|
Name |
Accession |
Description |
Interval |
E-value |
| D-HYD |
cd01314 |
D-hydantoinases (D-HYD) also called dihydropyrimidases (DHPase) and related proteins; DHPases ... |
10-459 |
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: 628.09 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66392186 10 ILIKGGKVVNDDFTQEADVYIENGIIQQVGKELMIPGGAKVIDATGKLVLPGGIDTSVHLNESFMNGTTADDFYSGTKAA 89
Cdd:cd01314 1 LIIKNGTIVTADGSFKADILIEDGKIVAIGPNLEAPGGVEVIDATGKYVLPGGIDPHTHLELPFMGTVTADDFESGTRAA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66392186 90 LAGGTTMVIGHVLPEKNESLLDAYEKARSHADAKACCDYALHMGVTWWGPKARAQMETLVrDKGVNSFQMYMAYKDMYML 169
Cdd:cd01314 81 AAGGTTTIIDFAIPNKGQSLLEAVEKWRGKADGKSVIDYGFHMIITDWTDSVIEELPELV-KKGISSFKVFMAYKGLLMV 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66392186 170 RDSELFQALQNCKDIGAVARVHAENGELVAEGAREALDLGISGPEGIEISRPEELEAEAVHRAITIANRAHCPIYLVNVS 249
Cdd:cd01314 160 DDEELLDVLKRAKELGALVMVHAENGDVIAELQKKLLAQGKTGPEYHALSRPPEVEAEATARAIRLAELAGAPLYIVHVS 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66392186 250 SMSAGDVLASAKMQGKVVHGETTTAHAVLNGmQYYHQDWAHAAAFVTVPPLRlDPNTPNYLLSLLGNDTLNVVTSDHRPF 329
Cdd:cd01314 240 SKEAADEIARARKKGLPVYGETCPQYLLLDD-SDYWKDWFEGAKYVCSPPLR-PKEDQEALWDGLSSGTLQTVGSDHCPF 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66392186 330 TTKQKAMGKDDFTKIPHGVPGVQDRMSVMWERGVVGGKMDENRFVAVTSSNAAKIYNLYPRKGRIIPGADADVVVWDPES 409
Cdd:cd01314 318 NFAQKARGKDDFTKIPNGVPGVETRMPLLWSEGVAKGRITLEKFVELTSTNPAKIFGLYPRKGTIAVGSDADLVIWDPNA 397
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|
gi 66392186 410 TRTISVTTQWQGGDVNLYENLRCHGVPLVTISRGRVVYENGIFTCAEGSG 459
Cdd:cd01314 398 EKTISADTHHHNVDYNIFEGMKVKGWPVVTISRGKVVVEDGELVGEKGSG 447
|
|
| D-hydantoinase |
TIGR02033 |
D-hydantoinase; This model represents the D-hydantoinase (dihydropyrimidinase) which primarily ... |
10-463 |
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: 558.93 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66392186 10 ILIKGGKVVNDDFTQEADVYIENGIIQQVGKELMIPGGAKVIDATGKLVLPGGIDTSVHLNESFMNGTTADDFYSGTKAA 89
Cdd:TIGR02033 1 LLIKGGTVVNADDVFQADVLIEGGKIVAVGDNLIPPDAVEVIDATGKYVLPGGIDVHTHLEMPFGGTTTADDFFTGTKAA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66392186 90 LAGGTTMVIGHVLPEKNESLLDAYEKARSHADAKACCDYALHMGVTWWGPKARAQMETLVRDKGVNSFQMYMAYKDMYML 169
Cdd:TIGR02033 81 AAGGTTTIIDFVVPEKGSSLTEALETWHEKAEGKSVIDYGFHMDITHWNDSVLEEHIPEVKEEGINSFKVFMAYKNLLMV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66392186 170 RDSELFQALQNCKDIGAVARVHAENGELVAEGAREALDLGISGPEGIEISRPEELEAEAVHRAITIANRAHCPIYLVNVS 249
Cdd:TIGR02033 161 DDEELFEILKRLKELGALLQVHAENGDIIAELQARMLAQGITGPEYHALSRPPELEAEAVARAITLAALADAPLYVVHVS 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66392186 250 SMSAGDVLASAKMQGKVVHGETTTAHAVLNGmQYYHQDWAHAAAFVTVPPLRlDPNTPNYLLSLLGNDTLNVVTSDHRPF 329
Cdd:TIGR02033 241 TKDAADEIAQARKKGQPVFGETCPQYLVLDD-THYDKPGFEGAKYVCSPPLR-EPEDQDALWSALSSGALQTVGSDHCTF 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66392186 330 -TTKQKAMGKDDFTKIPHGVPGVQDRMSVMWERGVVGGKMDENRFVAVTSSNAAKIYNLYPRKGRIIPGADADVVVWDPE 408
Cdd:TIGR02033 319 nFAQKKAIGKDDFTKIPNGGPGVEERMSLLFDEGVAKGRITLEKFVEVTSTNPAKIFNLYPRKGTIAVGSDADIVIWDPN 398
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*
gi 66392186 409 STRTISVTTQWQGGDVNLYENLRCHGVPLVTISRGRVVYENGIFTCAEGSGKFYP 463
Cdd:TIGR02033 399 RTTVISAETHHSNADYNPFEGFKVRGAPVSVLSRGRVVVEDGQLVGTAGAGRFVK 453
|
|
| PRK08323 |
PRK08323 |
phenylhydantoinase; Validated |
9-468 |
0e+00 |
|
phenylhydantoinase; Validated
Pssm-ID: 236240 [Multi-domain] Cd Length: 459 Bit Score: 552.09 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66392186 9 RILIKGGKVVNDDFTQEADVYIENGIIQQVGKelmiPGGAKVIDATGKLVLPGGIDTSVHLNESFMNGTTADDFYSGTKA 88
Cdd:PRK08323 2 STLIKNGTVVTADDTYKADVLIEDGKIAAIGA----NLGDEVIDATGKYVMPGGIDPHTHMEMPFGGTVSSDDFETGTRA 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66392186 89 ALAGGTTMVIGHVLPEKNESLLDAYEKARSHADAKACCDYALHMGVTWWGPKARAQMETLVrDKGVNSFQMYMAYKDMYM 168
Cdd:PRK08323 78 AACGGTTTIIDFALQPKGQSLREALEAWHGKAAGKAVIDYGFHMIITDWNEVVLDEMPELV-EEGITSFKLFMAYKGALM 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66392186 169 LRDSELFQALQNCKDIGAVARVHAENGELVAEGAREALDLGISGPEGIEISRPEELEAEAVHRAITIANRAHCPIYLVNV 248
Cdd:PRK08323 157 LDDDELLRALQRAAELGALPMVHAENGDAIAYLQAKLLAEGKTGPEYHALSRPPEVEGEATNRAIMLAELAGAPLYIVHV 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66392186 249 SSMSAGDVLASAKMQGKVVHGETTTAHAVLNGMQYYHQDWAHAAAFVTVPPLRlDPNTPNYLLSLLGNDTLNVVTSDHRP 328
Cdd:PRK08323 237 SCKEALEAIRRARARGQRVFGETCPQYLLLDESEYDGPDWFEGAKYVMSPPLR-DKEHQDALWRGLQDGDLQVVATDHCP 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66392186 329 FTTKQKAM-GKDDFTKIPHGVPGVQDRMSVMWERGVVGGKMDENRFVAVTSSNAAKIYNLYPRKGRIIPGADADVVVWDP 407
Cdd:PRK08323 316 FCFEQKKQlGRGDFTKIPNGTPGVEDRMPLLFSEGVMTGRITLNRFVELTSTNPAKIFGLYPRKGTIAVGADADIVIWDP 395
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 66392186 408 ESTRTISVTTQWQGGDVNLYENLRCHGVPLVTISRGRVVYENGIFTCAEGSGKFYPLRTFP 468
Cdd:PRK08323 396 NATKTISASTLHSNVDYNPYEGFEVTGWPVTTLSRGEVVVEDGEFRGKAGHGRFLKRKPFQ 456
|
|
| PLN02942 |
PLN02942 |
dihydropyrimidinase |
7-479 |
3.97e-175 |
|
dihydropyrimidinase
Pssm-ID: 178530 Cd Length: 486 Bit Score: 503.99 E-value: 3.97e-175
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66392186 7 TVRILIKGGKVVNDDFTQEADVYIENGIIQQVGKELMIPGGAKVIDATGKLVLPGGIDTSVHLNESFMNGTTADDFYSGT 86
Cdd:PLN02942 4 STKILIKGGTVVNAHHQELADVYVEDGIIVAVAPNLKVPDDVRVIDATGKFVMPGGIDPHTHLAMPFMGTETIDDFFSGQ 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66392186 87 KAALAGGTTMVIGHVLPeKNESLLDAYEKARSHAdAKACCDYALHMGVTWWGPKARAQMETLVRDKGVNSFQMYMAYKDM 166
Cdd:PLN02942 84 AAALAGGTTMHIDFVIP-VNGNLLAGYEAYEKKA-EKSCMDYGFHMAITKWDDTVSRDMETLVKEKGINSFKFFMAYKGS 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66392186 167 YMLRDSELFQALQNCKDIGAVARVHAENGELVAEGAREALDLGISGPEGIEISRPEELEAEAVHRAITIANRAHCPIYLV 246
Cdd:PLN02942 162 LMVTDELLLEGFKRCKSLGALAMVHAENGDAVFEGQKRMIELGITGPEGHALSRPPLLEGEATARAIRLAKFVNTPLYVV 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66392186 247 NVSSMSAGDVLASAKMQGKVVHGETTTAHAVLNGMQYYHQDWAHAAAFVTVPPLRldPNTPNYLL-SLLGNDTLNVVTSD 325
Cdd:PLN02942 242 HVMSIDAMEEIARARKSGQRVIGEPVVSGLVLDDSKLWDPDFTIASKYVMSPPIR--PAGHGKALqAALSSGILQLVGTD 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66392186 326 HRPFTTKQKAMGKDDFTKIPHGVPGVQDRMSVMWERGVVGGKMDENRFVAVTSSNAAKIYNLYPRKGRIIPGADADVVVW 405
Cdd:PLN02942 320 HCPFNSTQKAFGKDDFRKIPNGVNGIEERMHLVWDTMVESGQISPTDYVRVTSTECAKIFNIYPRKGAILAGSDADIIIL 399
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 66392186 406 DPESTRTISVTTQWQGGDVNLYENLRCHGVPLVTISRGRVVYENGIFTCAEGSGKFYPLRTFPdYLYKKMVQRE 479
Cdd:PLN02942 400 NPNSTFTISAKTHHSRIDTNVYEGRRGKGKVEVTISQGRVVWENGELKVVRGSGRYIEMPPFS-YLFDGIQKAD 472
|
|
| AllB |
COG0044 |
Dihydroorotase or related cyclic amidohydrolase [Nucleotide transport and metabolism]; ... |
11-461 |
8.30e-136 |
|
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: 401.78 E-value: 8.30e-136
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66392186 11 LIKGGKVVNDDFTQEADVYIENGIIQQVGKELMIPGGAKVIDATGKLVLPGGIDTSVHLNESFMngTTADDFYSGTKAAL 90
Cdd:COG0044 1 LIKNGRVVDPGGLERADVLIEDGRIAAIGPDLAAPEAAEVIDATGLLVLPGLIDLHVHLREPGL--EHKEDIETGTRAAA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66392186 91 AGGTTMVIGHVLPEKNESLLDAYEKARSHADAKACCDYALHMGVTWWGPKARAQMETLVrDKGVNSFQMYMAYKD-MYML 169
Cdd:COG0044 79 AGGVTTVVDMPNTNPVTDTPEALEFKLARAEEKALVDVGPHGALTKGLGENLAELGALA-EAGAVAFKVFMGSDDgNPVL 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66392186 170 RDSELFQALQNCKDIGAVARVHAENGELVAEGAREAldlGISGPEGIEISRPEELEAEAVHRAITIANRAHCPIYLVNVS 249
Cdd:COG0044 158 DDGLLRRALEYAAEFGALVAVHAEDPDLIRGGVMNE---GKTSPRLGLKGRPAEAEEEAVARDIALAEETGARLHIVHVS 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66392186 250 SMSAGDVLASAKMQGKVVHGETTTAHAVLNGMQYYHQDwahaAAFVTVPPLRlDPNTPNYLLSLLGNDTLNVVTSDHRPF 329
Cdd:COG0044 235 TAEAVELIREAKARGLPVTAEVCPHHLTLTDEDLERYG----TNFKVNPPLR-TEEDREALWEGLADGTIDVIATDHAPH 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66392186 330 TTKQKAmgkDDFTKIPHGVPGVQDRMSVMWERGVVGGKMDENRFVAVTSSNAAKIYNLyPRKGRIIPGADADVVVWDPES 409
Cdd:COG0044 310 TLEEKE---LPFAEAPNGIPGLETALPLLLTELVHKGRLSLERLVELLSTNPARIFGL-PRKGRIAVGADADLVLFDPDA 385
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|..
gi 66392186 410 TRTISVTTQWQGGDVNLYENLRCHGVPLVTISRGRVVYENGIFTcAEGSGKF 461
Cdd:COG0044 386 EWTVTAEDLHSKSKNTPFEGRELTGRVVATIVRGRVVYEDGEVV-GEPRGRF 436
|
|
| PRK13404 |
PRK13404 |
dihydropyrimidinase; Provisional |
12-469 |
1.77e-116 |
|
dihydropyrimidinase; Provisional
Pssm-ID: 184033 [Multi-domain] Cd Length: 477 Bit Score: 353.62 E-value: 1.77e-116
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66392186 12 IKGGKVVNDDFTQEADVYIENGIIQQVGKELmiPGGAKVIDATGKLVLPGGIDTSVHLN-ESFMNGTTADDFYSGTKAAL 90
Cdd:PRK13404 8 IRGGTVVTATDTFQADIGIRGGRIAALGEGL--GPGAREIDATGRLVLPGGVDSHCHIDqPSGDGIMMADDFYTGTVSAA 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66392186 91 AGGTTMVIGHVLPEKNESLLDAYEKARSHADAKACCDYALHMGVTWWGPKARAQ-METLVRDkGVNSFQMYMAYKDMyML 169
Cdd:PRK13404 86 FGGTTTVIPFAAQHRGQSLREAVEDYHRRAAGKAVIDYAFHLIVADPTEEVLTEeLPALIAQ-GYTSFKVFMTYDDL-KL 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66392186 170 RDSELFQALQNCKDIGAVARVHAENGELVAEGAREALDLGISGPEGIEISRPEELEAEAVHRAITIANRAHCPIYLVNVS 249
Cdd:PRK13404 164 DDRQILDVLAVARRHGAMVMVHAENHDMIAWLTKRLLAAGLTAPKYHAISRPMLAEREATHRAIALAELVDVPILIVHVS 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66392186 250 SMSAGDVLASAKMQGKVVHGETTTAHAVLNGMQYyHQDWAHAAAFVTVPPLRlDPNTPNYLLSLLGNDTLNVVTSDHRPF 329
Cdd:PRK13404 244 GREAAEQIRRARGRGLKIFAETCPQYLFLTAEDL-DRPGMEGAKYICSPPPR-DKANQEAIWNGLADGTFEVFSSDHAPF 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66392186 330 ---TTKQKAMGKDD--FTKIPHGVPGVQDRMSVMWERGVVGGKMDENRFVAVTSSNAAKIYNLYPRKGRIIPGADADVVV 404
Cdd:PRK13404 322 rfdDTDGKLAAGANpsFKAIANGIPGIETRLPLLFSEGVVKGRISLNRFVALTSTNPAKLYGLYPRKGAIAIGADADIAI 401
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 66392186 405 WDPESTRTISVTTQWQGGDVNLYENLRCHGVPLVTISRGRVVYENGIFTCAEGSGKFYPlRTFPD 469
Cdd:PRK13404 402 WDPDREVTITNADLHHAADYTPYEGMRVTGWPVTVLSRGRVVVEDGELVAERGSGQFLA-RSLPD 465
|
|
| L-HYD_ALN |
cd01315 |
L-Hydantoinases (L-HYDs) and Allantoinase (ALN); L-Hydantoinases are a member of the ... |
11-450 |
6.45e-76 |
|
L-Hydantoinases (L-HYDs) and Allantoinase (ALN); L-Hydantoinases are a member of the dihydropyrimidinase family, which catalyzes the reversible hydrolytic ring opening of dihydropyrimidines and hydantoins (five-membered cyclic diamides used in biotechnology). But L-HYDs differ by having an L-enantio specificity and by lacking activity on possible natural substrates such as dihydropyrimidines. Allantoinase catalyzes the hydrolytic cleavage of the five-member ring of allantoin (5-ureidohydantoin) to form allantoic acid.
Pssm-ID: 238640 [Multi-domain] Cd Length: 447 Bit Score: 247.59 E-value: 6.45e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66392186 11 LIKGGKVVNDDFTQEADVYIENGIIQQVGKELMIPGGAKVIDATGKLVLPGGIDTSVHLNEsfMNGTTADDFYSGTKAAL 90
Cdd:cd01315 3 VIKNGRVVTPDGVREADIAVKGGKIAAIGPDIANTEAEEVIDAGGLVVMPGLIDTHVHINE--PGRTEWEGFETGTKAAA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66392186 91 AGGTTMVIGhvLPEKN-------ESLLDAYEKARShadaKACCDYALHMGVTwwgPKARAQMETLVrDKGVNSFQMYMAY 163
Cdd:cd01315 81 AGGITTIID--MPLNSipptttvENLEAKLEAAQG----KLHVDVGFWGGLV---PGNLDQLRPLD-EAGVVGFKCFLCP 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66392186 164 K--DMY-MLRDSELFQALQNCKDIGAVARVHAENGELVAEGAREALDLGISGPEGIEISRPEELEAEAVHRAITIANRAH 240
Cdd:cd01315 151 SgvDEFpAVDDEQLEEAMKELAKTGSVLAVHAENPEITEALQEQAKAKGKRDYRDYLASRPVFTEVEAIQRILLLAKETG 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66392186 241 CPIYLVNVSSMSAGDVLASAKMQGKVVHGETTTAHAVLNgmqyyHQDW-AHAAAFVTVPPLRlDPNTPNYLLSLLGNDTL 319
Cdd:cd01315 231 CRLHIVHLSSAEAVPLIREARAEGVDVTVETCPHYLTFT-----AEDVpDGGTEFKCAPPIR-DAANQEQLWEALENGDI 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66392186 320 NVVTSDHRPFTTKQKAMGKDDFTKIPHGVPGVQDRMSVMWERGVVGGKMDENRFVAVTSSNAAKIYNLYPRKGRIIPGAD 399
Cdd:cd01315 305 DMVVSDHSPCTPELKLLGKGDFFKAWGGISGLQLGLPVMLTEAVNKRGLSLEDIARLMCENPAKLFGLSHQKGRIAVGYD 384
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....
gi 66392186 400 ADVVVWDPESTRTI---SVTTQWQggdVNLYENLRCHGVPLVTISRGRVVYENG 450
Cdd:cd01315 385 ADFVVWDPEEEFTVdaeDLYYKNK---ISPYVGRTLKGRVHATILRGTVVYQDG 435
|
|
| PRK02382 |
PRK02382 |
dihydroorotase; Provisional |
10-465 |
4.85e-67 |
|
dihydroorotase; Provisional
Pssm-ID: 179417 [Multi-domain] Cd Length: 443 Bit Score: 224.15 E-value: 4.85e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66392186 10 ILIKGGKVVNDDFTQEADVYIENGIIQQVGKELMIPGGAKVIDATGKLVLPGGIDTSVHLNEsfMNGTTADDFYSGTKAA 89
Cdd:PRK02382 4 ALLKDGRVYYNNSLQPRDVRIDGGKITAVGKDLDGSSSEEVIDARGMLLLPGGIDVHVHFRE--PGYTHKETWYTGSRSA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66392186 90 LAGGTTMVIGHvlPEKNESLLD--AYEKARSHADAKACCDYALHMGVT-WWGPkaraqMETLVRdKGVNSF-QMYMAYKD 165
Cdd:PRK02382 82 AAGGVTTVVDQ--PNTDPPTVDgeSFDEKAELAARKSIVDFGINGGVTgNWDP-----LESLWE-RGVFALgEIFMADST 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66392186 166 MYMLRDSELF-QALQNCKDIGAVARVHAENGELVAEGAREaLDlGISGPEGIEISRPEELEAEAVHRAITIANRAHCPIY 244
Cdd:PRK02382 154 GGMGIDEELFeEALAEAARLGVLATVHAEDEDLFDELAKL-LK-GDADADAWSAYRPAAAEAAAVERALEVASETGARIH 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66392186 245 LVNVSSMSAGDVLASAKMQgkvvhGETTTAHAVLNgmqyyHQDWAHAAAFVTV-PPLRLDPNTpNYLLSLLGNDTLNVVT 323
Cdd:PRK02382 232 IAHISTPEGVDAARREGIT-----CEVTPHHLFLS-----RRDWERLGTFGKMnPPLRSEKRR-EALWERLNDGTIDVVA 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66392186 324 SDHRPFTTKQKAMgkdDFTKIPHGVPGVQDRMSVMWErGVVGGKMDENRFVAVTSSNAAKIYNLyPRKGRIIPGADADVV 403
Cdd:PRK02382 301 SDHAPHTREEKDA---DIWDAPSGVPGVETMLPLLLA-AVRKNRLPLERVRDVTAANPARIFGL-DGKGRIAEGYDADLV 375
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 66392186 404 VWDPESTRTISVTTQWQGGDVNLYENLRchGV-PLVTISRGRVVYENGIFTCAEGSGKFYPLR 465
Cdd:PRK02382 376 LVDPDAAREIRGDDLHSKAGWTPFEGME--GVfPELTMVRGTVVWDGDDINAKRGRGEFLRGR 436
|
|
| allantoinase |
TIGR03178 |
allantoinase; This enzyme carries out the first step in the degradation of allantoin, a ... |
10-453 |
2.18e-61 |
|
allantoinase; This enzyme carries out the first step in the degradation of allantoin, a ring-opening hydrolysis. The seed members of this model are all in the vicinity of other genes involved in the processes of xanthine/urate/allantoin catabolism. Although not included in the seed, many eukaryotic homologs of this family are included above the trusted cutoff. Below the noise cutoff are related hydantoinases.
Pssm-ID: 163175 [Multi-domain] Cd Length: 443 Bit Score: 209.16 E-value: 2.18e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66392186 10 ILIKGGKVVNDDFTQEADVYIENGIIQQVGKElMIPGGAKVIDATGKLVLPGGIDTSVHLNESfmnGTTA-DDFYSGTKA 88
Cdd:TIGR03178 2 LIIRGGRVILPNGEREADVGVKGGKIAAIGPD-ILGPAAKIIDAGGLVVFPGVVDTHVHINEP---GRTEwEGFETGTRA 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66392186 89 ALAGGTT----MVIGHVLPEKNEsllDAYEKARSHADAKACCDYALHMGVTwwgPKARAQMETLvRDKGVNSFQMYMAY- 163
Cdd:TIGR03178 78 AAAGGITtyidMPLNSIPATTTR---ASLEAKFEAAKGKLAVDVGFWGGLV---PYNLDDLREL-DEAGVVGFKAFLSPs 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66392186 164 --KDMYMLRDSELFQALQNCKDIGAVARVHAENGELVAEGAREALDLGISGPEGIEISRPEELEAEAVHRAITIANRAHC 241
Cdd:TIGR03178 151 gdDEFPHVDDWQLYKGMRELARLGQLLLVHAENPAITSALGEEAPPQGGVGADAYLASRPVFAEVEAIRRTLALAKVTGC 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66392186 242 PIYLVNVSSMSAGDVLASAKMQGKVVHGETTTaHAVLngmqYYHQDWAH-AAAFVTVPPLRlDPNTPNYLLSLLGNDTLN 320
Cdd:TIGR03178 231 RVHVVHLSSAEAVELITEAKQEGLDVTVETCP-HYLT----LTAEEVPDgGTLAKCAPPIR-DLANQEGLWEALLNGLID 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66392186 321 VVTSDHRPFTTKQKAmgKDDFTKIPHGVPGVQDRMSVMWERGVVGGKMDENRFVAVTSSNAAKIYNLyPRKGRIIPGADA 400
Cdd:TIGR03178 305 CVVSDHSPCTPDLKR--AGDFFKAWGGIAGLQSTLDVMFDEAVQKRGLPLEDIARLMATNPAKRFGL-AQKGRIAPGKDA 381
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|...
gi 66392186 401 DVVVWDPESTRTISVTTQWQGGDVNLYENLRCHGVPLVTISRGRVVYENGIFT 453
Cdd:TIGR03178 382 DFVFVDPDESYTLTPDDLYYRHKVSPYVGRTIGGRVRATYLRGQCIYDDEQFI 434
|
|
| PRK06189 |
PRK06189 |
allantoinase; Provisional |
10-453 |
2.88e-58 |
|
allantoinase; Provisional
Pssm-ID: 235732 [Multi-domain] Cd Length: 451 Bit Score: 201.08 E-value: 2.88e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66392186 10 ILIKGGKVVNDDFTQEADVYIENGIIQQVGKELMIPGgAKVIDATGKLVLPGGIDTSVHLNESfmNGTTADDFYSGTKAA 89
Cdd:PRK06189 5 LIIRGGKVVTPEGVYRADIGIKNGKIAEIAPEISSPA-REIIDADGLYVFPGMIDVHVHFNEP--GRTHWEGFATGSAAL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66392186 90 LAGGTT----MVIGHVLPEKNESLLDAYEKArshADAKACCDYALHMGVTwwgPKARAQMETLVrDKGVNSFQMYMAYKD 165
Cdd:PRK06189 82 AAGGCTtyfdMPLNSIPPTVTREALDAKAEL---ARQKSAVDFALWGGLV---PGNLEHLRELA-EAGVIGFKAFMSNSG 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66392186 166 MYMLR---DSELFQALQNCKDIGAVARVHAENGELVAEGAREALDLGISGPEGIEISRPEELEAEAVHRAITIANRAHCP 242
Cdd:PRK06189 155 TDEFRssdDLTLYEGMKEIAALGKILALHAESDALTRHLTTQARQQGKTDVRDYLESRPVVAELEAVQRALLYAQETGCP 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66392186 243 IYLVNVSSMSAGDVLASAKMQGKVVHGETTtAHAVLngmqYYHQDWAH-AAAFVTVPPLRlDPNTPNYLLSLLGNDTLNV 321
Cdd:PRK06189 235 LHFVHISSGKAVALIAEAKKRGVDVSVETC-PHYLL----FTEEDFERiGAVAKCAPPLR-SRSQKEELWRGLLAGEIDM 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66392186 322 VTSDHRPFTTKQKAmgKDDFTKIPHGVPGVQDRMSVMWERGVVGGKMDENRFVAVTSSNAAKIYNLyPRKGRIIPGADAD 401
Cdd:PRK06189 309 ISSDHSPCPPELKE--GDDFFLVWGGISGGQSTLLVMLTEGYIERGIPLETIARLLATNPAKRFGL-PQKGRLEVGADAD 385
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|..
gi 66392186 402 VVVWDPESTRTISVTTQWQGGDVNLYENLRCHGVPLVTISRGRVVYENGIFT 453
Cdd:PRK06189 386 FVLVDLDETYTLTKEDLFYRHKQSPYEGRTFPGRVVATYLRGQCVYQDGEVF 437
|
|
| Cyclic_amidohydrolases |
cd01302 |
Cyclic amidohydrolases, including hydantoinase, dihydropyrimidinase, allantoinase, and ... |
56-439 |
5.36e-57 |
|
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: 194.15 E-value: 5.36e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66392186 56 KLVLPGGIDTSVHLNESFMnGTTADDFYSGTKAALAGGTTMVIGHVLPEKNESLLDAYEKARSHADAKACCDYALHMGVT 135
Cdd:cd01302 1 LLVLPGFIDIHVHLRDPGG-TTYKEDFESGSRAAAAGGVTTVIDMPNTGPPPIDLPAIELKIKLAEESSYVDFSFHAGIG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66392186 136 wwgpkARAQMETL--VRDKGVNSFQMYMAYK--DMYMLRDSELFQALQNCKDIGAVARVHAEngelvaegarealdlgis 211
Cdd:cd01302 80 -----PGDVTDELkkLFDAGINSLKVFMNYYfgELFDVDDGTLMRTFLEIASRGGPVMVHAE------------------ 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66392186 212 gpegieisrpeeleaeavhRAITIANRAHCPIYLVNVSSMSAGDVLASAKMQGKVVHGETTTAHAVLNgmqyyHQDWAHA 291
Cdd:cd01302 137 -------------------RAAQLAEEAGANVHIAHVSSGEALELIKFAKNKGVKVTCEVCPHHLFLD-----ESMLRLN 192
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66392186 292 AAFVTV-PPLRlDPNTPNYLLSLLGNDTLNVVTSDHRPFTTKQKAMGKdDFTKIPHGVPGVQDRMSVMWERGVVGGkMDE 370
Cdd:cd01302 193 GAWGKVnPPLR-SKEDREALWEGVKNGKIDTIASDHAPHSKEEKESGK-DIWKAPPGFPGLETRLPILLTEGVKRG-LSL 269
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 66392186 371 NRFVAVTSSNAAKIYNLYPrKGRIIPGADADVVVWDPESTRTISVTTQWQGGDVNLYENLRCHGVPLVT 439
Cdd:cd01302 270 ETLVEILSENPARIFGLYP-KGTIAVGYDADLVIVDPKKEWKVTAEEIESKADWTPFEGMEVTGKPVST 337
|
|
| pyrC_multi |
TIGR00857 |
dihydroorotase, multifunctional complex type; In contrast to the homodimeric type of ... |
25-449 |
1.53e-54 |
|
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: 189.96 E-value: 1.53e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66392186 25 EADVYIENGIIQQVGKeLMIPGGAKVIDATGKLVLPGGIDTSVHLNEsfMNGTTADDFYSGTKAALAGGTTMVIghVLPE 104
Cdd:TIGR00857 5 EVDILVEGGRIKKIGK-LRIPPDAEVIDAKGLLVLPGFIDLHVHLRD--PGEEYKEDIESGSKAAAHGGFTTVA--DMPN 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66392186 105 KNESLLDA--YEKARSHADAKACCDYALHMGVTW-WGPKARAQMETLVRDK--GVNSFQMYMAYKDMYMLRdselfQALQ 179
Cdd:TIGR00857 80 TKPPIDTPetLEWKLQRLKKVSLVDVHLYGGVTQgNQGKELTEAYELKEAGavGRMFTDDGSEVQDILSMR-----RALE 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66392186 180 NCKDIGAVARVHAENGELVAEG-AREaldlGISGPEGIEISRPEELEAEAVHRAITIANRAHCPIYLVNVSSMSAGDVLA 258
Cdd:TIGR00857 155 YAAIAGVPIALHAEDPDLIYGGvMHE----GPSAAQLGLPARPPEAEEVAVARLLELAKHAGCPVHICHISTKESLELIV 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66392186 259 SAKMQGKVVHGETTTAHAVLNgmqyyHQDWAHAAAFVTV-PPLRlDPNTPNYLLSLLGNDTLNVVTSDHRPFTTKQKAMG 337
Cdd:TIGR00857 231 KAKSQGIKITAEVTPHHLLLS-----EEDVARLDGNGKVnPPLR-EKEDRLALIEGLKDGIIDIIATDHAPHTLEEKTKE 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66392186 338 kddFTKIPHGVPGVQDRMSVMWERgVVGGKMDENRFVAVTSSNAAKIYNLyPRKGRIIPGADADVVVWDPESTRTISVTT 417
Cdd:TIGR00857 305 ---FAAAPPGIPGLETALPLLLQL-LVKGLISLKDLIRMLSINPARIFGL-PDKGTLEEGNPADITVFDLKKEWTINAET 379
|
410 420 430
....*....|....*....|....*....|..
gi 66392186 418 QWQGGDVNLYENLRCHGVPLVTISRGRVVYEN 449
Cdd:TIGR00857 380 FYSKAKNTPFEGMSLKGKPIATILRGKVVYED 411
|
|
| DHOase_IIa |
cd01317 |
Dihydroorotase (DHOase), subgroup IIa; DHOases catalyze the reversible interconversion of ... |
47-439 |
2.40e-46 |
|
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: 166.64 E-value: 2.40e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66392186 47 GAKVIDATGKLVLPGGIDTSVHLNESfmNGTTADDFYSGTKAALAGGTTMVIghVLP-----EKNESLLDAY-EKARSHA 120
Cdd:cd01317 1 DAEVIDAEGKILAPGLVDLHVHLREP--GFEYKETLESGAKAAAAGGFTTVV--CMPntnpvIDNPAVVELLkNRAKDVG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66392186 121 DAKACCDYALHMGVTwwGpKARAQMETLvRDKGVNSFQmymayKDMYMLRDSELFQ-ALQNCKDIGAVARVHAENGELVA 199
Cdd:cd01317 77 IVRVLPIGALTKGLK--G-EELTEIGEL-LEAGAVGFS-----DDGKPIQDAELLRrALEYAAMLDLPIIVHPEDPSLAG 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66392186 200 EGAreALDLGISGPEGIeISRPEELEAEAVHRAITIANRAHCPIYLVNVSSMSAGDVLASAKMQGKVVHGETTTAHAVLN 279
Cdd:cd01317 148 GGV--MNEGKVASRLGL-PGIPPEAETIMVARDLELAEATGARVHFQHLSTARSLELIRKAKAKGLPVTAEVTPHHLLLD 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66392186 280 GMQYYHQDwahaAAFVTVPPLRlDPNTPNYLLSLLGNDTLNVVTSDHRPFTTKQKAMGKDDftkIPHGVPGVQDRMSVMW 359
Cdd:cd01317 225 DEALESYD----TNAKVNPPLR-SEEDREALIEALKDGTIDAIASDHAPHTDEEKDLPFAE---APPGIIGLETALPLLW 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66392186 360 ERGVVGGKMDENRFVAVTSSNAAKIYNLYPrkGRIIPGADADVVVWDPESTRTISVTTQWQGGDVNLYENLRCHGVPLVT 439
Cdd:cd01317 297 TLLVKGGLLTLPDLIRALSTNPAKILGLPP--GRLEVGAPADLVLFDPDAEWIVDEETFRSKSKNTPFDGQKLKGRVLAT 374
|
|
| DHOase_IIb |
cd01318 |
Dihydroorotase (DHOase), subgroup IIb; DHOases catalyze the reversible interconversion of ... |
55-443 |
5.83e-45 |
|
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: 162.50 E-value: 5.83e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66392186 55 GKLVLPGGIDTSVHLNESFMngTTADDFYSGTKAALAGGTTMVIGhvLPEKNESLLD--AYEKARSHADAKACCDYALHM 132
Cdd:cd01318 1 GLLILPGVIDIHVHFREPGL--TYKEDFVSGSRAAAAGGVTTVMD--MPNTKPPTTTaeALYEKLRLAAAKSVVDYGLYF 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66392186 133 GVTwwGPKARAQMETLvrdkGVNSFQMYMAYKDMYMLRDSE-LFQALQNCKDIGAVarvHAENGELVAEGAREALDLGIs 211
Cdd:cd01318 77 GVT--GSEDLEELDKA----PPAGYKIFMGDSTGDLLDDEEtLERIFAEGSVLVTF---HAEDEDRLRENRKELKGESA- 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66392186 212 gpegIEISRPEELEAEAVHRAITIANRAHCPIYLVNVSSmsaGDVLASAKMQGKVVHGETTTAHAVLNgmqyyHQDWAHA 291
Cdd:cd01318 147 ----HPRIRDAEAAAVATARALKLARRHGARLHICHVST---PEELKLIKKAKPGVTVEVTPHHLFLD-----VEDYDRL 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66392186 292 AAFVTV-PPLRlDPNTPNYLLSLLGNDTLNVVTSDHRPFTTKQKAMGkddFTKIPHGVPGVQDRMSVM---WERGVVGGK 367
Cdd:cd01318 215 GTLGKVnPPLR-SREDRKALLQALADGRIDVIASDHAPHTLEEKRKG---YPAAPSGIPGVETALPLMltlVNKGILSLS 290
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 66392186 368 mdenRFVAVTSSNAAKIYNLyPRKGRIIPGADADVVVWDPESTRTIsvTTQWQGGDVNL--YENLRCHGVPLVTISRG 443
Cdd:cd01318 291 ----RVVRLTSHNPARIFGI-KNKGRIAEGYDADLTVVDLKEERTI--RAEEFHSKAGWtpFEGFEVTGFPVMTIVRG 361
|
|
| pyrC |
PRK09357 |
dihydroorotase; Validated |
9-449 |
1.06e-37 |
|
dihydroorotase; Validated
Pssm-ID: 236479 [Multi-domain] Cd Length: 423 Bit Score: 144.18 E-value: 1.06e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66392186 9 RILIKGGKVVN-DDFTQEADVYIENGIIQQVGKELmIPGGAKVIDATGKLVLPGGIDTSVHLNEsfmNGTT-ADDFYSGT 86
Cdd:PRK09357 2 MILIKNGRVIDpKGLDEVADVLIDDGKIAAIGENI-EAEGAEVIDATGLVVAPGLVDLHVHLRE---PGQEdKETIETGS 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66392186 87 KAALAGGTTMVigHVLPEKNeSLLDAYEKARSHADakaccdyalhmgvtwwgpkaRAQMETLVRDKGVNSFQMYMAYK-- 164
Cdd:PRK09357 78 RAAAAGGFTTV--VAMPNTK-PVIDTPEVVEYVLD--------------------RAKEAGLVDVLPVGAITKGLAGEel 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66392186 165 -DMYMLRDSE----------------LFQALQNCKDIGAVARVHAE-----NGELVAEGAREALdLGISGpegieisRPE 222
Cdd:PRK09357 135 tEFGALKEAGvvafsddgipvqdarlMRRALEYAKALDLLIAQHCEdpsltEGGVMNEGEVSAR-LGLPG-------IPA 206
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66392186 223 ELEAEAVHRAITIANRAHCPIYLVNVSSMSAGDVLASAKMQGKVVHGETTTAHAVLNgmqyyHQDWA-HAAAFVTVPPLR 301
Cdd:PRK09357 207 VAEEVMIARDVLLAEATGARVHICHVSTAGSVELIRWAKALGIKVTAEVTPHHLLLT-----DEDLLtYDPNYKVNPPLR 281
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66392186 302 LDPNTpNYLLSLLGNDTLNVVTSDHRPFTTKQKAMgkdDFTKIPHGVPGVQDRMSVMWERGVVGGKMDENRFVAVTSSNA 381
Cdd:PRK09357 282 TEEDR-EALIEGLKDGTIDAIATDHAPHAREEKEC---EFEAAPFGITGLETALSLLYTTLVKTGLLDLEQLLEKMTINP 357
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 66392186 382 AKIYNLYPrkGRIIPGADADVVVWDPESTRTISVTTQWQGGDVNLYENLRCHGVPLVTISRGRVVYEN 449
Cdd:PRK09357 358 ARILGLPA--GPLAEGEPADLVIFDPEAEWTVDGEDFASKGKNTPFIGMKLKGKVVYTIVDGKIVYQD 423
|
|
| PRK09060 |
PRK09060 |
dihydroorotase; Validated |
11-450 |
1.01e-35 |
|
dihydroorotase; Validated
Pssm-ID: 181632 [Multi-domain] Cd Length: 444 Bit Score: 138.90 E-value: 1.01e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66392186 11 LIKGGKVVNDDFTQEADVYIENGIIQQVGkELMIPGGAKVIDATGKLVLPGGIDTSVHLNESfmnGTTA-DDFYSGTKAA 89
Cdd:PRK09060 8 ILKGGTVVNPDGEGRADIGIRDGRIAAIG-DLSGASAGEVIDCRGLHVLPGVIDSQVHFREP---GLEHkEDLETGSRAA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66392186 90 LAGGTTMVIGhvLPEKNESLLDA--YEKARSHADAKACCDYALHMGVTWWGPKARAQMETLVRDKGVNSFqMYMAYKDMY 167
Cdd:PRK09060 84 VLGGVTAVFE--MPNTNPLTTTAeaLADKLARARHRMHCDFAFYVGGTRDNADELAELERLPGCAGIKVF-MGSSTGDLL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66392186 168 MLRDSELFQALQNckdIGAVARVHAENGELVaegaREALDLGISG-PEGIEISRPEELEAEAVHRAITIANRAHCPIYLV 246
Cdd:PRK09060 161 VEDDEGLRRILRN---GRRRAAFHSEDEYRL----RERKGLRVEGdPSSHPVWRDEEAALLATRRLVRLARETGRRIHVL 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66392186 247 NVSSMSAGDVLASAKmqgKVVHGETTTAHAVLNGMQYYHQDWAHAaafVTVPPLRlDPNTPNYLLSLLGNDTLNVVTSDH 326
Cdd:PRK09060 234 HVSTAEEIDFLADHK---DVATVEVTPHHLTLAAPECYERLGTLA---QMNPPIR-DARHRDGLWRGVRQGVVDVLGSDH 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66392186 327 RPFTTKQKAMgkdDFTKIPHGVPGVQDRMSVMWERgVVGGKMDENRFVAVTSSNAAKIYNLyPRKGRIIPGADADVVVWD 406
Cdd:PRK09060 307 APHTLEEKAK---PYPASPSGMTGVQTLVPIMLDH-VNAGRLSLERFVDLTSAGPARIFGI-AGKGRIAVGYDADFTIVD 381
|
410 420 430 440
....*....|....*....|....*....|....*....|....*.
gi 66392186 407 PESTRTIsvTTQWQGGDVNL--YENLRCHGVPLVTISRGRVVYENG 450
Cdd:PRK09060 382 LKRRETI--TNEWIASRCGWtpYDGKEVTGWPVGTIVRGQRVMWDG 425
|
|
| PRK08044 |
PRK08044 |
allantoinase AllB; |
10-463 |
4.95e-35 |
|
allantoinase AllB;
Pssm-ID: 169193 [Multi-domain] Cd Length: 449 Bit Score: 137.29 E-value: 4.95e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66392186 10 ILIKGGKVVNDDFTQEADVYIENGIIQQVGKELmiPGGAKVIDATGKLVLPGGIDTSVHLNESfmNGTTADDFYSGTKAA 89
Cdd:PRK08044 5 LIIKNGTVILENEARVVDIAVKGGKIAAIGQDL--GDAKEVMDASGLVVSPGMVDAHTHISEP--GRSHWEGYETGTRAA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66392186 90 LAGGTTMVIGHVLPE-----KNESLLDAYEKARShadaKACCDYALHMGVTwwgPKARAQMETLvRDKGVNSFQMYMAY- 163
Cdd:PRK08044 81 AKGGITTMIEMPLNQlpatvDRASIELKFDAAKG----KLTIDAAQLGGLV---SYNLDRLHEL-DEVGVVGFKCFVATc 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66392186 164 ------KDMYMLRDSELFQALQNCKDIGAVARVHAENGELVAEGAREALDLGISGPEGIEISRPEELEAEAVHRAITIAN 237
Cdd:PRK08044 153 gdrgidNDFRDVNDWQFYKGAQKLGELGQPVLVHCENALICDELGEEAKREGRVTAHDYVASRPVFTEVEAIRRVLYLAK 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66392186 238 RAHCPIYLVNVSSMSAGDVLASAKMQGKVVHGETTTAHAVLNGMQYyhqdwAHAAAFVTV-PPLRlDPNTPNYLLSLLGN 316
Cdd:PRK08044 233 VAGCRLHVCHISSPEGVEEVTRARQEGQDVTCESCPHYFVLDTDQF-----EEIGTLAKCsPPIR-DLENQKGMWEKLFN 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66392186 317 DTLNVVTSDHRPFTTKQKAmgkDDFTKIPHGVPGVQDRMSVMWERGVVGGKMDENRFVAVTSSNAAKIYNLyPRKGRIIP 396
Cdd:PRK08044 307 GEIDCLVSDHSPCPPEMKA---GNIMEAWGGIAGLQNCMDVMFDEAVQKRGMSLPMFGKLMATNAADIFGL-QQKGRIAP 382
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 66392186 397 GADADVVVWDPESTRTISVTTQWQGGDVNLYENLRCHGVPLVTISRGRVVY--ENGIftCAEGSGKFYP 463
Cdd:PRK08044 383 GKDADFVFIQPNSSYVLKNEDLEYRHKVSPYVGRTIGARITKTILRGDVIYdiEQGF--PVAPKGQFIL 449
|
|
| PLN02795 |
PLN02795 |
allantoinase |
15-450 |
8.13e-34 |
|
allantoinase
Pssm-ID: 178392 [Multi-domain] Cd Length: 505 Bit Score: 134.52 E-value: 8.13e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66392186 15 GKVVNDDFTQEADVYIENGIIQQVGKELMIPG---GAKVIDATGKLVLPGGIDTSVHLNESfmnGTTA-DDFYSGTKAAL 90
Cdd:PLN02795 51 KRVVTPAGVIPGAVEVEGGRIVSVTKEEEAPKsqkKPHVLDYGNAVVMPGLIDVHVHLNEP---GRTEwEGFPTGTKAAA 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66392186 91 AGGTTMVIGHVLPEK----NESLLDAYEKArshADAKaccdyaLHMGVTWWGP-----KARAQMETLVRDKGVNSFQMYM 161
Cdd:PLN02795 128 AGGITTLVDMPLNSFpsttSVETLELKIEA---AKGK------LYVDVGFWGGlvpenAHNASVLEELLDAGALGLKSFM 198
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66392186 162 ---AYKDMYMLRDSELFQALQNCKDIGAVARVHAENGELVAEGAREALDLGiSGPEGIEiSRPEELEAEAVHRAITIANR 238
Cdd:PLN02795 199 cpsGINDFPMTTATHIKAALPVLAKYGRPLLVHAEVVSPVESDSRLDADPR-SYSTYLK-SRPPSWEQEAIRQLLEVAKD 276
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66392186 239 AH-------CPIYLVNVS-SMSAGDVLASAKMQGKVVHGETTT------AHAVLNGmqyyhqdwahAAAFVTVPPLRLDP 304
Cdd:PLN02795 277 TRpggvaegAHVHIVHLSdAESSLELIKEAKAKGDSVTVETCPhylafsAEEIPDG----------DTRYKCAPPIRDAA 346
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66392186 305 NTPNyLLSLLGNDTLNVVTSDHRPFTTKQKAMGKDDFTKIPHGVPGVQDRMSVMWERGVVGGkMDENRFVAVTSSNAAKI 384
Cdd:PLN02795 347 NREL-LWKALLDGDIDMLSSDHSPSPPDLKLLEEGNFLRAWGGISSLQFVLPATWTAGRAYG-LTLEQLARWWSERPAKL 424
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 66392186 385 YNLyPRKGRIIPGADADVVVWDPESTRTI--SVTTQWQGGDVNLYENLRCHGVPLVTISRGRVVYENG 450
Cdd:PLN02795 425 AGL-DSKGAIAPGKDADIVVWDPEAEFVLdeSYPIYHKHKSLSPYLGTKLSGKVIATFVRGNLVFLEG 491
|
|
| PRK04250 |
PRK04250 |
dihydroorotase; Provisional |
15-450 |
2.24e-29 |
|
dihydroorotase; Provisional
Pssm-ID: 235265 [Multi-domain] Cd Length: 398 Bit Score: 119.87 E-value: 2.24e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66392186 15 GKVVNDDFTQEADVYIENGIIQQVGKELMipGGAKVIDATGKLVLPGGIDTSVHLNEsfMNGTTADDFYSGTKAALAGGT 94
Cdd:PRK04250 4 GKFLLKGRIVEGGIGIENGRISKISLRDL--KGKEVIKVKGGIILPGLIDVHVHLRD--FEESYKETIESGTKAALHGGI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66392186 95 TMVIGhvLPEKNESLLDA--YEKARSHADAKACCDYALHMGVTWWGPKARAQMETLvrdkgvnsfqmymaYKDMYMLRDS 172
Cdd:PRK04250 80 TLVFD--MPNTKPPIMDEktYEKRMRIAEKKSYADYALNFLIAGNCEKAEEIKADF--------------YKIFMGASTG 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66392186 173 ELF-QALQ-NCKDIGAVARVHAENGELVAEgarealdlgisGPEgieisRPEELEAEAVHRAITIANRAHCPIYLVNVSS 250
Cdd:PRK04250 144 GIFsENFEvDYACAPGIVSVHAEDPELIRE-----------FPE-----RPPEAEVVAIERALEAGKKLKKPLHICHIST 207
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66392186 251 MSAGDVLASAKMQgkVVHGETTTAHavlngMQYYHQDWAHAAAFVTVPPLRldpnTPNYLLSLLGN-DTLNVVTSDHRPF 329
Cdd:PRK04250 208 KDGLKLILKSNLP--WVSFEVTPHH-----LFLTRKDYERNPLLKVYPPLR----SEEDRKALWENfSKIPIIASDHAPH 276
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66392186 330 TTKQKAMGKDdftkiphGVPGVQDRMSVMWErGVVGGKMDENRFVAVTSSNAAKIYNlYPRKGrIIPGADADVVVWDPES 409
Cdd:PRK04250 277 TLEDKEAGAA-------GIPGLETEVPLLLD-AANKGMISLFDIVEKMHDNPARIFG-IKNYG-IEEGNYANFAVFDMKK 346
|
410 420 430 440
....*....|....*....|....*....|....*....|.
gi 66392186 410 TRTISVTTQWQGGDVNLYENLRCHGVPLVTISRGRVVYENG 450
Cdd:PRK04250 347 EWTIKAEELYTKAGWTPYEGFKLKGKVIMTILRGEVVMEDD 387
|
|
| PRK07575 |
PRK07575 |
dihydroorotase; Provisional |
9-450 |
3.88e-29 |
|
dihydroorotase; Provisional
Pssm-ID: 236055 [Multi-domain] Cd Length: 438 Bit Score: 120.16 E-value: 3.88e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66392186 9 RILIKGGKVVNDDFT-QEADVYIENGIIQQVGKELMIPGGAKVIDATGKLVLPGGIDTSVHLNESFMngTTADDFYSGTK 87
Cdd:PRK07575 4 SLLIRNARILLPSGElLLGDVLVEDGKIVAIAPEISATAVDTVIDAEGLTLLPGVIDPQVHFREPGL--EHKEDLFTASR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66392186 88 AALAGGTT----MVIGHVLPEKNESLLDAYEKARShadaKACCDYALHMGVTwwgPKARAQMETLVRDKGVNSFqMYMAY 163
Cdd:PRK07575 82 ACAKGGVTsfleMPNTKPLTTTQAALDDKLARAAE----KCVVNYGFFIGAT---PDNLPELLTANPTCGIKIF-MGSSH 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66392186 164 KDMYMLRDSELFQALQNCKDIGAVarvHAENGELVAegAREALDLGISGPEGIEISRPEELEAEAVHRAITIANRAHCPI 243
Cdd:PRK07575 154 GPLLVDEEAALERIFAEGTRLIAV---HAEDQARIR--ARRAEFAGISDPADHSQIQDEEAALLATRLALKLSKKYQRRL 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66392186 244 YLVNVSSMSAGDVLASAKmqGKVVHGETTTAHAVLNgmqyyHQDWAHAAAFVTV-PPLRlDPNTPNYLLSLLGNDTLNVV 322
Cdd:PRK07575 229 HILHLSTAIEAELLRQDK--PSWVTAEVTPQHLLLN-----TDAYERIGTLAQMnPPLR-SPEDNEALWQALRDGVIDFI 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66392186 323 TSDHRPFTTKQKAMGkddFTKIPHGVPGVQDRMSVMWERgVVGGKMDENRFVAVTSSNAAKIYNLyPRKGRIIPGADADV 402
Cdd:PRK07575 301 ATDHAPHTLEEKAQP---YPNSPSGMPGVETSLPLMLTA-AMRGKCTVAQVVRWMSTAVARAYGI-PNKGRIAPGYDADL 375
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*.
gi 66392186 403 VVWDPESTRTISVTTQ--------WQGgdvnlyENLRchGVPLVTISRGRVVYENG 450
Cdd:PRK07575 376 VLVDLNTYRPVRREELltkcgwspFEG------WNLT--GWPVTTIVGGQIVFDRG 423
|
|
| PRK09236 |
PRK09236 |
dihydroorotase; Reviewed |
9-450 |
1.79e-26 |
|
dihydroorotase; Reviewed
Pssm-ID: 181716 Cd Length: 444 Bit Score: 112.27 E-value: 1.79e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66392186 9 RILIKGGKVVNDDFTQEADVYIENGIIQQVGKELMIPGGAKVIDATGKLVLPGGIDTSVHLNESfmnGTTAD-DFYSGTK 87
Cdd:PRK09236 3 RILIKNARIVNEGKIFEGDVLIENGRIAKIASSISAKSADTVIDAAGRYLLPGMIDDQVHFREP---GLTHKgDIASESR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66392186 88 AALAGGTT--MVIGHVLPEKN--ESLLDAYEKARSHADAkaccDYALHMGVTwwgpkaRAQMETLVR-DK----GVNSFq 158
Cdd:PRK09236 80 AAVAGGITsfMEMPNTNPPTTtlEALEAKYQIAAQRSLA----NYSFYFGAT------NDNLDEIKRlDPkrvcGVKVF- 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66392186 159 myMAYKDMYMLRDSElfQALQNC-KDIGAVARVHAENGELVAegAREALDLGISGpEGIEIS-----RPEELEAEAVHRA 232
Cdd:PRK09236 149 --MGASTGNMLVDNP--ETLERIfRDAPTLIATHCEDTPTIK--ANLAKYKEKYG-DDIPAEmhpliRSAEACYKSSSLA 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66392186 233 ITIANRAHCPIYLVNVSSMSAGDVLASAKMQGKVVHGETTTAHavlngMQYYHQDWAHAAAFVTVPPLRLDPNTPNYLLS 312
Cdd:PRK09236 222 VSLAKKHGTRLHVLHISTAKELSLFENGPLAEKRITAEVCVHH-----LWFDDSDYARLGNLIKCNPAIKTASDREALRQ 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66392186 313 LLGNDTLNVVTSDHRPFTTKQKAMGkddFTKIPHGVPGVQDRMSVMWERgVVGGKMDENRFVAVTSSNAAKIYNLyPRKG 392
Cdd:PRK09236 297 ALADDRIDVIATDHAPHTWEEKQGP---YFQAPSGLPLVQHALPALLEL-VHEGKLSLEKVVEKTSHAPAILFDI-KERG 371
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 66392186 393 RIIPGADADVVVWDPESTRTISvttqwqgGDVNLYenlRCHGVPLV----------TISRGRVVYENG 450
Cdd:PRK09236 372 FIREGYWADLVLVDLNSPWTVT-------KENILY---KCGWSPFEgrtfrsrvatTFVNGQLVYHNG 429
|
|
| PRK01211 |
PRK01211 |
dihydroorotase; Provisional |
12-463 |
2.09e-23 |
|
dihydroorotase; Provisional
Pssm-ID: 179247 [Multi-domain] Cd Length: 409 Bit Score: 102.63 E-value: 2.09e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66392186 12 IKGGKVVNDDFtQEADVYIENGIIQQVGKELmipGGAKVIDATGkLVLPGGIDTSVHLNESfmNGTTADDFYSGTKAALA 91
Cdd:PRK01211 3 ICGNFYYKGKF-DYLEIEVEDGKIKSIKKDA---GNIGKKELKG-AILPAATDIHVHFRTP--GETEKEDFSTGTLSAIF 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66392186 92 GGTTMVIGhvLPEKNESLLD--AYEKARSHADAKACCDYALHmgvtwwgpkaraQMET----LVRDKGVNSFQMYMAYKD 165
Cdd:PRK01211 76 GGTTFIMD--MPNNNIPIKDynAFSDKLGRVAPKAYVDFSLY------------SMETgnnaLILDERSIGLKVYMGGTT 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66392186 166 MYMLRDSElFQALQNCKDIGAVARVHAENGELVAEGAREALDLgisgpEGIEISRPEELEAEAVHRAITIANRAHcpiYL 245
Cdd:PRK01211 142 NTNGTDIE-GGEIKKINEANIPVFFHAELSECLRKHQFESKNL-----RDHDLARPIECEIKAVKYVKNLDLKTK---II 212
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66392186 246 VNVSSM-SAGDVLAsakmqgkvvhgETTTAHAVLNgmqyyhqDWAHAAAFVTV-PPLRlDPNTPNYLLSLLGNDTLNVVT 323
Cdd:PRK01211 213 AHVSSIdVIGRFLR-----------EVTPHHLLLN-------DDMPLGSYGKVnPPLR-DRWTQERLLEEYISGRFDILS 273
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66392186 324 SDHRPFTTKQKAmgkdDFTKIPHGVPGVQDRMSVMWERgVVGGKMDENRFVAVTSSNAAKIYNLypRKGRIIPGADADVV 403
Cdd:PRK01211 274 SDHAPHTEEDKQ----EFEYAKSGIIGVETRVPLFLAL-VKKKILPLDVLYKTAIERPASLFGI--KKGKIEEGYDADFM 346
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|
gi 66392186 404 VWDPESTRTISVTTQWQGGDVNLYENLRCHgVPLVTISRGRVVYENgIFTCAEGSGKFYP 463
Cdd:PRK01211 347 AFDFTNIKKINDKRLHSKCPVSPFNGFDAI-FPSHVIMRGEVVIDN-YELISERTGKFVP 404
|
|
| HutI |
COG1228 |
Imidazolonepropionase or related amidohydrolase [Secondary metabolites biosynthesis, transport ... |
3-449 |
4.80e-17 |
|
Imidazolonepropionase or related amidohydrolase [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 440841 [Multi-domain] Cd Length: 386 Bit Score: 83.09 E-value: 4.80e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66392186 3 SSSATVRILIKGGKVV---NDDFTQEADVYIENGIIQQVGK--ELMIPGGAKVIDATGKLVLPGGIDTSVHLnesFMNGT 77
Cdd:COG1228 3 APAQAGTLLITNATLVdgtGGGVIENGTVLVEDGKIAAVGPaaDLAVPAGAEVIDATGKTVLPGLIDAHTHL---GLGGG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66392186 78 TADDFYSGT----------------KAALAGGTTMVigHVLPEKNESLLDAYEKARSH---------ADAKACCDYALHM 132
Cdd:COG1228 80 RAVEFEAGGgitptvdlvnpadkrlRRALAAGVTTV--RDLPGGPLGLRDAIIAGESKllpgprvlaAGPALSLTGGAHA 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66392186 133 GvtwwGPK-ARAQMETLVRDkGVNSFQMYMAYKDMYMLRDsELFQALQNCKDIGAVARVHAENgelvAEGAREALDLGIS 211
Cdd:COG1228 158 R----GPEeARAALRELLAE-GADYIKVFAEGGAPDFSLE-ELRAILEAAHALGLPVAAHAHQ----ADDIRLAVEAGVD 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66392186 212 GPEGIEISRPEELEAeavhraitIAnrAHCPIYLvnVSSMSAGDVLASAKmqgkvvhgettTAHAVLNGMQYYHQDWAHA 291
Cdd:COG1228 228 SIEHGTYLDDEVADL--------LA--EAGTVVL--VPTLSLFLALLEGA-----------AAPVAAKARKVREAALANA 284
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66392186 292 AAF----VTVpplrldpntpnyllsllgndtlnvvtsdhrpfttkqkAMGKDDFTKIPHGVpgvqdrmSVMWE-RGVVGG 366
Cdd:COG1228 285 RRLhdagVPV-------------------------------------ALGTDAGVGVPPGR-------SLHRElALAVEA 320
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66392186 367 KMDENR-FVAVTsSNAAKIYNLYPRKGRIIPGADADVVVWdpestrtisvttqwqggDVNLYENLRCHGVPLVTISRGRV 445
Cdd:COG1228 321 GLTPEEaLRAAT-INAAKALGLDDDVGSLEPGKLADLVLL-----------------DGDPLEDIAYLEDVRAVMKDGRV 382
|
....
gi 66392186 446 VYEN 449
Cdd:COG1228 383 VDRS 386
|
|
| PRK07369 |
PRK07369 |
dihydroorotase; Provisional |
26-417 |
5.13e-17 |
|
dihydroorotase; Provisional
Pssm-ID: 236002 [Multi-domain] Cd Length: 418 Bit Score: 83.50 E-value: 5.13e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66392186 26 ADVYIENGIIQQVGKELM-IPGGAKVIDATGKLVLPGGIDTSVHLNEsfMNGTTADDFYSGTKAALAGGTTMVIghVLPE 104
Cdd:PRK07369 22 ADVLIEDGKIQAIEPHIDpIPPDTQIIDASGLILGPGLVDLYSHSGE--PGFEERETLASLAAAAAAGGFTRVA--ILPD 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66392186 105 KNESLLDAYEKARSHADAKACCDYALHmgvtWWGP----KARAQMeTLVRD---KGVNSFQMYMAYKDMYMLRdselfQA 177
Cdd:PRK07369 98 TFPPLDNPATLARLQQQAQQIPPVQLH----FWGAltlgGQGKQL-TELAElaaAGVVGFTDGQPLENLALLR-----RL 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66392186 178 LQNCKDIGAVARVHAENGELVAEG-ARE---ALDLGISGpegieisRPEELEAEAVHRAITIANRAHCPIYLVNVSSMSA 253
Cdd:PRK07369 168 LEYLKPLGKPVALWPCDRSLAGNGvMREgllALRLGLPG-------DPASAETTALAALLELVAAIGTPVHLMRISTARS 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66392186 254 GDVLASAKMQGKVVHGETTTAHAVLNGMQYYHQDwahaaafvtvPPLRLDPNTPN-----YLLSLLGNDTLNVVTSDHRP 328
Cdd:PRK07369 241 VELIAQAKARGLPITASTTWMHLLLDTEALASYD----------PNLRLDPPLGNpsdrqALIEGVRTGVIDAIAIDHAP 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66392186 329 FTTKQKAMGkddFTKIPHGVPGVQDRMSVMWERGVVGGKMDENRFVAVTSSNAAKIYNLYPRkgRIIPGADADVVVWDPE 408
Cdd:PRK07369 311 YTYEEKTVA---FAEAPPGAIGLELALPLLWQNLVETGELSALQLWQALSTNPARCLGQEPP--SLAPGQPAELILFDPQ 385
|
....*....
gi 66392186 409 STRTISVTT 417
Cdd:PRK07369 386 KTWTVSAQT 394
|
|
| Amidohydro_1 |
pfam01979 |
Amidohydrolase family; This family of enzymes are a a large metal dependent hydrolase ... |
57-446 |
6.80e-17 |
|
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: 82.16 E-value: 6.80e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66392186 57 LVLPGGIDTSVHLNESFMNGTTADDFYS------GTKAALAGGTTMVIGHVLPEKN--ESLLDAYEKARS--HADAKACC 126
Cdd:pfam01979 1 IVLPGLIDAHVHLEMGLLRGIPVPPEFAyealrlGITTMLKSGTTTVLDMGATTSTgiEALLEAAEELPLglRFLGPGCS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66392186 127 ---DYALHMGVTWW-GPKARAQMETLVRDKGVNSfqmYMAYKDMYMLRDSELFQALQNCKDIGAVARVHAENGELVAEGA 202
Cdd:pfam01979 81 ldtDGELEGRKALReKLKAGAEFIKGMADGVVFV---GLAPHGAPTFSDDELKAALEEAKKYGLPVAIHALETKGEVEDA 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66392186 203 REAldlgisGPEGIEISRPEELEAEAVHRAITIANRAHCpIYLvnvsSMSAGDVLASAKMQGKVVHgetttahavlngmq 282
Cdd:pfam01979 158 IAA------FGGGIEHGTHLEVAESGGLLDIIKLILAHG-VHL----SPTEANLLAEHLKGAGVAH-------------- 212
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66392186 283 yyhqdwahaaafVTVPPLRLDPNTPNyLLSLLGNDTLNVVTSDHRpfttkqkAMGkddftkiphGVPGVQDRMSVM-WER 361
Cdd:pfam01979 213 ------------CPFSNSKLRSGRIA-LRKALEDGVKVGLGTDGA-------GSG---------NSLNMLEELRLAlELQ 263
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66392186 362 GVVGGKMDENRFVAVTSSNAAKIYNLYPRKGRIIPGADADVVVWDPESTRTISVTTqwqggdvnlyenlrCHGVPLVTIS 441
Cdd:pfam01979 264 FDPEGGLSPLEALRMATINPAKALGLDDKVGSIEVGKDADLVVVDLDPLAAFFGLK--------------PDGNVKKVIV 329
|
....*
gi 66392186 442 RGRVV 446
Cdd:pfam01979 330 KGKIV 334
|
|
| PRK09059 |
PRK09059 |
dihydroorotase; Validated |
21-448 |
1.09e-14 |
|
dihydroorotase; Validated
Pssm-ID: 181631 [Multi-domain] Cd Length: 429 Bit Score: 76.23 E-value: 1.09e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66392186 21 DFTQEADVYIENGIIQQVGKELM---IPGGAKVIDATGKLVLPGGIDTSVHLNESfmNGTTADDFYSGTKAALAGGTTMV 97
Cdd:PRK09059 18 GLDEIGTVLIEDGVIVAAGKGAGnqgAPEGAEIVDCAGKAVAPGLVDARVFVGEP--GAEHRETIASASRAAAAGGVTSI 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66392186 98 IghVLPEKNESLldayekarshaDAKACCDYALHmgvtwwgpkaRAQMETLVR-------DKGVNSFQMymayKDMYMLR 170
Cdd:PRK09059 96 I--MMPDTDPVI-----------DDVALVEFVKR----------TARDTAIVNihpaaaiTKGLAGEEM----TEFGLLR 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66392186 171 D----------------SELFQALQNCKDIGAVARVHAENGELVAEGARE----ALDLGISGPegieisrPEELEAEAVH 230
Cdd:PRK09059 149 AagavaftdgrrsvantQVMRRALTYARDFDAVIVHETRDPDLGGNGVMNeglfASWLGLSGI-------PREAEVIPLE 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66392186 231 RAITIANRAHCPIYLVNVSSMSAGDVLASAKMqgkvvHGETTTAHAVLNGMQYYHQDWAHAAAFVTV-PPLRLDPNTpNY 309
Cdd:PRK09059 222 RDLRLAALTRGRYHAAQISCAESAEALRRAKD-----RGLKVTAGVSINHLSLNENDIGEYRTFFKLsPPLRTEDDR-VA 295
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66392186 310 LLSLLGNDTLNVVTSDHRPFTTKQKAMgkdDFTKIPHGVPGVQDRMSVMWeRGVVGGKMDENRFVAVTSSNAAKIYNLyp 389
Cdd:PRK09059 296 MVEAVASGTIDIIVSSHDPQDVDTKRL---PFSEAAAGAIGLETLLAAAL-RLYHNGEVPLLRLIEALSTRPAEIFGL-- 369
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*....
gi 66392186 390 RKGRIIPGADADVVVWDPESTRTISVTTQWQGGDVNLYENLRCHGVPLVTISRGRVVYE 448
Cdd:PRK09059 370 PAGTLKPGAPADIIVIDLDEPWVVDPEDLKSRSKNTPFEEARFQGRVVRTIVAGKTVYE 428
|
|
| PRK08417 |
PRK08417 |
metal-dependent hydrolase; |
30-448 |
2.60e-13 |
|
metal-dependent hydrolase;
Pssm-ID: 236262 [Multi-domain] Cd Length: 386 Bit Score: 71.66 E-value: 2.60e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66392186 30 IENGIIQQVGKELmipGGAKVIDATGKLVLPGGIDTSVHL-NESFmngtTADDFYSGTKAALAGG--TTMVIGHVLPEKN 106
Cdd:PRK08417 3 IKDGKITEIGSDL---KGEEILDAKGKTLLPALVDLNVSLkNDSL----SSKNLKSLENECLKGGvgSIVLYPDSTPAID 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66392186 107 ESLLDAYEKARSHADAKACCDYALHMGvtwwgPKAR-AQMETLVrDKGVNSFQMYMAYKDMYMLRDSELFQALQ-----N 180
Cdd:PRK08417 76 NEIALELINSAQRELPMQIFPSIRALD-----EDGKlSNIATLL-KKGAKALELSSDLDANLLKVIAQYAKMLDvpifcR 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66392186 181 CKDigavaRVHAENGelVAEGAREALDLGISGPEGIEisrpeelEAEAVHRAITIANRAHCPIYLVNVSSMSAGDVLASA 260
Cdd:PRK08417 150 CED-----SSFDDSG--VMNDGELSFELGLPGIPSIA-------ETKEVAKMKELAKFYKNKVLFDTLALPRSLELLDKF 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66392186 261 KMQGKVVHGETTTAHAVLNgmQYYHQDWAHAAAFVtvPPLRlDPNTPNYLLSLLGNDTLNVVTSDHRPFTTKQKAMGkdd 340
Cdd:PRK08417 216 KSEGEKLLKEVSIHHLILD--DSACENFNTAAKLN--PPLR-SKEDRLALLEALKEGKIDFLTSLHSAKSNSKKDLA--- 287
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66392186 341 FTKIPHGVPGVQDRMSVMWERGVVGGKMDENRFVAVTSSNAAKIYNLypRKGRIIPGADADVVVWDPESTRTISVTTQWQ 420
Cdd:PRK08417 288 FDEAAFGIDSICEYFSLCYTYLVKEGIITWSELSRFTSYNPAQFLGL--NSGEIEVGKEADLVLFDPNESTIIDDNFSLY 365
|
410 420
....*....|....*....|....*...
gi 66392186 421 GGDvNLYENLRCHgvplvtISRGRVVYE 448
Cdd:PRK08417 366 SGD-ELYGKIEAV------IIKGKLYLE 386
|
|
| D-aminoacylase |
cd01297 |
D-aminoacylases (N-acyl-D-Amino acid amidohydrolases) catalyze the hydrolysis of ... |
10-453 |
5.66e-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: 67.71 E-value: 5.66e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66392186 10 ILIKGGKVV----NDDFTqeADVYIENGIIQQVGKELmIPGGAKVIDATGKLVLPGGIDTSVHLNESFMNGTTAddfysg 85
Cdd:cd01297 2 LVIRNGTVVdgtgAPPFT--ADVGIRDGRIAAIGPIL-STSAREVIDAAGLVVAPGFIDVHTHYDGQVFWDPDL------ 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66392186 86 TKAALAGGTTMVIGhvlpekNESLLDAYEKARSHADAK--ACCDYALHMGVTWWGPKARAQMETL-VRDKGVNSFQMyma 162
Cdd:cd01297 73 RPSSRQGVTTVVLG------NCGVSPAPANPDDLARLImlMEGLVALGEGLPWGWATFAEYLDALeARPPAVNVAAL--- 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66392186 163 ykdmymlrdseLFQALQNCKDIGAVARV-HAENGELVAEGAREALDlgiSGPEGIEISR---------PEELEAEAvhra 232
Cdd:cd01297 144 -----------VGHAALRRAVMGLDAREaTEEELAKMRELLREALE---AGALGISTGLayaprlyagTAELVALA---- 205
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66392186 233 iTIANRAHCPIYLV----NVSSMSA-GDVLASAKMQGKVVHGETTTAHAVLNGMQYYHQDWAHAAAFVTVPPLRLDpnTP 307
Cdd:cd01297 206 -RVAARYGGVYQTHvryeGDSILEAlDELLRLGRETGRPVHISHLKSAGAPNWGKIDRLLALIEAARAEGLQVTAD--VY 282
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66392186 308 NYLLSLLgNDTLNVVTSDHRPFTTKQKAMGKddftkiPH-GVPGVQDRMSVMWERGvvGGKMDENRFVAVTSSNAAKIYN 386
Cdd:cd01297 283 PYGAGSE-DDVRRIMAHPVVMGGSDGGALGK------PHpRSYGDFTRVLGHYVRE--RKLLSLEEAVRKMTGLPARVFG 353
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 66392186 387 LYPRkGRIIPGADADVVVWDPEstrTISVTTQWQggDVNLYENlrchGVPLVTISrGRVVYENGIFT 453
Cdd:cd01297 354 LADR-GRIAPGYRADIVVFDPD---TLADRATFT--RPNQPAE----GIEAVLVN-GVPVVRDGAFT 409
|
|
| PRK07627 |
PRK07627 |
dihydroorotase; Provisional |
9-449 |
5.96e-12 |
|
dihydroorotase; Provisional
Pssm-ID: 181059 [Multi-domain] Cd Length: 425 Bit Score: 67.78 E-value: 5.96e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66392186 9 RILIKGGKVVN--DDFTQEADVYIENGIIQQVGKelmIPGG---AKVIDATGKLVLPGGIDTSVHLNE-SFMNGTTADdf 82
Cdd:PRK07627 2 KIHIKGGRLIDpaAGTDRQADLYVAAGKIAAIGQ---APAGfnaDKTIDASGLIVCPGLVDLSARLREpGYEYKATLE-- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66392186 83 ySGTKAALAGGTTMVighVLPEKNESLLDAYE-----KARSHADAKAccdYALHMGVTWWGPKAR--AQMETLVrDKGVN 155
Cdd:PRK07627 77 -SEMAAAVAGGVTSL---VCPPDTDPVLDEPGlvemlKFRARNLNQA---HVYPLGALTVGLKGEvlTEMVELT-EAGCV 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66392186 156 SFQMYMAykdmyMLRDSE-LFQALQNCKDIGAVARVHAE-----NGELVAEGAReALDLGISGPegieisrPEELEAEAV 229
Cdd:PRK07627 149 GFSQANV-----PVVDTQvLLRALQYASTFGFTVWLRPLdaflgRGGVAASGAV-ASRLGLSGV-------PVAAETIAL 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66392186 230 HRAITIANRAHCPIYLVNVSSMSAGDVLASAKMQGKVVHGETTTAHAVLNGMQYYHQDwahaAAFVTVPPLRlDPNTPNY 309
Cdd:PRK07627 216 HTIFELMRVTGARVHLARLSSAAGVALVRAAKAEGLPVTCDVGVNHVHLIDVDIGYFD----SQFRLDPPLR-SQRDREA 290
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66392186 310 LLSLLGNDTLNVVTSDHRPFTTKQKAMgkdDFTKIPHGVPGVQDRMS--VMWERGVvggKMDENRFVAVTSSNAAKIYNL 387
Cdd:PRK07627 291 IRAALADGTIDAICSDHTPVDDDEKLL---PFAEATPGATGLELLLPltLKWADEA---KVPLARALARITSAPARVLGL 364
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 66392186 388 ypRKGRIIPGADADVVVWDPESTRTISVTTQWQGGDVNLYENLRCHGVPLVTISRGRVVYEN 449
Cdd:PRK07627 365 --PAGRLAEGAPADLCVFDPDAHWRVEPRALKSQGKNTPFLGYELPGRVRATLVAGQVAFER 424
|
|
| CAD_DHOase |
cd01316 |
The eukaryotic CAD protein is a trifunctional enzyme of carbamoylphosphate ... |
59-135 |
6.70e-12 |
|
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: 67.09 E-value: 6.70e-12
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 66392186 59 LPGGIDTSVHLNEsfMNGTTADDFYSGTKAALAGGTTMVigHVLPEKNESLLD--AYEKARSHADAKACCDYALHMGVT 135
Cdd:cd01316 5 LPGLIDVHVHLRE--PGATHKEDFASGTKAALAGGFTMV--RAMPNTNPSIVDvaSLKLVQSLAQAKARCDYAFSIGAT 79
|
|
| PRK09237 |
PRK09237 |
amidohydrolase/deacetylase family metallohydrolase; |
10-97 |
4.59e-11 |
|
amidohydrolase/deacetylase family metallohydrolase;
Pssm-ID: 236423 [Multi-domain] Cd Length: 380 Bit Score: 64.87 E-value: 4.59e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66392186 10 ILIKGGKVVNDDFTQEA--DVYIENGIIQQVGKELMIPGGAKVIDATGKLVLPGGIDTSVHLNESF-MNGTTADDFysgt 86
Cdd:PRK09237 1 LLLRGGRVIDPANGIDGviDIAIEDGKIAAVAGDIDGSQAKKVIDLSGLYVSPGWIDLHVHVYPGStPYGDEPDEV---- 76
|
90
....*....|.
gi 66392186 87 kAALAGGTTMV 97
Cdd:PRK09237 77 -GVRSGVTTVV 86
|
|
| pyrC |
PRK00369 |
dihydroorotase; Provisional |
45-461 |
4.98e-11 |
|
dihydroorotase; Provisional
Pssm-ID: 234738 [Multi-domain] Cd Length: 392 Bit Score: 64.78 E-value: 4.98e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66392186 45 PGGAKVIDAT-GKLVLPGGIDTSVHLNEsfMNGTTADDFYSGTKAALAGGTTMVI---GHVLPEKNESLLDayEKARSHA 120
Cdd:PRK00369 31 SRCKPDLDLPqGTLILPGAIDLHVHLRG--LKLSYKEDVASGTSEAAYGGVTLVAdmpNTIPPLNTPEAIT--EKLAELE 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66392186 121 dAKACCDYALHMGVtwwgPKARAQMETLvrdkGVNSFQMYMaykdmymlRDSELFQALQNCKDIGAVARVHAENGELVAE 200
Cdd:PRK00369 107 -YYSRVDYFVYSGV----TKDPEKVDKL----PIAGYKIFP--------EDLEREETFRVLLKSRKLKILHPEVPLALKS 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66392186 201 GAREALDLGIsgpegiEISRPEEL-EAEAVHraITianRAHCPiylvnvssmsaGDVLASAKMQGKVvhgETTTAHAVLN 279
Cdd:PRK00369 170 NRKLRRNCWY------EIAALYYVkDYQNVH--IT---HASNP-----------RTVRLAKELGFTV---DITPHHLLVN 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66392186 280 GMQyyhqdwaHAAAFVTvPPLRlDPNTPNYLLSLLGNdtLNVVTSDHRPFTTKQKAMgkdDFTKIPHGVPGVQDRMSVMW 359
Cdd:PRK00369 225 GEK-------DCLTKVN-PPIR-DINERLWLLQALSE--VDAIASDHAPHSSFEKLQ---PYEVCPPGIAALSFTPPFIY 290
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66392186 360 ERgVVGGKMDENRFVAVTSSNAAKIYNLypRKGRIIPGADADVVVWDPESTRTISVTTQWQGGDVNLYENLRChgvPLVT 439
Cdd:PRK00369 291 TL-VSKGILSIDRAVELISTNPARILGI--PYGEIKEGYRANFTVIQFEDWRYSTKYSKVIETPLDGFELKAS---VYAT 364
|
410 420
....*....|....*....|..
gi 66392186 440 ISRGRVVYENGIFTCAEGSGKF 461
Cdd:PRK00369 365 IVQGKLAYLEGEVFPVKGINPF 386
|
|
| SsnA |
COG0402 |
Cytosine/adenosine deaminase or related metal-dependent hydrolase [Nucleotide transport and ... |
9-116 |
5.16e-11 |
|
Cytosine/adenosine deaminase or related metal-dependent hydrolase [Nucleotide transport and metabolism, General function prediction only]; Cytosine/adenosine deaminase or related metal-dependent hydrolase is part of the Pathway/BioSystem: Pyrimidine salvage
Pssm-ID: 440171 [Multi-domain] Cd Length: 416 Bit Score: 64.85 E-value: 5.16e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66392186 9 RILIKGGKVV--NDDFT--QEADVYIENGIIQQVGKELMIP---GGAKVIDATGKLVLPGGIDTSVHLNESFMNGT---- 77
Cdd:COG0402 1 DLLIRGAWVLtmDPAGGvlEDGAVLVEDGRIAAVGPGAELParyPAAEVIDAGGKLVLPGLVNTHTHLPQTLLRGLaddl 80
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 66392186 78 -----------------TADDFYSGTKAA----LAGGTT--MVIGHVLPEKNESLLDAYEKA 116
Cdd:COG0402 81 plldwleeyiwplearlDPEDVYAGALLAlaemLRSGTTtvADFYYVHPESADALAEAAAEA 142
|
|
| ATZ_TRZ_like |
cd01298 |
TRZ/ATZ family contains enzymes from the atrazine degradation pathway and related hydrolases. ... |
10-120 |
1.53e-10 |
|
TRZ/ATZ family contains enzymes from the atrazine degradation pathway and related hydrolases. Atrazine, a chlorinated herbizide, can be catabolized by a variety of different bacteria. The first three steps of the atrazine dehalogenation pathway are catalyzed by atrazine chlorohydrolase (AtzA), hydroxyatrazine ethylaminohydrolase (AtzB), and N-isopropylammelide N-isopropylaminohydrolase (AtzC). All three enzymes belong to the superfamily of metal dependent hydrolases. AtzA and AtzB, beside other related enzymes are represented in this CD.
Pssm-ID: 238623 [Multi-domain] Cd Length: 411 Bit Score: 63.38 E-value: 1.53e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66392186 10 ILIKGGKVV---NDDFTQEADVYIENGIIQQVGK--ELMIPGGAKVIDATGKLVLPGGIDTSVHLNESFMNG-------- 76
Cdd:cd01298 1 ILIRNGTIVttdPRRVLEDGDVLVEDGRIVAVGPalPLPAYPADEVIDAKGKVVMPGLVNTHTHLAMTLLRGladdlplm 80
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 66392186 77 -------------TTADDFYSGTKAALA----GGTTMVIGHVLPEKNEsLLDAYEKA--RSHA 120
Cdd:cd01298 81 ewlkdliwplerlLTEEDVYLGALLALAemirSGTTTFADMYFFYPDA-VAEAAEELgiRAVL 142
|
|
| NagA |
cd00854 |
N-acetylglucosamine-6-phosphate deacetylase, NagA, catalyzes the hydrolysis of the N-acetyl ... |
10-95 |
6.78e-10 |
|
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: 61.06 E-value: 6.78e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66392186 10 ILIKGGKVVNDDFTQEADVYIENGIIQQVGKELMIPGGAKVIDATGKLVLPGGIDTSVH--LNESFMNGtTADDFYSGTK 87
Cdd:cd00854 1 LIIKNARILTPGGLEDGAVLVEDGKIVAIGPEDELEEADEIIDLKGQYLVPGFIDIHIHggGGADFMDG-TAEALKTIAE 79
|
....*...
gi 66392186 88 AALAGGTT 95
Cdd:cd00854 80 ALAKHGTT 87
|
|
| NagA |
COG1820 |
N-acetylglucosamine-6-phosphate deacetylase [Carbohydrate transport and metabolism]; |
11-95 |
7.53e-10 |
|
N-acetylglucosamine-6-phosphate deacetylase [Carbohydrate transport and metabolism];
Pssm-ID: 441425 [Multi-domain] Cd Length: 373 Bit Score: 60.88 E-value: 7.53e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66392186 11 LIKGGKVVNDD-FTQEADVYIENGIIQQVGKelMIPGGAKVIDATGKLVLPGGIDTSVH--LNESFMNGtTADDFYSGTK 87
Cdd:COG1820 1 AITNARIFTGDgVLEDGALLIEDGRIAAIGP--GAEPDAEVIDLGGGYLAPGFIDLHVHggGGVDFMDG-TPEALRTIAR 77
|
....*...
gi 66392186 88 AALAGGTT 95
Cdd:COG1820 78 AHARHGTT 85
|
|
| PRK07228 |
PRK07228 |
5'-deoxyadenosine deaminase; |
9-81 |
3.03e-09 |
|
5'-deoxyadenosine deaminase;
Pssm-ID: 180895 [Multi-domain] Cd Length: 445 Bit Score: 59.24 E-value: 3.03e-09
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 66392186 9 RILIKGGKVV---NDDFTQEADVYIENGIIQQVGKELMIPGGAKVIDATGKLVLPGGIDTSVHLNESFMNGtTADD 81
Cdd:PRK07228 2 TILIKNAGIVtmnAKREIVDGDVLIEDDRIAAVGDRLDLEDYDDHIDATGKVVIPGLIQGHIHLCQTLFRG-IADD 76
|
|
| AdeC |
COG1001 |
Adenine deaminase [Nucleotide transport and metabolism]; |
10-98 |
1.60e-08 |
|
Adenine deaminase [Nucleotide transport and metabolism];
Pssm-ID: 440625 [Multi-domain] Cd Length: 559 Bit Score: 57.42 E-value: 1.60e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66392186 10 ILIKGGKVVNDdFTQE---ADVYIENGIIQQVGKElmIPGGAKVIDATGKLVLPGGIDTSVHLnESFMngTTADDFYsgt 86
Cdd:COG1001 7 LVIKNGRLVNV-FTGEileGDIAIAGGRIAGVGDY--IGEATEVIDAAGRYLVPGFIDGHVHI-ESSM--VTPAEFA--- 77
|
90
....*....|..
gi 66392186 87 KAALAGGTTMVI 98
Cdd:COG1001 78 RAVLPHGTTTVI 89
|
|
| PRK08204 |
PRK08204 |
hypothetical protein; Provisional |
9-81 |
2.33e-08 |
|
hypothetical protein; Provisional
Pssm-ID: 181288 [Multi-domain] Cd Length: 449 Bit Score: 56.55 E-value: 2.33e-08
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 66392186 9 RILIKGGKVVNDD----FTQEADVYIENGIIQQVGKELMiPGGAKVIDATGKLVLPGGIDTSVHLNESFMNGTTADD 81
Cdd:PRK08204 3 RTLIRGGTVLTMDpaigDLPRGDILIEGDRIAAVAPSIE-APDAEVVDARGMIVMPGLVDTHRHTWQSVLRGIGADW 78
|
|
| Met_dep_hydrolase_B |
cd01307 |
Metallo-dependent hydrolases, subgroup B is part of the superfamily of metallo-dependent ... |
27-73 |
3.73e-08 |
|
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: 55.41 E-value: 3.73e-08
10 20 30 40
....*....|....*....|....*....|....*....|....*..
gi 66392186 27 DVYIENGIIQQVGKELMIPGGAKVIDATGKLVLPGGIDTSVHLNESF 73
Cdd:cd01307 1 DVAIENGKIAAVGAALAAPAATQIVDAGGCYVSPGWIDLHVHVYQGG 47
|
|
| Met_dep_hydrolase_C |
cd01309 |
Metallo-dependent hydrolases, subgroup C is part of the superfamily of metallo-dependent ... |
32-406 |
3.07e-07 |
|
Metallo-dependent hydrolases, subgroup C is part of the superfamily of metallo-dependent hydrolases, a large group of proteins that show conservation in their 3-dimensional fold (TIM barrel) and in details of their active site. The vast majority of the members have a conserved metal binding site, involving four histidines and one aspartic acid residue. In the common reaction mechanism, the metal ion (or ions) deprotonate a water molecule for a nucleophilic attack on the substrate. The function of this subgroup is unknown.
Pssm-ID: 238634 [Multi-domain] Cd Length: 359 Bit Score: 52.70 E-value: 3.07e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66392186 32 NGIIQQVGKELMIPGGAKVIDATGKLVLPGGIDTSVHLN---------ESFMNGTTAD--------DFY----SGTKAAL 90
Cdd:cd01309 1 DGKIVAVGAEITTPADAEVIDAKGKHVTPGLIDAHSHLGldeeggvreTSDANEETDPvtphvraiDGInpddEAFKRAR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66392186 91 AGGTTMVigHVLP-EKN-----ESLLDAYEKARSHADAKAccDYALHMG-------VTWWG---PKARAQMETLVRDkgv 154
Cdd:cd01309 81 AGGVTTV--QVLPgSANliggqGVVIKTDGGTIEDMFIKA--PAGLKMAlgenpkrVYGGKgkePATRMGVAALLRD--- 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66392186 155 nsfQMYMAYKDMYMLRDSELFQALQNCKDIGAVARVHAENGELVAEgarealdlgisgpegIEISRPEELEAeavhrAIT 234
Cdd:cd01309 154 ---AFIKAQEYGRKYDLGKNAKKDPPERDLKLEALLPVLKGEIPVR---------------IHAHRADDILT-----AIR 210
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66392186 235 IANR-------AHCPI-YLVnVSSMSAGDVLASakmqgkvvhgetttahavlngmqYYHQDWahaaAFVTVPPLRLDPNT 306
Cdd:cd01309 211 IAKEfgikitiEHGAEgYKL-ADELAKHGIPVI-----------------------YGPTLT----LPKKVEEVNDAIDT 262
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66392186 307 PNYLLSllgNDTLNV-VTSDHrPFTTKQKAMgkddftkiphgvpgVQDRMSVMWergvvgGKMDENRFVAVTsSNAAKIY 385
Cdd:cd01309 263 NAYLLK---KGGVAFaISSDH-PVLNIRNLN--------------LEAAKAVKY------GLSYEEALKAIT-INPAKIL 317
|
410 420
....*....|....*....|.
gi 66392186 386 NLYPRKGRIIPGADADVVVWD 406
Cdd:cd01309 318 GIEDRVGSLEPGKDADLVVWN 338
|
|
| FwdA |
COG1229 |
Formylmethanofuran dehydrogenase subunit A [Energy production and conversion]; |
10-68 |
5.36e-07 |
|
Formylmethanofuran dehydrogenase subunit A [Energy production and conversion];
Pssm-ID: 440842 Cd Length: 554 Bit Score: 52.50 E-value: 5.36e-07
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 66392186 10 ILIKGGKVVndDFTQE-----ADVYIENG-IIQQVGKelmiPGGAKVIDATGKLVLPGGIDTSVH 68
Cdd:COG1229 3 LIIKNGRVY--DPANGidgevMDIAIKDGkIVEEPSD----PKDAKVIDASGKVVMAGGVDIHTH 61
|
|
| PRK08393 |
PRK08393 |
N-ethylammeline chlorohydrolase; Provisional |
10-81 |
1.44e-06 |
|
N-ethylammeline chlorohydrolase; Provisional
Pssm-ID: 181411 [Multi-domain] Cd Length: 424 Bit Score: 50.95 E-value: 1.44e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 66392186 10 ILIKGGKVV-NDDFT-QEADVYIENGIIQQVGKELMIPGGaKVIDATGKLVLPGGIDTSVHLNESFMNGtTADD 81
Cdd:PRK08393 3 ILIKNGYVIyGENLKvIRADVLIEGNKIVEVKRNINKPAD-TVIDASGSVVSPGFINAHTHSPMVLLRG-LADD 74
|
|
| PRK06380 |
PRK06380 |
metal-dependent hydrolase; Provisional |
10-81 |
1.72e-06 |
|
metal-dependent hydrolase; Provisional
Pssm-ID: 180548 [Multi-domain] Cd Length: 418 Bit Score: 50.65 E-value: 1.72e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 66392186 10 ILIKGGKVVNDDFTQE---ADVYIENGIIQQVGKelMIPGGAKVIDATGKLVLPGGIDTSVHLNESFMNGtTADD 81
Cdd:PRK06380 3 ILIKNAWIVTQNEKREilqGNVYIEGNKIVYVGD--VNEEADYIIDATGKVVMPGLINTHAHVGMTASKG-LFDD 74
|
|
| PRK09061 |
PRK09061 |
D-glutamate deacylase; Validated |
1-450 |
2.03e-06 |
|
D-glutamate deacylase; Validated
Pssm-ID: 236369 [Multi-domain] Cd Length: 509 Bit Score: 50.46 E-value: 2.03e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66392186 1 MSSSSATVRILIKGGKVVNDD--FTQEADVYIENGIIQQVGKELMipGGAKVIDATGKLVLPGGIDTSVHlnesfmnGTT 78
Cdd:PRK09061 12 MPASMAPYDLVIRNGRVVDPEtgLDAVRDVGIKGGKIAAVGTAAI--EGDRTIDATGLVVAPGFIDLHAH-------GQS 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66392186 79 -ADDFYSgtkaALAGGTTMVighvlpeKNESLLDAYEKARSHADAKAccdYALHMGV-TWWGPKARAQMETLVRDKGVNS 156
Cdd:PRK09061 83 vAAYRMQ----AFDGVTTAL-------ELEAGVLPVARWYAEQAGEG---RPLNYGAsVGWTPARIAVLTGPQAEGTIAD 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66392186 157 FQMYMAYKD--MYMLRDSEL---FQALQNCKDIGAVArVHAENGELVAEGAREALDLG-ISGPEGI-------EISRPE- 222
Cdd:PRK09061 149 FGKALGDPRwqERAATPAELaeiLELLEQGLDEGALG-IGIGAGYAPGTGHKEYLELArLAARAGVptythvrYLSNVDp 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66392186 223 ELEAEAVHRAITIANRAHCPIYLVNVSSMSAGDV------LASAKMQGKVVHGET---TTAHAVLnGMQYYHQDW----- 288
Cdd:PRK09061 228 RSSVDAYQELIAAAAETGAHMHICHVNSTSLRDIdrclalVEKAQAQGLDVTTEAypyGAGSTVV-GAAFFDPGWlermg 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66392186 289 --AHAAAFV----------TVPPLR------------LDPNTPNY--LLSLLGNDTLNVVTSDHRPFTTKQKAMGKDDFT 342
Cdd:PRK09061 307 lgYGSLQWVetgerlltreELAKLRandpgglvlihfLDEDNPRDraLLDRSVLFPGAAIASDAMPWTWSDGTVYEGDAW 386
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66392186 343 KIPHGVPG---------------VQDRMSVMWERGVvgGKMdenrfvavtSSNAAKIYNLY----PRKGRIIPGADADVV 403
Cdd:PRK09061 387 PLPEDAVShprsagtfarflreyVRERKALSLLEAI--RKC---------TLMPAQILEDSvpamRRKGRLQAGADADIV 455
|
490 500 510 520
....*....|....*....|....*....|....*....|....*..
gi 66392186 404 VWDPEstrTISVTTQWQggDVNLYEnlrcHGVPLVTISrGRVVYENG 450
Cdd:PRK09061 456 VFDPE---TITDRATFE--DPNRPS----EGVRHVLVN-GVPVVSNG 492
|
|
| YtcJ |
COG1574 |
Predicted amidohydrolase YtcJ [General function prediction only]; |
1-69 |
3.55e-06 |
|
Predicted amidohydrolase YtcJ [General function prediction only];
Pssm-ID: 441182 [Multi-domain] Cd Length: 535 Bit Score: 49.80 E-value: 3.55e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 66392186 1 MSSSSATVRILIKGGKV--VNDDFTQEADVYIENGIIQQVGK----ELMIPGGAKVIDATGKLVLPGGIDTSVHL 69
Cdd:COG1574 1 MKLAAAAADLLLTNGRIytMDPAQPVAEAVAVRDGRIVAVGSdaevRALAGPATEVIDLGGKTVLPGFIDAHVHL 75
|
|
| Amidohydro_3 |
pfam07969 |
Amidohydrolase family; |
49-447 |
3.91e-06 |
|
Amidohydrolase family;
Pssm-ID: 400360 [Multi-domain] Cd Length: 464 Bit Score: 49.45 E-value: 3.91e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66392186 49 KVIDATGKLVLPGGIDTSVHLNESFMNGT-----------------------------------TADDFYSGTKAAL--- 90
Cdd:pfam07969 1 EVIDAKGRLVLPGFVDPHTHLDGGGLNLRelrlpdvlpnavvkgqagrtpkgrwlvgegwdeaqFAETRFPYALADLdev 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66392186 91 AGGTTMVIGHVLPekNESLLD--AYEKARSHADAKACCDYALHMGVTWWGPKA------------------RAQMETLVR 150
Cdd:pfam07969 81 APDGPVLLRALHT--HAAVANsaALDLAGITKATEDPPGGEIARDANGEGLTGllregayalppllareaeAAAVAAALA 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66392186 151 DKGVNSFQMYMAYKDMYMLRDS-ELFQALQNCKDIGAVARVHAENGELV--AEGAREALDLGISGPEG---IEISRP--- 221
Cdd:pfam07969 159 ALPGFGITSVDGGGGNVHSLDDyEPLRELTAAEKLKELLDAPERLGLPHsiYELRIGAMKLFADGVLGsrtAALTEPyfd 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66392186 222 ------EELEAEAVHRAITIANRAHCPIYLvnvssmsagdvlasakmqgkVVHGETTTAhAVLNGMQYYHQDWA------ 289
Cdd:pfam07969 239 apgtgwPDFEDEALAELVAAARERGLDVAI--------------------HAIGDATID-TALDAFEAVAEKLGnqgrvr 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66392186 290 --HAAAFVTVPPLRLDPntpnyLLSLLGNDTLNVVT-----SDHRPFTTKQKAMGKDD-FTKIPHGVP---------GVQ 352
Cdd:pfam07969 298 ieHAQGVVPYTYSQIER-----VAALGGAAGVQPVFdplwgDWLQDRLGAERARGLTPvKELLNAGVKvalgsdapvGPF 372
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66392186 353 DR--------MSVMWERGVVGGKMDENRF---VAVTSSNAAKIYNLYPRKGRIIPGADADVVVWDPESTRTisvttqwqg 421
Cdd:pfam07969 373 DPwprigaavMRQTAGGGEVLGPDEELSLeeaLALYTSGPAKALGLEDRKGTLGVGKDADLVVLDDDPLTV--------- 443
|
490 500
....*....|....*....|....*.
gi 66392186 422 gDVnlyENLRCHGVPLvTISRGRVVY 447
Cdd:pfam07969 444 -DP---PAIADIRVRL-TVVDGRVVY 464
|
|
| PRK06038 |
PRK06038 |
N-ethylammeline chlorohydrolase; Provisional |
10-82 |
6.31e-06 |
|
N-ethylammeline chlorohydrolase; Provisional
Pssm-ID: 180363 [Multi-domain] Cd Length: 430 Bit Score: 48.59 E-value: 6.31e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 66392186 10 ILIKGGKVVNDDF--TQEADVYIENGIIQQVGKElmIPGGA-KVIDATGKLVLPGGIDTSVHLNESFMNGtTADDF 82
Cdd:PRK06038 4 IIIKNAYVLTMDAgdLKKGSVVIEDGTITEVSES--TPGDAdTVIDAKGSVVMPGLVNTHTHAAMTLFRG-YADDL 76
|
|
| PRK07203 |
PRK07203 |
putative aminohydrolase SsnA; |
10-81 |
6.55e-06 |
|
putative aminohydrolase SsnA;
Pssm-ID: 235963 [Multi-domain] Cd Length: 442 Bit Score: 48.78 E-value: 6.55e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 66392186 10 ILIKGGKVVNDD----FTQEADVYIENGIIQQVGKELMIPG---GAKVIDATGKLVLPGGIDTSVHLNESFMNGTTADD 81
Cdd:PRK07203 2 LLIGNGTAITRDpakpVIEDGAIAIEGNVIVEIGTTDELKAkypDAEFIDAKGKLIMPGLINSHNHIYSGLARGMMANI 80
|
|
| Bact_CD |
cd01293 |
Bacterial cytosine deaminase and related metal-dependent hydrolases. Cytosine deaminases (CDs) ... |
26-73 |
6.57e-06 |
|
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: 48.78 E-value: 6.57e-06
10 20 30 40
....*....|....*....|....*....|....*....|....*...
gi 66392186 26 ADVYIENGIIQQVGKELMIPGGAKVIDATGKLVLPGGIDTSVHLNESF 73
Cdd:cd01293 15 VDIAIEDGRIAAIGPALAVPPDAEEVDAKGRLVLPAFVDPHIHLDKTF 62
|
|
| FMDH_A |
cd01304 |
Formylmethanofuran dehydrogenase (FMDH) subunit A; Methanogenic bacteria and archea derive ... |
12-406 |
7.55e-06 |
|
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: 48.56 E-value: 7.55e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66392186 12 IKGGKVV---NDDFTQEADVYIENGiiqQVGKELMIPGGAKVIDATGKLVLPGGIDTSVHLNESFMNGTT---ADDFYSG 85
Cdd:cd01304 1 IKNGTVYdplNGINGEKMDIFIRDG---KIVESSSGAKPAKVIDASGKVVMAGGVDMHSHIAGGKVNVGRilrPEDHRRD 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66392186 86 TKAALAGGTTMViGHVLPeknESLLDAYEKARshadakaccdyalhMGVTW-----WGP-KARAQ----METLVRDKGV- 154
Cdd:cd01304 78 PVPKGALRRAGV-GFSVP---STLATGYRYAE--------------MGYTTafeaaMPPlNARHTheemADTPILDKGAy 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66392186 155 -----NSFQM-YMAYKDMYMLRDSeLFQALQNCKDIGaVARVHAENGELVAEGAReALDLGISGPeGIEISRPEELE--A 226
Cdd:cd01304 140 pllgnNWFVLeYLRDGDMEKLAAY-VAWTLKASKGYG-IKVVNPGGTEAWGWGQN-VLSLDDPVP-YFDITPREILKglA 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66392186 227 EAVHR--------------------AITIA----------NRAHCPIYLVNVSSMSAG-----DVLASAKM--------- 262
Cdd:cd01304 216 EANEElglphsihvhcnnlgvpgnyETTLEtmkaaegvkpDPRRQVLHLTHVQFHSYGgtswrDFESGAERiadyvnand 295
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66392186 263 -----QGKVVHGETTTAHA---------VLNGMQYYHQDWAHAAAFVTVPPLRLDPNTPNYL-------LSLLGNDTLNV 321
Cdd:cd01304 296 hvtidVGQVIFGETTTMTGdgpmqfdlhGLTGLKWVNCDIELETGSGVVPFIYSPKNPVNALqwaigleLFLLIDDPWKV 375
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66392186 322 V-TSDHR---PFTT--------KQKAMGKDDFTKIPhgvPGVQDRMSVmwerGVVGGKMDENRFVAVTSSNAAKIYNLyP 389
Cdd:cd01304 376 IlTTDHPnggPFTRypriiawlMSKKFRAEEIATLH---KWAQDRSAL----PGIDREYSLYEIAIMTRAGPAKLLGL-S 447
|
490
....*....|....*..
gi 66392186 390 RKGRIIPGADADVVVWD 406
Cdd:cd01304 448 DKGHLGVGADADIAIYD 464
|
|
| NagA |
COG1820 |
N-acetylglucosamine-6-phosphate deacetylase [Carbohydrate transport and metabolism]; |
374-422 |
7.77e-06 |
|
N-acetylglucosamine-6-phosphate deacetylase [Carbohydrate transport and metabolism];
Pssm-ID: 441425 [Multi-domain] Cd Length: 373 Bit Score: 48.17 E-value: 7.77e-06
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 66392186 374 VAVTSSNAAKIYNLYPRKGRIIPGADADVVVWDPEstrtISVTTQWQGG 422
Cdd:COG1820 328 VRMASLNPARALGLDDRKGSIAPGKDADLVVLDDD----LNVRATWVGG 372
|
|
| PRK05985 |
PRK05985 |
cytosine deaminase; Provisional |
26-73 |
2.35e-05 |
|
cytosine deaminase; Provisional
Pssm-ID: 180337 [Multi-domain] Cd Length: 391 Bit Score: 46.85 E-value: 2.35e-05
10 20 30 40
....*....|....*....|....*....|....*....|....*...
gi 66392186 26 ADVYIENGIIQQVGKELMIPGGAKVIDATGKLVLPGGIDTSVHLNESF 73
Cdd:PRK05985 17 VDILIRDGRIAAIGPALAAPPGAEVEDGGGALALPGLVDGHIHLDKTF 64
|
|
| Isoaspartyl-dipeptidase |
cd01308 |
Isoaspartyl dipeptidase hydrolyzes the beta-L-isoaspartyl linkages in dipeptides, as part of ... |
11-69 |
4.55e-05 |
|
Isoaspartyl dipeptidase hydrolyzes the beta-L-isoaspartyl linkages in dipeptides, as part of the degradative pathway to eliminate proteins with beta-L-isoaspartyl peptide bonds, bonds whereby the beta-group of an aspartate forms the peptide link with the amino group of the following amino acid. Formation of this bond is a spontaneous nonenzymatic reaction in nature and can profoundly effect the function of the protein. Isoaspartyl dipeptidase is an octameric enzyme that contains a binuclear zinc center in the active site of each subunit and shows a strong preference of hydrolyzing Asp-Leu dipeptides.
Pssm-ID: 238633 [Multi-domain] Cd Length: 387 Bit Score: 45.84 E-value: 4.55e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 66392186 11 LIKGGKVVNDDFTQEADVYIENGIIQQVGKELMIPGGAK--VIDATGKLVLPGGIDTSVHL 69
Cdd:cd01308 3 LIKNAEVYAPEYLGKKDILIAGGKILAIEDQLNLPGYENvtVVDLHGKILVPGFIDQHVHI 63
|
|
| PRK08203 |
PRK08203 |
hydroxydechloroatrazine ethylaminohydrolase; Reviewed |
9-112 |
7.50e-05 |
|
hydroxydechloroatrazine ethylaminohydrolase; Reviewed
Pssm-ID: 236184 [Multi-domain] Cd Length: 451 Bit Score: 45.23 E-value: 7.50e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66392186 9 RILIKGGKVV---NDDFTQEAD--VYIENGIIQQVGKELMIPG-GAKVIDATGKLVLPGGIDTSVHLNES-------FMN 75
Cdd:PRK08203 2 TLWIKNPLAIvtmDAARREIADggLVVEGGRIVEVGPGGALPQpADEVFDARGHVVTPGLVNTHHHFYQTltralpaAQD 81
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 66392186 76 GT---------------TADDFYSGTKAALA----GGTTMVIGH--VLPEKNESLLDA 112
Cdd:PRK08203 82 AElfpwlttlypvwarlTPEMVRVATQTALAelllSGCTTSSDHhyLFPNGLRDALDD 139
|
|
| PRK09228 |
PRK09228 |
guanine deaminase; Provisional |
30-68 |
2.07e-04 |
|
guanine deaminase; Provisional
Pssm-ID: 236419 [Multi-domain] Cd Length: 433 Bit Score: 44.03 E-value: 2.07e-04
10 20 30 40
....*....|....*....|....*....|....*....|...
gi 66392186 30 IENGIIQQVGK--ELM--IPGGAKVIDATGKLVLPGGIDTSVH 68
Cdd:PRK09228 36 VEDGRIVAAGPyaELRaqLPADAEVTDYRGKLILPGFIDTHIH 78
|
|
| metallo-dependent_hydrolases |
cd01292 |
Superfamily of metallo-dependent hydrolases (also called amidohydrolase superfamily) is a ... |
63-213 |
2.86e-04 |
|
Superfamily of metallo-dependent hydrolases (also called amidohydrolase superfamily) is a large group of proteins that show conservation in their 3-dimensional fold (TIM barrel) and in details of their active site. The vast majority of the members have a conserved metal binding site, involving four histidines and one aspartic acid residue. In the common reaction mechanism, the metal ion (or ions) deprotonate a water molecule for a nucleophilic attack on the substrate. The family includes urease alpha, adenosine deaminase, phosphotriesterase dihydroorotases, allantoinases, hydantoinases, AMP-, adenine and cytosine deaminases, imidazolonepropionase, aryldialkylphosphatase, chlorohydrolases, formylmethanofuran dehydrogenases and others.
Pssm-ID: 238617 [Multi-domain] Cd Length: 275 Bit Score: 43.09 E-value: 2.86e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66392186 63 IDTSVHL----------------NESFMNGTTADDFYSGTKAALAGGTTMVIGHVLPEKNESLLDAYEKARSHADAKACC 126
Cdd:cd01292 2 IDTHVHLdgsalrgtrlnlelkeAEELSPEDLYEDTLRALEALLAGGVTTVVDMGSTPPPTTTKAAIEAVAEAARASAGI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66392186 127 DYALHMGV----TWWGPKARAQMETLVRD---KGVNSFQMYMAYKDmYMLRDSELFQALQNCKDIGAVARVHAENGELVA 199
Cdd:cd01292 82 RVVLGLGIpgvpAAVDEDAEALLLELLRRgleLGAVGLKLAGPYTA-TGLSDESLRRVLEEARKLGLPVVIHAGELPDPT 160
|
170
....*....|....
gi 66392186 200 EGAREALDLGISGP 213
Cdd:cd01292 161 RALEDLVALLRLGG 174
|
|
| Urease_alpha |
cd00375 |
Urease alpha-subunit; Urease is a nickel-dependent metalloenzyme that catalyzes the hydrolysis ... |
26-99 |
3.67e-04 |
|
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: 43.47 E-value: 3.67e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66392186 26 ADVYIENGIIQQVGK-----------ELMIPG-GAKVIDATGKLVLPGGIDTSVHlnesFMNGTTADdfysgtkAALAGG 93
Cdd:cd00375 83 ADIGIKDGRIVAIGKagnpdimdgvtPNMIVGpSTEVIAGEGKIVTAGGIDTHVH----FICPQQIE-------EALASG 151
|
....*.
gi 66392186 94 TTMVIG 99
Cdd:cd00375 152 ITTMIG 157
|
|
| ureC |
PRK13308 |
urease subunit alpha; Reviewed |
24-99 |
3.71e-04 |
|
urease subunit alpha; Reviewed
Pssm-ID: 183965 [Multi-domain] Cd Length: 569 Bit Score: 43.16 E-value: 3.71e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66392186 24 QEADVYIENGIIQQVGK------------ELMIPGGAKVIDATGKLVLPGGIDTSVHLNESFMngttaddfysgTKAALA 91
Cdd:PRK13308 85 VKGDIGIRDGRIVGIGKagnpdimdgvdpRLVVGPGTDVRPAEGLIATPGAIDVHVHFDSAQL-----------VDHALA 153
|
....*...
gi 66392186 92 GGTTMVIG 99
Cdd:PRK13308 154 SGITTMLG 161
|
|
| Imidazolone-5PH |
cd01296 |
Imidazolonepropionase/imidazolone-5-propionate hydrolase (Imidazolone-5PH) catalyzes the third ... |
28-98 |
5.12e-04 |
|
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: 42.63 E-value: 5.12e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 66392186 28 VYIENGIIQQVGKELMIPG----GAKVIDATGKLVLPGGIDTSVHLNESfmnGTTADDFYsgtkAALAGGTTMVI 98
Cdd:cd01296 1 IAIRDGRIAAVGPAASLPApgpaAAEEIDAGGRAVTPGLVDCHTHLVFA---GDRVDEFA----ARLAGASYEEI 68
|
|
| ureC |
PRK13207 |
urease subunit alpha; Reviewed |
26-78 |
7.09e-04 |
|
urease subunit alpha; Reviewed
Pssm-ID: 237305 [Multi-domain] Cd Length: 568 Bit Score: 42.47 E-value: 7.09e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 66392186 26 ADVYIENGIIQQVGK----------ELMIPGGAKVIDATGKLVLPGGIDTSVHL------NESFMNGTT 78
Cdd:PRK13207 85 ADIGIKDGRIVAIGKagnpdiqdgvDIIIGPGTEVIAGEGLIVTAGGIDTHIHFicpqqiEEALASGVT 153
|
|
| COG3653 |
COG3653 |
N-acyl-D-aspartate/D-glutamate deacylase [Secondary metabolites biosynthesis, transport and ... |
10-453 |
1.05e-03 |
|
N-acyl-D-aspartate/D-glutamate deacylase [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 442870 [Multi-domain] Cd Length: 528 Bit Score: 41.70 E-value: 1.05e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66392186 10 ILIKGGKVVndDFT----QEADVYIENGIIQQVGKeLMIPGGAKVIDATGKLVLPGGIDTSVH----------LNESFMN 75
Cdd:COG3653 4 LLIRGGTVV--DGTgappFRADVAIKGGRIVAVGD-LAAAEAARVIDATGLVVAPGFIDIHTHydlqllwdprLEPSLRQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66392186 76 GTT--------------ADDFYSGTKAALAGGTTMVIGhvLPEKNESL---LDAYEKARS---------HADAKACCdya 129
Cdd:COG3653 81 GVTtvvmgncgvsfapvRPEDRDRLIDLMEGVEGIPEG--LDWDWESFgeyLDALERRGLgvnvaslvgHGTLRAYV--- 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66392186 130 lhMGVTWWGPKAR--AQMETLVRdkgvnsfqmymaykdmymlrdselfQALQNckdiGAV----ARV-----HAENGELV 198
Cdd:COG3653 156 --MGLDDRPPTPEelARMRALLR-------------------------EAMEA----GALglstGLIyvpgtYASTDELV 204
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66392186 199 AEgAREALDLGisgpeGIEIS--RPEELEA-EAVHRAITIANRAHCP--IYLVNVS-------SMSAGDVLASAKMQGKV 266
Cdd:COG3653 205 AL-AKVVAEYG-----GVYQShmRDEGDGLlEAVDELIRIGREAGVPvhISHLKAAgkpnwgkADEVLALIEAARAEGLD 278
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66392186 267 VHGETTTAHAVLNGMQYYHQDWAHA---AAFVTvpplRL-DP------------NTPNYLLSLLGNDTLNVV-TSDHRPF 329
Cdd:COG3653 279 VTADVYPYPAGSTGLGALLPPWAAAgglDERLA----RLrDPatrariraeieeGLPDNLLGRGGWDNILISdSPPNEPL 354
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66392186 330 TTK-----QKAMGKDDF-----TKIPHGvPGVQDRMSVMWER----------------GVVGGK---------------- 367
Cdd:COG3653 355 VGKslaeiAAERGVDPAdaaldLLLEED-GRVLIVYFIMSEEdvrellrhpwvmigsdGGLGGKahpraygtfprvlghy 433
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66392186 368 -MDENRF-----VAVTSSNAAKIYNLYPRkGRIIPGADADVVVWDPEstrTIsvttqwqgGDVNLYENLRCH--GVPLVT 439
Cdd:COG3653 434 vRERGVLsleeaVRKLTSLPADRLGLKDR-GLLRPGYRADLVVFDPA---TL--------ADRATFDLPAQRadGIRAVI 501
|
570
....*....|....
gi 66392186 440 ISrGRVVYENGIFT 453
Cdd:COG3653 502 VN-GVVVVEDGKPT 514
|
|
| PRK15446 |
PRK15446 |
phosphonate metabolism protein PhnM; Provisional |
7-64 |
1.33e-03 |
|
phosphonate metabolism protein PhnM; Provisional
Pssm-ID: 237967 [Multi-domain] Cd Length: 383 Bit Score: 41.32 E-value: 1.33e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 66392186 7 TVRILIKGGKVVNDDFTQEADVYIENGIIQQVGKELMIPGGAkvIDATGKLVLPGGID 64
Cdd:PRK15446 1 MMEMILSNARLVLPDEVVDGSLLIEDGRIAAIDPGASALPGA--IDAEGDYLLPGLVD 56
|
|
| Isoaspartyl-dipeptidase |
cd01308 |
Isoaspartyl dipeptidase hydrolyzes the beta-L-isoaspartyl linkages in dipeptides, as part of ... |
376-408 |
2.75e-03 |
|
Isoaspartyl dipeptidase hydrolyzes the beta-L-isoaspartyl linkages in dipeptides, as part of the degradative pathway to eliminate proteins with beta-L-isoaspartyl peptide bonds, bonds whereby the beta-group of an aspartate forms the peptide link with the amino group of the following amino acid. Formation of this bond is a spontaneous nonenzymatic reaction in nature and can profoundly effect the function of the protein. Isoaspartyl dipeptidase is an octameric enzyme that contains a binuclear zinc center in the active site of each subunit and shows a strong preference of hydrolyzing Asp-Leu dipeptides.
Pssm-ID: 238633 [Multi-domain] Cd Length: 387 Bit Score: 40.45 E-value: 2.75e-03
10 20 30
....*....|....*....|....*....|...
gi 66392186 376 VTSSNAAKIYNLYPrKGRIIPGADADVVVWDPE 408
Cdd:cd01308 330 VITSNVARILKLRK-KGEIQPGFDADLVILDKD 361
|
|
| ureC |
PRK13206 |
urease subunit alpha; Reviewed |
26-99 |
5.52e-03 |
|
urease subunit alpha; Reviewed
Pssm-ID: 237304 [Multi-domain] Cd Length: 573 Bit Score: 39.69 E-value: 5.52e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66392186 26 ADVYIENGIIQQVGK------------ELMIPGGAKVIDATGKLVLPGGIDTSVHlnesFMNGTTADDfysgtkaALAGG 93
Cdd:PRK13206 89 ADVGIRDGRIVAIGKagnpdimdgvhpDLVIGPSTEIIAGNGRILTAGAIDCHVH----FICPQIVDE-------ALAAG 157
|
....*.
gi 66392186 94 TTMVIG 99
Cdd:PRK13206 158 ITTLIG 163
|
|
| |
