|
Name |
Accession |
Description |
Interval |
E-value |
| AllB |
COG0044 |
Dihydroorotase or related cyclic amidohydrolase [Nucleotide transport and metabolism]; ... |
14-431 |
3.65e-148 |
|
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: 428.36 E-value: 3.65e-148
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486032191 14 LTGGQLFEPGKGLISNpgLLVRNGRIEAVGEQAQAAESAATLDAAGQVIAPGFIDLCCNLREPGNGQKGNIASETRAAAH 93
Cdd:COG0044 2 IKNGRVVDPGGLERAD--VLIEDGRIAAIGPDLAAPEAAEVIDATGLLVLPGLIDLHVHLREPGLEHKEDIETGTRAAAA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486032191 94 GGFTTVCASPETSPVNDSGAVTNLILDSVASRGVVRVLPIGAITRGLdGDMLSDMAGLKAAGCVAV-----GNGSRGVRN 168
Cdd:COG0044 80 GGVTTVVDMPNTNPVTDTPEALEFKLARAEEKALVDVGPHGALTKGL-GENLAELGALAEAGAVAFkvfmgSDDGNPVLD 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486032191 169 ARILRRCMAYAQTFGLTVMFSPENTALAADGYAHDGQVTTRLGLLGIPEVAETAAVMEMLLLAEETGVRLHLSQLSCARS 248
Cdd:COG0044 159 DGLLRRALEYAAEFGALVAVHAEDPDLIRGGVMNEGKTSPRLGLKGRPAEAEEEAVARDIALAEETGARLHIVHVSTAEA 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486032191 249 VEMLAQARDRGVKVTADVAMHQLAFTESALAGFDSRFHVRPPLRGEADRQALVAGVRDGVIDAIVSQHQPHDSAAKQAPL 328
Cdd:COG0044 239 VELIREAKARGLPVTAEVCPHHLTLTDEDLERYGTNFKVNPPLRTEEDREALWEGLADGTIDVIATDHAPHTLEEKELPF 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486032191 329 PATEPGLSSIESVLSLGL-ELVQNHELELPDLLRALTAGPAAVLG--REVALTAGAAADLCLFAPDGHWQPSAATLLSAG 405
Cdd:COG0044 319 AEAPNGIPGLETALPLLLtELVHKGRLSLERLVELLSTNPARIFGlpRKGRIAVGADADLVLFDPDAEWTVTAEDLHSKS 398
|
410 420
....*....|....*....|....*.
gi 2486032191 406 RHAPVLERALPGEVKLTLVAGRTAWQ 431
Cdd:COG0044 399 KNTPFEGRELTGRVVATIVRGRVVYE 424
|
|
| pyrC |
PRK09357 |
dihydroorotase; Validated |
14-432 |
2.85e-144 |
|
dihydroorotase; Validated
Pssm-ID: 236479 [Multi-domain] Cd Length: 423 Bit Score: 418.06 E-value: 2.85e-144
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486032191 14 LTGGQLFEPgKGLISNPGLLVRNGRIEAVGEQAQAAESAaTLDAAGQVIAPGFIDLCCNLREPGNGQKGNIASETRAAAH 93
Cdd:PRK09357 5 IKNGRVIDP-KGLDEVADVLIDDGKIAAIGENIEAEGAE-VIDATGLVVAPGLVDLHVHLREPGQEDKETIETGSRAAAA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486032191 94 GGFTTVCASPETSPVNDSGAVTNLILDSVASRGVVRVLPIGAITRGLDGDMLSDMAGLKAAGCVAVGNGSRGVRNARILR 173
Cdd:PRK09357 83 GGFTTVVAMPNTKPVIDTPEVVEYVLDRAKEAGLVDVLPVGAITKGLAGEELTEFGALKEAGVVAFSDDGIPVQDARLMR 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486032191 174 RCMAYAQTFGLTVMFSPENTALAADGYAHDGQVTTRLGLLGIPEVAETAAVMEMLLLAEETGVRLHLSQLSCARSVEMLA 253
Cdd:PRK09357 163 RALEYAKALDLLIAQHCEDPSLTEGGVMNEGEVSARLGLPGIPAVAEEVMIARDVLLAEATGARVHICHVSTAGSVELIR 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486032191 254 QARDRGVKVTADVAMHQLAFTESALAGFDSRFHVRPPLRGEADRQALVAGVRDGVIDAIVSQHQPHDSAAKQAPLPATEP 333
Cdd:PRK09357 243 WAKALGIKVTAEVTPHHLLLTDEDLLTYDPNYKVNPPLRTEEDREALIEGLKDGTIDAIATDHAPHAREEKECEFEAAPF 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486032191 334 GLSSIESVLSLGL-ELVQNHELELPDLLRALTAGPAAVLG-REVALTAGAAADLCLFAPDGHWQPSAATLLSAGRHAPVL 411
Cdd:PRK09357 323 GITGLETALSLLYtTLVKTGLLDLEQLLEKMTINPARILGlPAGPLAEGEPADLVIFDPEAEWTVDGEDFASKGKNTPFI 402
|
410 420
....*....|....*....|.
gi 2486032191 412 ERALPGEVKLTLVAGRTAWQA 432
Cdd:PRK09357 403 GMKLKGKVVYTIVDGKIVYQD 423
|
|
| DHOase_IIa |
cd01317 |
Dihydroorotase (DHOase), subgroup IIa; DHOases catalyze the reversible interconversion of ... |
54-422 |
2.33e-142 |
|
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: 411.25 E-value: 2.33e-142
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486032191 54 TLDAAGQVIAPGFIDLCCNLREPGNGQKGNIASETRAAAHGGFTTVCASPETSPVNDSGAVTNLILDSVASRGVVRVLPI 133
Cdd:cd01317 4 VIDAEGKILAPGLVDLHVHLREPGFEYKETLESGAKAAAAGGFTTVVCMPNTNPVIDNPAVVELLKNRAKDVGIVRVLPI 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486032191 134 GAITRGLDGDMLSDMAGLKAAGCVAVGNGSRGVRNARILRRCMAYAQTFGLTVMFSPENTALAADGYAHDGQVTTRLGLL 213
Cdd:cd01317 84 GALTKGLKGEELTEIGELLEAGAVGFSDDGKPIQDAELLRRALEYAAMLDLPIIVHPEDPSLAGGGVMNEGKVASRLGLP 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486032191 214 GIPEVAETAAVMEMLLLAEETGVRLHLSQLSCARSVEMLAQARDRGVKVTADVAMHQLAFTESALAGFDSRFHVRPPLRG 293
Cdd:cd01317 164 GIPPEAETIMVARDLELAEATGARVHFQHLSTARSLELIRKAKAKGLPVTAEVTPHHLLLDDEALESYDTNAKVNPPLRS 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486032191 294 EADRQALVAGVRDGVIDAIVSQHQPHDSAAKQAPLPATEPGLSSIESVLSLGL-ELVQNHELELPDLLRALTAGPAAVLG 372
Cdd:cd01317 244 EEDREALIEALKDGTIDAIASDHAPHTDEEKDLPFAEAPPGIIGLETALPLLWtLLVKGGLLTLPDLIRALSTNPAKILG 323
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|.
gi 2486032191 373 REVA-LTAGAAADLCLFAPDGHWQPSAATLLSAGRHAPVLERALPGEVKLT 422
Cdd:cd01317 324 LPPGrLEVGAPADLVLFDPDAEWIVDEETFRSKSKNTPFDGQKLKGRVLAT 374
|
|
| PRK07627 |
PRK07627 |
dihydroorotase; Provisional |
12-433 |
2.07e-123 |
|
dihydroorotase; Provisional
Pssm-ID: 181059 [Multi-domain] Cd Length: 425 Bit Score: 364.77 E-value: 2.07e-123
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486032191 12 LKLTGGQLFEPGKGLISNPGLLVRNGRIEAVGEQAQAAESAATLDAAGQVIAPGFIDLCCNLREPGNGQKGNIASETRAA 91
Cdd:PRK07627 3 IHIKGGRLIDPAAGTDRQADLYVAAGKIAAIGQAPAGFNADKTIDASGLIVCPGLVDLSARLREPGYEYKATLESEMAAA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486032191 92 AHGGFTTVCASPETSPVNDSGAVTNLILDSVASRGVVRVLPIGAITRGLDGDMLSDMAGLKAAGCVAVGNGSRGVRNARI 171
Cdd:PRK07627 83 VAGGVTSLVCPPDTDPVLDEPGLVEMLKFRARNLNQAHVYPLGALTVGLKGEVLTEMVELTEAGCVGFSQANVPVVDTQV 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486032191 172 LRRCMAYAQTFGLTVMFSPENTALAADGYAHDGQVTTRLGLLGIPEVAETAAVMEMLLLAEETGVRLHLSQLSCARSVEM 251
Cdd:PRK07627 163 LLRALQYASTFGFTVWLRPLDAFLGRGGVAASGAVASRLGLSGVPVAAETIALHTIFELMRVTGARVHLARLSSAAGVAL 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486032191 252 LAQARDRGVKVTADVAMHQLAFTESALAGFDSRFHVRPPLRGEADRQALVAGVRDGVIDAIVSQHQPHDSAAKQAPLPAT 331
Cdd:PRK07627 243 VRAAKAEGLPVTCDVGVNHVHLIDVDIGYFDSQFRLDPPLRSQRDREAIRAALADGTIDAICSDHTPVDDDEKLLPFAEA 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486032191 332 EPGLSSIESVLSLGLELVQNHELELPDLLRALTAGPAAVLGREVA-LTAGAAADLCLFAPDGHWQPSAATLLSAGRHAPV 410
Cdd:PRK07627 323 TPGATGLELLLPLTLKWADEAKVPLARALARITSAPARVLGLPAGrLAEGAPADLCVFDPDAHWRVEPRALKSQGKNTPF 402
|
410 420
....*....|....*....|...
gi 2486032191 411 LERALPGEVKLTLVAGRTAWQAP 433
Cdd:PRK07627 403 LGYELPGRVRATLVAGQVAFERR 425
|
|
| PRK09059 |
PRK09059 |
dihydroorotase; Validated |
14-428 |
1.51e-96 |
|
dihydroorotase; Validated
Pssm-ID: 181631 [Multi-domain] Cd Length: 429 Bit Score: 296.18 E-value: 1.51e-96
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486032191 14 LTGGQLFEPGKGLISNPGLLVRNGRIEAVGEQAQAAES---AATLDAAGQVIAPGFIDLCCNLREPGNGQKGNIASETRA 90
Cdd:PRK09059 7 LANARIIDPSRGLDEIGTVLIEDGVIVAAGKGAGNQGApegAEIVDCAGKAVAPGLVDARVFVGEPGAEHRETIASASRA 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486032191 91 AAHGGFTTVCASPETSPVNDSGAVTNLILDSVASRGVVRVLPIGAITRGLDGDMLSDMAGLKAAGCVAVGNGSRGVRNAR 170
Cdd:PRK09059 87 AAAGGVTSIIMMPDTDPVIDDVALVEFVKRTARDTAIVNIHPAAAITKGLAGEEMTEFGLLRAAGAVAFTDGRRSVANTQ 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486032191 171 ILRRCMAYAQTFGLTVMFSPENTALAADGYAHDGQVTTRLGLLGIPEVAETAAVMEMLLLAEETGVRLHLSQLSCARSVE 250
Cdd:PRK09059 167 VMRRALTYARDFDAVIVHETRDPDLGGNGVMNEGLFASWLGLSGIPREAEVIPLERDLRLAALTRGRYHAAQISCAESAE 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486032191 251 MLAQARDRGVKVTADVAMHQLAFTESALAGFDSRFHVRPPLRGEADRQALVAGVRDGVIDAIVSQHQPHDSAAKQAPLPA 330
Cdd:PRK09059 247 ALRRAKDRGLKVTAGVSINHLSLNENDIGEYRTFFKLSPPLRTEDDRVAMVEAVASGTIDIIVSSHDPQDVDTKRLPFSE 326
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486032191 331 TEPGLSSIESVLSLGLELVQNHELELPDLLRALTAGPAAVLGREVA-LTAGAAADLCLFAPDGHWQPSAATLLSAGRHAP 409
Cdd:PRK09059 327 AAAGAIGLETLLAAALRLYHNGEVPLLRLIEALSTRPAEIFGLPAGtLKPGAPADIIVIDLDEPWVVDPEDLKSRSKNTP 406
|
410
....*....|....*....
gi 2486032191 410 VLERALPGEVKLTLVAGRT 428
Cdd:PRK09059 407 FEEARFQGRVVRTIVAGKT 425
|
|
| pyrC_multi |
TIGR00857 |
dihydroorotase, multifunctional complex type; In contrast to the homodimeric type of ... |
25-429 |
1.18e-89 |
|
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: 278.17 E-value: 1.18e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486032191 25 GLISNPGLLVRNGRIEAVGEQAQAAESAAtLDAAGQVIAPGFIDLCCNLREPGNGQKGNIASETRAAAHGGFTTVCASPE 104
Cdd:TIGR00857 1 GKETEVDILVEGGRIKKIGKLRIPPDAEV-IDAKGLLVLPGFIDLHVHLRDPGEEYKEDIESGSKAAAHGGFTTVADMPN 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486032191 105 TSPVNDSGAVTNLILDSVASRGVVRVLPIGAITRGLDGDMLSDMAGLKAAGCVA---VGNGSRgVRNARILRRCMAYAQT 181
Cdd:TIGR00857 80 TKPPIDTPETLEWKLQRLKKVSLVDVHLYGGVTQGNQGKELTEAYELKEAGAVGrmfTDDGSE-VQDILSMRRALEYAAI 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486032191 182 FGLTVMFSPENTALAADGYAHDGQVTTRLGLLGIPEVAETAAVMEMLLLAEETGVRLHLSQLSCARSVEMLAQARDRGVK 261
Cdd:TIGR00857 159 AGVPIALHAEDPDLIYGGVMHEGPSAAQLGLPARPPEAEEVAVARLLELAKHAGCPVHICHISTKESLELIVKAKSQGIK 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486032191 262 VTADVAMHQLAFTESALAGFDSRFHVRPPLRGEADRQALVAGVRDGVIDAIVSQHQPHDSAAKQAPLPATEPGLSSIESV 341
Cdd:TIGR00857 239 ITAEVTPHHLLLSEEDVARLDGNGKVNPPLREKEDRLALIEGLKDGIIDIIATDHAPHTLEEKTKEFAAAPPGIPGLETA 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486032191 342 LSLGLELVQNHELELPDLLRALTAGPAAVLG-REV-ALTAGAAADLCLFAPDGHWQPSAATLLSAGRHAPVLERALPGEV 419
Cdd:TIGR00857 319 LPLLLQLLVKGLISLKDLIRMLSINPARIFGlPDKgTLEEGNPADITVFDLKKEWTINAETFYSKAKNTPFEGMSLKGKP 398
|
410
....*....|
gi 2486032191 420 KLTLVAGRTA 429
Cdd:TIGR00857 399 IATILRGKVV 408
|
|
| PRK07369 |
PRK07369 |
dihydroorotase; Provisional |
33-419 |
6.69e-78 |
|
dihydroorotase; Provisional
Pssm-ID: 236002 [Multi-domain] Cd Length: 418 Bit Score: 247.98 E-value: 6.69e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486032191 33 LVRNGRIEAVGEQAQAAESAAT-LDAAGQVIAPGFIDLCCNLREPGNGQKGNIASETRAAAHGGFTTVCASPETSPVNDS 111
Cdd:PRK07369 25 LIEDGKIQAIEPHIDPIPPDTQiIDASGLILGPGLVDLYSHSGEPGFEERETLASLAAAAAAGGFTRVAILPDTFPPLDN 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486032191 112 GAVTNLILDSVASRGVVRVLPIGAITRGLDGDMLSDMAGLKAAGCVAVGNGsRGVRNARILRRCMAYAQTFGLTVMFSPE 191
Cdd:PRK07369 105 PATLARLQQQAQQIPPVQLHFWGALTLGGQGKQLTELAELAAAGVVGFTDG-QPLENLALLRRLLEYLKPLGKPVALWPC 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486032191 192 NTALAADGYAHDGQVTTRLGLLGIPEVAETAAVMEMLLLAEETGVRLHLSQLSCARSVEMLAQARDRGVKVTADVAMHQL 271
Cdd:PRK07369 184 DRSLAGNGVMREGLLALRLGLPGDPASAETTALAALLELVAAIGTPVHLMRISTARSVELIAQAKARGLPITASTTWMHL 263
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486032191 272 AFTESALAGFDSRFHVRPPLRGEADRQALVAGVRDGVIDAIVSQHQPHDSAAKQAPLPATEPGLSSIESVLS-LGLELVQ 350
Cdd:PRK07369 264 LLDTEALASYDPNLRLDPPLGNPSDRQALIEGVRTGVIDAIAIDHAPYTYEEKTVAFAEAPPGAIGLELALPlLWQNLVE 343
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486032191 351 NHELELPDLLRALTAGPAAVLGREV-ALTAGAAADLCLFAPDGHWQPSAATLLSAGRHAPVLERALPGEV 419
Cdd:PRK07369 344 TGELSALQLWQALSTNPARCLGQEPpSLAPGQPAELILFDPQKTWTVSAQTLHSLSRNTPWLGQTLKGRV 413
|
|
| PRK08417 |
PRK08417 |
metal-dependent hydrolase; |
32-428 |
1.90e-51 |
|
metal-dependent hydrolase;
Pssm-ID: 236262 [Multi-domain] Cd Length: 386 Bit Score: 177.97 E-value: 1.90e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486032191 32 LLVRNGRIEAVGEQAQAAEsaaTLDAAGQVIAPGFIDLCCNLREPGNGQKgNIASETRAAAHGGFTTVCASPETSPVNDS 111
Cdd:PRK08417 1 IRIKDGKITEIGSDLKGEE---ILDAKGKTLLPALVDLNVSLKNDSLSSK-NLKSLENECLKGGVGSIVLYPDSTPAIDN 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486032191 112 GAVTNLIlDSVASRGVVRVLPIGAITRglDGDMLSDMAGLKAAGCVAVGNGSrgVRNARILRRCMAYAQTFGLTVMFSPE 191
Cdd:PRK08417 77 EIALELI-NSAQRELPMQIFPSIRALD--EDGKLSNIATLLKKGAKALELSS--DLDANLLKVIAQYAKMLDVPIFCRCE 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486032191 192 NTALAADGYAHDGQVTTRLGLLGIPEVAETAAVMEMLLLAEETGVRLHLSQLSCARSVEMLAQARDRGVKVTADVAMHQL 271
Cdd:PRK08417 152 DSSFDDSGVMNDGELSFELGLPGIPSIAETKEVAKMKELAKFYKNKVLFDTLALPRSLELLDKFKSEGEKLLKEVSIHHL 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486032191 272 AFTESALAGFDSRFHVRPPLRGEADRQALVAGVRDGVIDAIVSQHQPHDSAAKQAPLPATEPGLSSIESVLSLGLE-LVQ 350
Cdd:PRK08417 232 ILDDSACENFNTAAKLNPPLRSKEDRLALLEALKEGKIDFLTSLHSAKSNSKKDLAFDEAAFGIDSICEYFSLCYTyLVK 311
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2486032191 351 NHELELPDLLRALTAGPAAVLGREV-ALTAGAAADLCLFAPDghwqpsaATLLSAGRHAPVLERALPGEVKLTLVAGRT 428
Cdd:PRK08417 312 EGIITWSELSRFTSYNPAQFLGLNSgEIEVGKEADLVLFDPN-------ESTIIDDNFSLYSGDELYGKIEAVIIKGKL 383
|
|
| DHOase_IIb |
cd01318 |
Dihydroorotase (DHOase), subgroup IIb; DHOases catalyze the reversible interconversion of ... |
59-426 |
3.96e-50 |
|
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: 173.67 E-value: 3.96e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486032191 59 GQVIAPGFIDLCCNLREPGNGQKGNIASETRAAAHGGFTTVCASPETSPVNDSGAVTNLILDSVASRGVVRVLPIGAITR 138
Cdd:cd01318 1 GLLILPGVIDIHVHFREPGLTYKEDFVSGSRAAAAGGVTTVMDMPNTKPPTTTAEALYEKLRLAAAKSVVDYGLYFGVTG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486032191 139 GLDGDMLSdmAGLKAAGCVAVGN--GSRGVRNARILRrcmAYAQTFGLTVmFSPENTAL---AADGYAHDGQVTTRLgll 213
Cdd:cd01318 81 SEDLEELD--KAPPAGYKIFMGDstGDLLDDEETLER---IFAEGSVLVT-FHAEDEDRlreNRKELKGESAHPRIR--- 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486032191 214 giPEVAETAAVMEMLLLAEETGVRLHLSQLSCARSVEMLAQARDRgvkVTADVAMHQLAFTESALAGFDSRFHVRPPLRG 293
Cdd:cd01318 152 --DAEAAAVATARALKLARRHGARLHICHVSTPEELKLIKKAKPG---VTVEVTPHHLFLDVEDYDRLGTLGKVNPPLRS 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486032191 294 EADRQALVAGVRDGVIDAIVSQHQPHDSAAKQAPLPATEPGLSSIESVLSLGLELVQNHELELPDLLRALTAGPAAVLGR 373
Cdd:cd01318 227 REDRKALLQALADGRIDVIASDHAPHTLEEKRKGYPAAPSGIPGVETALPLMLTLVNKGILSLSRVVRLTSHNPARIFGI 306
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*
gi 2486032191 374 EV--ALTAGAAADLCLFAPDGHWQPSAATLLSAGRHAPVLERALPGEVKLTLVAG 426
Cdd:cd01318 307 KNkgRIAEGYDADLTVVDLKEERTIRAEEFHSKAGWTPFEGFEVTGFPVMTIVRG 361
|
|
| L-HYD_ALN |
cd01315 |
L-Hydantoinases (L-HYDs) and Allantoinase (ALN); L-Hydantoinases are a member of the ... |
31-437 |
7.14e-49 |
|
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: 172.47 E-value: 7.14e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486032191 31 GLLVRNGRIEAVGEQAQAAESAATLDAAGQVIAPGFIDLCCNLREPGNGQKGNIASETRAAAHGGFTTVCASPETS-PVN 109
Cdd:cd01315 19 DIAVKGGKIAAIGPDIANTEAEEVIDAGGLVVMPGLIDTHVHINEPGRTEWEGFETGTKAAAAGGITTIIDMPLNSiPPT 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486032191 110 DSGAVTNLILDSVASRGVVRVLPIGaitrGLDGDMLSDMAGLKAAGCVA-------VGNGSRGVRNARILRRCMAYAQTF 182
Cdd:cd01315 99 TTVENLEAKLEAAQGKLHVDVGFWG----GLVPGNLDQLRPLDEAGVVGfkcflcpSGVDEFPAVDDEQLEEAMKELAKT 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486032191 183 GLTVMFSPEN----TALAADGYAhDGQVTTRLGLLGIPEVAETAAVMEMLLLAEETGVRLHLSQLSCARSVEMLAQARDR 258
Cdd:cd01315 175 GSVLAVHAENpeitEALQEQAKA-KGKRDYRDYLASRPVFTEVEAIQRILLLAKETGCRLHIVHLSSAEAVPLIREARAE 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486032191 259 GVKVTADVAMHQLAFTESALAGFDSRFHVRPPLRGEADRQALVAGVRDGVIDAIVSQHQPHDSAAKqapLPATE------ 332
Cdd:cd01315 254 GVDVTVETCPHYLTFTAEDVPDGGTEFKCAPPIRDAANQEQLWEALENGDIDMVVSDHSPCTPELK---LLGKGdffkaw 330
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486032191 333 PGLSSIESVLSLGLEL-VQNHELELPDLLRALTAGPAAVLG---REVALTAGAAADLCLFAPDGHWQPSAATLLSAGRHA 408
Cdd:cd01315 331 GGISGLQLGLPVMLTEaVNKRGLSLEDIARLMCENPAKLFGlshQKGRIAVGYDADFVVWDPEEEFTVDAEDLYYKNKIS 410
|
410 420 430
....*....|....*....|....*....|..
gi 2486032191 409 PVLERALPGEVKLTLVAGRTAWQ---APGTPL 437
Cdd:cd01315 411 PYVGRTLKGRVHATILRGTVVYQdgeVVGEPL 442
|
|
| Cyclic_amidohydrolases |
cd01302 |
Cyclic amidohydrolases, including hydantoinase, dihydropyrimidinase, allantoinase, and ... |
61-422 |
1.27e-45 |
|
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: 161.02 E-value: 1.27e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486032191 61 VIAPGFIDLCCNLREPGNGQ-KGNIASETRAAAHGGFTTVCASPETSP-----VNDSGAVTNLI----LDSVASRGVVRV 130
Cdd:cd01302 2 LVLPGFIDIHVHLRDPGGTTyKEDFESGSRAAAAGGVTTVIDMPNTGPppidlPAIELKIKLAEessyVDFSFHAGIGPG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486032191 131 LPIGAITRGLDgdmlSDMAGLKAAGCVAVGnGSRGVRNARILRRCMAYAqTFGLTVMFspentalaadgyaHdgqvttrl 210
Cdd:cd01302 82 DVTDELKKLFD----AGINSLKVFMNYYFG-ELFDVDDGTLMRTFLEIA-SRGGPVMV-------------H-------- 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486032191 211 gllgipevAETAAvmemlLLAEETGVRLHLSQLSCARSVEMLAQARDRGVKVTADVAMHQLAFTESALAGFDSRFHVRPP 290
Cdd:cd01302 135 --------AERAA-----QLAEEAGANVHIAHVSSGEALELIKFAKNKGVKVTCEVCPHHLFLDESMLRLNGAWGKVNPP 201
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486032191 291 LRGEADRQALVAGVRDGVIDAIVSQHQPHDSAAKQ--APLPATEPGLSSIESVLSLGLELVQNHELELPDLLRALTAGPA 368
Cdd:cd01302 202 LRSKEDREALWEGVKNGKIDTIASDHAPHSKEEKEsgKDIWKAPPGFPGLETRLPILLTEGVKRGLSLETLVEILSENPA 281
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*.
gi 2486032191 369 AVLGREVALT--AGAAADLCLFAPDGHWQPSAATLLSAGRHAPVLERALPGEVKLT 422
Cdd:cd01302 282 RIFGLYPKGTiaVGYDADLVIVDPKKEWKVTAEEIESKADWTPFEGMEVTGKPVST 337
|
|
| PRK02382 |
PRK02382 |
dihydroorotase; Provisional |
33-430 |
1.31e-38 |
|
dihydroorotase; Provisional
Pssm-ID: 179417 [Multi-domain] Cd Length: 443 Bit Score: 144.79 E-value: 1.31e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486032191 33 LVRNGRIEAVGEQAQAAESAATLDAAGQVIAPGFIDLCCNLREPGNGQKGNIASETRAAAHGGFTTVCASPETSPVNDSG 112
Cdd:PRK02382 23 RIDGGKITAVGKDLDGSSSEEVIDARGMLLLPGGIDVHVHFREPGYTHKETWYTGSRSAAAGGVTTVVDQPNTDPPTVDG 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486032191 113 AVTNLILDSVASRGVVRVLPIGAITRGLD-GDMLSDMaGLKAAGCV--AVGNGSRGVrNARILRRCMAYAQTFGLTVMFS 189
Cdd:PRK02382 103 ESFDEKAELAARKSIVDFGINGGVTGNWDpLESLWER-GVFALGEIfmADSTGGMGI-DEELFEEALAEAARLGVLATVH 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486032191 190 PENTAL---AADGYAHDG--QVTTRLGllgiPEVAETAAVMEMLLLAEETGVRLHLSQLSCARSVEMLaqardRGVKVTA 264
Cdd:PRK02382 181 AEDEDLfdeLAKLLKGDAdaDAWSAYR----PAAAEAAAVERALEVASETGARIHIAHISTPEGVDAA-----RREGITC 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486032191 265 DVAMHQLAFTESALAGFDSRFHVRPPLRGEADRQALVAGVRDGVIDAIVSQHQPHDSAAKQAPLPATEPGLSSIESVLSL 344
Cdd:PRK02382 252 EVTPHHLFLSRRDWERLGTFGKMNPPLRSEKRREALWERLNDGTIDVVASDHAPHTREEKDADIWDAPSGVPGVETMLPL 331
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486032191 345 GLELVQNHELELPDLLRALTAGPAAVLG--REVALTAGAAADLCLFAPDGHWQPSAATLLSAGRHAPV--LERALPgevK 420
Cdd:PRK02382 332 LLAAVRKNRLPLERVRDVTAANPARIFGldGKGRIAEGYDADLVLVDPDAAREIRGDDLHSKAGWTPFegMEGVFP---E 408
|
410
....*....|
gi 2486032191 421 LTLVAGRTAW 430
Cdd:PRK02382 409 LTMVRGTVVW 418
|
|
| PRK06189 |
PRK06189 |
allantoinase; Provisional |
34-431 |
3.43e-36 |
|
allantoinase; Provisional
Pssm-ID: 235732 [Multi-domain] Cd Length: 451 Bit Score: 138.30 E-value: 3.43e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486032191 34 VRNGRIEAVGEQAQAAESAaTLDAAGQVIAPGFIDLCCNLREPGNGQKGNIASETRAAAHGGFTTVCASPETS--PVnds 111
Cdd:PRK06189 25 IKNGKIAEIAPEISSPARE-IIDADGLYVFPGMIDVHVHFNEPGRTHWEGFATGSAALAAGGCTTYFDMPLNSipPT--- 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486032191 112 gaVTNLILDSVASRGVVRVLPIGAITRGLDGDMLSDMAGLKAAGcvAVG-------NGSRGVRNA--RILRRCMAYAQTF 182
Cdd:PRK06189 101 --VTREALDAKAELARQKSAVDFALWGGLVPGNLEHLRELAEAG--VIGfkafmsnSGTDEFRSSddLTLYEGMKEIAAL 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486032191 183 GLTVMFSPENTALA---ADGYAHDGQVTTRLGLLGIPEVAETAAVMEMLLLAEETGVRLHLSQLSCARSVEMLAQARDRG 259
Cdd:PRK06189 177 GKILALHAESDALTrhlTTQARQQGKTDVRDYLESRPVVAELEAVQRALLYAQETGCPLHFVHISSGKAVALIAEAKKRG 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486032191 260 VKVTADVAMHQLAFTESALAGFDSRFHVRPPLRGEADRQALVAGVRDGVIDAIVSQHQP-HDSAAKQAPLPATEPGLSSI 338
Cdd:PRK06189 257 VDVSVETCPHYLLFTEEDFERIGAVAKCAPPLRSRSQKEELWRGLLAGEIDMISSDHSPcPPELKEGDDFFLVWGGISGG 336
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486032191 339 ESVLSLGLEL-VQNHELELPDLLRALTAGPAAVLG--REVALTAGAAADLCLFAPDGHWQPSAATLLSAGRHAPVLERAL 415
Cdd:PRK06189 337 QSTLLVMLTEgYIERGIPLETIARLLATNPAKRFGlpQKGRLEVGADADFVLVDLDETYTLTKEDLFYRHKQSPYEGRTF 416
|
410
....*....|....*.
gi 2486032191 416 PGEVKLTLVAGRTAWQ 431
Cdd:PRK06189 417 PGRVVATYLRGQCVYQ 432
|
|
| PRK07575 |
PRK07575 |
dihydroorotase; Provisional |
32-431 |
5.14e-31 |
|
dihydroorotase; Provisional
Pssm-ID: 236055 [Multi-domain] Cd Length: 438 Bit Score: 123.63 E-value: 5.14e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486032191 32 LLVRNGRIEAVGEQAQAAESAATLDAAGQVIAPGFIDLCCNLREPGNGQKGNIASETRAAAHGGFTTVCASPETSPVNDS 111
Cdd:PRK07575 24 VLVEDGKIVAIAPEISATAVDTVIDAEGLTLLPGVIDPQVHFREPGLEHKEDLFTASRACAKGGVTSFLEMPNTKPLTTT 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486032191 112 GAVTNLILDSVASRGVVRV-LPIGAItrgldGDMLSDmagLKAAgcvavgNGSRGVRnarILRRCMAYA----QTFGLTV 186
Cdd:PRK07575 104 QAALDDKLARAAEKCVVNYgFFIGAT-----PDNLPE---LLTA------NPTCGIK---IFMGSSHGPllvdEEAALER 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486032191 187 MFSPENTALAAdgYAHD-GQVTTRLGLL-GIPEVA-------ETAAVMEM---LLLAEETGVRLHLSQLSCARSVEMLAQ 254
Cdd:PRK07575 167 IFAEGTRLIAV--HAEDqARIRARRAEFaGISDPAdhsqiqdEEAALLATrlaLKLSKKYQRRLHILHLSTAIEAELLRQ 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486032191 255 arDRGVKVTADVAMHQLAFTESALAGFDSRFHVRPPLRGEADRQALVAGVRDGVIDAIVSQHQPHDSAAKQAPLPATEPG 334
Cdd:PRK07575 245 --DKPSWVTAEVTPQHLLLNTDAYERIGTLAQMNPPLRSPEDNEALWQALRDGVIDFIATDHAPHTLEEKAQPYPNSPSG 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486032191 335 LSSIESVLSLGLELVQNHELELPDLLRALTAGPAAVLG--REVALTAGAAADLCLFAPDgHWQP-SAATLLSAGRHAPVL 411
Cdd:PRK07575 323 MPGVETSLPLMLTAAMRGKCTVAQVVRWMSTAVARAYGipNKGRIAPGYDADLVLVDLN-TYRPvRREELLTKCGWSPFE 401
|
410 420
....*....|....*....|
gi 2486032191 412 ERALPGEVKLTLVAGRTAWQ 431
Cdd:PRK07575 402 GWNLTGWPVTTIVGGQIVFD 421
|
|
| PRK09236 |
PRK09236 |
dihydroorotase; Reviewed |
32-431 |
8.70e-30 |
|
dihydroorotase; Reviewed
Pssm-ID: 181716 Cd Length: 444 Bit Score: 120.36 E-value: 8.70e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486032191 32 LLVRNGRIEAVGEQAQAAESAATLDAAGQVIAPGFIDLCCNLREPGNGQKGNIASETRAAAHGGFTTVCASPETSP---- 107
Cdd:PRK09236 22 VLIENGRIAKIASSISAKSADTVIDAAGRYLLPGMIDDQVHFREPGLTHKGDIASESRAAVAGGITSFMEMPNTNPpttt 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486032191 108 ----------------VNDS---GAvTNLILDSVASRGVVRVLPI----GAITrgldGDMLSDmaglkaagcvavgngsr 164
Cdd:PRK09236 102 lealeakyqiaaqrslANYSfyfGA-TNDNLDEIKRLDPKRVCGVkvfmGAST----GNMLVD----------------- 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486032191 165 gvrNARILRRCMAYAQTFGLTVMFSP----ENTALAADGYAHDgqvttrlgllgIPEVA------ETA-------AVMem 227
Cdd:PRK09236 160 ---NPETLERIFRDAPTLIATHCEDTptikANLAKYKEKYGDD-----------IPAEMhplirsAEAcykssslAVS-- 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486032191 228 llLAEETGVRLHLSQLSCARSVEMLAQARDRGVKVTADVAMHQLAFTESALAGFDSRFHVRPPLRGEADRQALVAGVRDG 307
Cdd:PRK09236 224 --LAKKHGTRLHVLHISTAKELSLFENGPLAEKRITAEVCVHHLWFDDSDYARLGNLIKCNPAIKTASDREALRQALADD 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486032191 308 VIDAIVSQHQPHDSAAKQAPLPATEPGLSSIESVLSLGLELVQNHELELPDLLRALTAGPAAVLG-------REvaltaG 380
Cdd:PRK09236 302 RIDVIATDHAPHTWEEKQGPYFQAPSGLPLVQHALPALLELVHEGKLSLEKVVEKTSHAPAILFDikergfiRE-----G 376
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|.
gi 2486032191 381 AAADLCLFAPDGHWQPSAATLLSAGRHAPVLERALPGEVKLTLVAGRTAWQ 431
Cdd:PRK09236 377 YWADLVLVDLNSPWTVTKENILYKCGWSPFEGRTFRSRVATTFVNGQLVYH 427
|
|
| PRK08044 |
PRK08044 |
allantoinase AllB; |
34-428 |
1.36e-26 |
|
allantoinase AllB;
Pssm-ID: 169193 [Multi-domain] Cd Length: 449 Bit Score: 111.10 E-value: 1.36e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486032191 34 VRNGRIEAVGEQAQAAESaaTLDAAGQVIAPGFIDLCCNLREPGNGQKGNIASETRAAAHGGFTTVCASPETS-PVNDSG 112
Cdd:PRK08044 25 VKGGKIAAIGQDLGDAKE--VMDASGLVVSPGMVDAHTHISEPGRSHWEGYETGTRAAAKGGITTMIEMPLNQlPATVDR 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486032191 113 AVTNLILDSVASRGVVRVLPIGA-ITRGLDGDMLSDMAGLKAAGCVAVGNGSRGVRNARI------LRRCMAYAQTFGLT 185
Cdd:PRK08044 103 ASIELKFDAAKGKLTIDAAQLGGlVSYNLDRLHELDEVGVVGFKCFVATCGDRGIDNDFRdvndwqFYKGAQKLGELGQP 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486032191 186 VMFSPENTA----LAADGYaHDGQVTTRLGLLGIPEVAETAAVMEMLLLAEETGVRLHLSQLSCARSVEMLAQARDRGVK 261
Cdd:PRK08044 183 VLVHCENALicdeLGEEAK-REGRVTAHDYVASRPVFTEVEAIRRVLYLAKVAGCRLHVCHISSPEGVEEVTRARQEGQD 261
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486032191 262 VTADVAMHQLAFTESALAGFDSRFHVRPPLRGEADRQALVAGVRDGVIDAIVSQHQPHDSAAKQAPLPATEPGLSSIESV 341
Cdd:PRK08044 262 VTCESCPHYFVLDTDQFEEIGTLAKCSPPIRDLENQKGMWEKLFNGEIDCLVSDHSPCPPEMKAGNIMEAWGGIAGLQNC 341
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486032191 342 LSLGL-ELVQNHELELPDLLRALTAGPAAVLG--REVALTAGAAADLCLFAPDGHWQPSAATLLSAGRHAPVLERALPGE 418
Cdd:PRK08044 342 MDVMFdEAVQKRGMSLPMFGKLMATNAADIFGlqQKGRIAPGKDADFVFIQPNSSYVLKNEDLEYRHKVSPYVGRTIGAR 421
|
410
....*....|
gi 2486032191 419 VKLTLVAGRT 428
Cdd:PRK08044 422 ITKTILRGDV 431
|
|
| PRK09060 |
PRK09060 |
dihydroorotase; Validated |
34-385 |
4.84e-26 |
|
dihydroorotase; Validated
Pssm-ID: 181632 [Multi-domain] Cd Length: 444 Bit Score: 109.62 E-value: 4.84e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486032191 34 VRNGRIEAVGEQAQAAESAaTLDAAGQVIAPGFIDLCCNLREPGNGQKGNIASETRAAAHGGFTTVCASPETSPVNDSGA 113
Cdd:PRK09060 27 IRDGRIAAIGDLSGASAGE-VIDCRGLHVLPGVIDSQVHFREPGLEHKEDLETGSRAAVLGGVTAVFEMPNTNPLTTTAE 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486032191 114 VtnlILDSVAsRGVVRV-----LPIGAiTRgldgDMLSDMAGL-KAAGC--VAVGNGSR----------GVRN--ARILR 173
Cdd:PRK09060 106 A---LADKLA-RARHRMhcdfaFYVGG-TR----DNADELAELeRLPGCagIKVFMGSStgdllveddeGLRRilRNGRR 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486032191 174 RcmayaqtfgltVMFSPENTALAAD--GYAHDGQVTTRlgllgiPEV-AETAAVM---EMLLLAEETGVRLHLSQLSCAR 247
Cdd:PRK09060 177 R-----------AAFHSEDEYRLRErkGLRVEGDPSSH------PVWrDEEAALLatrRLVRLARETGRRIHVLHVSTAE 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486032191 248 SVEMLAQARDRgvkVTADVAMHQLAFT-ESALAGFDSRFHVRPPLRGEADRQALVAGVRDGVIDAIVSQHQPHDSAAKQA 326
Cdd:PRK09060 240 EIDFLADHKDV---ATVEVTPHHLTLAaPECYERLGTLAQMNPPIRDARHRDGLWRGVRQGVVDVLGSDHAPHTLEEKAK 316
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2486032191 327 PLPATEPGLSSIESVLSLGLELVQNHELELPDLLRALTAGPAAVLG--REVALTAGAAADL 385
Cdd:PRK09060 317 PYPASPSGMTGVQTLVPIMLDHVNAGRLSLERFVDLTSAGPARIFGiaGKGRIAVGYDADF 377
|
|
| PLN02795 |
PLN02795 |
allantoinase |
55-437 |
6.65e-25 |
|
allantoinase
Pssm-ID: 178392 [Multi-domain] Cd Length: 505 Bit Score: 106.78 E-value: 6.65e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486032191 55 LDAAGQVIAPGFIDLCCNLREPGNGQKGNIASETRAAAHGGFTTVCASPETS-PVNDSGAVTNLILDSVASRGVVRV--- 130
Cdd:PLN02795 90 LDYGNAVVMPGLIDVHVHLNEPGRTEWEGFPTGTKAAAAGGITTLVDMPLNSfPSTTSVETLELKIEAAKGKLYVDVgfw 169
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486032191 131 ---LPIGAITRGLDGDMLSDMA-GLKAAGCVAVGNGSRGVrNARILRRCMAYAQTFGLTVMFSPE-------NTALAADG 199
Cdd:PLN02795 170 gglVPENAHNASVLEELLDAGAlGLKSFMCPSGINDFPMT-TATHIKAALPVLAKYGRPLLVHAEvvspvesDSRLDADP 248
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486032191 200 YAHDGQVTTRlgllgiPEVAETAAVMEMLLLAEET-------GVRLHLSQLS-CARSVEMLAQARDRGVKVTADVAMHQL 271
Cdd:PLN02795 249 RSYSTYLKSR------PPSWEQEAIRQLLEVAKDTrpggvaeGAHVHIVHLSdAESSLELIKEAKAKGDSVTVETCPHYL 322
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486032191 272 AFTESALAGFDSRFHVRPPLRGEADRQALVAGVRDGVIDAIVSQHQPHDSAAKqapLPATEP------GLSSIESVLSLG 345
Cdd:PLN02795 323 AFSAEEIPDGDTRYKCAPPIRDAANRELLWKALLDGDIDMLSSDHSPSPPDLK---LLEEGNflrawgGISSLQFVLPAT 399
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486032191 346 LELVQNHELELPDLLRALTAGPAAV--LGREVALTAGAAADLCLFAPDGHWQPSAATLLSAGRH--APVLERALPGEVKL 421
Cdd:PLN02795 400 WTAGRAYGLTLEQLARWWSERPAKLagLDSKGAIAPGKDADIVVWDPEAEFVLDESYPIYHKHKslSPYLGTKLSGKVIA 479
|
410 420
....*....|....*....|...
gi 2486032191 422 TLVAGRT-------AWQAPGTPL 437
Cdd:PLN02795 480 TFVRGNLvflegkhAKQACGSPI 502
|
|
| PRK04250 |
PRK04250 |
dihydroorotase; Provisional |
24-427 |
1.61e-22 |
|
dihydroorotase; Provisional
Pssm-ID: 235265 [Multi-domain] Cd Length: 398 Bit Score: 98.69 E-value: 1.61e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486032191 24 KGLISNPGLLVRNGRIEAVGEQAQAAESaaTLDAAGQVIAPGFIDLCCNLREPGNGQKGNIASETRAAAHGGFTTVCASP 103
Cdd:PRK04250 9 KGRIVEGGIGIENGRISKISLRDLKGKE--VIKVKGGIILPGLIDVHVHLRDFEESYKETIESGTKAALHGGITLVFDMP 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486032191 104 ETSP-VNDSGavTNLILDSVASRGVVRVLPIGAITRGLDGDMLSDMAGLKAAGCVAVGNGsrgvrnarilrrcmAYAQTF 182
Cdd:PRK04250 87 NTKPpIMDEK--TYEKRMRIAEKKSYADYALNFLIAGNCEKAEEIKADFYKIFMGASTGG--------------IFSENF 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486032191 183 GLTVMFSPENTALAADGYAHDGQVTTRlgllgiPEVAETAAVMEMLLLAEETGVRLHLSQLSCARSVEMLAQARDRGVkv 262
Cdd:PRK04250 151 EVDYACAPGIVSVHAEDPELIREFPER------PPEAEVVAIERALEAGKKLKKPLHICHISTKDGLKLILKSNLPWV-- 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486032191 263 TADVAMHQLAFTESalagfDSR----FHVRPPLRGEADRQALVAGVRDgvIDAIVSQHQPHDSAAKQaplpATEPGLSSI 338
Cdd:PRK04250 223 SFEVTPHHLFLTRK-----DYErnplLKVYPPLRSEEDRKALWENFSK--IPIIASDHAPHTLEDKE----AGAAGIPGL 291
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486032191 339 ESVLSLGLELVQNHELELPDLLRALTAGPAAVLG-REVALTAGAAADLCLFAPDGHWQPSAATLLSAGRHAPVLERALPG 417
Cdd:PRK04250 292 ETEVPLLLDAANKGMISLFDIVEKMHDNPARIFGiKNYGIEEGNYANFAVFDMKKEWTIKAEELYTKAGWTPYEGFKLKG 371
|
410
....*....|
gi 2486032191 418 EVKLTLVAGR 427
Cdd:PRK04250 372 KVIMTILRGE 381
|
|
| D-HYD |
cd01314 |
D-hydantoinases (D-HYD) also called dihydropyrimidases (DHPase) and related proteins; DHPases ... |
32-430 |
3.46e-22 |
|
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: 98.44 E-value: 3.46e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486032191 32 LLVRNGRIEAVGEQAQAAESAATLDAAGQVIAPGFIDLCCNLREP--GNGQKGNIASETRAAAHGGFTTV----CASPET 105
Cdd:cd01314 19 ILIEDGKIVAIGPNLEAPGGVEVIDATGKYVLPGGIDPHTHLELPfmGTVTADDFESGTRAAAAGGTTTIidfaIPNKGQ 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486032191 106 SpvndsgavtnlILDSV------ASRGVVrvlpI-----GAITRgLDGDMLSDMAGLKAAGCVAVG-----NGSRGVRNA 169
Cdd:cd01314 99 S-----------LLEAVekwrgkADGKSV----IdygfhMIITD-WTDSVIEELPELVKKGISSFKvfmayKGLLMVDDE 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486032191 170 RILRrCMAYAQTFGLTVMFSPENTALAADGyahdgqvTTRLGLLGI----------PEVAETAAVMEMLLLAEETGVRLH 239
Cdd:cd01314 163 ELLD-VLKRAKELGALVMVHAENGDVIAEL-------QKKLLAQGKtgpeyhalsrPPEVEAEATARAIRLAELAGAPLY 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486032191 240 LSQLSCARSVEMLAQARDRGVKVTADVAMHQLAFTESALA--GFD-SRFHVRPPLRGEADRQALVAGVRDGVIDAIVSQH 316
Cdd:cd01314 235 IVHVSSKEAADEIARARKKGLPVYGETCPQYLLLDDSDYWkdWFEgAKYVCSPPLRPKEDQEALWDGLSSGTLQTVGSDH 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486032191 317 QPHDSAAKQAPLPA-TE-P-GLSSIESVLSLGL-ELVQNHELELPDLLRALTAGPAAVLG---REVALTAGAAADLCLFA 389
Cdd:cd01314 315 CPFNFAQKARGKDDfTKiPnGVPGVETRMPLLWsEGVAKGRITLEKFVELTSTNPAKIFGlypRKGTIAVGSDADLVIWD 394
|
410 420 430 440
....*....|....*....|....*....|....*....|.
gi 2486032191 390 PDGHWQPSAATLLSAGRHAPVLERALPGEVKLTLVAGRTAW 430
Cdd:cd01314 395 PNAEKTISADTHHHNVDYNIFEGMKVKGWPVVTISRGKVVV 435
|
|
| PRK08323 |
PRK08323 |
phenylhydantoinase; Validated |
32-430 |
4.89e-19 |
|
phenylhydantoinase; Validated
Pssm-ID: 236240 [Multi-domain] Cd Length: 459 Bit Score: 89.08 E-value: 4.89e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486032191 32 LLVRNGRIEAVGEQAQAAesaaTLDAAGQVIAPGFIDLCCNLREPGNG--QKGNIASETRAAAHGGFTTV---CASPETS 106
Cdd:PRK08323 21 VLIEDGKIAAIGANLGDE----VIDATGKYVMPGGIDPHTHMEMPFGGtvSSDDFETGTRAAACGGTTTIidfALQPKGQ 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486032191 107 PVNDSGAVTNlilDSVASRGVVRVLPIGAITrGLDGDMLSDMAGLKAAGCVAVG-----NGSRGVRNARILRrCMAYAQT 181
Cdd:PRK08323 97 SLREALEAWH---GKAAGKAVIDYGFHMIIT-DWNEVVLDEMPELVEEGITSFKlfmayKGALMLDDDELLR-ALQRAAE 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486032191 182 FGLTVMFSPEN--------TALAADG----YAHdgqVTTRlgllgiPEVAETAAVMEMLLLAEETGVRLHLSQLSCARSV 249
Cdd:PRK08323 172 LGALPMVHAENgdaiaylqAKLLAEGktgpEYH---ALSR------PPEVEGEATNRAIMLAELAGAPLYIVHVSCKEAL 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486032191 250 EMLAQARDRGVKVTADVAMHQLAFTESALAGFDS----RFHVRPPLRGEADRQALVAGVRDGVIDAIVSQHQPHdSAAKQ 325
Cdd:PRK08323 243 EAIRRARARGQRVFGETCPQYLLLDESEYDGPDWfegaKYVMSPPLRDKEHQDALWRGLQDGDLQVVATDHCPF-CFEQK 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486032191 326 APLPATE----P-GLSSIESVLSLgL--ELVQNHELELPDLLRALTAGPAAVLG---REVALTAGAAADLCLFAPDGHWQ 395
Cdd:PRK08323 322 KQLGRGDftkiPnGTPGVEDRMPL-LfsEGVMTGRITLNRFVELTSTNPAKIFGlypRKGTIAVGADADIVIWDPNATKT 400
|
410 420 430
....*....|....*....|....*....|....*
gi 2486032191 396 PSAATLLSAGRHAPVLERALPGEVKLTLVAGRTAW 430
Cdd:PRK08323 401 ISASTLHSNVDYNPYEGFEVTGWPVTTLSRGEVVV 435
|
|
| pyrC |
PRK00369 |
dihydroorotase; Provisional |
59-429 |
1.14e-18 |
|
dihydroorotase; Provisional
Pssm-ID: 234738 [Multi-domain] Cd Length: 392 Bit Score: 87.12 E-value: 1.14e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486032191 59 GQVIAPGFIDLCCNLREPGNGQKGNIASETRAAAHGGFTTVCASPETSPVNDSGAVTNLILDSVASRGVVRVLPIGAITR 138
Cdd:PRK00369 42 GTLILPGAIDLHVHLRGLKLSYKEDVASGTSEAAYGGVTLVADMPNTIPPLNTPEAITEKLAELEYYSRVDYFVYSGVTK 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486032191 139 GLDGDMLSDMAGLKAAGCVAVGNGS-RGVRNARILrrcmayaqtfgltVMFSPEntalaadgyAHDGQVTTRLGLLGIpe 217
Cdd:PRK00369 122 DPEKVDKLPIAGYKIFPEDLEREETfRVLLKSRKL-------------KILHPE---------VPLALKSNRKLRRNC-- 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486032191 218 VAETAAVMEMLLLAeetgvRLHLSQLSCARSVEMlaqARDRGVkvTADVAMHQLAFtesaLAGFDSRFHVRPPLRGEADR 297
Cdd:PRK00369 178 WYEIAALYYVKDYQ-----NVHITHASNPRTVRL---AKELGF--TVDITPHHLLV----NGEKDCLTKVNPPIRDINER 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486032191 298 QALVAGVRDgvIDAIVSQHQPHDSAAKQAPLPATEPGLSSIESVLSLGLELVQNHELELPDLLRALTAGPAAVLG-REVA 376
Cdd:PRK00369 244 LWLLQALSE--VDAIASDHAPHSSFEKLQPYEVCPPGIAALSFTPPFIYTLVSKGILSIDRAVELISTNPARILGiPYGE 321
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|...
gi 2486032191 377 LTAGAAADLCLFAPDgHWQPSaaTLLSAGRHAPVLERALPGEVKLTLVAGRTA 429
Cdd:PRK00369 322 IKEGYRANFTVIQFE-DWRYS--TKYSKVIETPLDGFELKASVYATIVQGKLA 371
|
|
| CAD_DHOase |
cd01316 |
The eukaryotic CAD protein is a trifunctional enzyme of carbamoylphosphate ... |
61-370 |
5.85e-18 |
|
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: 84.81 E-value: 5.85e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486032191 61 VIAPGFIDLCCNLREPGNGQKGNIASETRAAAHGGFTTVCASPETSPVNDSGAVTNLIlDSVASRGVV--RVLPIGAITR 138
Cdd:cd01316 3 IRLPGLIDVHVHLREPGATHKEDFASGTKAALAGGFTMVRAMPNTNPSIVDVASLKLV-QSLAQAKARcdYAFSIGATST 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486032191 139 glDGDMLSDMAGlKAAGCVAVGNGSRGvrnARILRRCMAYAQTFgltvMFSPENTALAADgyahdgqvttrlgllgipev 218
Cdd:cd01316 82 --NAATVGELAS-EAVGLKFYLNETFS---TLILDKITAWASHF----NAWPSTKPIVTH-------------------- 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486032191 219 AETAAVMEMLLLAEETGVRLHLSQLSCARSVEMLAQARDRGVKVTADVAMHQLAFTESALAgfDSRFHVRPPLRGEADRQ 298
Cdd:cd01316 132 AKSQTLAAVLLLASLHNRSIHICHVSSKEEINLIRLAKARGLKVTCEVSPHHLFLSQDDLP--RGQYEVRPFLPTREDQE 209
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2486032191 299 ALVAGVrdGVIDAIVSQHQPHDSAAKQAPLPAtePGLSSIESVLSLGLELVQNHELELPDLLRALTAGPAAV 370
Cdd:cd01316 210 ALWENL--DYIDCFATDHAPHTLAEKTGNKPP--PGFPGVETSLPLLLTAVHEGRLTIEDIVDRLHTNPKRI 277
|
|
| PRK13404 |
PRK13404 |
dihydropyrimidinase; Provisional |
34-432 |
1.57e-14 |
|
dihydropyrimidinase; Provisional
Pssm-ID: 184033 [Multi-domain] Cd Length: 477 Bit Score: 75.12 E-value: 1.57e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486032191 34 VRNGRIEAVGEQAQAAESAatLDAAGQVIAPGFIDLCCNLREP---GNGQKGNIASETRAAAHGGFTTV---CAS----- 102
Cdd:PRK13404 26 IRGGRIAALGEGLGPGARE--IDATGRLVLPGGVDSHCHIDQPsgdGIMMADDFYTGTVSAAFGGTTTVipfAAQhrgqs 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486032191 103 -PETSPVNDSGAVTNLILD-------SVASRGVV-RVLPiGAITRGL---------DGDMLSDmaglkaagcvavgngsr 164
Cdd:PRK13404 104 lREAVEDYHRRAAGKAVIDyafhlivADPTEEVLtEELP-ALIAQGYtsfkvfmtyDDLKLDD----------------- 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486032191 165 gvrnaRILRRCMAYAQTFGLTVMFSPENT---ALAADGYAHDGQVTTRLGLLGIPEVAETAAVMEMLLLAEETGVRLHLS 241
Cdd:PRK13404 166 -----RQILDVLAVARRHGAMVMVHAENHdmiAWLTKRLLAAGLTAPKYHAISRPMLAEREATHRAIALAELVDVPILIV 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486032191 242 QLSCARSVEMLAQARDRGVKVTADVAMHQLAFTESAL--AGFD-SRFHVRPPLRGEADRQALVAGVRDGVIDAIVSQHQP 318
Cdd:PRK13404 241 HVSGREAAEQIRRARGRGLKIFAETCPQYLFLTAEDLdrPGMEgAKYICSPPPRDKANQEAIWNGLADGTFEVFSSDHAP 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486032191 319 H---DSAAK-----QAPLPATEPGLSSIESVLSLGL-ELVQNHELELPDLLrALTA-GPAAVLG---REVALTAGAAADL 385
Cdd:PRK13404 321 FrfdDTDGKlaagaNPSFKAIANGIPGIETRLPLLFsEGVVKGRISLNRFV-ALTStNPAKLYGlypRKGAIAIGADADI 399
|
410 420 430 440
....*....|....*....|....*....|....*....|....*..
gi 2486032191 386 CLFAPDGHWQPSAATLLSAGRHAPVLERALPGEVKLTLVAGRTAWQA 432
Cdd:PRK13404 400 AIWDPDREVTITNADLHHAADYTPYEGMRVTGWPVTVLSRGRVVVED 446
|
|
| PLN02942 |
PLN02942 |
dihydropyrimidinase |
32-431 |
2.52e-12 |
|
dihydropyrimidinase
Pssm-ID: 178530 Cd Length: 486 Bit Score: 68.33 E-value: 2.52e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486032191 32 LLVRNGRIEAVGEQAQAAESAATLDAAGQVIAPGFIDLCCNLREPGNGQKG--NIASETRAAAHGGFTTVCASpeTSPVN 109
Cdd:PLN02942 25 VYVEDGIIVAVAPNLKVPDDVRVIDATGKFVMPGGIDPHTHLAMPFMGTETidDFFSGQAAALAGGTTMHIDF--VIPVN 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486032191 110 DsgavtNLILDSVASRGVVR--VLPIG---AITRGLDG-----DMLSDMAGLKAAGCVAVGNGSRGVRNARIL---RRCm 176
Cdd:PLN02942 103 G-----NLLAGYEAYEKKAEksCMDYGfhmAITKWDDTvsrdmETLVKEKGINSFKFFMAYKGSLMVTDELLLegfKRC- 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486032191 177 ayaQTFGLTVMFSPENTALAADGyahdgqvTTRLGLLGI----------PEVAETAAVMEMLLLAEETGVRLHLSQLSCA 246
Cdd:PLN02942 177 ---KSLGALAMVHAENGDAVFEG-------QKRMIELGItgpeghalsrPPLLEGEATARAIRLAKFVNTPLYVVHVMSI 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486032191 247 RSVEMLAQARDRGVKVTADVAMHQLAFTESALAGFD----SRFHVRPPLRGEADRQALVAGVRDGVIDAIVSQHQPHDSA 322
Cdd:PLN02942 247 DAMEEIARARKSGQRVIGEPVVSGLVLDDSKLWDPDftiaSKYVMSPPIRPAGHGKALQAALSSGILQLVGTDHCPFNST 326
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486032191 323 AKQA------PLPAtepGLSSIESVLSLGL-ELVQNHELELPDLLRALTAGPAAVLG---REVALTAGAAADLCLfapdg 392
Cdd:PLN02942 327 QKAFgkddfrKIPN---GVNGIEERMHLVWdTMVESGQISPTDYVRVTSTECAKIFNiypRKGAILAGSDADIII----- 398
|
410 420 430 440
....*....|....*....|....*....|....*....|....*
gi 2486032191 393 hWQPSAATLLSAGRH-----APVLE-RALPGEVKLTLVAGRTAWQ 431
Cdd:PLN02942 399 -LNPNSTFTISAKTHhsridTNVYEgRRGKGKVEVTISQGRVVWE 442
|
|
| COG3653 |
COG3653 |
N-acyl-D-aspartate/D-glutamate deacylase [Secondary metabolites biosynthesis, transport and ... |
32-320 |
9.12e-09 |
|
N-acyl-D-aspartate/D-glutamate deacylase [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 442870 [Multi-domain] Cd Length: 528 Bit Score: 57.49 E-value: 9.12e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486032191 32 LLVRNGRIEAVGEQAQAAESAaTLDAAGQVIAPGFID--------LccnLREPGNGQK----------GN-------IAS 86
Cdd:COG3653 24 VAIKGGRIVAVGDLAAAEAAR-VIDATGLVVAPGFIDihthydlqL---LWDPRLEPSlrqgvttvvmGNcgvsfapVRP 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486032191 87 ETRAAAHGGFTTVCASPETSPVN--DSGAVtnliLDSVASRGV------------VRVLPIGAITRGLDGDMLSDMaglk 152
Cdd:COG3653 100 EDRDRLIDLMEGVEGIPEGLDWDweSFGEY----LDALERRGLgvnvaslvghgtLRAYVMGLDDRPPTPEELARM---- 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486032191 153 aagcvavgngsrgvrnARILRRCMAyAQTFGLTVMFSP---------ENTALAADGYAHDG--QVTTRlgllgiPEVAET 221
Cdd:COG3653 172 ----------------RALLREAME-AGALGLSTGLIYvpgtyastdELVALAKVVAEYGGvyQSHMR------DEGDGL 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486032191 222 -AAVMEMLLLAEETGVRLHLSQLSCA---------RSVEMLAQARDRGVKVTADVA-------MHQLAFTESALAGFDSR 284
Cdd:COG3653 229 lEAVDELIRIGREAGVPVHISHLKAAgkpnwgkadEVLALIEAARAEGLDVTADVYpypagstGLGALLPPWAAAGGLDE 308
|
330 340 350
....*....|....*....|....*....|....*.
gi 2486032191 285 FHVRppLRGEADRQALVAGVRDGVIDAIVSQHQPHD 320
Cdd:COG3653 309 RLAR--LRDPATRARIRAEIEEGLPDNLLGRGGWDN 342
|
|
| PRK01211 |
PRK01211 |
dihydroorotase; Provisional |
62-388 |
1.78e-07 |
|
dihydroorotase; Provisional
Pssm-ID: 179247 [Multi-domain] Cd Length: 409 Bit Score: 52.94 E-value: 1.78e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486032191 62 IAPGFIDLCCNLREPGNGQKGNIASETRAAAHGGFTTVCASPETS-PVNDSGAVTNLiLDSVASRGVVRvLPIGAITRGL 140
Cdd:PRK01211 44 ILPAATDIHVHFRTPGETEKEDFSTGTLSAIFGGTTFIMDMPNNNiPIKDYNAFSDK-LGRVAPKAYVD-FSLYSMETGN 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486032191 141 DGDMLSDMA-GLKaagcVAVGnGSRGVRNARILRRCMAYAQTFGLTVMFSPENTALAADGYAHDGQVttRLGLLGIPEVA 219
Cdd:PRK01211 122 NALILDERSiGLK----VYMG-GTTNTNGTDIEGGEIKKINEANIPVFFHAELSECLRKHQFESKNL--RDHDLARPIEC 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486032191 220 ETAAVMEMLLLAEETGVRLHLSQLscarsvemlaqarDRGVKVTADVAMHQLAFTESALAGfdSRFHVRPPLRGEADRQA 299
Cdd:PRK01211 195 EIKAVKYVKNLDLKTKIIAHVSSI-------------DVIGRFLREVTPHHLLLNDDMPLG--SYGKVNPPLRDRWTQER 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486032191 300 LVAGVRDGVIDAIVSQHQPHdSAAKQAPLPATEPGLSSIESVLSLGLELVQNHELELPDLLRALTAGPAAVLG-REVALT 378
Cdd:PRK01211 260 LLEEYISGRFDILSSDHAPH-TEEDKQEFEYAKSGIIGVETRVPLFLALVKKKILPLDVLYKTAIERPASLFGiKKGKIE 338
|
330
....*....|
gi 2486032191 379 AGAAADLCLF 388
Cdd:PRK01211 339 EGYDADFMAF 348
|
|
| PRK09061 |
PRK09061 |
D-glutamate deacylase; Validated |
14-99 |
8.05e-06 |
|
D-glutamate deacylase; Validated
Pssm-ID: 236369 [Multi-domain] Cd Length: 509 Bit Score: 48.15 E-value: 8.05e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486032191 14 LTGGQLFEPGKGLISNPGLLVRNGRIEAVGEQAQAAESaaTLDAAGQVIAPGFIDLCCNLREPGNgqkgniaseTRAAAH 93
Cdd:PRK09061 23 IRNGRVVDPETGLDAVRDVGIKGGKIAAVGTAAIEGDR--TIDATGLVVAPGFIDLHAHGQSVAA---------YRMQAF 91
|
....*.
gi 2486032191 94 GGFTTV 99
Cdd:PRK09061 92 DGVTTA 97
|
|
| HutI |
COG1228 |
Imidazolonepropionase or related amidohydrolase [Secondary metabolites biosynthesis, transport ... |
14-99 |
1.15e-05 |
|
Imidazolonepropionase or related amidohydrolase [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 440841 [Multi-domain] Cd Length: 386 Bit Score: 47.26 E-value: 1.15e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486032191 14 LTGGQLF-EPGKGLISNPGLLVRNGRIEAVGEQAQAAE--SAATLDAAGQVIAPGFIDLCCNL-----REPGNGQKGNIA 85
Cdd:COG1228 12 ITNATLVdGTGGGVIENGTVLVEDGKIAAVGPAADLAVpaGAEVIDATGKTVLPGLIDAHTHLglgggRAVEFEAGGGIT 91
|
90 100
....*....|....*....|....
gi 2486032191 86 SETRAAAH----------GGFTTV 99
Cdd:COG1228 92 PTVDLVNPadkrlrralaAGVTTV 115
|
|
| NagA |
cd00854 |
N-acetylglucosamine-6-phosphate deacetylase, NagA, catalyzes the hydrolysis of the N-acetyl ... |
12-69 |
1.77e-05 |
|
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: 46.80 E-value: 1.77e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 2486032191 12 LKLTGGQLFEPGKglISNPGLLVRNGRIEAVGEQAQAAESAATLDAAGQVIAPGFIDL 69
Cdd:cd00854 1 LIIKNARILTPGG--LEDGAVLVEDGKIVAIGPEDELEEADEIIDLKGQYLVPGFIDI 56
|
|
| COG3964 |
COG3964 |
Predicted amidohydrolase [General function prediction only]; |
14-69 |
1.93e-05 |
|
Predicted amidohydrolase [General function prediction only];
Pssm-ID: 443164 [Multi-domain] Cd Length: 376 Bit Score: 46.70 E-value: 1.93e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 2486032191 14 LTGGQLFEPGKGLISNPGLLVRNGRIEAVGEQAQAAESAATLDAAGQVIAPGFIDL 69
Cdd:COG3964 4 IKGGRVIDPANGIDGVMDIAIKDGKIAAVAKDIDAAEAKKVIDASGLYVTPGLIDL 59
|
|
| Amidohydro_1 |
pfam01979 |
Amidohydrolase family; This family of enzymes are a a large metal dependent hydrolase ... |
61-428 |
2.42e-05 |
|
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: 45.96 E-value: 2.42e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486032191 61 VIAPGFID--------LCCNLREPGNGQKGNIASETRAAAHGGFTTVCASPETSPVNDSG---AVTNLILD--------S 121
Cdd:pfam01979 1 IVLPGLIDahvhlemgLLRGIPVPPEFAYEALRLGITTMLKSGTTTVLDMGATTSTGIEAlleAAEELPLGlrflgpgcS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486032191 122 VASRGVVRVLPI-------GAITRGLDGDMLSdMAGLKAAGCVAVGNGSrgvrnariLRRCMAYAQTFGLTVMFSPENTa 194
Cdd:pfam01979 81 LDTDGELEGRKAlreklkaGAEFIKGMADGVV-FVGLAPHGAPTFSDDE--------LKAALEEAKKYGLPVAIHALET- 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486032191 195 lAADGYAHDGQVTTRLGLLGIPEVAETAAVMEMLLLAEETGVRLHlsqlscARSVEMLAQaRDRGVKVTAdvamhqLAFT 274
Cdd:pfam01979 151 -KGEVEDAIAAFGGGIEHGTHLEVAESGGLLDIIKLILAHGVHLS------PTEANLLAE-HLKGAGVAH------CPFS 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486032191 275 ESALagfdsrfhvrpplrgEADRQALVAGVRDGVIDAIVSqhqphDSAAKQAPLPATEpglssiESVLSLGLELVQNHEL 354
Cdd:pfam01979 217 NSKL---------------RSGRIALRKALEDGVKVGLGT-----DGAGSGNSLNMLE------ELRLALELQFDPEGGL 270
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2486032191 355 ELPDLLRALTAGPAAVLGREV---ALTAGAAADLCLFAPDghwqpsaatllsagRHAPVLERALPGEVKLTLVAGRT 428
Cdd:pfam01979 271 SPLEALRMATINPAKALGLDDkvgSIEVGKDADLVVVDLD--------------PLAAFFGLKPDGNVKKVIVKGKI 333
|
|
| NagA |
COG1820 |
N-acetylglucosamine-6-phosphate deacetylase [Carbohydrate transport and metabolism]; |
14-72 |
4.19e-05 |
|
N-acetylglucosamine-6-phosphate deacetylase [Carbohydrate transport and metabolism];
Pssm-ID: 441425 [Multi-domain] Cd Length: 373 Bit Score: 45.48 E-value: 4.19e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 2486032191 14 LTGGQLFEPGkGLISNPGLLVRNGRIEAVGEQAQAAESaaTLDAAGQVIAPGFIDLCCN 72
Cdd:COG1820 2 ITNARIFTGD-GVLEDGALLIEDGRIAAIGPGAEPDAE--VIDLGGGYLAPGFIDLHVH 57
|
|
| D-aminoacylase |
cd01297 |
D-aminoacylases (N-acyl-D-Amino acid amidohydrolases) catalyze the hydrolysis of ... |
34-267 |
1.70e-04 |
|
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: 43.82 E-value: 1.70e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486032191 34 VRNGRIEAVGEQAQAAESAaTLDAAGQVIAPGFIDLCCN-----LREP---------------GNGQKGNIASETRAAAH 93
Cdd:cd01297 24 IRDGRIAAIGPILSTSARE-VIDAAGLVVAPGFIDVHTHydgqvFWDPdlrpssrqgvttvvlGNCGVSPAPANPDDLAR 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486032191 94 GGFTTVCASPETSPVNDSGAVTNLILDSVASRG----VVRVLPIGAITR---GLDGDMLSD-----MAGLKA----AGCV 157
Cdd:cd01297 103 LIMLMEGLVALGEGLPWGWATFAEYLDALEARPpavnVAALVGHAALRRavmGLDAREATEeelakMRELLRealeAGAL 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486032191 158 AVGNGsrgvrnarilrrcMAYAQTFGLTVmfsPENTALAADGYAHDGQVTTRLGLLGIPEVaetAAVMEMLLLAEETGVR 237
Cdd:cd01297 183 GISTG-------------LAYAPRLYAGT---AELVALARVAARYGGVYQTHVRYEGDSIL---EALDELLRLGRETGRP 243
|
250 260 270
....*....|....*....|....*....|....*....
gi 2486032191 238 LHLSQLSCA---------RSVEMLAQARDRGVKVTADVA 267
Cdd:cd01297 244 VHISHLKSAgapnwgkidRLLALIEAARAEGLQVTADVY 282
|
|
| SsnA |
COG0402 |
Cytosine/adenosine deaminase or related metal-dependent hydrolase [Nucleotide transport and ... |
20-69 |
5.76e-04 |
|
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: 42.12 E-value: 5.76e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 2486032191 20 FEPGKGLISNPGLLVRNGRIEAVGEQAQAAESAA---TLDAAGQVIAPGFIDL 69
Cdd:COG0402 12 MDPAGGVLEDGAVLVEDGRIAAVGPGAELPARYPaaeVIDAGGKLVLPGLVNT 64
|
|
| SsnA |
COG0402 |
Cytosine/adenosine deaminase or related metal-dependent hydrolase [Nucleotide transport and ... |
358-427 |
1.07e-03 |
|
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: 40.97 E-value: 1.07e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2486032191 358 DLLRALTAGPAAVLGREV---ALTAGAAADLCLFAPDGHWQPSAATLLSAgrhapVLERALPGEVKLTLVAGR 427
Cdd:COG0402 344 EALEMATLGGARALGLDDeigSLEPGKRADLVVLDLDAPHLAPLHDPLSA-----LVYAADGRDVRTVWVAGR 411
|
|
| PRK09237 |
PRK09237 |
amidohydrolase/deacetylase family metallohydrolase; |
14-69 |
1.21e-03 |
|
amidohydrolase/deacetylase family metallohydrolase;
Pssm-ID: 236423 [Multi-domain] Cd Length: 380 Bit Score: 40.99 E-value: 1.21e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 2486032191 14 LTGGQLFEPGKGLISNPGLLVRNGRIEAVGEQAQAAESAATLDAAGQVIAPGFIDL 69
Cdd:PRK09237 3 LRGGRVIDPANGIDGVIDIAIEDGKIAAVAGDIDGSQAKKVIDLSGLYVSPGWIDL 58
|
|
| |
