|
Name |
Accession |
Description |
Interval |
E-value |
| pyrC |
PRK09357 |
dihydroorotase; Validated |
2-425 |
0e+00 |
|
dihydroorotase; Validated
Pssm-ID: 236479 [Multi-domain] Cd Length: 423 Bit Score: 592.17 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 400189753 2 GALLLKGGRVIDPAaKRNEICDVLIEDGVIRAVGANLSADGVEVYDASGKIVSPGFIDMHTHFREPGQEAKEDFASGSRA 81
Cdd:PRK09357 1 MMILIKNGRVIDPK-GLDEVADVLIDDGKIAAIGENIEAEGAEVIDATGLVVAPGLVDLHVHLREPGQEDKETIETGSRA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 400189753 82 GAAGGYTTIATMPNTRPVVDDAALVTSLKKRAEDVAVIHIEIIGAVTKNQEGKELAELGDMVEAGAVAFSDDGHFDPSAK 161
Cdd:PRK09357 80 AAAGGFTTVVAMPNTKPVIDTPEVVEYVLDRAKEAGLVDVLPVGAITKGLAGEELTEFGALKEAGVVAFSDDGIPVQDAR 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 400189753 162 VLLSAYDYLVPFDKAIINHEEDPSLVEDGAMNEGHRSAMLGIKGRPIVAEDIAVARDIMLAEYAGAHVHVAHISSGRAVQ 241
Cdd:PRK09357 160 LMRRALEYAKALDLLIAQHCEDPSLTEGGVMNEGEVSARLGLPGIPAVAEEVMIARDVLLAEATGARVHICHVSTAGSVE 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 400189753 242 LVREAKARGVRVTTEVTPHHLTMTDECVDPRDSSTKVNPPLRTEKDVEAMVAGLLDGTIDMVVTDHSPHAPEEKDREYIY 321
Cdd:PRK09357 240 LIRWAKALGIKVTAEVTPHHLLLTDEDLLTYDPNYKVNPPLRTEEDREALIEGLKDGTIDAIATDHAPHAREEKECEFEA 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 400189753 322 APSGFPGLETALGVLLTDLVHTGKIPMETLIERMTCAPARVFKLNAGTLAEGAPADVTVIDPELIWTVDPKAFYTRGRHS 401
Cdd:PRK09357 320 APFGITGLETALSLLYTTLVKTGLLDLEQLLEKMTINPARILGLPAGPLAEGEPADLVIFDPEAEWTVDGEDFASKGKNT 399
|
410 420
....*....|....*....|....
gi 400189753 402 PFAGRELKGRPVLTVVDGQIVMKD 425
Cdd:PRK09357 400 PFIGMKLKGKVVYTIVDGKIVYQD 423
|
|
| AllB |
COG0044 |
Dihydroorotase or related cyclic amidohydrolase [Nucleotide transport and metabolism]; ... |
5-429 |
0e+00 |
|
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: 587.06 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 400189753 5 LLKGGRVIDPAakRNEICDVLIEDGVIRAVGANLSA-DGVEVYDASGKIVSPGFIDMHTHFREPGQEAKEDFASGSRAGA 83
Cdd:COG0044 1 LIKNGRVVDPG--GLERADVLIEDGRIAAIGPDLAApEAAEVIDATGLLVLPGLIDLHVHLREPGLEHKEDIETGTRAAA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 400189753 84 AGGYTTIATMPNTRPVVDDAALVTSLKKRAEDVAVIHIEIIGAVTKNQeGKELAELGDMVEAGAVAF-----SDDGHFDP 158
Cdd:COG0044 79 AGGVTTVVDMPNTNPVTDTPEALEFKLARAEEKALVDVGPHGALTKGL-GENLAELGALAEAGAVAFkvfmgSDDGNPVL 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 400189753 159 SAKVLLSAYDYLVPFDKAIINHEEDPSLVEDGAMNEGHRSAMLGIKGRPIVAEDIAVARDIMLAEYAGAHVHVAHISSGR 238
Cdd:COG0044 158 DDGLLRRALEYAAEFGALVAVHAEDPDLIRGGVMNEGKTSPRLGLKGRPAEAEEEAVARDIALAEETGARLHIVHVSTAE 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 400189753 239 AVQLVREAKARGVRVTTEVTPHHLTMTDECVDPRDSSTKVNPPLRTEKDVEAMVAGLLDGTIDMVVTDHSPHAPEEKDRE 318
Cdd:COG0044 238 AVELIREAKARGLPVTAEVCPHHLTLTDEDLERYGTNFKVNPPLRTEEDREALWEGLADGTIDVIATDHAPHTLEEKELP 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 400189753 319 YIYAPSGFPGLETALGVLLTDLVHTGKIPMETLIERMTCAPARVFKL-NAGTLAEGAPADVTVIDPELIWTVDPKAFYTR 397
Cdd:COG0044 318 FAEAPNGIPGLETALPLLLTELVHKGRLSLERLVELLSTNPARIFGLpRKGRIAVGADADLVLFDPDAEWTVTAEDLHSK 397
|
410 420 430
....*....|....*....|....*....|..
gi 400189753 398 GRHSPFAGRELKGRPVLTVVDGQIVMKDGVII 429
Cdd:COG0044 398 SKNTPFEGRELTGRVVATIVRGRVVYEDGEVV 429
|
|
| DHOase_IIa |
cd01317 |
Dihydroorotase (DHOase), subgroup IIa; DHOases catalyze the reversible interconversion of ... |
42-415 |
2.48e-169 |
|
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: 479.43 E-value: 2.48e-169
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 400189753 42 GVEVYDASGKIVSPGFIDMHTHFREPGQEAKEDFASGSRAGAAGGYTTIATMPNTRPVVDDAALVTSLKKRAEDVAVIHI 121
Cdd:cd01317 1 DAEVIDAEGKILAPGLVDLHVHLREPGFEYKETLESGAKAAAAGGFTTVVCMPNTNPVIDNPAVVELLKNRAKDVGIVRV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 400189753 122 EIIGAVTKNQEGKELAELGDMVEAGAVAFSDDGHFDPSAKVLLSAYDYLVPFDKAIINHEEDPSLVEDGAMNEGHRSAML 201
Cdd:cd01317 81 LPIGALTKGLKGEELTEIGELLEAGAVGFSDDGKPIQDAELLRRALEYAAMLDLPIIVHPEDPSLAGGGVMNEGKVASRL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 400189753 202 GIKGRPIVAEDIAVARDIMLAEYAGAHVHVAHISSGRAVQLVREAKARGVRVTTEVTPHHLTMTDECVDPRDSSTKVNPP 281
Cdd:cd01317 161 GLPGIPPEAETIMVARDLELAEATGARVHFQHLSTARSLELIRKAKAKGLPVTAEVTPHHLLLDDEALESYDTNAKVNPP 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 400189753 282 LRTEKDVEAMVAGLLDGTIDMVVTDHSPHAPEEKDREYIYAPSGFPGLETALGVLLTDLVHTGKIPMETLIERMTCAPAR 361
Cdd:cd01317 241 LRSEEDREALIEALKDGTIDAIASDHAPHTDEEKDLPFAEAPPGIIGLETALPLLWTLLVKGGLLTLPDLIRALSTNPAK 320
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....
gi 400189753 362 VFKLNAGTLAEGAPADVTVIDPELIWTVDPKAFYTRGRHSPFAGRELKGRPVLT 415
Cdd:cd01317 321 ILGLPPGRLEVGAPADLVLFDPDAEWIVDEETFRSKSKNTPFDGQKLKGRVLAT 374
|
|
| pyrC_multi |
TIGR00857 |
dihydroorotase, multifunctional complex type; In contrast to the homodimeric type of ... |
23-425 |
4.37e-137 |
|
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: 399.12 E-value: 4.37e-137
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 400189753 23 DVLIEDGVIRAVGANLSADGVEVYDASGKIVSPGFIDMHTHFREPGQEAKEDFASGSRAGAAGGYTTIATMPNTRPVVDD 102
Cdd:TIGR00857 7 DILVEGGRIKKIGKLRIPPDAEVIDAKGLLVLPGFIDLHVHLRDPGEEYKEDIESGSKAAAHGGFTTVADMPNTKPPIDT 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 400189753 103 AALVTSLKKRAEDVAVIHIEIIGAVTKNQEGKELAELGDMVEAGAVA--FSDDGHFDPSAKVLLSAYDYLVPFDKAIINH 180
Cdd:TIGR00857 87 PETLEWKLQRLKKVSLVDVHLYGGVTQGNQGKELTEAYELKEAGAVGrmFTDDGSEVQDILSMRRALEYAAIAGVPIALH 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 400189753 181 EEDPSLVEDGAMNEGHRSAMLGIKGRPIVAEDIAVARDIMLAEYAGAHVHVAHISSGRAVQLVREAKARGVRVTTEVTPH 260
Cdd:TIGR00857 167 AEDPDLIYGGVMHEGPSAAQLGLPARPPEAEEVAVARLLELAKHAGCPVHICHISTKESLELIVKAKSQGIKITAEVTPH 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 400189753 261 HLTMTDECVDPRDSSTKVNPPLRTEKDVEAMVAGLLDGTIDMVVTDHSPHAPEEKDREYIYAPSGFPGLETALGVLLtDL 340
Cdd:TIGR00857 247 HLLLSEEDVARLDGNGKVNPPLREKEDRLALIEGLKDGIIDIIATDHAPHTLEEKTKEFAAAPPGIPGLETALPLLL-QL 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 400189753 341 VHTGKIPMETLIERMTCAPARVFKL-NAGTLAEGAPADVTVIDPELIWTVDPKAFYTRGRHSPFAGRELKGRPVLTVVDG 419
Cdd:TIGR00857 326 LVKGLISLKDLIRMLSINPARIFGLpDKGTLEEGNPADITVFDLKKEWTINAETFYSKAKNTPFEGMSLKGKPIATILRG 405
|
....*.
gi 400189753 420 QIVMKD 425
Cdd:TIGR00857 406 KVVYED 411
|
|
| PRK09059 |
PRK09059 |
dihydroorotase; Validated |
1-424 |
2.47e-125 |
|
dihydroorotase; Validated
Pssm-ID: 181631 [Multi-domain] Cd Length: 429 Bit Score: 369.75 E-value: 2.47e-125
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 400189753 1 MGALLLKGGRVIDPAAKRNEICDVLIEDGVIRAVGANLSA----DGVEVYDASGKIVSPGFIDMHTHFREPGQEAKEDFA 76
Cdd:PRK09059 2 MRPILLANARIIDPSRGLDEIGTVLIEDGVIVAAGKGAGNqgapEGAEIVDCAGKAVAPGLVDARVFVGEPGAEHRETIA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 400189753 77 SGSRAGAAGGYTTIATMPNTRPVVDDAALVTSLKKRAEDVAVIHIEIIGAVTKNQEGKELAELGDMVEAGAVAFSDDGHF 156
Cdd:PRK09059 82 SASRAAAAGGVTSIIMMPDTDPVIDDVALVEFVKRTARDTAIVNIHPAAAITKGLAGEEMTEFGLLRAAGAVAFTDGRRS 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 400189753 157 DPSAKVLLSAYDYLVPFDKAIINHEEDPSLVEDGAMNEGHRSAMLGIKGRPIVAEDIAVARDIMLAEYAGAHVHVAHISS 236
Cdd:PRK09059 162 VANTQVMRRALTYARDFDAVIVHETRDPDLGGNGVMNEGLFASWLGLSGIPREAEVIPLERDLRLAALTRGRYHAAQISC 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 400189753 237 GRAVQLVREAKARGVRVTTEVTPHHLTMTDECVDPRDSSTKVNPPLRTEKDVEAMVAGLLDGTIDMVVTDHSPHAPEEKD 316
Cdd:PRK09059 242 AESAEALRRAKDRGLKVTAGVSINHLSLNENDIGEYRTFFKLSPPLRTEDDRVAMVEAVASGTIDIIVSSHDPQDVDTKR 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 400189753 317 REYIYAPSGFPGLETALGVLLTdLVHTGKIPMETLIERMTCAPARVFKLNAGTLAEGAPADVTVIDPELIWTVDPKAFYT 396
Cdd:PRK09059 322 LPFSEAAAGAIGLETLLAAALR-LYHNGEVPLLRLIEALSTRPAEIFGLPAGTLKPGAPADIIVIDLDEPWVVDPEDLKS 400
|
410 420
....*....|....*....|....*...
gi 400189753 397 RGRHSPFAGRELKGRPVLTVVDGQIVMK 424
Cdd:PRK09059 401 RSKNTPFEEARFQGRVVRTIVAGKTVYE 428
|
|
| PRK07369 |
PRK07369 |
dihydroorotase; Provisional |
1-416 |
5.48e-108 |
|
dihydroorotase; Provisional
Pssm-ID: 236002 [Multi-domain] Cd Length: 418 Bit Score: 325.02 E-value: 5.48e-108
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 400189753 1 MGALLLKGGRVIDPAAKRNEICDVLIEDGVIRAV---GANLSADgVEVYDASGKIVSPGFIDMHTHFREPGQEAKEDFAS 77
Cdd:PRK07369 1 MSNELLQQVRVLDPVSNTDRIADVLIEDGKIQAIephIDPIPPD-TQIIDASGLILGPGLVDLYSHSGEPGFEERETLAS 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 400189753 78 GSRAGAAGGYTTIATMPNTRPVVDDAALVTSLKKRAEDVAVIHIEIIGAVTKNQEGKELAELGDMVEAGAVAFSDDGHFD 157
Cdd:PRK07369 80 LAAAAAAGGFTRVAILPDTFPPLDNPATLARLQQQAQQIPPVQLHFWGALTLGGQGKQLTELAELAAAGVVGFTDGQPLE 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 400189753 158 pSAKVLLSAYDYLVPFDKAIINHEEDPSLVEDGAMNEGHRSAMLGIKGRPIVAEDIAVARDIMLAEYAGAHVHVAHISSG 237
Cdd:PRK07369 160 -NLALLRRLLEYLKPLGKPVALWPCDRSLAGNGVMREGLLALRLGLPGDPASAETTALAALLELVAAIGTPVHLMRISTA 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 400189753 238 RAVQLVREAKARGVRVTTEVTPHHLTMTDECVDPRDSSTKVNPPLRTEKDVEAMVAGLLDGTIDMVVTDHSPHAPEEKDR 317
Cdd:PRK07369 239 RSVELIAQAKARGLPITASTTWMHLLLDTEALASYDPNLRLDPPLGNPSDRQALIEGVRTGVIDAIAIDHAPYTYEEKTV 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 400189753 318 EYIYAPSGFPGLETALGVLLTDLVHTGKIPMETLIERMTCAPARVFKLNAGTLAEGAPADVTVIDPELIWTVDPKAFYTR 397
Cdd:PRK07369 319 AFAEAPPGAIGLELALPLLWQNLVETGELSALQLWQALSTNPARCLGQEPPSLAPGQPAELILFDPQKTWTVSAQTLHSL 398
|
410
....*....|....*....
gi 400189753 398 GRHSPFAGRELKGRpVLTV 416
Cdd:PRK07369 399 SRNTPWLGQTLKGR-VLQT 416
|
|
| PRK07627 |
PRK07627 |
dihydroorotase; Provisional |
4-422 |
1.57e-103 |
|
dihydroorotase; Provisional
Pssm-ID: 181059 [Multi-domain] Cd Length: 425 Bit Score: 313.92 E-value: 1.57e-103
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 400189753 4 LLLKGGRVIDPAAKRNEICDVLIEDGVIRAVG---ANLSADgvEVYDASGKIVSPGFIDMHTHFREPGQEAKEDFASGSR 80
Cdd:PRK07627 3 IHIKGGRLIDPAAGTDRQADLYVAAGKIAAIGqapAGFNAD--KTIDASGLIVCPGLVDLSARLREPGYEYKATLESEMA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 400189753 81 AGAAGGYTTIATMPNTRPVVDDAALVTSLKKRAEDVAVIHIEIIGAVTKNQEGKELAELGDMVEAGAVAFSDDGHFDPSA 160
Cdd:PRK07627 81 AAVAGGVTSLVCPPDTDPVLDEPGLVEMLKFRARNLNQAHVYPLGALTVGLKGEVLTEMVELTEAGCVGFSQANVPVVDT 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 400189753 161 KVLLSAYDYLVPFDKAIINHEEDPSLVEDGAMNEGHRSAMLGIKGRPIVAEDIAVARDIMLAEYAGAHVHVAHISSGRAV 240
Cdd:PRK07627 161 QVLLRALQYASTFGFTVWLRPLDAFLGRGGVAASGAVASRLGLSGVPVAAETIALHTIFELMRVTGARVHLARLSSAAGV 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 400189753 241 QLVREAKARGVRVTTEVTPHHLTMTDECVDPRDSSTKVNPPLRTEKDVEAMVAGLLDGTIDMVVTDHSPHAPEEKDREYI 320
Cdd:PRK07627 241 ALVRAAKAEGLPVTCDVGVNHVHLIDVDIGYFDSQFRLDPPLRSQRDREAIRAALADGTIDAICSDHTPVDDDEKLLPFA 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 400189753 321 YAPSGFPGLETALGVLLTDLVHTgKIPMETLIERMTCAPARVFKLNAGTLAEGAPADVTVIDPELIWTVDPKAFYTRGRH 400
Cdd:PRK07627 321 EATPGATGLELLLPLTLKWADEA-KVPLARALARITSAPARVLGLPAGRLAEGAPADLCVFDPDAHWRVEPRALKSQGKN 399
|
410 420
....*....|....*....|..
gi 400189753 401 SPFAGRELKGRPVLTVVDGQIV 422
Cdd:PRK07627 400 TPFLGYELPGRVRATLVAGQVA 421
|
|
| DHOase_IIb |
cd01318 |
Dihydroorotase (DHOase), subgroup IIb; DHOases catalyze the reversible interconversion of ... |
50-419 |
1.61e-100 |
|
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: 303.87 E-value: 1.61e-100
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 400189753 50 GKIVSPGFIDMHTHFREPGQEAKEDFASGSRAGAAGGYTTIATMPNTRPVVDDAALVTSLKKRAEDVAVIHIEIIGAVTK 129
Cdd:cd01318 1 GLLILPGVIDIHVHFREPGLTYKEDFVSGSRAAAAGGVTTVMDMPNTKPPTTTAEALYEKLRLAAAKSVVDYGLYFGVTG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 400189753 130 NQEGKELAELGdmVEAGAV----AFSDDGHFDPSAKVLLSAYDYLVPFdkaiinHEEDPSLVEDGAMNEGHRSAMLGIkg 205
Cdd:cd01318 81 SEDLEELDKAP--PAGYKIfmgdSTGDLLDDEETLERIFAEGSVLVTF------HAEDEDRLRENRKELKGESAHPRI-- 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 400189753 206 RPIVAEDIAVARDIMLAEYAGAHVHVAHISSGRAVQLVREAKargVRVTTEVTPHHLTMTDECVDPRDSSTKVNPPLRTE 285
Cdd:cd01318 151 RDAEAAAVATARALKLARRHGARLHICHVSTPEELKLIKKAK---PGVTVEVTPHHLFLDVEDYDRLGTLGKVNPPLRSR 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 400189753 286 KDVEAMVAGLLDGTIDMVVTDHSPHAPEEKDREYIYAPSGFPGLETALGVLLTdLVHTGKIPMETLIERMTCAPARVFKL 365
Cdd:cd01318 228 EDRKALLQALADGRIDVIASDHAPHTLEEKRKGYPAAPSGIPGVETALPLMLT-LVNKGILSLSRVVRLTSHNPARIFGI 306
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*
gi 400189753 366 -NAGTLAEGAPADVTVIDPELIWTVDPKAFYTRGRHSPFAGRELKGRPVLTVVDG 419
Cdd:cd01318 307 kNKGRIAEGYDADLTVVDLKEERTIRAEEFHSKAGWTPFEGFEVTGFPVMTIVRG 361
|
|
| L-HYD_ALN |
cd01315 |
L-Hydantoinases (L-HYDs) and Allantoinase (ALN); L-Hydantoinases are a member of the ... |
4-426 |
1.20e-97 |
|
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: 299.59 E-value: 1.20e-97
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 400189753 4 LLLKGGRVIDPAAKRneICDVLIEDGVIRAVGANLS-ADGVEVYDASGKIVSPGFIDMHTHFREPGQEAKEDFASGSRAG 82
Cdd:cd01315 2 LVIKNGRVVTPDGVR--EADIAVKGGKIAAIGPDIAnTEAEEVIDAGGLVVMPGLIDTHVHINEPGRTEWEGFETGTKAA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 400189753 83 AAGGYTTIATMP-NTRPVVDDAAlvtSLKKRAEDVA-VIHIEII---GAVTKNqegkeLAELGDMVEAGAVAF------S 151
Cdd:cd01315 80 AAGGITTIIDMPlNSIPPTTTVE---NLEAKLEAAQgKLHVDVGfwgGLVPGN-----LDQLRPLDEAGVVGFkcflcpS 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 400189753 152 DDGHFDP-SAKVLLSAYDYLVPFDKAIINHEEDPSLVEDGAMNE---GHRSAMLGIKGRPIVAEDIAVARDIMLAEYAGA 227
Cdd:cd01315 152 GVDEFPAvDDEQLEEAMKELAKTGSVLAVHAENPEITEALQEQAkakGKRDYRDYLASRPVFTEVEAIQRILLLAKETGC 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 400189753 228 HVHVAHISSGRAVQLVREAKARGVRVTTEVTPHHLTMTDECVDPRDSSTKVNPPLRTEKDVEAMVAGLLDGTIDMVVTDH 307
Cdd:cd01315 232 RLHIVHLSSAEAVPLIREARAEGVDVTVETCPHYLTFTAEDVPDGGTEFKCAPPIRDAANQEQLWEALENGDIDMVVSDH 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 400189753 308 SPHAPEEKDRE---YIYAPSGFPGLETALGVLLTDLVHTGKIPMETLIERMTCAPARVFKLNA--GTLAEGAPADVTVID 382
Cdd:cd01315 312 SPCTPELKLLGkgdFFKAWGGISGLQLGLPVMLTEAVNKRGLSLEDIARLMCENPAKLFGLSHqkGRIAVGYDADFVVWD 391
|
410 420 430 440
....*....|....*....|....*....|....*....|....
gi 400189753 383 PELIWTVDPKAFYTRGRHSPFAGRELKGRPVLTVVDGQIVMKDG 426
Cdd:cd01315 392 PEEEFTVDAEDLYYKNKISPYVGRTLKGRVHATILRGTVVYQDG 435
|
|
| PRK02382 |
PRK02382 |
dihydroorotase; Provisional |
1-429 |
7.59e-89 |
|
dihydroorotase; Provisional
Pssm-ID: 179417 [Multi-domain] Cd Length: 443 Bit Score: 276.53 E-value: 7.59e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 400189753 1 MGALLLKGGRVidPAAKRNEICDVLIEDGVIRAVGANLSADGVE-VYDASGKIVSPGFIDMHTHFREPGQEAKEDFASGS 79
Cdd:PRK02382 1 MRDALLKDGRV--YYNNSLQPRDVRIDGGKITAVGKDLDGSSSEeVIDARGMLLLPGGIDVHVHFREPGYTHKETWYTGS 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 400189753 80 RAGAAGGYTTIATMPNTRPVVDDAALVTSLKKRAEDVAVIHIEIIGAVTKNQEgkELAELgdmVEAGAVAFSD------D 153
Cdd:PRK02382 79 RSAAAGGVTTVVDQPNTDPPTVDGESFDEKAELAARKSIVDFGINGGVTGNWD--PLESL---WERGVFALGEifmadsT 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 400189753 154 GHFDPSAKVLLSAYDYLVPFDKAIINHEEDPSLVEDGAMNEGHR-SAMLGIKGRPIVAEDIAVARDIMLAEYAGAHVHVA 232
Cdd:PRK02382 154 GGMGIDEELFEEALAEAARLGVLATVHAEDEDLFDELAKLLKGDaDADAWSAYRPAAAEAAAVERALEVASETGARIHIA 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 400189753 233 HISSGRAVQLVREAKargvrVTTEVTPHHLTMTDECVDPRDSSTKVNPPLRTEKDVEAMVAGLLDGTIDMVVTDHSPHAP 312
Cdd:PRK02382 234 HISTPEGVDAARREG-----ITCEVTPHHLFLSRRDWERLGTFGKMNPPLRSEKRREALWERLNDGTIDVVASDHAPHTR 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 400189753 313 EEKDREYIYAPSGFPGLETALGVLLtDLVHTGKIPMETLIERMTCAPARVFKLNA-GTLAEGAPADVTVIDPELIWTVDP 391
Cdd:PRK02382 309 EEKDADIWDAPSGVPGVETMLPLLL-AAVRKNRLPLERVRDVTAANPARIFGLDGkGRIAEGYDADLVLVDPDAAREIRG 387
|
410 420 430
....*....|....*....|....*....|....*...
gi 400189753 392 KAFYTRGRHSPFAGRElKGRPVLTVVDGQIVMKDGVII 429
Cdd:PRK02382 388 DDLHSKAGWTPFEGME-GVFPELTMVRGTVVWDGDDIN 424
|
|
| allantoinase |
TIGR03178 |
allantoinase; This enzyme carries out the first step in the degradation of allantoin, a ... |
4-429 |
3.39e-87 |
|
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: 272.33 E-value: 3.39e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 400189753 4 LLLKGGRVIDPAAKRNeiCDVLIEDGVIRAVGANLSADGVEVYDASGKIVSPGFIDMHTHFREPGQEAKEDFASGSRAGA 83
Cdd:TIGR03178 2 LIIRGGRVILPNGERE--ADVGVKGGKIAAIGPDILGPAAKIIDAGGLVVFPGVVDTHVHINEPGRTEWEGFETGTRAAA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 400189753 84 AGGYTTIATMP-NTRP-VVDDAALVTSLKKRAEDVAVIHIEIIGAVTKNqegkeLAELGDMVEAGAVAF------SDDGH 155
Cdd:TIGR03178 80 AGGITTYIDMPlNSIPaTTTRASLEAKFEAAKGKLAVDVGFWGGLVPYN-----LDDLRELDEAGVVGFkaflspSGDDE 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 400189753 156 FDP-SAKVLLSAYDYLVPFDKAIINHEEDPSL---VEDGAMNEGHRSAMLGIKGRPIVAEDIAVARDIMLAEYAGAHVHV 231
Cdd:TIGR03178 155 FPHvDDWQLYKGMRELARLGQLLLVHAENPAItsaLGEEAPPQGGVGADAYLASRPVFAEVEAIRRTLALAKVTGCRVHV 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 400189753 232 AHISSGRAVQLVREAKARGVRVTTEVTPHHLTMTDECVDPRDSSTKVNPPLRTEKDVEAMVAGLLDGTIDMVVTDHSPHA 311
Cdd:TIGR03178 235 VHLSSAEAVELITEAKQEGLDVTVETCPHYLTLTAEEVPDGGTLAKCAPPIRDLANQEGLWEALLNGLIDCVVSDHSPCT 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 400189753 312 PEEKDREYIY-APSGFPGLETALGVLLTDLVHTGKIPMETLIERMTCAPARVFKL-NAGTLAEGAPADVTVIDPELIWTV 389
Cdd:TIGR03178 315 PDLKRAGDFFkAWGGIAGLQSTLDVMFDEAVQKRGLPLEDIARLMATNPAKRFGLaQKGRIAPGKDADFVFVDPDESYTL 394
|
410 420 430 440
....*....|....*....|....*....|....*....|
gi 400189753 390 DPKAFYTRGRHSPFAGRELKGRPVLTVVDGQIVMKDGVII 429
Cdd:TIGR03178 395 TPDDLYYRHKVSPYVGRTIGGRVRATYLRGQCIYDDEQFI 434
|
|
| PRK06189 |
PRK06189 |
allantoinase; Provisional |
4-426 |
6.10e-85 |
|
allantoinase; Provisional
Pssm-ID: 235732 [Multi-domain] Cd Length: 451 Bit Score: 266.95 E-value: 6.10e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 400189753 4 LLLKGGRVIDPAAKRNeiCDVLIEDGVIRAVGANLSADGVEVYDASGKIVSPGFIDMHTHFREPGQEAKEDFASGSRAGA 83
Cdd:PRK06189 5 LIIRGGKVVTPEGVYR--ADIGIKNGKIAEIAPEISSPAREIIDADGLYVFPGMIDVHVHFNEPGRTHWEGFATGSAALA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 400189753 84 AGGYTTIATMP-NTRPVVDDAALVTSLKKRAEDVAVIHIEIIGAVTKNQegkeLAELGDMVEAGAVAF----SDDG--HF 156
Cdd:PRK06189 83 AGGCTTYFDMPlNSIPPTVTREALDAKAELARQKSAVDFALWGGLVPGN----LEHLRELAEAGVIGFkafmSNSGtdEF 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 400189753 157 D-PSAKVLLSAYDYLVPFDKAIINHEEDPSLV---EDGAMNEGHRSAMLGIKGRPIVAEDIAVARDIMLAEYAGAHVHVA 232
Cdd:PRK06189 159 RsSDDLTLYEGMKEIAALGKILALHAESDALTrhlTTQARQQGKTDVRDYLESRPVVAELEAVQRALLYAQETGCPLHFV 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 400189753 233 HISSGRAVQLVREAKARGVRVTTEVTPHHLTMTDECVDPRDSSTKVNPPLRTEKDVEAMVAGLLDGTIDMVVTDHSPHAP 312
Cdd:PRK06189 239 HISSGKAVALIAEAKKRGVDVSVETCPHYLLFTEEDFERIGAVAKCAPPLRSRSQKEELWRGLLAGEIDMISSDHSPCPP 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 400189753 313 EEKDREYIYAP-SGFPGLETALGVLLTDLVHTGKIPMETLIERMTCAPARVFKL-NAGTLAEGAPADVTVIDPELIWTVD 390
Cdd:PRK06189 319 ELKEGDDFFLVwGGISGGQSTLLVMLTEGYIERGIPLETIARLLATNPAKRFGLpQKGRLEVGADADFVLVDLDETYTLT 398
|
410 420 430
....*....|....*....|....*....|....*.
gi 400189753 391 PKAFYTRGRHSPFAGRELKGRPVLTVVDGQIVMKDG 426
Cdd:PRK06189 399 KEDLFYRHKQSPYEGRTFPGRVVATYLRGQCVYQDG 434
|
|
| Cyclic_amidohydrolases |
cd01302 |
Cyclic amidohydrolases, including hydantoinase, dihydropyrimidinase, allantoinase, and ... |
51-415 |
2.79e-82 |
|
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: 256.16 E-value: 2.79e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 400189753 51 KIVSPGFIDMHTHFREPGQEA-KEDFASGSRAGAAGGYTTIATMPNTRPVVDDAALVTSLKKRAEDVAVIHIEIIGAVTK 129
Cdd:cd01302 1 LLVLPGFIDIHVHLRDPGGTTyKEDFESGSRAAAAGGVTTVIDMPNTGPPPIDLPAIELKIKLAEESSYVDFSFHAGIGP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 400189753 130 NQEGKELAElgdMVEAGAVAFsddghfdpsaKVLLSAYDYlvpfdkaiinheeDPSLVEDGAMnEGHRSAMLGIKGRPIV 209
Cdd:cd01302 81 GDVTDELKK---LFDAGINSL----------KVFMNYYFG-------------ELFDVDDGTL-MRTFLEIASRGGPVMV 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 400189753 210 AEDIAvardIMLAEYAGAHVHVAHISSGRAVQLVREAKARGVRVTTEVTPHHLTMTDECVDPRDSSTKVNPPLRTEKDVE 289
Cdd:cd01302 134 HAERA----AQLAEEAGANVHIAHVSSGEALELIKFAKNKGVKVTCEVCPHHLFLDESMLRLNGAWGKVNPPLRSKEDRE 209
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 400189753 290 AMVAGLLDGTIDMVVTDHSPHAPEEKD--REYIYAPSGFPGLETALGVLLTDLVHtGKIPMETLIERMTCAPARVFKL-N 366
Cdd:cd01302 210 ALWEGVKNGKIDTIASDHAPHSKEEKEsgKDIWKAPPGFPGLETRLPILLTEGVK-RGLSLETLVEILSENPARIFGLyP 288
|
330 340 350 360
....*....|....*....|....*....|....*....|....*....
gi 400189753 367 AGTLAEGAPADVTVIDPELIWTVDPKAFYTRGRHSPFAGRELKGRPVLT 415
Cdd:cd01302 289 KGTIAVGYDADLVIVDPKKEWKVTAEEIESKADWTPFEGMEVTGKPVST 337
|
|
| PRK07575 |
PRK07575 |
dihydroorotase; Provisional |
1-426 |
4.99e-79 |
|
dihydroorotase; Provisional
Pssm-ID: 236055 [Multi-domain] Cd Length: 438 Bit Score: 251.13 E-value: 4.99e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 400189753 1 MGALLLKGGRVIDPAAKRnEICDVLIEDGVIRAVGANLSADGV-EVYDASGKIVSPGFIDMHTHFREPGQEAKEDFASGS 79
Cdd:PRK07575 2 MMSLLIRNARILLPSGEL-LLGDVLVEDGKIVAIAPEISATAVdTVIDAEGLTLLPGVIDPQVHFREPGLEHKEDLFTAS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 400189753 80 RAGAAGGYTTIATMPNTRPV-VDDAALVTSLKKRAEDVAVIHIEIIGAVTKNqegkelaeLGDMVEAGAVafsddghfdP 158
Cdd:PRK07575 81 RACAKGGVTSFLEMPNTKPLtTTQAALDDKLARAAEKCVVNYGFFIGATPDN--------LPELLTANPT---------C 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 400189753 159 SAKVLLSAY--DYLVPFDKA-----------IINHEEDPSLVEDgamneghRSAMLGIKGRPIV--------AEDIAVAR 217
Cdd:PRK07575 144 GIKIFMGSShgPLLVDEEAAlerifaegtrlIAVHAEDQARIRA-------RRAEFAGISDPADhsqiqdeeAALLATRL 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 400189753 218 DIMLAEYAGAHVHVAHISSGRAVQLVREAKarGVRVTTEVTPHHLTMTDECVDPRDSSTKVNPPLRTEKDVEAMVAGLLD 297
Cdd:PRK07575 217 ALKLSKKYQRRLHILHLSTAIEAELLRQDK--PSWVTAEVTPQHLLLNTDAYERIGTLAQMNPPLRSPEDNEALWQALRD 294
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 400189753 298 GTIDMVVTDHSPHAPEEKDREYIYAPSGFPGLETALGVLLTDLvHTGKIPMETLIERMTCAPARVFKL-NAGTLAEGAPA 376
Cdd:PRK07575 295 GVIDFIATDHAPHTLEEKAQPYPNSPSGMPGVETSLPLMLTAA-MRGKCTVAQVVRWMSTAVARAYGIpNKGRIAPGYDA 373
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|
gi 400189753 377 DVTVIDPELIWTVDPKAFYTRGRHSPFAGRELKGRPVLTVVDGQIVMKDG 426
Cdd:PRK07575 374 DLVLVDLNTYRPVRREELLTKCGWSPFEGWNLTGWPVTTIVGGQIVFDRG 423
|
|
| D-HYD |
cd01314 |
D-hydantoinases (D-HYD) also called dihydropyrimidases (DHPase) and related proteins; DHPases ... |
4-426 |
1.80e-76 |
|
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: 244.82 E-value: 1.80e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 400189753 4 LLLKGGRVIDpaAKRNEICDVLIEDGVIRAVGANLSA-DGVEVYDASGKIVSPGFIDMHTHFREP--GQEAKEDFASGSR 80
Cdd:cd01314 1 LIIKNGTIVT--ADGSFKADILIEDGKIVAIGPNLEApGGVEVIDATGKYVLPGGIDPHTHLELPfmGTVTADDFESGTR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 400189753 81 AGAAGGYTTIATMPNTRPVVDDAALVTSLKKRAEDVAVIHIEIIGAVTKNQEgKELAELGDMVEAGAVAFsddghfdpsa 160
Cdd:cd01314 79 AAAAGGTTTIIDFAIPNKGQSLLEAVEKWRGKADGKSVIDYGFHMIITDWTD-SVIEELPELVKKGISSF---------- 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 400189753 161 KVLLsAYDYLVPFD-----KAIINHEEDPSLV----EDGAMNEGHRSAML--GIKG-------RPIVAEDIAVARDIMLA 222
Cdd:cd01314 148 KVFM-AYKGLLMVDdeellDVLKRAKELGALVmvhaENGDVIAELQKKLLaqGKTGpeyhalsRPPEVEAEATARAIRLA 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 400189753 223 EYAGAHVHVAHISSGRAVQLVREAKARGVRVTTEVTPHHLTMTDECVD-PRDSSTK--VNPPLRTEKDVEAMVAGLLDGT 299
Cdd:cd01314 227 ELAGAPLYIVHVSSKEAADEIARARKKGLPVYGETCPQYLLLDDSDYWkDWFEGAKyvCSPPLRPKEDQEALWDGLSSGT 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 400189753 300 IDMVVTDHSPHAPEEKDR---EYIYAPSGFPGLETALGVLLTDLVHTGKIPMETLIERMTCAPARVFKL--NAGTLAEGA 374
Cdd:cd01314 307 LQTVGSDHCPFNFAQKARgkdDFTKIPNGVPGVETRMPLLWSEGVAKGRITLEKFVELTSTNPAKIFGLypRKGTIAVGS 386
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|..
gi 400189753 375 PADVTVIDPELIWTVDPKAFYTRGRHSPFAGRELKGRPVLTVVDGQIVMKDG 426
Cdd:cd01314 387 DADLVIWDPNAEKTISADTHHHNVDYNIFEGMKVKGWPVVTISRGKVVVEDG 438
|
|
| PRK09060 |
PRK09060 |
dihydroorotase; Validated |
4-429 |
1.95e-74 |
|
dihydroorotase; Validated
Pssm-ID: 181632 [Multi-domain] Cd Length: 444 Bit Score: 239.44 E-value: 1.95e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 400189753 4 LLLKGGRVIDPAAKrnEICDVLIEDGVIRAVGANLSADGVEVYDASGKIVSPGFIDMHTHFREPGQEAKEDFASGSRAGA 83
Cdd:PRK09060 7 LILKGGTVVNPDGE--GRADIGIRDGRIAAIGDLSGASAGEVIDCRGLHVLPGVIDSQVHFREPGLEHKEDLETGSRAAV 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 400189753 84 AGGYTTIATMPNTRPVVDDAALVTSLKKRAEDVAviHIEI---IGAVTKNQEgkELAELGDMVEAGAVafsddghfdpsa 160
Cdd:PRK09060 85 LGGVTAVFEMPNTNPLTTTAEALADKLARARHRM--HCDFafyVGGTRDNAD--ELAELERLPGCAGI------------ 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 400189753 161 KVLL--SAYDYLVPFDKAIIN-----------HEEDPSLVED--GAMNEGHRSAmlgikgRPIVAEDIAVA----RDIML 221
Cdd:PRK09060 149 KVFMgsSTGDLLVEDDEGLRRilrngrrraafHSEDEYRLRErkGLRVEGDPSS------HPVWRDEEAALlatrRLVRL 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 400189753 222 AEYAGAHVHVAHISSGRAVQLVREAKARgvrVTTEVTPHHLTMT-DECVDPRDSSTKVNPPLRTEKDVEAMVAGLLDGTI 300
Cdd:PRK09060 223 ARETGRRIHVLHVSTAEEIDFLADHKDV---ATVEVTPHHLTLAaPECYERLGTLAQMNPPIRDARHRDGLWRGVRQGVV 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 400189753 301 DMVVTDHSPHAPEEKDREYIYAPSGFPGLETALGVLLtDLVHTGKIPMETLIERMTCAPARVFKL-NAGTLAEGAPADVT 379
Cdd:PRK09060 300 DVLGSDHAPHTLEEKAKPYPASPSGMTGVQTLVPIML-DHVNAGRLSLERFVDLTSAGPARIFGIaGKGRIAVGYDADFT 378
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|
gi 400189753 380 VIDPELIWTVDPKAFYTRGRHSPFAGRELKGRPVLTVVDGQIVMKDGVII 429
Cdd:PRK09060 379 IVDLKRRETITNEWIASRCGWTPYDGKEVTGWPVGTIVRGQRVMWDGELV 428
|
|
| PRK09236 |
PRK09236 |
dihydroorotase; Reviewed |
1-426 |
1.80e-70 |
|
dihydroorotase; Reviewed
Pssm-ID: 181716 Cd Length: 444 Bit Score: 228.99 E-value: 1.80e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 400189753 1 MGALLLKGGRVIdpaakrNE----ICDVLIEDGVIRAVGANLSADGV-EVYDASGKIVSPGFIDMHTHFREPGQEAKEDF 75
Cdd:PRK09236 1 MKRILIKNARIV------NEgkifEGDVLIENGRIAKIASSISAKSAdTVIDAAGRYLLPGMIDDQVHFREPGLTHKGDI 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 400189753 76 ASGSRAGAAGGYTTIATMPNTRPVVDDAALVTSLKKRAEDVAVIH-----------IEIIGAVTKNQ-EGKEL---AELG 140
Cdd:PRK09236 75 ASESRAAVAGGITSFMEMPNTNPPTTTLEALEAKYQIAAQRSLANysfyfgatndnLDEIKRLDPKRvCGVKVfmgASTG 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 400189753 141 DM-VEAGAV---AFSDdghfdpsAKVLlsaydylvpfdkaIINHEEDPSLVEdgAMNEGHRSAMlgikGRPIVAEDIAVA 216
Cdd:PRK09236 155 NMlVDNPETlerIFRD-------APTL-------------IATHCEDTPTIK--ANLAKYKEKY----GDDIPAEMHPLI 208
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 400189753 217 RD-----------IMLAEYAGAHVHVAHISSGRAVQLVREAKARGVRVTTEVTPHHLTMTDECVDPRDSSTKVNPPLRTE 285
Cdd:PRK09236 209 RSaeacykssslaVSLAKKHGTRLHVLHISTAKELSLFENGPLAEKRITAEVCVHHLWFDDSDYARLGNLIKCNPAIKTA 288
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 400189753 286 KDVEAMVAGLLDGTIDMVVTDHSPHAPEEKDREYIYAPSGFPGLETALGVLLtDLVHTGKIPMETLIERMTCAPARVFKL 365
Cdd:PRK09236 289 SDREALRQALADDRIDVIATDHAPHTWEEKQGPYFQAPSGLPLVQHALPALL-ELVHEGKLSLEKVVEKTSHAPAILFDI 367
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 400189753 366 -NAGTLAEGAPADVTVIDPELIWTVDPKAFYTRGRHSPFAGRELKGRPVLTVVDGQIVMKDG 426
Cdd:PRK09236 368 kERGFIREGYWADLVLVDLNSPWTVTKENILYKCGWSPFEGRTFRSRVATTFVNGQLVYHNG 429
|
|
| PRK08323 |
PRK08323 |
phenylhydantoinase; Validated |
4-429 |
3.73e-70 |
|
phenylhydantoinase; Validated
Pssm-ID: 236240 [Multi-domain] Cd Length: 459 Bit Score: 228.90 E-value: 3.73e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 400189753 4 LLLKGGRVIDpaAKRNEICDVLIEDGVIRAVGANlsaDGVEVYDASGKIVSPGFIDMHTHFREP--GQEAKEDFASGSRA 81
Cdd:PRK08323 3 TLIKNGTVVT--ADDTYKADVLIEDGKIAAIGAN---LGDEVIDATGKYVMPGGIDPHTHMEMPfgGTVSSDDFETGTRA 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 400189753 82 GAAGGYTTIATMPNTRPvvdDAALVTSLK---KRAEDVAVIHIEIIGAVTKNQEgKELAELGDMVEAGAVAF-------- 150
Cdd:PRK08323 78 AACGGTTTIIDFALQPK---GQSLREALEawhGKAAGKAVIDYGFHMIITDWNE-VVLDEMPELVEEGITSFklfmaykg 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 400189753 151 ---SDDGhfdpsakVLLSAydylvpFDKA------IINHEEDPSLVE---DGAMNEGHRSAMLGIKGRPIVAEDIAVARD 218
Cdd:PRK08323 154 almLDDD-------ELLRA------LQRAaelgalPMVHAENGDAIAylqAKLLAEGKTGPEYHALSRPPEVEGEATNRA 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 400189753 219 IMLAEYAGAHVHVAHISSGRAVQLVREAKARGVRVTTEVTPHHLTMTDECVD--PRDSSTK--VNPPLRTEKDVEAMVAG 294
Cdd:PRK08323 221 IMLAELAGAPLYIVHVSCKEALEAIRRARARGQRVFGETCPQYLLLDESEYDgpDWFEGAKyvMSPPLRDKEHQDALWRG 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 400189753 295 LLDGTIDMVVTDHSPHAPEEK------DREYIyaPSGFPGLETALGVLLTDLVHTGKIPMETLIErMTCA-PARVFKL-- 365
Cdd:PRK08323 301 LQDGDLQVVATDHCPFCFEQKkqlgrgDFTKI--PNGTPGVEDRMPLLFSEGVMTGRITLNRFVE-LTSTnPAKIFGLyp 377
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 400189753 366 NAGTLAEGAPADVTVIDPELIWTVDPKAFYTRGRHSPFAGRELKGRPVLTVVDGQIVMKDGVII 429
Cdd:PRK08323 378 RKGTIAVGADADIVIWDPNATKTISASTLHSNVDYNPYEGFEVTGWPVTTLSRGEVVVEDGEFR 441
|
|
| PRK04250 |
PRK04250 |
dihydroorotase; Provisional |
2-429 |
2.06e-67 |
|
dihydroorotase; Provisional
Pssm-ID: 235265 [Multi-domain] Cd Length: 398 Bit Score: 220.03 E-value: 2.06e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 400189753 2 GALLLKGgRVIDpaakrneiCDVLIEDGVIRAVGANlSADGVEVYDASGKIVSPGFIDMHTHFREPGQEAKEDFASGSRA 81
Cdd:PRK04250 4 GKFLLKG-RIVE--------GGIGIENGRISKISLR-DLKGKEVIKVKGGIILPGLIDVHVHLRDFEESYKETIESGTKA 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 400189753 82 GAAGGYTTIATMPNTRPVVDDAAL----VTSLKKRAEDVAVIHIEIIGAVTKNQEGKELAELGDMVEAGAVAFSDDghFD 157
Cdd:PRK04250 74 ALHGGITLVFDMPNTKPPIMDEKTyekrMRIAEKKSYADYALNFLIAGNCEKAEEIKADFYKIFMGASTGGIFSEN--FE 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 400189753 158 PSAKVLLsaydylvpfdKAIINHEEDPSLVEDGAMneghrsamlgikgRPIVAEDIAVARDIMLAEYAGAHVHVAHISSG 237
Cdd:PRK04250 152 VDYACAP----------GIVSVHAEDPELIREFPE-------------RPPEAEVVAIERALEAGKKLKKPLHICHISTK 208
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 400189753 238 RAVQLVReaKARGVRVTTEVTPHHLTMTDECVDpRDSSTKVNPPLRTEKDVEAMVAGLldGTIDMVVTDHSPHAPEEKDR 317
Cdd:PRK04250 209 DGLKLIL--KSNLPWVSFEVTPHHLFLTRKDYE-RNPLLKVYPPLRSEEDRKALWENF--SKIPIIASDHAPHTLEDKEA 283
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 400189753 318 eyiyAPSGFPGLETALGVLLtDLVHTGKIPMETLIERMTCAPARVFKLNAGTLAEGAPADVTVIDPELIWTVDPKAFYTR 397
Cdd:PRK04250 284 ----GAAGIPGLETEVPLLL-DAANKGMISLFDIVEKMHDNPARIFGIKNYGIEEGNYANFAVFDMKKEWTIKAEELYTK 358
|
410 420 430
....*....|....*....|....*....|..
gi 400189753 398 GRHSPFAGRELKGRPVLTVVDGQIVMKDGVII 429
Cdd:PRK04250 359 AGWTPYEGFKLKGKVIMTILRGEVVMEDDEII 390
|
|
| D-hydantoinase |
TIGR02033 |
D-hydantoinase; This model represents the D-hydantoinase (dihydropyrimidinase) which primarily ... |
4-426 |
9.92e-66 |
|
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: 217.25 E-value: 9.92e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 400189753 4 LLLKGGRVIDpaAKRNEICDVLIEDGVIRAVGANLSA-DGVEVYDASGKIVSPGFIDMHTHFREP--GQEAKEDFASGSR 80
Cdd:TIGR02033 1 LLIKGGTVVN--ADDVFQADVLIEGGKIVAVGDNLIPpDAVEVIDATGKYVLPGGIDVHTHLEMPfgGTTTADDFFTGTK 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 400189753 81 AGAAGGYTTIATMPNTRPVVDDAALVTSLKKRAEDVAVIHIEIIGAVTK-NQEGKELAElGDMVEAGAVAFsddghfdps 159
Cdd:TIGR02033 79 AAAAGGTTTIIDFVVPEKGSSLTEALETWHEKAEGKSVIDYGFHMDITHwNDSVLEEHI-PEVKEEGINSF--------- 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 400189753 160 aKVLLsAYDYLVPFDKAIInHEEDPSLVEDGAMNEGH------------RSAMLGIKG-------RPIVAEDIAVARDIM 220
Cdd:TIGR02033 149 -KVFM-AYKNLLMVDDEEL-FEILKRLKELGALLQVHaengdiiaelqaRMLAQGITGpeyhalsRPPELEAEAVARAIT 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 400189753 221 LAEYAGAHVHVAHISSGRAVQLVREAKARGVRVTTEVTPHHLTMTDECVDPRD---SSTKVNPPLRTEKDVEAMVAGLLD 297
Cdd:TIGR02033 226 LAALADAPLYVVHVSTKDAADEIAQARKKGQPVFGETCPQYLVLDDTHYDKPGfegAKYVCSPPLREPEDQDALWSALSS 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 400189753 298 GTIDMVVTDHSPHAPEEKDR----EYIYAPSGFPGLETALGVLLTDLVHTGKIPMETLIERMTCAPARVFKL--NAGTLA 371
Cdd:TIGR02033 306 GALQTVGSDHCTFNFAQKKAigkdDFTKIPNGGPGVEERMSLLFDEGVAKGRITLEKFVEVTSTNPAKIFNLypRKGTIA 385
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*
gi 400189753 372 EGAPADVTVIDPELIWTVDPKAFYTRGRHSPFAGRELKGRPVLTVVDGQIVMKDG 426
Cdd:TIGR02033 386 VGSDADIVIWDPNRTTVISAETHHSNADYNPFEGFKVRGAPVSVLSRGRVVVEDG 440
|
|
| CAD_DHOase |
cd01316 |
The eukaryotic CAD protein is a trifunctional enzyme of carbamoylphosphate ... |
55-429 |
1.20e-60 |
|
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: 200.75 E-value: 1.20e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 400189753 55 PGFIDMHTHFREPGQEAKEDFASGSRAGAAGGYTTIATMPNTRPVVDDAALVTSLKKRAEDVAVIHIEI-IGAVTKNQeg 133
Cdd:cd01316 6 PGLIDVHVHLREPGATHKEDFASGTKAALAGGFTMVRAMPNTNPSIVDVASLKLVQSLAQAKARCDYAFsIGATSTNA-- 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 400189753 134 KELAELGDmvEAGAVAFSDDGHFDPSAKVLLSAYDYLV---PFDKAIINHeedpslvedgamneghrsamlgikgrpivA 210
Cdd:cd01316 84 ATVGELAS--EAVGLKFYLNETFSTLILDKITAWASHFnawPSTKPIVTH-----------------------------A 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 400189753 211 EDIAVARDIMLAEYAGAHVHVAHISSGRAVQLVREAKARGVRVTTEVTPHHLTMTDEcvDPRDSSTKVNPPLRTEKDVEA 290
Cdd:cd01316 133 KSQTLAAVLLLASLHNRSIHICHVSSKEEINLIRLAKARGLKVTCEVSPHHLFLSQD--DLPRGQYEVRPFLPTREDQEA 210
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 400189753 291 MVAGLldGTIDMVVTDHSPHAPEEKDREYIyaPSGFPGLETALGVLLTdLVHTGKIPMETLIERMTCAPARVFKL--NAG 368
Cdd:cd01316 211 LWENL--DYIDCFATDHAPHTLAEKTGNKP--PPGFPGVETSLPLLLT-AVHEGRLTIEDIVDRLHTNPKRIFNLppQSD 285
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 400189753 369 TLAEgapadvtvIDPELIWTVDPKAFYTRGRHSPFAGRELKGRPVLTVVDGQIVMKDGVII 429
Cdd:cd01316 286 TYVE--------VDLDEEWTIPKNPLQSKKGWTPFEGKKVKGKVQRVVLRGETAFIDGEIV 338
|
|
| PLN02795 |
PLN02795 |
allantoinase |
9-426 |
5.56e-58 |
|
allantoinase
Pssm-ID: 178392 [Multi-domain] Cd Length: 505 Bit Score: 198.08 E-value: 5.56e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 400189753 9 GRVIDPAAKRNEicDVLIEDGVIRAV----GANLSADGVEVYDASGKIVSPGFIDMHTHFREPGQEAKEDFASGSRAGAA 84
Cdd:PLN02795 51 KRVVTPAGVIPG--AVEVEGGRIVSVtkeeEAPKSQKKPHVLDYGNAVVMPGLIDVHVHLNEPGRTEWEGFPTGTKAAAA 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 400189753 85 GGYTTIATMP-NTRPVVDDAALVTSLKKRAEDVAVIHIEIIGA-VTKNQegKELAELGDMVEAGAVAFSD-------DGH 155
Cdd:PLN02795 129 GGITTLVDMPlNSFPSTTSVETLELKIEAAKGKLYVDVGFWGGlVPENA--HNASVLEELLDAGALGLKSfmcpsgiNDF 206
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 400189753 156 FDPSAKVLLSAYDYLVPFDKAIINHEEDPSLVEDGAMNEGH-RSAMLGIKGRPIVAEDIAVARDIMLAEYA-------GA 227
Cdd:PLN02795 207 PMTTATHIKAALPVLAKYGRPLLVHAEVVSPVESDSRLDADpRSYSTYLKSRPPSWEQEAIRQLLEVAKDTrpggvaeGA 286
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 400189753 228 HVHVAHIS-SGRAVQLVREAKARGVRVTTEVTPHHLTMTDECVDPRDSSTKVNPPLRTEKDVEAMVAGLLDGTIDMVVTD 306
Cdd:PLN02795 287 HVHIVHLSdAESSLELIKEAKAKGDSVTVETCPHYLAFSAEEIPDGDTRYKCAPPIRDAANRELLWKALLDGDIDMLSSD 366
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 400189753 307 HSPHAPEEKDRE---YIYAPSGFPGLETALGVLLTDLVHTGkIPMETLIERMTCAPARVFKLNA-GTLAEGAPADVTVID 382
Cdd:PLN02795 367 HSPSPPDLKLLEegnFLRAWGGISSLQFVLPATWTAGRAYG-LTLEQLARWWSERPAKLAGLDSkGAIAPGKDADIVVWD 445
|
410 420 430 440
....*....|....*....|....*....|....*....|....*..
gi 400189753 383 PELIWTVD---PKAFYTRgRHSPFAGRELKGRPVLTVVDGQIVMKDG 426
Cdd:PLN02795 446 PEAEFVLDesyPIYHKHK-SLSPYLGTKLSGKVIATFVRGNLVFLEG 491
|
|
| PRK08417 |
PRK08417 |
metal-dependent hydrolase; |
24-424 |
2.59e-53 |
|
metal-dependent hydrolase;
Pssm-ID: 236262 [Multi-domain] Cd Length: 386 Bit Score: 182.59 E-value: 2.59e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 400189753 24 VLIEDGVIRAVGANLsaDGVEVYDASGKIVSPGFIDMHTHFREPGQEAKeDFASGSRAGAAGGYTTIATMPNTRPVVDDA 103
Cdd:PRK08417 1 IRIKDGKITEIGSDL--KGEEILDAKGKTLLPALVDLNVSLKNDSLSSK-NLKSLENECLKGGVGSIVLYPDSTPAIDNE 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 400189753 104 ALVTSLKKRAEDVAVIHIEIIGAVTKNQEGKELAELGDMveaGAVAFSDDGHFDpsAKVLLSAYDYLVPFDKAIINHEED 183
Cdd:PRK08417 78 IALELINSAQRELPMQIFPSIRALDEDGKLSNIATLLKK---GAKALELSSDLD--ANLLKVIAQYAKMLDVPIFCRCED 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 400189753 184 PSLVEDGAMNEGHRSAMLGIKGRPIVAEDIAVARDIMLAEYAGAHVHVAHISSGRAVQLVREAKARGVRVTTEVTPHHLT 263
Cdd:PRK08417 153 SSFDDSGVMNDGELSFELGLPGIPSIAETKEVAKMKELAKFYKNKVLFDTLALPRSLELLDKFKSEGEKLLKEVSIHHLI 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 400189753 264 MTDECVDPRDSSTKVNPPLRTEKDVEAMVAGLLDGTIDMVVTDHSPHAPEEKDREYIYAPSGFPGLETALGVLLTDLVHT 343
Cdd:PRK08417 233 LDDSACENFNTAAKLNPPLRSKEDRLALLEALKEGKIDFLTSLHSAKSNSKKDLAFDEAAFGIDSICEYFSLCYTYLVKE 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 400189753 344 GKIPMETLIERMTCAPARVFKLNAGTLAEGAPADVTVIDPELIWTVDPKafytrgrHSPFAGRELKGRPVLTVVDGQIVM 423
Cdd:PRK08417 313 GIITWSELSRFTSYNPAQFLGLNSGEIEVGKEADLVLFDPNESTIIDDN-------FSLYSGDELYGKIEAVIIKGKLYL 385
|
.
gi 400189753 424 K 424
Cdd:PRK08417 386 E 386
|
|
| PRK08044 |
PRK08044 |
allantoinase AllB; |
4-422 |
3.58e-53 |
|
allantoinase AllB;
Pssm-ID: 169193 [Multi-domain] Cd Length: 449 Bit Score: 183.90 E-value: 3.58e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 400189753 4 LLLKGGRVIDPAAKRneICDVLIEDGVIRAVGANLSaDGVEVYDASGKIVSPGFIDMHTHFREPGQEAKEDFASGSRAGA 83
Cdd:PRK08044 5 LIIKNGTVILENEAR--VVDIAVKGGKIAAIGQDLG-DAKEVMDASGLVVSPGMVDAHTHISEPGRSHWEGYETGTRAAA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 400189753 84 AGGYTTIATMP-NTRP-VVDDAALVTSLKKRAEDVAVIHIEIIGAVTKNqegkeLAELGDMVEAGAVAF----------S 151
Cdd:PRK08044 82 KGGITTMIEMPlNQLPaTVDRASIELKFDAAKGKLTIDAAQLGGLVSYN-----LDRLHELDEVGVVGFkcfvatcgdrG 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 400189753 152 DDGHF-DPSAKVLLSAYDYLVPFDKAIINHEEDPSLVE---DGAMNEGHRSAMLGIKGRPIVAEDIAVARDIMLAEYAGA 227
Cdd:PRK08044 157 IDNDFrDVNDWQFYKGAQKLGELGQPVLVHCENALICDelgEEAKREGRVTAHDYVASRPVFTEVEAIRRVLYLAKVAGC 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 400189753 228 HVHVAHISSGRAVQLVREAKARGVRVTTEVTPHHLTMTDECVDPRDSSTKVNPPLRTEKDVEAMVAGLLDGTIDMVVTDH 307
Cdd:PRK08044 237 RLHVCHISSPEGVEEVTRARQEGQDVTCESCPHYFVLDTDQFEEIGTLAKCSPPIRDLENQKGMWEKLFNGEIDCLVSDH 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 400189753 308 SPHAPEEKDREYIYAPSGFPGLETALGVLLTDLVHTGKIPMETLIERMTCAPARVFKL-NAGTLAEGAPADVTVIDPELI 386
Cdd:PRK08044 317 SPCPPEMKAGNIMEAWGGIAGLQNCMDVMFDEAVQKRGMSLPMFGKLMATNAADIFGLqQKGRIAPGKDADFVFIQPNSS 396
|
410 420 430
....*....|....*....|....*....|....*.
gi 400189753 387 WTVDPKAFYTRGRHSPFAGRELKGRPVLTVVDGQIV 422
Cdd:PRK08044 397 YVLKNEDLEYRHKVSPYVGRTIGARITKTILRGDVI 432
|
|
| PRK13404 |
PRK13404 |
dihydropyrimidinase; Provisional |
4-428 |
1.03e-52 |
|
dihydropyrimidinase; Provisional
Pssm-ID: 184033 [Multi-domain] Cd Length: 477 Bit Score: 183.36 E-value: 1.03e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 400189753 4 LLLKGGRVIdpAAKRNEICDVLIEDGVIRAVGANLSAdGVEVYDASGKIVSPGFIDMHTHFREP---GQEAKEDFASGSR 80
Cdd:PRK13404 6 LVIRGGTVV--TATDTFQADIGIRGGRIAALGEGLGP-GAREIDATGRLVLPGGVDSHCHIDQPsgdGIMMADDFYTGTV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 400189753 81 AGAAGGYTTIAT--MPNTRPVVDDAalVTSLKKRAEDVAVI----HIeIIGAVTKNQEGKELAELgdmVEAGAVAFsddg 154
Cdd:PRK13404 83 SAAFGGTTTVIPfaAQHRGQSLREA--VEDYHRRAAGKAVIdyafHL-IVADPTEEVLTEELPAL---IAQGYTSF---- 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 400189753 155 hfdpsaKVLLSaYDYLVPFDKAIIN--------------HEEDPSLVE---DGAMNEGHRSAMLGIKGRPIVAEDIAVAR 217
Cdd:PRK13404 153 ------KVFMT-YDDLKLDDRQILDvlavarrhgamvmvHAENHDMIAwltKRLLAAGLTAPKYHAISRPMLAEREATHR 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 400189753 218 DIMLAEYAGAHVHVAHISSGRAVQLVREAKARGVRVTTEVTPHHLTMTDECVD-PRDSSTK--VNPPLRTEKDVEAMVAG 294
Cdd:PRK13404 226 AIALAELVDVPILIVHVSGREAAEQIRRARGRGLKIFAETCPQYLFLTAEDLDrPGMEGAKyiCSPPPRDKANQEAIWNG 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 400189753 295 LLDGTIDMVVTDHSPH---APEEKDRE-----YIYAPSGFPGLETALGVLLTDLVHTGKIPMETLIERMTCAPARVFKLN 366
Cdd:PRK13404 306 LADGTFEVFSSDHAPFrfdDTDGKLAAganpsFKAIANGIPGIETRLPLLFSEGVVKGRISLNRFVALTSTNPAKLYGLY 385
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 400189753 367 A--GTLAEGAPADVTVIDPELIWTVDPKAFYTRGRHSPFAGRELKGRPVLTVVDGQIVMKDGVI 428
Cdd:PRK13404 386 PrkGAIAIGADADIAIWDPDREVTITNADLHHAADYTPYEGMRVTGWPVTVLSRGRVVVEDGEL 449
|
|
| PLN02942 |
PLN02942 |
dihydropyrimidinase |
4-428 |
1.46e-48 |
|
dihydropyrimidinase
Pssm-ID: 178530 Cd Length: 486 Bit Score: 172.34 E-value: 1.46e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 400189753 4 LLLKGGRVIDpaAKRNEICDVLIEDGVIRAVGANLSA-DGVEVYDASGKIVSPGFIDMHTHFREP--GQEAKEDFASGSR 80
Cdd:PLN02942 7 ILIKGGTVVN--AHHQELADVYVEDGIIVAVAPNLKVpDDVRVIDATGKFVMPGGIDPHTHLAMPfmGTETIDDFFSGQA 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 400189753 81 AGAAGGYTTIATMpnTRPVVDD-AALVTSLKKRAEDVAV---IHIeiigAVTKNQEGKElAELGDMV-EAGAVAFsddgh 155
Cdd:PLN02942 85 AALAGGTTMHIDF--VIPVNGNlLAGYEAYEKKAEKSCMdygFHM----AITKWDDTVS-RDMETLVkEKGINSF----- 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 400189753 156 fdpsaKVLLSAYDYLVPFDKAIIN--------------HEEDPSLVEDGAmnegHRSAMLGIKG-------RPIVAEDIA 214
Cdd:PLN02942 153 -----KFFMAYKGSLMVTDELLLEgfkrckslgalamvHAENGDAVFEGQ----KRMIELGITGpeghalsRPPLLEGEA 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 400189753 215 VARDIMLAEYAGAHVHVAHISSGRAVQLVREAKARGVRVTTEVTPHHLTMTDECVDPRDSSTK----VNPPLRTEKDVEA 290
Cdd:PLN02942 224 TARAIRLAKFVNTPLYVVHVMSIDAMEEIARARKSGQRVIGEPVVSGLVLDDSKLWDPDFTIAskyvMSPPIRPAGHGKA 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 400189753 291 MVAGLLDGTIDMVVTDHSPHAPEEK-----DREYIyaPSGFPGLETALGVLLTDLVHTGKIPMETLIERMTCAPARVFKL 365
Cdd:PLN02942 304 LQAALSSGILQLVGTDHCPFNSTQKafgkdDFRKI--PNGVNGIEERMHLVWDTMVESGQISPTDYVRVTSTECAKIFNI 381
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 400189753 366 --NAGTLAEGAPADVTVIDPELIWTVDPKAFYTRGRHSPFAGRELKGRPVLTVVDGQIVMKDGVI 428
Cdd:PLN02942 382 ypRKGAILAGSDADIIILNPNSTFTISAKTHHSRIDTNVYEGRRGKGKVEVTISQGRVVWENGEL 446
|
|
| pyrC |
PRK00369 |
dihydroorotase; Provisional |
50-426 |
6.44e-46 |
|
dihydroorotase; Provisional
Pssm-ID: 234738 [Multi-domain] Cd Length: 392 Bit Score: 163.01 E-value: 6.44e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 400189753 50 GKIVSPGFIDMHTHFREPGQEAKEDFASGSRAGAAGGYTTIATMPNTRPVVDDAALVTSLKKRAEDVAVIHIEIIGAVTk 129
Cdd:PRK00369 42 GTLILPGAIDLHVHLRGLKLSYKEDVASGTSEAAYGGVTLVADMPNTIPPLNTPEAITEKLAELEYYSRVDYFVYSGVT- 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 400189753 130 nqegKELAELGDMVEAGAVAFSDDGHFDPSAKVLLSAYdylvpfdKAIINHEEDPslvedgAMNEGHRSAMlgikgRPIV 209
Cdd:PRK00369 121 ----KDPEKVDKLPIAGYKIFPEDLEREETFRVLLKSR-------KLKILHPEVP------LALKSNRKLR-----RNCW 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 400189753 210 AEDIAVardIMLAEYagAHVHVAHISSGRAvqlVREAKARGvrVTTEVTPHHLTMTDEcvdpRDSSTKVNPPLRTEKDVE 289
Cdd:PRK00369 179 YEIAAL---YYVKDY--QNVHITHASNPRT---VRLAKELG--FTVDITPHHLLVNGE----KDCLTKVNPPIRDINERL 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 400189753 290 AMVAGLLDgtIDMVVTDHSPHAPEEKDREYIYAPSGFPGLETALGVLLTdLVHTGKIPMETLIERMTCAPARVFKLNAGT 369
Cdd:PRK00369 245 WLLQALSE--VDAIASDHAPHSSFEKLQPYEVCPPGIAALSFTPPFIYT-LVSKGILSIDRAVELISTNPARILGIPYGE 321
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*..
gi 400189753 370 LAEGAPADVTVIDPELiWTVDPKafYTRGRHSPFAGRELKGRPVLTVVDGQIVMKDG 426
Cdd:PRK00369 322 IKEGYRANFTVIQFED-WRYSTK--YSKVIETPLDGFELKASVYATIVQGKLAYLEG 375
|
|
| PRK01211 |
PRK01211 |
dihydroorotase; Provisional |
23-405 |
2.31e-44 |
|
dihydroorotase; Provisional
Pssm-ID: 179247 [Multi-domain] Cd Length: 409 Bit Score: 159.25 E-value: 2.31e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 400189753 23 DVLIEDGVIRAVGANLSADGVEVYDASgkiVSPGFIDMHTHFREPGQEAKEDFASGSRAGAAGGYTTIATMPNTRPVVDD 102
Cdd:PRK01211 17 EIEVEDGKIKSIKKDAGNIGKKELKGA---ILPAATDIHVHFRTPGETEKEDFSTGTLSAIFGGTTFIMDMPNNNIPIKD 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 400189753 103 AA-----LVTSLKKRAEDVAVIHIE------IIGAVT---KNQEGKELAELGDMVEAGAVAFSDDGHFdpsakvllsayd 168
Cdd:PRK01211 94 YNafsdkLGRVAPKAYVDFSLYSMEtgnnalILDERSiglKVYMGGTTNTNGTDIEGGEIKKINEANI------------ 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 400189753 169 ylvpfdkAIINHEEDPSLVEDGAMNEghRSAMLGIKGRPIVAEDIAVArdiMLAEYAGAHVHVAHISSGRAVQlvreaka 248
Cdd:PRK01211 162 -------PVFFHAELSECLRKHQFES--KNLRDHDLARPIECEIKAVK---YVKNLDLKTKIIAHVSSIDVIG------- 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 400189753 249 rgvRVTTEVTPHHLTMTDECvdPRDSSTKVNPPLRTEKDVEAMVAGLLDGTIDMVVTDHSPHApEEKDREYIYAPSGFPG 328
Cdd:PRK01211 223 ---RFLREVTPHHLLLNDDM--PLGSYGKVNPPLRDRWTQERLLEEYISGRFDILSSDHAPHT-EEDKQEFEYAKSGIIG 296
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 400189753 329 LETALGVLLTdLVHTGKIPMETLIERMTCAPARVFKLNAGTLAEGAPADVTVIDPELIWTVDPKAFYTRGRHSPFAG 405
Cdd:PRK01211 297 VETRVPLFLA-LVKKKILPLDVLYKTAIERPASLFGIKKGKIEEGYDADFMAFDFTNIKKINDKRLHSKCPVSPFNG 372
|
|
| D-aminoacylase |
cd01297 |
D-aminoacylases (N-acyl-D-Amino acid amidohydrolases) catalyze the hydrolysis of ... |
4-426 |
8.62e-28 |
|
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: 113.93 E-value: 8.62e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 400189753 4 LLLKGGRVIDPAAKRNEICDVLIEDGVIRAVGANLSADGVEVYDASGKIVSPGFIDMHTH-----FREPG---------- 68
Cdd:cd01297 2 LVIRNGTVVDGTGAPPFTADVGIRDGRIAAIGPILSTSAREVIDAAGLVVAPGFIDVHTHydgqvFWDPDlrpssrqgvt 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 400189753 69 ------------------QEAKEDFASGSRAGAAGGYTTIATMPN-------TRPVVDDAALVTSLKKRAEDVAVIHIEi 123
Cdd:cd01297 82 tvvlgncgvspapanpddLARLIMLMEGLVALGEGLPWGWATFAEyldaleaRPPAVNVAALVGHAALRRAVMGLDARE- 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 400189753 124 igaVTKNQEGKELAELGDMVEAGAVAFSDDGHFDPSAKV----LLSAYDYLVPFDKAIINHEEDPSLVEDGAMNEghrsa 199
Cdd:cd01297 161 ---ATEEELAKMRELLREALEAGALGISTGLAYAPRLYAgtaeLVALARVAARYGGVYQTHVRYEGDSILEALDE----- 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 400189753 200 MLGIkgrpivaediavardimlAEYAGAHVHVAHISS---------GRAVQLVREAKARGVRVTTEVTPHhltmtdecvd 270
Cdd:cd01297 233 LLRL------------------GRETGRPVHISHLKSagapnwgkiDRLLALIEAARAEGLQVTADVYPY---------- 284
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 400189753 271 prdsstkvnpPLRTEKDVEAMvaglLDGTIDMVVTDHSPHapeekdreyiyaPSGFPGLETALGVLLTDLVH-TGKIPME 349
Cdd:cd01297 285 ----------GAGSEDDVRRI----MAHPVVMGGSDGGAL------------GKPHPRSYGDFTRVLGHYVReRKLLSLE 338
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 400189753 350 TLIERMTCAPARVFKL-NAGTLAEGAPADVTVIDPEliwTVDPKAFYTRGRHSPfAGRElkgrpvLTVVDGQIVMKDG 426
Cdd:cd01297 339 EAVRKMTGLPARVFGLaDRGRIAPGYRADIVVFDPD---TLADRATFTRPNQPA-EGIE------AVLVNGVPVVRDG 406
|
|
| COG3653 |
COG3653 |
N-acyl-D-aspartate/D-glutamate deacylase [Secondary metabolites biosynthesis, transport and ... |
4-427 |
3.82e-24 |
|
N-acyl-D-aspartate/D-glutamate deacylase [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 442870 [Multi-domain] Cd Length: 528 Bit Score: 104.49 E-value: 3.82e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 400189753 4 LLLKGGRVID----PAAKRneicDVLIEDGVIRAVGANLSADGVEVYDASGKIVSPGFIDMHTH-----FREPGQEAK-- 72
Cdd:COG3653 4 LLIRGGTVVDgtgaPPFRA----DVAIKGGRIVAVGDLAAAEAARVIDATGLVVAPGFIDIHTHydlqlLWDPRLEPSlr 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 400189753 73 ---------ED---FA---SGSRAGAAGGYTTIATMPNTRPVVDD--AALVTSLKKR--AEDVAV------IHIEIIGAV 127
Cdd:COG3653 80 qgvttvvmgNCgvsFApvrPEDRDRLIDLMEGVEGIPEGLDWDWEsfGEYLDALERRglGVNVASlvghgtLRAYVMGLD 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 400189753 128 TKNQEGKELAELGDMV----EAGAVAFSDDGHFDPS-----------AKVllsaydyLVPFDKAIINHEEDPSLVEDGAM 192
Cdd:COG3653 160 DRPPTPEELARMRALLreamEAGALGLSTGLIYVPGtyastdelvalAKV-------VAEYGGVYQSHMRDEGDGLLEAV 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 400189753 193 NEGhrsamlgikgrpivaediavardIMLAEYAGAHVHVAHIS---------SGRAVQLVREAKARGVRVTTEVTPHHLT 263
Cdd:COG3653 233 DEL-----------------------IRIGREAGVPVHISHLKaagkpnwgkADEVLALIEAARAEGLDVTADVYPYPAG 289
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 400189753 264 MTDecvdprdsSTKVNPPLRTEKDVEAMVAGLLD-----------------------GTIDMVVTDHSPHAP-EEKDREY 319
Cdd:COG3653 290 STG--------LGALLPPWAAAGGLDERLARLRDpatrariraeieeglpdnllgrgGWDNILISDSPPNEPlVGKSLAE 361
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 400189753 320 IYAPSGFPGLETALGVLLTD-------------------LVH---------------------------------TGKIP 347
Cdd:COG3653 362 IAAERGVDPADAALDLLLEEdgrvlivyfimseedvrelLRHpwvmigsdgglggkahpraygtfprvlghyvreRGVLS 441
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 400189753 348 METLIERMTCAPARVFKL-NAGTLAEGAPADVTVIDPEliwTVDPKAFYTRgrhsPFAgrelkgRP---VLTVVDGQIVM 423
Cdd:COG3653 442 LEEAVRKLTSLPADRLGLkDRGLLRPGYRADLVVFDPA---TLADRATFDL----PAQ------RAdgiRAVIVNGVVVV 508
|
....
gi 400189753 424 KDGV 427
Cdd:COG3653 509 EDGK 512
|
|
| COG3964 |
COG3964 |
Predicted amidohydrolase [General function prediction only]; |
4-422 |
2.99e-20 |
|
Predicted amidohydrolase [General function prediction only];
Pssm-ID: 443164 [Multi-domain] Cd Length: 376 Bit Score: 91.77 E-value: 2.99e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 400189753 4 LLLKGGRVIDPAAKRNEICDVLIEDGVIRAVGANL-SADGVEVYDASGKIVSPGFIDMHTH-FrePGQEAKEDFASGsrA 81
Cdd:COG3964 2 LLIKGGRVIDPANGIDGVMDIAIKDGKIAAVAKDIdAAEAKKVIDASGLYVTPGLIDLHTHvF--PGGTDYGVDPDG--V 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 400189753 82 GAAGGYTTI--------ATMPNTRPVVDDAALVTSLkkraedvAVIHIEIIGAVTKNqegkELAELGDMVEAGAV-AFSD 152
Cdd:COG3964 78 GVRSGVTTVvdagsagaANFDGFRKYVIDPSKTRVL-------AFLNISGIGLVGGN----ELQDLDDIDPDATAaAAEA 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 400189753 153 DGHFDPSAKVLLSA-----YDyLVPFDKAIInheedpslvedgAMNEGHRSAMLGIKGRPIVAEDIA---VARDIMLAEY 224
Cdd:COG3964 147 NPDFIVGIKVRASKgvvgdNG-IEPLKRAKE------------AAKEAGLPLMVHIGNPPPPLDEVLdllRPGDILTHCF 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 400189753 225 AGaHVHVAHISSGRAVQLVREAKARGVRVttevtphhltmtdecvdprdsstkvnpplrtekDV-------------EAM 291
Cdd:COG3964 214 NG-KPNGILDEDGKVRPSVREARKRGVLF---------------------------------DVghggasfsfkvaePAI 259
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 400189753 292 VAGLLDGTI--DMVVtdHSPHAPeekdreyiyAPSgfpgletaLGVLLTDLVHTGkIPMETLIERMTCAPARVFKL-NAG 368
Cdd:COG3964 260 AQGFLPDTIstDLHT--RNMNGP---------VFD--------LATVMSKFLALG-MPLEEVIAAVTWNPARAIGLpELG 319
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 400189753 369 TLAEGAPADVTVIDPeliwtvdpkafytrgRHSPF-----AGRELKG----RPVLTVVDGQIV 422
Cdd:COG3964 320 TLSVGADADITIFDL---------------REGPFgftdsEGETLEGdrllEPEATVRGGKVV 367
|
|
| PRK09237 |
PRK09237 |
amidohydrolase/deacetylase family metallohydrolase; |
4-90 |
6.60e-20 |
|
amidohydrolase/deacetylase family metallohydrolase;
Pssm-ID: 236423 [Multi-domain] Cd Length: 380 Bit Score: 90.68 E-value: 6.60e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 400189753 4 LLLKGGRVIDPAAKRNEICDVLIEDGVIRAVGANLSA-DGVEVYDASGKIVSPGFIDMHTHFRepgQEAKEDFASGSRAG 82
Cdd:PRK09237 1 LLLRGGRVIDPANGIDGVIDIAIEDGKIAAVAGDIDGsQAKKVIDLSGLYVSPGWIDLHVHVY---PGSTPYGDEPDEVG 77
|
....*...
gi 400189753 83 AAGGYTTI 90
Cdd:PRK09237 78 VRSGVTTV 85
|
|
| PRK09061 |
PRK09061 |
D-glutamate deacylase; Validated |
4-426 |
6.45e-19 |
|
D-glutamate deacylase; Validated
Pssm-ID: 236369 [Multi-domain] Cd Length: 509 Bit Score: 88.60 E-value: 6.45e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 400189753 4 LLLKGGRVIDPAAKRNEICDVLIEDGVIRAVGANLsADGVEVYDASGKIVSPGFIDMHTHfrepGQEAKEDfasgsRAGA 83
Cdd:PRK09061 21 LVIRNGRVVDPETGLDAVRDVGIKGGKIAAVGTAA-IEGDRTIDATGLVVAPGFIDLHAH----GQSVAAY-----RMQA 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 400189753 84 AGGYTT-----IATMPNTRPVVDDAALVTSLKKRAEdVAVIHIEIIGAVTKNQEG---------------------KELA 137
Cdd:PRK09061 91 FDGVTTaleleAGVLPVARWYAEQAGEGRPLNYGAS-VGWTPARIAVLTGPQAEGtiadfgkalgdprwqeraatpAELA 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 400189753 138 ELGDMVE----AGAVAFSDDGHFDP--SAKVLLSAYDYLVPFDKAIINHEEDPSLVEdgamneghrsamlgikgrPIVAE 211
Cdd:PRK09061 170 EILELLEqgldEGALGIGIGAGYAPgtGHKEYLELARLAARAGVPTYTHVRYLSNVD------------------PRSSV 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 400189753 212 DiAVARDIMLAEYAGAHVHVAHISS------GRAVQLVREAKARGVRVTTEVTPHHLTMTD---ECVDPR---------D 273
Cdd:PRK09061 232 D-AYQELIAAAAETGAHMHICHVNStslrdiDRCLALVEKAQAQGLDVTTEAYPYGAGSTVvgaAFFDPGwlermglgyG 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 400189753 274 SSTKV--NPPLRTEKDVEAMVAGLLDG----------------TIDMVVTD-----HSPHAPEEKDREYIYAPSGFPGLE 330
Cdd:PRK09061 311 SLQWVetGERLLTREELAKLRANDPGGlvlihfldednprdraLLDRSVLFpgaaiASDAMPWTWSDGTVYEGDAWPLPE 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 400189753 331 TALG----------VLLTDLVHTGKIPMETLIERMTCAPARVFKL------NAGTLAEGAPADVTVIDPEliwTVDPKAF 394
Cdd:PRK09061 391 DAVShprsagtfarFLREYVRERKALSLLEAIRKCTLMPAQILEDsvpamrRKGRLQAGADADIVVFDPE---TITDRAT 467
|
490 500 510
....*....|....*....|....*....|..
gi 400189753 395 YTRGRHsPFAGRelkgRPVLtvVDGQIVMKDG 426
Cdd:PRK09061 468 FEDPNR-PSEGV----RHVL--VNGVPVVSNG 492
|
|
| Amidohydro_1 |
pfam01979 |
Amidohydrolase family; This family of enzymes are a a large metal dependent hydrolase ... |
52-422 |
5.51e-15 |
|
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: 75.62 E-value: 5.51e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 400189753 52 IVSPGFIDMHTHFR--------EPGQEAKEDFASGSRAGAAGGYTTIATMPNTRPVVDDAalvtsLKKRAEDVAV-IHIE 122
Cdd:pfam01979 1 IVLPGLIDAHVHLEmgllrgipVPPEFAYEALRLGITTMLKSGTTTVLDMGATTSTGIEA-----LLEAAEELPLgLRFL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 400189753 123 IIGAVTKNqEGKELAELGDMVEagavafsddghFDPSAKVLLSAYDYLVpfdKAIINHEEDPSLVEDG---AMNEGHRsa 199
Cdd:pfam01979 76 GPGCSLDT-DGELEGRKALREK-----------LKAGAEFIKGMADGVV---FVGLAPHGAPTFSDDElkaALEEAKK-- 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 400189753 200 mlgiKGRPI---VAEDIAVARDiMLAEYAGAHVHVAHISSGRAVQLVREAKARGVRVTTeVTPHHLTMTDECVDPRDSST 276
Cdd:pfam01979 139 ----YGLPVaihALETKGEVED-AIAAFGGGIEHGTHLEVAESGGLLDIIKLILAHGVH-LSPTEANLLAEHLKGAGVAH 212
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 400189753 277 KVNPPLRTEKDVEAMVAGLLDGTIDMVVTDHSPHapeekdreyIYAPSGFPGLETAlgvLLTDLVHTGKIPMETLIERMT 356
Cdd:pfam01979 213 CPFSNSKLRSGRIALRKALEDGVKVGLGTDGAGS---------GNSLNMLEELRLA---LELQFDPEGGLSPLEALRMAT 280
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 400189753 357 CAPARVFKL--NAGTLAEGAPADVTVIDPELIwtvdpkafytrgrhSPFAGRELKGRPVLTVVDGQIV 422
Cdd:pfam01979 281 INPAKALGLddKVGSIEVGKDADLVVVDLDPL--------------AAFFGLKPDGNVKKVIVKGKIV 334
|
|
| PRK08204 |
PRK08204 |
hypothetical protein; Provisional |
1-63 |
4.01e-14 |
|
hypothetical protein; Provisional
Pssm-ID: 181288 [Multi-domain] Cd Length: 449 Bit Score: 73.88 E-value: 4.01e-14
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 400189753 1 MGALLLKGGRVI--DPAAKRNEICDVLIEDGVIRAVGANLSADGVEVYDASGKIVSPGFIDMHTH 63
Cdd:PRK08204 1 MKRTLIRGGTVLtmDPAIGDLPRGDILIEGDRIAAVAPSIEAPDAEVVDARGMIVMPGLVDTHRH 65
|
|
| HutI |
COG1228 |
Imidazolonepropionase or related amidohydrolase [Secondary metabolites biosynthesis, transport ... |
1-94 |
2.54e-13 |
|
Imidazolonepropionase or related amidohydrolase [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 440841 [Multi-domain] Cd Length: 386 Bit Score: 71.15 E-value: 2.54e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 400189753 1 MGALLLKGGRVIDPAAKRN-EICDVLIEDGVIRAVGANLSA---DGVEVYDASGKIVSPGFIDMHTHFREPGQEAKEDFA 76
Cdd:COG1228 7 AGTLLITNATLVDGTGGGViENGTVLVEDGKIAAVGPAADLavpAGAEVIDATGKTVLPGLIDAHTHLGLGGGRAVEFEA 86
|
90 100 110
....*....|....*....|....*....|...
gi 400189753 77 SGSRAGA---------------AGGYTTIATMP 94
Cdd:COG1228 87 GGGITPTvdlvnpadkrlrralAAGVTTVRDLP 119
|
|
| FwdA |
COG1229 |
Formylmethanofuran dehydrogenase subunit A [Energy production and conversion]; |
4-63 |
3.63e-13 |
|
Formylmethanofuran dehydrogenase subunit A [Energy production and conversion];
Pssm-ID: 440842 Cd Length: 554 Bit Score: 70.99 E-value: 3.63e-13
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 400189753 4 LLLKGGRVIDPAAKRN-EICDVLIEDGVIraVGANLSADGVEVYDASGKIVSPGFIDMHTH 63
Cdd:COG1229 3 LIIKNGRVYDPANGIDgEVMDIAIKDGKI--VEEPSDPKDAKVIDASGKVVMAGGVDIHTH 61
|
|
| SsnA |
COG0402 |
Cytosine/adenosine deaminase or related metal-dependent hydrolase [Nucleotide transport and ... |
4-105 |
2.20e-11 |
|
Cytosine/adenosine deaminase or related metal-dependent hydrolase [Nucleotide transport and metabolism, General function prediction only]; Cytosine/adenosine deaminase or related metal-dependent hydrolase is part of the Pathway/BioSystem: Pyrimidine salvage
Pssm-ID: 440171 [Multi-domain] Cd Length: 416 Bit Score: 65.23 E-value: 2.20e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 400189753 4 LLLKGGRVIDPAAKRNEI--CDVLIEDGVIRAVGANLSA----DGVEVYDASGKIVSPGFIDMHTH-----FREPGQ--- 69
Cdd:COG0402 2 LLIRGAWVLTMDPAGGVLedGAVLVEDGRIAAVGPGAELparyPAAEVIDAGGKLVLPGLVNTHTHlpqtlLRGLADdlp 81
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 400189753 70 ------------EAK---EDFASGSRAGAA----GGYTTIATMPNTRPVVDDAAL 105
Cdd:COG0402 82 lldwleeyiwplEARldpEDVYAGALLALAemlrSGTTTVADFYYVHPESADALA 136
|
|
| NagA |
COG1820 |
N-acetylglucosamine-6-phosphate deacetylase [Carbohydrate transport and metabolism]; |
5-63 |
2.36e-10 |
|
N-acetylglucosamine-6-phosphate deacetylase [Carbohydrate transport and metabolism];
Pssm-ID: 441425 [Multi-domain] Cd Length: 373 Bit Score: 61.65 E-value: 2.36e-10
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 400189753 5 LLKGGRVIDPAAKRNEiCDVLIEDGVIRAVGAnLSADGVEVYDASGKIVSPGFIDMHTH 63
Cdd:COG1820 1 AITNARIFTGDGVLED-GALLIEDGRIAAIGP-GAEPDAEVIDLGGGYLAPGFIDLHVH 57
|
|
| Bact_CD |
cd01293 |
Bacterial cytosine deaminase and related metal-dependent hydrolases. Cytosine deaminases (CDs) ... |
5-63 |
3.78e-10 |
|
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: 61.11 E-value: 3.78e-10
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 400189753 5 LLKGGRVidpAAKRNEICDVLIEDGVIRAVGANLS-ADGVEVYDASGKIVSPGFIDMHTH 63
Cdd:cd01293 1 LLRNARL---ADGGTALVDIAIEDGRIAAIGPALAvPPDAEEVDAKGRLVLPAFVDPHIH 57
|
|
| FMDH_A |
cd01304 |
Formylmethanofuran dehydrogenase (FMDH) subunit A; Methanogenic bacteria and archea derive ... |
6-106 |
5.09e-10 |
|
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: 61.28 E-value: 5.09e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 400189753 6 LKGGRVIDPAAKRN-EICDVLIEDGviRAVGANLSADGVEVYDASGKIVSPGFIDMHTH-----------FR-EPGQEAK 72
Cdd:cd01304 1 IKNGTVYDPLNGINgEKMDIFIRDG--KIVESSSGAKPAKVIDASGKVVMAGGVDMHSHiaggkvnvgriLRpEDHRRDP 78
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 400189753 73 EDFASGSRAG---------------AAGGYTTI---ATMP-NTR---------PVVDDAALV 106
Cdd:cd01304 79 VPKGALRRAGvgfsvpstlatgyryAEMGYTTAfeaAMPPlNARhtheemadtPILDKGAYP 140
|
|
| ATZ_TRZ_like |
cd01298 |
TRZ/ATZ family contains enzymes from the atrazine degradation pathway and related hydrolases. ... |
4-64 |
1.52e-09 |
|
TRZ/ATZ family contains enzymes from the atrazine degradation pathway and related hydrolases. Atrazine, a chlorinated herbizide, can be catabolized by a variety of different bacteria. The first three steps of the atrazine dehalogenation pathway are catalyzed by atrazine chlorohydrolase (AtzA), hydroxyatrazine ethylaminohydrolase (AtzB), and N-isopropylammelide N-isopropylaminohydrolase (AtzC). All three enzymes belong to the superfamily of metal dependent hydrolases. AtzA and AtzB, beside other related enzymes are represented in this CD.
Pssm-ID: 238623 [Multi-domain] Cd Length: 411 Bit Score: 59.52 E-value: 1.52e-09
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 400189753 4 LLLKGGRVI-DPAAKRNEICDVLIEDGVIRAVGANLSA---DGVEVYDASGKIVSPGFIDMHTHF 64
Cdd:cd01298 1 ILIRNGTIVtTDPRRVLEDGDVLVEDGRIVAVGPALPLpayPADEVIDAKGKVVMPGLVNTHTHL 65
|
|
| Isoaspartyl-dipeptidase |
cd01308 |
Isoaspartyl dipeptidase hydrolyzes the beta-L-isoaspartyl linkages in dipeptides, as part of ... |
4-400 |
2.57e-09 |
|
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: 58.55 E-value: 2.57e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 400189753 4 LLLKGGRVIDPAAKRNeiCDVLIEDGVIRAVGANLSADG---VEVYDASGKIVSPGFIDMHTHFREPGQEakedfasgsr 80
Cdd:cd01308 2 TLIKNAEVYAPEYLGK--KDILIAGGKILAIEDQLNLPGyenVTVVDLHGKILVPGFIDQHVHIIGGGGE---------- 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 400189753 81 agaaGGYTTiatmpntrpvvddaalvtslkkRAEDVAVIHI------EIIGAVTKNQEGKELAEL----GDMVEAGAVAF 150
Cdd:cd01308 70 ----GGPST----------------------RTPEVTLSDLttagvtTVVGCLGTDGISRSMEDLlakaRALEEEGITCF 123
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 400189753 151 SDDGHFD-PSAKVLLSAYDYLVPFDKAIINHEedpslvedgAMNEGHRSAmlgikgRPIVAEDIAVARDI----MLAEYA 225
Cdd:cd01308 124 VYTGSYEvPTRTITGSIRKDLLLIDKVIGVGE---------IAISDHRSS------QPTVEELARIAAEArvggLLGGKA 188
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 400189753 226 G-AHVHVAhiSSGRAVQLVREAKARGVRVTTEVTPHHLTMTDECVDPR----------DSSTKVNPPLRTEKDVEA--MV 292
Cdd:cd01308 189 GiVHIHLG--DGKRALSPIFELIEETEIPITQFLPTHINRTAPLFEQGvefakmggtiDLTSSIDPQFRKEGEVRPseAL 266
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 400189753 293 AGLLDGTIDM----VVTDHSPHAPeEKDREYIYAPSGFPGLETALgVLLTDLVHTGKIPMETLIERMTCAPARVFKL-NA 367
Cdd:cd01308 267 KRLLEQGVPLeritFSSDGNGSLP-KFDENGNLVGLGVGSVDTLL-REVREAVKCGDIPLEVALRVITSNVARILKLrKK 344
|
410 420 430
....*....|....*....|....*....|....
gi 400189753 368 GTLAEGAPADVTVIDPEL-IWTVdpkafYTRGRH 400
Cdd:cd01308 345 GEIQPGFDADLVILDKDLdINSV-----IAKGQI 373
|
|
| Met_dep_hydrolase_B |
cd01307 |
Metallo-dependent hydrolases, subgroup B is part of the superfamily of metallo-dependent ... |
23-382 |
5.67e-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: 57.34 E-value: 5.67e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 400189753 23 DVLIEDGVIRAVGANLSADGV-EVYDASGKIVSPGFIDMHTHFREPGQEAKEDfasGSRAGAAGGYTTIATMPNTRPVVD 101
Cdd:cd01307 1 DVAIENGKIAAVGAALAAPAAtQIVDAGGCYVSPGWIDLHVHVYQGGTRYGDR---PDMIGVKSGVTTVVDAGSAGADNI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 400189753 102 DAALVTSLKKRAEDV-AVIHIEIIGAVtknqEGKELAELgDMVEAGAV--AFSDDGHFDPSAKVLLSAYDY----LVPFD 174
Cdd:cd01307 78 DGFRYTVIERSATRVyAFLNISRVGLV----AQDELPDP-DNIDEDAVvaAAREYPDVIVGLKARASKSVVgewgIKPLE 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 400189753 175 --KAIINHEEDPSLVEDGAMneghrsamlgikgRPIVAEDIAVAR--DImLAEYAGAHVHVAHISSGRAVQLVREAKARG 250
Cdd:cd01307 153 laKKIAKEADLPLMVHIGSP-------------PPILDEVVPLLRrgDV-LTHCFNGKPNGIVDEEGEVLPLVRRARERG 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 400189753 251 VRVTTEVTPHHLTMtdecvdprdsstkvnpplRTEKdvEAMVAGLLDGTIDM-VVTDHSPHAPeekdreyiyAPSGFPGL 329
Cdd:cd01307 219 VIFDVGHGTASFSF------------------RVAR--AAIAAGLLPDTISSdIHGRNRTNGP---------VYALATTL 269
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*.
gi 400189753 330 ET--ALGVlltdlvhtgkiPMETLIERMTCAPARVFKL-NAGTLAEGAPADVTVID 382
Cdd:cd01307 270 SKllALGM-----------PLEEVIEAVTANPARMLGLaEIGTLAVGYDADLTVFD 314
|
|
| PRK07203 |
PRK07203 |
putative aminohydrolase SsnA; |
4-64 |
6.23e-09 |
|
putative aminohydrolase SsnA;
Pssm-ID: 235963 [Multi-domain] Cd Length: 442 Bit Score: 57.64 E-value: 6.23e-09
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 400189753 4 LLLKGGRVI--DPAAKRNEICDVLIEDGVIRAVG--ANLSA--DGVEVYDASGKIVSPGFIDMHTHF 64
Cdd:PRK07203 2 LLIGNGTAItrDPAKPVIEDGAIAIEGNVIVEIGttDELKAkyPDAEFIDAKGKLIMPGLINSHNHI 68
|
|
| PRK08393 |
PRK08393 |
N-ethylammeline chlorohydrolase; Provisional |
3-63 |
1.01e-08 |
|
N-ethylammeline chlorohydrolase; Provisional
Pssm-ID: 181411 [Multi-domain] Cd Length: 424 Bit Score: 57.12 E-value: 1.01e-08
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 400189753 3 ALLLKGGRVIDPAAKRNEICDVLIEDGVIRAVGANLSADGVEVYDASGKIVSPGFIDMHTH 63
Cdd:PRK08393 2 SILIKNGYVIYGENLKVIRADVLIEGNKIVEVKRNINKPADTVIDASGSVVSPGFINAHTH 62
|
|
| AdeC |
COG1001 |
Adenine deaminase [Nucleotide transport and metabolism]; |
4-64 |
2.44e-08 |
|
Adenine deaminase [Nucleotide transport and metabolism];
Pssm-ID: 440625 [Multi-domain] Cd Length: 559 Bit Score: 55.88 E-value: 2.44e-08
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 400189753 4 LLLKGGRVIDPAAKRNEICDVLIEDGVIRAVGaNLSADGVEVYDASGKIVSPGFIDMHTHF 64
Cdd:COG1001 7 LVIKNGRLVNVFTGEILEGDIAIAGGRIAGVG-DYIGEATEVIDAAGRYLVPGFIDGHVHI 66
|
|
| Imidazolone-5PH |
cd01296 |
Imidazolonepropionase/imidazolone-5-propionate hydrolase (Imidazolone-5PH) catalyzes the third ... |
24-115 |
3.08e-08 |
|
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: 55.34 E-value: 3.08e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 400189753 24 VLIEDGVIRAVG-----ANLSADGVEVYDASGKIVSPGFIDMHTHF-----REPGQEAKEDFASGSRAGAAGGyTTIATM 93
Cdd:cd01296 1 IAIRDGRIAAVGpaaslPAPGPAAAEEIDAGGRAVTPGLVDCHTHLvfagdRVDEFAARLAGASYEEILAAGG-GILSTV 79
|
90 100
....*....|....*....|..
gi 400189753 94 PNTRPvVDDAALVTSLKKRAED 115
Cdd:cd01296 80 RATRA-ASEDELFASALRRLAR 100
|
|
| NagA |
cd00854 |
N-acetylglucosamine-6-phosphate deacetylase, NagA, catalyzes the hydrolysis of the N-acetyl ... |
4-122 |
6.50e-08 |
|
N-acetylglucosamine-6-phosphate deacetylase, NagA, catalyzes the hydrolysis of the N-acetyl group of N-acetyl-glucosamine-6-phosphate (GlcNAc-6-P) to glucosamine 6-phosphate and acetate. This is the first committed step in the biosynthetic pathway to amino-sugar-nucleotides, which is needed for cell wall peptidoglycan and teichoic acid biosynthesis. Deacetylation of N-acetylglucosamine is also important in lipopolysaccharide synthesis and cell wall recycling.
Pssm-ID: 238434 [Multi-domain] Cd Length: 374 Bit Score: 54.12 E-value: 6.50e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 400189753 4 LLLKGGRVIDPAAKRNEicDVLIEDGVIRAVGANLSAD-GVEVYDASGKIVSPGFIDMHTH------FREPGQEAkedFA 76
Cdd:cd00854 1 LIIKNARILTPGGLEDG--AVLVEDGKIVAIGPEDELEeADEIIDLKGQYLVPGFIDIHIHggggadFMDGTAEA---LK 75
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 400189753 77 SGSRAGAAGGYTTI--ATMPNTRPVVDDAALVTSLKKRAEDVAVI---HIE 122
Cdd:cd00854 76 TIAEALAKHGTTSFlpTTVTAPPEEIAKALAAIAEAIAEGQGAEIlgiHLE 126
|
|
| YtcJ |
COG1574 |
Predicted amidohydrolase YtcJ [General function prediction only]; |
4-71 |
7.01e-08 |
|
Predicted amidohydrolase YtcJ [General function prediction only];
Pssm-ID: 441182 [Multi-domain] Cd Length: 535 Bit Score: 54.42 E-value: 7.01e-08
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 400189753 4 LLLKGGRVI--DPAAKRNEicDVLIEDGVIRAVG-----ANLSADGVEVYDASGKIVSPGFIDMHTHFREPGQEA 71
Cdd:COG1574 10 LLLTNGRIYtmDPAQPVAE--AVAVRDGRIVAVGsdaevRALAGPATEVIDLGGKTVLPGFIDAHVHLLGGGLAL 82
|
|
| PRK12394 |
PRK12394 |
metallo-dependent hydrolase; |
4-70 |
7.80e-08 |
|
metallo-dependent hydrolase;
Pssm-ID: 183497 [Multi-domain] Cd Length: 379 Bit Score: 54.00 E-value: 7.80e-08
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 400189753 4 LLLKGGRVIDPAAKRNEICDVLIEDGVIRAVGANLSADGVEVYDASGKIVSPGFIDMHTHFREPGQE 70
Cdd:PRK12394 5 ILITNGHIIDPARNINEINNLRIINDIIVDADKYPVASETRIIHADGCIVTPGLIDYHAHVFYDGTE 71
|
|
| PRK09228 |
PRK09228 |
guanine deaminase; Provisional |
24-64 |
1.24e-07 |
|
guanine deaminase; Provisional
Pssm-ID: 236419 [Multi-domain] Cd Length: 433 Bit Score: 53.66 E-value: 1.24e-07
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 400189753 24 VLIEDGVIRAVG--ANLSA---DGVEVYDASGKIVSPGFIDMHTHF 64
Cdd:PRK09228 34 LLVEDGRIVAAGpyAELRAqlpADAEVTDYRGKLILPGFIDTHIHY 79
|
|
| Amidohydro_3 |
pfam07969 |
Amidohydrolase family; |
44-422 |
1.66e-07 |
|
Amidohydrolase family;
Pssm-ID: 400360 [Multi-domain] Cd Length: 464 Bit Score: 53.30 E-value: 1.66e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 400189753 44 EVYDASGKIVSPGFIDMHTHFREPGQEAKE---------------------------------DFASGSRAGAAGGYTTI 90
Cdd:pfam07969 1 EVIDAKGRLVLPGFVDPHTHLDGGGLNLRElrlpdvlpnavvkgqagrtpkgrwlvgegwdeaQFAETRFPYALADLDEV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 400189753 91 A--TMPNTRPVVDDAALVTS-LKKRAEDVAVIHIEIIGAVTKNQEGKEL-----------------AELGDMVEAGAVAF 150
Cdd:pfam07969 81 ApdGPVLLRALHTHAAVANSaALDLAGITKATEDPPGGEIARDANGEGLtgllregayalppllarEAEAAAVAAALAAL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 400189753 151 SDDG--HFDPSAKVLLSAYDYLVPFD--KAIINHEEDPSLVEDGAMNEGHRSAMLGIKgrpiVAEDIAVARDI--MLAEY 224
Cdd:pfam07969 161 PGFGitSVDGGGGNVHSLDDYEPLREltAAEKLKELLDAPERLGLPHSIYELRIGAMK----LFADGVLGSRTaaLTEPY 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 400189753 225 AGA-HVHVAHISSGRAVQLVREAKARGVRV--------------------------TTEVTPHHLTMTdecVDPRDSSTK 277
Cdd:pfam07969 237 FDApGTGWPDFEDEALAELVAAARERGLDVaihaigdatidtaldafeavaeklgnQGRVRIEHAQGV---VPYTYSQIE 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 400189753 278 VNPPLRTEKDVEAMVAGLLDGTIDMVVTDHSPHaPEEKDREYIYAP--------------SGFPGLETAL-------GVL 336
Cdd:pfam07969 314 RVAALGGAAGVQPVFDPLWGDWLQDRLGAERAR-GLTPVKELLNAGvkvalgsdapvgpfDPWPRIGAAVmrqtaggGEV 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 400189753 337 LTDlvhTGKIPMETLIERMTCAPARVFKL--NAGTLAEGAPADVTVIDPELIwTVDPKAFYTRgrhspfagrelkgRPVL 414
Cdd:pfam07969 393 LGP---DEELSLEEALALYTSGPAKALGLedRKGTLGVGKDADLVVLDDDPL-TVDPPAIADI-------------RVRL 455
|
....*...
gi 400189753 415 TVVDGQIV 422
Cdd:pfam07969 456 TVVDGRVV 463
|
|
| metallo-dependent_hydrolases |
cd01292 |
Superfamily of metallo-dependent hydrolases (also called amidohydrolase superfamily) is a ... |
57-361 |
1.91e-07 |
|
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: 52.34 E-value: 1.91e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 400189753 57 FIDMHTHFREPG------------------QEAKEDFASGSRAGAAGGYTTIATMPNTRPVVDDAALVTSLKKRAEDVAV 118
Cdd:cd01292 1 FIDTHVHLDGSAlrgtrlnlelkeaeelspEDLYEDTLRALEALLAGGVTTVVDMGSTPPPTTTKAAIEAVAEAARASAG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 400189753 119 IHI-------EIIGAVTKNQEGKELAELGDMVEAGAVAF---SDDGHFDPSAKVLLSAYDYLVPFDKAI-INHEEDPSLV 187
Cdd:cd01292 81 IRVvlglgipGVPAAVDEDAEALLLELLRRGLELGAVGLklaGPYTATGLSDESLRRVLEEARKLGLPVvIHAGELPDPT 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 400189753 188 EDGamneghrsamlgikgrpivaediavaRDIMLAEYAGAHVHVAHISSGRAVQLVReAKARGVRVttEVTPHHLTMTDe 267
Cdd:cd01292 161 RAL--------------------------EDLVALLRLGGRVVIGHVSHLDPELLEL-LKEAGVSL--EVCPLSNYLLG- 210
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 400189753 268 cvdprdsstkvnpplRTEKDVEAMVAGLLDGTIDMVVTDHSPHApeekdreyiyapsgfpgLETALGVLLTDLVHTGKIP 347
Cdd:cd01292 211 ---------------RDGEGAEALRRLLELGIRVTLGTDGPPHP-----------------LGTDLLALLRLLLKVLRLG 258
|
330
....*....|....*.
gi 400189753 348 M--ETLIERMTCAPAR 361
Cdd:cd01292 259 LslEEALRLATINPAR 274
|
|
| PRK06846 |
PRK06846 |
putative deaminase; Validated |
8-63 |
5.10e-07 |
|
putative deaminase; Validated
Pssm-ID: 235873 [Multi-domain] Cd Length: 410 Bit Score: 51.55 E-value: 5.10e-07
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 400189753 8 GGRVIdpaAKRNEICDVLIEDGVIRAVGANLSA--DGVEVYDASGKIVSPGFIDMHTH 63
Cdd:PRK06846 21 NGVIV---QTETALCTLEIQDGKIVAIRPNKQVpdATLPTYDANGLLMLPAFREMHIH 75
|
|
| PRK05985 |
PRK05985 |
cytosine deaminase; Provisional |
1-64 |
5.16e-07 |
|
cytosine deaminase; Provisional
Pssm-ID: 180337 [Multi-domain] Cd Length: 391 Bit Score: 51.47 E-value: 5.16e-07
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 400189753 1 MGALLLKGGRVIDPAAkrneiCDVLIEDGVIRAVGANLSAD-GVEVYDASGKIVSPGFIDMHTHF 64
Cdd:PRK05985 1 MTDLLFRNVRPAGGAA-----VDILIRDGRIAAIGPALAAPpGAEVEDGGGALALPGLVDGHIHL 60
|
|
| PRK07572 |
PRK07572 |
cytosine deaminase; Validated |
1-63 |
8.50e-07 |
|
cytosine deaminase; Validated
Pssm-ID: 181039 Cd Length: 426 Bit Score: 50.79 E-value: 8.50e-07
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 400189753 1 MGALLLKGGRVIDPAAKrneiCDVLIEDGVIRAVGANLSADGVEVYDASGKIVSPGFIDMHTH 63
Cdd:PRK07572 1 MFDLIVRNANLPDGRTG----IDIGIAGGRIAAVEPGLQAEAAEEIDAAGRLVSPPFVDPHFH 59
|
|
| Met_dep_hydrolase_C |
cd01309 |
Metallo-dependent hydrolases, subgroup C is part of the superfamily of metallo-dependent ... |
28-94 |
1.16e-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: 50.39 E-value: 1.16e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 400189753 28 DGVIRAVGANLSAD-GVEVYDASGKIVSPGFIDMHTH---FREPGQEAKEDFASGS-------RAG-------------A 83
Cdd:cd01309 1 DGKIVAVGAEITTPaDAEVIDAKGKHVTPGLIDAHSHlglDEEGGVRETSDANEETdpvtphvRAIdginpddeafkraR 80
|
90
....*....|.
gi 400189753 84 AGGYTTIATMP 94
Cdd:cd01309 81 AGGVTTVQVLP 91
|
|
| PRK06038 |
PRK06038 |
N-ethylammeline chlorohydrolase; Provisional |
1-63 |
3.46e-06 |
|
N-ethylammeline chlorohydrolase; Provisional
Pssm-ID: 180363 [Multi-domain] Cd Length: 430 Bit Score: 48.98 E-value: 3.46e-06
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 400189753 1 MGALLLKGGRVIDPAAKRNEICDVLIEDGVIRAVGANLSADGVEVYDASGKIVSPGFIDMHTH 63
Cdd:PRK06038 1 MADIIIKNAYVLTMDAGDLKKGSVVIEDGTITEVSESTPGDADTVIDAKGSVVMPGLVNTHTH 63
|
|
| PRK08203 |
PRK08203 |
hydroxydechloroatrazine ethylaminohydrolase; Reviewed |
4-64 |
3.50e-06 |
|
hydroxydechloroatrazine ethylaminohydrolase; Reviewed
Pssm-ID: 236184 [Multi-domain] Cd Length: 451 Bit Score: 49.08 E-value: 3.50e-06
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 400189753 4 LLLKGGRVI-DPAAKRNEICD--VLIEDGVIRAVGAN--LSADGVEVYDASGKIVSPGFIDMHTHF 64
Cdd:PRK08203 3 LWIKNPLAIvTMDAARREIADggLVVEGGRIVEVGPGgaLPQPADEVFDARGHVVTPGLVNTHHHF 68
|
|
| DHOase |
pfam12890 |
Dihydro-orotase-like; This is a small family of dihydro-orotase-like proteins from various ... |
50-236 |
5.42e-06 |
|
Dihydro-orotase-like; This is a small family of dihydro-orotase-like proteins from various bacteria.
Pssm-ID: 315550 [Multi-domain] Cd Length: 142 Bit Score: 46.02 E-value: 5.42e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 400189753 50 GKIVSPGFIDMHTHFREPGQEAKEDFAsgsragaaggyTTIATMPNTRPVVddaalvtslkkraedvAVIHIEiigavtk 129
Cdd:pfam12890 1 GRLIVPGLAFLHVHLTAPSGEAQELKE-----------TTWAAYGVTFKAP----------------AGITVE------- 46
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 400189753 130 nQEGKElaelgdmveagAVAFSDDGHFDPSAKVLLSAYDYlVPFDKAIINHEEDPSLVEDGAMNEGHRSAMLG--IKGrp 207
Cdd:pfam12890 47 -DDSEE-----------GFIFTNDTYYITIQLLEGEGMKK-SELDQELKAIATDDEVTNQSAVQDFELPQFYGtqLKG-- 111
|
170 180
....*....|....*....|....*....
gi 400189753 208 iVAEDIAVARDIMLAEYAGAHVHVAHISS 236
Cdd:pfam12890 112 -NCETEHCVYSYLLAKAAGCGFYVSIIYT 139
|
|
| PRK07228 |
PRK07228 |
5'-deoxyadenosine deaminase; |
1-63 |
6.31e-06 |
|
5'-deoxyadenosine deaminase;
Pssm-ID: 180895 [Multi-domain] Cd Length: 445 Bit Score: 48.07 E-value: 6.31e-06
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 400189753 1 MGALLLKGGRVIDPAAKRNEICDVLIEDGVIRAVGANLSADGV-EVYDASGKIVSPGFIDMHTH 63
Cdd:PRK07228 1 MTILIKNAGIVTMNAKREIVDGDVLIEDDRIAAVGDRLDLEDYdDHIDATGKVVIPGLIQGHIH 64
|
|
| ade |
TIGR01178 |
adenine deaminase; The family described by this model includes an experimentally characterized ... |
23-63 |
9.68e-06 |
|
adenine deaminase; The family described by this model includes an experimentally characterized adenine deaminase of Bacillus subtilis. It also include a member from Methanobacterium thermoautotrophicum, in which adenine deaminase activity has been detected. [Purines, pyrimidines, nucleosides, and nucleotides, Salvage of nucleosides and nucleotides]
Pssm-ID: 130246 [Multi-domain] Cd Length: 552 Bit Score: 47.84 E-value: 9.68e-06
10 20 30 40
....*....|....*....|....*....|....*....|.
gi 400189753 23 DVLIEDGVIRAVGANlsaDGVEVYDASGKIVSPGFIDMHTH 63
Cdd:TIGR01178 21 DIAIANGHIAGVGKY---NGVKVIDALGEYAVPGFIDAHIH 58
|
|
| PRK15446 |
PRK15446 |
phosphonate metabolism protein PhnM; Provisional |
1-62 |
2.13e-05 |
|
phosphonate metabolism protein PhnM; Provisional
Pssm-ID: 237967 [Multi-domain] Cd Length: 383 Bit Score: 46.33 E-value: 2.13e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 400189753 1 MGALLLKGGRVIDPaakrNEI--CDVLIEDGVIRAVGANlSADGVEVYDASGKIVSPGFIDMHT 62
Cdd:PRK15446 1 MMEMILSNARLVLP----DEVvdGSLLIEDGRIAAIDPG-ASALPGAIDAEGDYLLPGLVDLHT 59
|
|
| PRK07583 |
PRK07583 |
cytosine deaminase; |
23-63 |
2.46e-05 |
|
cytosine deaminase;
Pssm-ID: 236062 Cd Length: 438 Bit Score: 46.13 E-value: 2.46e-05
10 20 30 40
....*....|....*....|....*....|....*....|..
gi 400189753 23 DVLIEDGVIRAVG-ANLSADGVEVYDASGKIVSPGFIDMHTH 63
Cdd:PRK07583 42 DIEIADGKIAAILpAGGAPDELPAVDLKGRMVWPCFVDMHTH 83
|
|
| YtcJ_like |
cd01300 |
YtcJ_like metal dependent amidohydrolases. YtcJ is a Bacillus subtilis ORF of unknown function. ... |
23-71 |
3.66e-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: 45.76 E-value: 3.66e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 400189753 23 DVLIEDGVIRAVG-----ANLSADGVEVYDASGKIVSPGFIDMHTHFREPGQEA 71
Cdd:cd01300 1 AVAVRDGRIVAVGsdaeaKALKGPATEVIDLKGKTVLPGFIDSHSHLLLGGLSL 54
|
|
| ureC |
PRK13308 |
urease subunit alpha; Reviewed |
2-98 |
1.62e-04 |
|
urease subunit alpha; Reviewed
Pssm-ID: 183965 [Multi-domain] Cd Length: 569 Bit Score: 43.93 E-value: 1.62e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 400189753 2 GAL--LLKGGRVIDPAAKRNEiCDVLIEDGVIRAVGAN---LSADGVE----------VYDASGKIVSPGFIDMHTHFRE 66
Cdd:PRK13308 66 GALdfVLCNVTVIDPVLGIVK-GDIGIRDGRIVGIGKAgnpDIMDGVDprlvvgpgtdVRPAEGLIATPGAIDVHVHFDS 144
|
90 100 110
....*....|....*....|....*....|..
gi 400189753 67 PGQeAKEDFASGSRAGAAGGYTTIATMPNTRP 98
Cdd:PRK13308 145 AQL-VDHALASGITTMLGGGLGPTVGIDSGGP 175
|
|
| DHOase |
cd01294 |
Dihydroorotase (DHOase) catalyzes the reversible interconversion of carbamoyl aspartate to ... |
233-342 |
9.53e-04 |
|
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: 41.11 E-value: 9.53e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 400189753 233 HISSGRAVQLVREAKArgvRVTTEVTPHHLTMTdecvdpRD--SSTKVNP-----P-LRTEKDVEAMVAGLLDGTID-MV 303
Cdd:cd01294 169 HITTADAVEYVKSCNE---NVAATITPHHLLLT------RDdlLGGGLNPhlyckPvAKRPEDREALRKAATSGHPKfFL 239
|
90 100 110
....*....|....*....|....*....|....*....
gi 400189753 304 VTDHSPHAPEEKdreyiYAPSGFPGLETALgVLLTDLVH 342
Cdd:cd01294 240 GSDSAPHPKSNK-----ESSCGCAGIFSAP-IALPYLAE 272
|
|
| hutI |
TIGR01224 |
imidazolonepropionase; This enzyme catalyzes the third step in histidine degradation. [Energy ... |
24-73 |
1.18e-03 |
|
imidazolonepropionase; This enzyme catalyzes the third step in histidine degradation. [Energy metabolism, Amino acids and amines]
Pssm-ID: 273512 [Multi-domain] Cd Length: 377 Bit Score: 40.86 E-value: 1.18e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 400189753 24 VLIEDGVIRAVG---ANLSADGVEVYDASGKIVSPGFIDMHTHFREPGQEAKE 73
Cdd:TIGR01224 6 ILIHGGKIVWIGqlaALPGEEATEIIDCGGGLVTPGLVDPHTHLVFAGDRVNE 58
|
|
| PRK06380 |
PRK06380 |
metal-dependent hydrolase; Provisional |
23-63 |
1.28e-03 |
|
metal-dependent hydrolase; Provisional
Pssm-ID: 180548 [Multi-domain] Cd Length: 418 Bit Score: 41.02 E-value: 1.28e-03
10 20 30 40
....*....|....*....|....*....|....*....|.
gi 400189753 23 DVLIEDGVIRAVGaNLSADGVEVYDASGKIVSPGFIDMHTH 63
Cdd:PRK06380 23 NVYIEGNKIVYVG-DVNEEADYIIDATGKVVMPGLINTHAH 62
|
|
| Urease_alpha |
cd00375 |
Urease alpha-subunit; Urease is a nickel-dependent metalloenzyme that catalyzes the hydrolysis ... |
23-150 |
1.78e-03 |
|
Urease alpha-subunit; Urease is a nickel-dependent metalloenzyme that catalyzes the hydrolysis of urea to form ammonia and carbon dioxide. Nickel-dependent ureases are found in bacteria, fungi and plants. Their primary role is to allow the use of external and internally generated urea as a nitrogen source. The enzyme consists of 3 subunits, alpha, beta and gamma, which can be fused and present on a single protein chain and which in turn forms multimers, mainly trimers. The large alpha subunit is the catalytic domain containing an active site with a bi-nickel center complexed by a carbamylated lysine. The beta and gamma subunits play a role in subunit association to form the higher order trimers.
Pssm-ID: 238221 [Multi-domain] Cd Length: 567 Bit Score: 40.39 E-value: 1.78e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 400189753 23 DVLIEDGVIRAVG--ANLSA-DGV----------EVYDASGKIVSPGFIDMHTHFREPgQEAKEDFASGSRAGAAGGY-- 87
Cdd:cd00375 84 DIGIKDGRIVAIGkaGNPDImDGVtpnmivgpstEVIAGEGKIVTAGGIDTHVHFICP-QQIEEALASGITTMIGGGTgp 162
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 400189753 88 --TTIATMPNTRPVVDDAALvtslkkRAEDVAVIHIEIIGavtKNQeGKELAELGDMVEAGAVAF 150
Cdd:cd00375 163 aaGTKATTCTPGPWNIKRML------QAADGLPVNIGFLG---KGN-GSSPDALAEQIEAGACGL 217
|
|
| ureC |
PRK13207 |
urease subunit alpha; Reviewed |
26-78 |
4.88e-03 |
|
urease subunit alpha; Reviewed
Pssm-ID: 237305 [Multi-domain] Cd Length: 568 Bit Score: 39.00 E-value: 4.88e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 400189753 26 IEDGVIRAVGAnlsadGVEVYDASGKIVSPGFIDMHTHFREPgQEAKEDFASG 78
Cdd:PRK13207 105 IQDGVDIIIGP-----GTEVIAGEGLIVTAGGIDTHIHFICP-QQIEEALASG 151
|
|
| GDEase |
cd01303 |
Guanine deaminase (GDEase). Guanine deaminase is an aminohydrolase responsible for the ... |
24-64 |
5.29e-03 |
|
Guanine deaminase (GDEase). Guanine deaminase is an aminohydrolase responsible for the conversion of guanine to xanthine and ammonia, the first step to utilize guanine as a nitrogen source. This reaction also removes the guanine base from the pool and therefore can play a role in the regulation of cellular GTP and the guanylate nucleotide pool.
Pssm-ID: 238628 [Multi-domain] Cd Length: 429 Bit Score: 38.80 E-value: 5.29e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 400189753 24 VLIEDGVIRAVGA-----NLSADGVEVYDASGKIVSPGFIDMHTHF 64
Cdd:cd01303 29 IVVVDGNIIAAGAaetlkRAAKPGARVIDSPNQFILPGFIDTHIHA 74
|
|
| nagA |
PRK11170 |
N-acetylglucosamine-6-phosphate deacetylase; Provisional |
24-60 |
9.35e-03 |
|
N-acetylglucosamine-6-phosphate deacetylase; Provisional
Pssm-ID: 183010 Cd Length: 382 Bit Score: 38.03 E-value: 9.35e-03
10 20 30
....*....|....*....|....*....|....*....
gi 400189753 24 VLIEDGVIRAV--GANLSAdGVEVYDASGKIVSPGFIDM 60
Cdd:PRK11170 21 VVIADGLIEAVcpVAELPP-GIEQRDLNGAILSPGFIDL 58
|
|
| |
