|
Name |
Accession |
Description |
Interval |
E-value |
| PRK08323 |
PRK08323 |
phenylhydantoinase; Validated |
1-453 |
0e+00 |
|
phenylhydantoinase; Validated
Pssm-ID: 236240 [Multi-domain] Cd Length: 459 Bit Score: 671.11 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489524267 1 MGTILRGGTIITSDKTYISDLRIEDEKIVEIGNNleiNGDKVIDATGKIVIPGGIDTHTHFDMNAGSITTADNFETGTRA 80
Cdd:PRK08323 1 MSTLIKNGTVVTADDTYKADVLIEDGKIAAIGAN---LGDEVIDATGKYVMPGGIDPHTHMEMPFGGTVSSDDFETGTRA 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489524267 81 AIAGGTTTILDFAEANEGENLLQGVEAYHKKASGNCYCDYGFHMTITCLNKDTFNHMEKLISDGIVSFKMYMAYDG-MKV 159
Cdd:PRK08323 78 AACGGTTTIIDFALQPKGQSLREALEAWHGKAAGKAVIDYGFHMIITDWNEVVLDEMPELVEEGITSFKLFMAYKGaLML 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489524267 160 DDGAIYRVLKKARDLGCIVEFHCENGDLLDVLIEENIQNGNLEPKYHPLTRPNIVEKESVSRLADITKLSNSKSYVVHLS 239
Cdd:PRK08323 158 DDDELLRALQRAAELGALPMVHAENGDAIAYLQAKLLAEGKTGPEYHALSRPPEVEGEATNRAIMLAELAGAPLYIVHVS 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489524267 240 CKESLETVKTAREKNIDMIVETCPQYLLL-EDNLYNKDKFEGAKYVMSPPLRKKEDINYLWEGLASGDIQTVGTDHCSFN 318
Cdd:PRK08323 238 CKEALEAIRRARARGQRVFGETCPQYLLLdESEYDGPDWFEGAKYVMSPPLRDKEHQDALWRGLQDGDLQVVATDHCPFC 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489524267 319 FKGQKDLGIDDFSKIPNGAPGVEHRLALLYTYGVLENRISANKFVEVTSTNAAKIFGMYPKKGEIAVGSDADIVILNVNK 398
Cdd:PRK08323 318 FEQKKQLGRGDFTKIPNGTPGVEDRMPLLFSEGVMTGRITLNRFVELTSTNPAKIFGLYPRKGTIAVGADADIVIWDPNA 397
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*.
gi 489524267 399 EETISYKTQKQNVDYTPYEGFKIKCKVEDVFLRGNHVVQSCNVKEHP-TGQYIKRK 453
Cdd:PRK08323 398 TKTISASTLHSNVDYNPYEGFEVTGWPVTTLSRGEVVVEDGEFRGKAgHGRFLKRK 453
|
|
| D-HYD |
cd01314 |
D-hydantoinases (D-HYD) also called dihydropyrimidases (DHPase) and related proteins; DHPases ... |
3-436 |
0e+00 |
|
D-hydantoinases (D-HYD) also called dihydropyrimidases (DHPase) and related proteins; DHPases are a family of enzymes that catalyze the reversible hydrolytic ring opening of the amide bond in five- or six-membered cyclic diamides, like dihydropyrimidine or hydantoin. The hydrolysis of dihydropyrimidines is the second step of reductive catabolism of pyrimidines in human. The hydrolysis of 5-substituted hydantoins in microorganisms leads to enantiomerically pure N-carbamyl amino acids, which are used for the production of antibiotics, peptide hormones, pyrethroids, and pesticides. HYDs are classified depending on their stereoselectivity. This family also includes collapsin response regulators (CRMPs), cytosolic proteins involved in neuronal differentiation and axonal guidance which have strong homology to DHPases, but lack most of the active site residues.
Pssm-ID: 238639 [Multi-domain] Cd Length: 447 Bit Score: 638.11 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489524267 3 TILRGGTIITSDKTYISDLRIEDEKIVEIGNNLEI-NGDKVIDATGKIVIPGGIDTHTHFDMNAGSITTADNFETGTRAA 81
Cdd:cd01314 1 LIIKNGTIVTADGSFKADILIEDGKIVAIGPNLEApGGVEVIDATGKYVLPGGIDPHTHLELPFMGTVTADDFESGTRAA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489524267 82 IAGGTTTILDFAEANEGENLLQGVEAYHKKASGNCYCDYGFHMTITCLNKDTFNHMEKLISDGIVSFKMYMAYDGMK-VD 160
Cdd:cd01314 81 AAGGTTTIIDFAIPNKGQSLLEAVEKWRGKADGKSVIDYGFHMIITDWTDSVIEELPELVKKGISSFKVFMAYKGLLmVD 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489524267 161 DGAIYRVLKKARDLGCIVEFHCENGDLLDVLIEENIQNGNLEPKYHPLTRPNIVEKESVSRLADITKLSNSKSYVVHLSC 240
Cdd:cd01314 161 DEELLDVLKRAKELGALVMVHAENGDVIAELQKKLLAQGKTGPEYHALSRPPEVEAEATARAIRLAELAGAPLYIVHVSS 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489524267 241 KESLETVKTAREKNIDMIVETCPQYLLLEDNLYNKDKFEGAKYVMSPPLRKKEDINYLWEGLASGDIQTVGTDHCSFNFk 320
Cdd:cd01314 241 KEAADEIARARKKGLPVYGETCPQYLLLDDSDYWKDWFEGAKYVCSPPLRPKEDQEALWDGLSSGTLQTVGSDHCPFNF- 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489524267 321 GQKDLGIDDFSKIPNGAPGVEHRLALLYTYGVLENRISANKFVEVTSTNAAKIFGMYPKKGEIAVGSDADIVILNVNKEE 400
Cdd:cd01314 320 AQKARGKDDFTKIPNGVPGVETRMPLLWSEGVAKGRITLEKFVELTSTNPAKIFGLYPRKGTIAVGSDADLVIWDPNAEK 399
|
410 420 430
....*....|....*....|....*....|....*.
gi 489524267 401 TISYKTQKQNVDYTPYEGFKIKCKVEDVFLRGNHVV 436
Cdd:cd01314 400 TISADTHHHNVDYNIFEGMKVKGWPVVTISRGKVVV 435
|
|
| D-hydantoinase |
TIGR02033 |
D-hydantoinase; This model represents the D-hydantoinase (dihydropyrimidinase) which primarily ... |
4-452 |
0e+00 |
|
D-hydantoinase; This model represents the D-hydantoinase (dihydropyrimidinase) which primarily converts 5,6-dihydrouracil to 3-ureidopropanoate but also acts on dihydrothymine and hydantoin. The enzyme is a metalloenzyme.
Pssm-ID: 273937 [Multi-domain] Cd Length: 454 Bit Score: 587.43 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489524267 4 ILRGGTIITSDKTYISDLRIEDEKIVEIGNNLEI-NGDKVIDATGKIVIPGGIDTHTHFDMNAGSITTADNFETGTRAAI 82
Cdd:TIGR02033 2 LIKGGTVVNADDVFQADVLIEGGKIVAVGDNLIPpDAVEVIDATGKYVLPGGIDVHTHLEMPFGGTTTADDFFTGTKAAA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489524267 83 AGGTTTILDFAEANEGENLLQGVEAYHKKASGNCYCDYGFHMTITCLNKDTFN-HMEKLISDGIVSFKMYMAYDG-MKVD 160
Cdd:TIGR02033 82 AGGTTTIIDFVVPEKGSSLTEALETWHEKAEGKSVIDYGFHMDITHWNDSVLEeHIPEVKEEGINSFKVFMAYKNlLMVD 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489524267 161 DGAIYRVLKKARDLGCIVEFHCENGDLLDVLIEENIQNGNLEPKYHPLTRPNIVEKESVSRLADITKLSNSKSYVVHLSC 240
Cdd:TIGR02033 162 DEELFEILKRLKELGALLQVHAENGDIIAELQARMLAQGITGPEYHALSRPPELEAEAVARAITLAALADAPLYVVHVST 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489524267 241 KESLETVKTAREKNIDMIVETCPQYLLLEDNLYNKDKFEGAKYVMSPPLRKKEDINYLWEGLASGDIQTVGTDHCSFNFK 320
Cdd:TIGR02033 242 KDAADEIAQARKKGQPVFGETCPQYLVLDDTHYDKPGFEGAKYVCSPPLREPEDQDALWSALSSGALQTVGSDHCTFNFA 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489524267 321 GQKDLGIDDFSKIPNGAPGVEHRLALLYTYGVLENRISANKFVEVTSTNAAKIFGMYPKKGEIAVGSDADIVILNVNKEE 400
Cdd:TIGR02033 322 QKKAIGKDDFTKIPNGGPGVEERMSLLFDEGVAKGRITLEKFVEVTSTNPAKIFNLYPRKGTIAVGSDADIVIWDPNRTT 401
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|...
gi 489524267 401 TISYKTQKQNVDYTPYEGFKIKCKVEDVFLRGNHVVQSCNVKEHP-TGQYIKR 452
Cdd:TIGR02033 402 VISAETHHSNADYNPFEGFKVRGAPVSVLSRGRVVVEDGQLVGTAgAGRFVKR 454
|
|
| AllB |
COG0044 |
Dihydroorotase or related cyclic amidohydrolase [Nucleotide transport and metabolism]; ... |
4-452 |
5.43e-177 |
|
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: 502.31 E-value: 5.43e-177
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489524267 4 ILRGGTIITSDKTYISDLRIEDEKIVEIGNNLE-INGDKVIDATGKIVIPGGIDTHTHFDMNAGsiTTADNFETGTRAAI 82
Cdd:COG0044 1 LIKNGRVVDPGGLERADVLIEDGRIAAIGPDLAaPEAAEVIDATGLLVLPGLIDLHVHLREPGL--EHKEDIETGTRAAA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489524267 83 AGGTTTILDFAEANEGENLLQGVEAYHKKASGNCYCDYGFHMTITCLNKDTFNHMEKLISDGIVSFKMYMAYDG--MKVD 160
Cdd:COG0044 79 AGGVTTVVDMPNTNPVTDTPEALEFKLARAEEKALVDVGPHGALTKGLGENLAELGALAEAGAVAFKVFMGSDDgnPVLD 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489524267 161 DGAIYRVLKKARDLGCIVEFHCENGDLLDVLIEEniqNGNLEPKYHPLTRPNIVEKESVSRLADITKLSNSKSYVVHLSC 240
Cdd:COG0044 159 DGLLRRALEYAAEFGALVAVHAEDPDLIRGGVMN---EGKTSPRLGLKGRPAEAEEEAVARDIALAEETGARLHIVHVST 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489524267 241 KESLETVKTAREKNIDMIVETCPQYLLLEDNLYnkdKFEGAKYVMSPPLRKKEDINYLWEGLASGDIQTVGTDHCSFNFK 320
Cdd:COG0044 236 AEAVELIREAKARGLPVTAEVCPHHLTLTDEDL---ERYGTNFKVNPPLRTEEDREALWEGLADGTIDVIATDHAPHTLE 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489524267 321 gQKDlgiDDFSKIPNGAPGVEHRLALLYTYGVLENRISANKFVEVTSTNAAKIFGMyPKKGEIAVGSDADIVILNVNKEE 400
Cdd:COG0044 313 -EKE---LPFAEAPNGIPGLETALPLLLTELVHKGRLSLERLVELLSTNPARIFGL-PRKGRIAVGADADLVLFDPDAEW 387
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|..
gi 489524267 401 TISYKTQKQNVDYTPYEGFKIKCKVEDVFLRGNHVVQSCNVKEHPTGQYIKR 452
Cdd:COG0044 388 TVTAEDLHSKSKNTPFEGRELTGRVVATIVRGRVVYEDGEVVGEPRGRFLRR 439
|
|
| PRK13404 |
PRK13404 |
dihydropyrimidinase; Provisional |
3-452 |
1.23e-156 |
|
dihydropyrimidinase; Provisional
Pssm-ID: 184033 [Multi-domain] Cd Length: 477 Bit Score: 452.23 E-value: 1.23e-156
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489524267 3 TILRGGTIITSDKTYISDLRIEDEKIVEIGNNLEiNGDKVIDATGKIVIPGGIDTHTHFDMNAGS-ITTADNFETGTRAA 81
Cdd:PRK13404 6 LVIRGGTVVTATDTFQADIGIRGGRIAALGEGLG-PGAREIDATGRLVLPGGVDSHCHIDQPSGDgIMMADDFYTGTVSA 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489524267 82 IAGGTTTILDFAEANEGENLLQGVEAYHKKASGNCYCDYGFHMTITCLNKDTFN-HMEKLISDGIVSFKMYMAYDGMKVD 160
Cdd:PRK13404 85 AFGGTTTVIPFAAQHRGQSLREAVEDYHRRAAGKAVIDYAFHLIVADPTEEVLTeELPALIAQGYTSFKVFMTYDDLKLD 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489524267 161 DGAIYRVLKKARDLGCIVEFHCENGDLLDVLIEENIQNGNLEPKYHPLTRPNIVEKESVSRLADITKLSNSKSYVVHLSC 240
Cdd:PRK13404 165 DRQILDVLAVARRHGAMVMVHAENHDMIAWLTKRLLAAGLTAPKYHAISRPMLAEREATHRAIALAELVDVPILIVHVSG 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489524267 241 KESLETVKTAREKNIDMIVETCPQYLLLEDNLYNKDKFEGAKYVMSPPLRKKEDINYLWEGLASGDIQTVGTDHCSFNFK 320
Cdd:PRK13404 245 REAAEQIRRARGRGLKIFAETCPQYLFLTAEDLDRPGMEGAKYICSPPPRDKANQEAIWNGLADGTFEVFSSDHAPFRFD 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489524267 321 GQ--KDLGIDD--FSKIPNGAPGVEHRLALLYTYGVLENRISANKFVEVTSTNAAKIFGMYPKKGEIAVGSDADIVILNV 396
Cdd:PRK13404 325 DTdgKLAAGANpsFKAIANGIPGIETRLPLLFSEGVVKGRISLNRFVALTSTNPAKLYGLYPRKGAIAIGADADIAIWDP 404
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*..
gi 489524267 397 NKEETISYKTQKQNVDYTPYEGFKIKCKVEDVFLRGNHVVQSCNVKEHP-TGQYIKR 452
Cdd:PRK13404 405 DREVTITNADLHHAADYTPYEGMRVTGWPVTVLSRGRVVVEDGELVAERgSGQFLAR 461
|
|
| PLN02942 |
PLN02942 |
dihydropyrimidinase |
4-453 |
9.69e-139 |
|
dihydropyrimidinase
Pssm-ID: 178530 Cd Length: 486 Bit Score: 406.92 E-value: 9.69e-139
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489524267 4 ILRGGTIITSDKTYISDLRIEDEKIVEIGNNLEINGD-KVIDATGKIVIPGGIDTHTHFDMNAGSITTADNFETGTRAAI 82
Cdd:PLN02942 8 LIKGGTVVNAHHQELADVYVEDGIIVAVAPNLKVPDDvRVIDATGKFVMPGGIDPHTHLAMPFMGTETIDDFFSGQAAAL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489524267 83 AGGTTTILDFAEANEGeNLLQGVEAYHKKASGNCyCDYGFHMTITCLNKDTFNHMEKLISD-GIVSFKMYMAYDG-MKVD 160
Cdd:PLN02942 88 AGGTTMHIDFVIPVNG-NLLAGYEAYEKKAEKSC-MDYGFHMAITKWDDTVSRDMETLVKEkGINSFKFFMAYKGsLMVT 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489524267 161 DGAIYRVLKKARDLGCIVEFHCENGDLLDVLIEENIQNGNLEPKYHPLTRPNIVEKESVSRLADITKLSNSKSYVVHLSC 240
Cdd:PLN02942 166 DELLLEGFKRCKSLGALAMVHAENGDAVFEGQKRMIELGITGPEGHALSRPPLLEGEATARAIRLAKFVNTPLYVVHVMS 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489524267 241 KESLETVKTAREKNIDMIVETCPQYLLLEDN-LYNKDKFEGAKYVMSPPLRKKEDINYLWEGLASGDIQTVGTDHCSFNf 319
Cdd:PLN02942 246 IDAMEEIARARKSGQRVIGEPVVSGLVLDDSkLWDPDFTIASKYVMSPPIRPAGHGKALQAALSSGILQLVGTDHCPFN- 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489524267 320 KGQKDLGIDDFSKIPNGAPGVEHRLALLYTYGVLENRISANKFVEVTSTNAAKIFGMYPKKGEIAVGSDADIVILNVNKE 399
Cdd:PLN02942 325 STQKAFGKDDFRKIPNGVNGIEERMHLVWDTMVESGQISPTDYVRVTSTECAKIFNIYPRKGAILAGSDADIIILNPNST 404
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*
gi 489524267 400 ETISYKTQKQNVDYTPYEGFKIKCKVEDVFLRGNHVVQSCNVKEHP-TGQYIKRK 453
Cdd:PLN02942 405 FTISAKTHHSRIDTNVYEGRRGKGKVEVTISQGRVVWENGELKVVRgSGRYIEMP 459
|
|
| Cyclic_amidohydrolases |
cd01302 |
Cyclic amidohydrolases, including hydantoinase, dihydropyrimidinase, allantoinase, and ... |
48-428 |
1.30e-101 |
|
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: 306.63 E-value: 1.30e-101
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489524267 48 KIVIPGGIDTHTHFDMnAGSITTADNFETGTRAAIAGGTTTILDFAEANEGENLLQGVEAYHKKASGNCYCDYGFHMTIT 127
Cdd:cd01302 1 LLVLPGFIDIHVHLRD-PGGTTYKEDFESGSRAAAAGGVTTVIDMPNTGPPPIDLPAIELKIKLAEESSYVDFSFHAGIG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489524267 128 clNKDTFNHMEKLISDGIVSFKMYMAY---DGMKVDDGAIYRVLKKARDLGCIVEFHCEngdlldvlieeniqngnlepk 204
Cdd:cd01302 80 --PGDVTDELKKLFDAGINSLKVFMNYyfgELFDVDDGTLMRTFLEIASRGGPVMVHAE--------------------- 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489524267 205 yhpltrpnivekesvsRLADITKLSNSKSYVVHLSCKESLETVKTAREKNIDMIVETCPQYLLLEDNLYNkdkFEGAKYV 284
Cdd:cd01302 137 ----------------RAAQLAEEAGANVHIAHVSSGEALELIKFAKNKGVKVTCEVCPHHLFLDESMLR---LNGAWGK 197
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489524267 285 MSPPLRKKEDINYLWEGLASGDIQTVGTDHCSFNFKGQKDLGidDFSKIPNGAPGVEHRLALLYTYGVlENRISANKFVE 364
Cdd:cd01302 198 VNPPLRSKEDREALWEGVKNGKIDTIASDHAPHSKEEKESGK--DIWKAPPGFPGLETRLPILLTEGV-KRGLSLETLVE 274
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 489524267 365 VTSTNAAKIFGMYPKKgEIAVGSDADIVILNVNKEETISYKTQKQNVDYTPYEGFKIKCKVEDV 428
Cdd:cd01302 275 ILSENPARIFGLYPKG-TIAVGYDADLVIVDPKKEWKVTAEEIESKADWTPFEGMEVTGKPVST 337
|
|
| L-HYD_ALN |
cd01315 |
L-Hydantoinases (L-HYDs) and Allantoinase (ALN); L-Hydantoinases are a member of the ... |
3-451 |
1.69e-91 |
|
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: 284.57 E-value: 1.69e-91
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489524267 3 TILRGGTIITSDKTYISDLRIEDEKIVEIGNNLE-INGDKVIDATGKIVIPGGIDTHTHFdmNAGSITTADNFETGTRAA 81
Cdd:cd01315 2 LVIKNGRVVTPDGVREADIAVKGGKIAAIGPDIAnTEAEEVIDAGGLVVMPGLIDTHVHI--NEPGRTEWEGFETGTKAA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489524267 82 IAGGTTTILDFAEANE-----GENLLQGVEAyhkkASGNCYCDYGFHMTITCLNKDtfnHMEKLISDGIVSFKMYMAYDG 156
Cdd:cd01315 80 AAGGITTIIDMPLNSIpptttVENLEAKLEA----AQGKLHVDVGFWGGLVPGNLD---QLRPLDEAGVVGFKCFLCPSG 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489524267 157 M----KVDDGAIYRVLKKARDLGCIVEFHCENGDLLDVLIEENIQNGnlEPKYHPL--TRPNIVEKESVSRLADITKLSN 230
Cdd:cd01315 153 VdefpAVDDEQLEEAMKELAKTGSVLAVHAENPEITEALQEQAKAKG--KRDYRDYlaSRPVFTEVEAIQRILLLAKETG 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489524267 231 SKSYVVHLSCKESLETVKTAREKNIDMIVETCPQYLLLEDnlynkDKFE--GAKYVMSPPLRKKEDINYLWEGLASGDIQ 308
Cdd:cd01315 231 CRLHIVHLSSAEAVPLIREARAEGVDVTVETCPHYLTFTA-----EDVPdgGTEFKCAPPIRDAANQEQLWEALENGDID 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489524267 309 TVGTDHcSFNFKGQKDLGIDDFSKIPNGAPGVEHRLALLYTYGVLENRISANKFVEVTSTNAAKIFGMYPKKGEIAVGSD 388
Cdd:cd01315 306 MVVSDH-SPCTPELKLLGKGDFFKAWGGISGLQLGLPVMLTEAVNKRGLSLEDIARLMCENPAKLFGLSHQKGRIAVGYD 384
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 489524267 389 ADIVILNVNKEETIS-----YKTQkqnvdYTPYEGFKIKCKVEDVFLRGNHVVQSCNVKEHPTGQYIK 451
Cdd:cd01315 385 ADFVVWDPEEEFTVDaedlyYKNK-----ISPYVGRTLKGRVHATILRGTVVYQDGEVVGEPLGQLLL 447
|
|
| PRK06189 |
PRK06189 |
allantoinase; Provisional |
4-456 |
4.20e-84 |
|
allantoinase; Provisional
Pssm-ID: 235732 [Multi-domain] Cd Length: 451 Bit Score: 265.80 E-value: 4.20e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489524267 4 ILRGGTIITSDKTYISDLRIEDEKIVEIGNNLEINGDKVIDATGKIVIPGGIDTHTHFdmNAGSITTADNFETGTRAAIA 83
Cdd:PRK06189 6 IIRGGKVVTPEGVYRADIGIKNGKIAEIAPEISSPAREIIDADGLYVFPGMIDVHVHF--NEPGRTHWEGFATGSAALAA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489524267 84 GGTTTILDFAeAN------EGENLLQGVEAyhkkASGNCYCDYGFHMTITCLNKDtfnHMEKLISDGIVSFKMYMAYDGM 157
Cdd:PRK06189 84 GGCTTYFDMP-LNsipptvTREALDAKAEL----ARQKSAVDFALWGGLVPGNLE---HLRELAEAGVIGFKAFMSNSGT 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489524267 158 K----VDDGAIYRVLKKARDLGCIVEFHCENGDLLDVLIEENIQNGNLEPKYHPLTRPNIVEKESVSRLADITKLSNSKS 233
Cdd:PRK06189 156 DefrsSDDLTLYEGMKEIAALGKILALHAESDALTRHLTTQARQQGKTDVRDYLESRPVVAELEAVQRALLYAQETGCPL 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489524267 234 YVVHLSCKESLETVKTAREKNIDMIVETCPQYLLLEDnlynkDKFE--GAKYVMSPPLRKKEDINYLWEGLASGDIQTVG 311
Cdd:PRK06189 236 HFVHISSGKAVALIAEAKKRGVDVSVETCPHYLLFTE-----EDFEriGAVAKCAPPLRSRSQKEELWRGLLAGEIDMIS 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489524267 312 TDH--CSFNFKGQkdlgiDDFSKIPNGAPGVEHRLALLYTYGVLENRISANKFVEVTSTNAAKIFGMyPKKGEIAVGSDA 389
Cdd:PRK06189 311 SDHspCPPELKEG-----DDFFLVWGGISGGQSTLLVMLTEGYIERGIPLETIARLLATNPAKRFGL-PQKGRLEVGADA 384
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 489524267 390 DIVILNVNKEETISYKTQKQNVDYTPYEGFKIKCKVEDVFLRGNHVVQSCNVKEHPTGQYIKRKITK 456
Cdd:PRK06189 385 DFVLVDLDETYTLTKEDLFYRHKQSPYEGRTFPGRVVATYLRGQCVYQDGEVFPPPRGQLLRPSVVK 451
|
|
| allantoinase |
TIGR03178 |
allantoinase; This enzyme carries out the first step in the degradation of allantoin, a ... |
2-450 |
5.47e-82 |
|
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: 260.01 E-value: 5.47e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489524267 2 GTILRGGTIITSDKTYISDLRIEDEKIVEIGNNLEINGDKVIDATGKIVIPGGIDTHTHFdmNAGSITTADNFETGTRAA 81
Cdd:TIGR03178 1 DLIIRGGRVILPNGEREADVGVKGGKIAAIGPDILGPAAKIIDAGGLVVFPGVVDTHVHI--NEPGRTEWEGFETGTRAA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489524267 82 IAGGTTTILDF------AEANEgENLLQGVEAyhkkASGNCYCDYGFHMTITCLNKDtfnHMEKLISDGIVSFKMYMAYD 155
Cdd:TIGR03178 79 AAGGITTYIDMplnsipATTTR-ASLEAKFEA----AKGKLAVDVGFWGGLVPYNLD---DLRELDEAGVVGFKAFLSPS 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489524267 156 G----MKVDDGAIYRVLKKARDLGCIVEFHCENGDLLDVLIEENIQNGnlEPKYHPL--TRPNIVEKESVSRLADITKLS 229
Cdd:TIGR03178 151 GddefPHVDDWQLYKGMRELARLGQLLLVHAENPAITSALGEEAPPQG--GVGADAYlaSRPVFAEVEAIRRTLALAKVT 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489524267 230 NSKSYVVHLSCKESLETVKTAREKNIDMIVETCPQYLLLednlyNKDKFE--GAKYVMSPPLRKKEDINYLWEGLASGDI 307
Cdd:TIGR03178 229 GCRVHVVHLSSAEAVELITEAKQEGLDVTVETCPHYLTL-----TAEEVPdgGTLAKCAPPIRDLANQEGLWEALLNGLI 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489524267 308 QTVGTDH--CSFNFKGQkdlgiDDFSKIPNGAPGVEHRLALLYTYGVLENRISANKFVEVTSTNAAKIFGMyPKKGEIAV 385
Cdd:TIGR03178 304 DCVVSDHspCTPDLKRA-----GDFFKAWGGIAGLQSTLDVMFDEAVQKRGLPLEDIARLMATNPAKRFGL-AQKGRIAP 377
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 489524267 386 GSDADIVILNVNKEETISYKTQKQNVDYTPYEGFKIKCKVEDVFLRGNHVVQSCNVKEHPTGQYI 450
Cdd:TIGR03178 378 GKDADFVFVDPDESYTLTPDDLYYRHKVSPYVGRTIGGRVRATYLRGQCIYDDEQFIGAPKGQLL 442
|
|
| pyrC_multi |
TIGR00857 |
dihydroorotase, multifunctional complex type; In contrast to the homodimeric type of ... |
20-432 |
1.00e-73 |
|
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: 237.34 E-value: 1.00e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489524267 20 DLRIEDEKIVEIGNNLEINGDKVIDATGKIVIPGGIDTHTHFDMNAGSitTADNFETGTRAAIAGGTTTILDFaeANEGE 99
Cdd:TIGR00857 7 DILVEGGRIKKIGKLRIPPDAEVIDAKGLLVLPGFIDLHVHLRDPGEE--YKEDIESGSKAAAHGGFTTVADM--PNTKP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489524267 100 NLLQGVEAYHKKASGN--CYCDYGFHMTITCLNK-DTFNHMEKLISDGIVSfKMYMAYDGMKVDDGAIYRVLKKARDLGC 176
Cdd:TIGR00857 83 PIDTPETLEWKLQRLKkvSLVDVHLYGGVTQGNQgKELTEAYELKEAGAVG-RMFTDDGSEVQDILSMRRALEYAAIAGV 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489524267 177 IVEFHCENgdlLDVLIEENIQNGNLEPKYHPLTRPNIVEKESVSRLADITKLSNSKSYVVHLSCKESLETVKTAREKNID 256
Cdd:TIGR00857 162 PIALHAED---PDLIYGGVMHEGPSAAQLGLPARPPEAEEVAVARLLELAKHAGCPVHICHISTKESLELIVKAKSQGIK 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489524267 257 MIVETCPQYLLLednlyNKDKFEGAK--YVMSPPLRKKEDINYLWEGLASGDIQTVGTDHCSFNFKgQKDLGIDDfskIP 334
Cdd:TIGR00857 239 ITAEVTPHHLLL-----SEEDVARLDgnGKVNPPLREKEDRLALIEGLKDGIIDIIATDHAPHTLE-EKTKEFAA---AP 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489524267 335 NGAPGVEHRLALLYTyGVLENRISANKFVEVTSTNAAKIFGMyPKKGEIAVGSDADIVILNVNKEETISYKTQKQNVDYT 414
Cdd:TIGR00857 310 PGIPGLETALPLLLQ-LLVKGLISLKDLIRMLSINPARIFGL-PDKGTLEEGNPADITVFDLKKEWTINAETFYSKAKNT 387
|
410
....*....|....*...
gi 489524267 415 PYEGFKIKCKVEDVFLRG 432
Cdd:TIGR00857 388 PFEGMSLKGKPIATILRG 405
|
|
| pyrC |
PRK09357 |
dihydroorotase; Validated |
1-437 |
3.26e-70 |
|
dihydroorotase; Validated
Pssm-ID: 236479 [Multi-domain] Cd Length: 423 Bit Score: 228.54 E-value: 3.26e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489524267 1 MGTILRGGTIIT-SDKTYISDLRIEDEKIVEIGNNLEINGDKVIDATGKIVIPGGIDTHTHFDMNAGsiTTADNFETGTR 79
Cdd:PRK09357 1 MMILIKNGRVIDpKGLDEVADVLIDDGKIAAIGENIEAEGAEVIDATGLVVAPGLVDLHVHLREPGQ--EDKETIETGSR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489524267 80 AAIAGGTTTIldFAEANE---GENlLQGVEAYHKKASGNCYCD---YGfhmTITC-LNKDTFNHMEKLISDGIVSFkmym 152
Cdd:PRK09357 79 AAAAGGFTTV--VAMPNTkpvIDT-PEVVEYVLDRAKEAGLVDvlpVG---AITKgLAGEELTEFGALKEAGVVAF---- 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489524267 153 AYDGMKVDDGAI-YRVLKKARDLGCIVEFHCEngdlLDVLIEENIQNGNLEPKYHPLT-RPNIVEKESVSRLADITKLSN 230
Cdd:PRK09357 149 SDDGIPVQDARLmRRALEYAKALDLLIAQHCE----DPSLTEGGVMNEGEVSARLGLPgIPAVAEEVMIARDVLLAEATG 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489524267 231 SKSYVVHLSCKESLETVKTAREKNIDMIVETCPQYLLL-EDNLYNKDkfegAKYVMSPPLRKKEDINYLWEGLASGDIQT 309
Cdd:PRK09357 225 ARVHICHVSTAGSVELIRWAKALGIKVTAEVTPHHLLLtDEDLLTYD----PNYKVNPPLRTEEDREALIEGLKDGTIDA 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489524267 310 VGTDH---------CsfnfkgqkdlgidDFSKIPNGAPGVEHRLALLYTYGVLENRISANKFVEVTSTNAAKIFGMypKK 380
Cdd:PRK09357 301 IATDHaphareekeC-------------EFEAAPFGITGLETALSLLYTTLVKTGLLDLEQLLEKMTINPARILGL--PA 365
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*..
gi 489524267 381 GEIAVGSDADIVILNVNKEETISYKTQKQNVDYTPYEGFKIKCKVEDVFLRGNHVVQ 437
Cdd:PRK09357 366 GPLAEGEPADLVIFDPEAEWTVDGEDFASKGKNTPFIGMKLKGKVVYTIVDGKIVYQ 422
|
|
| DHOase_IIb |
cd01318 |
Dihydroorotase (DHOase), subgroup IIb; DHOases catalyze the reversible interconversion of ... |
47-432 |
7.39e-69 |
|
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: 223.37 E-value: 7.39e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489524267 47 GKIVIPGGIDTHTHFdmNAGSITTADNFETGTRAAIAGGTTTILDFAEANEGENLLQGVEAYHKKASGNCYCDYGFHMTI 126
Cdd:cd01318 1 GLLILPGVIDIHVHF--REPGLTYKEDFVSGSRAAAAGGVTTVMDMPNTKPPTTTAEALYEKLRLAAAKSVVDYGLYFGV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489524267 127 TclNKDTFNHMEKLisdGIVSFKMYMA--YDGMKVDDGAIYRVLKKARDLgciVEFHCENGDLldvlIEENiQNGNLEPK 204
Cdd:cd01318 79 T--GSEDLEELDKA---PPAGYKIFMGdsTGDLLDDEETLERIFAEGSVL---VTFHAEDEDR----LREN-RKELKGES 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489524267 205 YHPLTRPNIVEKESVSRLADITKLSNSKSYVVHLSCKEsleTVKTAREKNIDMIVETCPQYLLLEDNLYNKDkfeGAKYV 284
Cdd:cd01318 146 AHPRIRDAEAAAVATARALKLARRHGARLHICHVSTPE---ELKLIKKAKPGVTVEVTPHHLFLDVEDYDRL---GTLGK 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489524267 285 MSPPLRKKEDINYLWEGLASGDIQTVGTDHCSFNFKgQKDLGIDDfskIPNGAPGVEHRLALLYTYgVLENRISANKFVE 364
Cdd:cd01318 220 VNPPLRSREDRKALLQALADGRIDVIASDHAPHTLE-EKRKGYPA---APSGIPGVETALPLMLTL-VNKGILSLSRVVR 294
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 489524267 365 VTSTNAAKIFGMyPKKGEIAVGSDADIVILNVNKEETISYKTQKQNVDYTPYEGFKIKCKVEDVFLRG 432
Cdd:cd01318 295 LTSHNPARIFGI-KNKGRIAEGYDADLTVVDLKEERTIRAEEFHSKAGWTPFEGFEVTGFPVMTIVRG 361
|
|
| PRK02382 |
PRK02382 |
dihydroorotase; Provisional |
20-420 |
3.17e-65 |
|
dihydroorotase; Provisional
Pssm-ID: 179417 [Multi-domain] Cd Length: 443 Bit Score: 216.06 E-value: 3.17e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489524267 20 DLRIEDEKIVEIGNNLEI-NGDKVIDATGKIVIPGGIDTHTHF-DMNAgsiTTADNFETGTRAAIAGGTTTILDfaEANE 97
Cdd:PRK02382 21 DVRIDGGKITAVGKDLDGsSSEEVIDARGMLLLPGGIDVHVHFrEPGY---THKETWYTGSRSAAAGGVTTVVD--QPNT 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489524267 98 GENLLQGvEAYHKK---ASGNCYCDYGFHMTITclnkDTFNHMEKLISDGIVSF-KMYMA--YDGMKVDDGAIYRVLKKA 171
Cdd:PRK02382 96 DPPTVDG-ESFDEKaelAARKSIVDFGINGGVT----GNWDPLESLWERGVFALgEIFMAdsTGGMGIDEELFEEALAEA 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489524267 172 RDLGCIVEFHCENGDLLDVLIEEniQNGNLEPKYHPLTRPNIVEKESVSRLADITKLSNSKSYVVHLSCKESLETVKTAR 251
Cdd:PRK02382 171 ARLGVLATVHAEDEDLFDELAKL--LKGDADADAWSAYRPAAAEAAAVERALEVASETGARIHIAHISTPEGVDAARREG 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489524267 252 eknidMIVETCPQYLLLEDNLYNKDKFEGAkyvMSPPLRKKEDINYLWEGLASGDIQTVGTDHCSfNFKGQKDLGIDDfs 331
Cdd:PRK02382 249 -----ITCEVTPHHLFLSRRDWERLGTFGK---MNPPLRSEKRREALWERLNDGTIDVVASDHAP-HTREEKDADIWD-- 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489524267 332 kIPNGAPGVEHRLALLYtYGVLENRISANKFVEVTSTNAAKIFGMyPKKGEIAVGSDADIVILNVNKEETISYKTQKQNV 411
Cdd:PRK02382 318 -APSGVPGVETMLPLLL-AAVRKNRLPLERVRDVTAANPARIFGL-DGKGRIAEGYDADLVLVDPDAAREIRGDDLHSKA 394
|
....*....
gi 489524267 412 DYTPYEGFK 420
Cdd:PRK02382 395 GWTPFEGME 403
|
|
| PRK08044 |
PRK08044 |
allantoinase AllB; |
3-451 |
2.13e-62 |
|
allantoinase AllB;
Pssm-ID: 169193 [Multi-domain] Cd Length: 449 Bit Score: 208.94 E-value: 2.13e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489524267 3 TILRGGTIITSDKTYISDLRIEDEKIVEIGNNLEiNGDKVIDATGKIVIPGGIDTHTHFDMNAGsiTTADNFETGTRAAI 82
Cdd:PRK08044 5 LIIKNGTVILENEARVVDIAVKGGKIAAIGQDLG-DAKEVMDASGLVVSPGMVDAHTHISEPGR--SHWEGYETGTRAAA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489524267 83 AGGTTTILDF------AEANEgenllQGVEAYHKKASGNCYCDYGFHMTITCLNKDtfnHMEKLISDGIVSFKMYMAY-- 154
Cdd:PRK08044 82 KGGITTMIEMplnqlpATVDR-----ASIELKFDAAKGKLTIDAAQLGGLVSYNLD---RLHELDEVGVVGFKCFVATcg 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489524267 155 ------DGMKVDDGAIYRVLKKARDLGCIVEFHCENGDLLDVLIEENIQNGNLEPKYHPLTRPNIVEKESVSRLADITKL 228
Cdd:PRK08044 154 drgidnDFRDVNDWQFYKGAQKLGELGQPVLVHCENALICDELGEEAKREGRVTAHDYVASRPVFTEVEAIRRVLYLAKV 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489524267 229 SNSKSYVVHLSCKESLETVKTAREKNIDMIVETCPQYLLLEdnlynKDKFE--GAKYVMSPPLRKKEDINYLWEGLASGD 306
Cdd:PRK08044 234 AGCRLHVCHISSPEGVEEVTRARQEGQDVTCESCPHYFVLD-----TDQFEeiGTLAKCSPPIRDLENQKGMWEKLFNGE 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489524267 307 IQTVGTDH--CSfnfkgqKDLGIDDFSKIPNGAPGVEHRLALLYTYGVLENRISANKFVEVTSTNAAKIFGMyPKKGEIA 384
Cdd:PRK08044 309 IDCLVSDHspCP------PEMKAGNIMEAWGGIAGLQNCMDVMFDEAVQKRGMSLPMFGKLMATNAADIFGL-QQKGRIA 381
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 489524267 385 VGSDADIVILNVNKeetiSYKTQKQNVDY----TPYEGFKIKCKVEDVFLRGNHVV-QSCNVKEHPTGQYIK 451
Cdd:PRK08044 382 PGKDADFVFIQPNS----SYVLKNEDLEYrhkvSPYVGRTIGARITKTILRGDVIYdIEQGFPVAPKGQFIL 449
|
|
| DHOase_IIa |
cd01317 |
Dihydroorotase (DHOase), subgroup IIa; DHOases catalyze the reversible interconversion of ... |
39-428 |
2.67e-60 |
|
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: 201.31 E-value: 2.67e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489524267 39 GDKVIDATGKIVIPGGIDTHTHFDmNAGSiTTADNFETGTRAAIAGGTTTILDFAEAN---EGENLLQGVEAYHKKASGN 115
Cdd:cd01317 1 DAEVIDAEGKILAPGLVDLHVHLR-EPGF-EYKETLESGAKAAAAGGFTTVVCMPNTNpviDNPAVVELLKNRAKDVGIV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489524267 116 CYCDYGfHMTITCLNKDTFNhMEKLISDGIVSFkmymAYDG-MKVDDGAIYRVLKKARDLGCIVEFHCENGDLLDvlieE 194
Cdd:cd01317 79 RVLPIG-ALTKGLKGEELTE-IGELLEAGAVGF----SDDGkPIQDAELLRRALEYAAMLDLPIIVHPEDPSLAG----G 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489524267 195 NIQNGNLEPKYHPLT-RPNIVEKESVSRLADITKLSNSKSYVVHLSCKESLETVKTAREKNIDMIVETCPQYLLL-EDNL 272
Cdd:cd01317 149 GVMNEGKVASRLGLPgIPPEAETIMVARDLELAEATGARVHFQHLSTARSLELIRKAKAKGLPVTAEVTPHHLLLdDEAL 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489524267 273 YNKDkfegAKYVMSPPLRKKEDINYLWEGLASGDIQTVGTDHCSFNfKGQKDLgidDFSKIPNGAPGVEHRLALLYTYGV 352
Cdd:cd01317 229 ESYD----TNAKVNPPLRSEEDREALIEALKDGTIDAIASDHAPHT-DEEKDL---PFAEAPPGIIGLETALPLLWTLLV 300
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 489524267 353 LENRISANKFVEVTSTNAAKIFGMYPkkGEIAVGSDADIVILNVNKEETISYKTQKQNVDYTPYEGFKIKCKVEDV 428
Cdd:cd01317 301 KGGLLTLPDLIRALSTNPAKILGLPP--GRLEVGAPADLVLFDPDAEWIVDEETFRSKSKNTPFDGQKLKGRVLAT 374
|
|
| PRK09060 |
PRK09060 |
dihydroorotase; Validated |
3-451 |
4.70e-52 |
|
dihydroorotase; Validated
Pssm-ID: 181632 [Multi-domain] Cd Length: 444 Bit Score: 181.66 E-value: 4.70e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489524267 3 TILRGGTIITSDKTYISDLRIEDEKIVEIGNNLEINGDKVIDATGKIVIPGGIDTHTHFdMNAGSiTTADNFETGTRAAI 82
Cdd:PRK09060 7 LILKGGTVVNPDGEGRADIGIRDGRIAAIGDLSGASAGEVIDCRGLHVLPGVIDSQVHF-REPGL-EHKEDLETGSRAAV 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489524267 83 AGGTTTILDFAEANEgenLLQGVEAYHKK---ASGNCYCDYGFHMTITCLNKDTFNHMEKLisDGIVSFKMYMAY---DG 156
Cdd:PRK09060 85 LGGVTAVFEMPNTNP---LTTTAEALADKlarARHRMHCDFAFYVGGTRDNADELAELERL--PGCAGIKVFMGSstgDL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489524267 157 MKVDDGAIYRVLKKARDLgciVEFHCENGDLLD---VLIEENiqngnlEPKYHPLTRPNIVEKESVSRLADITKLSNSKS 233
Cdd:PRK09060 160 LVEDDEGLRRILRNGRRR---AAFHSEDEYRLRerkGLRVEG------DPSSHPVWRDEEAALLATRRLVRLARETGRRI 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489524267 234 YVVHLSCKESLETVKTARekniDMI-VETCPQYLlledNLYNKDKFE--GAKYVMSPPLRKKEDINYLWEGLASGDIQTV 310
Cdd:PRK09060 231 HVLHVSTAEEIDFLADHK----DVAtVEVTPHHL----TLAAPECYErlGTLAQMNPPIRDARHRDGLWRGVRQGVVDVL 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489524267 311 GTDHC--SFNFKGQKdlgiddFSKIPNGAPGVEHRLALLYTYgVLENRISANKFVEVTSTNAAKIFGMyPKKGEIAVGSD 388
Cdd:PRK09060 303 GSDHAphTLEEKAKP------YPASPSGMTGVQTLVPIMLDH-VNAGRLSLERFVDLTSAGPARIFGI-AGKGRIAVGYD 374
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 489524267 389 ADIVILNVNKEETISYKTQKQNVDYTPYEGFKIKCKVEDVFLRGNHVVQSCNVKEHPTGQYIK 451
Cdd:PRK09060 375 ADFTIVDLKRRETITNEWIASRCGWTPYDGKEVTGWPVGTIVRGQRVMWDGELVGPPTGEPVR 437
|
|
| PRK09236 |
PRK09236 |
dihydroorotase; Reviewed |
1-448 |
2.19e-47 |
|
dihydroorotase; Reviewed
Pssm-ID: 181716 Cd Length: 444 Bit Score: 168.90 E-value: 2.19e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489524267 1 MGTIL-RGGTIITSDKTYISDLRIEDEKIVEIGNNLE-INGDKVIDATGKIVIPGGIDTHTHFD----MNAGSIttadnf 74
Cdd:PRK09236 1 MKRILiKNARIVNEGKIFEGDVLIENGRIAKIASSISaKSADTVIDAAGRYLLPGMIDDQVHFRepglTHKGDI------ 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489524267 75 ETGTRAAIAGGTTTILDFAEANEGENLLQGVEAYHKKASGNCYCDYGFHMTITCLNKDTFNHMEKLISDGIvsfKMYM-A 153
Cdd:PRK09236 75 ASESRAAVAGGITSFMEMPNTNPPTTTLEALEAKYQIAAQRSLANYSFYFGATNDNLDEIKRLDPKRVCGV---KVFMgA 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489524267 154 YDG-MKVDDgaiYRVLKKA-RDLGCIVEFHCENGDLLDVLIEENIQ--NGNLEPKYHPLTRPNIVEKESVSRLADITKLS 229
Cdd:PRK09236 152 STGnMLVDN---PETLERIfRDAPTLIATHCEDTPTIKANLAKYKEkyGDDIPAEMHPLIRSAEACYKSSSLAVSLAKKH 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489524267 230 NSKSYVVHLS-CKE-SLETVKTAREKNIdmIVETCPQYLLLEDNLYNKdkfEGAKYVMSPPLRKKEDINYLWEGLASGDI 307
Cdd:PRK09236 229 GTRLHVLHIStAKElSLFENGPLAEKRI--TAEVCVHHLWFDDSDYAR---LGNLIKCNPAIKTASDREALRQALADDRI 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489524267 308 QTVGTDHCSFNFKgQKDLGiddFSKIPNGAPGVEHRL-ALLYTygVLENRISANKFVEVTSTNAAKIFGMyPKKGEIAVG 386
Cdd:PRK09236 304 DVIATDHAPHTWE-EKQGP---YFQAPSGLPLVQHALpALLEL--VHEGKLSLEKVVEKTSHAPAILFDI-KERGFIREG 376
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 489524267 387 SDADIVILNVNKEETISyktqKQNVDY----TPYEGFKIKCKVEDVFLRGNHVVQSCNVKEHPTGQ 448
Cdd:PRK09236 377 YWADLVLVDLNSPWTVT----KENILYkcgwSPFEGRTFRSRVATTFVNGQLVYHNGQLVESCRGQ 438
|
|
| PRK07575 |
PRK07575 |
dihydroorotase; Provisional |
1-418 |
9.85e-46 |
|
dihydroorotase; Provisional
Pssm-ID: 236055 [Multi-domain] Cd Length: 438 Bit Score: 164.46 E-value: 9.85e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489524267 1 MGTILRGGTIITSDKT-YISDLRIEDEKIVEIGNNLEING-DKVIDATGKIVIPGGIDTHTHFdmNAGSITTADNFETGT 78
Cdd:PRK07575 3 MSLLIRNARILLPSGElLLGDVLVEDGKIVAIAPEISATAvDTVIDAEGLTLLPGVIDPQVHF--REPGLEHKEDLFTAS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489524267 79 RAAIAGGTTTILDFAEANEgenLLQGVEAYHKK---ASGNCYCDYGFHMTITclnKDtfNHMEKLISDGIVSFKMYM--A 153
Cdd:PRK07575 81 RACAKGGVTSFLEMPNTKP---LTTTQAALDDKlarAAEKCVVNYGFFIGAT---PD--NLPELLTANPTCGIKIFMgsS 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489524267 154 YDGMKVDD-GAIYRVLKKARDLGCIvefHCENgdllDVLIEENIQ--NGNLEPKYHPLTRPNIVEKESVSRLADITKLSN 230
Cdd:PRK07575 153 HGPLLVDEeAALERIFAEGTRLIAV---HAED----QARIRARRAefAGISDPADHSQIQDEEAALLATRLALKLSKKYQ 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489524267 231 SKSYVVHLSCKESLETVKtaREKNIDMIVETCPQYLLLEDNLYNKdkfEGAKYVMSPPLRKKEDINYLWEGLASGDIQTV 310
Cdd:PRK07575 226 RRLHILHLSTAIEAELLR--QDKPSWVTAEVTPQHLLLNTDAYER---IGTLAQMNPPLRSPEDNEALWQALRDGVIDFI 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489524267 311 GTDHCSFNF--KGQkdlgidDFSKIPNGAPGVEHRLALLYTyGVLENRISANKFVEVTSTNAAKIFGMyPKKGEIAVGSD 388
Cdd:PRK07575 301 ATDHAPHTLeeKAQ------PYPNSPSGMPGVETSLPLMLT-AAMRGKCTVAQVVRWMSTAVARAYGI-PNKGRIAPGYD 372
|
410 420 430
....*....|....*....|....*....|
gi 489524267 389 ADIVILNVNKEETISYKTQKQNVDYTPYEG 418
Cdd:PRK07575 373 ADLVLVDLNTYRPVRREELLTKCGWSPFEG 402
|
|
| PLN02795 |
PLN02795 |
allantoinase |
3-453 |
2.87e-45 |
|
allantoinase
Pssm-ID: 178392 [Multi-domain] Cd Length: 505 Bit Score: 164.56 E-value: 2.87e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489524267 3 TILRGGTIITSDKTYISDLRIEDEKIVEIGNNLE----INGDKVIDATGKIVIPGGIDTHTHfdMNAGSITTADNFETGT 78
Cdd:PLN02795 46 FVLYSKRVVTPAGVIPGAVEVEGGRIVSVTKEEEapksQKKPHVLDYGNAVVMPGLIDVHVH--LNEPGRTEWEGFPTGT 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489524267 79 RAAIAGGTTTILD-----FAEANEGENLLQGVEAyhkkASGNCYCDYGFHMTITCLNKDTFNHMEKLISDGIVSFKMYMA 153
Cdd:PLN02795 124 KAAAAGGITTLVDmplnsFPSTTSVETLELKIEA----AKGKLYVDVGFWGGLVPENAHNASVLEELLDAGALGLKSFMC 199
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489524267 154 YDGMK----VDDGAIYRVLKKARDLGCIVEFHCENGDLLDvlIEENIQNGNLEPKYHPLTRPNIVEKESVSRLADITKLS 229
Cdd:PLN02795 200 PSGINdfpmTTATHIKAALPVLAKYGRPLLVHAEVVSPVE--SDSRLDADPRSYSTYLKSRPPSWEQEAIRQLLEVAKDT 277
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489524267 230 NSKS-------YVVHLS-CKESLETVKTAREKNIDMIVETCPQYLLLE-DNLYNKDkfegAKYVMSPPLRKKEDINYLWE 300
Cdd:PLN02795 278 RPGGvaegahvHIVHLSdAESSLELIKEAKAKGDSVTVETCPHYLAFSaEEIPDGD----TRYKCAPPIRDAANRELLWK 353
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489524267 301 GLASGDIQTVGTDHcSFNFKGQKDLGIDDFSKIPNGAPGVEHRLALLYTYGvLENRISANKFVEVTSTNAAKIFGMyPKK 380
Cdd:PLN02795 354 ALLDGDIDMLSSDH-SPSPPDLKLLEEGNFLRAWGGISSLQFVLPATWTAG-RAYGLTLEQLARWWSERPAKLAGL-DSK 430
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 489524267 381 GEIAVGSDADIVILNVNKEETI--SYKTQKQNVDYTPYEGFKIKCKVEDVFLRGNHVVQSCNVKEHPTGQYIKRK 453
Cdd:PLN02795 431 GAIAPGKDADIVVWDPEAEFVLdeSYPIYHKHKSLSPYLGTKLSGKVIATFVRGNLVFLEGKHAKQACGSPILAK 505
|
|
| PRK04250 |
PRK04250 |
dihydroorotase; Provisional |
23-450 |
4.89e-40 |
|
dihydroorotase; Provisional
Pssm-ID: 235265 [Multi-domain] Cd Length: 398 Bit Score: 147.99 E-value: 4.89e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489524267 23 IEDEKIVEIGNNlEINGDKVIDATGKIVIPGGIDTHTHF-DMNAGSITTadnFETGTRAAIAGGTTTILDFAEAN----E 97
Cdd:PRK04250 19 IENGRISKISLR-DLKGKEVIKVKGGIILPGLIDVHVHLrDFEESYKET---IESGTKAALHGGITLVFDMPNTKppimD 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489524267 98 GENLLQGVEAYHKKasgnCYCDYGFHMTITClnkdtfNHMEKlisdGIVSFKMYMAYDGMKVddGAIYrvLKKAR-DLGC 176
Cdd:PRK04250 95 EKTYEKRMRIAEKK----SYADYALNFLIAG------NCEKA----EEIKADFYKIFMGAST--GGIF--SENFEvDYAC 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489524267 177 ---IVEFHCEngdlldvliEENIQNGNLEpkyhpltRPNIVEKESVSRLADITKLSNSKSYVVHLSCKESLETVKtarEK 253
Cdd:PRK04250 157 apgIVSVHAE---------DPELIREFPE-------RPPEAEVVAIERALEAGKKLKKPLHICHISTKDGLKLIL---KS 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489524267 254 NIDMIV-ETCPQYLLLEDNLYNKDKFegakYVMSPPLRKKEDINYLWEGLASGDIqtVGTDHCSFNfkgqkdlgIDDFSK 332
Cdd:PRK04250 218 NLPWVSfEVTPHHLFLTRKDYERNPL----LKVYPPLRSEEDRKALWENFSKIPI--IASDHAPHT--------LEDKEA 283
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489524267 333 IPNGAPGVEHRLALLYtYGVLENRISANKFVEVTSTNAAKIFGMypKKGEIAVGSDADIVILNVNKEETISYKTQKQNVD 412
Cdd:PRK04250 284 GAAGIPGLETEVPLLL-DAANKGMISLFDIVEKMHDNPARIFGI--KNYGIEEGNYANFAVFDMKKEWTIKAEELYTKAG 360
|
410 420 430
....*....|....*....|....*....|....*...
gi 489524267 413 YTPYEGFKIKCKVEDVFLRGNHVVQSCNVKEHPTGQYI 450
Cdd:PRK04250 361 WTPYEGFKLKGKVIMTILRGEVVMEDDEIIGKPRGVRI 398
|
|
| PRK08417 |
PRK08417 |
metal-dependent hydrolase; |
21-432 |
3.39e-37 |
|
metal-dependent hydrolase;
Pssm-ID: 236262 [Multi-domain] Cd Length: 386 Bit Score: 140.22 E-value: 3.39e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489524267 21 LRIEDEKIVEIGNNLeiNGDKVIDATGKIVIPGGIDTHTHFdmnAGSITTADNFETGTRAAIAGGTTTIL---DFAEANE 97
Cdd:PRK08417 1 IRIKDGKITEIGSDL--KGEEILDAKGKTLLPALVDLNVSL---KNDSLSSKNLKSLENECLKGGVGSIVlypDSTPAID 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489524267 98 GENLLQGVEAYHKKASGNCycdygFHMTITCLNKDTFNHMEKLISDGIVSfkMYMAYDgmkVDDGAIYRVLKKARDLGCI 177
Cdd:PRK08417 76 NEIALELINSAQRELPMQI-----FPSIRALDEDGKLSNIATLLKKGAKA--LELSSD---LDANLLKVIAQYAKMLDVP 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489524267 178 VEFHCENGDLLDVLIeenIQNGNLEPKYHPLTRPNIVEKESVSRLADITKLSNSKSYVVHLSCKESLETVKTAREKNIDM 257
Cdd:PRK08417 146 IFCRCEDSSFDDSGV---MNDGELSFELGLPGIPSIAETKEVAKMKELAKFYKNKVLFDTLALPRSLELLDKFKSEGEKL 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489524267 258 IVETCPQYLLLEDNL---YNKdkfeGAKyvMSPPLRKKEDINYLWEGLASGDIQTVGTDHC-SFNFKgqKDLGIDDFSki 333
Cdd:PRK08417 223 LKEVSIHHLILDDSAcenFNT----AAK--LNPPLRSKEDRLALLEALKEGKIDFLTSLHSaKSNSK--KDLAFDEAA-- 292
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489524267 334 pNGAPGVEHRLALLYTYGVLENRISANKFVEVTSTNAAKIFGMypKKGEIAVGSDADIVILNVNKEETIsyktqkqNVDY 413
Cdd:PRK08417 293 -FGIDSICEYFSLCYTYLVKEGIITWSELSRFTSYNPAQFLGL--NSGEIEVGKEADLVLFDPNESTII-------DDNF 362
|
410
....*....|....*....
gi 489524267 414 TPYEGFKIKCKVEDVFLRG 432
Cdd:PRK08417 363 SLYSGDELYGKIEAVIIKG 381
|
|
| PRK01211 |
PRK01211 |
dihydroorotase; Provisional |
23-452 |
1.99e-32 |
|
dihydroorotase; Provisional
Pssm-ID: 179247 [Multi-domain] Cd Length: 409 Bit Score: 127.28 E-value: 1.99e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489524267 23 IEDEKIVEIGNNLEINGDKVIDAtgkIVIPGGIDTHTHFdmNAGSITTADNFETGTRAAIAGGTTTILDFAEANEGENLL 102
Cdd:PRK01211 20 VEDGKIKSIKKDAGNIGKKELKG---AILPAATDIHVHF--RTPGETEKEDFSTGTLSAIFGGTTFIMDMPNNNIPIKDY 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489524267 103 QGVEAYHKKASGNCYCDYGFHMTITCLNKdtfnhmeKLISDGIVSFKMYMA----YDGMKVDDGAIyrvlKKARDLGCIV 178
Cdd:PRK01211 95 NAFSDKLGRVAPKAYVDFSLYSMETGNNA-------LILDERSIGLKVYMGgttnTNGTDIEGGEI----KKINEANIPV 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489524267 179 EFHcenGDLLDVLIEENIQNGNLepKYHPLTRPNIVEKESVSRLADITKlsNSKsyvvHLSCKESLETVKtarekniDMI 258
Cdd:PRK01211 164 FFH---AELSECLRKHQFESKNL--RDHDLARPIECEIKAVKYVKNLDL--KTK----IIAHVSSIDVIG-------RFL 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489524267 259 VETCPQYLLLednlyNKDKFEGAKYVMSPPLRKKEDINYLWEGLASGDIQTVGTDHCSFNFKGQKDlgiddFSKIPNGAP 338
Cdd:PRK01211 226 REVTPHHLLL-----NDDMPLGSYGKVNPPLRDRWTQERLLEEYISGRFDILSSDHAPHTEEDKQE-----FEYAKSGII 295
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489524267 339 GVEHRLALlYTYGVLENRISANKFVEVTSTNAAKIFGMypKKGEIAVGSDADIVILNVNKEETISYKTQKQNVDYTPYEG 418
Cdd:PRK01211 296 GVETRVPL-FLALVKKKILPLDVLYKTAIERPASLFGI--KKGKIEEGYDADFMAFDFTNIKKINDKRLHSKCPVSPFNG 372
|
410 420 430
....*....|....*....|....*....|....
gi 489524267 419 FKIKCKvEDVFLRGNHVVQSCNVKEHPTGQYIKR 452
Cdd:PRK01211 373 FDAIFP-SHVIMRGEVVIDNYELISERTGKFVPK 405
|
|
| CAD_DHOase |
cd01316 |
The eukaryotic CAD protein is a trifunctional enzyme of carbamoylphosphate ... |
49-436 |
8.74e-32 |
|
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: 124.10 E-value: 8.74e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489524267 49 IVIPGGIDTHTHFDmNAGSITTADnFETGTRAAIAGGTTTILDFAEANEGENLLQGVEAYHKKASGNCYCDYGFHMTITC 128
Cdd:cd01316 3 IRLPGLIDVHVHLR-EPGATHKED-FASGTKAALAGGFTMVRAMPNTNPSIVDVASLKLVQSLAQAKARCDYAFSIGATS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489524267 129 LNKDTFNhmeKLISDGiVSFKMYM--AYDGMKVDDGAIYRvlkkardlgcivefhcengDLLDVLieeniqngnlepkyh 206
Cdd:cd01316 81 TNAATVG---ELASEA-VGLKFYLneTFSTLILDKITAWA-------------------SHFNAW--------------- 122
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489524267 207 PLTRPNIVEKESVSrLADI---TKLSNSKSYVVHLSCKESLETVKTAREKNIDMIVETCPQYLLLednlyNKDKFEGAKY 283
Cdd:cd01316 123 PSTKPIVTHAKSQT-LAAVlllASLHNRSIHICHVSSKEEINLIRLAKARGLKVTCEVSPHHLFL-----SQDDLPRGQY 196
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489524267 284 VMSPPLRKKEDINYLWEGLASGDIqtVGTDHCSFNFKGQKDlgiddfSKIPNGAPGVEHRLALLYTyGVLENRISANKFV 363
Cdd:cd01316 197 EVRPFLPTREDQEALWENLDYIDC--FATDHAPHTLAEKTG------NKPPPGFPGVETSLPLLLT-AVHEGRLTIEDIV 267
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 489524267 364 EVTSTNAAKIFGMYPkkgeiavgsDADIVI-LNVNKEETISYKTQKQNVDYTPYEGFKIKCKVEDVFLRGNHVV 436
Cdd:cd01316 268 DRLHTNPKRIFNLPP---------QSDTYVeVDLDEEWTIPKNPLQSKKGWTPFEGKKVKGKVQRVVLRGETAF 332
|
|
| Amidohydro_1 |
pfam01979 |
Amidohydrolase family; This family of enzymes are a a large metal dependent hydrolase ... |
49-414 |
1.88e-24 |
|
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: 103.35 E-value: 1.88e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489524267 49 IVIPGGIDTHTHFDMNAGSITT------ADNFETGTRAAIAGGTTTILDFaeaneGENLLQGVEAYhKKASGNCYCDYGF 122
Cdd:pfam01979 1 IVLPGLIDAHVHLEMGLLRGIPvppefaYEALRLGITTMLKSGTTTVLDM-----GATTSTGIEAL-LEAAEELPLGLRF 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489524267 123 HMTITCLNKD--------------TFNHMEKLISDGIVSFKMYMAYDGMKVDDGaIYRVLKKARDLGCIVEFHCENGDLL 188
Cdd:pfam01979 75 LGPGCSLDTDgelegrkalreklkAGAEFIKGMADGVVFVGLAPHGAPTFSDDE-LKAALEEAKKYGLPVAIHALETKGE 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489524267 189 DVLIEENIQNGnlepkyhpLTRPNIVEKESVSRLADITKLSNSKSyvVHLSCKESLETVKTAREKNIDMivetCPqylll 268
Cdd:pfam01979 154 VEDAIAAFGGG--------IEHGTHLEVAESGGLLDIIKLILAHG--VHLSPTEANLLAEHLKGAGVAH----CP----- 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489524267 269 ednlynkdkfegakyvmSPPLRKKEDINYLWEGLASGDIQTVGTDHCSFNFKGQKDLGIddfskipngapgvehRLALLy 348
Cdd:pfam01979 215 -----------------FSNSKLRSGRIALRKALEDGVKVGLGTDGAGSGNSLNMLEEL---------------RLALE- 261
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 489524267 349 TYGVLENRISANKFVEVTSTNAAKIFGMYPKKGEIAVGSDADIVILNVNKEETISYKTQKQNVDYT 414
Cdd:pfam01979 262 LQFDPEGGLSPLEALRMATINPAKALGLDDKVGSIEVGKDADLVVVDLDPLAAFFGLKPDGNVKKV 327
|
|
| pyrC |
PRK00369 |
dihydroorotase; Provisional |
14-432 |
3.21e-22 |
|
dihydroorotase; Provisional
Pssm-ID: 234738 [Multi-domain] Cd Length: 392 Bit Score: 97.91 E-value: 3.21e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489524267 14 DKTYISDLRIEDEkIVEIGNNLEIN-------GDKVIDAT-GKIVIPGGIDTHTHfdMNAGSITTADNFETGTRAAIAGG 85
Cdd:PRK00369 2 ILWIKGKAYLGKE-IKEICINFDRRikeiksrCKPDLDLPqGTLILPGAIDLHVH--LRGLKLSYKEDVASGTSEAAYGG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489524267 86 TTTILDFAEA----NEGENL---LQGVEAYHKkasgncyCDYGFHMTITclnkdtfNHMEKLISDGIVSFKMYmAYDGMK 158
Cdd:PRK00369 79 VTLVADMPNTipplNTPEAItekLAELEYYSR-------VDYFVYSGVT-------KDPEKVDKLPIAGYKIF-PEDLER 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489524267 159 VDdgaIYRVLKKARDLgciVEFHCENGDLLDVLieeniqngnlepkyHPLTRPNIVEKESVSRLADITKLsnsksYVVHL 238
Cdd:PRK00369 144 EE---TFRVLLKSRKL---KILHPEVPLALKSN--------------RKLRRNCWYEIAALYYVKDYQNV-----HITHA 198
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489524267 239 SCkesLETVKTAREknIDMIVETCPQYLLL--EDNLYNKdkfegakyvMSPPLRKKEDINYLWEGLASGDiqTVGTDHCS 316
Cdd:PRK00369 199 SN---PRTVRLAKE--LGFTVDITPHHLLVngEKDCLTK---------VNPPIRDINERLWLLQALSEVD--AIASDHAP 262
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489524267 317 fNFKGQKdlgIDDFSKIPNGAPGVEHRLALLYTYgVLENRISANKFVEVTSTNAAKIFGMypKKGEIAVGSDADIVILnv 396
Cdd:PRK00369 263 -HSSFEK---LQPYEVCPPGIAALSFTPPFIYTL-VSKGILSIDRAVELISTNPARILGI--PYGEIKEGYRANFTVI-- 333
|
410 420 430
....*....|....*....|....*....|....*.
gi 489524267 397 nKEETISYKTQKQNVDYTPYEGFKIKCKVEDVFLRG 432
Cdd:PRK00369 334 -QFEDWRYSTKYSKVIETPLDGFELKASVYATIVQG 368
|
|
| HutI |
COG1228 |
Imidazolonepropionase or related amidohydrolase [Secondary metabolites biosynthesis, transport ... |
3-404 |
1.77e-16 |
|
Imidazolonepropionase or related amidohydrolase [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 440841 [Multi-domain] Cd Length: 386 Bit Score: 80.78 E-value: 1.77e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489524267 3 TILRGGTIITSDKTYI---SDLRIEDEKIVEIGNNLEI---NGDKVIDATGKIVIPGGIDTHTH----------FDMNAG 66
Cdd:COG1228 10 LLITNATLVDGTGGGVienGTVLVEDGKIAAVGPAADLavpAGAEVIDATGKTVLPGLIDAHTHlglgggraveFEAGGG 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489524267 67 SITTADNFETGT---RAAIAGGTTTILD--------FAEANEGEN-LLQGVEAYhkkASGNC-YCDYGFHMTITclnKDT 133
Cdd:COG1228 90 ITPTVDLVNPADkrlRRALAAGVTTVRDlpggplglRDAIIAGESkLLPGPRVL---AAGPAlSLTGGAHARGP---EEA 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489524267 134 FNHMEKLISDGIVSFKMYMAYDGMKVDDGAIYRVLKKARDLGCIVEFHCENGDLLDVLIEENIQNgnlepkyhpltrpni 213
Cdd:COG1228 164 RAALRELLAEGADYIKVFAEGGAPDFSLEELRAILEAAHALGLPVAAHAHQADDIRLAVEAGVDS--------------- 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489524267 214 vekesvsrladitklsnsksyVVHLSCkesletvktAREKNIDMIVETCPQYLLLEDNLYNKDKFEGAKYVMSPPLRKKE 293
Cdd:COG1228 229 ---------------------IEHGTY---------LDDEVADLLAEAGTVVLVPTLSLFLALLEGAAAPVAAKARKVRE 278
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489524267 294 DINYLWEGLASGDIQTV-GTDHCSFNFKGQkDLgiddfskipngapgveHR-LALLYTYGvLENR--ISAnkfveVTStN 369
Cdd:COG1228 279 AALANARRLHDAGVPVAlGTDAGVGVPPGR-SL----------------HReLALAVEAG-LTPEeaLRA-----ATI-N 334
|
410 420 430
....*....|....*....|....*....|....*
gi 489524267 370 AAKIFGMYPKKGEIAVGSDADIVILNVNKEETISY 404
Cdd:COG1228 335 AAKALGLDDDVGSLEPGKLADLVLLDGDPLEDIAY 369
|
|
| D-aminoacylase |
cd01297 |
D-aminoacylases (N-acyl-D-Amino acid amidohydrolases) catalyze the hydrolysis of ... |
3-90 |
1.94e-16 |
|
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: 80.80 E-value: 1.94e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489524267 3 TILRGGTII--TSDKTYISDLRIEDEKIVEIGNNLEINGDKVIDATGKIVIPGGIDTHTHFDMNAGSITTAdnfetgtRA 80
Cdd:cd01297 2 LVIRNGTVVdgTGAPPFTADVGIRDGRIAAIGPILSTSAREVIDAAGLVVAPGFIDVHTHYDGQVFWDPDL-------RP 74
|
90
....*....|
gi 489524267 81 AIAGGTTTIL 90
Cdd:cd01297 75 SSRQGVTTVV 84
|
|
| metallo-dependent_hydrolases |
cd01292 |
Superfamily of metallo-dependent hydrolases (also called amidohydrolase superfamily) is a ... |
55-373 |
1.87e-15 |
|
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: 76.22 E-value: 1.87e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489524267 55 IDTHTHFDMNAGS----------------ITTADNFETGTRAAIAGGTTTILDFAEANEGENLLQGVEAYHKKASGNCYC 118
Cdd:cd01292 2 IDTHVHLDGSALRgtrlnlelkeaeelspEDLYEDTLRALEALLAGGVTTVVDMGSTPPPTTTKAAIEAVAEAARASAGI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489524267 119 DYGFHMTITCLNK----DTFNHMEKLISDG----IVSFKMYMAYDGMKVDDGAIYRVLKKARDLGCIVEFHCENGDlldv 190
Cdd:cd01292 82 RVVLGLGIPGVPAavdeDAEALLLELLRRGlelgAVGLKLAGPYTATGLSDESLRRVLEEARKLGLPVVIHAGELP---- 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489524267 191 lieeniqngnlepkyhpltrpniVEKESVSRLADITKLsNSKSYVVHLSCKESlETVKTAREKNIdmIVETCPQYllled 270
Cdd:cd01292 158 -----------------------DPTRALEDLVALLRL-GGRVVIGHVSHLDP-ELLELLKEAGV--SLEVCPLS----- 205
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489524267 271 NLYNKdkfegakyvmspplRKKEDINYLWEGLASGDIQTVGTDHCSFNFKGQkdlgiddfskipngaPGVEHRLALLYTY 350
Cdd:cd01292 206 NYLLG--------------RDGEGAEALRRLLELGIRVTLGTDGPPHPLGTD---------------LLALLRLLLKVLR 256
|
330 340
....*....|....*....|...
gi 489524267 351 GVLenriSANKFVEVTSTNAAKI 373
Cdd:cd01292 257 LGL----SLEEALRLATINPARA 275
|
|
| COG3653 |
COG3653 |
N-acyl-D-aspartate/D-glutamate deacylase [Secondary metabolites biosynthesis, transport and ... |
3-90 |
2.28e-15 |
|
N-acyl-D-aspartate/D-glutamate deacylase [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 442870 [Multi-domain] Cd Length: 528 Bit Score: 78.29 E-value: 2.28e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489524267 3 TILRGGTII--TSDKTYISDLRIEDEKIVEIGNNLEINGDKVIDATGKIVIPGGIDTHTHFDmnaGSITTADNFEtgtrA 80
Cdd:COG3653 4 LLIRGGTVVdgTGAPPFRADVAIKGGRIVAVGDLAAAEAARVIDATGLVVAPGFIDIHTHYD---LQLLWDPRLE----P 76
|
90
....*....|
gi 489524267 81 AIAGGTTTIL 90
Cdd:COG3653 77 SLRQGVTTVV 86
|
|
| SsnA |
COG0402 |
Cytosine/adenosine deaminase or related metal-dependent hydrolase [Nucleotide transport and ... |
3-93 |
2.33e-15 |
|
Cytosine/adenosine deaminase or related metal-dependent hydrolase [Nucleotide transport and metabolism, General function prediction only]; Cytosine/adenosine deaminase or related metal-dependent hydrolase is part of the Pathway/BioSystem: Pyrimidine salvage
Pssm-ID: 440171 [Multi-domain] Cd Length: 416 Bit Score: 77.56 E-value: 2.33e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489524267 3 TILRGGTIITSDK--TYISD--LRIEDEKIVEIGNNLEI----NGDKVIDATGKIVIPGGIDTHTHFDMNA--------- 65
Cdd:COG0402 2 LLIRGAWVLTMDPagGVLEDgaVLVEDGRIAAVGPGAELparyPAAEVIDAGGKLVLPGLVNTHTHLPQTLlrgladdlp 81
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 489524267 66 ------------GSITTADNFETGTRAAIA----GGTTTILDFA 93
Cdd:COG0402 82 lldwleeyiwplEARLDPEDVYAGALLALAemlrSGTTTVADFY 125
|
|
| PRK08204 |
PRK08204 |
hypothetical protein; Provisional |
3-91 |
4.18e-15 |
|
hypothetical protein; Provisional
Pssm-ID: 181288 [Multi-domain] Cd Length: 449 Bit Score: 76.96 E-value: 4.18e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489524267 3 TILRGGTIITSDKTyISDLR-----IEDEKIVEIGNNLEINGDKVIDATGKIVIPGGIDTHTH----------------- 60
Cdd:PRK08204 4 TLIRGGTVLTMDPA-IGDLPrgdilIEGDRIAAVAPSIEAPDAEVVDARGMIVMPGLVDTHRHtwqsvlrgigadwtlqt 82
|
90 100 110
....*....|....*....|....*....|....*....
gi 489524267 61 --FDM--NAGSITTADNFETGTRA----AIAGGTTTILD 91
Cdd:PRK08204 83 yfREIhgNLGPMFRPEDVYIANLLgaleALDAGVTTLLD 121
|
|
| ATZ_TRZ_like |
cd01298 |
TRZ/ATZ family contains enzymes from the atrazine degradation pathway and related hydrolases. ... |
3-91 |
1.19e-14 |
|
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: 75.32 E-value: 1.19e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489524267 3 TILRGGTIITSDKTYI---SDLRIEDEKIVEIGNNLE---INGDKVIDATGKIVIPGGIDTHTHFDMNAG---------- 66
Cdd:cd01298 1 ILIRNGTIVTTDPRRVledGDVLVEDGRIVAVGPALPlpaYPADEVIDAKGKVVMPGLVNTHTHLAMTLLrgladdlplm 80
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 489524267 67 -----------SITTADNFETGTRAAIA----GGTTTILD 91
Cdd:cd01298 81 ewlkdliwpleRLLTEEDVYLGALLALAemirSGTTTFAD 120
|
|
| PRK09059 |
PRK09059 |
dihydroorotase; Validated |
18-435 |
4.59e-14 |
|
dihydroorotase; Validated
Pssm-ID: 181631 [Multi-domain] Cd Length: 429 Bit Score: 73.92 E-value: 4.59e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489524267 18 ISDLRIEDEKIV----EIGNNLEINGDKVIDATGKIVIPGGIDTHTHF-DMNAGSITTadnFETGTRAAIAGGTTTILDF 92
Cdd:PRK09059 22 IGTVLIEDGVIVaagkGAGNQGAPEGAEIVDCAGKAVAPGLVDARVFVgEPGAEHRET---IASASRAAAAGGVTSIIMM 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489524267 93 AEANEGENLLQGVEAYHK----KASGNCY----CDYGFH---MTITCLNKDTfnhmeklisdGIVSFkmymaYDGMK-VD 160
Cdd:PRK09059 99 PDTDPVIDDVALVEFVKRtardTAIVNIHpaaaITKGLAgeeMTEFGLLRAA----------GAVAF-----TDGRRsVA 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489524267 161 DGAIYR-VLKKARDLGCIVEFHCENGDLldvlIEENIQNGNLEPKYHPLTR-PNIVEKESVSRLADITKLSNSKSYVVHL 238
Cdd:PRK09059 164 NTQVMRrALTYARDFDAVIVHETRDPDL----GGNGVMNEGLFASWLGLSGiPREAEVIPLERDLRLAALTRGRYHAAQI 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489524267 239 SCKESLETVKTAREKNIDMIVETCPQYLLLEDNlynkDKFEGAKYV-MSPPLRKKEDINYLWEGLASGDIQTVGTDHCSF 317
Cdd:PRK09059 240 SCAESAEALRRAKDRGLKVTAGVSINHLSLNEN----DIGEYRTFFkLSPPLRTEDDRVAMVEAVASGTIDIIVSSHDPQ 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489524267 318 NFKGqKDLgidDFSKIPNGAPGVEHRLAL---LYTYGvlenRISANKFVEVTSTNAAKIFGMypKKGEIAVGSDADIVIL 394
Cdd:PRK09059 316 DVDT-KRL---PFSEAAAGAIGLETLLAAalrLYHNG----EVPLLRLIEALSTRPAEIFGL--PAGTLKPGAPADIIVI 385
|
410 420 430 440
....*....|....*....|....*....|....*....|.
gi 489524267 395 NVNKEETISYKTQKQNVDYTPYEGFKIKCKVEDVFLRGNHV 435
Cdd:PRK09059 386 DLDEPWVVDPEDLKSRSKNTPFEEARFQGRVVRTIVAGKTV 426
|
|
| NagA |
COG1820 |
N-acetylglucosamine-6-phosphate deacetylase [Carbohydrate transport and metabolism]; |
4-90 |
7.29e-13 |
|
N-acetylglucosamine-6-phosphate deacetylase [Carbohydrate transport and metabolism];
Pssm-ID: 441425 [Multi-domain] Cd Length: 373 Bit Score: 69.74 E-value: 7.29e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489524267 4 ILRGGTIITSDKTYIS-DLRIEDEKIVEIGNNLEInGDKVIDATGKIVIPGGIDTHTH----FDMNAGsitTADNFETGT 78
Cdd:COG1820 1 AITNARIFTGDGVLEDgALLIEDGRIAAIGPGAEP-DAEVIDLGGGYLAPGFIDLHVHggggVDFMDG---TPEALRTIA 76
|
90
....*....|..
gi 489524267 79 RAAIAGGTTTIL 90
Cdd:COG1820 77 RAHARHGTTSFL 88
|
|
| PRK07228 |
PRK07228 |
5'-deoxyadenosine deaminase; |
1-121 |
3.57e-12 |
|
5'-deoxyadenosine deaminase;
Pssm-ID: 180895 [Multi-domain] Cd Length: 445 Bit Score: 68.10 E-value: 3.57e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489524267 1 MGTILRGGTIITSDKT---YISDLRIEDEKIVEIGNNLEING-DKVIDATGKIVIPGGIDTHTH---------------- 60
Cdd:PRK07228 1 MTILIKNAGIVTMNAKreiVDGDVLIEDDRIAAVGDRLDLEDyDDHIDATGKVVIPGLIQGHIHlcqtlfrgiaddlell 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 489524267 61 ---FD--------MNAGSITTADnfETGTRAAIAGGTTTILDFAEANEGENLLQGVEAYHKKA-SGNCYCDYG 121
Cdd:PRK07228 81 dwlKDriwpleaaHDAESMYYSA--LLGIGELIESGTTTIVDMESVHHTDSAFEAAGESGIRAvLGKVMMDYG 151
|
|
| NagA |
cd00854 |
N-acetylglucosamine-6-phosphate deacetylase, NagA, catalyzes the hydrolysis of the N-acetyl ... |
3-90 |
1.89e-11 |
|
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: 65.29 E-value: 1.89e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489524267 3 TILRGGTIITSDKTYISDLRIEDEKIVEIGNNLE-INGDKVIDATGKIVIPGGIDTHTH----FDMNAGsitTADNFETG 77
Cdd:cd00854 1 LIIKNARILTPGGLEDGAVLVEDGKIVAIGPEDElEEADEIIDLKGQYLVPGFIDIHIHggggADFMDG---TAEALKTI 77
|
90
....*....|...
gi 489524267 78 TRAAIAGGTTTIL 90
Cdd:cd00854 78 AEALAKHGTTSFL 90
|
|
| COG3964 |
COG3964 |
Predicted amidohydrolase [General function prediction only]; |
4-91 |
3.43e-11 |
|
Predicted amidohydrolase [General function prediction only];
Pssm-ID: 443164 [Multi-domain] Cd Length: 376 Bit Score: 64.42 E-value: 3.43e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489524267 4 ILRGGTII--TSDKTYISDLRIEDEKIVEIGNNLEI-NGDKVIDATGKIVIPGGIDTHTHfdmnagsittadNFETGTR- 79
Cdd:COG3964 3 LIKGGRVIdpANGIDGVMDIAIKDGKIAAVAKDIDAaEAKKVIDASGLYVTPGLIDLHTH------------VFPGGTDy 70
|
90
....*....|....*...
gi 489524267 80 ------AAIAGGTTTILD 91
Cdd:COG3964 71 gvdpdgVGVRSGVTTVVD 88
|
|
| PRK07369 |
PRK07369 |
dihydroorotase; Provisional |
18-425 |
9.85e-11 |
|
dihydroorotase; Provisional
Pssm-ID: 236002 [Multi-domain] Cd Length: 418 Bit Score: 63.47 E-value: 9.85e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489524267 18 ISDLRIEDEKIVEIGNNL-EINGD-KVIDATGKIVIPGGIDTHTHfdmnAGSITTAD--NFETGTRAAIAGGTTTILDFA 93
Cdd:PRK07369 21 IADVLIEDGKIQAIEPHIdPIPPDtQIIDASGLILGPGLVDLYSH----SGEPGFEEreTLASLAAAAAAGGFTRVAILP 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489524267 94 EANEGENLLQGVEAYHKKASGNC--YCDYGFHMTITCLNKDTFNHMEkLISDGIVSFKmymayDGMKVDD-GAIYRVLKK 170
Cdd:PRK07369 97 DTFPPLDNPATLARLQQQAQQIPpvQLHFWGALTLGGQGKQLTELAE-LAAAGVVGFT-----DGQPLENlALLRRLLEY 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489524267 171 ARDLGCIVEFHCENGDLLD--VLIEeniqnGNLEPKYHPLTRPNIVEKESVSRLADITKLSNSKSYVVHLSCKESLETVK 248
Cdd:PRK07369 171 LKPLGKPVALWPCDRSLAGngVMRE-----GLLALRLGLPGDPASAETTALAALLELVAAIGTPVHLMRISTARSVELIA 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489524267 249 TAREKNIDMIVETCPQYLLL-EDNLYNKD---KFEgakyvmsPPLRKKEDINYLWEGLASGDIQTVGTDHCSFNFKgQKD 324
Cdd:PRK07369 246 QAKARGLPITASTTWMHLLLdTEALASYDpnlRLD-------PPLGNPSDRQALIEGVRTGVIDAIAIDHAPYTYE-EKT 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489524267 325 LGiddFSKIPNGAPGVEHRLALLYTYGVLENRISANKFVEVTSTNAAKIFGMYPKKgeIAVGSDADIVILNVNKEETISY 404
Cdd:PRK07369 318 VA---FAEAPPGAIGLELALPLLWQNLVETGELSALQLWQALSTNPARCLGQEPPS--LAPGQPAELILFDPQKTWTVSA 392
|
410 420
....*....|....*....|.
gi 489524267 405 KTQKQNVDYTPYEGFKIKCKV 425
Cdd:PRK07369 393 QTLHSLSRNTPWLGQTLKGRV 413
|
|
| YtcJ |
COG1574 |
Predicted amidohydrolase YtcJ [General function prediction only]; |
3-104 |
1.63e-10 |
|
Predicted amidohydrolase YtcJ [General function prediction only];
Pssm-ID: 441182 [Multi-domain] Cd Length: 535 Bit Score: 62.89 E-value: 1.63e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489524267 3 TILRGGTIITSDK--TYISDLRIEDEKIVEIGNNLEI-----NGDKVIDATGKIVIPGGIDTHTHFDMNAGSITTADNFE 75
Cdd:COG1574 10 LLLTNGRIYTMDPaqPVAEAVAVRDGRIVAVGSDAEVralagPATEVIDLGGKTVLPGFIDAHVHLLGGGLALLGVDLSG 89
|
90 100
....*....|....*....|....*....
gi 489524267 76 TGTRAAIAggtTTILDFAEANEGENLLQG 104
Cdd:COG1574 90 ARSLDELL---ARLRAAAAELPPGEWILG 115
|
|
| PRK06038 |
PRK06038 |
N-ethylammeline chlorohydrolase; Provisional |
4-63 |
1.70e-10 |
|
N-ethylammeline chlorohydrolase; Provisional
Pssm-ID: 180363 [Multi-domain] Cd Length: 430 Bit Score: 62.85 E-value: 1.70e-10
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 489524267 4 ILRGGTIITSDKtyiSDLR-----IEDEKIVEIGNNLEINGDKVIDATGKIVIPGGIDTHTHFDM 63
Cdd:PRK06038 5 IIKNAYVLTMDA---GDLKkgsvvIEDGTITEVSESTPGDADTVIDAKGSVVMPGLVNTHTHAAM 66
|
|
| PRK08393 |
PRK08393 |
N-ethylammeline chlorohydrolase; Provisional |
1-63 |
2.00e-10 |
|
N-ethylammeline chlorohydrolase; Provisional
Pssm-ID: 181411 [Multi-domain] Cd Length: 424 Bit Score: 62.51 E-value: 2.00e-10
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 489524267 1 MGTILRGGTIITSDKTYI--SDLRIEDEKIVEIGNNLEINGDKVIDATGKIVIPGGIDTHTHFDM 63
Cdd:PRK08393 1 MSILIKNGYVIYGENLKVirADVLIEGNKIVEVKRNINKPADTVIDASGSVVSPGFINAHTHSPM 65
|
|
| PRK07627 |
PRK07627 |
dihydroorotase; Provisional |
1-436 |
2.47e-10 |
|
dihydroorotase; Provisional
Pssm-ID: 181059 [Multi-domain] Cd Length: 425 Bit Score: 62.00 E-value: 2.47e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489524267 1 MGTILRGGTII--TSDKTYISDLRIEDEKIVEIGNNLE-INGDKVIDATGKIVIPGGIDTHTHFdMNAGSITTAdNFETG 77
Cdd:PRK07627 1 MKIHIKGGRLIdpAAGTDRQADLYVAAGKIAAIGQAPAgFNADKTIDASGLIVCPGLVDLSARL-REPGYEYKA-TLESE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489524267 78 TRAAIAGGTTTI---------LDFAEANE-----GENLLQGvEAYHKKAsgncycdygfhMTITcLNKDTFNHMEKLISD 143
Cdd:PRK07627 79 MAAAVAGGVTSLvcppdtdpvLDEPGLVEmlkfrARNLNQA-HVYPLGA-----------LTVG-LKGEVLTEMVELTEA 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489524267 144 GIVSFKMYmayDGMKVDDGAIYRVLKKARDLGCIVEFHCEngdllDVLIEEN--IQNGNLEPKyhpLTRPNI-VEKESVs 220
Cdd:PRK07627 146 GCVGFSQA---NVPVVDTQVLLRALQYASTFGFTVWLRPL-----DAFLGRGgvAASGAVASR---LGLSGVpVAAETI- 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489524267 221 RLADITKLSNSKSYVVHL---SCKESLETVKTAREKNIDMIVETCPQYLLLEDNlynkD-KFEGAKYVMSPPLRKKEDIN 296
Cdd:PRK07627 214 ALHTIFELMRVTGARVHLarlSSAAGVALVRAAKAEGLPVTCDVGVNHVHLIDV----DiGYFDSQFRLDPPLRSQRDRE 289
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489524267 297 YLWEGLASGDIQTVGTDHCSfnfkgqkdlgIDD------FSKIPNGAPGVEHRLALLYTYGVlENRISANKFVEVTSTNA 370
Cdd:PRK07627 290 AIRAALADGTIDAICSDHTP----------VDDdekllpFAEATPGATGLELLLPLTLKWAD-EAKVPLARALARITSAP 358
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 489524267 371 AKIFGMypKKGEIAVGSDADIVILNVNKEETISYKTQKQNVDYTPYEGFKIKCKVEdVFLRGNHVV 436
Cdd:PRK07627 359 ARVLGL--PAGRLAEGAPADLCVFDPDAHWRVEPRALKSQGKNTPFLGYELPGRVR-ATLVAGQVA 421
|
|
| FwdA |
COG1229 |
Formylmethanofuran dehydrogenase subunit A [Energy production and conversion]; |
1-60 |
4.42e-10 |
|
Formylmethanofuran dehydrogenase subunit A [Energy production and conversion];
Pssm-ID: 440842 Cd Length: 554 Bit Score: 61.75 E-value: 4.42e-10
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 489524267 1 MGTILRGGTIItsDKTY-----ISDLRIEDEKIVEigNNLEINGDKVIDATGKIVIPGGIDTHTH 60
Cdd:COG1229 1 MELIIKNGRVY--DPANgidgeVMDIAIKDGKIVE--EPSDPKDAKVIDASGKVVMAGGVDIHTH 61
|
|
| PRK09237 |
PRK09237 |
amidohydrolase/deacetylase family metallohydrolase; |
4-91 |
9.80e-10 |
|
amidohydrolase/deacetylase family metallohydrolase;
Pssm-ID: 236423 [Multi-domain] Cd Length: 380 Bit Score: 60.25 E-value: 9.80e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489524267 4 ILRGGTIITSDKTY--ISDLRIEDEKIVEIGNNLEI-NGDKVIDATGKIVIPGGIDTHTHfdmnagsittadNFETGT-- 78
Cdd:PRK09237 2 LLRGGRVIDPANGIdgVIDIAIEDGKIAAVAGDIDGsQAKKVIDLSGLYVSPGWIDLHVH------------VYPGSTpy 69
|
90
....*....|....*...
gi 489524267 79 -----RAAIAGGTTTILD 91
Cdd:PRK09237 70 gdepdEVGVRSGVTTVVD 87
|
|
| Met_dep_hydrolase_C |
cd01309 |
Metallo-dependent hydrolases, subgroup C is part of the superfamily of metallo-dependent ... |
25-407 |
5.39e-09 |
|
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: 57.71 E-value: 5.39e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489524267 25 DEKIVEIGNNLEINGD-KVIDATGKIVIPGGIDTHTHFDMN---AGSITTADNFETGT-----RA-------------AI 82
Cdd:cd01309 1 DGKIVAVGAEITTPADaEVIDAKGKHVTPGLIDAHSHLGLDeegGVRETSDANEETDPvtphvRAidginpddeafkrAR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489524267 83 AGGTTTILdfaeANEGENLLQGveayhkkasgncycdyGFHMTITCLNKDTfnhMEKLIsDGIVSFKMYMAYDGMKVDDG 162
Cdd:cd01309 81 AGGVTTVQ----VLPGSANLIG----------------GQGVVIKTDGGTI---EDMFI-KAPAGLKMALGENPKRVYGG 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489524267 163 aiyRVLKKARDLGcivefhcENGDLLDVLIE-----ENIQNGNLEPKYHPLTRPnivEKESVSRLADitklsnsKSYVVH 237
Cdd:cd01309 137 ---KGKEPATRMG-------VAALLRDAFIKaqeygRKYDLGKNAKKDPPERDL---KLEALLPVLK-------GEIPVR 196
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489524267 238 LSC---KESLETVKTAREKNIDMIVETCPQYLLLEDNLynkdKFEGAKYVMSPPL---RKKEDINYLWEG----LASGDI 307
Cdd:cd01309 197 IHAhraDDILTAIRIAKEFGIKITIEHGAEGYKLADEL----AKHGIPVIYGPTLtlpKKVEEVNDAIDTnaylLKKGGV 272
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489524267 308 QTVG-TDHcsfNFKGQKDLgiddfskipNGAPGVEHRLALLYTygvlenriSANKFVevtSTNAAKIFGMYPKKGEIAVG 386
Cdd:cd01309 273 AFAIsSDH---PVLNIRNL---------NLEAAKAVKYGLSYE--------EALKAI---TINPAKILGIEDRVGSLEPG 329
|
410 420
....*....|....*....|.
gi 489524267 387 SDADIVILNVNKEETISYKTQ 407
Cdd:cd01309 330 KDADLVVWNGDPLEPTSKPEQ 350
|
|
| PRK06380 |
PRK06380 |
metal-dependent hydrolase; Provisional |
1-65 |
2.25e-08 |
|
metal-dependent hydrolase; Provisional
Pssm-ID: 180548 [Multi-domain] Cd Length: 418 Bit Score: 56.05 E-value: 2.25e-08
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 489524267 1 MGTILRGGTIITSD---KTYISDLRIEDEKIVEIGNnLEINGDKVIDATGKIVIPGGIDTHTHFDMNA 65
Cdd:PRK06380 1 MSILIKNAWIVTQNekrEILQGNVYIEGNKIVYVGD-VNEEADYIIDATGKVVMPGLINTHAHVGMTA 67
|
|
| AdeC |
COG1001 |
Adenine deaminase [Nucleotide transport and metabolism]; |
3-89 |
3.99e-08 |
|
Adenine deaminase [Nucleotide transport and metabolism];
Pssm-ID: 440625 [Multi-domain] Cd Length: 559 Bit Score: 55.49 E-value: 3.99e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489524267 3 TILRGGTII--TSDKTYISDLRIEDEKIVEIGNnLEINGDKVIDATGKIVIPGGIDTHTHFDmnaGSITTADNFEtgtRA 80
Cdd:COG1001 7 LVIKNGRLVnvFTGEILEGDIAIAGGRIAGVGD-YIGEATEVIDAAGRYLVPGFIDGHVHIE---SSMVTPAEFA---RA 79
|
....*....
gi 489524267 81 AIAGGTTTI 89
Cdd:COG1001 80 VLPHGTTTV 88
|
|
| Met_dep_hydrolase_B |
cd01307 |
Metallo-dependent hydrolases, subgroup B is part of the superfamily of metallo-dependent ... |
20-402 |
4.64e-08 |
|
Metallo-dependent hydrolases, subgroup B is part of the superfamily of metallo-dependent hydrolases, a large group of proteins that show conservation in their 3-dimensional fold (TIM barrel) and in details of their active site. The vast majority of the members have a conserved metal binding site, involving four histidines and one aspartic acid residue. In the common reaction mechanism, the metal ion (or ions) deprotonate a water molecule for a nucleophilic attack on the substrate. The function of this subgroup is unknown.
Pssm-ID: 238632 [Multi-domain] Cd Length: 338 Bit Score: 54.64 E-value: 4.64e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489524267 20 DLRIEDEKIVEIGNNLEINGDK-VIDATGKIVIPGGIDTHTH--FDMNAGSItTADnfetgtRAAIAGGTTTILDfaean 96
Cdd:cd01307 1 DVAIENGKIAAVGAALAAPAATqIVDAGGCYVSPGWIDLHVHvyQGGTRYGD-RPD------MIGVKSGVTTVVD----- 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489524267 97 egenllqgveayhkkaSGNCYCD--YGFHMTITCLNKDTFNHMEKLISDGIVSFKMYmaYDGMKVDDGAIYRVLKKARDL 174
Cdd:cd01307 69 ----------------AGSAGADniDGFRYTVIERSATRVYAFLNISRVGLVAQDEL--PDPDNIDEDAVVAAAREYPDV 130
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489524267 175 GCIVEFH------CENGdlLDVL-IEENIQNGNLEPKYHPLTRPNIVEKESVSRL--ADI-TKLSNSKSyvvhlsckesl 244
Cdd:cd01307 131 IVGLKARasksvvGEWG--IKPLeLAKKIAKEADLPLMVHIGSPPPILDEVVPLLrrGDVlTHCFNGKP----------- 197
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489524267 245 etvktareknidmivetcpqylllednlynkdkfegakyvmSPPLRKKEDI-NYLWEGLASGDIQTVGTDHCSFNFKGQK 323
Cdd:cd01307 198 -----------------------------------------NGIVDEEGEVlPLVRRARERGVIFDVGHGTASFSFRVAR 236
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489524267 324 ---DLGIDDFS-------------KIPNGAPGVEHRLALLYTygvLENRISAnkfveVTsTNAAKIFGMyPKKGEIAVGS 387
Cdd:cd01307 237 aaiAAGLLPDTissdihgrnrtngPVYALATTLSKLLALGMP---LEEVIEA-----VT-ANPARMLGL-AEIGTLAVGY 306
|
410
....*....|....*
gi 489524267 388 DADIVILNVNKEETI 402
Cdd:cd01307 307 DADLTVFDLKDGRVE 321
|
|
| FMDH_A |
cd01304 |
Formylmethanofuran dehydrogenase (FMDH) subunit A; Methanogenic bacteria and archea derive ... |
20-71 |
1.00e-07 |
|
Formylmethanofuran dehydrogenase (FMDH) subunit A; Methanogenic bacteria and archea derive the energy for autotrophic growth from methanogenesis, the reduction of CO2 with molecular hydrogen as the electron donor. FMDH catalyzes the first step in methanogenesis, the formyl-methanofuran synthesis. In this step, CO2 is bound to methanofuran and subsequently reduced to the formyl state with electrons derived from hydrogen.
Pssm-ID: 238629 [Multi-domain] Cd Length: 541 Bit Score: 54.34 E-value: 1.00e-07
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 489524267 20 DLRIEDEKIVEIGNNLEinGDKVIDATGKIVIPGGIDTHTHFdmnAGSITTA 71
Cdd:cd01304 19 DIFIRDGKIVESSSGAK--PAKVIDASGKVVMAGGVDMHSHI---AGGKVNV 65
|
|
| PRK09061 |
PRK09061 |
D-glutamate deacylase; Validated |
1-60 |
1.47e-07 |
|
D-glutamate deacylase; Validated
Pssm-ID: 236369 [Multi-domain] Cd Length: 509 Bit Score: 53.55 E-value: 1.47e-07
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 489524267 1 MGTILRGGTII--TSDKTYISDLRIEDEKIVEIGNNLeINGDKVIDATGKIVIPGGIDTHTH 60
Cdd:PRK09061 19 YDLVIRNGRVVdpETGLDAVRDVGIKGGKIAAVGTAA-IEGDRTIDATGLVVAPGFIDLHAH 79
|
|
| Bact_CD |
cd01293 |
Bacterial cytosine deaminase and related metal-dependent hydrolases. Cytosine deaminases (CDs) ... |
20-62 |
1.52e-07 |
|
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: 53.40 E-value: 1.52e-07
10 20 30 40
....*....|....*....|....*....|....*....|....
gi 489524267 20 DLRIEDEKIVEIGNNLEINGDK-VIDATGKIVIPGGIDTHTHFD 62
Cdd:cd01293 16 DIAIEDGRIAAIGPALAVPPDAeEVDAKGRLVLPAFVDPHIHLD 59
|
|
| Imidazolone-5PH |
cd01296 |
Imidazolonepropionase/imidazolone-5-propionate hydrolase (Imidazolone-5PH) catalyzes the third ... |
23-99 |
2.63e-07 |
|
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: 52.65 E-value: 2.63e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489524267 23 IEDEKIVEIGN-----NLEINGDKVIDATGKIVIPGGIDTHTHFdMNAGSitTADNFE---TGT---RAAIAGG--TTTI 89
Cdd:cd01296 3 IRDGRIAAVGPaaslpAPGPAAAEEIDAGGRAVTPGLVDCHTHL-VFAGD--RVDEFAarlAGAsyeEILAAGGgiLSTV 79
|
90
....*....|
gi 489524267 90 LDFAEANEGE 99
Cdd:cd01296 80 RATRAASEDE 89
|
|
| PRK15446 |
PRK15446 |
phosphonate metabolism protein PhnM; Provisional |
1-91 |
1.26e-06 |
|
phosphonate metabolism protein PhnM; Provisional
Pssm-ID: 237967 [Multi-domain] Cd Length: 383 Bit Score: 50.18 E-value: 1.26e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489524267 1 MGTILRGGTIITSDKTYISDLRIEDEKIVEIGNNLEINGDkVIDATGKIVIPGGIDTHT-------------HFDMNAGs 67
Cdd:PRK15446 2 MEMILSNARLVLPDEVVDGSLLIEDGRIAAIDPGASALPG-AIDAEGDYLLPGLVDLHTdnlekhlaprpgvDWPADAA- 79
|
90 100
....*....|....*....|....
gi 489524267 68 ITTADnfetgtRAAIAGGTTTILD 91
Cdd:PRK15446 80 LAAHD------AQLAAAGITTVFD 97
|
|
| PRK07203 |
PRK07203 |
putative aminohydrolase SsnA; |
4-61 |
1.69e-06 |
|
putative aminohydrolase SsnA;
Pssm-ID: 235963 [Multi-domain] Cd Length: 442 Bit Score: 50.32 E-value: 1.69e-06
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 489524267 4 ILRGGTIITSDKT--YISD--LRIEDEKIVEIGNNLEINGD----KVIDATGKIVIPGGIDTHTHF 61
Cdd:PRK07203 3 LIGNGTAITRDPAkpVIEDgaIAIEGNVIVEIGTTDELKAKypdaEFIDAKGKLIMPGLINSHNHI 68
|
|
| ureC |
PRK13308 |
urease subunit alpha; Reviewed |
20-90 |
6.67e-06 |
|
urease subunit alpha; Reviewed
Pssm-ID: 183965 [Multi-domain] Cd Length: 569 Bit Score: 48.55 E-value: 6.67e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489524267 20 DLRIEDEKIVEIGN--NLEI-----------NGDKVIDATGKIVIPGGIDTHTHFDmnagsitTADNFEtgtrAAIAGGT 86
Cdd:PRK13308 88 DIGIRDGRIVGIGKagNPDImdgvdprlvvgPGTDVRPAEGLIATPGAIDVHVHFD-------SAQLVD----HALASGI 156
|
....
gi 489524267 87 TTIL 90
Cdd:PRK13308 157 TTML 160
|
|
| Met_dep_hydrolase_A |
cd01299 |
Metallo-dependent hydrolases, subgroup A is part of the superfamily of metallo-dependent ... |
40-91 |
1.04e-05 |
|
Metallo-dependent hydrolases, subgroup A 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: 238624 [Multi-domain] Cd Length: 342 Bit Score: 47.29 E-value: 1.04e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 489524267 40 DKVIDATGKIVIPGGIDTHTHFDMNAGSITTADNFETGTRAAIAG---------GTTTILD 91
Cdd:cd01299 1 AQVIDLGGKTLMPGLIDAHTHLGSDPGDLPLDLALPVEYRTIRATrqaraalraGFTTVRD 61
|
|
| PRK12393 |
PRK12393 |
amidohydrolase; Provisional |
20-60 |
1.09e-05 |
|
amidohydrolase; Provisional
Pssm-ID: 237088 [Multi-domain] Cd Length: 457 Bit Score: 47.75 E-value: 1.09e-05
10 20 30 40
....*....|....*....|....*....|....*....|.
gi 489524267 20 DLRIEDEKIVEIGNNLEINGDKVIDATGKIVIPGGIDTHTH 60
Cdd:PRK12393 27 DIRIRDGRIAAIGALTPLPGERVIDATDCVVYPGWVNTHHH 67
|
|
| PRK12394 |
PRK12394 |
metallo-dependent hydrolase; |
1-92 |
1.34e-05 |
|
metallo-dependent hydrolase;
Pssm-ID: 183497 [Multi-domain] Cd Length: 379 Bit Score: 47.06 E-value: 1.34e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489524267 1 MGTILRGGTII--TSDKTYISDLRIEDEKIVEIGNNLEINGDKVIDATGKIVIPGGIDTHTH--FDMNAGSIT-TADNFE 75
Cdd:PRK12394 3 NDILITNGHIIdpARNINEINNLRIINDIIVDADKYPVASETRIIHADGCIVTPGLIDYHAHvfYDGTEGGVRpDMYMPP 82
|
90
....*....|....*..
gi 489524267 76 TGTRAAIAGGTTTILDF 92
Cdd:PRK12394 83 NGVTTVVDAGSAGTANF 99
|
|
| PRK08203 |
PRK08203 |
hydroxydechloroatrazine ethylaminohydrolase; Reviewed |
20-80 |
1.36e-05 |
|
hydroxydechloroatrazine ethylaminohydrolase; Reviewed
Pssm-ID: 236184 [Multi-domain] Cd Length: 451 Bit Score: 47.15 E-value: 1.36e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 489524267 20 DLRIEDEKIVEIGNNLEI--NGDKVIDATGKIVIPGGIDTHTHFdmnagsittadnFETGTRA 80
Cdd:PRK08203 25 GLVVEGGRIVEVGPGGALpqPADEVFDARGHVVTPGLVNTHHHF------------YQTLTRA 75
|
|
| YtcJ_like |
cd01300 |
YtcJ_like metal dependent amidohydrolases. YtcJ is a Bacillus subtilis ORF of unknown function. ... |
23-63 |
1.58e-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: 47.30 E-value: 1.58e-05
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 489524267 23 IEDEKIVEIGNNLEI-----NGDKVIDATGKIVIPGGIDTHTHFDM 63
Cdd:cd01300 4 VRDGRIVAVGSDAEAkalkgPATEVIDLKGKTVLPGFIDSHSHLLL 49
|
|
| Isoaspartyl-dipeptidase |
cd01308 |
Isoaspartyl dipeptidase hydrolyzes the beta-L-isoaspartyl linkages in dipeptides, as part of ... |
3-395 |
1.80e-05 |
|
Isoaspartyl dipeptidase hydrolyzes the beta-L-isoaspartyl linkages in dipeptides, as part of the degradative pathway to eliminate proteins with beta-L-isoaspartyl peptide bonds, bonds whereby the beta-group of an aspartate forms the peptide link with the amino group of the following amino acid. Formation of this bond is a spontaneous nonenzymatic reaction in nature and can profoundly effect the function of the protein. Isoaspartyl dipeptidase is an octameric enzyme that contains a binuclear zinc center in the active site of each subunit and shows a strong preference of hydrolyzing Asp-Leu dipeptides.
Pssm-ID: 238633 [Multi-domain] Cd Length: 387 Bit Score: 46.61 E-value: 1.80e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489524267 3 TILRGGTIITSDKTYISDLRIEDEKIVEIGNNLEING---DKVIDATGKIVIPGGIDTHTHFDMNAGsittadnfETG-- 77
Cdd:cd01308 2 TLIKNAEVYAPEYLGKKDILIAGGKILAIEDQLNLPGyenVTVVDLHGKILVPGFIDQHVHIIGGGG--------EGGps 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489524267 78 TRA-------AIAGGTTTIldfaeanegenllqgveayhkkasgncycdygfhmtITCLNKD-TFNHMEKLIS------- 142
Cdd:cd01308 74 TRTpevtlsdLTTAGVTTV------------------------------------VGCLGTDgISRSMEDLLAkaralee 117
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489524267 143 DGIVSFKMYMAYDgmkVDDGAIYRVLKKardlgcivefhcengDLLdvLIEENIQNGNLEPKYHPLTRPNIVEKESVSRL 222
Cdd:cd01308 118 EGITCFVYTGSYE---VPTRTITGSIRK---------------DLL--LIDKVIGVGEIAISDHRSSQPTVEELARIAAE 177
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489524267 223 ADITKLSNSKSYVVHLSCKESLETVKTareknIDMIVETC--PQYLLLEDNL-YNKDKFEGA------------------ 281
Cdd:cd01308 178 ARVGGLLGGKAGIVHIHLGDGKRALSP-----IFELIEETeiPITQFLPTHInRTAPLFEQGvefakmggtidltssidp 252
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489524267 282 KYVMSPPLRKKEDINYLWEglasgdiQTVGTDHCSFNFKGQKDLGIDDFSK--IPNGAPGVEHRLALLYTyGVLENRISA 359
Cdd:cd01308 253 QFRKEGEVRPSEALKRLLE-------QGVPLERITFSSDGNGSLPKFDENGnlVGLGVGSVDTLLREVRE-AVKCGDIPL 324
|
410 420 430
....*....|....*....|....*....|....*.
gi 489524267 360 NKFVEVTSTNAAKIFGMYpKKGEIAVGSDADIVILN 395
Cdd:cd01308 325 EVALRVITSNVARILKLR-KKGEIQPGFDADLVILD 359
|
|
| Amidohydro_3 |
pfam07969 |
Amidohydrolase family; |
41-62 |
4.22e-05 |
|
Amidohydrolase family;
Pssm-ID: 400360 [Multi-domain] Cd Length: 464 Bit Score: 45.60 E-value: 4.22e-05
|
| Urease_alpha |
cd00375 |
Urease alpha-subunit; Urease is a nickel-dependent metalloenzyme that catalyzes the hydrolysis ... |
3-86 |
9.73e-05 |
|
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: 44.63 E-value: 9.73e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489524267 3 TILRGGTIITSDKTYISDLRIEDEKIVEIGN--NLEI-----------NGDKVIDATGKIVIPGGIDTHTHFdMNAGSIT 69
Cdd:cd00375 67 LVITNALIIDYTGIYKADIGIKDGRIVAIGKagNPDImdgvtpnmivgPSTEVIAGEGKIVTAGGIDTHVHF-ICPQQIE 145
|
90
....*....|....*..
gi 489524267 70 TAdnFETGTRAAIAGGT 86
Cdd:cd00375 146 EA--LASGITTMIGGGT 160
|
|
| PRK07572 |
PRK07572 |
cytosine deaminase; Validated |
1-62 |
1.51e-04 |
|
cytosine deaminase; Validated
Pssm-ID: 181039 Cd Length: 426 Bit Score: 43.85 E-value: 1.51e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 489524267 1 MGTILRGGTIitSDKTYISDLRIEDEKIVEIGNNLEINGDKVIDATGKIVIPGGIDTHTHFD 62
Cdd:PRK07572 2 FDLIVRNANL--PDGRTGIDIGIAGGRIAAVEPGLQAEAAEEIDAAGRLVSPPFVDPHFHMD 61
|
|
| ureC |
PRK13207 |
urease subunit alpha; Reviewed |
9-90 |
1.70e-04 |
|
urease subunit alpha; Reviewed
Pssm-ID: 237305 [Multi-domain] Cd Length: 568 Bit Score: 44.01 E-value: 1.70e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489524267 9 TIITS----DKTYI--SDLRIEDEKIVEIG--------NNLEI---NGDKVIDATGKIVIPGGIDTHTHFdmnagsiTTA 71
Cdd:PRK13207 69 TVITNalilDHWGIvkADIGIKDGRIVAIGkagnpdiqDGVDIiigPGTEVIAGEGLIVTAGGIDTHIHF-------ICP 141
|
90
....*....|....*....
gi 489524267 72 DNFETgtraAIAGGTTTIL 90
Cdd:PRK13207 142 QQIEE----ALASGVTTMI 156
|
|
| PRK05985 |
PRK05985 |
cytosine deaminase; Provisional |
20-62 |
2.43e-04 |
|
cytosine deaminase; Provisional
Pssm-ID: 180337 [Multi-domain] Cd Length: 391 Bit Score: 43.38 E-value: 2.43e-04
10 20 30 40
....*....|....*....|....*....|....*....|....
gi 489524267 20 DLRIEDEKIVEIGNNLEIN-GDKVIDATGKIVIPGGIDTHTHFD 62
Cdd:PRK05985 18 DILIRDGRIAAIGPALAAPpGAEVEDGGGALALPGLVDGHIHLD 61
|
|
| AdeC |
cd01295 |
Adenine deaminase (AdeC) directly deaminates adenine to form hypoxanthine. This reaction is ... |
44-89 |
3.41e-04 |
|
Adenine deaminase (AdeC) directly deaminates adenine to form hypoxanthine. This reaction is part of one of the adenine salvage pathways, as well as the degradation pathway. It is important for adenine utilization as a purine, as well as a nitrogen source in bacteria and archea.
Pssm-ID: 238620 [Multi-domain] Cd Length: 422 Bit Score: 42.98 E-value: 3.41e-04
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 489524267 44 DATGKIVIPGGIDTHTHFDMnagSITTADNFEtgtRAAIAGGTTTI 89
Cdd:cd01295 1 DAEGKYIVPGFIDAHLHIES---SMLTPSEFA---KAVLPHGTTTV 40
|
|
| ureB |
PRK13985 |
urease subunit alpha; |
4-86 |
3.92e-04 |
|
urease subunit alpha;
Pssm-ID: 184438 [Multi-domain] Cd Length: 568 Bit Score: 42.96 E-value: 3.92e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489524267 4 ILRGGTIITSDKTYISDLRIEDEKIVEIG------------NNLEIN-GDKVIDATGKIVIPGGIDTHTHFdMNAGSITT 70
Cdd:PRK13985 68 IITNALIIDYTGIYKADIGIKDGKIAGIGkggnkdmqdgvkNNLSVGpATEALAGEGLIVTAGGIDTHIHF-ISPQQIPT 146
|
90
....*....|....*.
gi 489524267 71 AdnFETGTRAAIAGGT 86
Cdd:PRK13985 147 A--FASGVTTMIGGGT 160
|
|
| PRK09228 |
PRK09228 |
guanine deaminase; Provisional |
17-61 |
7.33e-04 |
|
guanine deaminase; Provisional
Pssm-ID: 236419 [Multi-domain] Cd Length: 433 Bit Score: 41.71 E-value: 7.33e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 489524267 17 YISD--LRIEDEKIVEIGNNLEI-----NGDKVIDATGKIVIPGGIDTHTHF 61
Cdd:PRK09228 28 YIEDglLLVEDGRIVAAGPYAELraqlpADAEVTDYRGKLILPGFIDTHIHY 79
|
|
| PRK06846 |
PRK06846 |
putative deaminase; Validated |
11-62 |
1.17e-03 |
|
putative deaminase; Validated
Pssm-ID: 235873 [Multi-domain] Cd Length: 410 Bit Score: 41.15 E-value: 1.17e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 489524267 11 ITSDKTYISDLRIEDEKIVEIGNNLEIN--GDKVIDATGKIVIPGGIDTHTHFD 62
Cdd:PRK06846 24 IVQTETALCTLEIQDGKIVAIRPNKQVPdaTLPTYDANGLLMLPAFREMHIHLD 77
|
|
| Amidohydro_3 |
pfam07969 |
Amidohydrolase family; |
325-397 |
1.95e-03 |
|
Amidohydrolase family;
Pssm-ID: 400360 [Multi-domain] Cd Length: 464 Bit Score: 40.59 E-value: 1.95e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 489524267 325 LGIDDFSKIPNGAPGVeHRLALLYTYGVL-----ENRISANKFVEVTSTNAAKIFGMYPKKGEIAVGSDADIVILNVN 397
Cdd:pfam07969 363 LGSDAPVGPFDPWPRI-GAAVMRQTAGGGevlgpDEELSLEEALALYTSGPAKALGLEDRKGTLGVGKDADLVVLDDD 439
|
|
| ureC |
PRK13206 |
urease subunit alpha; Reviewed |
19-86 |
3.01e-03 |
|
urease subunit alpha; Reviewed
Pssm-ID: 237304 [Multi-domain] Cd Length: 573 Bit Score: 40.08 E-value: 3.01e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489524267 19 SDLRIEDEKIVEIGN------------NLEIN-GDKVIDATGKIVIPGGIDTHTHFdMNAGSITTAdnFETGTRAAIAGG 85
Cdd:PRK13206 89 ADVGIRDGRIVAIGKagnpdimdgvhpDLVIGpSTEIIAGNGRILTAGAIDCHVHF-ICPQIVDEA--LAAGITTLIGGG 165
|
.
gi 489524267 86 T 86
Cdd:PRK13206 166 T 166
|
|
| PRK07213 |
PRK07213 |
chlorohydrolase; Provisional |
21-60 |
6.00e-03 |
|
chlorohydrolase; Provisional
Pssm-ID: 235969 [Multi-domain] Cd Length: 375 Bit Score: 38.87 E-value: 6.00e-03
10 20 30 40
....*....|....*....|....*....|....*....|
gi 489524267 21 LRIEDEKIVEIGNnlEINGDKVIDATGkIVIPGGIDTHTH 60
Cdd:PRK07213 22 LVIEDGIIKGFTN--EVHEGNVIDAKG-LVIPPLINAHTH 58
|
|
| Met_dep_hydrolase_A |
cd01299 |
Metallo-dependent hydrolases, subgroup A is part of the superfamily of metallo-dependent ... |
367-403 |
6.14e-03 |
|
Metallo-dependent hydrolases, subgroup A 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: 238624 [Multi-domain] Cd Length: 342 Bit Score: 38.81 E-value: 6.14e-03
10 20 30
....*....|....*....|....*....|....*..
gi 489524267 367 STNAAKIFGMYPKKGEIAVGSDADIVILNVNKEETIS 403
Cdd:cd01299 304 TANAAELLGLSDELGVIEAGKLADLLVVDGDPLEDIA 340
|
|
| FMDH_A |
cd01304 |
Formylmethanofuran dehydrogenase (FMDH) subunit A; Methanogenic bacteria and archea derive ... |
365-447 |
7.86e-03 |
|
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: 38.55 E-value: 7.86e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489524267 365 VTSTNAAKIFGMyPKKGEIAVGSDADIVILNVNKEEtisyktqkqnVDYTPYEgfkikcKVEDVFLR-------GNHVVQ 437
Cdd:cd01304 435 MTRAGPAKLLGL-SDKGHLGVGADADIAIYDDDPDQ----------VDPSDYE------KVEKAFSRaayvlkdGEIVVK 497
|
90
....*....|
gi 489524267 438 SCNVKEHPTG 447
Cdd:cd01304 498 DGEVVAEPWG 507
|
|
| PLN02303 |
PLN02303 |
urease |
3-90 |
9.80e-03 |
|
urease
Pssm-ID: 215172 [Multi-domain] Cd Length: 837 Bit Score: 38.58 E-value: 9.80e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489524267 3 TILRGGTIITSDKTYISDLRIEDEKIVEIG------------NNLEI-NGDKVIDATGKIVIPGGIDTHTHFdmnagsIT 69
Cdd:PLN02303 336 TVITNAVIIDYTGIYKADIGIKDGLIVGIGkagnpdvmdgvtSNMIVgVNTEVIAGEGMIVTAGGIDCHVHF------IC 409
|
90 100
....*....|....*....|.
gi 489524267 70 TADNFEtgtraAIAGGTTTIL 90
Cdd:PLN02303 410 PQLATE-----AIASGITTLV 425
|
|
| |
