|
Name |
Accession |
Description |
Interval |
E-value |
| DHOase_IIa |
cd01317 |
Dihydroorotase (DHOase), subgroup IIa; DHOases catalyze the reversible interconversion of ... |
37-493 |
5.66e-149 |
|
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: 430.89 E-value: 5.66e-149
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925976 37 DGADIDATGLTLAPGFEDPHVHFRDPGQTYKESMVSGCRASASGGYTNVLIMPNTLPALDGqtvtdasapgakevldagf 116
Cdd:cd01317 1 DAEVIDAEGKILAPGLVDLHVHLREPGFEYKETLESGAKAAAAGGFTTVVCMPNTNPVIDN------------------- 61
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925976 117 DNVIDFLQQYdaAHNVkLPVRYDLCVCASKDRAGHEASDVADWLKY-VPGFEDDAKTpamlahpvtavsddgsAVTPKIL 195
Cdd:cd01317 62 PAVVELLKNR--AKDV-GIVRVLPIGALTKGLKGEELTEIGELLEAgAVGFSDDGKP----------------IQDAELL 122
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925976 196 DQVLENVKTSDLYLIEHCEHHD---TGAVNEGPVSRELGVPGIPEDTELKIVARDIEAARRTGVHVHFQHVSTAISFEAI 272
Cdd:cd01317 123 RRALEYAAMLDLPIIVHPEDPSlagGGVMNEGKVASRLGLPGIPPEAETIMVARDLELAEATGARVHFQHLSTARSLELI 202
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925976 273 RKAKAEGLPITCETAPHYLALSDEALLKYGTLAKMNPPLRSEADRKATIAAIADGTVDLLATDHAPHTLEEKELGFLEAP 352
Cdd:cd01317 203 RKAKAKGLPVTAEVTPHHLLLDDEALESYDTNAKVNPPLRSEEDREALIEALKDGTIDAIASDHAPHTDEEKDLPFAEAP 282
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925976 353 NGIIGLECAYGVCHKVLVDGGFISDERLIELMSVGPAELMGHaptdvaalvedyaepaptgedPDGVIageqvadaaESG 432
Cdd:cd01317 283 PGIIGLETALPLLWTLLVKGGLLTLPDLIRALSTNPAKILGL---------------------PPGRL---------EVG 332
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 489925976 433 ASQregvnrlldfshvddadavDLVVLDTAEEWTVDPEQFHSKARNTPFGGWQVTGRPLAT 493
Cdd:cd01317 333 APA-------------------DLVLFDPDAEWIVDEETFRSKSKNTPFDGQKLKGRVLAT 374
|
|
| pyrC |
PRK09357 |
dihydroorotase; Validated |
1-503 |
1.44e-138 |
|
dihydroorotase; Validated
Pssm-ID: 236479 [Multi-domain] Cd Length: 423 Bit Score: 406.12 E-value: 1.44e-138
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925976 1 MSITLRNIKVWN---TGEIIDLVVPGTAAAYFADTSSVVDGADIDATGLTLAPGFEDPHVHFRDPGQTYKESMVSGCRAS 77
Cdd:PRK09357 1 MMILIKNGRVIDpkgLDEVADVLIDDGKIAAIGENIEAEGAEVIDATGLVVAPGLVDLHVHLREPGQEDKETIETGSRAA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925976 78 ASGGYTNVLIMPNTLPALDgqtvtdaSAPGAKEVLDAGFDN-VIDFLQqydaahnvklpvrydlcVCA-SKDRAGHEASD 155
Cdd:PRK09357 81 AAGGFTTVVAMPNTKPVID-------TPEVVEYVLDRAKEAgLVDVLP-----------------VGAiTKGLAGEELTE 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925976 156 VAdwlkyvpgfeddaktpAMLAHPVTAVSDDGSAV-TPKILDQVLENVKTSDLYLIEHCEHHD---TGAVNEGPVSRELG 231
Cdd:PRK09357 137 FG----------------ALKEAGVVAFSDDGIPVqDARLMRRALEYAKALDLLIAQHCEDPSlteGGVMNEGEVSARLG 200
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925976 232 VPGIPEDTELKIVARDIEAARRTGVHVHFQHVSTAISFEAIRKAKAEGLPITCETAPHYLALSDEALLKYGTLAKMNPPL 311
Cdd:PRK09357 201 LPGIPAVAEEVMIARDVLLAEATGARVHICHVSTAGSVELIRWAKALGIKVTAEVTPHHLLLTDEDLLTYDPNYKVNPPL 280
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925976 312 RSEADRKATIAAIADGTVDLLATDHAPHTLEEKELGFLEAPNGIIGLECAYGVCHKVLVDGGFISDERLIELMSVGPAEL 391
Cdd:PRK09357 281 RTEEDREALIEGLKDGTIDAIATDHAPHAREEKECEFEAAPFGITGLETALSLLYTTLVKTGLLDLEQLLEKMTINPARI 360
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925976 392 MGHAPTDVAALvedyaEPAptgedpdgviageqvadaaesgasqregvnrlldfshvddadavDLVVLDTAEEWTVDPEQ 471
Cdd:PRK09357 361 LGLPAGPLAEG-----EPA--------------------------------------------DLVIFDPEAEWTVDGED 391
|
490 500 510
....*....|....*....|....*....|..
gi 489925976 472 FHSKARNTPFGGWQVTGRPLATIIGSKLMFSR 503
Cdd:PRK09357 392 FASKGKNTPFIGMKLKGKVVYTIVDGKIVYQD 423
|
|
| AllB |
COG0044 |
Dihydroorotase or related cyclic amidohydrolase [Nucleotide transport and metabolism]; ... |
5-503 |
4.52e-133 |
|
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: 392.53 E-value: 4.52e-133
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925976 5 LRNIKVWNTGEIID---LVVPGTAAAyFADTSSVVDGAD-IDATGLTLAPGFEDPHVHFRDPGQTYKESMVSGCRASASG 80
Cdd:COG0044 2 IKNGRVVDPGGLERadvLIEDGRIAA-IGPDLAAPEAAEvIDATGLLVLPGLIDLHVHLREPGLEHKEDIETGTRAAAAG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925976 81 GYTNVLIMPNTLPALDgqtvtdaSAPGAKEVLDAgfdnvidflqqydAAHnvKLPVRYDLCVCASKDRaGHEASDVADWL 160
Cdd:COG0044 81 GVTTVVDMPNTNPVTD-------TPEALEFKLAR-------------AEE--KALVDVGPHGALTKGL-GENLAELGALA 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925976 161 KY-VPGFEddaktpamlahpVTAVSDDGSAV-TPKILDQVLENVKTSDLYLIEHCEHHDT---GAVNEGPVSRELGVPGI 235
Cdd:COG0044 138 EAgAVAFK------------VFMGSDDGNPVlDDGLLRRALEYAAEFGALVAVHAEDPDLirgGVMNEGKTSPRLGLKGR 205
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925976 236 PEDTELKIVARDIEAARRTGVHVHFQHVSTAISFEAIRKAKAEGLPITCETAPHYLALSDEALLKYGTLAKMNPPLRSEA 315
Cdd:COG0044 206 PAEAEEEAVARDIALAEETGARLHIVHVSTAEAVELIREAKARGLPVTAEVCPHHLTLTDEDLERYGTNFKVNPPLRTEE 285
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925976 316 DRKATIAAIADGTVDLLATDHAPHTLEEKELGFLEAPNGIIGLECAYGVCHKVLVDGGFISDERLIELMSVGPAELMGHA 395
Cdd:COG0044 286 DREALWEGLADGTIDVIATDHAPHTLEEKELPFAEAPNGIPGLETALPLLLTELVHKGRLSLERLVELLSTNPARIFGLP 365
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925976 396 PTdvaalvedyaepaptgedpdGVIAgeqvadaaesgasqrEGvnrlldfshvddADAvDLVVLDTAEEWTVDPEQFHSK 475
Cdd:COG0044 366 RK--------------------GRIA---------------VG------------ADA-DLVLFDPDAEWTVTAEDLHSK 397
|
490 500
....*....|....*....|....*...
gi 489925976 476 ARNTPFGGWQVTGRPLATIIGSKLMFSR 503
Cdd:COG0044 398 SKNTPFEGRELTGRVVATIVRGRVVYED 425
|
|
| pyrC_multi |
TIGR00857 |
dihydroorotase, multifunctional complex type; In contrast to the homodimeric type of ... |
14-499 |
3.90e-95 |
|
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: 294.35 E-value: 3.90e-95
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925976 14 GEII--DLVVPGTAAAYFADTSSVVDGADIDATGLTLAPGFEDPHVHFRDPGQTYKESMVSGCRASASGGYTNVLIMPNT 91
Cdd:TIGR00857 1 GKETevDILVEGGRIKKIGKLRIPPDAEVIDAKGLLVLPGFIDLHVHLRDPGEEYKEDIESGSKAAAHGGFTTVADMPNT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925976 92 LPALDGQTVtdasapgakevldagFDNVIDFLQQydaahnvKLPVRYDLCVCASKDRAGHEasdvadwlkyvpgfedDAK 171
Cdd:TIGR00857 81 KPPIDTPET---------------LEWKLQRLKK-------VSLVDVHLYGGVTQGNQGKE----------------LTE 122
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925976 172 TPAMLAHPVTAV--SDDGSAV-TPKILDQVLENVKTSDLYLIEHCEHHDT---GAVNEGPVSRELGVPGIPEDTELKIVA 245
Cdd:TIGR00857 123 AYELKEAGAVGRmfTDDGSEVqDILSMRRALEYAAIAGVPIALHAEDPDLiygGVMHEGPSAAQLGLPARPPEAEEVAVA 202
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925976 246 RDIEAARRTGVHVHFQHVSTAISFEAIRKAKAEGLPITCETAPHYLALSDEALLKYGTLAKMNPPLRSEADRKATIAAIA 325
Cdd:TIGR00857 203 RLLELAKHAGCPVHICHISTKESLELIVKAKSQGIKITAEVTPHHLLLSEEDVARLDGNGKVNPPLREKEDRLALIEGLK 282
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925976 326 DGTVDLLATDHAPHTLEEKELGFLEAPNGIIGLECAYGvCHKVLVDGGFISDERLIELMSVGPAELMGhaptdvaalved 405
Cdd:TIGR00857 283 DGIIDIIATDHAPHTLEEKTKEFAAAPPGIPGLETALP-LLLQLLVKGLISLKDLIRMLSINPARIFG------------ 349
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925976 406 yaepaptgedpdgviageqvadaaesgasqregvnrLLDFSHVDDADAVDLVVLDTAEEWTVDPEQFHSKARNTPFGGWQ 485
Cdd:TIGR00857 350 ------------------------------------LPDKGTLEEGNPADITVFDLKKEWTINAETFYSKAKNTPFEGMS 393
|
490
....*....|....
gi 489925976 486 VTGRPLATIIGSKL 499
Cdd:TIGR00857 394 LKGKPIATILRGKV 407
|
|
| Amidohydro_1 |
pfam01979 |
Amidohydrolase family; This family of enzymes are a a large metal dependent hydrolase ... |
47-393 |
5.20e-08 |
|
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: 54.82 E-value: 5.20e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925976 47 TLAPGFEDPHVHFRD--------PGQTYKESMVSGCRASASGGYTNVLIMPNTlpaldgqtvTDASAPGAKEvldagfdn 118
Cdd:pfam01979 1 IVLPGLIDAHVHLEMgllrgipvPPEFAYEALRLGITTMLKSGTTTVLDMGAT---------TSTGIEALLE-------- 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925976 119 vidflqqydAAHNVKLPVRYDLCVCaSKDRAGHEASDVADWLKYVPGFE------DDAKTPAMLAHPVTAVSDDGsavtp 192
Cdd:pfam01979 64 ---------AAEELPLGLRFLGPGC-SLDTDGELEGRKALREKLKAGAEfikgmaDGVVFVGLAPHGAPTFSDDE----- 128
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925976 193 kiLDQVLENVKTSDLYLIEHCEHHD-TGAVNEGPVSRELGVPGIPEDTELKIVARDIEAARRTGVHVHfqhvstaisfea 271
Cdd:pfam01979 129 --LKAALEEAKKYGLPVAIHALETKgEVEDAIAAFGGGIEHGTHLEVAESGGLLDIIKLILAHGVHLS------------ 194
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925976 272 irkakaeglpitcetaPHYLALSDEALLKYGTLAKMNPPLRSEADRKATIAAIADGTVDLLATDHAPHTleeKELGFLEa 351
Cdd:pfam01979 195 ----------------PTEANLLAEHLKGAGVAHCPFSNSKLRSGRIALRKALEDGVKVGLGTDGAGSG---NSLNMLE- 254
|
330 340 350 360
....*....|....*....|....*....|....*....|..
gi 489925976 352 pngiiglECAYGVcHKVLVDGGFISDERLIELMSVGPAELMG 393
Cdd:pfam01979 255 -------ELRLAL-ELQFDPEGGLSPLEALRMATINPAKALG 288
|
|
| AdeC |
COG1001 |
Adenine deaminase [Nucleotide transport and metabolism]; |
5-59 |
3.61e-03 |
|
Adenine deaminase [Nucleotide transport and metabolism];
Pssm-ID: 440625 [Multi-domain] Cd Length: 559 Bit Score: 40.08 E-value: 3.61e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 489925976 5 LRNIKVWN--TGEII--DLVVpgtAAAYFADTSSVVDGAD--IDATGLTLAPGFEDPHVHF 59
Cdd:COG1001 9 IKNGRLVNvfTGEILegDIAI---AGGRIAGVGDYIGEATevIDAAGRYLVPGFIDGHVHI 66
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| DHOase_IIa |
cd01317 |
Dihydroorotase (DHOase), subgroup IIa; DHOases catalyze the reversible interconversion of ... |
37-493 |
5.66e-149 |
|
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: 430.89 E-value: 5.66e-149
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925976 37 DGADIDATGLTLAPGFEDPHVHFRDPGQTYKESMVSGCRASASGGYTNVLIMPNTLPALDGqtvtdasapgakevldagf 116
Cdd:cd01317 1 DAEVIDAEGKILAPGLVDLHVHLREPGFEYKETLESGAKAAAAGGFTTVVCMPNTNPVIDN------------------- 61
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925976 117 DNVIDFLQQYdaAHNVkLPVRYDLCVCASKDRAGHEASDVADWLKY-VPGFEDDAKTpamlahpvtavsddgsAVTPKIL 195
Cdd:cd01317 62 PAVVELLKNR--AKDV-GIVRVLPIGALTKGLKGEELTEIGELLEAgAVGFSDDGKP----------------IQDAELL 122
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925976 196 DQVLENVKTSDLYLIEHCEHHD---TGAVNEGPVSRELGVPGIPEDTELKIVARDIEAARRTGVHVHFQHVSTAISFEAI 272
Cdd:cd01317 123 RRALEYAAMLDLPIIVHPEDPSlagGGVMNEGKVASRLGLPGIPPEAETIMVARDLELAEATGARVHFQHLSTARSLELI 202
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925976 273 RKAKAEGLPITCETAPHYLALSDEALLKYGTLAKMNPPLRSEADRKATIAAIADGTVDLLATDHAPHTLEEKELGFLEAP 352
Cdd:cd01317 203 RKAKAKGLPVTAEVTPHHLLLDDEALESYDTNAKVNPPLRSEEDREALIEALKDGTIDAIASDHAPHTDEEKDLPFAEAP 282
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925976 353 NGIIGLECAYGVCHKVLVDGGFISDERLIELMSVGPAELMGHaptdvaalvedyaepaptgedPDGVIageqvadaaESG 432
Cdd:cd01317 283 PGIIGLETALPLLWTLLVKGGLLTLPDLIRALSTNPAKILGL---------------------PPGRL---------EVG 332
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 489925976 433 ASQregvnrlldfshvddadavDLVVLDTAEEWTVDPEQFHSKARNTPFGGWQVTGRPLAT 493
Cdd:cd01317 333 APA-------------------DLVLFDPDAEWIVDEETFRSKSKNTPFDGQKLKGRVLAT 374
|
|
| pyrC |
PRK09357 |
dihydroorotase; Validated |
1-503 |
1.44e-138 |
|
dihydroorotase; Validated
Pssm-ID: 236479 [Multi-domain] Cd Length: 423 Bit Score: 406.12 E-value: 1.44e-138
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925976 1 MSITLRNIKVWN---TGEIIDLVVPGTAAAYFADTSSVVDGADIDATGLTLAPGFEDPHVHFRDPGQTYKESMVSGCRAS 77
Cdd:PRK09357 1 MMILIKNGRVIDpkgLDEVADVLIDDGKIAAIGENIEAEGAEVIDATGLVVAPGLVDLHVHLREPGQEDKETIETGSRAA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925976 78 ASGGYTNVLIMPNTLPALDgqtvtdaSAPGAKEVLDAGFDN-VIDFLQqydaahnvklpvrydlcVCA-SKDRAGHEASD 155
Cdd:PRK09357 81 AAGGFTTVVAMPNTKPVID-------TPEVVEYVLDRAKEAgLVDVLP-----------------VGAiTKGLAGEELTE 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925976 156 VAdwlkyvpgfeddaktpAMLAHPVTAVSDDGSAV-TPKILDQVLENVKTSDLYLIEHCEHHD---TGAVNEGPVSRELG 231
Cdd:PRK09357 137 FG----------------ALKEAGVVAFSDDGIPVqDARLMRRALEYAKALDLLIAQHCEDPSlteGGVMNEGEVSARLG 200
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925976 232 VPGIPEDTELKIVARDIEAARRTGVHVHFQHVSTAISFEAIRKAKAEGLPITCETAPHYLALSDEALLKYGTLAKMNPPL 311
Cdd:PRK09357 201 LPGIPAVAEEVMIARDVLLAEATGARVHICHVSTAGSVELIRWAKALGIKVTAEVTPHHLLLTDEDLLTYDPNYKVNPPL 280
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925976 312 RSEADRKATIAAIADGTVDLLATDHAPHTLEEKELGFLEAPNGIIGLECAYGVCHKVLVDGGFISDERLIELMSVGPAEL 391
Cdd:PRK09357 281 RTEEDREALIEGLKDGTIDAIATDHAPHAREEKECEFEAAPFGITGLETALSLLYTTLVKTGLLDLEQLLEKMTINPARI 360
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925976 392 MGHAPTDVAALvedyaEPAptgedpdgviageqvadaaesgasqregvnrlldfshvddadavDLVVLDTAEEWTVDPEQ 471
Cdd:PRK09357 361 LGLPAGPLAEG-----EPA--------------------------------------------DLVIFDPEAEWTVDGED 391
|
490 500 510
....*....|....*....|....*....|..
gi 489925976 472 FHSKARNTPFGGWQVTGRPLATIIGSKLMFSR 503
Cdd:PRK09357 392 FASKGKNTPFIGMKLKGKVVYTIVDGKIVYQD 423
|
|
| AllB |
COG0044 |
Dihydroorotase or related cyclic amidohydrolase [Nucleotide transport and metabolism]; ... |
5-503 |
4.52e-133 |
|
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: 392.53 E-value: 4.52e-133
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925976 5 LRNIKVWNTGEIID---LVVPGTAAAyFADTSSVVDGAD-IDATGLTLAPGFEDPHVHFRDPGQTYKESMVSGCRASASG 80
Cdd:COG0044 2 IKNGRVVDPGGLERadvLIEDGRIAA-IGPDLAAPEAAEvIDATGLLVLPGLIDLHVHLREPGLEHKEDIETGTRAAAAG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925976 81 GYTNVLIMPNTLPALDgqtvtdaSAPGAKEVLDAgfdnvidflqqydAAHnvKLPVRYDLCVCASKDRaGHEASDVADWL 160
Cdd:COG0044 81 GVTTVVDMPNTNPVTD-------TPEALEFKLAR-------------AEE--KALVDVGPHGALTKGL-GENLAELGALA 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925976 161 KY-VPGFEddaktpamlahpVTAVSDDGSAV-TPKILDQVLENVKTSDLYLIEHCEHHDT---GAVNEGPVSRELGVPGI 235
Cdd:COG0044 138 EAgAVAFK------------VFMGSDDGNPVlDDGLLRRALEYAAEFGALVAVHAEDPDLirgGVMNEGKTSPRLGLKGR 205
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925976 236 PEDTELKIVARDIEAARRTGVHVHFQHVSTAISFEAIRKAKAEGLPITCETAPHYLALSDEALLKYGTLAKMNPPLRSEA 315
Cdd:COG0044 206 PAEAEEEAVARDIALAEETGARLHIVHVSTAEAVELIREAKARGLPVTAEVCPHHLTLTDEDLERYGTNFKVNPPLRTEE 285
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925976 316 DRKATIAAIADGTVDLLATDHAPHTLEEKELGFLEAPNGIIGLECAYGVCHKVLVDGGFISDERLIELMSVGPAELMGHA 395
Cdd:COG0044 286 DREALWEGLADGTIDVIATDHAPHTLEEKELPFAEAPNGIPGLETALPLLLTELVHKGRLSLERLVELLSTNPARIFGLP 365
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925976 396 PTdvaalvedyaepaptgedpdGVIAgeqvadaaesgasqrEGvnrlldfshvddADAvDLVVLDTAEEWTVDPEQFHSK 475
Cdd:COG0044 366 RK--------------------GRIA---------------VG------------ADA-DLVLFDPDAEWTVTAEDLHSK 397
|
490 500
....*....|....*....|....*...
gi 489925976 476 ARNTPFGGWQVTGRPLATIIGSKLMFSR 503
Cdd:COG0044 398 SKNTPFEGRELTGRVVATIVRGRVVYED 425
|
|
| pyrC_multi |
TIGR00857 |
dihydroorotase, multifunctional complex type; In contrast to the homodimeric type of ... |
14-499 |
3.90e-95 |
|
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: 294.35 E-value: 3.90e-95
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925976 14 GEII--DLVVPGTAAAYFADTSSVVDGADIDATGLTLAPGFEDPHVHFRDPGQTYKESMVSGCRASASGGYTNVLIMPNT 91
Cdd:TIGR00857 1 GKETevDILVEGGRIKKIGKLRIPPDAEVIDAKGLLVLPGFIDLHVHLRDPGEEYKEDIESGSKAAAHGGFTTVADMPNT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925976 92 LPALDGQTVtdasapgakevldagFDNVIDFLQQydaahnvKLPVRYDLCVCASKDRAGHEasdvadwlkyvpgfedDAK 171
Cdd:TIGR00857 81 KPPIDTPET---------------LEWKLQRLKK-------VSLVDVHLYGGVTQGNQGKE----------------LTE 122
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925976 172 TPAMLAHPVTAV--SDDGSAV-TPKILDQVLENVKTSDLYLIEHCEHHDT---GAVNEGPVSRELGVPGIPEDTELKIVA 245
Cdd:TIGR00857 123 AYELKEAGAVGRmfTDDGSEVqDILSMRRALEYAAIAGVPIALHAEDPDLiygGVMHEGPSAAQLGLPARPPEAEEVAVA 202
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925976 246 RDIEAARRTGVHVHFQHVSTAISFEAIRKAKAEGLPITCETAPHYLALSDEALLKYGTLAKMNPPLRSEADRKATIAAIA 325
Cdd:TIGR00857 203 RLLELAKHAGCPVHICHISTKESLELIVKAKSQGIKITAEVTPHHLLLSEEDVARLDGNGKVNPPLREKEDRLALIEGLK 282
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925976 326 DGTVDLLATDHAPHTLEEKELGFLEAPNGIIGLECAYGvCHKVLVDGGFISDERLIELMSVGPAELMGhaptdvaalved 405
Cdd:TIGR00857 283 DGIIDIIATDHAPHTLEEKTKEFAAAPPGIPGLETALP-LLLQLLVKGLISLKDLIRMLSINPARIFG------------ 349
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925976 406 yaepaptgedpdgviageqvadaaesgasqregvnrLLDFSHVDDADAVDLVVLDTAEEWTVDPEQFHSKARNTPFGGWQ 485
Cdd:TIGR00857 350 ------------------------------------LPDKGTLEEGNPADITVFDLKKEWTINAETFYSKAKNTPFEGMS 393
|
490
....*....|....
gi 489925976 486 VTGRPLATIIGSKL 499
Cdd:TIGR00857 394 LKGKPIATILRGKV 407
|
|
| DHOase_IIb |
cd01318 |
Dihydroorotase (DHOase), subgroup IIb; DHOases catalyze the reversible interconversion of ... |
45-496 |
1.25e-70 |
|
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: 229.14 E-value: 1.25e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925976 45 GLTLAPGFEDPHVHFRDPGQTYKESMVSGCRASASGGYTNVLIMPNTLPAldgqtVTDASAPGAKEVLDAGfDNVIDFL- 123
Cdd:cd01318 1 GLLILPGVIDIHVHFREPGLTYKEDFVSGSRAAAAGGVTTVMDMPNTKPP-----TTTAEALYEKLRLAAA-KSVVDYGl 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925976 124 -----QQYDAAHNVKLPVrydlcvcaskdrAGHE---ASDVADWLKYVPGFEDDAktpAMLAHPVTAvsddgsavtpkil 195
Cdd:cd01318 75 yfgvtGSEDLEELDKAPP------------AGYKifmGDSTGDLLDDEETLERIF---AEGSVLVTF------------- 126
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925976 196 dqvlenvktsdlylieHCEHHDTGAVNEGPVSRELGVPGI-PEDTELKIVARDIEAARRTGVHVHFQHVSTAISFEAIRK 274
Cdd:cd01318 127 ----------------HAEDEDRLRENRKELKGESAHPRIrDAEAAAVATARALKLARRHGARLHICHVSTPEELKLIKK 190
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925976 275 AKAEglpITCETAPHYLALSDEALLKYGTLAKMNPPLRSEADRKATIAAIADGTVDLLATDHAPHTLEEKELGFLEAPNG 354
Cdd:cd01318 191 AKPG---VTVEVTPHHLFLDVEDYDRLGTLGKVNPPLRSREDRKALLQALADGRIDVIASDHAPHTLEEKRKGYPAAPSG 267
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925976 355 IIGLECAYGVCHKvLVDGGFISDERLIELMSVGPAELMGhaptdvaalVEDYAEpaptgedpdgviageqvadaaesgas 434
Cdd:cd01318 268 IPGVETALPLMLT-LVNKGILSLSRVVRLTSHNPARIFG---------IKNKGR-------------------------- 311
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 489925976 435 QREGvnrlldfshvDDAdavDLVVLDTAEEWTVDPEQFHSKARNTPFGGWQVTGRPLATIIG 496
Cdd:cd01318 312 IAEG----------YDA---DLTVVDLKEERTIRAEEFHSKAGWTPFEGFEVTGFPVMTIVR 360
|
|
| PRK02382 |
PRK02382 |
dihydroorotase; Provisional |
1-485 |
2.70e-61 |
|
dihydroorotase; Provisional
Pssm-ID: 179417 [Multi-domain] Cd Length: 443 Bit Score: 207.20 E-value: 2.70e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925976 1 MSITLRNIKVWNTGEIID---LVVPGTAAAYFADTSSVVDGADIDATGLTLAPGFEDPHVHFRDPGQTYKESMVSGCRAS 77
Cdd:PRK02382 2 RDALLKDGRVYYNNSLQPrdvRIDGGKITAVGKDLDGSSSEEVIDARGMLLLPGGIDVHVHFREPGYTHKETWYTGSRSA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925976 78 ASGGYTNVLIMPNTLPaldgqTVTDASAPGAKEVLdAGFDNVIDFlqqydaahnvklpvrydlcvcaskdraGHEASDVA 157
Cdd:PRK02382 82 AAGGVTTVVDQPNTDP-----PTVDGESFDEKAEL-AARKSIVDF---------------------------GINGGVTG 128
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925976 158 DWlkyvpgfeddAKTPAMLAHPVTAV-------SDDGSAVTPKILDQVLENVKTSDLYLIEHCEHHDTGAVNEGPVSREL 230
Cdd:PRK02382 129 NW----------DPLESLWERGVFALgeifmadSTGGMGIDEELFEEALAEAARLGVLATVHAEDEDLFDELAKLLKGDA 198
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925976 231 GvPGI-----PEDTELKIVARDIEAARRTGVHVHFQHVSTAISFEAIRKAKaeglpITCETAPHYLALSDEALLKYGTLA 305
Cdd:PRK02382 199 D-ADAwsayrPAAAEAAAVERALEVASETGARIHIAHISTPEGVDAARREG-----ITCEVTPHHLFLSRRDWERLGTFG 272
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925976 306 KMNPPLRSEADRKATIAAIADGTVDLLATDHAPHTLEEKELGFLEAPNGIIGLECAYGVCHKVLVDGGFiSDERLIELMS 385
Cdd:PRK02382 273 KMNPPLRSEKRREALWERLNDGTIDVVASDHAPHTREEKDADIWDAPSGVPGVETMLPLLLAAVRKNRL-PLERVRDVTA 351
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925976 386 VGPAELMGHaptdvaalvedyaepaptgeDPDGVIAgeqvadaaesgasqrEGvnrlldfshvddADAvDLVVLDTAEEW 465
Cdd:PRK02382 352 ANPARIFGL--------------------DGKGRIA---------------EG------------YDA-DLVLVDPDAAR 383
|
490 500
....*....|....*....|
gi 489925976 466 TVDPEQFHSKARNTPFGGWQ 485
Cdd:PRK02382 384 EIRGDDLHSKAGWTPFEGME 403
|
|
| L-HYD_ALN |
cd01315 |
L-Hydantoinases (L-HYDs) and Allantoinase (ALN); L-Hydantoinases are a member of the ... |
5-495 |
1.56e-58 |
|
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: 200.21 E-value: 1.56e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925976 5 LRNIKVWNTGEII--DLVVPGTAAAYFADTSSVVDGAD-IDATGLTLAPGFEDPHVHFRDPGQTYKESMVSGCRASASGG 81
Cdd:cd01315 4 IKNGRVVTPDGVReaDIAVKGGKIAAIGPDIANTEAEEvIDAGGLVVMPGLIDTHVHINEPGRTEWEGFETGTKAAAAGG 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925976 82 YTNVLIMP-NTLPAldgqTVTDASapgakevldagfdnvidFLQQYDAAHNvKLPVrydlcvcaskdragheasDVADWL 160
Cdd:cd01315 84 ITTIIDMPlNSIPP----TTTVEN-----------------LEAKLEAAQG-KLHV------------------DVGFWG 123
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925976 161 KYVPGFEDDAKT---------PAMLAHPVTavsDDGSAVTPKILDQVLENVKTSDLYLIEHCE------HHDTGAVNEGP 225
Cdd:cd01315 124 GLVPGNLDQLRPldeagvvgfKCFLCPSGV---DEFPAVDDEQLEEAMKELAKTGSVLAVHAEnpeiteALQEQAKAKGK 200
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925976 226 VSRELGVPGIPEDTELKIVARDIEAARRTGVHVHFQHVSTAISFEAIRKAKAEGLPITCETAPHYLALSDEALLKYGTLA 305
Cdd:cd01315 201 RDYRDYLASRPVFTEVEAIQRILLLAKETGCRLHIVHLSSAEAVPLIREARAEGVDVTVETCPHYLTFTAEDVPDGGTEF 280
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925976 306 KMNPPLRSEADRKATIAAIADGTVDLLATDHAPHTLEEKELG---FLEAPNGIIGLECAYGVCHKVLVDGGFISDERLIE 382
Cdd:cd01315 281 KCAPPIRDAANQEQLWEALENGDIDMVVSDHSPCTPELKLLGkgdFFKAWGGISGLQLGLPVMLTEAVNKRGLSLEDIAR 360
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925976 383 LMSVGPAELMGHAPTdvaalvedyaepaptgedpDGVIAgeqvadaaesgasqrEGvnrlldfshvddADAvDLVVLDTA 462
Cdd:cd01315 361 LMCENPAKLFGLSHQ-------------------KGRIA---------------VG------------YDA-DFVVWDPE 393
|
490 500 510
....*....|....*....|....*....|...
gi 489925976 463 EEWTVDPEQFHSKARNTPFGGWQVTGRPLATII 495
Cdd:cd01315 394 EEFTVDAEDLYYKNKISPYVGRTLKGRVHATIL 426
|
|
| Cyclic_amidohydrolases |
cd01302 |
Cyclic amidohydrolases, including hydantoinase, dihydropyrimidinase, allantoinase, and ... |
50-493 |
2.72e-58 |
|
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: 196.07 E-value: 2.72e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925976 50 PGFEDPHVHFRDPGQT-YKESMVSGCRASASGGYTNVLIMPNTLPaldGQTVTDASApgaKEVLDAGFDNVIDFlqqydA 128
Cdd:cd01302 5 PGFIDIHVHLRDPGGTtYKEDFESGSRAAAAGGVTTVIDMPNTGP---PPIDLPAIE---LKIKLAEESSYVDF-----S 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925976 129 AHnvklpvrydlcvcaskdrAGHEASDVADWLKyvPGFEDDA---KTPAMLAHPVTAVSDDGSavtpkiLDQVLENVKTS 205
Cdd:cd01302 74 FH------------------AGIGPGDVTDELK--KLFDAGInslKVFMNYYFGELFDVDDGT------LMRTFLEIASR 127
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925976 206 DLYLIEHCEhhdtgavnegpvsrelgvpgipedtelkivaRDIEAARRTGVHVHFQHVSTAISFEAIRKAKAEGLPITCE 285
Cdd:cd01302 128 GGPVMVHAE-------------------------------RAAQLAEEAGANVHIAHVSSGEALELIKFAKNKGVKVTCE 176
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925976 286 TAPHYLALSDEALLKYGTLAKMNPPLRSEADRKATIAAIADGTVDLLATDHAPHTLEEKELG--FLEAPNGIIGLECAY- 362
Cdd:cd01302 177 VCPHHLFLDESMLRLNGAWGKVNPPLRSKEDREALWEGVKNGKIDTIASDHAPHSKEEKESGkdIWKAPPGFPGLETRLp 256
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925976 363 GVCHKVLVDGgfISDERLIELMSVGPAELMghaptdvaalvedyaepaptGEDPDGVIAgeqvadaaeSGASQregvnrl 442
Cdd:cd01302 257 ILLTEGVKRG--LSLETLVEILSENPARIF--------------------GLYPKGTIA---------VGYDA------- 298
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|.
gi 489925976 443 ldfshvddadavDLVVLDTAEEWTVDPEQFHSKARNTPFGGWQVTGRPLAT 493
Cdd:cd01302 299 ------------DLVIVDPKKEWKVTAEEIESKADWTPFEGMEVTGKPVST 337
|
|
| PRK09059 |
PRK09059 |
dihydroorotase; Validated |
24-502 |
4.95e-57 |
|
dihydroorotase; Validated
Pssm-ID: 181631 [Multi-domain] Cd Length: 429 Bit Score: 195.64 E-value: 4.95e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925976 24 TAAAYFADTSSVVDGADI-DATGLTLAPGFEDPHVHFRDPGQTYKESMVSGCRASASGGYTNVLIMPNTLPALDGQTVTD 102
Cdd:PRK09059 33 VAAGKGAGNQGAPEGAEIvDCAGKAVAPGLVDARVFVGEPGAEHRETIASASRAAAAGGVTSIIMMPDTDPVIDDVALVE 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925976 103 ASAPGAKEVldagfdnvidflqqydAAHNVKlPVrydlcVCASKDRAGHEASDVadwlkyvpGFEDDAKtpamlahpVTA 182
Cdd:PRK09059 113 FVKRTARDT----------------AIVNIH-PA-----AAITKGLAGEEMTEF--------GLLRAAG--------AVA 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925976 183 VSDDGSAVT-PKILDQVLENVKTSDLYLIEHCEHHD---TGAVNEGPVSRELGVPGIPEDTELKIVARDIEAARRTGVHV 258
Cdd:PRK09059 155 FTDGRRSVAnTQVMRRALTYARDFDAVIVHETRDPDlggNGVMNEGLFASWLGLSGIPREAEVIPLERDLRLAALTRGRY 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925976 259 HFQHVSTAISFEAIRKAKAEGLPITCETAPHYLALSDEALLKYGTLAKMNPPLRSEADRKATIAAIADGTVDLLATDHAP 338
Cdd:PRK09059 235 HAAQISCAESAEALRRAKDRGLKVTAGVSINHLSLNENDIGEYRTFFKLSPPLRTEDDRVAMVEAVASGTIDIIVSSHDP 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925976 339 HTLEEKELGFLEAPNGIIGLECAYGVCHKvLVDGGFISDERLIELMSVGPAELMGHaptdvaalvedyaePAPTgedpdg 418
Cdd:PRK09059 315 QDVDTKRLPFSEAAAGAIGLETLLAAALR-LYHNGEVPLLRLIEALSTRPAEIFGL--------------PAGT------ 373
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925976 419 viageqvadaAESGAsqregvnrlldfshvddadAVDLVVLDTAEEWTVDPEQFHSKARNTPFGGWQVTGRPLATIIGSK 498
Cdd:PRK09059 374 ----------LKPGA-------------------PADIIVIDLDEPWVVDPEDLKSRSKNTPFEEARFQGRVVRTIVAGK 424
|
....
gi 489925976 499 LMFS 502
Cdd:PRK09059 425 TVYE 428
|
|
| PRK07369 |
PRK07369 |
dihydroorotase; Provisional |
41-493 |
1.37e-55 |
|
dihydroorotase; Provisional
Pssm-ID: 236002 [Multi-domain] Cd Length: 418 Bit Score: 191.35 E-value: 1.37e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925976 41 IDATGLTLAPGFEDPHVHFRDPGQTYKESMVSGCRASASGGYTNVLIMPNTLPALDGqtvtdasaPGAkevldagfdnvI 120
Cdd:PRK07369 48 IDASGLILGPGLVDLYSHSGEPGFEERETLASLAAAAAAGGFTRVAILPDTFPPLDN--------PAT-----------L 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925976 121 DFLQQYDAAhnvKLPVRYDLCVCASKDRAGHEASDVADWLKY-VPGFeddaktpamlahpvtavSDDGSAVTPKILDQVL 199
Cdd:PRK07369 109 ARLQQQAQQ---IPPVQLHFWGALTLGGQGKQLTELAELAAAgVVGF-----------------TDGQPLENLALLRRLL 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925976 200 ENVKT---------SDLYLiehcehHDTGAVNEGPVSRELGVPGIPEDTELKIVARDIEAARRTGVHVHFQHVSTAISFE 270
Cdd:PRK07369 169 EYLKPlgkpvalwpCDRSL------AGNGVMREGLLALRLGLPGDPASAETTALAALLELVAAIGTPVHLMRISTARSVE 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925976 271 AIRKAKAEGLPITCETAPHYLALSDEALLKYGTLAKMNPPLRSEADRKATIAAIADGTVDLLATDHAPHTLEEKELGFLE 350
Cdd:PRK07369 243 LIAQAKARGLPITASTTWMHLLLDTEALASYDPNLRLDPPLGNPSDRQALIEGVRTGVIDAIAIDHAPYTYEEKTVAFAE 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925976 351 APNGIIGLECAYGVCHKVLVDGGFISDERLIELMSVGPAELMGHAPTDVAalVEDYAEpaptgedpdgviageqvadaae 430
Cdd:PRK07369 323 APPGAIGLELALPLLWQNLVETGELSALQLWQALSTNPARCLGQEPPSLA--PGQPAE---------------------- 378
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 489925976 431 sgasqregvnrlldfshvddadavdLVVLDTAEEWTVDPEQFHSKARNTPFGGWQVTGRPLAT 493
Cdd:PRK07369 379 -------------------------LILFDPQKTWTVSAQTLHSLSRNTPWLGQTLKGRVLQT 416
|
|
| PRK07575 |
PRK07575 |
dihydroorotase; Provisional |
1-503 |
2.28e-55 |
|
dihydroorotase; Provisional
Pssm-ID: 236055 [Multi-domain] Cd Length: 438 Bit Score: 191.43 E-value: 2.28e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925976 1 MSITLRNIK-VWNTGEII--DLVVPGTAAAYFADTSSVVDGAD-IDATGLTLAPGFEDPHVHFRDPGQTYKESMVSGCRA 76
Cdd:PRK07575 3 MSLLIRNARiLLPSGELLlgDVLVEDGKIVAIAPEISATAVDTvIDAEGLTLLPGVIDPQVHFREPGLEHKEDLFTASRA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925976 77 SASGGYTNVLIMPNTLP-ALDGQTVTDASAPGA-KEVLDAGF------DNVIDfLQQYDAAHNVKLPVrydlcvcaskdr 148
Cdd:PRK07575 83 CAKGGVTSFLEMPNTKPlTTTQAALDDKLARAAeKCVVNYGFfigatpDNLPE-LLTANPTCGIKIFM------------ 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925976 149 agheasdvadwlkyvpgfeddaktpamlahpvtavsddGSAVTPKILDQ--VLENVKTSDLYLIE-HCEhhDTGAVNEgp 225
Cdd:PRK07575 150 --------------------------------------GSSHGPLLVDEeaALERIFAEGTRLIAvHAE--DQARIRA-- 187
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925976 226 vsRELGVPGIPE--------DTELKIVA--RDIEAARRTGVHVHFQHVSTAISFEAIRKAKaeGLPITCETAPHYLALSD 295
Cdd:PRK07575 188 --RRAEFAGISDpadhsqiqDEEAALLAtrLALKLSKKYQRRLHILHLSTAIEAELLRQDK--PSWVTAEVTPQHLLLNT 263
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925976 296 EALLKYGTLAKMNPPLRSEADRKATIAAIADGTVDLLATDHAPHTLEEKELGFLEAPNGIIGLECAYGVCHKVLVDgGFI 375
Cdd:PRK07575 264 DAYERIGTLAQMNPPLRSPEDNEALWQALRDGVIDFIATDHAPHTLEEKAQPYPNSPSGMPGVETSLPLMLTAAMR-GKC 342
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925976 376 SDERLIELMSVGPAELMGhaptdvaalvedyaepaptgedpdgvIAGEqvaDAAESGAsqregvnrlldfshvdDADAVd 455
Cdd:PRK07575 343 TVAQVVRWMSTAVARAYG--------------------------IPNK---GRIAPGY----------------DADLV- 376
|
490 500 510 520
....*....|....*....|....*....|....*....|....*...
gi 489925976 456 LVVLDTAEewTVDPEQFHSKARNTPFGGWQVTGRPLATIIGSKLMFSR 503
Cdd:PRK07575 377 LVDLNTYR--PVRREELLTKCGWSPFEGWNLTGWPVTTIVGGQIVFDR 422
|
|
| PRK09060 |
PRK09060 |
dihydroorotase; Validated |
14-500 |
7.14e-50 |
|
dihydroorotase; Validated
Pssm-ID: 181632 [Multi-domain] Cd Length: 444 Bit Score: 177.03 E-value: 7.14e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925976 14 GEIIDLVVPGTAAAyfadtssvvdGADIDATGLTLAPGFEDPHVHFRDPGQTYKESMVSGCRASASGGYTNVLIMPNTLP 93
Cdd:PRK09060 30 GRIAAIGDLSGASA----------GEVIDCRGLHVLPGVIDSQVHFREPGLEHKEDLETGSRAAVLGGVTAVFEMPNTNP 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925976 94 aldgqTVTDASAPGAKevldagfdnvidflqqYDAAHNvKLPVRYDLCVCASKDRAGHEASdvadwLKYVPG------FE 167
Cdd:PRK09060 100 -----LTTTAEALADK----------------LARARH-RMHCDFAFYVGGTRDNADELAE-----LERLPGcagikvFM 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925976 168 DdAKTPAMLahpvtaVSDDGSavtpkiLDQVLENVKTSDLYlieHCEhhDTGAVNEgpvSRELGVPGipeDTELKIVARD 247
Cdd:PRK09060 153 G-SSTGDLL------VEDDEG------LRRILRNGRRRAAF---HSE--DEYRLRE---RKGLRVEG---DPSSHPVWRD 208
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925976 248 IEAA-----------RRTGVHVHFQHVSTAISFEAIRKAKAEglpITCETAPHYLALS-DEALLKYGTLAKMNPPLRSEA 315
Cdd:PRK09060 209 EEAAllatrrlvrlaRETGRRIHVLHVSTAEEIDFLADHKDV---ATVEVTPHHLTLAaPECYERLGTLAQMNPPIRDAR 285
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925976 316 DRKATIAAIADGTVDLLATDHAPHTLEEKELGFLEAPNGIIGLECAYGVC--HkvlVDGGFISDERLIELMSVGPAELMG 393
Cdd:PRK09060 286 HRDGLWRGVRQGVVDVLGSDHAPHTLEEKAKPYPASPSGMTGVQTLVPIMldH---VNAGRLSLERFVDLTSAGPARIFG 362
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925976 394 HAPTdvaalvedyaepaptgedpdGVIAgeqvadaaesgasqrEGVnrlldfshvdDAdavDLVVLDTAEEWTVDPEQFH 473
Cdd:PRK09060 363 IAGK--------------------GRIA---------------VGY----------DA---DFTIVDLKRRETITNEWIA 394
|
490 500
....*....|....*....|....*...
gi 489925976 474 SKARNTPFGGWQVTGRPLATII-GSKLM 500
Cdd:PRK09060 395 SRCGWTPYDGKEVTGWPVGTIVrGQRVM 422
|
|
| PRK09236 |
PRK09236 |
dihydroorotase; Reviewed |
1-501 |
1.50e-49 |
|
dihydroorotase; Reviewed
Pssm-ID: 181716 Cd Length: 444 Bit Score: 175.83 E-value: 1.50e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925976 1 MSITLRNIKVWNTGEIID---LVVPGTAAAYFADTSSVVDGADIDATGLTLAPGFEDPHVHFRDPGQTYKESMVSGCRAS 77
Cdd:PRK09236 2 KRILIKNARIVNEGKIFEgdvLIENGRIAKIASSISAKSADTVIDAAGRYLLPGMIDDQVHFREPGLTHKGDIASESRAA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925976 78 ASGGYTNVLIMPNTLPaldgQTVTDAsAPGAKEVLDA-------GF------DNvIDFLQQYDAAHnvklpvrydlcVCA 144
Cdd:PRK09236 82 VAGGITSFMEMPNTNP----PTTTLE-ALEAKYQIAAqrslanySFyfgatnDN-LDEIKRLDPKR-----------VCG 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925976 145 SKDRAGheasdvadwlkyvpgfeddAKTPAMLAhpvtavsDDgsavtPKILDQVLENvktSDLYLIEHCEHHDTGAVNEG 224
Cdd:PRK09236 145 VKVFMG-------------------ASTGNMLV-------DN-----PETLERIFRD---APTLIATHCEDTPTIKANLA 190
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925976 225 PVSRELGVPgIPEDTELKIvaRDIEA-----------ARRTGVHVHFQHVSTAISFEAIRKAKAEGLPITCETAPHYLAL 293
Cdd:PRK09236 191 KYKEKYGDD-IPAEMHPLI--RSAEAcykssslavslAKKHGTRLHVLHISTAKELSLFENGPLAEKRITAEVCVHHLWF 267
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925976 294 SDEALLKYGTLAKMNPPLRSEADRKATIAAIADGTVDLLATDHAPHTLEEKELGFLEAPNG--------IIGLEcaygvc 365
Cdd:PRK09236 268 DDSDYARLGNLIKCNPAIKTASDREALRQALADDRIDVIATDHAPHTWEEKQGPYFQAPSGlplvqhalPALLE------ 341
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925976 366 hkvLVDGGFISDERLIELMSVGPAELMGhaptdvaalVEDyaepaptgedpDGVIageqvadaaesgasqREGVnrlldf 445
Cdd:PRK09236 342 ---LVHEGKLSLEKVVEKTSHAPAILFD---------IKE-----------RGFI---------------REGY------ 377
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*.
gi 489925976 446 shvddadAVDLVVLDTAEEWTVDPEQFHSKARNTPFGGWQVTGRPLATIIGSKLMF 501
Cdd:PRK09236 378 -------WADLVLVDLNSPWTVTKENILYKCGWSPFEGRTFRSRVATTFVNGQLVY 426
|
|
| allantoinase |
TIGR03178 |
allantoinase; This enzyme carries out the first step in the degradation of allantoin, a ... |
41-495 |
2.65e-48 |
|
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: 172.57 E-value: 2.65e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925976 41 IDATGLTLAPGFEDPHVHFRDPGQTYKESMVSGCRASASGGYTNVLIMP-NTLPAldgqTVTDASapgakevldagfdnv 119
Cdd:TIGR03178 42 IDAGGLVVFPGVVDTHVHINEPGRTEWEGFETGTRAAAAGGITTYIDMPlNSIPA----TTTRAS--------------- 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925976 120 idFLQQYDAAhnvklpvrydlcvcaskdrAGHEASDVADWLKYVPGFEDDakTPAMLAHPVTAV--------SDDGSAVT 191
Cdd:TIGR03178 103 --LEAKFEAA-------------------KGKLAVDVGFWGGLVPYNLDD--LRELDEAGVVGFkaflspsgDDEFPHVD 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925976 192 PKILDQVLENVKTSDLYLIEHCE---HHD---TGAVNEGPVSRELGVPGIPEDTELKIVARDIEAARRTGVHVHFQHVST 265
Cdd:TIGR03178 160 DWQLYKGMRELARLGQLLLVHAEnpaITSalgEEAPPQGGVGADAYLASRPVFAEVEAIRRTLALAKVTGCRVHVVHLSS 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925976 266 AISFEAIRKAKAEGLPITCETAPHYLALSDEALLKYGTLAKMNPPLRSEADRKATIAAIADGTVDLLATDHAPHTLEEKE 345
Cdd:TIGR03178 240 AEAVELITEAKQEGLDVTVETCPHYLTLTAEEVPDGGTLAKCAPPIRDLANQEGLWEALLNGLIDCVVSDHSPCTPDLKR 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925976 346 LG-FLEAPNGIIGLECAYGVCHKVLVDGGFISDERLIELMSVGPAELMGHAPTdvaalvedyaepaptgedpdGVIAGeq 424
Cdd:TIGR03178 320 AGdFFKAWGGIAGLQSTLDVMFDEAVQKRGLPLEDIARLMATNPAKRFGLAQK--------------------GRIAP-- 377
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 489925976 425 vadaaesgasqregvnrlldfshvdDADAvDLVVLDTAEEWTVDPEQFHSKARNTPFGGWQVTGRPLATII 495
Cdd:TIGR03178 378 -------------------------GKDA-DFVFVDPDESYTLTPDDLYYRHKVSPYVGRTIGGRVRATYL 422
|
|
| PRK08417 |
PRK08417 |
metal-dependent hydrolase; |
30-393 |
7.27e-44 |
|
metal-dependent hydrolase;
Pssm-ID: 236262 [Multi-domain] Cd Length: 386 Bit Score: 159.10 E-value: 7.27e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925976 30 ADTSSVVDGADI-DATGLTLAPGFEDPHVHFRDPGQTYK--ESMVSGCRAsasGGYTNVLIMPNTLPALDGQtvtdasap 106
Cdd:PRK08417 9 TEIGSDLKGEEIlDAKGKTLLPALVDLNVSLKNDSLSSKnlKSLENECLK---GGVGSIVLYPDSTPAIDNE-------- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925976 107 gakevldagfdNVIDFLQQYDaaHNVKLPVRYDLCVCASKDRAgheaSDVADWLKYvpgfedDAKTPAMlahpvtavsdd 186
Cdd:PRK08417 78 -----------IALELINSAQ--RELPMQIFPSIRALDEDGKL----SNIATLLKK------GAKALEL----------- 123
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925976 187 GSAVTPKILDQVLENVKTSDLYLIEHCEHH---DTGAVNEGPVSRELGVPGIPEDTELKIVARDIEAARRTGVHVHFQHV 263
Cdd:PRK08417 124 SSDLDANLLKVIAQYAKMLDVPIFCRCEDSsfdDSGVMNDGELSFELGLPGIPSIAETKEVAKMKELAKFYKNKVLFDTL 203
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925976 264 STAISFEAIRKAKAEGLPITCETAPHYLALSDEALLKYGTLAKMNPPLRSEADRKATIAAIADGTVDLLATDHAPHTLEE 343
Cdd:PRK08417 204 ALPRSLELLDKFKSEGEKLLKEVSIHHLILDDSACENFNTAAKLNPPLRSKEDRLALLEALKEGKIDFLTSLHSAKSNSK 283
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|
gi 489925976 344 KELGFLEAPNGIIGLECAYGVCHKVLVDGGFISDERLIELMSVGPAELMG 393
Cdd:PRK08417 284 KDLAFDEAAFGIDSICEYFSLCYTYLVKEGIITWSELSRFTSYNPAQFLG 333
|
|
| PRK06189 |
PRK06189 |
allantoinase; Provisional |
18-494 |
5.39e-41 |
|
allantoinase; Provisional
Pssm-ID: 235732 [Multi-domain] Cd Length: 451 Bit Score: 152.93 E-value: 5.39e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925976 18 DLVVPGTAAAYFADTSSVVDGADIDATGLTLAPGFEDPHVHFRDPGQTYKESMVSGCRASASGGYTNVLIMP-NTLPAld 96
Cdd:PRK06189 22 DIGIKNGKIAEIAPEISSPAREIIDADGLYVFPGMIDVHVHFNEPGRTHWEGFATGSAALAAGGCTTYFDMPlNSIPP-- 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925976 97 gqTVTdasapgaKEVLDAgfdnvidflqqydaahnvklpvrydlcvcasKDRAGHEAS--DVADWLKYVPGFEDDAKT-- 172
Cdd:PRK06189 100 --TVT-------REALDA-------------------------------KAELARQKSavDFALWGGLVPGNLEHLREla 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925976 173 -------PAMLAHPVTavsDDGSAVTPKILDQVLENVKTSDLYLIEHCE------HHDTGAVNEGPVSRELGVPGIPEDT 239
Cdd:PRK06189 140 eagvigfKAFMSNSGT---DEFRSSDDLTLYEGMKEIAALGKILALHAEsdaltrHLTTQARQQGKTDVRDYLESRPVVA 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925976 240 ELKIVARDIEAARRTGVHVHFQHVSTAISFEAIRKAKAEGLPITCETAPHYLALSDEALLKYGTLAKMNPPLRSEADRKA 319
Cdd:PRK06189 217 ELEAVQRALLYAQETGCPLHFVHISSGKAVALIAEAKKRGVDVSVETCPHYLLFTEEDFERIGAVAKCAPPLRSRSQKEE 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925976 320 TIAAIADGTVDLLATDHAPHTLEEKE-LGFLEAPNGIIGLECAYGVchkVLVDGGF---ISDERLIELMSVGPAELMGHA 395
Cdd:PRK06189 297 LWRGLLAGEIDMISSDHSPCPPELKEgDDFFLVWGGISGGQSTLLV---MLTEGYIergIPLETIARLLATNPAKRFGLP 373
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925976 396 PTdvaalvedyaepaptgedpdGVIAgeqvadaaesgasqrEGvnrlldfshvddADAvDLVVLDTAEEWTVDPEQFHSK 475
Cdd:PRK06189 374 QK--------------------GRLE---------------VG------------ADA-DFVLVDLDETYTLTKEDLFYR 405
|
490
....*....|....*....
gi 489925976 476 ARNTPFGGWQVTGRPLATI 494
Cdd:PRK06189 406 HKQSPYEGRTFPGRVVATY 424
|
|
| PRK07627 |
PRK07627 |
dihydroorotase; Provisional |
23-503 |
1.22e-40 |
|
dihydroorotase; Provisional
Pssm-ID: 181059 [Multi-domain] Cd Length: 425 Bit Score: 151.37 E-value: 1.22e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925976 23 GTAAAYFADTSSvvdgadIDATGLTLAPGFEDPHVHFRDPGQTYKESMVSGCRASASGGYTNVLIMPNTLPALDgqtvtd 102
Cdd:PRK07627 34 GQAPAGFNADKT------IDASGLIVCPGLVDLSARLREPGYEYKATLESEMAAAVAGGVTSLVCPPDTDPVLD------ 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925976 103 asAPGAKEVLDAgfdnvidflqqydAAHNVKLPVRYDLCVCASKDR--------AGHEASDVadwlkyvpGFEDdAKTPA 174
Cdd:PRK07627 102 --EPGLVEMLKF-------------RARNLNQAHVYPLGALTVGLKgevltemvELTEAGCV--------GFSQ-ANVPV 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925976 175 mlahpvtavsddgsaVTPKILDQVLENVKT---------SDLYLIEHcehhdtGAVNEGPVSRELGVPGIPEDTELKIVA 245
Cdd:PRK07627 158 ---------------VDTQVLLRALQYASTfgftvwlrpLDAFLGRG------GVAASGAVASRLGLSGVPVAAETIALH 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925976 246 RDIEAARRTGVHVHFQHVSTAISFEAIRKAKAEGLPITCETAPHYLALSDEALLKYGTLAKMNPPLRSEADRKATIAAIA 325
Cdd:PRK07627 217 TIFELMRVTGARVHLARLSSAAGVALVRAAKAEGLPVTCDVGVNHVHLIDVDIGYFDSQFRLDPPLRSQRDREAIRAALA 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925976 326 DGTVDLLATDHAPHTLEEKELGFLEAPNGIIGLECAYGVCHKvlvdggfISDERLIELmsvgpaelmghaptdVAALVED 405
Cdd:PRK07627 297 DGTIDAICSDHTPVDDDEKLLPFAEATPGATGLELLLPLTLK-------WADEAKVPL---------------ARALARI 354
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925976 406 YAEPAptgeDPDGVIAGEQVADAaesgasqregvnrlldfshvddadAVDLVVLDTAEEWTVDPEQFHSKARNTPFGGWQ 485
Cdd:PRK07627 355 TSAPA----RVLGLPAGRLAEGA------------------------PADLCVFDPDAHWRVEPRALKSQGKNTPFLGYE 406
|
490
....*....|....*...
gi 489925976 486 VTGRPLATIIGSKLMFSR 503
Cdd:PRK07627 407 LPGRVRATLVAGQVAFER 424
|
|
| PRK04250 |
PRK04250 |
dihydroorotase; Provisional |
41-500 |
3.51e-40 |
|
dihydroorotase; Provisional
Pssm-ID: 235265 [Multi-domain] Cd Length: 398 Bit Score: 149.53 E-value: 3.51e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925976 41 IDATGLTLAPGFEDPHVHFRDPGQTYKESMVSGCRASASGGYTNVLIMPNTLPALDGQTVTDasapgaKEVLDAGFDNVI 120
Cdd:PRK04250 38 IKVKGGIILPGLIDVHVHLRDFEESYKETIESGTKAALHGGITLVFDMPNTKPPIMDEKTYE------KRMRIAEKKSYA 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925976 121 DFLQQYDAAHNVKL--PVRYDLcvcaSKDRAGHEASDVadwlkYVPGFEDDAKTpamlahpvtavsddgsavTPKILdqv 198
Cdd:PRK04250 112 DYALNFLIAGNCEKaeEIKADF----YKIFMGASTGGI-----FSENFEVDYAC------------------APGIV--- 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925976 199 leNVktsdlylieHCEhhDTGAVNEGPVSrelgvpgiPEDTELKIVARDIEAARRTGVHVHFQHVSTAISFEAIRKAkae 278
Cdd:PRK04250 162 --SV---------HAE--DPELIREFPER--------PPEAEVVAIERALEAGKKLKKPLHICHISTKDGLKLILKS--- 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925976 279 GLP-ITCETAPHYLALSDEALlKYGTLAKMNPPLRSEADRKATIAAIAdgTVDLLATDHAPHTLEEKELGfleAPnGIIG 357
Cdd:PRK04250 218 NLPwVSFEVTPHHLFLTRKDY-ERNPLLKVYPPLRSEEDRKALWENFS--KIPIIASDHAPHTLEDKEAG---AA-GIPG 290
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925976 358 LECAYGVCHKvLVDGGFISDERLIELMSVGPAELMGhaptdvaalVEDYaepaptgedpdgviageqvadaaesgasqre 437
Cdd:PRK04250 291 LETEVPLLLD-AANKGMISLFDIVEKMHDNPARIFG---------IKNY------------------------------- 329
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 489925976 438 gvnrllDFSHVDDAdavDLVVLDTAEEWTVDPEQFHSKARNTPFGGWQVTGRPLATII-GSKLM 500
Cdd:PRK04250 330 ------GIEEGNYA---NFAVFDMKKEWTIKAEELYTKAGWTPYEGFKLKGKVIMTILrGEVVM 384
|
|
| PRK08044 |
PRK08044 |
allantoinase AllB; |
41-393 |
1.43e-34 |
|
allantoinase AllB;
Pssm-ID: 169193 [Multi-domain] Cd Length: 449 Bit Score: 134.98 E-value: 1.43e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925976 41 IDATGLTLAPGFEDPHVHFRDPGQTYKESMVSGCRASASGGYTNVLIMP-NTLPAldgqTVTDAS------APGAKEVLD 113
Cdd:PRK08044 44 MDASGLVVSPGMVDAHTHISEPGRSHWEGYETGTRAAAKGGITTMIEMPlNQLPA----TVDRASielkfdAAKGKLTID 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925976 114 AG-------FDnvIDFLQQYDAAHNVKlpvrYDLCVCASKDRA-GHEASDVADWlkyvpGFEDDAKTPAMLAHPVtAVSD 185
Cdd:PRK08044 120 AAqlgglvsYN--LDRLHELDEVGVVG----FKCFVATCGDRGiDNDFRDVNDW-----QFYKGAQKLGELGQPV-LVHC 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925976 186 DGSAVTPKILDQvlenvktsdlyliehcehhdtgAVNEGPVSRELGVPGIPEDTELKIVARDIEAARRTGVHVHFQHVST 265
Cdd:PRK08044 188 ENALICDELGEE----------------------AKREGRVTAHDYVASRPVFTEVEAIRRVLYLAKVAGCRLHVCHISS 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925976 266 AISFEAIRKAKAEGLPITCETAPHYLALSDEALLKYGTLAKMNPPLRSEADRKATIAAIADGTVDLLATDHAPHTLEEKE 345
Cdd:PRK08044 246 PEGVEEVTRARQEGQDVTCESCPHYFVLDTDQFEEIGTLAKCSPPIRDLENQKGMWEKLFNGEIDCLVSDHSPCPPEMKA 325
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|..
gi 489925976 346 LGFLEAPNGIIGLECaygvCHKVLVDGGF----ISDERLIELMSVGPAELMG 393
Cdd:PRK08044 326 GNIMEAWGGIAGLQN----CMDVMFDEAVqkrgMSLPMFGKLMATNAADIFG 373
|
|
| D-HYD |
cd01314 |
D-hydantoinases (D-HYD) also called dihydropyrimidases (DHPase) and related proteins; DHPases ... |
41-501 |
4.32e-33 |
|
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: 130.80 E-value: 4.32e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925976 41 IDATGLTLAPGFEDPHVHFRDP--GQTYKESMVSGCRASASGGYTnvlimpntlpaldgqTVTDASAPGAKEVLDAGFDN 118
Cdd:cd01314 42 IDATGKYVLPGGIDPHTHLELPfmGTVTADDFESGTRAAAAGGTT---------------TIIDFAIPNKGQSLLEAVEK 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925976 119 VIDFlqqydAAHNVklpvrydlcVCaskDRAGHEAsdVADWlkyvpGFEDDAKTPAMLAHPVTAVS-----DDGSAVTPK 193
Cdd:cd01314 107 WRGK-----ADGKS---------VI---DYGFHMI--ITDW-----TDSVIEELPELVKKGISSFKvfmayKGLLMVDDE 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925976 194 ILDQVLENVKTSDLYLIEHCEHHD--------------TGAVNEgPVSRelgvpgiPEDTELKIVARDIEAARRTGVHVH 259
Cdd:cd01314 163 ELLDVLKRAKELGALVMVHAENGDviaelqkkllaqgkTGPEYH-ALSR-------PPEVEAEATARAIRLAELAGAPLY 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925976 260 FQHVSTAISFEAIRKAKAEGLPITCETAPHYLALSDEALLK---YGTLAKMNPPLRSEADRKATIAAIADGTVDLLATDH 336
Cdd:cd01314 235 IVHVSSKEAADEIARARKKGLPVYGETCPQYLLLDDSDYWKdwfEGAKYVCSPPLRPKEDQEALWDGLSSGTLQTVGSDH 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925976 337 APHTLEEKELG---FLEAPNGIIGLECAYGVCHKVLVDGGFISDERLIELMSVGPAELMGHAPTdvaalvedyaepaptg 413
Cdd:cd01314 315 CPFNFAQKARGkddFTKIPNGVPGVETRMPLLWSEGVAKGRITLEKFVELTSTNPAKIFGLYPR---------------- 378
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925976 414 edpDGVIAGeqVADAaesgasqregvnrlldfshvddadavDLVVLDTAEEWTVDPEQFHSKARNTPFGGWQVTGRPLAT 493
Cdd:cd01314 379 ---KGTIAV--GSDA--------------------------DLVIWDPNAEKTISADTHHHNVDYNIFEGMKVKGWPVVT 427
|
....*...
gi 489925976 494 IIGSKLMF 501
Cdd:cd01314 428 ISRGKVVV 435
|
|
| PLN02795 |
PLN02795 |
allantoinase |
14-502 |
1.58e-31 |
|
allantoinase
Pssm-ID: 178392 [Multi-domain] Cd Length: 505 Bit Score: 127.20 E-value: 1.58e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925976 14 GEIIDLVVPGTAAAYFADTSSVVDGADidatgLTLAPGFEDPHVHFRDPGQTYKESMVSGCRASASGGYTNVLIMP-NTL 92
Cdd:PLN02795 68 GGRIVSVTKEEEAPKSQKKPHVLDYGN-----AVVMPGLIDVHVHLNEPGRTEWEGFPTGTKAAAAGGITTLVDMPlNSF 142
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925976 93 PaldgqTVTDASApgakevldagfdnvidfLQQYDAAHNVKLPVrydlcvcaskdragheasDVADWLKYVPgfeDDAKT 172
Cdd:PLN02795 143 P-----STTSVET-----------------LELKIEAAKGKLYV------------------DVGFWGGLVP---ENAHN 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925976 173 PAMLAHPVTAVS------------DDGSAVTPKILDQVLENVKTSDLYLIEHCEHHDTGAVNEG----PVSRELGVPGIP 236
Cdd:PLN02795 180 ASVLEELLDAGAlglksfmcpsgiNDFPMTTATHIKAALPVLAKYGRPLLVHAEVVSPVESDSRldadPRSYSTYLKSRP 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925976 237 EDTELKIVARDIEAARRT-------GVHVHFQHVSTAI-SFEAIRKAKAEGLPITCETAPHYLALSDEALLKYGTLAKMN 308
Cdd:PLN02795 260 PSWEQEAIRQLLEVAKDTrpggvaeGAHVHIVHLSDAEsSLELIKEAKAKGDSVTVETCPHYLAFSAEEIPDGDTRYKCA 339
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925976 309 PPLRSEADRKATIAAIADGTVDLLATDHAPHTLEEK---ELGFLEAPNGIIGLECAYGVCHKVLVDGGfISDERLIELMS 385
Cdd:PLN02795 340 PPIRDAANRELLWKALLDGDIDMLSSDHSPSPPDLKlleEGNFLRAWGGISSLQFVLPATWTAGRAYG-LTLEQLARWWS 418
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925976 386 VGPAELmghaptdvaalvedyaepapTGEDPDGVIAgeqvadaaesgasqregvnrlldFSHvdDAdavDLVVLDTAEEW 465
Cdd:PLN02795 419 ERPAKL--------------------AGLDSKGAIA-----------------------PGK--DA---DIVVWDPEAEF 450
|
490 500 510 520
....*....|....*....|....*....|....*....|
gi 489925976 466 TVD---PEQFHSKARnTPFGGWQVTGRPLATIIGSKLMFS 502
Cdd:PLN02795 451 VLDesyPIYHKHKSL-SPYLGTKLSGKVIATFVRGNLVFL 489
|
|
| D-hydantoinase |
TIGR02033 |
D-hydantoinase; This model represents the D-hydantoinase (dihydropyrimidinase) which primarily ... |
41-501 |
2.38e-31 |
|
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: 125.96 E-value: 2.38e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925976 41 IDATGLTLAPGFEDPHVHFRDP--GQTYKESMVSGCRASASGGYTNVLIMPNTLPaldGQTVTDASA-----PGAKEVLD 113
Cdd:TIGR02033 42 IDATGKYVLPGGIDVHTHLEMPfgGTTTADDFFTGTKAAAAGGTTTIIDFVVPEK---GSSLTEALEtwhekAEGKSVID 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925976 114 AGFDNVIDflqqyDAAHNVKlpvrydlcvcaskdragheasdvadwlkyvpgfedDAKTPAMLAHPVTAVS-----DDGS 188
Cdd:TIGR02033 119 YGFHMDIT-----HWNDSVL-----------------------------------EEHIPEVKEEGINSFKvfmayKNLL 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925976 189 AVTPKILDQVLENVKTSDLYLIEHCEHHDTGA------VNEG-------PVSRelgvpgiPEDTELKIVARDIEAARRTG 255
Cdd:TIGR02033 159 MVDDEELFEILKRLKELGALLQVHAENGDIIAelqarmLAQGitgpeyhALSR-------PPELEAEAVARAITLAALAD 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925976 256 VHVHFQHVSTAISFEAIRKAKAEGLPITCETAPHYLALSDEALLKYGTLAK---MNPPLRSEADRKATIAAIADGTVDLL 332
Cdd:TIGR02033 232 APLYVVHVSTKDAADEIAQARKKGQPVFGETCPQYLVLDDTHYDKPGFEGAkyvCSPPLREPEDQDALWSALSSGALQTV 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925976 333 ATDHAPHTLEEK-ELG---FLEAPNGIIGLECAYGVCHKVLVDGGFISDERLIELMSVGPAELMGHAPTdvaalvedyae 408
Cdd:TIGR02033 312 GSDHCTFNFAQKkAIGkddFTKIPNGGPGVEERMSLLFDEGVAKGRITLEKFVEVTSTNPAKIFNLYPR----------- 380
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925976 409 paptgedpDGVIAgeqvadaaesgasqrEGvnrlldfshvddADAvDLVVLDTAEEWTVDPEQFHSKARNTPFGGWQVTG 488
Cdd:TIGR02033 381 --------KGTIA---------------VG------------SDA-DIVIWDPNRTTVISAETHHSNADYNPFEGFKVRG 424
|
490
....*....|...
gi 489925976 489 RPLATIIGSKLMF 501
Cdd:TIGR02033 425 APVSVLSRGRVVV 437
|
|
| PRK08323 |
PRK08323 |
phenylhydantoinase; Validated |
1-494 |
7.42e-30 |
|
phenylhydantoinase; Validated
Pssm-ID: 236240 [Multi-domain] Cd Length: 459 Bit Score: 121.82 E-value: 7.42e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925976 1 MSITLRNIKVWNTGEIID---LVVPGTAAAYFADTSSVVdgadIDATGLTLAPGFEDPHVHFRDP--GQTYKESMVSGCR 75
Cdd:PRK08323 1 MSTLIKNGTVVTADDTYKadvLIEDGKIAAIGANLGDEV----IDATGKYVMPGGIDPHTHMEMPfgGTVSSDDFETGTR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925976 76 ASASGGYTnvlimpntlpaldgqTVTDASAPGAKEVLDAGfdnvidfLQQYD--AAHNvklpvrydlCVCaskDRAGHEA 153
Cdd:PRK08323 77 AAACGGTT---------------TIIDFALQPKGQSLREA-------LEAWHgkAAGK---------AVI---DYGFHMI 122
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925976 154 sdVADWlkyvpgfEDDAKT--PAMLAHPVTA-----------VSDDGSAVtpKILDQVLEN-----VktsdlylieHCEH 215
Cdd:PRK08323 123 --ITDW-------NEVVLDemPELVEEGITSfklfmaykgalMLDDDELL--RALQRAAELgalpmV---------HAEN 182
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925976 216 HD------TGAVNEG-------PVSRelgvpgiPEDTELKIVARDIEAARRTGVHVHFQHVSTAISFEAIRKAKAEGLPI 282
Cdd:PRK08323 183 GDaiaylqAKLLAEGktgpeyhALSR-------PPEVEGEATNRAIMLAELAGAPLYIVHVSCKEALEAIRRARARGQRV 255
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925976 283 TCETAPHYLALSDEALLKYGTL--AK--MNPPLRSEADRKATIAAIADGTVDLLATDHAPHTLE-EKELG---FLEAPNG 354
Cdd:PRK08323 256 FGETCPQYLLLDESEYDGPDWFegAKyvMSPPLRDKEHQDALWRGLQDGDLQVVATDHCPFCFEqKKQLGrgdFTKIPNG 335
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925976 355 IIGLECAYGVCHKVLVDGGFISDERLIELMSVGPAELMGHAPTdvaalvedyaepaptgedpDGVIAgeqvadaaesgas 434
Cdd:PRK08323 336 TPGVEDRMPLLFSEGVMTGRITLNRFVELTSTNPAKIFGLYPR-------------------KGTIA------------- 383
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925976 435 qrEGvnrlldfshvddADAvDLVVLDTAEEWTVDPEQFHSKARNTPFGGWQVTGRPLATI 494
Cdd:PRK08323 384 --VG------------ADA-DIVIWDPNATKTISASTLHSNVDYNPYEGFEVTGWPVTTL 428
|
|
| pyrC |
PRK00369 |
dihydroorotase; Provisional |
40-393 |
1.24e-24 |
|
dihydroorotase; Provisional
Pssm-ID: 234738 [Multi-domain] Cd Length: 392 Bit Score: 105.61 E-value: 1.24e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925976 40 DIDATGLTLA-PGFEDPHVHFRDPGQTYKESMVSGCRASASGGYTNVLIMPNTLPALDgqtvtdasapgAKEVLDAgfdn 118
Cdd:PRK00369 36 DLDLPQGTLIlPGAIDLHVHLRGLKLSYKEDVASGTSEAAYGGVTLVADMPNTIPPLN-----------TPEAITE---- 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925976 119 vidflqqydaahnvKLpvrydlcvcaskdrAGHEASDVADWLKYvPGFEDDAKTPAMLahPVTavsddGSAVTPKILDQ- 197
Cdd:PRK00369 101 --------------KL--------------AELEYYSRVDYFVY-SGVTKDPEKVDKL--PIA-----GYKIFPEDLERe 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925976 198 -VLENVKTSDLYLIEHCEHHDTGAVNegpvsRELGVPGIPEDTELKIVArdiEAARrtgvhVHFQHVStaiSFEAIRKAK 276
Cdd:PRK00369 145 eTFRVLLKSRKLKILHPEVPLALKSN-----RKLRRNCWYEIAALYYVK---DYQN-----VHITHAS---NPRTVRLAK 208
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925976 277 AEGLpiTCETAPHYLALSDEAllkyGTLAKMNPPLRSEADRKATIAAIADgtVDLLATDHAPHTLEEKELGFLEAPNGII 356
Cdd:PRK00369 209 ELGF--TVDITPHHLLVNGEK----DCLTKVNPPIRDINERLWLLQALSE--VDAIASDHAPHSSFEKLQPYEVCPPGIA 280
|
330 340 350
....*....|....*....|....*....|....*..
gi 489925976 357 GLECAYGVCHKvLVDGGFISDERLIELMSVGPAELMG 393
Cdd:PRK00369 281 ALSFTPPFIYT-LVSKGILSIDRAVELISTNPARILG 316
|
|
| PRK13404 |
PRK13404 |
dihydropyrimidinase; Provisional |
40-494 |
2.13e-24 |
|
dihydropyrimidinase; Provisional
Pssm-ID: 184033 [Multi-domain] Cd Length: 477 Bit Score: 105.94 E-value: 2.13e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925976 40 DIDATGLTLAPGFEDPHVHFRDP---GQTYKESMVSGCRASASGGYTNVLimPNTLPAlDGQTVTDASA-----PGAKEV 111
Cdd:PRK13404 44 EIDATGRLVLPGGVDSHCHIDQPsgdGIMMADDFYTGTVSAAFGGTTTVI--PFAAQH-RGQSLREAVEdyhrrAAGKAV 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925976 112 LDAGFDNVI-----DFLQQydaahnvKLPVRYdlcvcaskdRAGHEASDVadWLKYvpgfeDDAKtpamlahpvtaVSDD 186
Cdd:PRK13404 121 IDYAFHLIVadpteEVLTE-------ELPALI---------AQGYTSFKV--FMTY-----DDLK-----------LDDR 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925976 187 GsavtpkILDqVLENVKTSDLYLIEHCEHHDTGA-VNEGPVSRELGVPGI-----PEDTELKIVARDIEAARRTGVHVHF 260
Cdd:PRK13404 167 Q------ILD-VLAVARRHGAMVMVHAENHDMIAwLTKRLLAAGLTAPKYhaisrPMLAEREATHRAIALAELVDVPILI 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925976 261 QHVSTAISFEAIRKAKAEGLPITCETAPHYLALSDEALLKYGTL-AKM--NPPLRSEADRKATIAAIADGTVDLLATDHA 337
Cdd:PRK13404 240 VHVSGREAAEQIRRARGRGLKIFAETCPQYLFLTAEDLDRPGMEgAKYicSPPPRDKANQEAIWNGLADGTFEVFSSDHA 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925976 338 PHTLEE--------KELGFLEAPNGIIGLECAYGVCHKVLVDGGFISDERLIELMSVGPAELMGHAPtdvaalvedyaep 409
Cdd:PRK13404 320 PFRFDDtdgklaagANPSFKAIANGIPGIETRLPLLFSEGVVKGRISLNRFVALTSTNPAKLYGLYP------------- 386
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925976 410 aptgedpdgviageqvadaaesgasqREGvnrlldfSHVDDADAvDLVVLDTAEEWTVDPEQFHSKARNTPFGGWQVTGR 489
Cdd:PRK13404 387 --------------------------RKG-------AIAIGADA-DIAIWDPDREVTITNADLHHAADYTPYEGMRVTGW 432
|
....*
gi 489925976 490 PLATI 494
Cdd:PRK13404 433 PVTVL 437
|
|
| PRK01211 |
PRK01211 |
dihydroorotase; Provisional |
50-393 |
6.19e-23 |
|
dihydroorotase; Provisional
Pssm-ID: 179247 [Multi-domain] Cd Length: 409 Bit Score: 100.70 E-value: 6.19e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925976 50 PGFEDPHVHFRDPGQTYKESMVSGCRASASGGYTNVLIMPNTLPAldgqtVTDASAPGAKEVLDAGFDNViDF-LQQYDA 128
Cdd:PRK01211 46 PAATDIHVHFRTPGETEKEDFSTGTLSAIFGGTTFIMDMPNNNIP-----IKDYNAFSDKLGRVAPKAYV-DFsLYSMET 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925976 129 AHNVKLPvrydlcvcaskdragheasdvadwlkyvpgfedDAKTPAMLAHPVTAVSDDGSAVTpkilDQVLENVKTSDLY 208
Cdd:PRK01211 120 GNNALIL---------------------------------DERSIGLKVYMGGTTNTNGTDIE----GGEIKKINEANIP 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925976 209 LIEHCE------HHDTGAVN--EGPVSRelgvpgiPEDTELKIVARDIEAARRTGVHVHFQHVSTAISFeairkakaegl 280
Cdd:PRK01211 163 VFFHAElseclrKHQFESKNlrDHDLAR-------PIECEIKAVKYVKNLDLKTKIIAHVSSIDVIGRF----------- 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925976 281 piTCETAPHYLALSDEALLkyGTLAKMNPPLRSEADRKATIAAIADGTVDLLATDHAPHTlEEKELGFLEAPNGIIGLEc 360
Cdd:PRK01211 225 --LREVTPHHLLLNDDMPL--GSYGKVNPPLRDRWTQERLLEEYISGRFDILSSDHAPHT-EEDKQEFEYAKSGIIGVE- 298
|
330 340 350
....*....|....*....|....*....|...
gi 489925976 361 AYGVCHKVLVDGGFISDERLIELMSVGPAELMG 393
Cdd:PRK01211 299 TRVPLFLALVKKKILPLDVLYKTAIERPASLFG 331
|
|
| CAD_DHOase |
cd01316 |
The eukaryotic CAD protein is a trifunctional enzyme of carbamoylphosphate ... |
50-344 |
7.09e-20 |
|
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: 90.97 E-value: 7.09e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925976 50 PGFEDPHVHFRDPGQTYKESMVSGCRASASGGYTNVLIMPNTLPAldgqTVTDASAPGAKEVLDAGfdnvidflqqydaA 129
Cdd:cd01316 6 PGLIDVHVHLREPGATHKEDFASGTKAALAGGFTMVRAMPNTNPS----IVDVASLKLVQSLAQAK-------------A 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925976 130 HnvklpVRYDLCVCASKDRAgHEASDVAD---WLKYVPgFEDDAktpamlahpvTAVSDDGSAVTPKIldqvleNVKTSD 206
Cdd:cd01316 69 R-----CDYAFSIGATSTNA-ATVGELASeavGLKFYL-NETFS----------TLILDKITAWASHF------NAWPST 125
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925976 207 LYLIEHCEHHDTGAVnegpvsrelgvpgipedtelkivardIEAARRTGVHVHFQHVSTAISFEAIRKAKAEGLPITCET 286
Cdd:cd01316 126 KPIVTHAKSQTLAAV--------------------------LLLASLHNRSIHICHVSSKEEINLIRLAKARGLKVTCEV 179
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 489925976 287 APHYLALSDEALLKygTLAKMNPPLRSEADRKATIAAIAdgTVDLLATDHAPHTLEEK 344
Cdd:cd01316 180 SPHHLFLSQDDLPR--GQYEVRPFLPTREDQEALWENLD--YIDCFATDHAPHTLAEK 233
|
|
| PLN02942 |
PLN02942 |
dihydropyrimidinase |
19-501 |
5.19e-16 |
|
dihydropyrimidinase
Pssm-ID: 178530 Cd Length: 486 Bit Score: 80.27 E-value: 5.19e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925976 19 LVVPGTAAAYFADTSSVVDGADIDATGLTLAPGFEDPHVHFRDP--GQTYKESMVSGCRASASGGYTnvLIMPNTLPAlD 96
Cdd:PLN02942 26 YVEDGIIVAVAPNLKVPDDVRVIDATGKFVMPGGIDPHTHLAMPfmGTETIDDFFSGQAAALAGGTT--MHIDFVIPV-N 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925976 97 GQTVTDASA---PGAKEVLDAGFDNVIDFLQQyDAAHNVKLPVRYdlcvcaskdragHEASDVADWLKYvpgfeddaKTP 173
Cdd:PLN02942 103 GNLLAGYEAyekKAEKSCMDYGFHMAITKWDD-TVSRDMETLVKE------------KGINSFKFFMAY--------KGS 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925976 174 AMlahpvtavsddgsaVTPKILDQVLENVKTSDLYLIEHCEHHDtgAVNEGPvSR--ELGVPGI-------PEDTELKIV 244
Cdd:PLN02942 162 LM--------------VTDELLLEGFKRCKSLGALAMVHAENGD--AVFEGQ-KRmiELGITGPeghalsrPPLLEGEAT 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925976 245 ARDIEAARRTGVHVHFQHVSTAISFEAIRKAKAEGLPITCETAPHYLALSDEALLK--YGTLAK--MNPPLRSEADRKAT 320
Cdd:PLN02942 225 ARAIRLAKFVNTPLYVVHVMSIDAMEEIARARKSGQRVIGEPVVSGLVLDDSKLWDpdFTIASKyvMSPPIRPAGHGKAL 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925976 321 IAAIADGTVDLLATDHAPHTLEEKELG---FLEAPNGIIGLECAYGVCHKVLVDGGFISDERLIELMSVGPAELMGHAPT 397
Cdd:PLN02942 305 QAALSSGILQLVGTDHCPFNSTQKAFGkddFRKIPNGVNGIEERMHLVWDTMVESGQISPTDYVRVTSTECAKIFNIYPR 384
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925976 398 DVAalvedyaepaptgedpdgVIAGeqvADAaesgasqregvnrlldfshvddadavDLVVLDTAEEWTVDPEQFHSKAR 477
Cdd:PLN02942 385 KGA------------------ILAG---SDA--------------------------DIIILNPNSTFTISAKTHHSRID 417
|
490 500
....*....|....*....|....
gi 489925976 478 NTPFGGWQVTGRPLATIIGSKLMF 501
Cdd:PLN02942 418 TNVYEGRRGKGKVEVTISQGRVVW 441
|
|
| D-aminoacylase |
cd01297 |
D-aminoacylases (N-acyl-D-Amino acid amidohydrolases) catalyze the hydrolysis of ... |
14-299 |
1.13e-09 |
|
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: 60.39 E-value: 1.13e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925976 14 GEIIDlvvPGTAAAYFAD------------TSSVVDGAD-IDATGLTLAPGFEDPHVH-----FRDPGQtykesmvsgcR 75
Cdd:cd01297 7 GTVVD---GTGAPPFTADvgirdgriaaigPILSTSAREvIDAAGLVVAPGFIDVHTHydgqvFWDPDL----------R 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925976 76 ASASGGYTNVLIM-------PNTLPALDGQTVTDASAPGAKEVLDAGFDNVIDFLQQYDAAhnvklpvRYDLCVCASkdr 148
Cdd:cd01297 74 PSSRQGVTTVVLGncgvspaPANPDDLARLIMLMEGLVALGEGLPWGWATFAEYLDALEAR-------PPAVNVAAL--- 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925976 149 AGHEASDVADWlkyvpGFEDDAKTPAMLAHpvtavsddgsavTPKILDQVLE----NVKTSDLYLieHCEHHDTGAVNE- 223
Cdd:cd01297 144 VGHAALRRAVM-----GLDAREATEEELAK------------MRELLREALEagalGISTGLAYA--PRLYAGTAELVAl 204
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925976 224 -GPVSRELGV----PGIPEDTELKIVARDIEAARRTGVHVHFQH--VSTAISFEA-------IRKAKAEGLPITCETAPh 289
Cdd:cd01297 205 aRVAARYGGVyqthVRYEGDSILEALDELLRLGRETGRPVHISHlkSAGAPNWGKidrllalIEAARAEGLQVTADVYP- 283
|
330
....*....|
gi 489925976 290 YLALSDEALL 299
Cdd:cd01297 284 YGAGSEDDVR 293
|
|
| Amidohydro_1 |
pfam01979 |
Amidohydrolase family; This family of enzymes are a a large metal dependent hydrolase ... |
47-393 |
5.20e-08 |
|
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: 54.82 E-value: 5.20e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925976 47 TLAPGFEDPHVHFRD--------PGQTYKESMVSGCRASASGGYTNVLIMPNTlpaldgqtvTDASAPGAKEvldagfdn 118
Cdd:pfam01979 1 IVLPGLIDAHVHLEMgllrgipvPPEFAYEALRLGITTMLKSGTTTVLDMGAT---------TSTGIEALLE-------- 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925976 119 vidflqqydAAHNVKLPVRYDLCVCaSKDRAGHEASDVADWLKYVPGFE------DDAKTPAMLAHPVTAVSDDGsavtp 192
Cdd:pfam01979 64 ---------AAEELPLGLRFLGPGC-SLDTDGELEGRKALREKLKAGAEfikgmaDGVVFVGLAPHGAPTFSDDE----- 128
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925976 193 kiLDQVLENVKTSDLYLIEHCEHHD-TGAVNEGPVSRELGVPGIPEDTELKIVARDIEAARRTGVHVHfqhvstaisfea 271
Cdd:pfam01979 129 --LKAALEEAKKYGLPVAIHALETKgEVEDAIAAFGGGIEHGTHLEVAESGGLLDIIKLILAHGVHLS------------ 194
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925976 272 irkakaeglpitcetaPHYLALSDEALLKYGTLAKMNPPLRSEADRKATIAAIADGTVDLLATDHAPHTleeKELGFLEa 351
Cdd:pfam01979 195 ----------------PTEANLLAEHLKGAGVAHCPFSNSKLRSGRIALRKALEDGVKVGLGTDGAGSG---NSLNMLE- 254
|
330 340 350 360
....*....|....*....|....*....|....*....|..
gi 489925976 352 pngiiglECAYGVcHKVLVDGGFISDERLIELMSVGPAELMG 393
Cdd:pfam01979 255 -------ELRLAL-ELQFDPEGGLSPLEALRMATINPAKALG 288
|
|
| DHOase |
cd01294 |
Dihydroorotase (DHOase) catalyzes the reversible interconversion of carbamoyl aspartate to ... |
180-345 |
9.46e-06 |
|
Dihydroorotase (DHOase) catalyzes the reversible interconversion of carbamoyl aspartate to dihydroorotate, a key reaction in the pyrimidine biosynthesis. In contrast to the large polyfunctional CAD proteins of higher organisms, this group of DHOases is monofunctional and mainly dimeric.
Pssm-ID: 238619 Cd Length: 335 Bit Score: 47.66 E-value: 9.46e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925976 180 VTAVSDDGSAVTPKILdQVLENVKTSDLYLIEHCEHHDtgaVNEGPVSRELGVPGIPED-----TELKIVardieaarrt 254
Cdd:cd01294 101 ATTNSQGGVTDLEKIY-PVLEAMQKLGMPLLVHGEVPD---FKIDVLDREAKFIPVLEPlaqrfPKLKIV---------- 166
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925976 255 gvhvhFQHVSTAISFEAIRKAKAE-GLPITcetaPHYLALSDEALLKYGtlakMNP-----P-LRSEADRKATIAAIADG 327
Cdd:cd01294 167 -----LEHITTADAVEYVKSCNENvAATIT----PHHLLLTRDDLLGGG----LNPhlyckPvAKRPEDREALRKAATSG 233
|
170
....*....|....*....
gi 489925976 328 TVDL-LATDHAPHTLEEKE 345
Cdd:cd01294 234 HPKFfLGSDSAPHPKSNKE 252
|
|
| AdeC |
COG1001 |
Adenine deaminase [Nucleotide transport and metabolism]; |
5-59 |
3.61e-03 |
|
Adenine deaminase [Nucleotide transport and metabolism];
Pssm-ID: 440625 [Multi-domain] Cd Length: 559 Bit Score: 40.08 E-value: 3.61e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 489925976 5 LRNIKVWN--TGEII--DLVVpgtAAAYFADTSSVVDGAD--IDATGLTLAPGFEDPHVHF 59
Cdd:COG1001 9 IKNGRLVNvfTGEILegDIAI---AGGRIAGVGDYIGEATevIDAAGRYLVPGFIDGHVHI 66
|
|
| |
