|
Name |
Accession |
Description |
Interval |
E-value |
| D-HYD |
cd01314 |
D-hydantoinases (D-HYD) also called dihydropyrimidases (DHPase) and related proteins; DHPases ... |
17-466 |
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: 703.59 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131245802 17 LLIRGGKIVNDDQSFHADLYVEDGLIKQIGENLIVPG*IRTIDAHGLLVLPGGVDVHTRLLMPVLGMTPADDFCQGTKAA 96
Cdd:cd01314 1 LIIKNGTIVTADGSFKADILIEDGKIVAIGPNLEAPGGVEVIDATGKYVLPGGIDPHTHLELPFMGTVTADDFESGTRAA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131245802 97 LAGGTTMILDHVFPEAGVSLLAAYEQWRERADGGACCDYSLHVDIPRWHESTREELEALVrDKGVNSFLVFMAYKDRHQC 176
Cdd:cd01314 81 AAGGTTTIIDFAIPNKGQSLLEAVEKWRGKADGKSVIDYGFHMIITDWTDSVIEELPELV-KKGISSFKVFMAYKGLLMV 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131245802 177 TDGQIYEIFSVIRDLGAVAQVHAENGDIVDEEQKRLLELGVTGPEGHVLSHPEEVEAEAVYRAITIARQASCPLYVTKVM 256
Cdd:cd01314 160 DDEELLDVLKRAKELGALVMVHAENGDVIAELQKKLLAQGKTGPEYHALSRPPEVEAEATARAIRLAELAGAPLYIVHVS 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131245802 257 SK*AADVIARAKRRGVVVFGEPITAGLGADGSHYWsKNWAKAAAFVTSPPISPDpSTADHLTALLSSGDLQVTGSAHCTF 336
Cdd:cd01314 240 SKEAADEIARARKKGLPVYGETCPQYLLLDDSDYW-KDWFEGAKYVCSPPLRPK-EDQEALWDGLSSGTLQTVGSDHCPF 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131245802 337 TTAQKAVGRDNFTLIPEGTNGVEERMSVVWEKCVASGQMDENEFVAVTSTNAAKIFNFYPRKGRVAVGSDADLVIWNPRA 416
Cdd:cd01314 318 NFAQKARGKDDFTKIPNGVPGVETRMPLLWSEGVAKGRITLEKFVELTSTNPAKIFGLYPRKGTIAVGSDADLVIWDPNA 397
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|
gi 1131245802 417 TRIISAKSHSLNVEYNIFEGLECRGAPSVVISQGRVVLEDGALCVTPGTG 466
Cdd:cd01314 398 EKTISADTHHHNVDYNIFEGMKVKGWPVVTISRGKVVVEDGELVGEKGSG 447
|
|
| D-hydantoinase |
TIGR02033 |
D-hydantoinase; This model represents the D-hydantoinase (dihydropyrimidinase) which primarily ... |
17-471 |
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 1131245802 17 LLIRGGKIVNDDQSFHADLYVEDGLIKQIGENLIVPG*IRTIDAHGLLVLPGGVDVHTRLLMPVLGMTPADDFCQGTKAA 96
Cdd:TIGR02033 1 LLIKGGTVVNADDVFQADVLIEGGKIVAVGDNLIPPDAVEVIDATGKYVLPGGIDVHTHLEMPFGGTTTADDFFTGTKAA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131245802 97 LAGGTTMILDHVFPEAGVSLLAAYEQWRERADGGACCDYSLHVDIPRWHESTREELEALVRDKGVNSFLVFMAYKDRHQC 176
Cdd:TIGR02033 81 AAGGTTTIIDFVVPEKGSSLTEALETWHEKAEGKSVIDYGFHMDITHWNDSVLEEHIPEVKEEGINSFKVFMAYKNLLMV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131245802 177 TDGQIYEIFSVIRDLGAVAQVHAENGDIVDEEQKRLLELGVTGPEGHVLSHPEEVEAEAVYRAITIARQASCPLYVTKVM 256
Cdd:TIGR02033 161 DDEELFEILKRLKELGALLQVHAENGDIIAELQARMLAQGITGPEYHALSRPPELEAEAVARAITLAALADAPLYVVHVS 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131245802 257 SK*AADVIARAKRRGVVVFGEPITAGLGADGSHYWsKNWAKAAAFVTSPPISpDPSTADHLTALLSSGDLQVTGSAHCTF 336
Cdd:TIGR02033 241 TKDAADEIAQARKKGQPVFGETCPQYLVLDDTHYD-KPGFEGAKYVCSPPLR-EPEDQDALWSALSSGALQTVGSDHCTF 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131245802 337 TTAQK-AVGRDNFTLIPEGTNGVEERMSVVWEKCVASGQMDENEFVAVTSTNAAKIFNFYPRKGRVAVGSDADLVIWNPR 415
Cdd:TIGR02033 319 NFAQKkAIGKDDFTKIPNGGPGVEERMSLLFDEGVAKGRITLEKFVEVTSTNPAKIFNLYPRKGTIAVGSDADIVIWDPN 398
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*.
gi 1131245802 416 ATRIISAKSHSLNVEYNIFEGLECRGAPSVVISQGRVVLEDGALCVTPGTGRFIPR 471
Cdd:TIGR02033 399 RTTVISAETHHSNADYNPFEGFKVRGAPVSVLSRGRVVVEDGQLVGTAGAGRFVKR 454
|
|
| PRK08323 |
PRK08323 |
phenylhydantoinase; Validated |
16-475 |
0e+00 |
|
phenylhydantoinase; Validated
Pssm-ID: 236240 [Multi-domain] Cd Length: 459 Bit Score: 562.49 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131245802 16 RLLIRGGKIVNDDQSFHADLYVEDGLIKQIGENlivpG*IRTIDAHGLLVLPGGVDVHTRLLMPVLGMTPADDFCQGTKA 95
Cdd:PRK08323 2 STLIKNGTVVTADDTYKADVLIEDGKIAAIGAN----LGDEVIDATGKYVMPGGIDPHTHMEMPFGGTVSSDDFETGTRA 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131245802 96 ALAGGTTMILDHVFPEAGVSLLAAYEQWRERADGGACCDYSLHVDIPRWHESTREELEALVrDKGVNSFLVFMAYKDRHQ 175
Cdd:PRK08323 78 AACGGTTTIIDFALQPKGQSLREALEAWHGKAAGKAVIDYGFHMIITDWNEVVLDEMPELV-EEGITSFKLFMAYKGALM 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131245802 176 CTDGQIYEIFSVIRDLGAVAQVHAENGDIVDEEQKRLLELGVTGPEGHVLSHPEEVEAEAVYRAITIARQASCPLYVTKV 255
Cdd:PRK08323 157 LDDDELLRALQRAAELGALPMVHAENGDAIAYLQAKLLAEGKTGPEYHALSRPPEVEGEATNRAIMLAELAGAPLYIVHV 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131245802 256 MSK*AADVIARAKRRGVVVFGEPITAGLGADGSHYWSKNWAKAAAFVTSPPISPdPSTADHLTALLSSGDLQVTGSAHCT 335
Cdd:PRK08323 237 SCKEALEAIRRARARGQRVFGETCPQYLLLDESEYDGPDWFEGAKYVMSPPLRD-KEHQDALWRGLQDGDLQVVATDHCP 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131245802 336 FTTAQKA-VGRDNFTLIPEGTNGVEERMSVVWEKCVASGQMDENEFVAVTSTNAAKIFNFYPRKGRVAVGSDADLVIWNP 414
Cdd:PRK08323 316 FCFEQKKqLGRGDFTKIPNGTPGVEDRMPLLFSEGVMTGRITLNRFVELTSTNPAKIFGLYPRKGTIAVGADADIVIWDP 395
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1131245802 415 RATRIISAKSHSLNVEYNIFEGLECRGAPSVVISQGRVVLEDGALCVTPGTGRFIPRKTFP 475
Cdd:PRK08323 396 NATKTISASTLHSNVDYNPYEGFEVTGWPVTTLSRGEVVVEDGEFRGKAGHGRFLKRKPFQ 456
|
|
| PLN02942 |
PLN02942 |
dihydropyrimidinase |
12-486 |
0e+00 |
|
dihydropyrimidinase
Pssm-ID: 178530 Cd Length: 486 Bit Score: 544.05 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131245802 12 ITSDRLLIRGGKIVNDDQSFHADLYVEDGLIKQIGENLIVPG*IRTIDAHGLLVLPGGVDVHTRLLMPVLGMTPADDFCQ 91
Cdd:PLN02942 2 ASSTKILIKGGTVVNAHHQELADVYVEDGIIVAVAPNLKVPDDVRVIDATGKFVMPGGIDPHTHLAMPFMGTETIDDFFS 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131245802 92 GTKAALAGGTTMILDHVFPEAGvSLLAAYEQWRERADGgACCDYSLHVDIPRWHESTREELEALVRDKGVNSFLVFMAYK 171
Cdd:PLN02942 82 GQAAALAGGTTMHIDFVIPVNG-NLLAGYEAYEKKAEK-SCMDYGFHMAITKWDDTVSRDMETLVKEKGINSFKFFMAYK 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131245802 172 DRHQCTDGQIYEIFSVIRDLGAVAQVHAENGDIVDEEQKRLLELGVTGPEGHVLSHPEEVEAEAVYRAITIARQASCPLY 251
Cdd:PLN02942 160 GSLMVTDELLLEGFKRCKSLGALAMVHAENGDAVFEGQKRMIELGITGPEGHALSRPPLLEGEATARAIRLAKFVNTPLY 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131245802 252 VTKVMSK*AADVIARAKRRGVVVFGEPITAGLGADGSHYWSKNWAKAAAFVTSPPISPdpstADH---LTALLSSGDLQV 328
Cdd:PLN02942 240 VVHVMSIDAMEEIARARKSGQRVIGEPVVSGLVLDDSKLWDPDFTIASKYVMSPPIRP----AGHgkaLQAALSSGILQL 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131245802 329 TGSAHCTFTTAQKAVGRDNFTLIPEGTNGVEERMSVVWEKCVASGQMDENEFVAVTSTNAAKIFNFYPRKGRVAVGSDAD 408
Cdd:PLN02942 316 VGTDHCPFNSTQKAFGKDDFRKIPNGVNGIEERMHLVWDTMVESGQISPTDYVRVTSTECAKIFNIYPRKGAILAGSDAD 395
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1131245802 409 LVIWNPRATRIISAKSHSLNVEYNIFEGLECRGAPSVVISQGRVVLEDGALCVTPGTGRFIPRKTFPdFVYKRIKARN 486
Cdd:PLN02942 396 IIILNPNSTFTISAKTHHSRIDTNVYEGRRGKGKVEVTISQGRVVWENGELKVVRGSGRYIEMPPFS-YLFDGIQKAD 472
|
|
| AllB |
COG0044 |
Dihydroorotase or related cyclic amidohydrolase [Nucleotide transport and metabolism]; ... |
18-471 |
1.22e-123 |
|
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: 370.96 E-value: 1.22e-123
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131245802 18 LIRGGKIVNDDQSFHADLYVEDGLIKQIGENLIVPG*IRTIDAHGLLVLPGGVDVHTRLLMPvlGMTPADDFCQGTKAAL 97
Cdd:COG0044 1 LIKNGRVVDPGGLERADVLIEDGRIAAIGPDLAAPEAAEVIDATGLLVLPGLIDLHVHLREP--GLEHKEDIETGTRAAA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131245802 98 AGGTTMILDHVFPEAGVSLLAAYEQWRERADGGACCDYSLHVDIPRWHESTREELEALVrDKGVNSFLVFMAYKDRHQCT 177
Cdd:COG0044 79 AGGVTTVVDMPNTNPVTDTPEALEFKLARAEEKALVDVGPHGALTKGLGENLAELGALA-EAGAVAFKVFMGSDDGNPVL 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131245802 178 D-GQIYEIFSVIRDLGAVAQVHAENGDIVDEeqkRLLELGVTGPEGHVLSHPEEVEAEAVYRAITIARQASCPLYVTKVM 256
Cdd:COG0044 158 DdGLLRRALEYAAEFGALVAVHAEDPDLIRG---GVMNEGKTSPRLGLKGRPAEAEEEAVARDIALAEETGARLHIVHVS 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131245802 257 SK*AADVIARAKRRGVVVFGE--PitaglgadgsHYWS---KNWAK-AAAFVTSPPIspdpSTADHLTAL---LSSGDLQ 327
Cdd:COG0044 235 TAEAVELIREAKARGLPVTAEvcP----------HHLTltdEDLERyGTNFKVNPPL----RTEEDREALwegLADGTID 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131245802 328 VTGSAHCTFTTAQKavgRDNFTLIPEGTNGVEERMSVVWEKCVASGQMDENEFVAVTSTNAAKIFNFyPRKGRVAVGSDA 407
Cdd:COG0044 301 VIATDHAPHTLEEK---ELPFAEAPNGIPGLETALPLLLTELVHKGRLSLERLVELLSTNPARIFGL-PRKGRIAVGADA 376
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1131245802 408 DLVIWNPRATRIISAKS-HSlNVEYNIFEGLECRGAPSVVISQGRVVLEDGALCVTPgTGRFIPR 471
Cdd:COG0044 377 DLVLFDPDAEWTVTAEDlHS-KSKNTPFEGRELTGRVVATIVRGRVVYEDGEVVGEP-RGRFLRR 439
|
|
| PRK13404 |
PRK13404 |
dihydropyrimidinase; Provisional |
17-473 |
1.38e-119 |
|
dihydropyrimidinase; Provisional
Pssm-ID: 184033 [Multi-domain] Cd Length: 477 Bit Score: 362.09 E-value: 1.38e-119
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131245802 17 LLIRGGKIVNDDQSFHADLYVEDGLIKQIGENLivPG*IRTIDAHGLLVLPGGVDVHTRLLMPV-LGMTPADDFCQGTKA 95
Cdd:PRK13404 6 LVIRGGTVVTATDTFQADIGIRGGRIAALGEGL--GPGAREIDATGRLVLPGGVDSHCHIDQPSgDGIMMADDFYTGTVS 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131245802 96 ALAGGTTMILDHVFPEAGVSLLAAYEQWRERADGGACCDYSLHVDIPRWHEST-REELEALVRDkGVNSFLVFMAYkDRH 174
Cdd:PRK13404 84 AAFGGTTTVIPFAAQHRGQSLREAVEDYHRRAAGKAVIDYAFHLIVADPTEEVlTEELPALIAQ-GYTSFKVFMTY-DDL 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131245802 175 QCTDGQIYEIFSVIRDLGAVAQVHAENGDIVDEEQKRLLELGVTGPEGHVLSHPEEVEAEAVYRAITIARQASCPLYVTK 254
Cdd:PRK13404 162 KLDDRQILDVLAVARRHGAMVMVHAENHDMIAWLTKRLLAAGLTAPKYHAISRPMLAEREATHRAIALAELVDVPILIVH 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131245802 255 VMSK*AADVIARAKRRGVVVFGEP------ITA-GLGADGSHywsknwakAAAFVTSPPispdPSTADHLTAL---LSSG 324
Cdd:PRK13404 242 VSGREAAEQIRRARGRGLKIFAETcpqylfLTAeDLDRPGME--------GAKYICSPP----PRDKANQEAIwngLADG 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131245802 325 DLQVTGSAHCTF---TTAQKAVGRDN--FTLIPEGTNGVEERMSVVWEKCVASGQMDENEFVAVTSTNAAKIFNFYPRKG 399
Cdd:PRK13404 310 TFEVFSSDHAPFrfdDTDGKLAAGANpsFKAIANGIPGIETRLPLLFSEGVVKGRISLNRFVALTSTNPAKLYGLYPRKG 389
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1131245802 400 RVAVGSDADLVIWNPRATRIISAKSHSLNVEYNIFEGLECRGAPSVVISQGRVVLEDGALCVTPGTGRFIPRKT 473
Cdd:PRK13404 390 AIAIGADADIAIWDPDREVTITNADLHHAADYTPYEGMRVTGWPVTVLSRGRVVVEDGELVAERGSGQFLARSL 463
|
|
| L-HYD_ALN |
cd01315 |
L-Hydantoinases (L-HYDs) and Allantoinase (ALN); L-Hydantoinases are a member of the ... |
17-469 |
2.67e-60 |
|
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: 206.37 E-value: 2.67e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131245802 17 LLIRGGKIVNDDQSFHADLYVEDGLIKQIGENLIVPG*IRTIDAHGLLVLPGGVDVHTRLLMPvlGMTPADDFCQGTKAA 96
Cdd:cd01315 2 LVIKNGRVVTPDGVREADIAVKGGKIAAIGPDIANTEAEEVIDAGGLVVMPGLIDTHVHINEP--GRTEWEGFETGTKAA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131245802 97 LAGGTTMILD---HVFPEA--GVSLLAAYEQWRERadggaccdysLHVDIPRWHESTR---EELEALVrDKGVNSFLVFM 168
Cdd:cd01315 80 AAGGITTIIDmplNSIPPTttVENLEAKLEAAQGK----------LHVDVGFWGGLVPgnlDQLRPLD-EAGVVGFKCFL 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131245802 169 A---YKDRHQCTDGQIYEIFSVIRDLGAVAQVHAENGDIVDEEQKRLLELGVTGPEGHVLSHPEEVEAEAVYRAITIARQ 245
Cdd:cd01315 149 CpsgVDEFPAVDDEQLEEAMKELAKTGSVLAVHAENPEITEALQEQAKAKGKRDYRDYLASRPVFTEVEAIQRILLLAKE 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131245802 246 ASCPLYVTKVMSK*AADVIARAKRRGVVVFGEPITaglgadgsHYWS-------KNwakAAAFVTSPPISpDPSTADHLT 318
Cdd:cd01315 229 TGCRLHIVHLSSAEAVPLIREARAEGVDVTVETCP--------HYLTftaedvpDG---GTEFKCAPPIR-DAANQEQLW 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131245802 319 ALLSSGDLQVTGSAHCTFTTAQKAVGRDNFTLIPEGTNGVEERMSVVWEKCVASGQMDENEFVAVTSTNAAKIFNFYPRK 398
Cdd:cd01315 297 EALENGDIDMVVSDHSPCTPELKLLGKGDFFKAWGGISGLQLGLPVMLTEAVNKRGLSLEDIARLMCENPAKLFGLSHQK 376
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1131245802 399 GRVAVGSDADLVIWNPRATRIISAKSHSLNVEYNIFEGLECRGAPSVVISQGRVVLEDGALCVTPgTGRFI 469
Cdd:cd01315 377 GRIAVGYDADFVVWDPEEEFTVDAEDLYYKNKISPYVGRTLKGRVHATILRGTVVYQDGEVVGEP-LGQLL 446
|
|
| Cyclic_amidohydrolases |
cd01302 |
Cyclic amidohydrolases, including hydantoinase, dihydropyrimidinase, allantoinase, and ... |
63-443 |
2.43e-55 |
|
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: 189.91 E-value: 2.43e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131245802 63 LLVLPGGVDVHTRLLMPVLGMTpADDFCQGTKAALAGGTTMILDHVFPEAGVSLLAAYEQWRERADGGACCDYSLHVDIp 142
Cdd:cd01302 1 LLVLPGFIDIHVHLRDPGGTTY-KEDFESGSRAAAAGGVTTVIDMPNTGPPPIDLPAIELKIKLAEESSYVDFSFHAGI- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131245802 143 rWHESTREELEaLVRDKGVNSFLVFMAYK--DRHQCTDGQIYEIFSVIRDLGAVAQVHAEngdivdeeqkrllelgvtgp 220
Cdd:cd01302 79 -GPGDVTDELK-KLFDAGINSLKVFMNYYfgELFDVDDGTLMRTFLEIASRGGPVMVHAE-------------------- 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131245802 221 eghvlshpeeveaeavyRAITIARQASCPLYVTKVMSK*AADVIARAKRRGVVVFGEPITAGLGADGShYWSKNWAKaaa 300
Cdd:cd01302 137 -----------------RAAQLAEEAGANVHIAHVSSGEALELIKFAKNKGVKVTCEVCPHHLFLDES-MLRLNGAW--- 195
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131245802 301 FVTSPPISPdPSTADHLTALLSSGDLQVTGSAHCTFTTAQKAVGRDnFTLIPEGTNGVEERMSVVWEKCVASGqMDENEF 380
Cdd:cd01302 196 GKVNPPLRS-KEDREALWEGVKNGKIDTIASDHAPHSKEEKESGKD-IWKAPPGFPGLETRLPILLTEGVKRG-LSLETL 272
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1131245802 381 VAVTSTNAAKIFNFYPrKGRVAVGSDADLVIWNPRATRIISAKSHSLNVEYNIFEGLECRGAP 443
Cdd:cd01302 273 VEILSENPARIFGLYP-KGTIAVGYDADLVIVDPKKEWKVTAEEIESKADWTPFEGMEVTGKP 334
|
|
| PRK06189 |
PRK06189 |
allantoinase; Provisional |
17-469 |
1.96e-46 |
|
allantoinase; Provisional
Pssm-ID: 235732 [Multi-domain] Cd Length: 451 Bit Score: 169.11 E-value: 1.96e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131245802 17 LLIRGGKIVNDDQSFHADLYVEDGLIKQIGENLIVPG*iRTIDAHGLLVLPGGVDVHTRLLMPvlGMTPADDFCQGTKAA 96
Cdd:PRK06189 5 LIIRGGKVVTPEGVYRADIGIKNGKIAEIAPEISSPAR-EIIDADGLYVFPGMIDVHVHFNEP--GRTHWEGFATGSAAL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131245802 97 LAGGTTMILDhvFPEAGV-SLLAAYEQWRERADGGAccdySLHVDIPRWHESTREELEAL--VRDKGVNSFLVFMAYK-- 171
Cdd:PRK06189 82 AAGGCTTYFD--MPLNSIpPTVTREALDAKAELARQ----KSAVDFALWGGLVPGNLEHLreLAEAGVIGFKAFMSNSgt 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131245802 172 DRHQ-CTDGQIYEIFSVIRDLGAVAQVHAENGDIVDEEQKRLLELGVTGPEGHVLSHPEEVEAEAVYRAITIARQASCPL 250
Cdd:PRK06189 156 DEFRsSDDLTLYEGMKEIAALGKILALHAESDALTRHLTTQARQQGKTDVRDYLESRPVVAELEAVQRALLYAQETGCPL 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131245802 251 YVTKVMSK*AADVIARAKRRGVVV----------FGEPITAGLGAdgshywsknWAKAAafvtsPPISpDPSTADHLTAL 320
Cdd:PRK06189 236 HFVHISSGKAVALIAEAKKRGVDVsvetcphyllFTEEDFERIGA---------VAKCA-----PPLR-SRSQKEELWRG 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131245802 321 LSSGDLQVTGSAHCTFTTAQKAvgRDNFTLIPEGTNGVEERMSVVWEKCVASGQMDENEFVAVTSTNAAKIFNFyPRKGR 400
Cdd:PRK06189 301 LLAGEIDMISSDHSPCPPELKE--GDDFFLVWGGISGGQSTLLVMLTEGYIERGIPLETIARLLATNPAKRFGL-PQKGR 377
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1131245802 401 VAVGSDADLVIWNPRATRIISAKSHSLNVEYNIFEGLECRGAPSVVISQGRVVLEDGALcVTPGTGRFI 469
Cdd:PRK06189 378 LEVGADADFVLVDLDETYTLTKEDLFYRHKQSPYEGRTFPGRVVATYLRGQCVYQDGEV-FPPPRGQLL 445
|
|
| PRK02382 |
PRK02382 |
dihydroorotase; Provisional |
17-472 |
6.17e-44 |
|
dihydroorotase; Provisional
Pssm-ID: 179417 [Multi-domain] Cd Length: 443 Bit Score: 162.13 E-value: 6.17e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131245802 17 LLIRGGKIVNDDQSFHADLYVEDGLIKQIGENLIVPG*IRTIDAHGLLVLPGGVDVHTRLLMPvlGMTPADDFCQGTKAA 96
Cdd:PRK02382 4 ALLKDGRVYYNNSLQPRDVRIDGGKITAVGKDLDGSSSEEVIDARGMLLLPGGIDVHVHFREP--GYTHKETWYTGSRSA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131245802 97 LAGGTTMILDHVFPEAGVSLLAAYEQWRERADGGACCDYSLHVDI-PRWhestrEELEALVRdKGVNSF-LVFMAYKDRH 174
Cdd:PRK02382 82 AAGGVTTVVDQPNTDPPTVDGESFDEKAELAARKSIVDFGINGGVtGNW-----DPLESLWE-RGVFALgEIFMADSTGG 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131245802 175 QCTDGQIY-EIFSVIRDLGAVAQVHAENGDIVDEeQKRLLElGVTGPEGHVLSHPEEVEAEAVYRAITIARQASCPLYVT 253
Cdd:PRK02382 156 MGIDEELFeEALAEAARLGVLATVHAEDEDLFDE-LAKLLK-GDADADAWSAYRPAAAEAAAVERALEVASETGARIHIA 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131245802 254 KVMSK*AADVIaraKRRGVVVFGEPITAGLGADgshywskNWAKAAAFV-TSPPISPDPSTaDHLTALLSSGDLQVTGSA 332
Cdd:PRK02382 234 HISTPEGVDAA---RREGITCEVTPHHLFLSRR-------DWERLGTFGkMNPPLRSEKRR-EALWERLNDGTIDVVASD 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131245802 333 HCTFTTAQKAVG-RDnftlIPEGTNGVEERMSVVWEKcVASGQMDENEFVAVTSTNAAKIFNFyPRKGRVAVGSDADLVI 411
Cdd:PRK02382 303 HAPHTREEKDADiWD----APSGVPGVETMLPLLLAA-VRKNRLPLERVRDVTAANPARIFGL-DGKGRIAEGYDADLVL 376
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1131245802 412 WNPRATRIISAKS-HSlNVEYNIFEGLEcrGA-PSVVISQGRVVLEDGALCVTPGTGRFIPRK 472
Cdd:PRK02382 377 VDPDAAREIRGDDlHS-KAGWTPFEGME--GVfPELTMVRGTVVWDGDDINAKRGRGEFLRGR 436
|
|
| pyrC_multi |
TIGR00857 |
dihydroorotase, multifunctional complex type; In contrast to the homodimeric type of ... |
33-456 |
4.92e-40 |
|
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: 150.67 E-value: 4.92e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131245802 33 ADLYVEDGLIKQIGENLIVPG*iRTIDAHGLLVLPGGVDVHTRLLMPvlGMTPADDFCQGTKAALAGGTTMILDHVFPEA 112
Cdd:TIGR00857 6 VDILVEGGRIKKIGKLRIPPDA-EVIDAKGLLVLPGFIDLHVHLRDP--GEEYKEDIESGSKAAAHGGFTTVADMPNTKP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131245802 113 GVSLLAAYEQWRERADGGACCDYSLHVDIPRwHESTREELEAlvrdkgvnSFLVFMA-----YKDRHQC--TDGQIYEIF 185
Cdd:TIGR00857 83 PIDTPETLEWKLQRLKKVSLVDVHLYGGVTQ-GNQGKELTEA--------YELKEAGavgrmFTDDGSEvqDILSMRRAL 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131245802 186 SVIRDLGAVAQVHAENGDIVDEEQKRLLELgvtGPEGHVLSHPEEVEAEAVYRAITIARQASCPLYVTKVMSK*AADVIA 265
Cdd:TIGR00857 154 EYAAIAGVPIALHAEDPDLIYGGVMHEGPS---AAQLGLPARPPEAEEVAVARLLELAKHAGCPVHICHISTKESLELIV 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131245802 266 RAKRRGVVVFGEpITAG--LGADGSHYWSKNWAKaaafvTSPPISPdPSTADHLTALLSSGDLQVTGSAHCTFTTAQKav 343
Cdd:TIGR00857 231 KAKSQGIKITAE-VTPHhlLLSEEDVARLDGNGK-----VNPPLRE-KEDRLALIEGLKDGIIDIIATDHAPHTLEEK-- 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131245802 344 gRDNFTLIPEGTNGVEERMSVVWEKCVAsGQMDENEFVAVTSTNAAKIFNFyPRKGRVAVGSDADLVIWNPRATRIISAK 423
Cdd:TIGR00857 302 -TKEFAAAPPGIPGLETALPLLLQLLVK-GLISLKDLIRMLSINPARIFGL-PDKGTLEEGNPADITVFDLKKEWTINAE 378
|
410 420 430
....*....|....*....|....*....|...
gi 1131245802 424 SHSLNVEYNIFEGLECRGAPSVVISQGRVVLED 456
Cdd:TIGR00857 379 TFYSKAKNTPFEGMSLKGKPIATILRGKVVYED 411
|
|
| PRK08044 |
PRK08044 |
allantoinase AllB; |
17-422 |
1.07e-31 |
|
allantoinase AllB;
Pssm-ID: 169193 [Multi-domain] Cd Length: 449 Bit Score: 127.66 E-value: 1.07e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131245802 17 LLIRGGKIVNDDQSFHADLYVEDGLIKQIGENLIVPG*iRTIDAHGLLVLPGGVDVHTRLLMPvlGMTPADDFCQGTKAA 96
Cdd:PRK08044 5 LIIKNGTVILENEARVVDIAVKGGKIAAIGQDLGDAK--EVMDASGLVVSPGMVDAHTHISEP--GRSHWEGYETGTRAA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131245802 97 LAGG-TTMIldhVFPEAGVSLLAAYEQWRERADGGaccDYSLHVDIPRWHESTREELEAL--VRDKGVNSFLVFMAY--- 170
Cdd:PRK08044 81 AKGGiTTMI---EMPLNQLPATVDRASIELKFDAA---KGKLTIDAAQLGGLVSYNLDRLheLDEVGVVGFKCFVATcgd 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131245802 171 ----KDRHQCTDGQIYEIFSVIRDLGAVAQVHAENGDIVDEEQKRLLELGVTGPEGHVLSHPEEVEAEAVYRAITIARQA 246
Cdd:PRK08044 155 rgidNDFRDVNDWQFYKGAQKLGELGQPVLVHCENALICDELGEEAKREGRVTAHDYVASRPVFTEVEAIRRVLYLAKVA 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131245802 247 SCPLYVTKVMSK*AADVIARAKRRGVVVFGEPITaglgadgsHYWSKNWAKAAAFVT----SPPISpDPSTADHLTALLS 322
Cdd:PRK08044 235 GCRLHVCHISSPEGVEEVTRARQEGQDVTCESCP--------HYFVLDTDQFEEIGTlakcSPPIR-DLENQKGMWEKLF 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131245802 323 SGDLQVTGSAHCTFTTAQKAvgrDNFTLIPEGTNGVEERMSVVWEKCVASGQMDENEFVAVTSTNAAKIFNFyPRKGRVA 402
Cdd:PRK08044 306 NGEIDCLVSDHSPCPPEMKA---GNIMEAWGGIAGLQNCMDVMFDEAVQKRGMSLPMFGKLMATNAADIFGL-QQKGRIA 381
|
410 420
....*....|....*....|
gi 1131245802 403 VGSDADLVIWNPRATRIISA 422
Cdd:PRK08044 382 PGKDADFVFIQPNSSYVLKN 401
|
|
| pyrC |
PRK09357 |
dihydroorotase; Validated |
16-456 |
3.12e-30 |
|
dihydroorotase; Validated
Pssm-ID: 236479 [Multi-domain] Cd Length: 423 Bit Score: 123.00 E-value: 3.12e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131245802 16 RLLIRGGKIVN---DDQsfHADLYVEDGLIKQIGENLIVPG*iRTIDAHGLLVLPGGVDVHTRLLMPvlGMTPADDFCQG 92
Cdd:PRK09357 2 MILIKNGRVIDpkgLDE--VADVLIDDGKIAAIGENIEAEGA-EVIDATGLVVAPGLVDLHVHLREP--GQEDKETIETG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131245802 93 TKAALAGG---------TTMILD------------------HVFP-------EAGVSL--LAAYEQWRERA--DGGACCD 134
Cdd:PRK09357 77 SRAAAAGGfttvvampnTKPVIDtpevveyvldrakeaglvDVLPvgaitkgLAGEELteFGALKEAGVVAfsDDGIPVQ 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131245802 135 YSLHVDiprwhestreelEALVRDKGVNSFLVFMAyKDRHQCTDGQIYEifsvirdlGAVAQvhaengdivdeeqkrllE 214
Cdd:PRK09357 157 DARLMR------------RALEYAKALDLLIAQHC-EDPSLTEGGVMNE--------GEVSA-----------------R 198
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131245802 215 LGVTGpeghvlsHPEEVEAEAVYRAITIARQASCPLYVTKVMSK*AADVIARAKRRGVvvfgePITA------------- 281
Cdd:PRK09357 199 LGLPG-------IPAVAEEVMIARDVLLAEATGARVHICHVSTAGSVELIRWAKALGI-----KVTAevtphhllltded 266
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131245802 282 GLGADGShywsknwakaaaFVTSPPISpDPSTADHLTALLSSGDLQVTGSAHCTFTTAQKAVGrdnFTLIPEGTNGVEER 361
Cdd:PRK09357 267 LLTYDPN------------YKVNPPLR-TEEDREALIEGLKDGTIDAIATDHAPHAREEKECE---FEAAPFGITGLETA 330
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131245802 362 MSVVWEKCVASGQMDENEFVAVTSTNAAKIFNFYPrkGRVAVGSDADLVIWNPRATRIISA---KSHSLNveyNIFEGLE 438
Cdd:PRK09357 331 LSLLYTTLVKTGLLDLEQLLEKMTINPARILGLPA--GPLAEGEPADLVIFDPEAEWTVDGedfASKGKN---TPFIGMK 405
|
490
....*....|....*...
gi 1131245802 439 CRGAPSVVISQGRVVLED 456
Cdd:PRK09357 406 LKGKVVYTIVDGKIVYQD 423
|
|
| PRK09060 |
PRK09060 |
dihydroorotase; Validated |
17-467 |
4.36e-30 |
|
dihydroorotase; Validated
Pssm-ID: 181632 [Multi-domain] Cd Length: 444 Bit Score: 123.11 E-value: 4.36e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131245802 17 LLIRGGKIVNDDQSFHADLYVEDGLIKQIGEnLIVPG*IRTIDAHGLLVLPGGVDVHTRLLMPvlGMTPADDFCQGTKAA 96
Cdd:PRK09060 7 LILKGGTVVNPDGEGRADIGIRDGRIAAIGD-LSGASAGEVIDCRGLHVLPGVIDSQVHFREP--GLEHKEDLETGSRAA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131245802 97 LAGGTTMILDHVFPEAGVSLLAAYEQWRERADGGACCDYSLHVDiprwheSTRE---ELEALVRDKGVNSFLVFMA---- 169
Cdd:PRK09060 84 VLGGVTAVFEMPNTNPLTTTAEALADKLARARHRMHCDFAFYVG------GTRDnadELAELERLPGCAGIKVFMGsstg 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131245802 170 ---YKDrhqctDGQIYEIFSVIRdlgAVAQVHAEngdivDEEqkRLLELGVTGPEGHVLSHP----EEVEAEAVYRAITI 242
Cdd:PRK09060 158 dllVED-----DEGLRRILRNGR---RRAAFHSE-----DEY--RLRERKGLRVEGDPSSHPvwrdEEAALLATRRLVRL 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131245802 243 ARQASCPLYVTKVMSK*AADVIARAKRRGVV-VFGEPITagLGADGSHYWSKNWAkaaafVTSPPIspdpSTADHLTAL- 320
Cdd:PRK09060 223 ARETGRRIHVLHVSTAEEIDFLADHKDVATVeVTPHHLT--LAAPECYERLGTLA-----QMNPPI----RDARHRDGLw 291
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131245802 321 --LSSGDLQVTGSAHCTFTTAQKAvgrDNFTLIPEGTNGVEERMSVVWEKcVASGQMDENEFVAVTSTNAAKIFNFyPRK 398
Cdd:PRK09060 292 rgVRQGVVDVLGSDHAPHTLEEKA---KPYPASPSGMTGVQTLVPIMLDH-VNAGRLSLERFVDLTSAGPARIFGI-AGK 366
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1131245802 399 GRVAVGSDADLVIWNPRATRIISAKSHSLNVEYNIFEGLECRGAPSVVISQGRVVLEDGALcVTPGTGR 467
Cdd:PRK09060 367 GRIAVGYDADFTIVDLKRRETITNEWIASRCGWTPYDGKEVTGWPVGTIVRGQRVMWDGEL-VGPPTGE 434
|
|
| DHOase_IIb |
cd01318 |
Dihydroorotase (DHOase), subgroup IIb; DHOases catalyze the reversible interconversion of ... |
62-450 |
5.22e-30 |
|
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: 121.29 E-value: 5.22e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131245802 62 GLLVLPGGVDVHTRLLMPvlGMTPADDFCQGTKAALAGGTTMILD---HVFPeagVSLLAAYEQWRERADGGACCDYSLH 138
Cdd:cd01318 1 GLLILPGVIDIHVHFREP--GLTYKEDFVSGSRAAAAGGVTTVMDmpnTKPP---TTTAEALYEKLRLAAAKSVVDYGLY 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131245802 139 VDIprwhesTREELEALVRDKGVNSFLVFMAykdrHQCTDGQIYE--IFSVIRDLGAVAQVHAENGDIVDEEQKRLLELG 216
Cdd:cd01318 76 FGV------TGSEDLEELDKAPPAGYKIFMG----DSTGDLLDDEetLERIFAEGSVLVTFHAEDEDRLRENRKELKGES 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131245802 217 VtgpegHVLSHPEEVEAEAVYRAITIARQASCPLYVTKVMSK*AADVIARAKRRGVV-------VFGEPITAGLGAdgsh 289
Cdd:cd01318 146 A-----HPRIRDAEAAAVATARALKLARRHGARLHICHVSTPEELKLIKKAKPGVTVevtphhlFLDVEDYDRLGT---- 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131245802 290 ywsknWAKaaafvTSPPISpDPSTADHLTALLSSGDLQVTGSAHCTFTTAQKAVGRDNftlIPEGTNGVEERMSVVWEKc 369
Cdd:cd01318 217 -----LGK-----VNPPLR-SREDRKALLQALADGRIDVIASDHAPHTLEEKRKGYPA---APSGIPGVETALPLMLTL- 281
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131245802 370 VASGQMDENEFVAVTSTNAAKIFNFyPRKGRVAVGSDADLVIWNPRATRIISA-KSHSlNVEYNIFEGLECRGAPSVVIS 448
Cdd:cd01318 282 VNKGILSLSRVVRLTSHNPARIFGI-KNKGRIAEGYDADLTVVDLKEERTIRAeEFHS-KAGWTPFEGFEVTGFPVMTIV 359
|
..
gi 1131245802 449 QG 450
Cdd:cd01318 360 RG 361
|
|
| DHOase_IIa |
cd01317 |
Dihydroorotase (DHOase), subgroup IIa; DHOases catalyze the reversible interconversion of ... |
56-441 |
1.90e-29 |
|
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: 119.65 E-value: 1.90e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131245802 56 RTIDAHGLLVLPGGVDVHTRLLMPvlGMTPADDFCQGTKAALAGGTTMILDHVFPEAGVSLLAAYEQWRERADggaccDY 135
Cdd:cd01317 3 EVIDAEGKILAPGLVDLHVHLREP--GFEYKETLESGAKAAAAGGFTTVVCMPNTNPVIDNPAVVELLKNRAK-----DV 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131245802 136 SLHVDIPrWHESTR----EELE--ALVRDKGVNSFlvfmaYKDRHQCTDGQI-YEIFSVIRDLGAVAQVHAENGDIVDE- 207
Cdd:cd01317 76 GIVRVLP-IGALTKglkgEELTeiGELLEAGAVGF-----SDDGKPIQDAELlRRALEYAAMLDLPIIVHPEDPSLAGGg 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131245802 208 ---EQKRLLELGVTGpeghvlsHPEEVEAEAVYRAITIARQASCPLYVTKVMSK*AADVIARAKRRGVvvfgePITAG-- 282
Cdd:cd01317 150 vmnEGKVASRLGLPG-------IPPEAETIMVARDLELAEATGARVHFQHLSTARSLELIRKAKAKGL-----PVTAEvt 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131245802 283 ---LGADGShyWSKNWAkaAAFVTSPPISpDPSTADHLTALLSSGDLQVTGSAHCTFTTAQKAVGrdnFTLIPEGTNGVE 359
Cdd:cd01317 218 phhLLLDDE--ALESYD--TNAKVNPPLR-SEEDREALIEALKDGTIDAIASDHAPHTDEEKDLP---FAEAPPGIIGLE 289
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131245802 360 ERMSVVWEKCVASGQMDENEFVAVTSTNAAKIFNFYPrkGRVAVGSDADLVIWNPRATRIISAKSHSLNVEYNIFEGLEC 439
Cdd:cd01317 290 TALPLLWTLLVKGGLLTLPDLIRALSTNPAKILGLPP--GRLEVGAPADLVLFDPDAEWIVDEETFRSKSKNTPFDGQKL 367
|
..
gi 1131245802 440 RG 441
Cdd:cd01317 368 KG 369
|
|
| Amidohydro_1 |
pfam01979 |
Amidohydrolase family; This family of enzymes are a a large metal dependent hydrolase ... |
64-453 |
1.09e-24 |
|
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: 105.28 E-value: 1.09e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131245802 64 LVLPGGVDVHTRLLMPVLGMTPADDFC------QGTKAALAGGTTMILDHVF--PEAGVSLLAAYEQWRE--RADGGACC 133
Cdd:pfam01979 1 IVLPGLIDAHVHLEMGLLRGIPVPPEFayealrLGITTMLKSGTTTVLDMGAttSTGIEALLEAAEELPLglRFLGPGCS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131245802 134 ---DYSLHVDIPRWHESTREELEALVRDKGVnsFLVFMAYKDRHQCTDGQIYEIFSVIRDLGAVAQVHAENGDivdEEQK 210
Cdd:pfam01979 81 ldtDGELEGRKALREKLKAGAEFIKGMADGV--VFVGLAPHGAPTFSDDELKAALEEAKKYGLPVAIHALETK---GEVE 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131245802 211 RLLELGVTGPEghVLSHPEEVEAEAVYRAITIARQASCPLYVTKvmsk*AADVIARAKRRGVVvfgepitagLGADGSHY 290
Cdd:pfam01979 156 DAIAAFGGGIE--HGTHLEVAESGGLLDIIKLILAHGVHLSPTE-----ANLLAEHLKGAGVA---------HCPFSNSK 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131245802 291 WSKNWAKAAAfvtsppispdpstadhltaLLSSGDLQVTGSAHCtfttaqkaVGRDNFTLIPEGTNGVEERMsvvwekcV 370
Cdd:pfam01979 220 LRSGRIALRK-------------------ALEDGVKVGLGTDGA--------GSGNSLNMLEELRLALELQF-------D 265
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131245802 371 ASGQMDENEFVAVTSTNAAKIFNFYPRKGRVAVGSDADLVIWNPRatriisakshslnvEYNIFEGLECRGAPSVVISQG 450
Cdd:pfam01979 266 PEGGLSPLEALRMATINPAKALGLDDKVGSIEVGKDADLVVVDLD--------------PLAAFFGLKPDGNVKKVIVKG 331
|
...
gi 1131245802 451 RVV 453
Cdd:pfam01979 332 KIV 334
|
|
| PRK07575 |
PRK07575 |
dihydroorotase; Provisional |
14-457 |
3.07e-24 |
|
dihydroorotase; Provisional
Pssm-ID: 236055 [Multi-domain] Cd Length: 438 Bit Score: 105.53 E-value: 3.07e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131245802 14 SDRLLIRGGKIVNDDQSF-HADLYVEDGLIKQIGENLIVPG*IRTIDAHGLLVLPGGVD--VHTRllMPvlGMTPADDFC 90
Cdd:PRK07575 2 MMSLLIRNARILLPSGELlLGDVLVEDGKIVAIAPEISATAVDTVIDAEGLTLLPGVIDpqVHFR--EP--GLEHKEDLF 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131245802 91 QGTKAALAGGTTMILDHVFPEAGVSLLAAYEQWRERADGGACCDYSLHVDiprwheSTREELEALVRDKGVNSFLVFMAY 170
Cdd:PRK07575 78 TASRACAKGGVTSFLEMPNTKPLTTTQAALDDKLARAAEKCVVNYGFFIG------ATPDNLPELLTANPTCGIKIFMGS 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131245802 171 KDRHQCTDGQ--IYEIFSVIRDLGAvaqVHAENGDIVDEEQKRLleLGVTGPEGHVLSHPEEVEAEAVYRAITIARQASC 248
Cdd:PRK07575 152 SHGPLLVDEEaaLERIFAEGTRLIA---VHAEDQARIRARRAEF--AGISDPADHSQIQDEEAALLATRLALKLSKKYQR 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131245802 249 PLYVTKVMSK*AADVIARAKRRGVVVFGEPitaglgadgsHYWSKNWAKAAAFVT----SPPISpDPSTADHLTALLSSG 324
Cdd:PRK07575 227 RLHILHLSTAIEAELLRQDKPSWVTAEVTP----------QHLLLNTDAYERIGTlaqmNPPLR-SPEDNEALWQALRDG 295
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131245802 325 DLQVTGSAHCTFTTAQKAVGRDNftlIPEGTNGVEERMSVVWEKCVAsGQMDENEFVAVTSTNAAKIFNFyPRKGRVAVG 404
Cdd:PRK07575 296 VIDFIATDHAPHTLEEKAQPYPN---SPSGMPGVETSLPLMLTAAMR-GKCTVAQVVRWMSTAVARAYGI-PNKGRIAPG 370
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|...
gi 1131245802 405 SDADLVIWNPRATRIISAKSHSLNVEYNIFEGLECRGAPSVVISQGRVVLEDG 457
Cdd:PRK07575 371 YDADLVLVDLNTYRPVRREELLTKCGWSPFEGWNLTGWPVTTIVGGQIVFDRG 423
|
|
| PRK04250 |
PRK04250 |
dihydroorotase; Provisional |
22-457 |
2.85e-22 |
|
dihydroorotase; Provisional
Pssm-ID: 235265 [Multi-domain] Cd Length: 398 Bit Score: 99.07 E-value: 2.85e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131245802 22 GKIVNDDQSFHADLYVEDGLIKQIGENLIvPG*iRTIDAHGLLVLPGGVDVHTRLlmpvlgmtpaDDFCQ--------GT 93
Cdd:PRK04250 4 GKFLLKGRIVEGGIGIENGRISKISLRDL-KGK-EVIKVKGGIILPGLIDVHVHL----------RDFEEsyketiesGT 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131245802 94 KAALAGGTTMILDHVFPEAGVSLLAAYEQWRERADGGACCDYSLHVDIprwhESTREELEALVRDkgvnsflvfmAYKDR 173
Cdd:PRK04250 72 KAALHGGITLVFDMPNTKPPIMDEKTYEKRMRIAEKKSYADYALNFLI----AGNCEKAEEIKAD----------FYKIF 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131245802 174 HQCTDGQIY-EIFSV-IRDLGAVAQVHAENGDIVDEEQKRllelgvtgpeghvlshPEEVEAEAVYRAITIARQASCPLY 251
Cdd:PRK04250 138 MGASTGGIFsENFEVdYACAPGIVSVHAEDPELIREFPER----------------PPEAEVVAIERALEAGKKLKKPLH 201
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131245802 252 VTKVMSK*AADVIARAKRRGVVVFGEPitaglgadgSH--YWSKNWAKAAAFVTSPPISpdpsTADHLTALLSSGD-LQV 328
Cdd:PRK04250 202 ICHISTKDGLKLILKSNLPWVSFEVTP---------HHlfLTRKDYERNPLLKVYPPLR----SEEDRKALWENFSkIPI 268
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131245802 329 TGSAHCTFTTAQKAVGrdnftliPEGTNGVEERMSVVWEkCVASGQMDENEFVAVTSTNAAKIFNFyPRKGrVAVGSDAD 408
Cdd:PRK04250 269 IASDHAPHTLEDKEAG-------AAGIPGLETEVPLLLD-AANKGMISLFDIVEKMHDNPARIFGI-KNYG-IEEGNYAN 338
|
410 420 430 440
....*....|....*....|....*....|....*....|....*....
gi 1131245802 409 LVIWNPRATRIISAKSHSLNVEYNIFEGLECRGAPSVVISQGRVVLEDG 457
Cdd:PRK04250 339 FAVFDMKKEWTIKAEELYTKAGWTPYEGFKLKGKVIMTILRGEVVMEDD 387
|
|
| PRK01211 |
PRK01211 |
dihydroorotase; Provisional |
37-471 |
1.12e-19 |
|
dihydroorotase; Provisional
Pssm-ID: 179247 [Multi-domain] Cd Length: 409 Bit Score: 91.46 E-value: 1.12e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131245802 37 VEDGLIKQIGENLivpG*IRTIDAHGLlVLPGGVDVHTRLLMPvlGMTPADDFCQGTKAALAGGTTMILDHVFPEAGVSL 116
Cdd:PRK01211 20 VEDGKIKSIKKDA---GNIGKKELKGA-ILPAATDIHVHFRTP--GETEKEDFSTGTLSAIFGGTTFIMDMPNNNIPIKD 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131245802 117 LAAYEQWRERADGGACCDYSLHvdiprwheSTREELEALVRDKGVNSFLVFMAYKDRHQCTDGQIYEIfSVIRDLGAVAQ 196
Cdd:PRK01211 94 YNAFSDKLGRVAPKAYVDFSLY--------SMETGNNALILDERSIGLKVYMGGTTNTNGTDIEGGEI-KKINEANIPVF 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131245802 197 VHAENGDIVDE---EQKRLLElgvtgpegHVLSHPEEVEAEAVYRAITIARQascplyvTKVMS-K*AADVIARAKRRgv 272
Cdd:PRK01211 165 FHAELSECLRKhqfESKNLRD--------HDLARPIECEIKAVKYVKNLDLK-------TKIIAhVSSIDVIGRFLRE-- 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131245802 273 vvfgepitaglgADGSHYWSKNWAKAAAF-VTSPPISpDPSTADHLTALLSSGDLQVTGSAHCTFTTAQKAvgrdNFTLI 351
Cdd:PRK01211 228 ------------VTPHHLLLNDDMPLGSYgKVNPPLR-DRWTQERLLEEYISGRFDILSSDHAPHTEEDKQ----EFEYA 290
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131245802 352 PEGTNGVEERMSVVWeKCVASGQMDENEFVAVTSTNAAKIFNFypRKGRVAVGSDADLVIWNPRATRIISAKS-HSLN-- 428
Cdd:PRK01211 291 KSGIIGVETRVPLFL-ALVKKKILPLDVLYKTAIERPASLFGI--KKGKIEEGYDADFMAFDFTNIKKINDKRlHSKCpv 367
|
410 420 430 440
....*....|....*....|....*....|....*....|...
gi 1131245802 429 VEYNIFEGLecrgAPSVVISQGRVVLEDGALCVTPgTGRFIPR 471
Cdd:PRK01211 368 SPFNGFDAI----FPSHVIMRGEVVIDNYELISER-TGKFVPK 405
|
|
| PLN02795 |
PLN02795 |
allantoinase |
12-417 |
1.77e-19 |
|
allantoinase
Pssm-ID: 178392 [Multi-domain] Cd Length: 505 Bit Score: 91.76 E-value: 1.77e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131245802 12 ITSDRLLIRGGKIVNDdqsfhadLYVEDGLIKQIGENLIVPG*I---RTIDAHGLLVLPGGVDVHTRLLMPvlGMTPADD 88
Cdd:PLN02795 48 LYSKRVVTPAGVIPGA-------VEVEGGRIVSVTKEEEAPKSQkkpHVLDYGNAVVMPGLIDVHVHLNEP--GRTEWEG 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131245802 89 FCQGTKAALAGGTTMILD---HVFPEagVSLLAAYEQWRERADGgaccdySLHVDIPRW--------HESTreELEALVr 157
Cdd:PLN02795 119 FPTGTKAAAAGGITTLVDmplNSFPS--TTSVETLELKIEAAKG------KLYVDVGFWgglvpenaHNAS--VLEELL- 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131245802 158 DKGVNSFLVFM---AYKDRHQCTDGQIYEIFSVIRDLGAVAQVHAENGDIVDEEQKrlLELGVTGPEGHVLSHPEEVEAE 234
Cdd:PLN02795 188 DAGALGLKSFMcpsGINDFPMTTATHIKAALPVLAKYGRPLLVHAEVVSPVESDSR--LDADPRSYSTYLKSRPPSWEQE 265
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131245802 235 AVYRAITIARQA-------SCPLYVTKVM-SK*AADVIARAKRRGVVVFGEPITaglgadgsHYWsknwAKAAA------ 300
Cdd:PLN02795 266 AIRQLLEVAKDTrpggvaeGAHVHIVHLSdAESSLELIKEAKAKGDSVTVETCP--------HYL----AFSAEeipdgd 333
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131245802 301 --FVTSPPISpDPSTADHLTALLSSGDLQVTGSAHCTFTTAQKAVGRDNFTLIPEGTNGVEERMSVVWEKCVASGqMDEN 378
Cdd:PLN02795 334 trYKCAPPIR-DAANRELLWKALLDGDIDMLSSDHSPSPPDLKLLEEGNFLRAWGGISSLQFVLPATWTAGRAYG-LTLE 411
|
410 420 430
....*....|....*....|....*....|....*....
gi 1131245802 379 EFVAVTSTNAAKIFNFyPRKGRVAVGSDADLVIWNPRAT 417
Cdd:PLN02795 412 QLARWWSERPAKLAGL-DSKGAIAPGKDADIVVWDPEAE 449
|
|
| PRK09236 |
PRK09236 |
dihydroorotase; Reviewed |
15-138 |
2.36e-15 |
|
dihydroorotase; Reviewed
Pssm-ID: 181716 Cd Length: 444 Bit Score: 78.37 E-value: 2.36e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131245802 15 DRLLIRGGKIVNDDQSFHADLYVEDGLIKQIGENLIVPG*IRTIDAHGLLVLPGGVD--VHTRllMPvlGMTPADDFCQG 92
Cdd:PRK09236 2 KRILIKNARIVNEGKIFEGDVLIENGRIAKIASSISAKSADTVIDAAGRYLLPGMIDdqVHFR--EP--GLTHKGDIASE 77
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 1131245802 93 TKAALAGGTTMILD--HVFPEAgvSLLAAYEQWRERADGGACCDYSLH 138
Cdd:PRK09236 78 SRAAVAGGITSFMEmpNTNPPT--TTLEALEAKYQIAAQRSLANYSFY 123
|
|
| PRK15446 |
PRK15446 |
phosphonate metabolism protein PhnM; Provisional |
16-243 |
4.95e-13 |
|
phosphonate metabolism protein PhnM; Provisional
Pssm-ID: 237967 [Multi-domain] Cd Length: 383 Bit Score: 70.98 E-value: 4.95e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131245802 16 RLLIRGGKIVNDDQSFHADLYVEDGLIKQIGENLIVPG*IrtIDAHGLLVLPGGVDVHT----RLLMPVLG-MTPADDFC 90
Cdd:PRK15446 3 EMILSNARLVLPDEVVDGSLLIEDGRIAAIDPGASALPGA--IDAEGDYLLPGLVDLHTdnleKHLAPRPGvDWPADAAL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131245802 91 QGTKAALAG-GTTMILDHVF-----------PEAGVSLLAAYEQWRERadGGACCDYSLH--VDIPrwHESTREELEALV 156
Cdd:PRK15446 81 AAHDAQLAAaGITTVFDALSvgdeedgglrsRDLARKLIDAIEEARAR--GLLRADHRLHlrCELT--NPDALELFEALL 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131245802 157 RDKGVnSFLVFMaykDrHqcTDGQiyeifSVIRDLGAVAQVHAENGDIVDEEQKRLLELGVTGPEGHVLSHPEEVEAEAV 236
Cdd:PRK15446 157 AHPRV-DLVSLM---D-H--TPGQ-----RQFRDLEKYREYYAGKYGLSDEEFDAFVEERIALSARYAPPNRRAIAALAR 224
|
....*..
gi 1131245802 237 YRAITIA 243
Cdd:PRK15446 225 ARGIPLA 231
|
|
| HutI |
COG1228 |
Imidazolonepropionase or related amidohydrolase [Secondary metabolites biosynthesis, transport ... |
13-413 |
1.00e-12 |
|
Imidazolonepropionase or related amidohydrolase [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 440841 [Multi-domain] Cd Length: 386 Bit Score: 69.99 E-value: 1.00e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131245802 13 TSDRLLIRGGKIVNDDQS---FHADLYVEDGLIKQIGEN--LIVPG*IRTIDAHGLLVLPGGVDVHTRLlmpVLGMTPAD 87
Cdd:COG1228 6 QAGTLLITNATLVDGTGGgviENGTVLVEDGKIAAVGPAadLAVPAGAEVIDATGKTVLPGLIDAHTHL---GLGGGRAV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131245802 88 DFCQGT----------------KAALAGGTTMILDhvfpeagvsLLAAYEQWRERADGGaccdYSLHVDIPR-------- 143
Cdd:COG1228 83 EFEAGGgitptvdlvnpadkrlRRALAAGVTTVRD---------LPGGPLGLRDAIIAG----ESKLLPGPRvlaagpal 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131245802 144 -----WHESTREELEALVRD---KGVNsFLVFMAYKDRHQCTDGQIYEIFSVIRDLGAVAQVHAENgdivDEEQKRLLEL 215
Cdd:COG1228 150 sltggAHARGPEEARAALREllaEGAD-YIKVFAEGGAPDFSLEELRAILEAAHALGLPVAAHAHQ----ADDIRLAVEA 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131245802 216 GVtgpegHVLSHPEEVEAEavyraitiarqascplyvtkvmsk*aadVIARAKRRGVVV------FGEPITAGLGADGSH 289
Cdd:COG1228 225 GV-----DSIEHGTYLDDE----------------------------VADLLAEAGTVVlvptlsLFLALLEGAAAPVAA 271
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131245802 290 YWSKNWAKAAAFVtsppispdpstadhltALLSSGDLQVtgsahctfttaqkAVGRDNFTLIPEGTNgveerMSVVWEKC 369
Cdd:COG1228 272 KARKVREAALANA----------------RRLHDAGVPV-------------ALGTDAGVGVPPGRS-----LHRELALA 317
|
410 420 430 440
....*....|....*....|....*....|....*....|....*
gi 1131245802 370 VASGqMDENE-FVAVTStNAAKIFNFYPRKGRVAVGSDADLVIWN 413
Cdd:COG1228 318 VEAG-LTPEEaLRAATI-NAAKALGLDDDVGSLEPGKLADLVLLD 360
|
|
| D-aminoacylase |
cd01297 |
D-aminoacylases (N-acyl-D-Amino acid amidohydrolases) catalyze the hydrolysis of ... |
17-414 |
1.86e-12 |
|
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: 69.25 E-value: 1.86e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131245802 17 LLIRGGKIVndDQS----FHADLYVEDGLIKQIGENLIVPG*iRTIDAHGLLVLPGGVDVHTRLLMPVL---GMTPaddf 89
Cdd:cd01297 2 LVIRNGTVV--DGTgappFTADVGIRDGRIAAIGPILSTSAR-EVIDAAGLVVAPGFIDVHTHYDGQVFwdpDLRP---- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131245802 90 cqgtkAALAGGTTMILDhvfpEAGVSL-------------------------------LAAYEQWRERADGG--ACCDYS 136
Cdd:cd01297 75 -----SSRQGVTTVVLG----NCGVSPapanpddlarlimlmeglvalgeglpwgwatFAEYLDALEARPPAvnVAALVG 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131245802 137 lHVDIPRWH------ESTREELEALVR--DKGVNS----FLVFMAYKDRHQCTDGQIYEIFSVIRDLGAVAQVHaengdi 204
Cdd:cd01297 146 -HAALRRAVmgldarEATEEELAKMREllREALEAgalgISTGLAYAPRLYAGTAELVALARVAARYGGVYQTH------ 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131245802 205 VDEEQKRLLelgvtgpeghvlshpeeveaEAVYRAITIARQASCPLYVT--KVMSK*-------AADVIARAKRRGVVVF 275
Cdd:cd01297 219 VRYEGDSIL--------------------EALDELLRLGRETGRPVHIShlKSAGAPnwgkidrLLALIEAARAEGLQVT 278
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131245802 276 GE--PITAGLGADgshywsknwakAAAFVTSPPispdpstadhltaLLSSGDLQVTGSAH----CTFT--TAQKAVGRDN 347
Cdd:cd01297 279 ADvyPYGAGSEDD-----------VRRIMAHPV-------------VMGGSDGGALGKPHprsyGDFTrvLGHYVRERKL 334
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1131245802 348 FTLIpegtngveermsvvwekcvasgqmdenEFVAVTSTNAAKIFNFYPRkGRVAVGSDADLVIWNP 414
Cdd:cd01297 335 LSLE---------------------------EAVRKMTGLPARVFGLADR-GRIAPGYRADIVVFDP 373
|
|
| Amidohydro_3 |
pfam07969 |
Amidohydrolase family; |
56-436 |
9.65e-12 |
|
Amidohydrolase family;
Pssm-ID: 400360 [Multi-domain] Cd Length: 464 Bit Score: 67.17 E-value: 9.65e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131245802 56 RTIDAHGLLVLPGGVDVHTRL-----------LMPVLGMTPADDFCQGTKAAL----------------AGGTTMILDHV 108
Cdd:pfam07969 1 EVIDAKGRLVLPGFVDPHTHLdggglnlrelrLPDVLPNAVVKGQAGRTPKGRwlvgegwdeaqfaetrFPYALADLDEV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131245802 109 FPEAGVSLLAA--YEQWRERAdGGACCDYSLHVDIPR----WHESTREELEALVRDKG------------VNSFLVFMAY 170
Cdd:pfam07969 81 APDGPVLLRALhtHAAVANSA-ALDLAGITKATEDPPggeiARDANGEGLTGLLREGAyalppllareaeAAAVAAALAA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131245802 171 KDRHQCT--DGQIYEIFSvIRDLGAVAQVHAENGDIvdEEQKRLLELGVTGPEGHV-------------------LSHP- 228
Cdd:pfam07969 160 LPGFGITsvDGGGGNVHS-LDDYEPLRELTAAEKLK--ELLDAPERLGLPHSIYELrigamklfadgvlgsrtaaLTEPy 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131245802 229 --------EEVEAEAVYRAITIARQASCPLYV-----TKVMSk*AADVIARAKRR-------------GVVVFG----EP 278
Cdd:pfam07969 237 fdapgtgwPDFEDEALAELVAAARERGLDVAIhaigdATIDT--ALDAFEAVAEKlgnqgrvriehaqGVVPYTysqiER 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131245802 279 ITAGLGADGSHYWSknWAKAAAFVTSPPISPDPSTADHLTALLSSGDLQVTGS-AHCTFTTAQKAVGRdNFTLIPEGTNG 357
Cdd:pfam07969 315 VAALGGAAGVQPVF--DPLWGDWLQDRLGAERARGLTPVKELLNAGVKVALGSdAPVGPFDPWPRIGA-AVMRQTAGGGE 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131245802 358 V---EERMSVvwekcvasgqmdeNEFVAVTSTNAAKIFNFYPRKGRVAVGSDADLVIWNPRATRIISAKSHSLNVEYNIF 434
Cdd:pfam07969 392 VlgpDEELSL-------------EEALALYTSGPAKALGLEDRKGTLGVGKDADLVVLDDDPLTVDPPAIADIRVRLTVV 458
|
..
gi 1131245802 435 EG 436
Cdd:pfam07969 459 DG 460
|
|
| SsnA |
COG0402 |
Cytosine/adenosine deaminase or related metal-dependent hydrolase [Nucleotide transport and ... |
16-456 |
2.44e-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: 65.62 E-value: 2.44e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131245802 16 RLLIRGGKIVNDDQSF----HADLYVEDGLIKQIGENLIVPG*I---RTIDAHGLLVLPGGVDVHTRL------------ 76
Cdd:COG0402 1 DLLIRGAWVLTMDPAGgvleDGAVLVEDGRIAAVGPGAELPARYpaaEVIDAGGKLVLPGLVNTHTHLpqtllrgladdl 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131245802 77 -LMPVLG---------MTPADDFcQGTKAA----LAGGTTMILDH--VFPEAGVSLLAAYEQWRERADGG-ACCDYSLHv 139
Cdd:COG0402 81 pLLDWLEeyiwplearLDPEDVY-AGALLAlaemLRSGTTTVADFyyVHPESADALAEAAAEAGIRAVLGrGLMDRGFP- 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131245802 140 diPRWHESTREELEALVRdkgvnsflVFMAYKDRHQ--------------CTDGQIYEIFSVIRDLGAVAQVH-----AE 200
Cdd:COG0402 159 --DGLREDADEGLADSER--------LIERWHGAADgrirvalaphapytVSPELLRAAAALARELGLPLHTHlaetrDE 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131245802 201 NGDIVDEEQKR----LLELGVTGPeGHVLSH-----PEEVE--AE----AVYRAITIARQAS--CPlyvtkvmsk*aadv 263
Cdd:COG0402 229 VEWVLELYGKRpveyLDELGLLGP-RTLLAHcvhltDEEIAllAEtgasVAHCPTSNLKLGSgiAP-------------- 293
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131245802 264 IARAKRRGVVVfgepitaGLGADGShywsknwakaaafvtSPPISPDPSTADHLTALLssgdlqvtgsahctfttaQKAV 343
Cdd:COG0402 294 VPRLLAAGVRV-------GLGTDGA---------------ASNNSLDMFEEMRLAALL------------------QRLR 333
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131245802 344 GRDnftlipegtngveermsvvwEKCVASGQMdeneFVAVTsTNAAKIFNFYPRKGRVAVGSDADLVIWNPRATRIISAk 423
Cdd:COG0402 334 GGD--------------------PTALSAREA----LEMAT-LGGARALGLDDEIGSLEPGKRADLVVLDLDAPHLAPL- 387
|
490 500 510
....*....|....*....|....*....|....*.
gi 1131245802 424 shslnveYNIFEGL-ECRGAPSV--VISQGRVVLED 456
Cdd:COG0402 388 -------HDPLSALvYAADGRDVrtVWVAGRVVVRD 416
|
|
| PRK07369 |
PRK07369 |
dihydroorotase; Provisional |
32-428 |
2.58e-10 |
|
dihydroorotase; Provisional
Pssm-ID: 236002 [Multi-domain] Cd Length: 418 Bit Score: 62.70 E-value: 2.58e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131245802 32 HADLYVEDGLIKQIGENLI-VPG*IRTIDAHGLLVLPGGVDVHTRLLMPvlGMTPADDFCQGTKAALAGGTTM--ILDHV 108
Cdd:PRK07369 21 IADVLIEDGKIQAIEPHIDpIPPDTQIIDASGLILGPGLVDLYSHSGEP--GFEERETLASLAAAAAAGGFTRvaILPDT 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131245802 109 FPeaGVSLLAAYEQWRERADGGAccdySLHVDIprWHESTRE-------ELEALVRdKGVNSFlvfmaykdrhqcTDGQI 181
Cdd:PRK07369 99 FP--PLDNPATLARLQQQAQQIP----PVQLHF--WGALTLGgqgkqltELAELAA-AGVVGF------------TDGQP 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131245802 182 YEIFSVIRDLGAVAQVH-------------AENGdiVDEEQKRLLELGVTGpeghvlsHPEEVEAEAVYRAITIARQASC 248
Cdd:PRK07369 158 LENLALLRRLLEYLKPLgkpvalwpcdrslAGNG--VMREGLLALRLGLPG-------DPASAETTALAALLELVAAIGT 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131245802 249 PLYVTKVMSK*AADVIARAKRRGVvvfgePITAglgadgshywSKNWAK---AAAFVTS--------PPIsPDPSTADHL 317
Cdd:PRK07369 229 PVHLMRISTARSVELIAQAKARGL-----PITA----------STTWMHlllDTEALASydpnlrldPPL-GNPSDRQAL 292
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131245802 318 TALLSSGDLQVTGSAHCTFTTAQKAVGrdnFTLIPEGTNGVEERMSVVWEKCVASGQMDENEFVAVTSTNAAKIFNFYPR 397
Cdd:PRK07369 293 IEGVRTGVIDAIAIDHAPYTYEEKTVA---FAEAPPGAIGLELALPLLWQNLVETGELSALQLWQALSTNPARCLGQEPP 369
|
410 420 430
....*....|....*....|....*....|..
gi 1131245802 398 kgRVAVGSDADLVIWNPRATRIISAKS-HSLN 428
Cdd:PRK07369 370 --SLAPGQPAELILFDPQKTWTVSAQTlHSLS 399
|
|
| ATZ_TRZ_like |
cd01298 |
TRZ/ATZ family contains enzymes from the atrazine degradation pathway and related hydrolases. ... |
17-112 |
2.66e-09 |
|
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: 59.52 E-value: 2.66e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131245802 17 LLIRGGKIVNDDQS---FHADLYVEDGLIKQIGENLIVPG*I--RTIDAHGLLVLPGGVDVHTRLLM------------- 78
Cdd:cd01298 1 ILIRNGTIVTTDPRrvlEDGDVLVEDGRIVAVGPALPLPAYPadEVIDAKGKVVMPGLVNTHTHLAMtllrgladdlplm 80
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 1131245802 79 --------PVLGMTPADDFCQGTKAALA----GGTTMILDHVFPEA 112
Cdd:cd01298 81 ewlkdliwPLERLLTEEDVYLGALLALAemirSGTTTFADMYFFYP 126
|
|
| COG3964 |
COG3964 |
Predicted amidohydrolase [General function prediction only]; |
17-106 |
2.90e-09 |
|
Predicted amidohydrolase [General function prediction only];
Pssm-ID: 443164 [Multi-domain] Cd Length: 376 Bit Score: 59.03 E-value: 2.90e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131245802 17 LLIRGGKIVNDDQSFHA--DLYVEDGLIKQIGENLIVPG*IRTIDAHGLLVLPGGVDVHTRL--LMPVLGMtPADDFCqg 92
Cdd:COG3964 2 LLIKGGRVIDPANGIDGvmDIAIKDGKIAAVAKDIDAAEAKKVIDASGLYVTPGLIDLHTHVfpGGTDYGV-DPDGVG-- 78
|
90
....*....|....
gi 1131245802 93 tkaaLAGGTTMILD 106
Cdd:COG3964 79 ----VRSGVTTVVD 88
|
|
| PRK09061 |
PRK09061 |
D-glutamate deacylase; Validated |
16-471 |
4.32e-09 |
|
D-glutamate deacylase; Validated
Pssm-ID: 236369 [Multi-domain] Cd Length: 509 Bit Score: 58.94 E-value: 4.32e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131245802 16 RLLIRGGKIVNDDQSFHA--DLYVEDGLIKQIGENLIVPG*iRTIDAHGLLVLPGGVDVHTRllmpvlGMTPADDFCQgt 93
Cdd:PRK09061 20 DLVIRNGRVVDPETGLDAvrDVGIKGGKIAAVGTAAIEGD--RTIDATGLVVAPGFIDLHAH------GQSVAAYRMQ-- 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131245802 94 kaALAGGTTMiLDHvfpEAGVSLLAayeQWRERADG----------------------GACCDYSL-----HVDIPRWHE 146
Cdd:PRK09061 90 --AFDGVTTA-LEL---EAGVLPVA---RWYAEQAGegrplnygasvgwtpariavltGPQAEGTIadfgkALGDPRWQE 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131245802 147 --STREELEALVR------DKGVNSFLVFMAYKDRHqcTDGQIYEIFSVIRDLGAVAQVHAENGDIVDEEqkrllelgvT 218
Cdd:PRK09061 161 raATPAELAEILElleqglDEGALGIGIGAGYAPGT--GHKEYLELARLAARAGVPTYTHVRYLSNVDPR---------S 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131245802 219 GPEGHvlshpEEVEAEAvyrAITIARQASCPLYVTKVMS-K*AADVIARAKRRGVVVFGE--PITAG---LGAD------ 286
Cdd:PRK09061 230 SVDAY-----QELIAAA---AETGAHMHICHVNSTSLRDiDRCLALVEKAQAQGLDVTTEayPYGAGstvVGAAffdpgw 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131245802 287 ----GSHYWSKNW----------AKAAAFVTSPPISP---------DPSTADHLTALLSSGDLQVTGSAHCTFTTAQKAV 343
Cdd:PRK09061 302 lermGLGYGSLQWvetgerlltrEELAKLRANDPGGLvlihfldedNPRDRALLDRSVLFPGAAIASDAMPWTWSDGTVY 381
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131245802 344 GRDNFTLIPEG-----TNG---------VEERMSVVWekcvasgqmdeNEFVAVTSTNAAKIF-NFYP---RKGRVAVGS 405
Cdd:PRK09061 382 EGDAWPLPEDAvshprSAGtfarflreyVRERKALSL-----------LEAIRKCTLMPAQILeDSVPamrRKGRLQAGA 450
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1131245802 406 DADLVIWNP-----RATrIISAKSHSLNVEYnifeglecrgapsvVISQGRVVLEDGALCVTPGTGRFIPR 471
Cdd:PRK09061 451 DADIVVFDPetitdRAT-FEDPNRPSEGVRH--------------VLVNGVPVVSNGELVRDARPGRPVRR 506
|
|
| CAD_DHOase |
cd01316 |
The eukaryotic CAD protein is a trifunctional enzyme of carbamoylphosphate ... |
63-466 |
7.84e-09 |
|
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: 57.46 E-value: 7.84e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131245802 63 LLVLPGGVDVHTRLlmPVLGMTPADDFCQGTKAALAGGTTMILdhVFPEAGVSLL--AAYEQWRERADGGACCDYSLHVD 140
Cdd:cd01316 2 TIRLPGLIDVHVHL--REPGATHKEDFASGTKAALAGGFTMVR--AMPNTNPSIVdvASLKLVQSLAQAKARCDYAFSIG 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131245802 141 IPRWHESTREELEalvrDKGVNS-FLVFmaykdrhqctdgqiyEIFSVIR--DLGAVAQvhaengdivdeeqkrllELGV 217
Cdd:cd01316 78 ATSTNAATVGELA----SEAVGLkFYLN---------------ETFSTLIldKITAWAS-----------------HFNA 121
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131245802 218 TGPEGHVLSHPEEVEAEAVyraITIARQASCPLYVTKVMSK*AADVIARAKRRGVVVFGE--PITAGLGADGSHYWSKnw 295
Cdd:cd01316 122 WPSTKPIVTHAKSQTLAAV---LLLASLHNRSIHICHVSSKEEINLIRLAKARGLKVTCEvsPHHLFLSQDDLPRGQY-- 196
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131245802 296 akaaafvtspPISPDPSTADHLTAL---LSSGDLQVTGSAhcTFTTAQKAVGRdnftlIPEGTNGVEERMSVVWeKCVAS 372
Cdd:cd01316 197 ----------EVRPFLPTREDQEALwenLDYIDCFATDHA--PHTLAEKTGNK-----PPPGFPGVETSLPLLL-TAVHE 258
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131245802 373 GQMDENEFVAVTSTNAAKIFNFYPRKGrVAVGSDADlVIWNPRATRIISAKShslnveYNIFEGLECRGAPSVVISQGRV 452
Cdd:cd01316 259 GRLTIEDIVDRLHTNPKRIFNLPPQSD-TYVEVDLD-EEWTIPKNPLQSKKG------WTPFEGKKVKGKVQRVVLRGET 330
|
410
....*....|....
gi 1131245802 453 VLEDGALCVTPGTG 466
Cdd:cd01316 331 AFIDGEIVAPPGFG 344
|
|
| COG3653 |
COG3653 |
N-acyl-D-aspartate/D-glutamate deacylase [Secondary metabolites biosynthesis, transport and ... |
17-74 |
2.94e-08 |
|
N-acyl-D-aspartate/D-glutamate deacylase [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 442870 [Multi-domain] Cd Length: 528 Bit Score: 56.34 E-value: 2.94e-08
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131245802 17 LLIRGGKIVN--DDQSFHADLYVEDGLIKQIGENLIVPG*iRTIDAHGLLVLPGGVDVHT 74
Cdd:COG3653 4 LLIRGGTVVDgtGAPPFRADVAIKGGRIVAVGDLAAAEAA-RVIDATGLVVAPGFIDIHT 62
|
|
| PRK08204 |
PRK08204 |
hypothetical protein; Provisional |
15-228 |
4.24e-08 |
|
hypothetical protein; Provisional
Pssm-ID: 181288 [Multi-domain] Cd Length: 449 Bit Score: 55.78 E-value: 4.24e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131245802 15 DRLLIRGGKIVNDDQSFH----ADLYVEDGLIKQIGENLIVPG*IRtIDAHGLLVLPGGVDVH----------------- 73
Cdd:PRK08204 2 KRTLIRGGTVLTMDPAIGdlprGDILIEGDRIAAVAPSIEAPDAEV-VDARGMIVMPGLVDTHrhtwqsvlrgigadwtl 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131245802 74 TRLLMPVLG-----MTPADDFCQ---GTKAALAGGTTMILD--HVF--PEAGVSLLAAYEQWRERADGGaccdYSLHVDI 141
Cdd:PRK08204 81 QTYFREIHGnlgpmFRPEDVYIAnllGALEALDAGVTTLLDwsHINnsPEHADAAIRGLAEAGIRAVFA----HGSPGPS 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131245802 142 PRWHEST----REELEAlVRDKGVNS--FLVFM--AYKDRHQCTDGQIYEIFSVIRDLGAVAQVHAENGDIV--DEEQKR 211
Cdd:PRK08204 157 PYWPFDSvphpREDIRR-VKKRYFSSddGLLTLglAIRGPEFSSWEVARADFRLARELGLPISMHQGFGPWGatPRGVEQ 235
|
250
....*....|....*..
gi 1131245802 212 LLELGVTGPeGHVLSHP 228
Cdd:PRK08204 236 LHDAGLLGP-DLNLVHG 251
|
|
| NagA |
cd00854 |
N-acetylglucosamine-6-phosphate deacetylase, NagA, catalyzes the hydrolysis of the N-acetyl ... |
17-74 |
4.56e-08 |
|
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: 55.28 E-value: 4.56e-08
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 1131245802 17 LLIRGGKIVNDDQSFHADLYVEDGLIKQIGENLIVPG*IRTIDAHGLLVLPGGVDVHT 74
Cdd:cd00854 1 LIIKNARILTPGGLEDGAVLVEDGKIVAIGPEDELEEADEIIDLKGQYLVPGFIDIHI 58
|
|
| pyrC |
PRK00369 |
dihydroorotase; Provisional |
62-466 |
2.23e-07 |
|
dihydroorotase; Provisional
Pssm-ID: 234738 [Multi-domain] Cd Length: 392 Bit Score: 53.23 E-value: 2.23e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131245802 62 GLLVLPGGVDVHTRLLMpvLGMTPADDFCQGTKAALAGGTTMILDhvFPEAgVSLLAAYEQWRERA---DGGACCDYSLH 138
Cdd:PRK00369 42 GTLILPGAIDLHVHLRG--LKLSYKEDVASGTSEAAYGGVTLVAD--MPNT-IPPLNTPEAITEKLaelEYYSRVDYFVY 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131245802 139 VDIPRwhestreELEALvrDKgvnsfLVFMAYKdrhqctdgqiyeifsvirdlgavaqVHAEngDIVDEEQKRLLE---- 214
Cdd:PRK00369 117 SGVTK-------DPEKV--DK-----LPIAGYK-------------------------IFPE--DLEREETFRVLLksrk 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131245802 215 LGVTGPEGHVLSHPEE-------VEAEAVYRAITIAR----QASCPlyvtkvmsk*aaDVIARAKRRGvvvFGEPITAG- 282
Cdd:PRK00369 156 LKILHPEVPLALKSNRklrrncwYEIAALYYVKDYQNvhitHASNP------------RTVRLAKELG---FTVDITPHh 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131245802 283 -LGADGSHYWSKnwakaaafvTSPPISpDPSTADHLTALLSSGDLQVtgSAHCTFTTAQKavgRDNFTLIPEGTNGVEER 361
Cdd:PRK00369 221 lLVNGEKDCLTK---------VNPPIR-DINERLWLLQALSEVDAIA--SDHAPHSSFEK---LQPYEVCPPGIAALSFT 285
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131245802 362 MSVVWeKCVASGQMDENEFVAVTSTNAAKIFNFypRKGRVAVGSDADLVIWNPRATRIISAKShslNVEYNIFEGLECRG 441
Cdd:PRK00369 286 PPFIY-TLVSKGILSIDRAVELISTNPARILGI--PYGEIKEGYRANFTVIQFEDWRYSTKYS---KVIETPLDGFELKA 359
|
410 420
....*....|....*....|....*
gi 1131245802 442 APSVVISQGRVVLEDGAlcVTPGTG 466
Cdd:PRK00369 360 SVYATIVQGKLAYLEGE--VFPVKG 382
|
|
| PRK09237 |
PRK09237 |
amidohydrolase/deacetylase family metallohydrolase; |
17-74 |
3.04e-07 |
|
amidohydrolase/deacetylase family metallohydrolase;
Pssm-ID: 236423 [Multi-domain] Cd Length: 380 Bit Score: 52.93 E-value: 3.04e-07
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131245802 17 LLIRGGKIVNDDQSFHA--DLYVEDGLIKQIGENLIVPG*IRTIDAHGLLVLPGGVDVHT 74
Cdd:PRK09237 1 LLLRGGRVIDPANGIDGviDIAIEDGKIAAVAGDIDGSQAKKVIDLSGLYVSPGWIDLHV 60
|
|
| FwdA |
COG1229 |
Formylmethanofuran dehydrogenase subunit A [Energy production and conversion]; |
17-79 |
9.62e-07 |
|
Formylmethanofuran dehydrogenase subunit A [Energy production and conversion];
Pssm-ID: 440842 Cd Length: 554 Bit Score: 51.73 E-value: 9.62e-07
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1131245802 17 LLIRGGKI------VNDDQsfhADLYVEDGlikQIGENLIVPG*IRTIDAHGLLVLPGGVDVHT----------RLLMP 79
Cdd:COG1229 3 LIIKNGRVydpangIDGEV---MDIAIKDG---KIVEEPSDPKDAKVIDASGKVVMAGGVDIHThiaggkvnvgRMMRP 75
|
|
| PRK07228 |
PRK07228 |
5'-deoxyadenosine deaminase; |
16-107 |
1.22e-06 |
|
5'-deoxyadenosine deaminase;
Pssm-ID: 180895 [Multi-domain] Cd Length: 445 Bit Score: 51.15 E-value: 1.22e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131245802 16 RLLIRGGKIVNDDQS---FHADLYVEDGLIKQIGENLIVPG*IRTIDAHGLLVLPGGVDVHTRLLMpVLGMTPADDF--- 89
Cdd:PRK07228 2 TILIKNAGIVTMNAKreiVDGDVLIEDDRIAAVGDRLDLEDYDDHIDATGKVVIPGLIQGHIHLCQ-TLFRGIADDLell 80
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 1131245802 90 -----------------------CQGTKAALAGGTTMILDH 107
Cdd:PRK07228 81 dwlkdriwpleaahdaesmyysaLLGIGELIESGTTTIVDM 121
|
|
| PRK07627 |
PRK07627 |
dihydroorotase; Provisional |
16-102 |
1.48e-06 |
|
dihydroorotase; Provisional
Pssm-ID: 181059 [Multi-domain] Cd Length: 425 Bit Score: 50.83 E-value: 1.48e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131245802 16 RLLIRGGKIVN-----DDQsfhADLYVEDGLIKQIGEnliVPG*I---RTIDAHGLLVLPGGVDVHTRLLMPvlGMTPAD 87
Cdd:PRK07627 2 KIHIKGGRLIDpaagtDRQ---ADLYVAAGKIAAIGQ---APAGFnadKTIDASGLIVCPGLVDLSARLREP--GYEYKA 73
|
90
....*....|....*
gi 1131245802 88 DFCQGTKAALAGGTT 102
Cdd:PRK07627 74 TLESEMAAAVAGGVT 88
|
|
| NagA |
COG1820 |
N-acetylglucosamine-6-phosphate deacetylase [Carbohydrate transport and metabolism]; |
18-74 |
2.83e-06 |
|
N-acetylglucosamine-6-phosphate deacetylase [Carbohydrate transport and metabolism];
Pssm-ID: 441425 [Multi-domain] Cd Length: 373 Bit Score: 49.71 E-value: 2.83e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 1131245802 18 LIRGGKIVNDDQSFH-ADLYVEDGLIKQIGENliVPG*IRTIDAHGLLVLPGGVDVHT 74
Cdd:COG1820 1 AITNARIFTGDGVLEdGALLIEDGRIAAIGPG--AEPDAEVIDLGGGYLAPGFIDLHV 56
|
|
| Met_dep_hydrolase_B |
cd01307 |
Metallo-dependent hydrolases, subgroup B is part of the superfamily of metallo-dependent ... |
34-425 |
1.10e-05 |
|
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: 47.71 E-value: 1.10e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131245802 34 DLYVEDGLIKQIGENLIVPG*IRTIDAHGLLVLPGGVDVHTRLL--MPVLGMTPadDFCqgtkaALAGGTTMILDHVFPE 111
Cdd:cd01307 1 DVAIENGKIAAVGAALAAPAATQIVDAGGCYVSPGWIDLHVHVYqgGTRYGDRP--DMI-----GVKSGVTTVVDAGSAG 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131245802 112 AGvSLLAAYEQWRERAdggaccdyslhvdiprwhestREELEALvrdkgVNSFLVFMAYKDrhqctdgQIYEIFSVirDL 191
Cdd:cd01307 74 AD-NIDGFRYTVIERS---------------------ATRVYAF-----LNISRVGLVAQD-------ELPDPDNI--DE 117
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131245802 192 GAVAQVHAENGDIVDEEQKRlLELGVTGPEGhvlshpeeveAEAVYRAITIARQASCPLYVTKVMSK*AADVIARAKRRG 271
Cdd:cd01307 118 DAVVAAAREYPDVIVGLKAR-ASKSVVGEWG----------IKPLELAKKIAKEADLPLMVHIGSPPPILDEVVPLLRRG 186
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131245802 272 VVVfgepitaglgadgSHYWSknwAKAAAFVTsppisPDPSTADHLTALLSSG---DLQvTGSAHCTFTTAQKAVGRDnf 348
Cdd:cd01307 187 DVL-------------THCFN---GKPNGIVD-----EEGEVLPLVRRARERGvifDVG-HGTASFSFRVARAAIAAG-- 242
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131245802 349 tLIPE----------GTNGVEERMSVVWEKCVASGqMDENEFVAVTSTNAAKIFNFyPRKGRVAVGSDADLVIWNPRATR 418
Cdd:cd01307 243 -LLPDtissdihgrnRTNGPVYALATTLSKLLALG-MPLEEVIEAVTANPARMLGL-AEIGTLAVGYDADLTVFDLKDGR 319
|
....*..
gi 1131245802 419 IISAKSH 425
Cdd:cd01307 320 VELVDSE 326
|
|
| Bact_CD |
cd01293 |
Bacterial cytosine deaminase and related metal-dependent hydrolases. Cytosine deaminases (CDs) ... |
33-128 |
1.62e-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: 1.62e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131245802 33 ADLYVEDGLIKQIGENLIVPG*IRTIDAHGLLVLPGGVDVHTRL---LmpVLGMTPADDFCQGTKA-------------- 95
Cdd:cd01293 15 VDIAIEDGRIAAIGPALAVPPDAEEVDAKGRLVLPAFVDPHIHLdktF--TGGRWPNNSGGTLLEAiiaweerkllltae 92
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 1131245802 96 ------------ALAGGTTMILDHV--FPEAGV----SLLAAYEQWRERAD 128
Cdd:cd01293 93 dvkeraeralelAIAHGTTAIRTHVdvDPAAGLkaleALLELREEWADLID 143
|
|
| PRK08203 |
PRK08203 |
hydroxydechloroatrazine ethylaminohydrolase; Reviewed |
16-119 |
2.58e-04 |
|
hydroxydechloroatrazine ethylaminohydrolase; Reviewed
Pssm-ID: 236184 [Multi-domain] Cd Length: 451 Bit Score: 43.69 E-value: 2.58e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131245802 16 RLLIRGGKIV---NDDQSFHAD--LYVEDGLIKQIGENLIVPG*I-RTIDAHGLLVLPGGVDVH-------TRLLMPVL- 81
Cdd:PRK08203 2 TLWIKNPLAIvtmDAARREIADggLVVEGGRIVEVGPGGALPQPAdEVFDARGHVVTPGLVNTHhhfyqtlTRALPAAQd 81
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 1131245802 82 ---------------GMTPaDDFCQGTKAALA----GGTTMILDH--VFPEAGVSLLAA 119
Cdd:PRK08203 82 aelfpwlttlypvwaRLTP-EMVRVATQTALAelllSGCTTSSDHhyLFPNGLRDALDD 139
|
|
| YtcJ |
COG1574 |
Predicted amidohydrolase YtcJ [General function prediction only]; |
17-78 |
2.58e-04 |
|
Predicted amidohydrolase YtcJ [General function prediction only];
Pssm-ID: 441182 [Multi-domain] Cd Length: 535 Bit Score: 43.63 E-value: 2.58e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1131245802 17 LLIRGGKI--VNDDQSFHADLYVEDGLIKQIG-----ENLIVPG*iRTIDAHGLLVLPGGVDVHTRLLM 78
Cdd:COG1574 10 LLLTNGRIytMDPAQPVAEAVAVRDGRIVAVGsdaevRALAGPAT-EVIDLGGKTVLPGFIDAHVHLLG 77
|
|
| PRK05985 |
PRK05985 |
cytosine deaminase; Provisional |
33-128 |
4.60e-04 |
|
cytosine deaminase; Provisional
Pssm-ID: 180337 [Multi-domain] Cd Length: 391 Bit Score: 42.61 E-value: 4.60e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131245802 33 ADLYVEDGLIKQIGENLIVPG*IRTIDAHGLLVLPGGVDVHTRLLMPVLGM--------------------------TPA 86
Cdd:PRK05985 17 VDILIRDGRIAAIGPALAAPPGAEVEDGGGALALPGLVDGHIHLDKTFWGDpwypnepgpslrerianerrrraasgHPA 96
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 1131245802 87 DDfcQGTK---AALAGGTTMILDHVF--PEAGVS----LLAAYEQWRERAD 128
Cdd:PRK05985 97 AE--RALAlarAAAAAGTTAMRSHVDvdPDAGLRhleaVLAARETLRGLID 145
|
|
| PRK08393 |
PRK08393 |
N-ethylammeline chlorohydrolase; Provisional |
17-88 |
5.37e-04 |
|
N-ethylammeline chlorohydrolase; Provisional
Pssm-ID: 181411 [Multi-domain] Cd Length: 424 Bit Score: 42.48 E-value: 5.37e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1131245802 17 LLIRGGKIVNDD--QSFHADLYVEDGLIKQIGENLIVPG*iRTIDAHGLLVLPGGVDVHTRLLMPVL-GMtpADD 88
Cdd:PRK08393 3 ILIKNGYVIYGEnlKVIRADVLIEGNKIVEVKRNINKPAD-TVIDASGSVVSPGFINAHTHSPMVLLrGL--ADD 74
|
|
| ureC |
PRK13308 |
urease subunit alpha; Reviewed |
33-123 |
1.27e-03 |
|
urease subunit alpha; Reviewed
Pssm-ID: 183965 [Multi-domain] Cd Length: 569 Bit Score: 41.62 E-value: 1.27e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131245802 33 ADLYVEDGLIKQIG------------ENLIVPG*IRTIDAHGLLVLPGGVDVHTRLLMPvlgmtpaddfcQGTKAALAGG 100
Cdd:PRK13308 87 GDIGIRDGRIVGIGkagnpdimdgvdPRLVVGPGTDVRPAEGLIATPGAIDVHVHFDSA-----------QLVDHALASG 155
|
90 100 110
....*....|....*....|....*....|...
gi 1131245802 101 -TTMILDHVFPEAGVS---------LLAAYEQW 123
Cdd:PRK13308 156 iTTMLGGGLGPTVGIDsggpfntgrMLQAAEAW 188
|
|
| Met_dep_hydrolase_C |
cd01309 |
Metallo-dependent hydrolases, subgroup C is part of the superfamily of metallo-dependent ... |
368-413 |
1.44e-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: 1.44e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 1131245802 368 KCVASGQMDENEFVAVTStNAAKIFNFYPRKGRVAVGSDADLVIWN 413
Cdd:cd01309 294 KAVKYGLSYEEALKAITI-NPAKILGIEDRVGSLEPGKDADLVVWN 338
|
|
| PRK07583 |
PRK07583 |
cytosine deaminase; |
25-126 |
1.49e-03 |
|
cytosine deaminase;
Pssm-ID: 236062 Cd Length: 438 Bit Score: 41.12 E-value: 1.49e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131245802 25 VNDDQSFHADLYVEDGLIKQIGENLIVPG*IRTIDAHGLLVLPGGVDVHTRL---------------LMPVLGMTPAD-- 87
Cdd:PRK07583 33 DTLEGLVLVDIEIADGKIAAILPAGGAPDELPAVDLKGRMVWPCFVDMHTHLdkghiwprspnpdgtFPGALDAVTADre 112
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 1131245802 88 ------------DFcqGTKAALAGGTTMI---LDHVFPEAGVSlLAAYEQWRER 126
Cdd:PRK07583 113 ahwsaedlyrrmEF--GLRCAYAHGTSAIrthLDSFAPQAAIS-WEVFAELREA 163
|
|
| AdeC |
COG1001 |
Adenine deaminase [Nucleotide transport and metabolism]; |
17-73 |
2.60e-03 |
|
Adenine deaminase [Nucleotide transport and metabolism];
Pssm-ID: 440625 [Multi-domain] Cd Length: 559 Bit Score: 40.47 E-value: 2.60e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 1131245802 17 LLIRGGKIVN--DDQSFHADLYVEDGLIKQIGEnLIVPG*iRTIDAHGLLVLPGGVDVH 73
Cdd:COG1001 7 LVIKNGRLVNvfTGEILEGDIAIAGGRIAGVGD-YIGEAT-EVIDAAGRYLVPGFIDGH 63
|
|
| Imidazolone-5PH |
cd01296 |
Imidazolonepropionase/imidazolone-5-propionate hydrolase (Imidazolone-5PH) catalyzes the third ... |
35-77 |
2.72e-03 |
|
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: 40.32 E-value: 2.72e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*..
gi 1131245802 35 LYVEDGLIKQIGE----NLIVPG*IRTIDAHGLLVLPGGVDVHTRLL 77
Cdd:cd01296 1 IAIRDGRIAAVGPaaslPAPGPAAAEEIDAGGRAVTPGLVDCHTHLV 47
|
|
| FMDH_A |
cd01304 |
Formylmethanofuran dehydrogenase (FMDH) subunit A; Methanogenic bacteria and archea derive ... |
34-74 |
3.23e-03 |
|
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: 40.47 E-value: 3.23e-03
10 20 30 40
....*....|....*....|....*....|....*....|.
gi 1131245802 34 DLYVEDGlikQIGENLIVPG*IRTIDAHGLLVLPGGVDVHT 74
Cdd:cd01304 19 DIFIRDG---KIVESSSGAKPAKVIDASGKVVMAGGVDMHS 56
|
|
| PRK06038 |
PRK06038 |
N-ethylammeline chlorohydrolase; Provisional |
17-89 |
4.16e-03 |
|
N-ethylammeline chlorohydrolase; Provisional
Pssm-ID: 180363 [Multi-domain] Cd Length: 430 Bit Score: 39.73 E-value: 4.16e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1131245802 17 LLIRGGKIVNDDQS--FHADLYVEDGLIKQIGENliVPG*IRT-IDAHGLLVLPGGVDVHTRLLMPVL-GMtpADDF 89
Cdd:PRK06038 4 IIIKNAYVLTMDAGdlKKGSVVIEDGTITEVSES--TPGDADTvIDAKGSVVMPGLVNTHTHAAMTLFrGY--ADDL 76
|
|
| Met_dep_hydrolase_C |
cd01309 |
Metallo-dependent hydrolases, subgroup C is part of the superfamily of metallo-dependent ... |
39-76 |
4.81e-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: 39.60 E-value: 4.81e-03
10 20 30
....*....|....*....|....*....|....*...
gi 1131245802 39 DGLIKQIGENLIVPG*IRTIDAHGLLVLPGGVDVHTRL 76
Cdd:cd01309 1 DGKIVAVGAEITTPADAEVIDAKGKHVTPGLIDAHSHL 38
|
|
| Urease_alpha |
cd00375 |
Urease alpha-subunit; Urease is a nickel-dependent metalloenzyme that catalyzes the hydrolysis ... |
33-104 |
7.31e-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: 39.23 E-value: 7.31e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131245802 33 ADLYVEDGLIKQIG------------ENLIVPG*IRTIDAHGLLVLPGGVDVHTRLLMPvlgmtpaddfcQGTKAALAGG 100
Cdd:cd00375 83 ADIGIKDGRIVAIGkagnpdimdgvtPNMIVGPSTEVIAGEGKIVTAGGIDTHVHFICP-----------QQIEEALASG 151
|
....*
gi 1131245802 101 -TTMI 104
Cdd:cd00375 152 iTTMI 156
|
|
| ureB |
PRK13985 |
urease subunit alpha; |
19-113 |
8.86e-03 |
|
urease subunit alpha;
Pssm-ID: 184438 [Multi-domain] Cd Length: 568 Bit Score: 38.72 E-value: 8.86e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131245802 19 IRGGKIVNDDQSFHADLyvEDGlikqIGENLIVPG*IRTIDAHGLLVLPGGVDVHTRLLMPvlgmtpaddfcQGTKAALA 98
Cdd:PRK13985 87 IKDGKIAGIGKGGNKDM--QDG----VKNNLSVGPATEALAGEGLIVTAGGIDTHIHFISP-----------QQIPTAFA 149
|
90
....*....|....*.
gi 1131245802 99 GG-TTMILDHVFPEAG 113
Cdd:PRK13985 150 SGvTTMIGGGTGPADG 165
|
|
| |
