|
Name |
Accession |
Description |
Interval |
E-value |
| PRK08044 |
PRK08044 |
allantoinase AllB; |
1-449 |
0e+00 |
|
allantoinase AllB;
Pssm-ID: 169193 [Multi-domain] Cd Length: 449 Bit Score: 943.52 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445929010 1 MSFDLIIKNGTVILENEARVIDIAVQGGKIAAIGENLGEAKNVLDATGLIVSPGMVDAHTHISEPGRTHWEGYETGTRAA 80
Cdd:PRK08044 1 MSFDLIIKNGTVILENEARVVDIAVKGGKIAAIGQDLGDAKEVMDASGLVVSPGMVDAHTHISEPGRSHWEGYETGTRAA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445929010 81 AKGGITTMIEMPLNQLPATVDRETIELKFDAAKGKLTIDAAQLGGLVSYNLDRLHELDEVGVVGFKCFVATCGDRGIDND 160
Cdd:PRK08044 81 AKGGITTMIEMPLNQLPATVDRASIELKFDAAKGKLTIDAAQLGGLVSYNLDRLHELDEVGVVGFKCFVATCGDRGIDND 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445929010 161 FRDVNDWQFYKGAQKLGEMDQTVLVHCENALICDELGEEAKREGRVTAHDYVASRPVFTEVEAIRRVLYLAKAAGCRLHV 240
Cdd:PRK08044 161 FRDVNDWQFYKGAQKLGELGQPVLVHCENALICDELGEEAKREGRVTAHDYVASRPVFTEVEAIRRVLYLAKVAGCRLHV 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445929010 241 CHISSPEGVEEVTRARQEGQDVTCESCPHYFVLDTDQFEEIGTLAKCSPPIRDQENQKGMWEKLFNGEIDCLVSDHSPCP 320
Cdd:PRK08044 241 CHISSPEGVEEVTRARQEGQDVTCESCPHYFVLDTDQFEEIGTLAKCSPPIRDLENQKGMWEKLFNGEIDCLVSDHSPCP 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445929010 321 PEMKAGNIMQAWGGIAGLQNCMDVMFDEAVQKRGMSLPMFGKLMATNAADIFGLKHKGRIAPGKDADLVFIQPDSSYVLK 400
Cdd:PRK08044 321 PEMKAGNIMEAWGGIAGLQNCMDVMFDEAVQKRGMSLPMFGKLMATNAADIFGLQQKGRIAPGKDADFVFIQPNSSYVLK 400
|
410 420 430 440
....*....|....*....|....*....|....*....|....*....
gi 445929010 401 NEDLEYRHKVSPYVGRTIGARITKTILRGDVIYDIEHGFPVPPKGQFIL 449
Cdd:PRK08044 401 NEDLEYRHKVSPYVGRTIGARITKTILRGDVIYDIEQGFPVAPKGQFIL 449
|
|
| allantoinase |
TIGR03178 |
allantoinase; This enzyme carries out the first step in the degradation of allantoin, a ... |
4-449 |
0e+00 |
|
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: 744.20 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445929010 4 DLIIKNGTVILENEARVIDIAVQGGKIAAIG-ENLGEAKNVLDATGLIVSPGMVDAHTHISEPGRTHWEGYETGTRAAAK 82
Cdd:TIGR03178 1 DLIIRGGRVILPNGEREADVGVKGGKIAAIGpDILGPAAKIIDAGGLVVFPGVVDTHVHINEPGRTEWEGFETGTRAAAA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445929010 83 GGITTMIEMPLNQLPATVDRETIELKFDAAKGKLTIDAAQLGGLVSYNLDRLHELDEVGVVGFKCFVATCGDrgidNDFR 162
Cdd:TIGR03178 81 GGITTYIDMPLNSIPATTTRASLEAKFEAAKGKLAVDVGFWGGLVPYNLDDLRELDEAGVVGFKAFLSPSGD----DEFP 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445929010 163 DVNDWQFYKGAQKLGEMDQTVLVHCENALICDELGEEAKREGRVTAHDYVASRPVFTEVEAIRRVLYLAKAAGCRLHVCH 242
Cdd:TIGR03178 157 HVDDWQLYKGMRELARLGQLLLVHAENPAITSALGEEAPPQGGVGADAYLASRPVFAEVEAIRRTLALAKVTGCRVHVVH 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445929010 243 ISSPEGVEEVTRARQEGQDVTCESCPHYFVLDTDQFEEIGTLAKCSPPIRDQENQKGMWEKLFNGEIDCLVSDHSPCPPE 322
Cdd:TIGR03178 237 LSSAEAVELITEAKQEGLDVTVETCPHYLTLTAEEVPDGGTLAKCAPPIRDLANQEGLWEALLNGLIDCVVSDHSPCTPD 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445929010 323 MK-AGNIMQAWGGIAGLQNCMDVMFDEAVQKRGMSLPMFGKLMATNAADIFGLKHKGRIAPGKDADLVFIQPDSSYVLKN 401
Cdd:TIGR03178 317 LKrAGDFFKAWGGIAGLQSTLDVMFDEAVQKRGLPLEDIARLMATNPAKRFGLAQKGRIAPGKDADFVFVDPDESYTLTP 396
|
410 420 430 440
....*....|....*....|....*....|....*....|....*...
gi 445929010 402 EDLEYRHKVSPYVGRTIGARITKTILRGDVIYDIEHgFPVPPKGQFIL 449
Cdd:TIGR03178 397 DDLYYRHKVSPYVGRTIGGRVRATYLRGQCIYDDEQ-FIGAPKGQLLL 443
|
|
| L-HYD_ALN |
cd01315 |
L-Hydantoinases (L-HYDs) and Allantoinase (ALN); L-Hydantoinases are a member of the ... |
4-449 |
0e+00 |
|
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: 692.88 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445929010 4 DLIIKNGTVILENEARVIDIAVQGGKIAAIGENL--GEAKNVLDATGLIVSPGMVDAHTHISEPGRTHWEGYETGTRAAA 81
Cdd:cd01315 1 DLVIKNGRVVTPDGVREADIAVKGGKIAAIGPDIanTEAEEVIDAGGLVVMPGLIDTHVHINEPGRTEWEGFETGTKAAA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445929010 82 KGGITTMIEMPLNQLPATVDRETIELKFDAAKGKLTIDAAQLGGLVSYNLDRLHELDEVGVVGFKCFVATCGDrgidNDF 161
Cdd:cd01315 81 AGGITTIIDMPLNSIPPTTTVENLEAKLEAAQGKLHVDVGFWGGLVPGNLDQLRPLDEAGVVGFKCFLCPSGV----DEF 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445929010 162 RDVNDWQFYKGAQKLGEMDQTVLVHCENALICDELGEEAKREGRVTAHDYVASRPVFTEVEAIRRVLYLAKAAGCRLHVC 241
Cdd:cd01315 157 PAVDDEQLEEAMKELAKTGSVLAVHAENPEITEALQEQAKAKGKRDYRDYLASRPVFTEVEAIQRILLLAKETGCRLHIV 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445929010 242 HISSPEGVEEVTRARQEGQDVTCESCPHYFVLDTDQFEEIGTLAKCSPPIRDQENQKGMWEKLFNGEIDCLVSDHSPCPP 321
Cdd:cd01315 237 HLSSAEAVPLIREARAEGVDVTVETCPHYLTFTAEDVPDGGTEFKCAPPIRDAANQEQLWEALENGDIDMVVSDHSPCTP 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445929010 322 EMKA---GNIMQAWGGIAGLQNCMDVMFDEAVQKRGMSLPMFGKLMATNAADIFGLKH-KGRIAPGKDADLVFIQPDSSY 397
Cdd:cd01315 317 ELKLlgkGDFFKAWGGISGLQLGLPVMLTEAVNKRGLSLEDIARLMCENPAKLFGLSHqKGRIAVGYDADFVVWDPEEEF 396
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|..
gi 445929010 398 VLKNEDLEYRHKVSPYVGRTIGARITKTILRGDVIYDIEhGFPVPPKGQFIL 449
Cdd:cd01315 397 TVDAEDLYYKNKISPYVGRTLKGRVHATILRGTVVYQDG-EVVGEPLGQLLL 447
|
|
| AllB |
COG0044 |
Dihydroorotase or related cyclic amidohydrolase [Nucleotide transport and metabolism]; ... |
6-448 |
3.80e-180 |
|
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: 510.40 E-value: 3.80e-180
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445929010 6 IIKNGTVILENEARVIDIAVQGGKIAAIGENL--GEAKNVLDATGLIVSPGMVDAHTHISEPGRTHWEGYETGTRAAAKG 83
Cdd:COG0044 1 LIKNGRVVDPGGLERADVLIEDGRIAAIGPDLaaPEAAEVIDATGLLVLPGLIDLHVHLREPGLEHKEDIETGTRAAAAG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445929010 84 GITTMIEMPlNQLPATVDRETIELKFDAAKGKLTIDAAQLGGLV---SYNLDRLHELDEVGVVGFKCFVATCGDRGIDND 160
Cdd:COG0044 81 GVTTVVDMP-NTNPVTDTPEALEFKLARAEEKALVDVGPHGALTkglGENLAELGALAEAGAVAFKVFMGSDDGNPVLDD 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445929010 161 frdvndWQFYKGAQKLGEMDQTVLVHCENALICDELgeeAKREGRVTAHDYVASRPVFTEVEAIRRVLYLAKAAGCRLHV 240
Cdd:COG0044 160 ------GLLRRALEYAAEFGALVAVHAEDPDLIRGG---VMNEGKTSPRLGLKGRPAEAEEEAVARDIALAEETGARLHI 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445929010 241 CHISSPEGVEEVTRARQEGQDVTCESCPHYFVLDTDQFEEIGTLAKCSPPIRDQENQKGMWEKLFNGEIDCLVSDHSPCP 320
Cdd:COG0044 231 VHVSTAEAVELIREAKARGLPVTAEVCPHHLTLTDEDLERYGTNFKVNPPLRTEEDREALWEGLADGTIDVIATDHAPHT 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445929010 321 PEMKAGNIMQAWGGIAGLQNCMDVMFDEAVQKRGMSLPMFGKLMATNAADIFGLKHKGRIAPGKDADLVFIQPDSSYVLK 400
Cdd:COG0044 311 LEEKELPFAEAPNGIPGLETALPLLLTELVHKGRLSLERLVELLSTNPARIFGLPRKGRIAVGADADLVLFDPDAEWTVT 390
|
410 420 430 440
....*....|....*....|....*....|....*....|....*...
gi 445929010 401 NEDLEYRHKVSPYVGRTIGARITKTILRGDVIYDiEHGFPVPPKGQFI 448
Cdd:COG0044 391 AEDLHSKSKNTPFEGRELTGRVVATIVRGRVVYE-DGEVVGEPRGRFL 437
|
|
| PRK06189 |
PRK06189 |
allantoinase; Provisional |
1-451 |
1.26e-178 |
|
allantoinase; Provisional
Pssm-ID: 235732 [Multi-domain] Cd Length: 451 Bit Score: 506.93 E-value: 1.26e-178
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445929010 1 MSFDLIIKNGTVILENEARVIDIAVQGGKIAAIGENL-GEAKNVLDATGLIVSPGMVDAHTHISEPGRTHWEGYETGTRA 79
Cdd:PRK06189 1 MMYDLIIRGGKVVTPEGVYRADIGIKNGKIAEIAPEIsSPAREIIDADGLYVFPGMIDVHVHFNEPGRTHWEGFATGSAA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445929010 80 AAKGGITTMIEMPLNQLPATVDRETIELKFDAAKGKLTIDAAQLGGLVSYNLDRLHELDEVGVVGFKCFVATCGDrgidN 159
Cdd:PRK06189 81 LAAGGCTTYFDMPLNSIPPTVTREALDAKAELARQKSAVDFALWGGLVPGNLEHLRELAEAGVIGFKAFMSNSGT----D 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445929010 160 DFRDVNDWQFYKGAQKLGEMDQTVLVHCENALICDELGEEAKREGRVTAHDYVASRPVFTEVEAIRRVLYLAKAAGCRLH 239
Cdd:PRK06189 157 EFRSSDDLTLYEGMKEIAALGKILALHAESDALTRHLTTQARQQGKTDVRDYLESRPVVAELEAVQRALLYAQETGCPLH 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445929010 240 VCHISSPEGVEEVTRARQEGQDVTCESCPHYFVLDTDQFEEIGTLAKCSPPIRDQENQKGMWEKLFNGEIDCLVSDHSPC 319
Cdd:PRK06189 237 FVHISSGKAVALIAEAKKRGVDVSVETCPHYLLFTEEDFERIGAVAKCAPPLRSRSQKEELWRGLLAGEIDMISSDHSPC 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445929010 320 PPEMKAG-NIMQAWGGIAGLQNCMDVMFDEAVQKRGMSLPMFGKLMATNAADIFGLKHKGRIAPGKDADLVFIQPDSSYV 398
Cdd:PRK06189 317 PPELKEGdDFFLVWGGISGGQSTLLVMLTEGYIERGIPLETIARLLATNPAKRFGLPQKGRLEVGADADFVLVDLDETYT 396
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|...
gi 445929010 399 LKNEDLEYRHKVSPYVGRTIGARITKTILRGDVIYDiEHGFPVPPKGQFILKH 451
Cdd:PRK06189 397 LTKEDLFYRHKQSPYEGRTFPGRVVATYLRGQCVYQ-DGEVFPPPRGQLLRPS 448
|
|
| PLN02795 |
PLN02795 |
allantoinase |
25-450 |
9.23e-115 |
|
allantoinase
Pssm-ID: 178392 [Multi-domain] Cd Length: 505 Bit Score: 346.38 E-value: 9.23e-115
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445929010 25 VQGGKIAAIGENLGEAKN-----VLDATGLIVSPGMVDAHTHISEPGRTHWEGYETGTRAAAKGGITTMIEMPLNQLPAT 99
Cdd:PLN02795 66 VEGGRIVSVTKEEEAPKSqkkphVLDYGNAVVMPGLIDVHVHLNEPGRTEWEGFPTGTKAAAAGGITTLVDMPLNSFPST 145
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445929010 100 VDRETIELKFDAAKGKLTIDAAQLGGLVS---YNLDRLHELDEVGVVGFKCFVATCGdrgiDNDFRDVNDWQFYKGAQKL 176
Cdd:PLN02795 146 TSVETLELKIEAAKGKLYVDVGFWGGLVPenaHNASVLEELLDAGALGLKSFMCPSG----INDFPMTTATHIKAALPVL 221
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445929010 177 GEMDQTVLVHCEnalICDELGEEAKREGRVTAHD-YVASRPVFTEVEAIRRVLYLAK-------AAGCRLHVCHIS-SPE 247
Cdd:PLN02795 222 AKYGRPLLVHAE---VVSPVESDSRLDADPRSYStYLKSRPPSWEQEAIRQLLEVAKdtrpggvAEGAHVHIVHLSdAES 298
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445929010 248 GVEEVTRARQEGQDVTCESCPHYFVLDTDQFEEIGTLAKCSPPIRDQENQKGMWEKLFNGEIDCLVSDHSPCPPEMK--- 324
Cdd:PLN02795 299 SLELIKEAKAKGDSVTVETCPHYLAFSAEEIPDGDTRYKCAPPIRDAANRELLWKALLDGDIDMLSSDHSPSPPDLKlle 378
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445929010 325 AGNIMQAWGGIAGLQNCMDVMFdEAVQKRGMSLPMFGKLMATNAADIFGLKHKGRIAPGKDADLVFIQPDSSYVLkNED- 403
Cdd:PLN02795 379 EGNFLRAWGGISSLQFVLPATW-TAGRAYGLTLEQLARWWSERPAKLAGLDSKGAIAPGKDADIVVWDPEAEFVL-DESy 456
|
410 420 430 440
....*....|....*....|....*....|....*....|....*....
gi 445929010 404 -LEYRHK-VSPYVGRTIGARITKTILRGDVIYDIEHGFPVpPKGQFILK 450
Cdd:PLN02795 457 pIYHKHKsLSPYLGTKLSGKVIATFVRGNLVFLEGKHAKQ-ACGSPILA 504
|
|
| PRK02382 |
PRK02382 |
dihydroorotase; Provisional |
4-448 |
3.57e-102 |
|
dihydroorotase; Provisional
Pssm-ID: 179417 [Multi-domain] Cd Length: 443 Bit Score: 311.97 E-value: 3.57e-102
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445929010 4 DLIIKNGTVILENEARVIDIAVQGGKIAAIGENL--GEAKNVLDATGLIVSPGMVDAHTHISEPGRTHWEGYETGTRAAA 81
Cdd:PRK02382 3 DALLKDGRVYYNNSLQPRDVRIDGGKITAVGKDLdgSSSEEVIDARGMLLLPGGIDVHVHFREPGYTHKETWYTGSRSAA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445929010 82 KGGITTMIEMPlNQLPATVDRETIELKFDAAKGKLTIDAAQLGGlVSYNLDRLHELDEVGVVGF-KCFVA-TCGDRGIDN 159
Cdd:PRK02382 83 AGGVTTVVDQP-NTDPPTVDGESFDEKAELAARKSIVDFGINGG-VTGNWDPLESLWERGVFALgEIFMAdSTGGMGIDE 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445929010 160 DfrdvndwQFYKGAQKLGEMDQTVLVHCENALICDELGEEAKREGRVTAHDyvASRPVFTEVEAIRRVLYLAKAAGCRLH 239
Cdd:PRK02382 161 E-------LFEEALAEAARLGVLATVHAEDEDLFDELAKLLKGDADADAWS--AYRPAAAEAAAVERALEVASETGARIH 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445929010 240 VCHISSPEGVEEVTRARqegqdVTCESCPHYFVLDTDQFEEIGTLAKCSPPIRDQENQKGMWEKLFNGEIDCLVSDHSPC 319
Cdd:PRK02382 232 IAHISTPEGVDAARREG-----ITCEVTPHHLFLSRRDWERLGTFGKMNPPLRSEKRREALWERLNDGTIDVVASDHAPH 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445929010 320 PPEMKAGNIMQAWGGIAGLQNCMDVMFdEAVQKRGMSLPMFGKLMATNAADIFGLKHKGRIAPGKDADLVFIQPDSSYVL 399
Cdd:PRK02382 307 TREEKDADIWDAPSGVPGVETMLPLLL-AAVRKNRLPLERVRDVTAANPARIFGLDGKGRIAEGYDADLVLVDPDAAREI 385
|
410 420 430 440
....*....|....*....|....*....|....*....|....*....
gi 445929010 400 KNEDLEYRHKVSPYVGRTiGARITKTILRGDVIYDIEHGFPVPPKGQFI 448
Cdd:PRK02382 386 RGDDLHSKAGWTPFEGME-GVFPELTMVRGTVVWDGDDINAKRGRGEFL 433
|
|
| D-HYD |
cd01314 |
D-hydantoinases (D-HYD) also called dihydropyrimidases (DHPase) and related proteins; DHPases ... |
5-434 |
1.50e-97 |
|
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: 299.90 E-value: 1.50e-97
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445929010 5 LIIKNGTVILENEARVIDIAVQGGKIAAIGENLGEAKN--VLDATGLIVSPGMVDAHTHISEP--GRTHWEGYETGTRAA 80
Cdd:cd01314 1 LIIKNGTIVTADGSFKADILIEDGKIVAIGPNLEAPGGveVIDATGKYVLPGGIDPHTHLELPfmGTVTADDFESGTRAA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445929010 81 AKGGITTMIEMpLNQLPATVDRETIELKFDAAKGKLTIDAAQLGGLVSYNLDRLHELDEV---GVVGFKCFVATcgdrgi 157
Cdd:cd01314 81 AAGGTTTIIDF-AIPNKGQSLLEAVEKWRGKADGKSVIDYGFHMIITDWTDSVIEELPELvkkGISSFKVFMAY------ 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445929010 158 dNDFRDVNDWQFYKGAQKLGEMDQTVLVHCENALICDELGEEAKREGRVTAHDYVASRPVFTEVEAIRRVLYLAKAAGCR 237
Cdd:cd01314 154 -KGLLMVDDEELLDVLKRAKELGALVMVHAENGDVIAELQKKLLAQGKTGPEYHALSRPPEVEAEATARAIRLAELAGAP 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445929010 238 LHVCHISSPEGVEEVTRARQEGQDVTCESCPHYFVLDTDQFE---EIGTLAKCSPPIRDQENQKGMWEKLFNGEIDCLVS 314
Cdd:cd01314 233 LYIVHVSSKEAADEIARARKKGLPVYGETCPQYLLLDDSDYWkdwFEGAKYVCSPPLRPKEDQEALWDGLSSGTLQTVGS 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445929010 315 DHSPCPPEMKA---GNIMQAWGGIAGLQNCMDVMFDEAVQKRGMSLPMFGKLMATNAADIFGL-KHKGRIAPGKDADLVF 390
Cdd:cd01314 313 DHCPFNFAQKArgkDDFTKIPNGVPGVETRMPLLWSEGVAKGRITLEKFVELTSTNPAKIFGLyPRKGTIAVGSDADLVI 392
|
410 420 430 440
....*....|....*....|....*....|....*....|....
gi 445929010 391 IQPDSSYVLKNEDLEYRHKVSPYVGRTIGARITKTILRGDVIYD 434
Cdd:cd01314 393 WDPNAEKTISADTHHHNVDYNIFEGMKVKGWPVVTISRGKVVVE 436
|
|
| PRK08323 |
PRK08323 |
phenylhydantoinase; Validated |
3-434 |
1.46e-94 |
|
phenylhydantoinase; Validated
Pssm-ID: 236240 [Multi-domain] Cd Length: 459 Bit Score: 292.85 E-value: 1.46e-94
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445929010 3 FDLIIKNGTVILENEARVIDIAVQGGKIAAIGENlgEAKNVLDATGLIVSPGMVDAHTHISEP--GRTHWEGYETGTRAA 80
Cdd:PRK08323 1 MSTLIKNGTVVTADDTYKADVLIEDGKIAAIGAN--LGDEVIDATGKYVMPGGIDPHTHMEMPfgGTVSSDDFETGTRAA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445929010 81 AKGGITTMIEMPLnQLPATVDRETIELKFDAAKGKLTIDAAQLGGLVSYNLDRLHELDEV---GVVGFKCFVAtcgdrgI 157
Cdd:PRK08323 79 ACGGTTTIIDFAL-QPKGQSLREALEAWHGKAAGKAVIDYGFHMIITDWNEVVLDEMPELveeGITSFKLFMA------Y 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445929010 158 DNDFRdVNDWQFYKGAQKLGEMDQTVLVHCENALICDELGEEAKREGRVTAHDYVASRPVFTEVEAIRRVLYLAKAAGCR 237
Cdd:PRK08323 152 KGALM-LDDDELLRALQRAAELGALPMVHAENGDAIAYLQAKLLAEGKTGPEYHALSRPPEVEGEATNRAIMLAELAGAP 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445929010 238 LHVCHISSPEGVEEVTRARQEGQDVTCESCPHYFVLDTDQFEEIGTL--AK--CSPPIRDQENQKGMWEKLFNGEIDCLV 313
Cdd:PRK08323 231 LYIVHVSCKEALEAIRRARARGQRVFGETCPQYLLLDESEYDGPDWFegAKyvMSPPLRDKEHQDALWRGLQDGDLQVVA 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445929010 314 SDHspCP-----PEMKA-GNIMQAWGGIAGLQNCMDVMFDEAVQKRGMSLPMFGKLMATNAADIFGL-KHKGRIAPGKDA 386
Cdd:PRK08323 311 TDH--CPfcfeqKKQLGrGDFTKIPNGTPGVEDRMPLLFSEGVMTGRITLNRFVELTSTNPAKIFGLyPRKGTIAVGADA 388
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|
gi 445929010 387 DLVFIQPDSSYVLKNEDLeyRHKV--SPYVGRTIGARITKTILRGDVIYD 434
Cdd:PRK08323 389 DIVIWDPNATKTISASTL--HSNVdyNPYEGFEVTGWPVTTLSRGEVVVE 436
|
|
| DHOase_IIb |
cd01318 |
Dihydroorotase (DHOase), subgroup IIb; DHOases catalyze the reversible interconversion of ... |
48-429 |
1.74e-89 |
|
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: 276.52 E-value: 1.74e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445929010 48 GLIVSPGMVDAHTHISEPGRTHWEGYETGTRAAAKGGITTMIEMPlNQLPATVDRETIELKFDAAKGKLTIDAAqLGGLV 127
Cdd:cd01318 1 GLLILPGVIDIHVHFREPGLTYKEDFVSGSRAAAAGGVTTVMDMP-NTKPPTTTAEALYEKLRLAAAKSVVDYG-LYFGV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445929010 128 SYNLDrLHELDEVGVVGFKCFVATC-GDRGID-NDFRDVndwqfykgaqkLGEMDQTVLVHCENALICDELGEEAKREgr 205
Cdd:cd01318 79 TGSED-LEELDKAPPAGYKIFMGDStGDLLDDeETLERI-----------FAEGSVLVTFHAEDEDRLRENRKELKGE-- 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445929010 206 vtaHDYVASRPVFTEVEAIRRVLYLAKAAGCRLHVCHISSPEGVEEvtrARQEGQDVTCESCPHYFVLDTDQFEEIGTLA 285
Cdd:cd01318 145 ---SAHPRIRDAEAAAVATARALKLARRHGARLHICHVSTPEELKL---IKKAKPGVTVEVTPHHLFLDVEDYDRLGTLG 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445929010 286 KCSPPIRDQENQKGMWEKLFNGEIDCLVSDHSPCPPEMKAGNIMQAWGGIAGLQNCMDVMFDeAVQKRGMSLPMFGKLMA 365
Cdd:cd01318 219 KVNPPLRSREDRKALLQALADGRIDVIASDHAPHTLEEKRKGYPAAPSGIPGVETALPLMLT-LVNKGILSLSRVVRLTS 297
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 445929010 366 TNAADIFGLKHKGRIAPGKDADLVFIQPDSSYVLKNEDLEYRHKVSPYVGRTIGARITKTILRG 429
Cdd:cd01318 298 HNPARIFGIKNKGRIAEGYDADLTVVDLKEERTIRAEEFHSKAGWTPFEGFEVTGFPVMTIVRG 361
|
|
| pyrC_multi |
TIGR00857 |
dihydroorotase, multifunctional complex type; In contrast to the homodimeric type of ... |
22-433 |
2.83e-88 |
|
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: 275.09 E-value: 2.83e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445929010 22 DIAVQGGKIAAIGENLGEA-KNVLDATGLIVSPGMVDAHTHISEPGRTHWEGYETGTRAAAKGGITTMIEMPLNQLPATv 100
Cdd:TIGR00857 7 DILVEGGRIKKIGKLRIPPdAEVIDAKGLLVLPGFIDLHVHLRDPGEEYKEDIESGSKAAAHGGFTTVADMPNTKPPID- 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445929010 101 DRETIELKFDAAKGKLTIDAAqLGGLVSYNLDrlheLDEVGVVGFKCFVATCGDRGIDNDFRDVNDWQFYKGAQKLGEMD 180
Cdd:TIGR00857 86 TPETLEWKLQRLKKVSLVDVH-LYGGVTQGNQ----GKELTEAYELKEAGAVGRMFTDDGSEVQDILSMRRALEYAAIAG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445929010 181 QTVLVHCENAlicDELGEEAKREGRVTAHDYVASRPVFTEVEAIRRVLYLAKAAGCRLHVCHISSPEGVEEVTRARQEGQ 260
Cdd:TIGR00857 161 VPIALHAEDP---DLIYGGVMHEGPSAAQLGLPARPPEAEEVAVARLLELAKHAGCPVHICHISTKESLELIVKAKSQGI 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445929010 261 DVTCESCPHYFVLDTDQFEEIGTLAKCSPPIRDQENQKGMWEKLFNGEIDCLVSDHSPCPPEMKAGNIMQAWGGIAGLQN 340
Cdd:TIGR00857 238 KITAEVTPHHLLLSEEDVARLDGNGKVNPPLREKEDRLALIEGLKDGIIDIIATDHAPHTLEEKTKEFAAAPPGIPGLET 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445929010 341 CMDVMFDEAVQKRgMSLPMFGKLMATNAADIFGLKHKGRIAPGKDADLVFIQPDSSYVLKNEDLEYRHKVSPYVGRTIGA 420
Cdd:TIGR00857 318 ALPLLLQLLVKGL-ISLKDLIRMLSINPARIFGLPDKGTLEEGNPADITVFDLKKEWTINAETFYSKAKNTPFEGMSLKG 396
|
410
....*....|...
gi 445929010 421 RITKTILRGDVIY 433
Cdd:TIGR00857 397 KPIATILRGKVVY 409
|
|
| D-hydantoinase |
TIGR02033 |
D-hydantoinase; This model represents the D-hydantoinase (dihydropyrimidinase) which primarily ... |
5-432 |
5.43e-88 |
|
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: 275.80 E-value: 5.43e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445929010 5 LIIKNGTVILENEARVIDIAVQGGKIAAIGENLG--EAKNVLDATGLIVSPGMVDAHTHISEP--GRTHWEGYETGTRAA 80
Cdd:TIGR02033 1 LLIKGGTVVNADDVFQADVLIEGGKIVAVGDNLIppDAVEVIDATGKYVLPGGIDVHTHLEMPfgGTTTADDFFTGTKAA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445929010 81 AKGGITTMIEMPLnQLPATVDRETIELKFDAAKGKLTIDAAQLGGLVSYNLDRLHE----LDEVGVVGFKCFVATcgdrg 156
Cdd:TIGR02033 81 AAGGTTTIIDFVV-PEKGSSLTEALETWHEKAEGKSVIDYGFHMDITHWNDSVLEEhipeVKEEGINSFKVFMAY----- 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445929010 157 idNDFRDVNDWQFYKGAQKLGEMDQTVLVHCENALICDELGEEAKREGRVTAHDYVASRPVFTEVEAIRRVLYLAKAAGC 236
Cdd:TIGR02033 155 --KNLLMVDDEELFEILKRLKELGALLQVHAENGDIIAELQARMLAQGITGPEYHALSRPPELEAEAVARAITLAALADA 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445929010 237 RLHVCHISSPEGVEEVTRARQEGQDVTCESCPHYFVLDTDQFE---EIGTLAKCSPPIRDQENQKGMWEKLFNGEIDCLV 313
Cdd:TIGR02033 233 PLYVVHVSTKDAADEIAQARKKGQPVFGETCPQYLVLDDTHYDkpgFEGAKYVCSPPLREPEDQDALWSALSSGALQTVG 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445929010 314 SDHspCP------PEMKAGNIMQAWGGIAGLQNCMDVMFDEAVQKRGMSLPMFGKLMATNAADIFGL-KHKGRIAPGKDA 386
Cdd:TIGR02033 313 SDH--CTfnfaqkKAIGKDDFTKIPNGGPGVEERMSLLFDEGVAKGRITLEKFVEVTSTNPAKIFNLyPRKGTIAVGSDA 390
|
410 420 430 440
....*....|....*....|....*....|....*....|....*.
gi 445929010 387 DLVFIQPDSSYVLKNEDLEYRHKVSPYVGRTIGARITKTILRGDVI 432
Cdd:TIGR02033 391 DIVIWDPNRTTVISAETHHSNADYNPFEGFKVRGAPVSVLSRGRVV 436
|
|
| pyrC |
PRK09357 |
dihydroorotase; Validated |
5-433 |
1.95e-86 |
|
dihydroorotase; Validated
Pssm-ID: 236479 [Multi-domain] Cd Length: 423 Bit Score: 270.53 E-value: 1.95e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445929010 5 LIIKNGTVI-LENEARVIDIAVQGGKIAAIGENLG-EAKNVLDATGLIVSPGMVDAHTHISEPGRTHWEGYETGTRAAAK 82
Cdd:PRK09357 3 ILIKNGRVIdPKGLDEVADVLIDDGKIAAIGENIEaEGAEVIDATGLVVAPGLVDLHVHLREPGQEDKETIETGSRAAAA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445929010 83 GGITTMIEMPlNQLPATVDRETIELKFDAAKGKLTIDAAQLG----GLVSYNLDRLHELDEVGVVGFkcfvatcGDRGID 158
Cdd:PRK09357 83 GGFTTVVAMP-NTKPVIDTPEVVEYVLDRAKEAGLVDVLPVGaitkGLAGEELTEFGALKEAGVVAF-------SDDGIP 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445929010 159 NDFRDVndwqFYKGAQKLGEMDQTVLVHCENalicDELGEEAK-REGRVTAHDYVASRPVFTEVEAIRRVLYLAKAAGCR 237
Cdd:PRK09357 155 VQDARL----MRRALEYAKALDLLIAQHCED----PSLTEGGVmNEGEVSARLGLPGIPAVAEEVMIARDVLLAEATGAR 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445929010 238 LHVCHISSPEGVEEVTRARQEGQDVTCESCPHYFVLDTDQFEEIGTLAKCSPPIRDQENQKGMWEKLFNGEIDCLVSDHS 317
Cdd:PRK09357 227 VHICHVSTAGSVELIRWAKALGIKVTAEVTPHHLLLTDEDLLTYDPNYKVNPPLRTEEDREALIEGLKDGTIDAIATDHA 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445929010 318 PCPPEMKAGNIMQAWGGIAGLQNCMDVMFDEAVQKRGMSLPMFGKLMATNAADIFGLKHkGRIAPGKDADLVFIQPDSSY 397
Cdd:PRK09357 307 PHAREEKECEFEAAPFGITGLETALSLLYTTLVKTGLLDLEQLLEKMTINPARILGLPA-GPLAEGEPADLVIFDPEAEW 385
|
410 420 430
....*....|....*....|....*....|....*.
gi 445929010 398 VLKNEDLEYRHKVSPYVGRTIGARITKTILRGDVIY 433
Cdd:PRK09357 386 TVDGEDFASKGKNTPFIGMKLKGKVVYTIVDGKIVY 421
|
|
| Cyclic_amidohydrolases |
cd01302 |
Cyclic amidohydrolases, including hydantoinase, dihydropyrimidinase, allantoinase, and ... |
49-425 |
2.58e-84 |
|
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: 262.33 E-value: 2.58e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445929010 49 LIVSPGMVDAHTHISEPGRT-HWEGYETGTRAAAKGGITTMIEMPLNQLPATVDREtIELKFDAAKGKLTIDAAQLGGLV 127
Cdd:cd01302 1 LLVLPGFIDIHVHLRDPGGTtYKEDFESGSRAAAAGGVTTVIDMPNTGPPPIDLPA-IELKIKLAEESSYVDFSFHAGIG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445929010 128 S-YNLDRLHELDEVGVVGFKCFVATCGdrgidNDFRDVNDWQFYKGAQKLGEMDQTVLVHCEnalicdelgeeakregrv 206
Cdd:cd01302 80 PgDVTDELKKLFDAGINSLKVFMNYYF-----GELFDVDDGTLMRTFLEIASRGGPVMVHAE------------------ 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445929010 207 tahdyvasrpvfteveairRVLYLAKAAGCRLHVCHISSPEGVEEVTRARQEGQDVTCESCPHYFVLDTDQFEEIGTLAK 286
Cdd:cd01302 137 -------------------RAAQLAEEAGANVHIAHVSSGEALELIKFAKNKGVKVTCEVCPHHLFLDESMLRLNGAWGK 197
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445929010 287 CSPPIRDQENQKGMWEKLFNGEIDCLVSDHSPCPPEMK--AGNIMQAWGGIAGLQNCMDVMFdEAVQKRGMSLPMFGKLM 364
Cdd:cd01302 198 VNPPLRSKEDREALWEGVKNGKIDTIASDHAPHSKEEKesGKDIWKAPPGFPGLETRLPILL-TEGVKRGLSLETLVEIL 276
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 445929010 365 ATNAADIFGLKHKGRIAPGKDADLVFIQPDSSYVLKNEDLEYRHKVSPYVGRTIGARITKT 425
Cdd:cd01302 277 SENPARIFGLYPKGTIAVGYDADLVIVDPKKEWKVTAEEIESKADWTPFEGMEVTGKPVST 337
|
|
| PRK09060 |
PRK09060 |
dihydroorotase; Validated |
1-432 |
1.21e-80 |
|
dihydroorotase; Validated
Pssm-ID: 181632 [Multi-domain] Cd Length: 444 Bit Score: 256.39 E-value: 1.21e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445929010 1 MSFDLIIKNGTVILENEARVIDIAVQGGKIAAIGENLG-EAKNVLDATGLIVSPGMVDAHTHISEPGRTHWEGYETGTRA 79
Cdd:PRK09060 3 QTFDLILKGGTVVNPDGEGRADIGIRDGRIAAIGDLSGaSAGEVIDCRGLHVLPGVIDSQVHFREPGLEHKEDLETGSRA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445929010 80 AAKGGITTMIEMPlNQLPATVDRETIELKFDAAKGKLTIDAAQLGGLVSYNLDRLHELDEV-GVVGFKCFV-ATCGDRGI 157
Cdd:PRK09060 83 AVLGGVTAVFEMP-NTNPLTTTAEALADKLARARHRMHCDFAFYVGGTRDNADELAELERLpGCAGIKVFMgSSTGDLLV 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445929010 158 DND--FRDVndwqfykgaqkLGEMDQTVLVHCEnalicDELGEEAKREGRVTAHdyVASRPVFTEVE----AIRRVLYLA 231
Cdd:PRK09060 162 EDDegLRRI-----------LRNGRRRAAFHSE-----DEYRLRERKGLRVEGD--PSSHPVWRDEEaallATRRLVRLA 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445929010 232 KAAGCRLHVCHISSPEGVEEVTRARqegqDV-TCESCPHYFVLD-TDQFEEIGTLAKCSPPIRDQENQKGMWEKLFNGEI 309
Cdd:PRK09060 224 RETGRRIHVLHVSTAEEIDFLADHK----DVaTVEVTPHHLTLAaPECYERLGTLAQMNPPIRDARHRDGLWRGVRQGVV 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445929010 310 DCLVSDHSPCPPEMKAGNIMQAWGGIAGLQNCMDVMFDEAVQKRgMSLPMFGKLMATNAADIFGLKHKGRIAPGKDADLV 389
Cdd:PRK09060 300 DVLGSDHAPHTLEEKAKPYPASPSGMTGVQTLVPIMLDHVNAGR-LSLERFVDLTSAGPARIFGIAGKGRIAVGYDADFT 378
|
410 420 430 440
....*....|....*....|....*....|....*....|...
gi 445929010 390 FIQPDSSYVLKNEDLEYRHKVSPYVGRTIGARITKTILRGDVI 432
Cdd:PRK09060 379 IVDLKRRETITNEWIASRCGWTPYDGKEVTGWPVGTIVRGQRV 421
|
|
| PRK13404 |
PRK13404 |
dihydropyrimidinase; Provisional |
1-448 |
1.41e-80 |
|
dihydropyrimidinase; Provisional
Pssm-ID: 184033 [Multi-domain] Cd Length: 477 Bit Score: 257.32 E-value: 1.41e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445929010 1 MSFDLIIKNGTVILENEARVIDIAVQGGKIAAIGENLGEAKNVLDATGLIVSPGMVDAHTHISEP---GRTHWEGYETGT 77
Cdd:PRK13404 2 MAFDLVIRGGTVVTATDTFQADIGIRGGRIAALGEGLGPGAREIDATGRLVLPGGVDSHCHIDQPsgdGIMMADDFYTGT 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445929010 78 RAAAKGGITTMIEMPLNQLPATVdRETIELKFDAAKGKLTIDaaqlgglVSYNL-----------DRLHELDEVGVVGFK 146
Cdd:PRK13404 82 VSAAFGGTTTVIPFAAQHRGQSL-REAVEDYHRRAAGKAVID-------YAFHLivadpteevltEELPALIAQGYTSFK 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445929010 147 CFVA----TCGDRGIdNDFRDVndwqfykgAQKLGEMdqtVLVHCENALICDELGEEAKREGRVTAHDYVASRPVFTEVE 222
Cdd:PRK13404 154 VFMTyddlKLDDRQI-LDVLAV--------ARRHGAM---VMVHAENHDMIAWLTKRLLAAGLTAPKYHAISRPMLAERE 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445929010 223 AIRRVLYLAKAAGCRLHVCHISSPEGVEEVTRARQEGQDVTCESCPHYFV-----LDTDQFEeiGTLAKCSPPIRDQENQ 297
Cdd:PRK13404 222 ATHRAIALAELVDVPILIVHVSGREAAEQIRRARGRGLKIFAETCPQYLFltaedLDRPGME--GAKYICSPPPRDKANQ 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445929010 298 KGMWEKLFNGEIDCLVSDHSPCPPEMKAG--------NIMQAWGGIAGLQNCMDVMFDEAVQKRGMSLPMFGKLMATNAA 369
Cdd:PRK13404 300 EAIWNGLADGTFEVFSSDHAPFRFDDTDGklaaganpSFKAIANGIPGIETRLPLLFSEGVVKGRISLNRFVALTSTNPA 379
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445929010 370 DIFGLK-HKGRIAPGKDADLVFIQPDSSYVLKNEDLEYRHKVSPYVGRTIGARITKTILRGDVIYDIEHGFPVPPKGQFI 448
Cdd:PRK13404 380 KLYGLYpRKGAIAIGADADIAIWDPDREVTITNADLHHAADYTPYEGMRVTGWPVTVLSRGRVVVEDGELVAERGSGQFL 459
|
|
| DHOase_IIa |
cd01317 |
Dihydroorotase (DHOase), subgroup IIa; DHOases catalyze the reversible interconversion of ... |
43-425 |
9.24e-77 |
|
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: 244.07 E-value: 9.24e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445929010 43 VLDATGLIVSPGMVDAHTHISEPGRTHWEGYETGTRAAAKGGITTMIEMPlNQLPATVDRETIELKFDAAKGKLTIDAAQ 122
Cdd:cd01317 4 VIDAEGKILAPGLVDLHVHLREPGFEYKETLESGAKAAAAGGFTTVVCMP-NTNPVIDNPAVVELLKNRAKDVGIVRVLP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445929010 123 LGGLVSYN----LDRLHELDEVGVVGFKcfvatcgdrgidNDFRDVNDWQ-FYKGAQKLGEMDQTVLVHCENALICDEL- 196
Cdd:cd01317 83 IGALTKGLkgeeLTEIGELLEAGAVGFS------------DDGKPIQDAElLRRALEYAAMLDLPIIVHPEDPSLAGGGv 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445929010 197 ---GEEAKREGrvtahdyVASRPVFTEVEAIRRVLYLAKAAGCRLHVCHISSPEGVEEVTRARQEGQDVTCESCPHYFVL 273
Cdd:cd01317 151 mneGKVASRLG-------LPGIPPEAETIMVARDLELAEATGARVHFQHLSTARSLELIRKAKAKGLPVTAEVTPHHLLL 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445929010 274 DTDQFEEIGTLAKCSPPIRDQENQKGMWEKLFNGEIDCLVSDHSPCPPEMKAGNIMQAWGGIAGLQNCMDVMFDEAVQKR 353
Cdd:cd01317 224 DDEALESYDTNAKVNPPLRSEEDREALIEALKDGTIDAIASDHAPHTDEEKDLPFAEAPPGIIGLETALPLLWTLLVKGG 303
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 445929010 354 GMSLPMFGKLMATNAADIFGLKhKGRIAPGKDADLVFIQPDSSYVLKNEDLEYRHKVSPYVGRTIGARITKT 425
Cdd:cd01317 304 LLTLPDLIRALSTNPAKILGLP-PGRLEVGAPADLVLFDPDAEWIVDEETFRSKSKNTPFDGQKLKGRVLAT 374
|
|
| PRK07575 |
PRK07575 |
dihydroorotase; Provisional |
1-434 |
4.13e-75 |
|
dihydroorotase; Provisional
Pssm-ID: 236055 [Multi-domain] Cd Length: 438 Bit Score: 241.89 E-value: 4.13e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445929010 1 MSFDLIIKNGTVILEN-EARVIDIAVQGGKIAAIGENLG--EAKNVLDATGLIVSPGMVDAHTHISEPGRTHWEGYETGT 77
Cdd:PRK07575 1 MMMSLLIRNARILLPSgELLLGDVLVEDGKIVAIAPEISatAVDTVIDAEGLTLLPGVIDPQVHFREPGLEHKEDLFTAS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445929010 78 RAAAKGGITTMIEMPlNQLPATVDRETIELKFDAAKGKLTIDAAQLGGLVSYNLDRLHELDevGVVGFKCFV-ATCGDRG 156
Cdd:PRK07575 81 RACAKGGVTSFLEMP-NTKPLTTTQAALDDKLARAAEKCVVNYGFFIGATPDNLPELLTAN--PTCGIKIFMgSSHGPLL 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445929010 157 IDNDfrDVNDWQFYKGaqklgemDQTVLVHCEnalicDELGEEAKRE---GRVTAHDYVASRPVFTEVEAIRRVLYLAKA 233
Cdd:PRK07575 158 VDEE--AALERIFAEG-------TRLIAVHAE-----DQARIRARRAefaGISDPADHSQIQDEEAALLATRLALKLSKK 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445929010 234 AGCRLHVCHISSpeGVEEVTRARQEGQDVTCESCPHYFVLDTDQFEEIGTLAKCSPPIRDQENQKGMWEKLFNGEIDCLV 313
Cdd:PRK07575 224 YQRRLHILHLST--AIEAELLRQDKPSWVTAEVTPQHLLLNTDAYERIGTLAQMNPPLRSPEDNEALWQALRDGVIDFIA 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445929010 314 SDHSPCPPEMKAGNIMQAWGGIAGLQNCMDVMFDEAVQKRgMSLPMFGKLMATNAADIFGLKHKGRIAPGKDADLVFIQP 393
Cdd:PRK07575 302 TDHAPHTLEEKAQPYPNSPSGMPGVETSLPLMLTAAMRGK-CTVAQVVRWMSTAVARAYGIPNKGRIAPGYDADLVLVDL 380
|
410 420 430 440
....*....|....*....|....*....|....*....|.
gi 445929010 394 DSSYVLKNEDLEYRHKVSPYVGRTIGARITKTILRGDVIYD 434
Cdd:PRK07575 381 NTYRPVRREELLTKCGWSPFEGWNLTGWPVTTIVGGQIVFD 421
|
|
| PRK09236 |
PRK09236 |
dihydroorotase; Reviewed |
1-434 |
6.23e-65 |
|
dihydroorotase; Reviewed
Pssm-ID: 181716 Cd Length: 444 Bit Score: 215.50 E-value: 6.23e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445929010 1 MSfDLIIKNGTVILENEARVIDIAVQGGKIAAIGENLG--EAKNVLDATGLIVSPGMVDAHTHISEPGRTHWEGYETGTR 78
Cdd:PRK09236 1 MK-RILIKNARIVNEGKIFEGDVLIENGRIAKIASSISakSADTVIDAAGRYLLPGMIDDQVHFREPGLTHKGDIASESR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445929010 79 AAAKGGITTMIEMPlNQLPATVDRETIELKFDAAKGKLTIDAAQLGGLVSYNLDRLHELDEVGVVGFKCFV-ATCGDRGI 157
Cdd:PRK09236 80 AAVAGGITSFMEMP-NTNPPTTTLEALEAKYQIAAQRSLANYSFYFGATNDNLDEIKRLDPKRVCGVKVFMgASTGNMLV 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445929010 158 DND------FRDVndwqfykgaqklgemDQTVLVHCENALICDELGEEAKRE-GR-VTAHDYvasrPVFTEVEAI----R 225
Cdd:PRK09236 159 DNPetleriFRDA---------------PTLIATHCEDTPTIKANLAKYKEKyGDdIPAEMH----PLIRSAEACykssS 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445929010 226 RVLYLAKAAGCRLHVCHISSPEGVEEVTRARQEGQDVTCESCPHYFVLDTDQFEEIGTLAKCSPPIRDQENQKGMWEKLF 305
Cdd:PRK09236 220 LAVSLAKKHGTRLHVLHISTAKELSLFENGPLAEKRITAEVCVHHLWFDDSDYARLGNLIKCNPAIKTASDREALRQALA 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445929010 306 NGEIDCLVSDHSPCPPEMKAGNIMQAWGGIAGLQNCMDVMFdEAVQKRGMSLPMFGKLMATNAADIFGLKHKGRIAPGKD 385
Cdd:PRK09236 300 DDRIDVIATDHAPHTWEEKQGPYFQAPSGLPLVQHALPALL-ELVHEGKLSLEKVVEKTSHAPAILFDIKERGFIREGYW 378
|
410 420 430 440
....*....|....*....|....*....|....*....|....*....
gi 445929010 386 ADLVFIQPDSSYVLKNEDLEYRHKVSPYVGRTIGARITKTILRGDVIYD 434
Cdd:PRK09236 379 ADLVLVDLNSPWTVTKENILYKCGWSPFEGRTFRSRVATTFVNGQLVYH 427
|
|
| PRK04250 |
PRK04250 |
dihydroorotase; Provisional |
10-432 |
8.41e-55 |
|
dihydroorotase; Provisional
Pssm-ID: 235265 [Multi-domain] Cd Length: 398 Bit Score: 187.67 E-value: 8.41e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445929010 10 GTVILENeaRVID--IAVQGGKIAAIGENLGEAKNVLDATGLIVSPGMVDAHTHISEPGRTHWEGYETGTRAAAKGGITT 87
Cdd:PRK04250 4 GKFLLKG--RIVEggIGIENGRISKISLRDLKGKEVIKVKGGIILPGLIDVHVHLRDFEESYKETIESGTKAALHGGITL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445929010 88 MIEMPlNQLPATVDRETIELKFDAAKGKLTIDAAqLGGLVSYNLDrlhELDEVGVVGFKCF-VATCGDRGIDNDFRDvnd 166
Cdd:PRK04250 82 VFDMP-NTKPPIMDEKTYEKRMRIAEKKSYADYA-LNFLIAGNCE---KAEEIKADFYKIFmGASTGGIFSENFEVD--- 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445929010 167 wqfYKGAQKLgemdqtVLVHCENALICDELGEeakregrvtahdyvasRPVFTEVEAIRRVLYLAKAAGCRLHVCHISSP 246
Cdd:PRK04250 154 ---YACAPGI------VSVHAEDPELIREFPE----------------RPPEAEVVAIERALEAGKKLKKPLHICHISTK 208
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445929010 247 EGVEEVTRARQEGqdVTCESCPHYFVLDTDQFEEiGTLAKCSPPIRDQENQKGMWEKLFNgeIDCLVSDHSPCPPEMK-A 325
Cdd:PRK04250 209 DGLKLILKSNLPW--VSFEVTPHHLFLTRKDYER-NPLLKVYPPLRSEEDRKALWENFSK--IPIIASDHAPHTLEDKeA 283
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445929010 326 GNimqawGGIAGLQNCMDVMFDEAvqKRGM-SLPMFGKLMATNAADIFGLKHKGrIAPGKDADLVFIQPDSSYVLKNEDL 404
Cdd:PRK04250 284 GA-----AGIPGLETEVPLLLDAA--NKGMiSLFDIVEKMHDNPARIFGIKNYG-IEEGNYANFAVFDMKKEWTIKAEEL 355
|
410 420
....*....|....*....|....*...
gi 445929010 405 EYRHKVSPYVGRTIGARITKTILRGDVI 432
Cdd:PRK04250 356 YTKAGWTPYEGFKLKGKVIMTILRGEVV 383
|
|
| PLN02942 |
PLN02942 |
dihydropyrimidinase |
2-448 |
3.06e-52 |
|
dihydropyrimidinase
Pssm-ID: 178530 Cd Length: 486 Bit Score: 183.12 E-value: 3.06e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445929010 2 SFDLIIKNGTVILENEARVIDIAVQGGKIAAIGENL--GEAKNVLDATGLIVSPGMVDAHTHISEP--GRTHWEGYETGT 77
Cdd:PLN02942 4 STKILIKGGTVVNAHHQELADVYVEDGIIVAVAPNLkvPDDVRVIDATGKFVMPGGIDPHTHLAMPfmGTETIDDFFSGQ 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445929010 78 RAAAKGGITTMIE--MPLNQlpatvdreTIELKFDAAKGKLTIDAAQLG---------GLVSYNLDRLheLDEVGVVGFK 146
Cdd:PLN02942 84 AAALAGGTTMHIDfvIPVNG--------NLLAGYEAYEKKAEKSCMDYGfhmaitkwdDTVSRDMETL--VKEKGINSFK 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445929010 147 CFVATCGDRGidndfrdVNDWQFYKGAQKLGEMDQTVLVHCENALICDELGEEAKREGRVTAHDYVASRPVFTEVEAIRR 226
Cdd:PLN02942 154 FFMAYKGSLM-------VTDELLLEGFKRCKSLGALAMVHAENGDAVFEGQKRMIELGITGPEGHALSRPPLLEGEATAR 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445929010 227 VLYLAKAAGCRLHVCHISSPEGVEEVTRARQEGQDVTCESCPHYFVLDTDQF--EEIGTLAK--CSPPIRDQENQKGMWE 302
Cdd:PLN02942 227 AIRLAKFVNTPLYVVHVMSIDAMEEIARARKSGQRVIGEPVVSGLVLDDSKLwdPDFTIASKyvMSPPIRPAGHGKALQA 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445929010 303 KLFNGEIDCLVSDHSPCPPEMKA---GNIMQAWGGIAGLQNCMDVMFDEAVQKRGMSLPMFGKLMATNAADIFGL-KHKG 378
Cdd:PLN02942 307 ALSSGILQLVGTDHCPFNSTQKAfgkDDFRKIPNGVNGIEERMHLVWDTMVESGQISPTDYVRVTSTECAKIFNIyPRKG 386
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445929010 379 RIAPGKDADLVFIQPDSSYVLKNEDLEYRHKVSPYVGRTIGARITKTILRGDVIYDIEHGFPVPPKGQFI 448
Cdd:PLN02942 387 AILAGSDADIIILNPNSTFTISAKTHHSRIDTNVYEGRRGKGKVEVTISQGRVVWENGELKVVRGSGRYI 456
|
|
| PRK07627 |
PRK07627 |
dihydroorotase; Provisional |
7-434 |
6.21e-47 |
|
dihydroorotase; Provisional
Pssm-ID: 181059 [Multi-domain] Cd Length: 425 Bit Score: 167.16 E-value: 6.21e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445929010 7 IKNGTVI--LENEARVIDIAVQGGKIAAIGENLG--EAKNVLDATGLIVSPGMVDAHTHISEPGRTHWEGYETGTRAAAK 82
Cdd:PRK07627 5 IKGGRLIdpAAGTDRQADLYVAAGKIAAIGQAPAgfNADKTIDASGLIVCPGLVDLSARLREPGYEYKATLESEMAAAVA 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445929010 83 GGITTMI-----EMPLNQlPATVDRetieLKFDAAK---------GKLTIdaaqlgGLVSYNLDRLHELDEVGVVGFkcf 148
Cdd:PRK07627 85 GGVTSLVcppdtDPVLDE-PGLVEM----LKFRARNlnqahvyplGALTV------GLKGEVLTEMVELTEAGCVGF--- 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445929010 149 vaTCGDRGIdndfrdVNDWQFYKGAQKLGEMDQTVLVHCENALICDelgeeakreGRVTAHDYVASR------PVFTEVE 222
Cdd:PRK07627 151 --SQANVPV------VDTQVLLRALQYASTFGFTVWLRPLDAFLGR---------GGVAASGAVASRlglsgvPVAAETI 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445929010 223 AIRRVLYLAKAAGCRLHVCHISSPEGVEEVTRARQEGQDVTCE-SCPHYFVLDTDqfeeIGTL-AKC--SPPIRDQENQK 298
Cdd:PRK07627 214 ALHTIFELMRVTGARVHLARLSSAAGVALVRAAKAEGLPVTCDvGVNHVHLIDVD----IGYFdSQFrlDPPLRSQRDRE 289
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445929010 299 GMWEKLFNGEIDCLVSDHSPCPPEMKAGNIMQAWGGIAGLQNCMDVMFDEAvQKRGMSLPMFGKLMATNAADIFGLKhKG 378
Cdd:PRK07627 290 AIRAALADGTIDAICSDHTPVDDDEKLLPFAEATPGATGLELLLPLTLKWA-DEAKVPLARALARITSAPARVLGLP-AG 367
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*.
gi 445929010 379 RIAPGKDADLVFIQPDSSYVLKNEDLEYRHKVSPYVGRTIGARITKTILRGDVIYD 434
Cdd:PRK07627 368 RLAEGAPADLCVFDPDAHWRVEPRALKSQGKNTPFLGYELPGRVRATLVAGQVAFE 423
|
|
| PRK09059 |
PRK09059 |
dihydroorotase; Validated |
12-433 |
1.75e-43 |
|
dihydroorotase; Validated
Pssm-ID: 181631 [Multi-domain] Cd Length: 429 Bit Score: 157.89 E-value: 1.75e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445929010 12 VILENeARVID----------IAVQGGKIAAIGENLG-----EAKNVLDATGLIVSPGMVDAHTHISEPGRTHWEGYETG 76
Cdd:PRK09059 5 ILLAN-ARIIDpsrgldeigtVLIEDGVIVAAGKGAGnqgapEGAEIVDCAGKAVAPGLVDARVFVGEPGAEHRETIASA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445929010 77 TRAAAKGGITTMIEMPlNQLPATVDRETIELKFDAAKGKLTID----AAQLGGLVSYNLDRLHELDEVGVVGFkcfvaTC 152
Cdd:PRK09059 84 SRAAAAGGVTSIIMMP-DTDPVIDDVALVEFVKRTARDTAIVNihpaAAITKGLAGEEMTEFGLLRAAGAVAF-----TD 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445929010 153 GDRGIDNDfrdvndwQFYKGAQKLG-EMDQTVLVHCENAlicDELGEEAKREGRVTAHDYVASRPVFTEVEAIRRVLYLA 231
Cdd:PRK09059 158 GRRSVANT-------QVMRRALTYArDFDAVIVHETRDP---DLGGNGVMNEGLFASWLGLSGIPREAEVIPLERDLRLA 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445929010 232 KAAGCRLHVCHISSPEGVEEVTRARQEGQDVTCESCPHYFVLDTDQFEEIGTLAKCSPPIRDQENQKGMWEKLFNGEIDC 311
Cdd:PRK09059 228 ALTRGRYHAAQISCAESAEALRRAKDRGLKVTAGVSINHLSLNENDIGEYRTFFKLSPPLRTEDDRVAMVEAVASGTIDI 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445929010 312 LVSDHSPCPPEMKAGNIMQAWGGIAGLQNcmdvMFDEA---VQKRGMSLPMFGKLMATNAADIFGLKhKGRIAPGKDADL 388
Cdd:PRK09059 308 IVSSHDPQDVDTKRLPFSEAAAGAIGLET----LLAAAlrlYHNGEVPLLRLIEALSTRPAEIFGLP-AGTLKPGAPADI 382
|
410 420 430 440
....*....|....*....|....*....|....*....|....*
gi 445929010 389 VFIQPDSSYVLKNEDLEYRHKVSPYVGRTIGARITKTILRGDVIY 433
Cdd:PRK09059 383 IVIDLDEPWVVDPEDLKSRSKNTPFEEARFQGRVVRTIVAGKTVY 427
|
|
| PRK01211 |
PRK01211 |
dihydroorotase; Provisional |
21-453 |
1.12e-41 |
|
dihydroorotase; Provisional
Pssm-ID: 179247 [Multi-domain] Cd Length: 409 Bit Score: 152.70 E-value: 1.12e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445929010 21 IDIAVQGGKIAAIGENLGEAKNVlDATGLIVsPGMVDAHTHISEPGRTHWEGYETGTRAAAKGGITTMIEMPLNQLPATv 100
Cdd:PRK01211 16 LEIEVEDGKIKSIKKDAGNIGKK-ELKGAIL-PAATDIHVHFRTPGETEKEDFSTGTLSAIFGGTTFIMDMPNNNIPIK- 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445929010 101 DRETIELKFDAAKGKLTIDAaqlgGLVSYNLDRLHE-LDEVGvVGFKCFVA-TCGDRGIDNDFRDVndwqfykgaQKLGE 178
Cdd:PRK01211 93 DYNAFSDKLGRVAPKAYVDF----SLYSMETGNNALiLDERS-IGLKVYMGgTTNTNGTDIEGGEI---------KKINE 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445929010 179 MDQTVLVHCENALICDELGEEAKregrvTAHDYVASRPVFTEVEAIRRVLYLAKAAGcrlHVCHISSPEGVEEVTRarqe 258
Cdd:PRK01211 159 ANIPVFFHAELSECLRKHQFESK-----NLRDHDLARPIECEIKAVKYVKNLDLKTK---IIAHVSSIDVIGRFLR---- 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445929010 259 gqdvtcESCPHYFVLDTDQfeEIGTLAKCSPPIRDQENQKGMWEKLFNGEIDCLVSDHSPCPPEMKAgNIMQAWGGIAGL 338
Cdd:PRK01211 227 ------EVTPHHLLLNDDM--PLGSYGKVNPPLRDRWTQERLLEEYISGRFDILSSDHAPHTEEDKQ-EFEYAKSGIIGV 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445929010 339 QNCMDVMFdEAVQKRGMSLPMFGKLMATNAADIFGLKhKGRIAPGKDADLVFIQPDSSYVLKNEDLEYRHKVSPYVGrtI 418
Cdd:PRK01211 298 ETRVPLFL-ALVKKKILPLDVLYKTAIERPASLFGIK-KGKIEEGYDADFMAFDFTNIKKINDKRLHSKCPVSPFNG--F 373
|
410 420 430
....*....|....*....|....*....|....*.
gi 445929010 419 GARITKT-ILRGDVIYDiEHGFPVPPKGQFILKHQQ 453
Cdd:PRK01211 374 DAIFPSHvIMRGEVVID-NYELISERTGKFVPKGGE 408
|
|
| pyrC |
PRK00369 |
dihydroorotase; Provisional |
4-441 |
7.65e-34 |
|
dihydroorotase; Provisional
Pssm-ID: 234738 [Multi-domain] Cd Length: 392 Bit Score: 131.04 E-value: 7.65e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445929010 4 DLIIKnGTVILENEARVIdiavQGGKIAAIGENLGEAKNVLDAT-GLIVSPGMVDAHTHISEPGRTHWEGYETGTRAAAK 82
Cdd:PRK00369 2 ILWIK-GKAYLGKEIKEI----CINFDRRIKEIKSRCKPDLDLPqGTLILPGAIDLHVHLRGLKLSYKEDVASGTSEAAY 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445929010 83 GGITTMIEMPlNQLPATVDRETIELKFDAAKGKLTIDAAQLGGLVsynlDRLHELDEVGVVGFKCFVatcgdrgidndfR 162
Cdd:PRK00369 77 GGVTLVADMP-NTIPPLNTPEAITEKLAELEYYSRVDYFVYSGVT----KDPEKVDKLPIAGYKIFP------------E 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445929010 163 DVNDWQFYKgaqKLGEMDQTVLVHCENALicdelgeeAKREGRVTAhdyvasRPVFTEVEAirrvLYLAKAAGcRLHVCH 242
Cdd:PRK00369 140 DLEREETFR---VLLKSRKLKILHPEVPL--------ALKSNRKLR------RNCWYEIAA----LYYVKDYQ-NVHITH 197
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445929010 243 ISSPEGVEEvtrARQEG--QDVTcescPHYFVLDTdqfeEIGTLAKCSPPIRDQENQKGMWEKLFngEIDCLVSDHSPCP 320
Cdd:PRK00369 198 ASNPRTVRL---AKELGftVDIT----PHHLLVNG----EKDCLTKVNPPIRDINERLWLLQALS--EVDAIASDHAPHS 264
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445929010 321 PEMKAGNIMQAWGGIAGLQncMDVMFDEAVQKRG-MSLPMFGKLMATNAADIFGLKHkGRIAPGKDADLVfiqpdssyVL 399
Cdd:PRK00369 265 SFEKLQPYEVCPPGIAALS--FTPPFIYTLVSKGiLSIDRAVELISTNPARILGIPY-GEIKEGYRANFT--------VI 333
|
410 420 430 440
....*....|....*....|....*....|....*....|....*..
gi 445929010 400 KNEDLEYRHKVS-----PYVGRTIGARITKTILRGDVIYDIEHGFPV 441
Cdd:PRK00369 334 QFEDWRYSTKYSkvietPLDGFELKASVYATIVQGKLAYLEGEVFPV 380
|
|
| PRK08417 |
PRK08417 |
metal-dependent hydrolase; |
23-433 |
2.97e-32 |
|
metal-dependent hydrolase;
Pssm-ID: 236262 [Multi-domain] Cd Length: 386 Bit Score: 126.36 E-value: 2.97e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445929010 23 IAVQGGKIAAIGENLgEAKNVLDATGLIVSPGMVD--AHTHISEPGRTHWEGYETgtrAAAKGGITTMIEMPlNQLPATV 100
Cdd:PRK08417 1 IRIKDGKITEIGSDL-KGEEILDAKGKTLLPALVDlnVSLKNDSLSSKNLKSLEN---ECLKGGVGSIVLYP-DSTPAID 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445929010 101 DRETIELkfdaakgkltiDAAQLGGLVSYNLDRLHELDEVGVVGFKCFVATCGDRGIDNDfRDVNDWQFYKGAQKLGEMD 180
Cdd:PRK08417 76 NEIALEL-----------INSAQRELPMQIFPSIRALDEDGKLSNIATLLKKGAKALELS-SDLDANLLKVIAQYAKMLD 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445929010 181 QTVLVHCENALICDElgeEAKREGRVTAHDYVASRPVFTEVEAIRRVLYLAKAAGCRLHVCHISSPEGVEEVTRARQEGQ 260
Cdd:PRK08417 144 VPIFCRCEDSSFDDS---GVMNDGELSFELGLPGIPSIAETKEVAKMKELAKFYKNKVLFDTLALPRSLELLDKFKSEGE 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445929010 261 DVTCESCPHYFVLDTDQFEEIGTLAKCSPPIRDQENQKGMWEKLFNGEIDCLVSDHSPCPPEMKAGNIMQAWGGIAGLQN 340
Cdd:PRK08417 221 KLLKEVSIHHLILDDSACENFNTAAKLNPPLRSKEDRLALLEALKEGKIDFLTSLHSAKSNSKKDLAFDEAAFGIDSICE 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445929010 341 CMDVMFDEAVQKRGMSLPMFGKLMATNAADIFGLKhKGRIAPGKDADLVFIQPDSSYVLKNedleyrhKVSPYVGRTIGA 420
Cdd:PRK08417 301 YFSLCYTYLVKEGIITWSELSRFTSYNPAQFLGLN-SGEIEVGKEADLVLFDPNESTIIDD-------NFSLYSGDELYG 372
|
410
....*....|...
gi 445929010 421 RITKTILRGDVIY 433
Cdd:PRK08417 373 KIEAVIIKGKLYL 385
|
|
| CAD_DHOase |
cd01316 |
The eukaryotic CAD protein is a trifunctional enzyme of carbamoylphosphate ... |
49-445 |
5.12e-27 |
|
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: 111.00 E-value: 5.12e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445929010 49 LIVSPGMVDAHTHISEPGRTHWEGYETGTRAAAKGGITTMIEMPlNQLPATVDRETIELKFDAAKGKLTIDAAQLGGLVS 128
Cdd:cd01316 2 TIRLPGLIDVHVHLREPGATHKEDFASGTKAALAGGFTMVRAMP-NTNPSIVDVASLKLVQSLAQAKARCDYAFSIGATS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445929010 129 YNLdrlHELDEVG--VVGFKCFVATCGDRGIDNDfrdVNDWQFYKGAqklgemdqtvlvhcenalicdelgeeakregrv 206
Cdd:cd01316 81 TNA---ATVGELAseAVGLKFYLNETFSTLILDK---ITAWASHFNA--------------------------------- 121
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445929010 207 tahdYVASRPVFTEVEA--IRRVLYLAKAAGCRLHVCHISSPEGVEEVTRARQEGQDVTCESCPHYFVLDTDQFEEigTL 284
Cdd:cd01316 122 ----WPSTKPIVTHAKSqtLAAVLLLASLHNRSIHICHVSSKEEINLIRLAKARGLKVTCEVSPHHLFLSQDDLPR--GQ 195
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445929010 285 AKCSPPIRDQENQKGMWEKLfnGEIDCLVSDHSPCPPEMKAGNIMQAwgGIAGLQNCMDVMFdEAVQKRGMSLPMFGKLM 364
Cdd:cd01316 196 YEVRPFLPTREDQEALWENL--DYIDCFATDHAPHTLAEKTGNKPPP--GFPGVETSLPLLL-TAVHEGRLTIEDIVDRL 270
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445929010 365 ATNAADIFGLkhkgriaPGKDADLVFIQPDSSYVLKNEDLEYRHKVSPYVGRTIGARITKTILRGDVIY-DIEHGFPvPP 443
Cdd:cd01316 271 HTNPKRIFNL-------PPQSDTYVEVDLDEEWTIPKNPLQSKKGWTPFEGKKVKGKVQRVVLRGETAFiDGEIVAP-PG 342
|
..
gi 445929010 444 KG 445
Cdd:cd01316 343 FG 344
|
|
| D-aminoacylase |
cd01297 |
D-aminoacylases (N-acyl-D-Amino acid amidohydrolases) catalyze the hydrolysis of ... |
4-394 |
5.63e-26 |
|
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: 109.31 E-value: 5.63e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445929010 4 DLIIKNGTVI--LENEARVIDIAVQGGKIAAIGENLG-EAKNVLDATGLIVSPGMVDAHTHisEPGRTHWEGyetGTRAA 80
Cdd:cd01297 1 DLVIRNGTVVdgTGAPPFTADVGIRDGRIAAIGPILStSAREVIDAAGLVVAPGFIDVHTH--YDGQVFWDP---DLRPS 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445929010 81 AKGGITTMIEMPLNQLPATVDRETIELKFDAAKGkltIDAAQLGGLVSYN-----LDRL----HELDEVGVVGFKCF-VA 150
Cdd:cd01297 76 SRQGVTTVVLGNCGVSPAPANPDDLARLIMLMEG---LVALGEGLPWGWAtfaeyLDALearpPAVNVAALVGHAALrRA 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445929010 151 TCGDRG----------IDNDFRDVNDwqfyKGAqkLGEMDQTVLVHCENA----LIcdELGEEAKREGRV--TAHDYVAS 214
Cdd:cd01297 153 VMGLDAreateeelakMRELLREALE----AGA--LGISTGLAYAPRLYAgtaeLV--ALARVAARYGGVyqTHVRYEGD 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445929010 215 RPvfteVEAIRRVLYLAKAAGCRLHVCHISS---------PEGVEEVTRARQEGQDVTCESCPHyfvldtdqfeEIGTLA 285
Cdd:cd01297 225 SI----LEALDELLRLGRETGRPVHISHLKSagapnwgkiDRLLALIEAARAEGLQVTADVYPY----------GAGSED 290
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445929010 286 KCSPPIRDQENqkgmweklfNGEIDCLVSDHSPCppemkagnimQAWGGIAglqncmDVMFDEAVQKRGMSLPMFGKLMA 365
Cdd:cd01297 291 DVRRIMAHPVV---------MGGSDGGALGKPHP----------RSYGDFT------RVLGHYVRERKLLSLEEAVRKMT 345
|
410 420
....*....|....*....|....*....
gi 445929010 366 TNAADIFGLKHKGRIAPGKDADLVFIQPD 394
Cdd:cd01297 346 GLPARVFGLADRGRIAPGYRADIVVFDPD 374
|
|
| PRK07369 |
PRK07369 |
dihydroorotase; Provisional |
19-425 |
5.95e-26 |
|
dihydroorotase; Provisional
Pssm-ID: 236002 [Multi-domain] Cd Length: 418 Bit Score: 109.31 E-value: 5.95e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445929010 19 RVIDIAVQGGKIAAIGENLGE---AKNVLDATGLIVSPGMVDAHTHISEPGRTHWEGYETGTRAAAKGGITTmiempLNQ 95
Cdd:PRK07369 20 RIADVLIEDGKIQAIEPHIDPippDTQIIDASGLILGPGLVDLYSHSGEPGFEERETLASLAAAAAAGGFTR-----VAI 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445929010 96 LPAT---VDRETIelkFDAAKGKL-TIDAAQLGGLVSYNLDR-------LHELDEVGVVGFkcfvatCGDRGIDNdfrdv 164
Cdd:PRK07369 95 LPDTfppLDNPAT---LARLQQQAqQIPPVQLHFWGALTLGGqgkqlteLAELAAAGVVGF------TDGQPLEN----- 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445929010 165 ndWQFYKGA-QKLGEMDQTVLVHCENALICdelGEEAKREGRVTAHDYVASRPVFTEVEAIRRVLYLAKAAGCRLHVCHI 243
Cdd:PRK07369 161 --LALLRRLlEYLKPLGKPVALWPCDRSLA---GNGVMREGLLALRLGLPGDPASAETTALAALLELVAAIGTPVHLMRI 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445929010 244 SSPEGVEEVTRARQEGQDVTCESCPHYFVLDTDQFEEIGTLAKCSPPIRDQENQKGMWEKLFNGEIDCLVSDHSPCPPEM 323
Cdd:PRK07369 236 STARSVELIAQAKARGLPITASTTWMHLLLDTEALASYDPNLRLDPPLGNPSDRQALIEGVRTGVIDAIAIDHAPYTYEE 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445929010 324 KAGNIMQAWGGIAGLQNCMDVMFDEAVQKRGMSLPMFGKLMATNAADIFGLKHKgRIAPGKDADLVFIQPDSSYVLKNED 403
Cdd:PRK07369 316 KTVAFAEAPPGAIGLELALPLLWQNLVETGELSALQLWQALSTNPARCLGQEPP-SLAPGQPAELILFDPQKTWTVSAQT 394
|
410 420
....*....|....*....|..
gi 445929010 404 LEYRHKVSPYVGRTIGARITKT 425
Cdd:PRK07369 395 LHSLSRNTPWLGQTLKGRVLQT 416
|
|
| PRK09061 |
PRK09061 |
D-glutamate deacylase; Validated |
2-269 |
1.80e-18 |
|
D-glutamate deacylase; Validated
Pssm-ID: 236369 [Multi-domain] Cd Length: 509 Bit Score: 87.83 E-value: 1.80e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445929010 2 SFDLIIKNGTVIlENEAR---VIDIAVQGGKIAAIGENLGEAKNVLDATGLIVSPGMVDAHTHISEPGrthwegyetGTR 78
Cdd:PRK09061 18 PYDLVIRNGRVV-DPETGldaVRDVGIKGGKIAAVGTAAIEGDRTIDATGLVVAPGFIDLHAHGQSVA---------AYR 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445929010 79 AAAKGGITTMIEMPLNQLP-----ATVDRETIELKFDAAKGKLTIDAAQLGGlvsynldrlheldevgvvgfkcfvatcg 153
Cdd:PRK09061 88 MQAFDGVTTALELEAGVLPvarwyAEQAGEGRPLNYGASVGWTPARIAVLTG---------------------------- 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445929010 154 dRGIDNDFRDVNDWQFYKGAQklgemdqtvlvhcENALICDELGEEAKR------EG------------RVTAHDYV--- 212
Cdd:PRK09061 140 -PQAEGTIADFGKALGDPRWQ-------------ERAATPAELAEILELleqgldEGalgigigagyapGTGHKEYLela 205
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445929010 213 --ASR---PVFTEV------------EAIRRVLYLAKAAGCRLHVCHISS------PEGVEEVTRARQEGQDVTCESCPH 269
Cdd:PRK09061 206 rlAARagvPTYTHVrylsnvdprssvDAYQELIAAAAETGAHMHICHVNStslrdiDRCLALVEKAQAQGLDVTTEAYPY 285
|
|
| COG3964 |
COG3964 |
Predicted amidohydrolase [General function prediction only]; |
4-89 |
2.06e-18 |
|
Predicted amidohydrolase [General function prediction only];
Pssm-ID: 443164 [Multi-domain] Cd Length: 376 Bit Score: 86.37 E-value: 2.06e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445929010 4 DLIIKNGTVILE--NEARVIDIAVQGGKIAAIGENL--GEAKNVLDATGLIVSPGMVDAHTHIsepgrthwegYETGTR- 78
Cdd:COG3964 1 DLLIKGGRVIDPanGIDGVMDIAIKDGKIAAVAKDIdaAEAKKVIDASGLYVTPGLIDLHTHV----------FPGGTDy 70
|
90
....*....|....*..
gi 445929010 79 ------AAAKGGITTMI 89
Cdd:COG3964 71 gvdpdgVGVRSGVTTVV 87
|
|
| PRK09237 |
PRK09237 |
amidohydrolase/deacetylase family metallohydrolase; |
5-89 |
5.65e-16 |
|
amidohydrolase/deacetylase family metallohydrolase;
Pssm-ID: 236423 [Multi-domain] Cd Length: 380 Bit Score: 79.12 E-value: 5.65e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445929010 5 LIIKNGTVI--LENEARVIDIAVQGGKIAAIGENL--GEAKNVLDATGLIVSPGMVDAHTHISePGRTHWeGYETgTRAA 80
Cdd:PRK09237 1 LLLRGGRVIdpANGIDGVIDIAIEDGKIAAVAGDIdgSQAKKVIDLSGLYVSPGWIDLHVHVY-PGSTPY-GDEP-DEVG 77
|
....*....
gi 445929010 81 AKGGITTMI 89
Cdd:PRK09237 78 VRSGVTTVV 86
|
|
| ATZ_TRZ_like |
cd01298 |
TRZ/ATZ family contains enzymes from the atrazine degradation pathway and related hydrolases. ... |
5-433 |
7.64e-16 |
|
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: 79.17 E-value: 7.64e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445929010 5 LIIKNGTVILENEARVI---DIAVQGGKIAAIGENL----GEAKNVLDATGLIVSPGMVDAHTHISE------------- 64
Cdd:cd01298 1 ILIRNGTIVTTDPRRVLedgDVLVEDGRIVAVGPALplpaYPADEVIDAKGKVVMPGLVNTHTHLAMtllrgladdlplm 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445929010 65 ----------PGRTHWEGYETGTRAA----AKGGITTMIEMpLNQLPATVDRETIELKFDAAKGKLTIDaaqLGGLVSYN 130
Cdd:cd01298 81 ewlkdliwplERLLTEEDVYLGALLAlaemIRSGTTTFADM-YFFYPDAVAEAAEELGIRAVLGRGIMD---LGTEDVEE 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445929010 131 LdrlheldevgvvgfkcfvatcgDRGIDNDFRDVNDWQFykgaqklgemdqtvlvhcenalicdelgeeaKREGRVTAHd 210
Cdd:cd01298 157 T----------------------EEALAEAERLIREWHG-------------------------------AADGRIRVA- 182
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445929010 211 yVASRPVFT-EVEAIRRVLYLAKAAGCRLHvCHISspEGVEEVTRARQEGQDVTCESCPHYFVLDTDQF---------EE 280
Cdd:cd01298 183 -LAPHAPYTcSDELLREVAELAREYGVPLH-IHLA--ETEDEVEESLEKYGKRPVEYLEELGLLGPDVVlahcvwltdEE 258
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445929010 281 IGTLAK---------CSppirdqeNQKgmweklfngeidcLVSDHSPCPPEMKAG-NImqawgGI----AGLQNCMDvMF 346
Cdd:cd01298 259 IELLAEtgtgvahnpAS-------NMK-------------LASGIAPVPEMLEAGvNV-----GLgtdgAASNNNLD-MF 312
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445929010 347 DEA-----VQKRG----MSLPMFGKL-MAT-NAADIFGLKHKGRIAPGKDADLVFIQPDSSYVLKNEDLeyrhkVSPYVG 415
Cdd:cd01298 313 EEMrlaalLQKLAhgdpTALPAEEALeMATiGGAKALGLDEIGSLEVGKKADLILIDLDGPHLLPVHDP-----ISHLVY 387
|
490
....*....|....*...
gi 445929010 416 RTIGARITKTILRGDVIY 433
Cdd:cd01298 388 SANGGDVDTVIVNGRVVM 405
|
|
| SsnA |
COG0402 |
Cytosine/adenosine deaminase or related metal-dependent hydrolase [Nucleotide transport and ... |
4-395 |
1.91e-15 |
|
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: 77.94 E-value: 1.91e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445929010 4 DLIIKNGTVILENEARVI----DIAVQGGKIAAIGENL-----GEAKNVLDATGLIVSPGMVDAHTHISE---------- 64
Cdd:COG0402 1 DLLIRGAWVLTMDPAGGVledgAVLVEDGRIAAVGPGAelparYPAAEVIDAGGKLVLPGLVNTHTHLPQtllrgladdl 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445929010 65 -----------PGRTHW--EGYETGTRAAA----KGGITTMIEMplnqlpATVDRETIELKFDAAKgkltidAAQLGGLV 127
Cdd:COG0402 81 plldwleeyiwPLEARLdpEDVYAGALLALaemlRSGTTTVADF------YYVHPESADALAEAAA------EAGIRAVL 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445929010 128 SYnldrlheldevgvvgfkcfvaTCGDRGIDNDFRDvndwqfyKGAQKLGEMDqtvlvhcenALIcDELgeEAKREGRVT 207
Cdd:COG0402 149 GR---------------------GLMDRGFPDGLRE-------DADEGLADSE---------RLI-ERW--HGAADGRIR 188
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445929010 208 AHdyVASRPVFT-EVEAIRRVLYLAKAAGCRLHVcHISspEGVEEVTRARQE-GQDvtcescphyfvlDTDQFEEIGTLa 285
Cdd:COG0402 189 VA--LAPHAPYTvSPELLRAAAALARELGLPLHT-HLA--ETRDEVEWVLELyGKR------------PVEYLDELGLL- 250
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445929010 286 kcSPP--------IRDQEnqkgmWEKLfnGEIDCLVSdHSPCpPEMKAGN-I-----MQAWGGIAGL-------QNCMDv 344
Cdd:COG0402 251 --GPRtllahcvhLTDEE-----IALL--AETGASVA-HCPT-SNLKLGSgIapvprLLAAGVRVGLgtdgaasNNSLD- 318
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 445929010 345 MFDEA-----VQK----RGMSLPMFGKL-MAT-NAADIFGLKHK-GRIAPGKDADLVFIQPDS 395
Cdd:COG0402 319 MFEEMrlaalLQRlrggDPTALSAREALeMATlGGARALGLDDEiGSLEPGKRADLVVLDLDA 381
|
|
| AdeC |
COG1001 |
Adenine deaminase [Nucleotide transport and metabolism]; |
3-62 |
3.99e-14 |
|
Adenine deaminase [Nucleotide transport and metabolism];
Pssm-ID: 440625 [Multi-domain] Cd Length: 559 Bit Score: 74.37 E-value: 3.99e-14
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 445929010 3 FDLIIKNGTV-------ILENearviDIAVQGGKIAAIGENLGEAKNVLDATGLIVSPGMVDAHTHI 62
Cdd:COG1001 5 ADLVIKNGRLvnvftgeILEG-----DIAIAGGRIAGVGDYIGEATEVIDAAGRYLVPGFIDGHVHI 66
|
|
| HutI |
COG1228 |
Imidazolonepropionase or related amidohydrolase [Secondary metabolites biosynthesis, transport ... |
4-389 |
1.62e-13 |
|
Imidazolonepropionase or related amidohydrolase [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 440841 [Multi-domain] Cd Length: 386 Bit Score: 71.92 E-value: 1.62e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445929010 4 DLIIKNGTVILENEARVI---DIAVQGGKIAAIGENLG----EAKNVLDATGLIVSPGMVDAHTHISEPGRTHWEGYETG 76
Cdd:COG1228 9 TLLITNATLVDGTGGGVIengTVLVEDGKIAAVGPAADlavpAGAEVIDATGKTVLPGLIDAHTHLGLGGGRAVEFEAGG 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445929010 77 T---------------RAAAKGGITTMIEMPLNqlpatvdreTIELKFDAAKGKLtidaAQLGGlvsynlDRLheldevg 141
Cdd:COG1228 89 GitptvdlvnpadkrlRRALAAGVTTVRDLPGG---------PLGLRDAIIAGES----KLLPG------PRV------- 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445929010 142 vvgfkcFVAtcgDRGIDndfrdvndwqFYKGAQKLGEMDqtvlvhCENALicdelgEEAKREGrvtAhDYV-----ASRP 216
Cdd:COG1228 143 ------LAA---GPALS----------LTGGAHARGPEE------ARAAL------RELLAEG---A-DYIkvfaeGGAP 187
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445929010 217 VFTEvEAIRRVLYLAKAAGcrLHV-CHISSPEGVEEVTRA-----------RQEGQDVTCESCPHYFVLDTDQFEEIGTL 284
Cdd:COG1228 188 DFSL-EELRAILEAAHALG--LPVaAHAHQADDIRLAVEAgvdsiehgtylDDEVADLLAEAGTVVLVPTLSLFLALLEG 264
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445929010 285 AKCSPPIRDQENQKGMWE---KLFNGEIDCLVsdHSPCPPEMKAG-------NIMQAWGgiaglqncMDVMfdEAVQkrg 354
Cdd:COG1228 265 AAAPVAAKARKVREAALAnarRLHDAGVPVAL--GTDAGVGVPPGrslhrelALAVEAG--------LTPE--EALR--- 329
|
410 420 430
....*....|....*....|....*....|....*..
gi 445929010 355 mslpmfgklMAT-NAADIFGLKHK-GRIAPGKDADLV 389
Cdd:COG1228 330 ---------AATiNAAKALGLDDDvGSLEPGKLADLV 357
|
|
| PRK07572 |
PRK07572 |
cytosine deaminase; Validated |
3-62 |
3.65e-13 |
|
cytosine deaminase; Validated
Pssm-ID: 181039 Cd Length: 426 Bit Score: 70.82 E-value: 3.65e-13
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 445929010 3 FDLIIKNGTviLENEARVIDIAVQGGKIAAIGENL-GEAKNVLDATGLIVSPGMVDAHTHI 62
Cdd:PRK07572 2 FDLIVRNAN--LPDGRTGIDIGIAGGRIAAVEPGLqAEAAEEIDAAGRLVSPPFVDPHFHM 60
|
|
| Imidazolone-5PH |
cd01296 |
Imidazolonepropionase/imidazolone-5-propionate hydrolase (Imidazolone-5PH) catalyzes the third ... |
23-395 |
4.28e-13 |
|
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: 70.36 E-value: 4.28e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445929010 23 IAVQGGKIAAIG------ENLGEAKNVLDATGLIVSPGMVDAHTHISEPG-RTH-----WEGYETGTRAAAKGGITTMIE 90
Cdd:cd01296 1 IAIRDGRIAAVGpaaslpAPGPAAAEEIDAGGRAVTPGLVDCHTHLVFAGdRVDefaarLAGASYEEILAAGGGILSTVR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445929010 91 mplnqlpATVDRETIELKfdaAKGKLTIDAAQLGGLVS------YNLDR---------LHELDEVGVVGfkcFVAT-CGD 154
Cdd:cd01296 81 -------ATRAASEDELF---ASALRRLARMLRHGTTTvevksgYGLDLetelkmlrvIRRLKEEGPVD---LVSTfLGA 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445929010 155 RGIDNDFRDvnDWQFYKgaqklgemdqtvlvhcenaLICDELGEEAKREGRVTAHDYVASRPVFTeVEAIRRVLYLAKAA 234
Cdd:cd01296 148 HAVPPEYKG--REEYID-------------------LVIEEVLPAVAEENLADFCDVFCEKGAFS-LEQSRRILEAAKEA 205
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445929010 235 G--CRLHVCHISSPEGVEevtrarqEGQDVTCESCPHYFVLDTDQFE---EIGTLA----------KCSPPIRDQENQKG 299
Cdd:cd01296 206 GlpVKIHADELSNIGGAE-------LAAELGALSADHLEHTSDEGIAalaEAGTVAvllpgtafslRETYPPARKLIDAG 278
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445929010 300 MweklfngeIDCLVSDHSP--CPPEMkagnimqawggiaglqncMDVMFDEAVqkRGMSLPMFGKLMAT--NAADIFGLK 375
Cdd:cd01296 279 V--------PVALGTDFNPgsSPTSS------------------MPLVMHLAC--RLMRMTPEEALTAAtiNAAAALGLG 330
|
410 420
....*....|....*....|.
gi 445929010 376 HK-GRIAPGKDADLVFIQPDS 395
Cdd:cd01296 331 ETvGSLEVGKQADLVILDAPS 351
|
|
| Amidohydro_1 |
pfam01979 |
Amidohydrolase family; This family of enzymes are a a large metal dependent hydrolase ... |
50-432 |
4.44e-13 |
|
Amidohydrolase family; This family of enzymes are a a large metal dependent hydrolase superfamily. The family includes Adenine deaminase EC:3.5.4.2 that hydrolyses adenine to form hypoxanthine and ammonia. Adenine deaminases reaction is important for adenine utilization as a purine and also as a nitrogen source. This family also includes dihydroorotase and N-acetylglucosamine-6-phosphate deacetylases, EC:3.5.1.25 These enzymes catalyze the reaction N-acetyl-D-glucosamine 6-phosphate + H2O <=> D-glucosamine 6-phosphate + acetate. This family includes the catalytic domain of urease alpha subunit. Dihydroorotases (EC:3.5.2.3) are also included.
Pssm-ID: 460401 [Multi-domain] Cd Length: 334 Bit Score: 69.84 E-value: 4.44e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445929010 50 IVSPGMVDAHTHIS--------EPGRTHWEGYETGTRAAAKGGITTMIEMPLNQLPAtvdretIELKFDAAkgkltiDAA 121
Cdd:pfam01979 1 IVLPGLIDAHVHLEmgllrgipVPPEFAYEALRLGITTMLKSGTTTVLDMGATTSTG------IEALLEAA------EEL 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445929010 122 QLGglvsynldrlheldeVGVVGFKCFVATcgdRGIDNDFRDVNDwQFYKGAQKLGEMdqtvlvhcenalicdelgeeak 201
Cdd:pfam01979 69 PLG---------------LRFLGPGCSLDT---DGELEGRKALRE-KLKAGAEFIKGM---------------------- 107
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445929010 202 REGRVTAHDYVASRPVFTEvEAIRRVLYLAKAAGCRLHVcHISSPEGVEEVTRARqEGQDVTC----ESCPHYFVLDTDQ 277
Cdd:pfam01979 108 ADGVVFVGLAPHGAPTFSD-DELKAALEEAKKYGLPVAI-HALETKGEVEDAIAA-FGGGIEHgthlEVAESGGLLDIIK 184
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445929010 278 F----------EEIGTLAK-------CSPPIRDQENQKG---MWEKLFNGEIDCLVSDHSPcppemkAGNIMQAWGGIAg 337
Cdd:pfam01979 185 LilahgvhlspTEANLLAEhlkgagvAHCPFSNSKLRSGriaLRKALEDGVKVGLGTDGAG------SGNSLNMLEELR- 257
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445929010 338 lqncmDVMFDEAVQKRGMSLPMFGKLMATNAADIFGLKHK-GRIAPGKDADLVFIQPDssyvlknedleyrhKVSPYVGR 416
Cdd:pfam01979 258 -----LALELQFDPEGGLSPLEALRMATINPAKALGLDDKvGSIEVGKDADLVVVDLD--------------PLAAFFGL 318
|
410
....*....|....*.
gi 445929010 417 TIGARITKTILRGDVI 432
Cdd:pfam01979 319 KPDGNVKKVIVKGKIV 334
|
|
| metallo-dependent_hydrolases |
cd01292 |
Superfamily of metallo-dependent hydrolases (also called amidohydrolase superfamily) is a ... |
56-371 |
2.73e-11 |
|
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: 63.89 E-value: 2.73e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445929010 56 VDAHTHISEPGRTHW------------------EGYETGTRAAAKGGITTMIEMPLNqLPATVDRETIELKFDAAKGKLT 117
Cdd:cd01292 2 IDTHVHLDGSALRGTrlnlelkeaeelspedlyEDTLRALEALLAGGVTTVVDMGST-PPPTTTKAAIEAVAEAARASAG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445929010 118 IDAAQLGGLVSYN-----------LDRLHELDEVGVVGFKCFVAtCGDRGIDNDFRDvndwQFYKGAQKLGEMdqtVLVH 186
Cdd:cd01292 81 IRVVLGLGIPGVPaavdedaeallLELLRRGLELGAVGLKLAGP-YTATGLSDESLR----RVLEEARKLGLP---VVIH 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445929010 187 CENALICDELGEEakregrvtahdyvasrpvfteveairrvLYLAKAAGCRLHVCHISSPEgVEEVTRARQEGqdVTCES 266
Cdd:cd01292 153 AGELPDPTRALED----------------------------LVALLRLGGRVVIGHVSHLD-PELLELLKEAG--VSLEV 201
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445929010 267 CPHYFVLDTdqfeeigtlakcsppiRDQENQKGMWEKLFNGEIDCLVSDHSPCPPEMKAGNIMQAWggiaglqncmdvmf 346
Cdd:cd01292 202 CPLSNYLLG----------------RDGEGAEALRRLLELGIRVTLGTDGPPHPLGTDLLALLRLL-------------- 251
|
330 340
....*....|....*....|....*
gi 445929010 347 dEAVQKRGMSLPMFGKLMATNAADI 371
Cdd:cd01292 252 -LKVLRLGLSLEEALRLATINPARA 275
|
|
| Isoaspartyl-dipeptidase |
cd01308 |
Isoaspartyl dipeptidase hydrolyzes the beta-L-isoaspartyl linkages in dipeptides, as part of ... |
5-394 |
8.46e-10 |
|
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: 60.48 E-value: 8.46e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445929010 5 LIIKNGTVILENEARVIDIAVQGGKIAAIGENL----GEAKNVLDATGLIVSPGMVDAHTHISEPGRThwEGYETGT--- 77
Cdd:cd01308 2 TLIKNAEVYAPEYLGKKDILIAGGKILAIEDQLnlpgYENVTVVDLHGKILVPGFIDQHVHIIGGGGE--GGPSTRTpev 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445929010 78 --RAAAKGGITTMIemplnqlpatvdretielkfdaakGKLTIDAAQLG--GLVSynldRLHELDEVGVvgfKCFVatcg 153
Cdd:cd01308 80 tlSDLTTAGVTTVV------------------------GCLGTDGISRSmeDLLA----KARALEEEGI---TCFV---- 124
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445929010 154 drgidndfrdvndwqfYKGAQKLGEMDQTVLVHCENALICDELGeeakrEGRVTAHDYVASRPVFTEVEAI----RRVLY 229
Cdd:cd01308 125 ----------------YTGSYEVPTRTITGSIRKDLLLIDKVIG-----VGEIAISDHRSSQPTVEELARIaaeaRVGGL 183
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445929010 230 LAKAAGCrLHVCHISSPEGVEEVTRARQEGQDVTCESCPHYFVLDTDQFEEIGTLAK----------------CSPPIRD 293
Cdd:cd01308 184 LGGKAGI-VHIHLGDGKRALSPIFELIEETEIPITQFLPTHINRTAPLFEQGVEFAKmggtidltssidpqfrKEGEVRP 262
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445929010 294 QENQKGMWEKLFNGEIDCLVSDHSPCPPEMKAGNIMQawggiaGLQNC-MDVMFD---EAVQKRGMSLPMFGKLMATNAA 369
Cdd:cd01308 263 SEALKRLLEQGVPLERITFSSDGNGSLPKFDENGNLV------GLGVGsVDTLLRevrEAVKCGDIPLEVALRVITSNVA 336
|
410 420
....*....|....*....|....*
gi 445929010 370 DIFGLKHKGRIAPGKDADLVFIQPD 394
Cdd:cd01308 337 RILKLRKKGEIQPGFDADLVILDKD 361
|
|
| PRK15446 |
PRK15446 |
phosphonate metabolism protein PhnM; Provisional |
4-394 |
1.04e-09 |
|
phosphonate metabolism protein PhnM; Provisional
Pssm-ID: 237967 [Multi-domain] Cd Length: 383 Bit Score: 59.81 E-value: 1.04e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445929010 4 DLIIKNGTVILENEARVIDIAVQGGKIAAIGENLGEAKNVLDATGLIVSPGMVDAHT-----HIS-EPGrTHWEgYETGT 77
Cdd:PRK15446 3 EMILSNARLVLPDEVVDGSLLIEDGRIAAIDPGASALPGAIDAEGDYLLPGLVDLHTdnlekHLApRPG-VDWP-ADAAL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445929010 78 RAA----AKGGITTMiemplnqlpatvdretielkFDAakgkLTIDAAQLGGLVSYNLD--------------------R 133
Cdd:PRK15446 81 AAHdaqlAAAGITTV--------------------FDA----LSVGDEEDGGLRSRDLArklidaieearargllradhR 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445929010 134 LH---ELDEVGVVGFkcFVATCGDRGID----ND-------FRDVNDW-QFYKGAQKLGEmdqtvlvhCENALICDELGE 198
Cdd:PRK15446 137 LHlrcELTNPDALEL--FEALLAHPRVDlvslMDhtpgqrqFRDLEKYrEYYAGKYGLSD--------EEFDAFVEERIA 206
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445929010 199 EAKREGRvtahdyvasrpvftevEAIRRVLYLAKAAGCRL--HvchisSPEGVEEVTRARQEGQDVTcescphyfvldtd 276
Cdd:PRK15446 207 LSARYAP----------------PNRRAIAALARARGIPLasH-----DDDTPEHVAEAHALGVAIA------------- 252
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445929010 277 QF---EEIGTLAKcsppirdqenQKGMW---------------------EKLFNGEIDCLVSDHSPcppemkagnimqaw 332
Cdd:PRK15446 253 EFpttLEAARAAR----------ALGMSvlmgapnvvrggshsgnvsalDLAAAGLLDILSSDYYP-------------- 308
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 445929010 333 ggiAGLqncMDVMFDEAvQKRGMSLPMFGKLMATNAADIFGLKHKGRIAPGKDADLVFIQPD 394
Cdd:PRK15446 309 ---ASL---LDAAFRLA-DDGGLDLPQAVALVTANPARAAGLDDRGEIAPGKRADLVRVRRA 363
|
|
| NagA |
COG1820 |
N-acetylglucosamine-6-phosphate deacetylase [Carbohydrate transport and metabolism]; |
6-106 |
1.32e-09 |
|
N-acetylglucosamine-6-phosphate deacetylase [Carbohydrate transport and metabolism];
Pssm-ID: 441425 [Multi-domain] Cd Length: 373 Bit Score: 59.73 E-value: 1.32e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445929010 6 IIKNGTVILENeaRVID---IAVQGGKIAAIGENLGEAKNVLDATGLIVSPGMVDAHTH------ISEPGrthWEGYETG 76
Cdd:COG1820 1 AITNARIFTGD--GVLEdgaLLIEDGRIAAIGPGAEPDAEVIDLGGGYLAPGFIDLHVHggggvdFMDGT---PEALRTI 75
|
90 100 110
....*....|....*....|....*....|..
gi 445929010 77 TRAAAKGGITTMiemplnqLPATV--DRETIE 106
Cdd:COG1820 76 ARAHARHGTTSF-------LPTTItaPPEDLL 100
|
|
| Met_dep_hydrolase_B |
cd01307 |
Metallo-dependent hydrolases, subgroup B is part of the superfamily of metallo-dependent ... |
22-90 |
2.13e-09 |
|
Metallo-dependent hydrolases, subgroup B is part of the superfamily of metallo-dependent hydrolases, a large group of proteins that show conservation in their 3-dimensional fold (TIM barrel) and in details of their active site. The vast majority of the members have a conserved metal binding site, involving four histidines and one aspartic acid residue. In the common reaction mechanism, the metal ion (or ions) deprotonate a water molecule for a nucleophilic attack on the substrate. The function of this subgroup is unknown.
Pssm-ID: 238632 [Multi-domain] Cd Length: 338 Bit Score: 58.88 E-value: 2.13e-09
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 445929010 22 DIAVQGGKIAAIGENL--GEAKNVLDATGLIVSPGMVDAHTHIsepgrtHWEGYETGTRA---AAKGGITTMIE 90
Cdd:cd01307 1 DVAIENGKIAAVGAALaaPAATQIVDAGGCYVSPGWIDLHVHV------YQGGTRYGDRPdmiGVKSGVTTVVD 68
|
|
| Bact_CD |
cd01293 |
Bacterial cytosine deaminase and related metal-dependent hydrolases. Cytosine deaminases (CDs) ... |
6-62 |
6.78e-09 |
|
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: 57.64 E-value: 6.78e-09
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 445929010 6 IIKNGTVILENEARViDIAVQGGKIAAIGENL--GEAKNVLDATGLIVSPGMVDAHTHI 62
Cdd:cd01293 1 LLRNARLADGGTALV-DIAIEDGRIAAIGPALavPPDAEEVDAKGRLVLPAFVDPHIHL 58
|
|
| YtcJ |
COG1574 |
Predicted amidohydrolase YtcJ [General function prediction only]; |
4-68 |
1.02e-08 |
|
Predicted amidohydrolase YtcJ [General function prediction only];
Pssm-ID: 441182 [Multi-domain] Cd Length: 535 Bit Score: 57.12 E-value: 1.02e-08
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 445929010 4 DLIIKNGTVILENEARVI--DIAVQGGKIAAIGEN------LGEAKNVLDATGLIVSPGMVDAHTHISEPGRT 68
Cdd:COG1574 9 DLLLTNGRIYTMDPAQPVaeAVAVRDGRIVAVGSDaevralAGPATEVIDLGGKTVLPGFIDAHVHLLGGGLA 81
|
|
| PRK07228 |
PRK07228 |
5'-deoxyadenosine deaminase; |
4-61 |
1.56e-08 |
|
5'-deoxyadenosine deaminase;
Pssm-ID: 180895 [Multi-domain] Cd Length: 445 Bit Score: 56.55 E-value: 1.56e-08
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 445929010 4 DLIIKNGTVILENEARVI---DIAVQGGKIAAIGEN--LGEAKNVLDATGLIVSPGMVDAHTH 61
Cdd:PRK07228 2 TILIKNAGIVTMNAKREIvdgDVLIEDDRIAAVGDRldLEDYDDHIDATGKVVIPGLIQGHIH 64
|
|
| PRK08393 |
PRK08393 |
N-ethylammeline chlorohydrolase; Provisional |
5-61 |
1.59e-08 |
|
N-ethylammeline chlorohydrolase; Provisional
Pssm-ID: 181411 [Multi-domain] Cd Length: 424 Bit Score: 56.35 E-value: 1.59e-08
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 445929010 5 LIIKNGTVILENEARVI--DIAVQGGKIAAIGENLGE-AKNVLDATGLIVSPGMVDAHTH 61
Cdd:PRK08393 3 ILIKNGYVIYGENLKVIraDVLIEGNKIVEVKRNINKpADTVIDASGSVVSPGFINAHTH 62
|
|
| PRK07203 |
PRK07203 |
putative aminohydrolase SsnA; |
5-62 |
4.16e-08 |
|
putative aminohydrolase SsnA;
Pssm-ID: 235963 [Multi-domain] Cd Length: 442 Bit Score: 55.33 E-value: 4.16e-08
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 445929010 5 LIIKNGTVILENEARVI----DIAVQGGKIAAIG--ENLGEA---KNVLDATGLIVSPGMVDAHTHI 62
Cdd:PRK07203 2 LLIGNGTAITRDPAKPViedgAIAIEGNVIVEIGttDELKAKypdAEFIDAKGKLIMPGLINSHNHI 68
|
|
| PRK12394 |
PRK12394 |
metallo-dependent hydrolase; |
1-90 |
1.90e-07 |
|
metallo-dependent hydrolase;
Pssm-ID: 183497 [Multi-domain] Cd Length: 379 Bit Score: 52.84 E-value: 1.90e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445929010 1 MSFDLIIKNGtVILENEARVI---DIAVQGGKIAAIgENLGEA--KNVLDATGLIVSPGMVDAHTHIsepgrtHWEGYET 75
Cdd:PRK12394 1 MKNDILITNG-HIIDPARNINeinNLRIINDIIVDA-DKYPVAseTRIIHADGCIVTPGLIDYHAHV------FYDGTEG 72
|
90
....*....|....*...
gi 445929010 76 GTR---AAAKGGITTMIE 90
Cdd:PRK12394 73 GVRpdmYMPPNGVTTVVD 90
|
|
| PRK08204 |
PRK08204 |
hypothetical protein; Provisional |
6-84 |
1.96e-07 |
|
hypothetical protein; Provisional
Pssm-ID: 181288 [Multi-domain] Cd Length: 449 Bit Score: 53.08 E-value: 1.96e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445929010 6 IIKNGTVILENEA----RVIDIAVQGGKIAAIGENLG-EAKNVLDATGLIVSPGMVDAHTHIsepgrthWegyETGTRAA 80
Cdd:PRK08204 5 LIRGGTVLTMDPAigdlPRGDILIEGDRIAAVAPSIEaPDAEVVDARGMIVMPGLVDTHRHT-------W---QSVLRGI 74
|
....
gi 445929010 81 AKGG 84
Cdd:PRK08204 75 GADW 78
|
|
| PRK06038 |
PRK06038 |
N-ethylammeline chlorohydrolase; Provisional |
4-63 |
5.28e-07 |
|
N-ethylammeline chlorohydrolase; Provisional
Pssm-ID: 180363 [Multi-domain] Cd Length: 430 Bit Score: 51.67 E-value: 5.28e-07
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 445929010 4 DLIIKNGTVILENEARVID--IAVQGGKIAAIGENL-GEAKNVLDATGLIVSPGMVDAHTHIS 63
Cdd:PRK06038 3 DIIIKNAYVLTMDAGDLKKgsVVIEDGTITEVSESTpGDADTVIDAKGSVVMPGLVNTHTHAA 65
|
|
| PRK05985 |
PRK05985 |
cytosine deaminase; Provisional |
2-70 |
5.70e-07 |
|
cytosine deaminase; Provisional
Pssm-ID: 180337 [Multi-domain] Cd Length: 391 Bit Score: 51.47 E-value: 5.70e-07
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 445929010 2 SFDLIIKNgtVILENEARViDIAVQGGKIAAIGENLG--EAKNVLDATGLIVSPGMVDAHTHisePGRTHW 70
Cdd:PRK05985 1 MTDLLFRN--VRPAGGAAV-DILIRDGRIAAIGPALAapPGAEVEDGGGALALPGLVDGHIH---LDKTFW 65
|
|
| FMDH_A |
cd01304 |
Formylmethanofuran dehydrogenase (FMDH) subunit A; Methanogenic bacteria and archea derive ... |
7-94 |
7.87e-07 |
|
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: 51.26 E-value: 7.87e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445929010 7 IKNGTVI---LENEARVIDIAVQGGKIAAIGENLGEAKnVLDATGLIVSPGMVDAHTHI-------------------SE 64
Cdd:cd01304 1 IKNGTVYdplNGINGEKMDIFIRDGKIVESSSGAKPAK-VIDASGKVVMAGGVDMHSHIaggkvnvgrilrpedhrrdPV 79
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 445929010 65 PGR-------------THWEGYETgtraaAKGGITTMIE---MPLN 94
Cdd:cd01304 80 PKGalrragvgfsvpsTLATGYRY-----AEMGYTTAFEaamPPLN 120
|
|
| NagA |
cd00854 |
N-acetylglucosamine-6-phosphate deacetylase, NagA, catalyzes the hydrolysis of the N-acetyl ... |
5-106 |
1.11e-06 |
|
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: 50.66 E-value: 1.11e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445929010 5 LIIKNGTVILENEARVIDIAVQGGKIAAIGEN--LGEAKNVLDATGLIVSPGMVDAHTHisepGR-------THWEGYET 75
Cdd:cd00854 1 LIIKNARILTPGGLEDGAVLVEDGKIVAIGPEdeLEEADEIIDLKGQYLVPGFIDIHIH----GGggadfmdGTAEALKT 76
|
90 100 110
....*....|....*....|....*....|...
gi 445929010 76 GTRAAAKGGITTMiemplnqLPATV--DRETIE 106
Cdd:cd00854 77 IAEALAKHGTTSF-------LPTTVtaPPEEIA 102
|
|
| PRK06380 |
PRK06380 |
metal-dependent hydrolase; Provisional |
1-62 |
1.27e-06 |
|
metal-dependent hydrolase; Provisional
Pssm-ID: 180548 [Multi-domain] Cd Length: 418 Bit Score: 50.65 E-value: 1.27e-06
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 445929010 1 MSfdLIIKNGTVILENEARVI---DIAVQGGKIAAIGENLGEAKNVLDATGLIVSPGMVDAHTHI 62
Cdd:PRK06380 1 MS--ILIKNAWIVTQNEKREIlqgNVYIEGNKIVYVGDVNEEADYIIDATGKVVMPGLINTHAHV 63
|
|
| Met_dep_hydrolase_C |
cd01309 |
Metallo-dependent hydrolases, subgroup C is part of the superfamily of metallo-dependent ... |
28-389 |
3.03e-06 |
|
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: 49.23 E-value: 3.03e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445929010 28 GKIAAIGENL--GEAKNVLDATGLIVSPGMVDAHTHI----SEPGRTHWEGYETGT------RA-------------AAK 82
Cdd:cd01309 2 GKIVAVGAEIttPADAEVIDAKGKHVTPGLIDAHSHLgldeEGGVRETSDANEETDpvtphvRAidginpddeafkrARA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445929010 83 GGITTMIEMPLNQLPatVDRETIELKFDAA--KGKLTIDAAQLGGLVSYNLDRLHEldevgvvGFKCFVATcgdR-GIDN 159
Cdd:cd01309 82 GGVTTVQVLPGSANL--IGGQGVVIKTDGGtiEDMFIKAPAGLKMALGENPKRVYG-------GKGKEPAT---RmGVAA 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445929010 160 DFRDvndwQFYKgAQKLGEMDQTVLVHCENALICD----ELGEEAKREGRVTAHDYVASrpvfteveAIRRVLYLAKAAG 235
Cdd:cd01309 150 LLRD----AFIK-AQEYGRKYDLGKNAKKDPPERDlkleALLPVLKGEIPVRIHAHRAD--------DILTAIRIAKEFG 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445929010 236 CRLHVCHISspEGVEEVTRARQEGQDVTcescphYFVLDTdqfeeigtlakcsPPIRDQENQKGMWEK---LFNGEID-C 311
Cdd:cd01309 217 IKITIEHGA--EGYKLADELAKHGIPVI------YGPTLT-------------LPKKVEEVNDAIDTNaylLKKGGVAfA 275
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 445929010 312 LVSDHspcpPEMKAGNIMQAwggiAGLqncmdvmfdeAVqKRGMSLPMFGKLMATNAADIFGLKHK-GRIAPGKDADLV 389
Cdd:cd01309 276 ISSDH----PVLNIRNLNLE----AAK----------AV-KYGLSYEEALKAITINPAKILGIEDRvGSLEPGKDADLV 335
|
|
| Urease_alpha |
cd00375 |
Urease alpha-subunit; Urease is a nickel-dependent metalloenzyme that catalyzes the hydrolysis ... |
4-89 |
3.39e-06 |
|
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: 49.25 E-value: 3.39e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445929010 4 DLIIKNGTVILENEARVIDIAVQGGKIAAIGEN--------------LGEAKNVLDATGLIVSPGMVDAHTHISEPgRTH 69
Cdd:cd00375 66 DLVITNALIIDYTGIYKADIGIKDGRIVAIGKAgnpdimdgvtpnmiVGPSTEVIAGEGKIVTAGGIDTHVHFICP-QQI 144
|
90 100
....*....|....*....|
gi 445929010 70 WEgyetgtraAAKGGITTMI 89
Cdd:cd00375 145 EE--------ALASGITTMI 156
|
|
| ureC |
PRK13308 |
urease subunit alpha; Reviewed |
4-89 |
5.08e-06 |
|
urease subunit alpha; Reviewed
Pssm-ID: 183965 [Multi-domain] Cd Length: 569 Bit Score: 48.93 E-value: 5.08e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445929010 4 DLIIKNGTVIlENEARVI--DIAVQGGKIAAIGEN--------------LGEAKNVLDATGLIVSPGMVDAHTHISEPGR 67
Cdd:PRK13308 69 DFVLCNVTVI-DPVLGIVkgDIGIRDGRIVGIGKAgnpdimdgvdprlvVGPGTDVRPAEGLIATPGAIDVHVHFDSAQL 147
|
90 100
....*....|....*....|...
gi 445929010 68 T-HwegyetgtraAAKGGITTMI 89
Cdd:PRK13308 148 VdH----------ALASGITTML 160
|
|
| ureB |
PRK13985 |
urease subunit alpha; |
2-146 |
1.21e-05 |
|
urease subunit alpha;
Pssm-ID: 184438 [Multi-domain] Cd Length: 568 Bit Score: 47.58 E-value: 1.21e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445929010 2 SFDLIIKNGTVILENEARVIDIAVQGGKIAAIG------------ENL--GEAKNVLDATGLIVSPGMVDAHTHISEPgr 67
Cdd:PRK13985 64 ELDLIITNALIIDYTGIYKADIGIKDGKIAGIGkggnkdmqdgvkNNLsvGPATEALAGEGLIVTAGGIDTHIHFISP-- 141
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445929010 68 thwegyeTGTRAAAKGGITTMI---EMPLNQLPATV---DRETIELKFDAAKgKLTIDAAQLGGLVSYNLDRLHELDEVG 141
Cdd:PRK13985 142 -------QQIPTAFASGVTTMIgggTGPADGTNATTitpGRRNLKWMLRAAE-EYSMNLGFLGKGNSSNDASLADQIEAG 213
|
....*
gi 445929010 142 VVGFK 146
Cdd:PRK13985 214 AIGFK 218
|
|
| Amidohydro_3 |
pfam07969 |
Amidohydrolase family; |
43-433 |
5.19e-05 |
|
Amidohydrolase family;
Pssm-ID: 400360 [Multi-domain] Cd Length: 464 Bit Score: 45.60 E-value: 5.19e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445929010 43 VLDATGLIVSPGMVDAHTHISEPG----RTHWEGYETGTRAAAKGGITTMIEMPL------NQLPATVDRETI------- 105
Cdd:pfam07969 2 VIDAKGRLVLPGFVDPHTHLDGGGlnlrELRLPDVLPNAVVKGQAGRTPKGRWLVgegwdeAQFAETRFPYALadldeva 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445929010 106 ----------------------------ELKFDAAKGKLTIDA--AQLGGLV---SYNLDRLHELDEV------GVVGFK 146
Cdd:pfam07969 82 pdgpvllralhthaavansaaldlagitKATEDPPGGEIARDAngEGLTGLLregAYALPPLLAREAEaaavaaALAALP 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445929010 147 CFVATCGDRGIDNDFR--DVNDWQFYKGAQKLGEMDQ----TVLVHCENALICDELGEEAKREG--------RVTAHDYV 212
Cdd:pfam07969 162 GFGITSVDGGGGNVHSldDYEPLRELTAAEKLKELLDaperLGLPHSIYELRIGAMKLFADGVLgsrtaaltEPYFDAPG 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445929010 213 ASRPVFTEvEAIRRVLYLAKAAGCRLHvCHISSPEGVEEVTRA-----RQEGQD--VTCESCPHYFVLDTDQFEEIGTLA 285
Cdd:pfam07969 242 TGWPDFED-EALAELVAAARERGLDVA-IHAIGDATIDTALDAfeavaEKLGNQgrVRIEHAQGVVPYTYSQIERVAALG 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445929010 286 KCSP------------PIRDQENQKGMW-----EKLFNGEIDCLVSDHSPCP----PEMKAGNIMQAWGGIAGLQNCMDV 344
Cdd:pfam07969 320 GAAGvqpvfdplwgdwLQDRLGAERARGltpvkELLNAGVKVALGSDAPVGPfdpwPRIGAAVMRQTAGGGEVLGPDEEL 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445929010 345 MFDEAVQkrgmslpmfgkLMATNAADIFGL-KHKGRIAPGKDADLVfiqpdssyVLKNEDLeyrhKVSPYVGRTIGARit 423
Cdd:pfam07969 400 SLEEALA-----------LYTSGPAKALGLeDRKGTLGVGKDADLV--------VLDDDPL----TVDPPAIADIRVR-- 454
|
490
....*....|
gi 445929010 424 KTILRGDVIY 433
Cdd:pfam07969 455 LTVVDGRVVY 464
|
|
| YtcJ_like |
cd01300 |
YtcJ_like metal dependent amidohydrolases. YtcJ is a Bacillus subtilis ORF of unknown function. ... |
22-64 |
8.66e-05 |
|
YtcJ_like metal dependent amidohydrolases. YtcJ is a Bacillus subtilis ORF of unknown function. The Arabidopsis homolog LAF3 has been identified as a factor required for phytochrome A signalling.
Pssm-ID: 238625 [Multi-domain] Cd Length: 479 Bit Score: 44.61 E-value: 8.66e-05
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 445929010 22 DIAVQGGKIAAIGEN------LGEAKNVLDATGLIVSPGMVDAHTHISE 64
Cdd:cd01300 1 AVAVRDGRIVAVGSDaeakalKGPATEVIDLKGKTVLPGFIDSHSHLLL 49
|
|
| PRK08203 |
PRK08203 |
hydroxydechloroatrazine ethylaminohydrolase; Reviewed |
5-79 |
1.15e-04 |
|
hydroxydechloroatrazine ethylaminohydrolase; Reviewed
Pssm-ID: 236184 [Multi-domain] Cd Length: 451 Bit Score: 44.46 E-value: 1.15e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445929010 5 LIIKNGTVIL-ENEARVID----IAVQGGKIAAIG---ENLGEAKNVLDATGLIVSPGMVDAHTHIsepgrthwegYETG 76
Cdd:PRK08203 3 LWIKNPLAIVtMDAARREIadggLVVEGGRIVEVGpggALPQPADEVFDARGHVVTPGLVNTHHHF----------YQTL 72
|
...
gi 445929010 77 TRA 79
Cdd:PRK08203 73 TRA 75
|
|
| PRK12393 |
PRK12393 |
amidohydrolase; Provisional |
4-62 |
1.31e-04 |
|
amidohydrolase; Provisional
Pssm-ID: 237088 [Multi-domain] Cd Length: 457 Bit Score: 44.29 E-value: 1.31e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 445929010 4 DLIIKNGTVILE----NEARV--IDIAVQGGKIAAIG---ENLGEakNVLDATGLIVSPGMVDAHTHI 62
Cdd:PRK12393 3 SLLIRNAAAIMTglpgDAARLggPDIRIRDGRIAAIGaltPLPGE--RVIDATDCVVYPGWVNTHHHL 68
|
|
| PhnM |
cd01306 |
PhnM is believed to be a subunit of the membrane associated C-P lyase complex. C-P lyase is ... |
307-394 |
1.65e-04 |
|
PhnM is believed to be a subunit of the membrane associated C-P lyase complex. C-P lyase is thought to catalyze the direct cleavage of inactivated C-P bonds to yield inorganic phosphate and the corresponding hydrocarbons. It is responsible for cleavage of alkylphosphonates, which are utilized as sole phosphorus sources by many bacteria.
Pssm-ID: 238631 Cd Length: 325 Bit Score: 43.42 E-value: 1.65e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445929010 307 GEIDCLVSDHSPcppemkaGNIMQAWGGIAglqncmdvmfdeavQKRGMSLPMFGKLMATNAADIFGLKHKGRIAPGKDA 386
Cdd:cd01306 246 GLLDILSSDYVP-------ASLLHAAFRLA--------------DLGGWSLPEAVALVSANPARAVGLTDRGSIAPGKRA 304
|
....*...
gi 445929010 387 DLVFIQPD 394
Cdd:cd01306 305 DLILVDDM 312
|
|
| ureC |
PRK13207 |
urease subunit alpha; Reviewed |
4-89 |
2.22e-04 |
|
urease subunit alpha; Reviewed
Pssm-ID: 237305 [Multi-domain] Cd Length: 568 Bit Score: 43.63 E-value: 2.22e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445929010 4 DLIIKNGTVILENEARVIDIAVQGGKIAAIGE--N----------LGEAKNVLDATGLIVSPGMVDAHTHISEPGRthwe 71
Cdd:PRK13207 68 DTVITNALILDHWGIVKADIGIKDGRIVAIGKagNpdiqdgvdiiIGPGTEVIAGEGLIVTAGGIDTHIHFICPQQ---- 143
|
90
....*....|....*...
gi 445929010 72 gyetgTRAAAKGGITTMI 89
Cdd:PRK13207 144 -----IEEALASGVTTMI 156
|
|
| AdeC |
cd01295 |
Adenine deaminase (AdeC) directly deaminates adenine to form hypoxanthine. This reaction is ... |
342-392 |
2.38e-04 |
|
Adenine deaminase (AdeC) directly deaminates adenine to form hypoxanthine. This reaction is part of one of the adenine salvage pathways, as well as the degradation pathway. It is important for adenine utilization as a purine, as well as a nitrogen source in bacteria and archea.
Pssm-ID: 238620 [Multi-domain] Cd Length: 422 Bit Score: 43.37 E-value: 2.38e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 445929010 342 MDVMFDEAVQKrGMSlPMFGKLMAT-NAADIFGLKHKGRIAPGKDADLVFIQ 392
Cdd:cd01295 223 LDYIVRRAIEA-GIP-PEDAIQMATiNPAECYGLHDLGAIAPGRIADIVILD 272
|
|
| NagA |
cd00854 |
N-acetylglucosamine-6-phosphate deacetylase, NagA, catalyzes the hydrolysis of the N-acetyl ... |
333-389 |
7.63e-04 |
|
N-acetylglucosamine-6-phosphate deacetylase, NagA, catalyzes the hydrolysis of the N-acetyl group of N-acetyl-glucosamine-6-phosphate (GlcNAc-6-P) to glucosamine 6-phosphate and acetate. This is the first committed step in the biosynthetic pathway to amino-sugar-nucleotides, which is needed for cell wall peptidoglycan and teichoic acid biosynthesis. Deacetylation of N-acetylglucosamine is also important in lipopolysaccharide synthesis and cell wall recycling.
Pssm-ID: 238434 [Multi-domain] Cd Length: 374 Bit Score: 41.41 E-value: 7.63e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 445929010 333 GGIAGLQNCMDVMFDEAVQKRGMSLPmFGKLMAT-NAADIFGLKH-KGRIAPGKDADLV 389
Cdd:cd00854 302 GTLAGSTLTMDQAVRNMVKWGGCPLE-EAVRMASlNPAKLLGLDDrKGSLKPGKDADLV 359
|
|
| PRK10027 |
PRK10027 |
cryptic adenine deaminase; Provisional |
342-391 |
1.33e-03 |
|
cryptic adenine deaminase; Provisional
Pssm-ID: 182201 [Multi-domain] Cd Length: 588 Bit Score: 40.97 E-value: 1.33e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 445929010 342 MDVMFDEAVQKRGMSLPMFGKLMATNAADIFGLKHKGRIAPGKDADLVFI 391
Cdd:PRK10027 297 IDALIRRLIEQHNVPLHVAYRVASWSTARHFGLNHLGLLAPGKQADIVLL 346
|
|
| PRK07583 |
PRK07583 |
cytosine deaminase; |
21-62 |
1.78e-03 |
|
cytosine deaminase;
Pssm-ID: 236062 Cd Length: 438 Bit Score: 40.35 E-value: 1.78e-03
10 20 30 40
....*....|....*....|....*....|....*....|....
gi 445929010 21 IDIAVQGGKIAAIGENLGEAKNV--LDATGLIVSPGMVDAHTHI 62
Cdd:PRK07583 41 VDIEIADGKIAAILPAGGAPDELpaVDLKGRMVWPCFVDMHTHL 84
|
|
| PRK10027 |
PRK10027 |
cryptic adenine deaminase; Provisional |
4-89 |
1.79e-03 |
|
cryptic adenine deaminase; Provisional
Pssm-ID: 182201 [Multi-domain] Cd Length: 588 Bit Score: 40.58 E-value: 1.79e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445929010 4 DLIIKNGTVILENEARVID--IAVQGGKIAAIGE--NLGEAKNVLDATGLIVSPGMVDAHTHISEPGRTHWEgYETGTRA 79
Cdd:PRK10027 31 DYIIDNVSILDLINGGEISgpIVIKGRYIAGVGAeyADAPALQRIDARGATAVPGFIDAHLHIESSMMTPVT-FETATLP 109
|
90
....*....|
gi 445929010 80 AakgGITTMI 89
Cdd:PRK10027 110 R---GLTTVI 116
|
|
| PRK07213 |
PRK07213 |
chlorohydrolase; Provisional |
5-62 |
1.94e-03 |
|
chlorohydrolase; Provisional
Pssm-ID: 235969 [Multi-domain] Cd Length: 375 Bit Score: 40.41 E-value: 1.94e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 445929010 5 LIIKNGTVI--LENEARVIDIAVQGGKIAAIGENLgEAKNVLDATGLIVsPGMVDAHTHI 62
Cdd:PRK07213 2 LVYLNGNFLygEDFEPKKGNLVIEDGIIKGFTNEV-HEGNVIDAKGLVI-PPLINAHTHI 59
|
|
| PRK06846 |
PRK06846 |
putative deaminase; Validated |
8-107 |
5.47e-03 |
|
putative deaminase; Validated
Pssm-ID: 235873 [Multi-domain] Cd Length: 410 Bit Score: 38.84 E-value: 5.47e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445929010 8 KNGTVILENEARVIDIAVQGGKIAAIGEN---LGEAKNVLDATGLIVSPGMVDAHTHISepgRTHWEG-YETGTRAaakG 83
Cdd:PRK06846 19 YENGVIVQTETALCTLEIQDGKIVAIRPNkqvPDATLPTYDANGLLMLPAFREMHIHLD---KTYYGGpWKACRPA---K 92
|
90 100 110
....*....|....*....|....*....|.
gi 445929010 84 GITTMI-----EMPlNQLPATVDRET--IEL 107
Cdd:PRK06846 93 TIQDRIeleqkELP-ELLPTTQERAEklIEL 122
|
|
| ureC |
PRK13206 |
urease subunit alpha; Reviewed |
4-89 |
6.44e-03 |
|
urease subunit alpha; Reviewed
Pssm-ID: 237304 [Multi-domain] Cd Length: 573 Bit Score: 38.92 E-value: 6.44e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445929010 4 DLIIkNGTVILENEARVI-DIAVQGGKIAAIGEN--------------LGEAKNVLDATGLIVSPGMVDAHTHISEPGRT 68
Cdd:PRK13206 72 DTVI-TGAVILDHWGIVKaDVGIRDGRIVAIGKAgnpdimdgvhpdlvIGPSTEIIAGNGRILTAGAIDCHVHFICPQIV 150
|
90 100
....*....|....*....|.
gi 445929010 69 HwegyetgtrAAAKGGITTMI 89
Cdd:PRK13206 151 D---------EALAAGITTLI 162
|
|
| AdeC |
cd01295 |
Adenine deaminase (AdeC) directly deaminates adenine to form hypoxanthine. This reaction is ... |
45-89 |
7.37e-03 |
|
Adenine deaminase (AdeC) directly deaminates adenine to form hypoxanthine. This reaction is part of one of the adenine salvage pathways, as well as the degradation pathway. It is important for adenine utilization as a purine, as well as a nitrogen source in bacteria and archea.
Pssm-ID: 238620 [Multi-domain] Cd Length: 422 Bit Score: 38.36 E-value: 7.37e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*
gi 445929010 45 DATGLIVSPGMVDAHTHISEPGRTHWEgYEtgtRAAAKGGITTMI 89
Cdd:cd01295 1 DAEGKYIVPGFIDAHLHIESSMLTPSE-FA---KAVLPHGTTTVI 41
|
|
| PRK09045 |
PRK09045 |
TRZ/ATZ family hydrolase; |
12-61 |
8.77e-03 |
|
TRZ/ATZ family hydrolase;
Pssm-ID: 236366 [Multi-domain] Cd Length: 443 Bit Score: 38.35 E-value: 8.77e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 445929010 12 VILENEArvidIAVQGGKIAAIGENLG-----EAKNVLDATGLIVSPGMVDAHTH 61
Cdd:PRK09045 24 VVLEDHA----VAIRDGRIVAILPRAEararyAAAETVELPDHVLIPGLINAHTH 74
|
|
| |
