAGRFV 406
Cdd:PRK06189 428 QCVYQDGE-VFPPPRGQLL 445
|
|
| DHOase_IIa |
cd01317 |
Dihydroorotase (DHOase), subgroup IIa; DHOases catalyze the reversible interconversion of ... |
2-361 |
6.59e-27 |
|
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: 111.95 E-value: 6.59e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034565965 2 VLPGGVDVHTRLQMPvlGMTPADDFCQGTKAALAGGTTMILdhVFPDTGVSL--LAAYEQWRERADSAACCDYSLHVDIT 79
Cdd:cd01317 12 LAPGLVDLHVHLREP--GFEYKETLESGAKAAAAGGFTTVV--CMPNTNPVIdnPAVVELLKNRAKDVGIVRVLPIGALT 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034565965 80 RwhESIKEELE--ALVKEKGVNSFlvfmAYKDRCQCSDSQMYEIFSIIRDLGALAQVHAENGDIVEE----EQKRLLELG 153
Cdd:cd01317 88 K--GLKGEELTeiGELLEAGAVGF----SDDGKPIQDAELLRRALEYAAMLDLPIIVHPEDPSLAGGgvmnEGKVASRLG 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034565965 154 ITGpeghvlsHPEEVEAEAVYRAVTIAKQANCPLYVTKVMSKGAADAIAQAKRRGVvvfgePITASLGtdgSHYWSKNWA 233
Cdd:cd01317 162 LPG-------IPPEAETIMVARDLELAEATGARVHFQHLSTARSLELIRKAKAKGL-----PVTAEVT---PHHLLLDDE 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034565965 234 KAAAFVTSPPVNP---DPTTADHLTCLLSSGDLQVTGSAHCTFTTAQKAVGkdnFALIPEGTNGIEERMSMVWEKCVASG 310
Cdd:cd01317 227 ALESYDTNAKVNPplrSEEDREALIEALKDGTIDAIASDHAPHTDEEKDLP---FAEAPPGIIGLETALPLLWTLLVKGG 303
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|.
gi 1034565965 311 KMDENEFVAVTSTNAAKIFNFYPrkGRVAVGSDADLVIWNPKATKIISAKT 361
Cdd:cd01317 304 LLTLPDLIRALSTNPAKILGLPP--GRLEVGAPADLVLFDPDAEWIVDEET 352
|
|
| Amidohydro_1 |
pfam01979 |
Amidohydrolase family; This family of enzymes are a a large metal dependent hydrolase ... |
1-389 |
1.26e-25 |
|
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: 107.59 E-value: 1.26e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034565965 1 MVLPGGVDVHTRLQMPVLGMTPADDFC------QGTKAALAGGTTMILDHVFPD-TGVSLL--AAYEQWRE-RADSAACC 70
Cdd:pfam01979 1 IVLPGLIDAHVHLEMGLLRGIPVPPEFayealrLGITTMLKSGTTTVLDMGATTsTGIEALleAAEELPLGlRFLGPGCS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034565965 71 ---DYSLHVDITRWHEsIKEELEALVKEKGVNSFLVFMAYKDRcQCSDSQMYEIFSIIRDLGALAQVHAENGDiveEEQK 147
Cdd:pfam01979 81 ldtDGELEGRKALREK-LKAGAEFIKGMADGVVFVGLAPHGAP-TFSDDELKAALEEAKKYGLPVAIHALETK---GEVE 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034565965 148 RLLELGITGPEghVLSHPEEVEAEAVYRAVTIAKQANCPLYVTkvmskGAADAIAQAKRRGVVvfgepitasLGTDGSHY 227
Cdd:pfam01979 156 DAIAAFGGGIE--HGTHLEVAESGGLLDIIKLILAHGVHLSPT-----EANLLAEHLKGAGVA---------HCPFSNSK 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034565965 228 WSKNWAKAAAfvtsppvnpdpttadhltcLLSSGDLQVTGSAHCtfttaqkaVGKDNFALIPEGTNGIEERMsmvwekcV 307
Cdd:pfam01979 220 LRSGRIALRK-------------------ALEDGVKVGLGTDGA--------GSGNSLNMLEELRLALELQF-------D 265
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034565965 308 ASGKMDENEFVAVTSTNAAKIFNFYPRKGRVAVGSDADLVIWNPKatkiisakthnlnvEYNIFEGVECRGAPAVVISQG 387
Cdd:pfam01979 266 PEGGLSPLEALRMATINPAKALGLDDKVGSIEVGKDADLVVVDLD--------------PLAAFFGLKPDGNVKKVIVKG 331
|
..
gi 1034565965 388 RV 389
Cdd:pfam01979 332 KI 333
|
|
| PRK08044 |
PRK08044 |
allantoinase AllB; |
1-407 |
1.12e-21 |
|
allantoinase AllB;
Pssm-ID: 169193 [Multi-domain] Cd Length: 449 Bit Score: 97.62 E-value: 1.12e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034565965 1 MVLPGGVDVHTRLQMPvlGMTPADDFCQGTKAALAGG-TTMIldhVFPDTGVSLLAAYEQWRERADSAaccDYSLHVDIT 79
Cdd:PRK08044 50 VVSPGMVDAHTHISEP--GRSHWEGYETGTRAAAKGGiTTMI---EMPLNQLPATVDRASIELKFDAA---KGKLTIDAA 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034565965 80 RWHESIKEELEAL--VKEKGVNSFLVFMAY-------KDRCQCSDSQMYEIFSIIRDLGALAQVHAENGDIVEEEQKRLL 150
Cdd:PRK08044 122 QLGGLVSYNLDRLheLDEVGVVGFKCFVATcgdrgidNDFRDVNDWQFYKGAQKLGELGQPVLVHCENALICDELGEEAK 201
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034565965 151 ELGITGPEGHVLSHPEEVEAEAVYRAVTIAKQANCPLYVTKVMSKGAADAIAQAKRRGVVVFGEPITaslgtdgsHYWSK 230
Cdd:PRK08044 202 REGRVTAHDYVASRPVFTEVEAIRRVLYLAKVAGCRLHVCHISSPEGVEEVTRARQEGQDVTCESCP--------HYFVL 273
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034565965 231 NWAKAAAFVT----SPPVNpDPTTADHLTCLLSSGDLQVTGSAHCTFTTAQKAvgkDNFALIPEGTNGIEERMSMVWEKC 306
Cdd:PRK08044 274 DTDQFEEIGTlakcSPPIR-DLENQKGMWEKLFNGEIDCLVSDHSPCPPEMKA---GNIMEAWGGIAGLQNCMDVMFDEA 349
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034565965 307 VASGKMDENEFVAVTSTNAAKIFNFyPRKGRVAVGSDADLVIWNPKATKIISAKTHNLNVEYNIFEGVECRGAPAVVISQ 386
Cdd:PRK08044 350 VQKRGMSLPMFGKLMATNAADIFGL-QQKGRIAPGKDADFVFIQPNSSYVLKNEDLEYRHKVSPYVGRTIGARITKTILR 428
|
410 420
....*....|....*....|.
gi 1034565965 387 GRVALEDGKMFVTPGAGRFVP 407
Cdd:PRK08044 429 GDVIYDIEQGFPVAPKGQFIL 449
|
|
| pyrC |
PRK09357 |
dihydroorotase; Validated |
2-393 |
5.84e-20 |
|
dihydroorotase; Validated
Pssm-ID: 236479 [Multi-domain] Cd Length: 423 Bit Score: 92.18 E-value: 5.84e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034565965 2 VLPGGVDVHTRLQMPvlGMTPADDFCQGTKAALAGGTTMIldHVFPDTG--VSLLAAYEQWRERADSAACCDysLHV--D 77
Cdd:PRK09357 51 VAPGLVDLHVHLREP--GQEDKETIETGSRAAAAGGFTTV--VAMPNTKpvIDTPEVVEYVLDRAKEAGLVD--VLPvgA 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034565965 78 ITRWHESiKE--ELEALVKEKgvnsflVFMAYKDRCQCSDSQ-MYEIFSIIRDLGALAQVHAENGDIVEE----EQKRLL 150
Cdd:PRK09357 125 ITKGLAG-EEltEFGALKEAG------VVAFSDDGIPVQDARlMRRALEYAKALDLLIAQHCEDPSLTEGgvmnEGEVSA 197
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034565965 151 ELGITGpeghvlsHPEEVEAEAVYRAVTIAKQANCPLYVTKVMSKGAADAIAQAKRRGVvvfgePITA------------ 218
Cdd:PRK09357 198 RLGLPG-------IPAVAEEVMIARDVLLAEATGARVHICHVSTAGSVELIRWAKALGI-----KVTAevtphhllltde 265
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034565965 219 SLGTDGSHYwsknwaKaaafvtsppVNPdP--TTADHLTCL--LSSGDLQVTGSAHCTFTTAQKAVGkdnFALIPEGTNG 294
Cdd:PRK09357 266 DLLTYDPNY------K---------VNP-PlrTEEDREALIegLKDGTIDAIATDHAPHAREEKECE---FEAAPFGITG 326
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034565965 295 IEERMSMVWEKCVASGKMDENEFVAVTSTNAAKIFNFYPrkGRVAVGSDADLVIWNPKATKIISAKTHNLNVEYNIFEGV 374
Cdd:PRK09357 327 LETALSLLYTTLVKTGLLDLEQLLEKMTINPARILGLPA--GPLAEGEPADLVIFDPEAEWTVDGEDFASKGKNTPFIGM 404
|
410
....*....|....*....
gi 1034565965 375 ECRGAPAVVISQGRVALED 393
Cdd:PRK09357 405 KLKGKVVYTIVDGKIVYQD 423
|
|
| PRK04250 |
PRK04250 |
dihydroorotase; Provisional |
1-394 |
4.56e-18 |
|
dihydroorotase; Provisional
Pssm-ID: 235265 [Multi-domain] Cd Length: 398 Bit Score: 85.98 E-value: 4.56e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034565965 1 MVLPGGVDVHTRLQmpvlgmtpadDFCQ--------GTKAALAGGTTMILDHvfPDTGVSLLAA--YEQWRERADSAACC 70
Cdd:PRK04250 44 IILPGLIDVHVHLR----------DFEEsyketiesGTKAALHGGITLVFDM--PNTKPPIMDEktYEKRMRIAEKKSYA 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034565965 71 DYSLHVDITRWHESIKEELEALVKEkgvnsflvFMAykdrcqcsdSQMYEIFS------IIRDLGALAqVHAENGDIVEE 144
Cdd:PRK04250 112 DYALNFLIAGNCEKAEEIKADFYKI--------FMG---------ASTGGIFSenfevdYACAPGIVS-VHAEDPELIRE 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034565965 145 EQKRllelgitgpeghvlshPEEVEAEAVYRAVTIAKQANCPLYVTKVMSKGAADAIAQAKRRGVVVFGEPitaslgtdg 224
Cdd:PRK04250 174 FPER----------------PPEAEVVAIERALEAGKKLKKPLHICHISTKDGLKLILKSNLPWVSFEVTP--------- 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034565965 225 SH--YWSKNWAKAAAFVTSPPVNpdptTADHLTCLLSSGD-LQVTGSAHCTFTTAQKAVGKdnfALIPegtnGIEERMSM 301
Cdd:PRK04250 229 HHlfLTRKDYERNPLLKVYPPLR----SEEDRKALWENFSkIPIIASDHAPHTLEDKEAGA---AGIP----GLETEVPL 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034565965 302 VWEkCVASGKMDENEFVAVTSTNAAKIFNFyPRKGrVAVGSDADLVIWNPKATKIISAKTHNLNVEYNIFEGVECRGAPA 381
Cdd:PRK04250 298 LLD-AANKGMISLFDIVEKMHDNPARIFGI-KNYG-IEEGNYANFAVFDMKKEWTIKAEELYTKAGWTPYEGFKLKGKVI 374
|
410
....*....|...
gi 1034565965 382 VVISQGRVALEDG 394
Cdd:PRK04250 375 MTILRGEVVMEDD 387
|
|
| PLN02795 |
PLN02795 |
allantoinase |
1-395 |
1.12e-17 |
|
allantoinase
Pssm-ID: 178392 [Multi-domain] Cd Length: 505 Bit Score: 85.60 E-value: 1.12e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034565965 1 MVLPGGVDVHTRLQMPvlGMTPADDFCQGTKAALAGGTTMILD---HVFPDTgvsllAAYEQWRERADSAAccdYSLHVD 77
Cdd:PLN02795 96 VVMPGLIDVHVHLNEP--GRTEWEGFPTGTKAAAAGGITTLVDmplNSFPST-----TSVETLELKIEAAK---GKLYVD 165
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034565965 78 ITRWHESIKE------ELEALVkEKGVNSFLVFM---AYKDRCQCSDSQMYEIFSIIRDLGALAQVHAENGDIVEEEQKr 148
Cdd:PLN02795 166 VGFWGGLVPEnahnasVLEELL-DAGALGLKSFMcpsGINDFPMTTATHIKAALPVLAKYGRPLLVHAEVVSPVESDSR- 243
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034565965 149 lLELGITGPEGHVLSHPEEVEAEAVYRAVTIAKQAN-------CPLYVTKVM-SKGAADAIAQAKRRGVVVFGEPITasl 220
Cdd:PLN02795 244 -LDADPRSYSTYLKSRPPSWEQEAIRQLLEVAKDTRpggvaegAHVHIVHLSdAESSLELIKEAKAKGDSVTVETCP--- 319
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034565965 221 gtdgsHYWsknwAKAAA--------FVTSPPVNpDPTTADHLTCLLSSGDLQVTGSAHCTFTTAQKAVGKDNFALIPEGT 292
Cdd:PLN02795 320 -----HYL----AFSAEeipdgdtrYKCAPPIR-DAANRELLWKALLDGDIDMLSSDHSPSPPDLKLLEEGNFLRAWGGI 389
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034565965 293 NGIEERMSMVWEKCVASGkMDENEFVAVTSTNAAKIFNFyPRKGRVAVGSDADLVIWNPKATKIISA------KTHNLNV 366
Cdd:PLN02795 390 SSLQFVLPATWTAGRAYG-LTLEQLARWWSERPAKLAGL-DSKGAIAPGKDADIVVWDPEAEFVLDEsypiyhKHKSLSP 467
|
410 420
....*....|....*....|....*....
gi 1034565965 367 eyniFEGVECRGAPAVVISQGRVALEDGK 395
Cdd:PLN02795 468 ----YLGTKLSGKVIATFVRGNLVFLEGK 492
|
|
| PRK09060 |
PRK09060 |
dihydroorotase; Validated |
2-406 |
1.81e-16 |
|
dihydroorotase; Validated
Pssm-ID: 181632 [Multi-domain] Cd Length: 444 Bit Score: 81.50 E-value: 1.81e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034565965 2 VLPGGVDVHTRLQMPvlGMTPADDFCQGTKAALAGGTTMILDhvFPDTGVSLL--AAYEQWRERADSAACCDYSLHVDIT 79
Cdd:PRK09060 54 VLPGVIDSQVHFREP--GLEHKEDLETGSRAAVLGGVTAVFE--MPNTNPLTTtaEALADKLARARHRMHCDFAFYVGGT 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034565965 80 rwHESIkEELEALVKEKGVNSFLVFM--AYKDRCQCSDSQMYEIFSIIRDLGAlaqVHAEngdivEEEqkRLLELGITGP 157
Cdd:PRK09060 130 --RDNA-DELAELERLPGCAGIKVFMgsSTGDLLVEDDEGLRRILRNGRRRAA---FHSE-----DEY--RLRERKGLRV 196
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034565965 158 EGHVLSHP----EEVEAEAVYRAVTIAKQANCPLYVTKVMSKGAADAIAQAKRRGVV--------VFGEPITASLGTdgs 225
Cdd:PRK09060 197 EGDPSSHPvwrdEEAALLATRRLVRLARETGRRIHVLHVSTAEEIDFLADHKDVATVevtphhltLAAPECYERLGT--- 273
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034565965 226 hYWSKNwakaaafvtsPPVNpDPTTADHLTCLLSSGDLQVTGSAHCTFTTAQKAvgkDNFALIPEGTNGIEERMSMVWEK 305
Cdd:PRK09060 274 -LAQMN----------PPIR-DARHRDGLWRGVRQGVVDVLGSDHAPHTLEEKA---KPYPASPSGMTGVQTLVPIMLDH 338
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034565965 306 cVASGKMDENEFVAVTSTNAAKIFNFyPRKGRVAVGSDADLVIWNPKATKIISAKTHNLNVEYNIFEGVECRGAPAVVIS 385
Cdd:PRK09060 339 -VNAGRLSLERFVDLTSAGPARIFGI-AGKGRIAVGYDADFTIVDLKRRETITNEWIASRCGWTPYDGKEVTGWPVGTIV 416
|
410 420
....*....|....*....|.
gi 1034565965 386 QGRVALEDGKMfVTPGAGRFV 406
Cdd:PRK09060 417 RGQRVMWDGEL-VGPPTGEPV 436
|
|
| PRK01211 |
PRK01211 |
dihydroorotase; Provisional |
2-408 |
5.70e-15 |
|
dihydroorotase; Provisional
Pssm-ID: 179247 [Multi-domain] Cd Length: 409 Bit Score: 76.82 E-value: 5.70e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034565965 2 VLPGGVDVHTRLQMPvlGMTPADDFCQGTKAALAGGTTMILDhvFPDTGVSL--LAAYEQWRERADSAACCDYSLHvdit 79
Cdd:PRK01211 44 ILPAATDIHVHFRTP--GETEKEDFSTGTLSAIFGGTTFIMD--MPNNNIPIkdYNAFSDKLGRVAPKAYVDFSLY---- 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034565965 80 rwheSIKEELEALVKEKGVNSFLVFMAYKDRCQCSDSQMYEIfSIIRDLGALAQVHAENGDIVEE---EQKRLLElgitg 156
Cdd:PRK01211 116 ----SMETGNNALILDERSIGLKVYMGGTTNTNGTDIEGGEI-KKINEANIPVFFHAELSECLRKhqfESKNLRD----- 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034565965 157 pegHVLSHPEEVEAEAVYRAVTIAKQANCPLYVTKVMSKGaaDAIAQAKRRGVVVFGEpitASLGTDGShywsknwakaa 236
Cdd:PRK01211 186 ---HDLARPIECEIKAVKYVKNLDLKTKIIAHVSSIDVIG--RFLREVTPHHLLLNDD---MPLGSYGK----------- 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034565965 237 afvTSPPVNpDPTTADHLTCLLSSGDLQVTGSAHCTFTTAQKAvgkdNFALIPEGTNGIEERMSMVWeKCVASGKMDENE 316
Cdd:PRK01211 247 ---VNPPLR-DRWTQERLLEEYISGRFDILSSDHAPHTEEDKQ----EFEYAKSGIIGVETRVPLFL-ALVKKKILPLDV 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034565965 317 FVAVTSTNAAKIFNFypRKGRVAVGSDADLVIWNPKATKIISAKTHNLNVEYNIFEGVECRgAPAVVISQGRVALEDGKM 396
Cdd:PRK01211 318 LYKTAIERPASLFGI--KKGKIEEGYDADFMAFDFTNIKKINDKRLHSKCPVSPFNGFDAI-FPSHVIMRGEVVIDNYEL 394
|
410
....*....|..
gi 1034565965 397 FVTPgAGRFVPR 408
Cdd:PRK01211 395 ISER-TGKFVPK 405
|
|
| PRK07575 |
PRK07575 |
dihydroorotase; Provisional |
1-395 |
6.86e-12 |
|
dihydroorotase; Provisional
Pssm-ID: 236055 [Multi-domain] Cd Length: 438 Bit Score: 67.39 E-value: 6.86e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034565965 1 MVLPGGVD--VHTRlqMPvlGMTPADDFCQGTKAALAGGTTMILDhvFPDTG--VSLLAAYEQWRERADSAACCDYSLHV 76
Cdd:PRK07575 53 TLLPGVIDpqVHFR--EP--GLEHKEDLFTASRACAKGGVTSFLE--MPNTKplTTTQAALDDKLARAAEKCVVNYGFFI 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034565965 77 DITrwhesiKEELEALVKEKGVNSFLVFM--AYKDRCQCSDSQMYEIFSIIRDLGAlaqVHAENGDIVEEEQKRLLelGI 154
Cdd:PRK07575 127 GAT------PDNLPELLTANPTCGIKIFMgsSHGPLLVDEEAALERIFAEGTRLIA---VHAEDQARIRARRAEFA--GI 195
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034565965 155 TGPEGHVLSHPEEVEAEAVYRAVTIAKQANCPLYVTKVMSKGAADAIAQAKRRGVVVFGEPitaslgtdgsHYWSKNWAK 234
Cdd:PRK07575 196 SDPADHSQIQDEEAALLATRLALKLSKKYQRRLHILHLSTAIEAELLRQDKPSWVTAEVTP----------QHLLLNTDA 265
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034565965 235 AAAFVTSPPVNPDPTTADHLTCL---LSSGDLQVTGSAHCTFTTAQKAVGkdnFALIPEGTNGIEERMSMVWEKCVAsGK 311
Cdd:PRK07575 266 YERIGTLAQMNPPLRSPEDNEALwqaLRDGVIDFIATDHAPHTLEEKAQP---YPNSPSGMPGVETSLPLMLTAAMR-GK 341
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034565965 312 MDENEFVAVTSTNAAKIFNFyPRKGRVAVGSDADLVIWNPKATKIISAKTHNLNVEYNIFEGVECRGAPAVVISQGRVAL 391
Cdd:PRK07575 342 CTVAQVVRWMSTAVARAYGI-PNKGRIAPGYDADLVLVDLNTYRPVRREELLTKCGWSPFEGWNLTGWPVTTIVGGQIVF 420
|
....
gi 1034565965 392 EDGK 395
Cdd:PRK07575 421 DRGQ 424
|
|
| CAD_DHOase |
cd01316 |
The eukaryotic CAD protein is a trifunctional enzyme of carbamoylphosphate ... |
3-403 |
1.51e-10 |
|
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: 62.47 E-value: 1.51e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034565965 3 LPGGVDVHTRLqmPVLGMTPADDFCQGTKAALAGGTTMILdhVFPDTGVSLL--AAYEQWRERADSAACCDYSLHVDITR 80
Cdd:cd01316 5 LPGLIDVHVHL--REPGATHKEDFASGTKAALAGGFTMVR--AMPNTNPSIVdvASLKLVQSLAQAKARCDYAFSIGATS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034565965 81 WHESIKEELEAlvkekgvnsflvfmaykdrcQCSDSQMYeifsiirdlgalaqvhaengdiVEEEQKRLLELGITGPEGH 160
Cdd:cd01316 81 TNAATVGELAS--------------------EAVGLKFY----------------------LNETFSTLILDKITAWASH 118
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034565965 161 VLSHPEE----VEAEAVYRAVTI--AKQANCPLYVTKVMSKGAADAIAQAKRRGVVVFGEPITASLgtdgshYWSKNWAK 234
Cdd:cd01316 119 FNAWPSTkpivTHAKSQTLAAVLllASLHNRSIHICHVSSKEEINLIRLAKARGLKVTCEVSPHHL------FLSQDDLP 192
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034565965 235 AAAFvtspPVNPDPTTADHLTCL---LSSGDLQVTGSAhcTFTTAQKAVGKdnfalIPEGTNGIEERMSMVWeKCVASGK 311
Cdd:cd01316 193 RGQY----EVRPFLPTREDQEALwenLDYIDCFATDHA--PHTLAEKTGNK-----PPPGFPGVETSLPLLL-TAVHEGR 260
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034565965 312 MDENEFVAVTSTNAAKIFNFYPRKGrVAVGSDADlVIWNPKATKIISAKthnlnvEYNIFEGVECRGAPAVVISQGRVAL 391
Cdd:cd01316 261 LTIEDIVDRLHTNPKRIFNLPPQSD-TYVEVDLD-EEWTIPKNPLQSKK------GWTPFEGKKVKGKVQRVVLRGETAF 332
|
410
....*....|..
gi 1034565965 392 EDGKMFVTPGAG 403
Cdd:cd01316 333 IDGEIVAPPGFG 344
|
|
| pyrC |
PRK00369 |
dihydroorotase; Provisional |
1-403 |
1.18e-07 |
|
dihydroorotase; Provisional
Pssm-ID: 234738 [Multi-domain] Cd Length: 392 Bit Score: 54.00 E-value: 1.18e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034565965 1 MVLPGGVDVHTRLQMpvLGMTPADDFCQGTKAALAGGTTMILDhvFPDTgVSLLAAYEQWRERADSAAC---CDYSLHVD 77
Cdd:PRK00369 44 LILPGAIDLHVHLRG--LKLSYKEDVASGTSEAAYGGVTLVAD--MPNT-IPPLNTPEAITEKLAELEYysrVDYFVYSG 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034565965 78 ITRWHESIKEelealvkekgvnsfLVFMAYKdrcqcsdsqmyeifsiirdlgalaqVHAEngDIVEEEQKRLLElgitgp 157
Cdd:PRK00369 119 VTKDPEKVDK--------------LPIAGYK-------------------------IFPE--DLEREETFRVLL------ 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034565965 158 EGHVLS--HPEEVEAEAVYRAVtiakQANCPLYVTKVMS-KGAADA-IAQAKRRGVVVFGEPITASlgTDGS-HYWSKNW 232
Cdd:PRK00369 152 KSRKLKilHPEVPLALKSNRKL----RRNCWYEIAALYYvKDYQNVhITHASNPRTVRLAKELGFT--VDITpHHLLVNG 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034565965 233 AKAAAFVTSPPVNpDPTTADHLTCLLSSGDLQVtgSAHCTFTTAQKavgKDNFALIPEGTNGIEERMSMVWeKCVASGKM 312
Cdd:PRK00369 226 EKDCLTKVNPPIR-DINERLWLLQALSEVDAIA--SDHAPHSSFEK---LQPYEVCPPGIAALSFTPPFIY-TLVSKGIL 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034565965 313 DENEFVAVTSTNAAKIFNFypRKGRVAVGSDADLVIWNPKATKIISAKThnlNVEYNIFEGVECRGAPAVVISQGRVALE 392
Cdd:PRK00369 299 SIDRAVELISTNPARILGI--PYGEIKEGYRANFTVIQFEDWRYSTKYS---KVIETPLDGFELKASVYATIVQGKLAYL 373
|
410
....*....|.
gi 1034565965 393 DGKmfVTPGAG 403
Cdd:PRK00369 374 EGE--VFPVKG 382
|
|
| PRK07369 |
PRK07369 |
dihydroorotase; Provisional |
165-361 |
3.42e-06 |
|
dihydroorotase; Provisional
Pssm-ID: 236002 [Multi-domain] Cd Length: 418 Bit Score: 49.21 E-value: 3.42e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034565965 165 PEEVEAEAVYRAVTIAKQANCPLYVTKVMSKGAADAIAQAKRRGVvvfgePITAS-------LGT-DGSHYwSKNWAKAa 236
Cdd:PRK07369 208 PASAETTALAALLELVAAIGTPVHLMRISTARSVELIAQAKARGL-----PITASttwmhllLDTeALASY-DPNLRLD- 280
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034565965 237 afvtsPPV-NPDPTTAdhLTCLLSSGDLQVTGSAHCTFTTAQKAVGkdnFALIPEGTNGIEERMSMVWEKCVASGKMDEN 315
Cdd:PRK07369 281 -----PPLgNPSDRQA--LIEGVRTGVIDAIAIDHAPYTYEEKTVA---FAEAPPGAIGLELALPLLWQNLVETGELSAL 350
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1034565965 316 EFVAVTSTNAAKIFNFYPRkgRVAVGSDADLVIWNPKATKIISAKT 361
Cdd:PRK07369 351 QLWQALSTNPARCLGQEPP--SLAPGQPAELILFDPQKTWTVSAQT 394
|
|
| Amidohydro_3 |
pfam07969 |
Amidohydrolase family; |
308-374 |
6.15e-05 |
|
Amidohydrolase family;
Pssm-ID: 400360 [Multi-domain] Cd Length: 464 Bit Score: 45.60 E-value: 6.15e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1034565965 308 ASGKMDENEFVAVTSTNAAKIFNFYPRKGRVAVGSDADLVIWNPKATKIISAKTHNLNVEYNIFEGV 374
Cdd:pfam07969 395 PDEELSLEEALALYTSGPAKALGLEDRKGTLGVGKDADLVVLDDDPLTVDPPAIADIRVRLTVVDGR 461
|
|
| NagA |
cd00854 |
N-acetylglucosamine-6-phosphate deacetylase, NagA, catalyzes the hydrolysis of the N-acetyl ... |
318-373 |
2.44e-04 |
|
N-acetylglucosamine-6-phosphate deacetylase, NagA, catalyzes the hydrolysis of the N-acetyl group of N-acetyl-glucosamine-6-phosphate (GlcNAc-6-P) to glucosamine 6-phosphate and acetate. This is the first committed step in the biosynthetic pathway to amino-sugar-nucleotides, which is needed for cell wall peptidoglycan and teichoic acid biosynthesis. Deacetylation of N-acetylglucosamine is also important in lipopolysaccharide synthesis and cell wall recycling.
Pssm-ID: 238434 [Multi-domain] Cd Length: 374 Bit Score: 43.34 E-value: 2.44e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 1034565965 318 VAVTSTNAAKIFNFYPRKGRVAVGSDADLVIWNPkatkiisakthNLNVEYNIFEG 373
Cdd:cd00854 330 VRMASLNPAKLLGLDDRKGSLKPGKDADLVVLDD-----------DLNVKATWING 374
|
|
| SsnA |
COG0402 |
Cytosine/adenosine deaminase or related metal-dependent hydrolase [Nucleotide transport and ... |
2-225 |
2.48e-04 |
|
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: 43.28 E-value: 2.48e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034565965 2 VLPGGVDVHTRL-QMPVLGMTPADDFCQ--------------------GTKAA----LAGGTTMILDH--VFPDTGVSLL 54
Cdd:COG0402 57 VLPGLVNTHTHLpQTLLRGLADDLPLLDwleeyiwplearldpedvyaGALLAlaemLRSGTTTVADFyyVHPESADALA 136
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034565965 55 AAYEQWRERADSA-ACCDYSLHVDITRWHESIKEELEALVKEkgvnsflVFMAYKDRCQ----------CSDSQMYEIFS 123
Cdd:COG0402 137 EAAAEAGIRAVLGrGLMDRGFPDGLREDADEGLADSERLIER-------WHGAADGRIRvalaphapytVSPELLRAAAA 209
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034565965 124 IIRDLGALAQVH-----AENGDIVEEEQKR----LLELGITGPeGHVLSH-----PEEVE--AEavyRAVTIakqANCP- 186
Cdd:COG0402 210 LARELGLPLHTHlaetrDEVEWVLELYGKRpveyLDELGLLGP-RTLLAHcvhltDEEIAllAE---TGASV---AHCPt 282
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 1034565965 187 --LYvtkvMSKGAADaIAQAKRRGVVVfgepitaSLGTDGS 225
Cdd:COG0402 283 snLK----LGSGIAP-VPRLLAAGVRV-------GLGTDGA 311
|
|
| Met_dep_hydrolase_C |
cd01309 |
Metallo-dependent hydrolases, subgroup C is part of the superfamily of metallo-dependent ... |
305-350 |
1.08e-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: 41.14 E-value: 1.08e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 1034565965 305 KCVASGKMDENEFVAVTStNAAKIFNFYPRKGRVAVGSDADLVIWN 350
Cdd:cd01309 294 KAVKYGLSYEEALKAITI-NPAKILGIEDRVGSLEPGKDADLVVWN 338
|
|
| HutI |
COG1228 |
Imidazolonepropionase or related amidohydrolase [Secondary metabolites biosynthesis, transport ... |
279-374 |
5.62e-03 |
|
Imidazolonepropionase or related amidohydrolase [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 440841 [Multi-domain] Cd Length: 386 Bit Score: 39.17 E-value: 5.62e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034565965 279 AVGKDNFALIPEGTNgieerMSMVWEKCVASGkMDENE-FVAVTStNAAKIFNFYPRKGRVAVGSDADLVIWNPKATKII 357
Cdd:COG1228 295 ALGTDAGVGVPPGRS-----LHRELALAVEAG-LTPEEaLRAATI-NAAKALGLDDDVGSLEPGKLADLVLLDGDPLEDI 367
|
90
....*....|....*..
gi 1034565965 358 SAKTHnlnVEYNIFEGV 374
Cdd:COG1228 368 AYLED---VRAVMKDGR 381
|
|
|