|
Name |
Accession |
Description |
Interval |
E-value |
| Isoaspartyl-dipeptidase |
cd01308 |
Isoaspartyl dipeptidase hydrolyzes the beta-L-isoaspartyl linkages in dipeptides, as part of ... |
2-377 |
7.27e-160 |
|
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: 453.77 E-value: 7.27e-160
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507083921 2 FTLLTNARVFSPEDLGLCSLLIHADRIVAVEKDISLFDGVD-EVIDCHGKWVIPGIIDQHVHLTGGGGEAGFASRTPAVK 80
Cdd:cd01308 1 FTLIKNAEVYAPEYLGKKDILIAGGKILAIEDQLNLPGYENvTVVDLHGKILVPGFIDQHVHIIGGGGEGGPSTRTPEVT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507083921 81 LRDLIQAGITTVVGVLGTDAISRSPKDLYAKMQSLNLEGLRAFMHTGAYAVPSPTITRSIRDDMTFIPAILGVK-IALAD 159
Cdd:cd01308 81 LSDLTTAGVTTVVGCLGTDGISRSMEDLLAKARALEEEGITCFVYTGSYEVPTRTITGSIRKDLLLIDKVIGVGeIAISD 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507083921 160 HRGSYPSFQELLRIVSDIRVASLLAGKKGLLHVHLGNLPEGMSQLIELCD-AGIPIHHISPTHVARTAPLFEQAIAFAHR 238
Cdd:cd01308 161 HRSSQPTVEELARIAAEARVGGLLGGKAGIVHIHLGDGKRALSPIFELIEeTEIPITQFLPTHINRTAPLFEQGVEFAKM 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507083921 239 GGHIDVTSGGSRFMPQE------QAILHALEAQVPADRITISSDGNGSVPRFNAQGIVEGLSAAPVAGNLNLLPRLIDVG 312
Cdd:cd01308 241 GGTIDLTSSIDPQFRKEgevrpsEALKRLLEQGVPLERITFSSDGNGSLPKFDENGNLVGLGVGSVDTLLREVREAVKCG 320
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 507083921 313 -IPVPQAIAMLTANVARSLGISG-GVLCAGERADICVLNDDLSLAHLFAAGKPLLRDGECLVTGNFE 377
Cdd:cd01308 321 dIPLEVALRVITSNVARILKLRKkGEIQPGFDADLVILDKDLDINSVIAKGQIMVRNGKLLVKGTFE 387
|
|
| isoAsp_dipep |
TIGR01975 |
isoaspartyl dipeptidase IadA; The L-isoaspartyl derivative of Asp arises non-enzymatically ... |
2-377 |
1.29e-114 |
|
isoaspartyl dipeptidase IadA; The L-isoaspartyl derivative of Asp arises non-enzymatically over time as a form of protein damage. In this isomerization, the connectivity of the polypeptide changes to pass through the beta-carboxyl of the side chain. Much but not all of this damage can be repaired by protein-L-isoaspartate (D-aspartate) O-methyltransferase. This model describes the isoaspartyl dipeptidase IadA, apparently one of two such enzymes in E. coli, an enzyme that degrades isoaspartyl dipeptides and may unblock degradation of proteins that cannot be repaired. This model also describes closely related proteins from other species (e.g. Clostridium perfringens, Thermoanaerobacter tengcongensis) that we assume to be equivalent in function. This family shows homology to dihydroorotases. [Protein fate, Degradation of proteins, peptides, and glycopeptides]
Pssm-ID: 131030 Cd Length: 389 Bit Score: 339.07 E-value: 1.29e-114
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507083921 2 FTLLTNARVFSPEDLGLCSLLIHADRIVAVEKDISLF-DGVDE--VIDCHGKWVIPGIIDQHVHLTGGGGEAGFASRTPA 78
Cdd:TIGR01975 1 FTLLKGAEVYAPEYIGKKDILIANDKIIAIADEIPSTkDFVPNcvVVGLEGMIAVPGFIDQHVHIIGGGGEGGPTTRTPE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507083921 79 VKLRDLIQAGITTVVGVLGTDAISRSPKDLYAKMQSLNLEGLRAFMHTGAYAVPSPTITRSIRDDMTFIPAILGV-KIAL 157
Cdd:TIGR01975 81 LTLSDITKGGVTTVVGLLGTDGITRHMESLLAKARALEEEGISCYMLTGAYHVPSRTITGSVESDLLLIDKVIGVgEIAI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507083921 158 ADHRGSYPSFQELLRIVSDIRVASLLAGKKGLLHVHLGNLPEGMS---QLIELCDagIPIHHISPTHVARTAPLFEQAIA 234
Cdd:TIGR01975 161 SDHRSAQPTVEHLTNMAAEARVGGLLGGKPGIVNFHVGDSKRALQpiyELVENTD--VPITQFLPTHINRNVPLFEAGLE 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507083921 235 FAHRGGHIDVTSG-------GSRFMPQEqAILHALEAQVPADRITISSDGNGSVPRFNAQGIVEGLSAAPVAGNLNLLPR 307
Cdd:TIGR01975 239 FAKKGGTIDLTSSidpqfrkEGEVAPAE-GIKKALEAGVPLEKVTFSSDGNGSQPFFDENGELTGLGVGSFETLFEEVRE 317
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 507083921 308 LIDVGI-PVPQAIAMLTANVARSLGISG-GVLCAGERADICVLNDDLSLAHLFAAGKPLLRDGECLVTGNFE 377
Cdd:TIGR01975 318 AVKDGDvPLEKALRVITSNVAGVLNLTGkGEISPGNDADLVVLDPDLRIHSVIARGKLMVKDGKACVKGTFE 389
|
|
| HutI |
COG1228 |
Imidazolonepropionase or related amidohydrolase [Secondary metabolites biosynthesis, transport ... |
3-351 |
2.30e-21 |
|
Imidazolonepropionase or related amidohydrolase [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 440841 [Multi-domain] Cd Length: 386 Bit Score: 94.26 E-value: 2.30e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507083921 3 TLLTNARVFSPEDLGL---CSLLIHADRIVAVEKDISL-FDGVDEVIDCHGKWVIPGIIDQHVHLTGGGGEAGFASRT-- 76
Cdd:COG1228 10 LLITNATLVDGTGGGVienGTVLVEDGKIAAVGPAADLaVPAGAEVIDATGKTVLPGLIDAHTHLGLGGGRAVEFEAGgg 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507083921 77 ---------PAVK-LRDLIQAGITTVVGVLGTDAisrSPKDLYAKMQSLNLEGLRAFMHTGAYAVPSPTITRSIRDDMTF 146
Cdd:COG1228 90 itptvdlvnPADKrLRRALAAGVTTVRDLPGGPL---GLRDAIIAGESKLLPGPRVLAAGPALSLTGGAHARGPEEARAA 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507083921 147 IPAILG-----VKIAlADHRGSYPSFQELLRIVSdirvASLLAGKKGLLHVHlgnLPEGMSQLIElcdAGIP-IHHIS-- 218
Cdd:COG1228 167 LRELLAegadyIKVF-AEGGAPDFSLEELRAILE----AAHALGLPVAAHAH---QADDIRLAVE---AGVDsIEHGTyl 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507083921 219 ------------PTHVARTAPLFEQAIAFAHRGGHIDVTSGGSRFMPqeqAILHALEAQVPadrITISSDGNGSVPrfna 286
Cdd:COG1228 236 ddevadllaeagTVVLVPTLSLFLALLEGAAAPVAAKARKVREAALA---NARRLHDAGVP---VALGTDAGVGVP---- 305
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 507083921 287 qgivEGLSAAPVAGNlnllprLIDVGIPVPQAIAMLTANVARSLGISG--GVLCAGERADICVLNDD 351
Cdd:COG1228 306 ----PGRSLHRELAL------AVEAGLTPEEALRAATINAAKALGLDDdvGSLEPGKLADLVLLDGD 362
|
|
| COG3964 |
COG3964 |
Predicted amidohydrolase [General function prediction only]; |
4-350 |
2.02e-16 |
|
Predicted amidohydrolase [General function prediction only];
Pssm-ID: 443164 [Multi-domain] Cd Length: 376 Bit Score: 79.83 E-value: 2.02e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507083921 4 LLTNARVFSPEDL--GLCSLLIHADRIVAVEKDISLFDGvDEVIDCHGKWVIPGIIDQHVHLTGGGG-------EAGFAS 74
Cdd:COG3964 3 LIKGGRVIDPANGidGVMDIAIKDGKIAAVAKDIDAAEA-KKVIDASGLYVTPGLIDLHTHVFPGGTdygvdpdGVGVRS 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507083921 75 rtpavklrdliqaGITTVVgvlgtDAISRSPKdlyakmqslNLEGLR------------AFMH---TGAYAVPSPTITRS 139
Cdd:COG3964 82 -------------GVTTVV-----DAGSAGAA---------NFDGFRkyvidpsktrvlAFLNisgIGLVGGNELQDLDD 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507083921 140 IRDDMTFIPA------ILGVKIALADHRGSYPSFQELLRIVSdirvaslLAGKKGL-LHVHLGNLPEGMSQLIELCDAGI 212
Cdd:COG3964 135 IDPDATAAAAeanpdfIVGIKVRASKGVVGDNGIEPLKRAKE-------AAKEAGLpLMVHIGNPPPPLDEVLDLLRPGD 207
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507083921 213 PIhhispTHVARTAP---------LFEQAIAFAHRGGHIDVTSGGSRFmPQEQAIlHALEAQVPADriTISSDgngsVPR 283
Cdd:COG3964 208 IL-----THCFNGKPngildedgkVRPSVREARKRGVLFDVGHGGASF-SFKVAE-PAIAQGFLPD--TISTD----LHT 274
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 507083921 284 FNAQGiveglsaaPVAGNLNLLPRLIDVGIPVPQAIAMLTANVARSLGISG-GVLCAGERADICVLND 350
Cdd:COG3964 275 RNMNG--------PVFDLATVMSKFLALGMPLEEVIAAVTWNPARAIGLPElGTLSVGADADITIFDL 334
|
|
| AllB |
COG0044 |
Dihydroorotase or related cyclic amidohydrolase [Nucleotide transport and metabolism]; ... |
4-93 |
5.30e-16 |
|
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: 78.98 E-value: 5.30e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507083921 4 LLTNARVFSPEDLGLCSLLIHADRIVAVEKDISLFDGvDEVIDCHGKWVIPGIIDQHVHLTGGGGE--AGFASRTPAvkl 81
Cdd:COG0044 1 LIKNGRVVDPGGLERADVLIEDGRIAAIGPDLAAPEA-AEVIDATGLLVLPGLIDLHVHLREPGLEhkEDIETGTRA--- 76
|
90
....*....|....*
gi 507083921 82 rdliqA---GITTVV 93
Cdd:COG0044 77 -----AaagGVTTVV 86
|
|
| PRK09237 |
PRK09237 |
amidohydrolase/deacetylase family metallohydrolase; |
4-350 |
3.23e-14 |
|
amidohydrolase/deacetylase family metallohydrolase;
Pssm-ID: 236423 [Multi-domain] Cd Length: 380 Bit Score: 73.35 E-value: 3.23e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507083921 4 LLTNARVFSPEDL--GLCSLLIHADRIVAVEKDISLFDGVdEVIDCHGKWVIPGIIDQHVH----LTGGGGEA-GFASRT 76
Cdd:PRK09237 2 LLRGGRVIDPANGidGVIDIAIEDGKIAAVAGDIDGSQAK-KVIDLSGLYVSPGWIDLHVHvypgSTPYGDEPdEVGVRS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507083921 77 pavklrdliqaGITTVVgvlgtDAISRSPKDL-----YAKMQS-------LNL--EGLRAFMHTG--AYAVPSPTItRSI 140
Cdd:PRK09237 81 -----------GVTTVV-----DAGSAGADNFddfrkLTIEASktrvlafLNIsrIGLLAQDELAdlEDIDADAVA-EAV 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507083921 141 RDDMTFipaILGVKIALADHRGSYPSFQELlrivsdiRVASLLAGKKGL-LHVHLGNLPEGMSQLIEL---------CDA 210
Cdd:PRK09237 144 KRNPDF---IVGIKARMSSSVVGDNGIEPL-------ELAKAIAAEANLpLMVHIGNPPPSLEEILELlrpgdilthCFN 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507083921 211 GIPIHHISPThvARTAPLFEQAIAfahRGGHIDVTSGGSRFmPQEQAIlHALEAQVPADriTISSDgngsVPRFNAqgiV 290
Cdd:PRK09237 214 GKPNRILDED--GELRPSVLEALE---RGVRLDVGHGTASF-SFKVAE-AAIAAGILPD--TISTD----IYCRNR---I 277
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 507083921 291 EGlsaaPVAGNLNLLPRLIDVGIPVPQAIAMLTANVARSLGISG-GVLCAGERADICVLND 350
Cdd:PRK09237 278 NG----PVYSLATVMSKFLALGMPLEEVIAAVTKNAADALRLPElGRLQVGSDADLTLFTL 334
|
|
| NagA |
COG1820 |
N-acetylglucosamine-6-phosphate deacetylase [Carbohydrate transport and metabolism]; |
4-362 |
8.10e-13 |
|
N-acetylglucosamine-6-phosphate deacetylase [Carbohydrate transport and metabolism];
Pssm-ID: 441425 [Multi-domain] Cd Length: 373 Bit Score: 68.97 E-value: 8.10e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507083921 4 LLTNARVFSPED-LGLCSLLIHADRIVAVEKDIslfDGVDEVIDCHGKWVIPGIIDQHVHltGGGGeAGFASRTPAvKLR 82
Cdd:COG1820 1 AITNARIFTGDGvLEDGALLIEDGRIAAIGPGA---EPDAEVIDLGGGYLAPGFIDLHVH--GGGG-VDFMDGTPE-ALR 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507083921 83 DLIQA----GITTVVGVLGTDAISR-----------SPKDLYAKMQSLNLEG-----LRAFMHTGAYAVPsPTItrsirD 142
Cdd:COG1820 74 TIARAharhGTTSFLPTTITAPPEDllralaaiaeaIEQGGGAGILGIHLEGpflspEKKGAHPPEYIRP-PDP-----E 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507083921 143 DMTFI--PAILGVK-IALADHRgsyPSFQELLRIVSD--IRVAsllAG-------------KKGLLHV-HLGNlpeGMSQ 203
Cdd:COG1820 148 ELDRLleAAGGLIKlVTLAPEL---PGALEFIRYLVEagVVVS---LGhtdatyeqaraafEAGATHVtHLFN---AMSP 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507083921 204 L------------------IEL-CDaGipiHHISPThVARtaplfeqaIAFAHRG-GHI----DVTSGGSrfMPQEQAIL 259
Cdd:COG1820 219 LhhrepgvvgaalddddvyAELiAD-G---IHVHPA-AVR--------LALRAKGpDRLilvtDAMAAAG--LPDGEYEL 283
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507083921 260 HALEAQVPADRITIsSDGN--GSVprfnaqgiveglsaapvagnLNL---LPRLID-VGIPVPQAIAMLTANVARSLGIS 333
Cdd:COG1820 284 GGLEVTVKDGVARL-ADGTlaGST--------------------LTMddaVRNLVEwTGLPLEEAVRMASLNPARALGLD 342
|
410 420 430
....*....|....*....|....*....|.
gi 507083921 334 G--GVLCAGERADICVLNDDLSLAHLFAAGK 362
Cdd:COG1820 343 DrkGSIAPGKDADLVVLDDDLNVRATWVGGE 373
|
|
| Met_dep_hydrolase_B |
cd01307 |
Metallo-dependent hydrolases, subgroup B is part of the superfamily of metallo-dependent ... |
21-350 |
1.56e-12 |
|
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: 67.74 E-value: 1.56e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507083921 21 LLIHADRIVAVEKDIsLFDGVDEVIDCHGKWVIPGIIDQHVHLTGGGGEAGFASRTPAVKlrdliqAGITTVV--GVLGT 98
Cdd:cd01307 2 VAIENGKIAAVGAAL-AAPAATQIVDAGGCYVSPGWIDLHVHVYQGGTRYGDRPDMIGVK------SGVTTVVdaGSAGA 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507083921 99 DAIS--------RSPKDLYAKMqSLNLEGLRAFMHtgayaVPSPT------ITRSIRDDMTFIpaiLGVKiALADHRGSY 164
Cdd:cd01307 75 DNIDgfrytvieRSATRVYAFL-NISRVGLVAQDE-----LPDPDnidedaVVAAAREYPDVI---VGLK-ARASKSVVG 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507083921 165 PSFQELLRIVSDIrvasllAGKKGL-LHVHLGNLPEGMSQLIELCDAGIPIHHI----SPTHVARTAPLFEQAIAFAHRG 239
Cdd:cd01307 145 EWGIKPLELAKKI------AKEADLpLMVHIGSPPPILDEVVPLLRRGDVLTHCfngkPNGIVDEEGEVLPLVRRARERG 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507083921 240 GHIDVTSGGSRF--MPQEQAILHALEAQvpadriTISSDGNGsvpRFNAQGiveglsaaPVAGNLNLLPRLIDVGIPVPQ 317
Cdd:cd01307 219 VIFDVGHGTASFsfRVARAAIAAGLLPD------TISSDIHG---RNRTNG--------PVYALATTLSKLLALGMPLEE 281
|
330 340 350
....*....|....*....|....*....|....
gi 507083921 318 AIAMLTANVARSLGISG-GVLCAGERADICVLND 350
Cdd:cd01307 282 VIEAVTANPARMLGLAEiGTLAVGYDADLTVFDL 315
|
|
| Amidohydro_1 |
pfam01979 |
Amidohydrolase family; This family of enzymes are a a large metal dependent hydrolase ... |
51-363 |
3.26e-12 |
|
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: 66.76 E-value: 3.26e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507083921 51 WVIPGIIDQHVHLTGGGGEA-----GFASRTPAVKLRDLIQAGITTVVGVLGTD--AISRSPKDLYAKMQSLNLEGLRAF 123
Cdd:pfam01979 1 IVLPGLIDAHVHLEMGLLRGipvppEFAYEALRLGITTMLKSGTTTVLDMGATTstGIEALLEAAEELPLGLRFLGPGCS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507083921 124 MHTGAYAVPSPTITRSIRDDMTFI--PAILGVKIALADHrGSYPSFQELLRIVSDirvaslLAGKKGL-LHVHLGNLPEG 200
Cdd:pfam01979 81 LDTDGELEGRKALREKLKAGAEFIkgMADGVVFVGLAPH-GAPTFSDDELKAALE------EAKKYGLpVAIHALETKGE 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507083921 201 MSQLIElcDAGIPIHHISPTHVARTAPLFEQAIAFAHRGGHIDVTS------------------GGSRFMPQEQAILHAL 262
Cdd:pfam01979 154 VEDAIA--AFGGGIEHGTHLEVAESGGLLDIIKLILAHGVHLSPTEanllaehlkgagvahcpfSNSKLRSGRIALRKAL 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507083921 263 EAQVpadRITISSDGNGSVPRFNaqgIVEGLSaapvagNLNLLPRLIDVGIPVPQAIAMLTANVARSLGISG--GVLCAG 340
Cdd:pfam01979 232 EDGV---KVGLGTDGAGSGNSLN---MLEELR------LALELQFDPEGGLSPLEALRMATINPAKALGLDDkvGSIEVG 299
|
330 340
....*....|....*....|...
gi 507083921 341 ERADICVLnDDLSLAHLFAAGKP 363
Cdd:pfam01979 300 KDADLVVV-DLDPLAAFFGLKPD 321
|
|
| SsnA |
COG0402 |
Cytosine/adenosine deaminase or related metal-dependent hydrolase [Nucleotide transport and ... |
3-367 |
7.68e-12 |
|
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: 66.00 E-value: 7.68e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507083921 3 TLLTNARVFSPE-DLGL---CSLLIHADRIVAVEKDISLFD--GVDEVIDCHGKWVIPGIIDQHVH-----LTGGGGEAG 71
Cdd:COG0402 2 LLIRGAWVLTMDpAGGVledGAVLVEDGRIAAVGPGAELPAryPAAEVIDAGGKLVLPGLVNTHTHlpqtlLRGLADDLP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507083921 72 F------------ASRTP-------AVKLRDLIQAGITTVVgvlgtDAISRSPKDLYAKMQSLNLEGLRAFMHTGAYAVP 132
Cdd:COG0402 82 LldwleeyiwpleARLDPedvyagaLLALAEMLRSGTTTVA-----DFYYVHPESADALAEAAAEAGIRAVLGRGLMDRG 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507083921 133 SP-----TITRSIRDDMTFIPAILG-----VKIALADHrGSYPSFQELLRivsdiRVASLLAGKKGLLHVHLGnlpEGMS 202
Cdd:COG0402 157 FPdglreDADEGLADSERLIERWHGaadgrIRVALAPH-APYTVSPELLR-----AAAALARELGLPLHTHLA---ETRD 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507083921 203 QlIELCDAGipiHHISPTHV-ARTAPLFEQAIaFAHrGGHID-------VTSG-------------GSRFMPqeqaILHA 261
Cdd:COG0402 228 E-VEWVLEL---YGKRPVEYlDELGLLGPRTL-LAH-CVHLTdeeiallAETGasvahcptsnlklGSGIAP----VPRL 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507083921 262 LEAQVpadRITISSDGNGSVPRFNaqgIVEGLSAAPVAGNLNLLPRLIdvgIPVPQAIAMLTANVARSLGISG--GVLCA 339
Cdd:COG0402 298 LAAGV---RVGLGTDGAASNNSLD---MFEEMRLAALLQRLRGGDPTA---LSAREALEMATLGGARALGLDDeiGSLEP 368
|
410 420 430 440
....*....|....*....|....*....|....*....|....*...
gi 507083921 340 GERADICVLN-DDLSLA-------------------HLFAAGKPLLRD 367
Cdd:COG0402 369 GKRADLVVLDlDAPHLAplhdplsalvyaadgrdvrTVWVAGRVVVRD 416
|
|
| metallo-dependent_hydrolases |
cd01292 |
Superfamily of metallo-dependent hydrolases (also called amidohydrolase superfamily) is a ... |
57-328 |
1.29e-11 |
|
Superfamily of metallo-dependent hydrolases (also called amidohydrolase superfamily) is a large group of proteins that show conservation in their 3-dimensional fold (TIM barrel) and in details of their active site. The vast majority of the members have a conserved metal binding site, involving four histidines and one aspartic acid residue. In the common reaction mechanism, the metal ion (or ions) deprotonate a water molecule for a nucleophilic attack on the substrate. The family includes urease alpha, adenosine deaminase, phosphotriesterase dihydroorotases, allantoinases, hydantoinases, AMP-, adenine and cytosine deaminases, imidazolonepropionase, aryldialkylphosphatase, chlorohydrolases, formylmethanofuran dehydrogenases and others.
Pssm-ID: 238617 [Multi-domain] Cd Length: 275 Bit Score: 64.28 E-value: 1.29e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507083921 57 IDQHVHLTGGGGEAGFASRTPAVK---------------LRDLIQAGITTVVGVLGTDAISRSPK--DLYAKMqSLNLEG 119
Cdd:cd01292 2 IDTHVHLDGSALRGTRLNLELKEAeelspedlyedtlraLEALLAGGVTTVVDMGSTPPPTTTKAaiEAVAEA-ARASAG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507083921 120 LRAFMHTGAY---AVPSPTITRSIRDDMTFIPAILGVKIALADHRGSYPSFQELLRivsdiRVASLLAGKKGLLHVHLGN 196
Cdd:cd01292 81 IRVVLGLGIPgvpAAVDEDAEALLLELLRRGLELGAVGLKLAGPYTATGLSDESLR-----RVLEEARKLGLPVVIHAGE 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507083921 197 LPEGMSQLIELCDAGIPIHHISPTHVARTAPlfEQAIAFAHRGGHIDVTSGGSRFMPQEQAILHAL-EAQVPADRITISS 275
Cdd:cd01292 156 LPDPTRALEDLVALLRLGGRVVIGHVSHLDP--ELLELLKEAGVSLEVCPLSNYLLGRDGEGAEALrRLLELGIRVTLGT 233
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 507083921 276 DGNGSVPRFNaqgiveglsaapVAGNLNLLPRLIDVGIPVPQAIAMLTANVAR 328
Cdd:cd01292 234 DGPPHPLGTD------------LLALLRLLLKVLRLGLSLEEALRLATINPAR 274
|
|
| PRK08204 |
PRK08204 |
hypothetical protein; Provisional |
3-374 |
8.46e-11 |
|
hypothetical protein; Provisional
Pssm-ID: 181288 [Multi-domain] Cd Length: 449 Bit Score: 63.10 E-value: 8.46e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507083921 3 TLLTNARVFSPE----DLGLCSLLIHADRIVAVEKDISLFDgvDEVIDCHGKWVIPGIIDQHVH-----LTGGGGE---- 69
Cdd:PRK08204 4 TLIRGGTVLTMDpaigDLPRGDILIEGDRIAAVAPSIEAPD--AEVVDARGMIVMPGLVDTHRHtwqsvLRGIGADwtlq 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507083921 70 -------AGFAS-RTPA-------VKLRDLIQAGITTVVgvlgtD--AISRSPKDLYAKMQSLNLEGLRA-FMHTGAYAV 131
Cdd:PRK08204 82 tyfreihGNLGPmFRPEdvyianlLGALEALDAGVTTLL-----DwsHINNSPEHADAAIRGLAEAGIRAvFAHGSPGPS 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507083921 132 PSPTITrSIRDDMTFIPAILG---------VKIALADhRGsyPSFQELLRIVSDIRVASLLagkkGL---LHVHLGNL-- 197
Cdd:PRK08204 157 PYWPFD-SVPHPREDIRRVKKryfssddglLTLGLAI-RG--PEFSSWEVARADFRLAREL----GLpisMHQGFGPWga 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507083921 198 -PEGMSQLIelcDAGIPIHHISPTHVARTAPlfEQAIAFAHRGGHIDVTSGGSRFMPQEQAILHALEAQvpADRITISSD 276
Cdd:PRK08204 229 tPRGVEQLH---DAGLLGPDLNLVHGNDLSD--DELKLLADSGGSFSVTPEIEMMMGHGYPVTGRLLAH--GVRPSLGVD 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507083921 277 GNGSVP----------------RFNAQGIVEGLSAAPvagnlnllprliDVGIPVPQAIAMLTANVARSLGISG--GVLC 338
Cdd:PRK08204 302 VVTSTGgdmftqmrfalqaeraRDNAVHLREGGMPPP------------RLTLTARQVLEWATIEGARALGLEDriGSLT 369
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*.
gi 507083921 339 AGERADICVLN-DDLSLA-------------------HLFAAGKPLLRDGECLVTG 374
Cdd:PRK08204 370 PGKQADLVLIDaTDLNLApvhdpvgavvqsahpgnvdSVMVAGRAVKRNGKLLGVD 425
|
|
| NagA |
cd00854 |
N-acetylglucosamine-6-phosphate deacetylase, NagA, catalyzes the hydrolysis of the N-acetyl ... |
3-361 |
1.32e-10 |
|
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: 62.21 E-value: 1.32e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507083921 3 TLLTNARVFSPEDLGLCSLLIHADRIVAVEKDISLFDGvDEVIDCHGKWVIPGIIDQHVHltgGGGEAGFASRTPAVKL- 81
Cdd:cd00854 1 LIIKNARILTPGGLEDGAVLVEDGKIVAIGPEDELEEA-DEIIDLKGQYLVPGFIDIHIH---GGGGADFMDGTAEALKt 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507083921 82 --RDLIQAGITTVVGVLgtdaISRSPKDLYAkmqslNLEGLRAFMHTGAYAVpsptitrsirddmtfipaILGVK----- 154
Cdd:cd00854 77 iaEALAKHGTTSFLPTT----VTAPPEEIAK-----ALAAIAEAIAEGQGAE------------------ILGIHlegpf 129
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507083921 155 IAlADHRGSYPsfQELLRIVSDIRVASLLAGKKGllHVHLGNL-PE--GMSQLIE-LCDAGIpihHISPTHVARTAPLFE 230
Cdd:cd00854 130 IS-PEKKGAHP--PEYLRAPDPEELKKWLEAAGG--LIKLVTLaPEldGALELIRyLVERGI---IVSIGHSDATYEQAV 201
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507083921 231 QAIA---------------FAHR---------------------GGHIDvtsggsrfmpqeQAILHALEAQVPADRITIS 274
Cdd:cd00854 202 AAFEagathvthlfnamspLHHRepgvvgaalsdddvyaeliadGIHVH------------PAAVRLAYRAKGADKIVLV 269
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507083921 275 SD-------GNGSVpRFNAQGI-VEGLSAAPVAGNL--------NLLPRLID-VGIPVPQAIAMLTANVARSLGISG--G 335
Cdd:cd00854 270 TDamaaaglPDGEY-ELGGQTVtVKDGVARLADGTLagstltmdQAVRNMVKwGGCPLEEAVRMASLNPAKLLGLDDrkG 348
|
410 420
....*....|....*....|....*.
gi 507083921 336 VLCAGERADICVLNDDLSLAHLFAAG 361
Cdd:cd00854 349 SLKPGKDADLVVLDDDLNVKATWING 374
|
|
| ATZ_TRZ_like |
cd01298 |
TRZ/ATZ family contains enzymes from the atrazine degradation pathway and related hydrolases. ... |
3-371 |
5.93e-10 |
|
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: 60.29 E-value: 5.93e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507083921 3 TLLTNARV---FSPEDLGLCSLLIHADRIVAVEKDISLFDG-VDEVIDCHGKWVIPGIIDQHVH----LTGGGGEAG--- 71
Cdd:cd01298 1 ILIRNGTIvttDPRRVLEDGDVLVEDGRIVAVGPALPLPAYpADEVIDAKGKVVMPGLVNTHTHlamtLLRGLADDLplm 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507083921 72 ---------FASRTPAVKLR--------DLIQAGITTVV--GVLGTDAISRSPKDLyakmqslnleGLRAFMHTGAYAVP 132
Cdd:cd01298 81 ewlkdliwpLERLLTEEDVYlgallalaEMIRSGTTTFAdmYFFYPDAVAEAAEEL----------GIRAVLGRGIMDLG 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507083921 133 SP---TITRSIRDDMTFIPAILG-----VKIALADHrGSYPSFQELLRIVSDirvaslLAGKKGL-LHVHLG-NLPE--- 199
Cdd:cd01298 151 TEdveETEEALAEAERLIREWHGaadgrIRVALAPH-APYTCSDELLREVAE------LAREYGVpLHIHLAeTEDEvee 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507083921 200 -----GMSQL------------------IELCDAGIPIHHISPTHVArtaplfeqaiafahrggHIDVTSG--GSRFMPq 254
Cdd:cd01298 224 slekyGKRPVeyleelgllgpdvvlahcVWLTDEEIELLAETGTGVA-----------------HNPASNMklASGIAP- 285
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507083921 255 eqaILHALEAQVPadrITISSDGNGSVprfNAQGIVEGLSAAPVAGNLNLLPRLIdvgIPVPQAIAMLTANVARSLGI-S 333
Cdd:cd01298 286 ---VPEMLEAGVN---VGLGTDGAASN---NNLDMFEEMRLAALLQKLAHGDPTA---LPAEEALEMATIGGAKALGLdE 353
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*...
gi 507083921 334 GGVLCAGERADICVLN---------DDLSLAHLFAA-----------GKPLLRDGECL 371
Cdd:cd01298 354 IGSLEVGKKADLILIDldgphllpvHDPISHLVYSAnggdvdtvivnGRVVMEDGELL 411
|
|
| PRK15446 |
PRK15446 |
phosphonate metabolism protein PhnM; Provisional |
3-368 |
1.20e-09 |
|
phosphonate metabolism protein PhnM; Provisional
Pssm-ID: 237967 [Multi-domain] Cd Length: 383 Bit Score: 59.42 E-value: 1.20e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507083921 3 TLLTNARVFSPEDLGLCSLLIHADRIVAVEKDISlfdGVDEVIDCHGKWVIPGIIDQHV-HLtggggEAGFASRtPAVKL 81
Cdd:PRK15446 4 MILSNARLVLPDEVVDGSLLIEDGRIAAIDPGAS---ALPGAIDAEGDYLLPGLVDLHTdNL-----EKHLAPR-PGVDW 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507083921 82 ----------RDLIQAGITTVVgvlgtDAIS---------RSPkDLYAKMqslnLEGLRAFMHTGA----------YAVP 132
Cdd:PRK15446 75 padaalaahdAQLAAAGITTVF-----DALSvgdeedgglRSR-DLARKL----IDAIEEARARGLlradhrlhlrCELT 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507083921 133 SPtitrsirDDMTFIPAILGVK----IALADH---------RGSYPSFQELLRIVSDIRVASLLAGKKGLLHVHlgnLPE 199
Cdd:PRK15446 145 NP-------DALELFEALLAHPrvdlVSLMDHtpgqrqfrdLEKYREYYAGKYGLSDEEFDAFVEERIALSARY---APP 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507083921 200 GMSQLIELCDA-GIPI-HH--ISPTHVARTA---------PLFEQAIAFAH-RGGHI-----DVTSGGSrfmpqeqailH 260
Cdd:PRK15446 215 NRRAIAALARArGIPLaSHddDTPEHVAEAHalgvaiaefPTTLEAARAARaLGMSVlmgapNVVRGGS----------H 284
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507083921 261 -----ALEAqVPADRITI-SSDgngSVPrfnaqgiveglsAAPVAGNLnLLPRliDVGIPVPQAIAMLTANVARSLGISG 334
Cdd:PRK15446 285 sgnvsALDL-AAAGLLDIlSSD---YYP------------ASLLDAAF-RLAD--DGGLDLPQAVALVTANPARAAGLDD 345
|
410 420 430
....*....|....*....|....*....|....*...
gi 507083921 335 -GVLCAGERADICVLNDDLSL---AHLFAAGKPLLRDG 368
Cdd:PRK15446 346 rGEIAPGKRADLVRVRRAGGLpvvRAVWRGGRRVFLAG 383
|
|
| PRK06687 |
PRK06687 |
TRZ/ATZ family protein; |
21-371 |
1.57e-09 |
|
TRZ/ATZ family protein;
Pssm-ID: 180657 [Multi-domain] Cd Length: 419 Bit Score: 59.25 E-value: 1.57e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507083921 21 LLIHADRIVAV-EKDISLFDGVDEVIDCHGKWVIPGIIDQHVH--LTGGGG------------------EAGFASR--TP 77
Cdd:PRK06687 24 LAVKDSQIVYVgQDKPAFLEQAEQIIDYQGAWIMPGLVNCHTHsaMTGLRGirddsnlhewlndyiwpaESEFTPDmtTN 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507083921 78 AVK--LRDLIQAGITTVvgvlgTDAISRSPKDLYAKMQSLNLEGLRAFMHTGAYAVPSPTITRSIRDDMTFIPAIL---- 151
Cdd:PRK06687 104 AVKeaLTEMLQSGTTTF-----NDMYNPNGVDIQQIYQVVKTSKMRCYFSPTLFSSETETTAETISRTRSIIDEILkykn 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507083921 152 -GVKIALADHrGSYPSFQELLRivSDIRVASLLAGKkglLHVHLGNLPEGMSQLIELcdagipiHHISPTHVARTAPLFE 230
Cdd:PRK06687 179 pNFKVMVAPH-SPYSCSRDLLE--ASLEMAKELNIP---LHVHVAETKEESGIILKR-------YGKRPLAFLEELGYLD 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507083921 231 QAIAFAHrgghidvtsgGSRFMPQEQAILHALE---AQVPADRITISSdGNGSVPRFNAQGIVEGLSAAPVAGNLNL--- 304
Cdd:PRK06687 246 HPSVFAH----------GVELNEREIERLASSQvaiAHNPISNLKLAS-GIAPIIQLQKAGVAVGIATDSVASNNNLdmf 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507083921 305 -------LPRLIDVG----IPVPQAIAMLTANVARSLGISG--GVLCAGERADICVLND---------DLSLAHL----- 357
Cdd:PRK06687 315 eegrtaaLLQKMKSGdasqFPIETALKVLTIEGAKALGMENqiGSLEVGKQADFLVIQPqgkihlqpqENMLSHLvyavk 394
|
410 420
....*....|....*....|.
gi 507083921 358 -------FAAGKPLLRDGECL 371
Cdd:PRK06687 395 ssdvddvYIAGEQVVKQGQVL 415
|
|
| L-HYD_ALN |
cd01315 |
L-Hydantoinases (L-HYDs) and Allantoinase (ALN); L-Hydantoinases are a member of the ... |
3-93 |
2.04e-09 |
|
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: 58.84 E-value: 2.04e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507083921 3 TLLTNARVFSPEDLGLCSLLIHADRIVAVEKDISLFDGVdEVIDCHGKWVIPGIIDQHVHLTGGGGE--AGFASRTPAvk 80
Cdd:cd01315 2 LVIKNGRVVTPDGVREADIAVKGGKIAAIGPDIANTEAE-EVIDAGGLVVMPGLIDTHVHINEPGRTewEGFETGTKA-- 78
|
90
....*....|...
gi 507083921 81 lrdLIQAGITTVV 93
Cdd:cd01315 79 ---AAAGGITTII 88
|
|
| Met_dep_hydrolase_A |
cd01299 |
Metallo-dependent hydrolases, subgroup A is part of the superfamily of metallo-dependent ... |
42-351 |
2.17e-09 |
|
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: 58.46 E-value: 2.17e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507083921 42 DEVIDCHGKWVIPGIIDQHVHLTGGGGEAGFASRTPAVK--------LRDLIQAGITTVVGVLGTDAIsrspkdLYAKMQ 113
Cdd:cd01299 1 AQVIDLGGKTLMPGLIDAHTHLGSDPGDLPLDLALPVEYrtiratrqARAALRAGFTTVRDAGGADYG------LLRDAI 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507083921 114 SlnlEGL----------RAFMHTGAYAVPSPTITRSIRDDMTFIP-----AILGV-----------KIA-------LADH 160
Cdd:cd01299 75 D---AGLipgprvfasgRALSQTGGHGDPRGLSGLFPAGGLAAVVdgveeVRAAVreqlrrgadqiKIMatggvlsPGDP 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507083921 161 RG-SYPSFQELLRIVSD-----IRVA-----------SLLAGKKGLLHVHLGNlPEGmsqlIELC-DAGIpihHISPTHV 222
Cdd:cd01299 152 PPdTQFSEEELRAIVDEahkagLYVAahaygaeairrAIRAGVDTIEHGFLID-DET----IELMkEKGI---FLVPTLA 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507083921 223 ARTAPLFEQAiafahrgghidvtsggSRFMPQEQAILHALEAQvpadritissDGNGSVPRFNAQG--IVEG--LSAAPV 298
Cdd:cd01299 224 TYEALAAEGA----------------APGLPADSAEKVALVLE----------AGRDALRRAHKAGvkIAFGtdAGFPVP 277
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*..
gi 507083921 299 AGNLNL--LPRLIDVGIPVPQAIAMLTANVARSLGISG--GVLCAGERADICVLNDD 351
Cdd:cd01299 278 PHGWNAreLELLVKAGGTPAEALRAATANAAELLGLSDelGVIEAGKLADLLVVDGD 334
|
|
| YtcJ |
COG1574 |
Predicted amidohydrolase YtcJ [General function prediction only]; |
3-67 |
2.87e-09 |
|
Predicted amidohydrolase YtcJ [General function prediction only];
Pssm-ID: 441182 [Multi-domain] Cd Length: 535 Bit Score: 58.66 E-value: 2.87e-09
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507083921 3 TLLTNARVFSPEDLGLC--SLLIHADRIVAV--EKDI-SLFDGVDEVIDCHGKWVIPGIIDQHVHLTGGG 67
Cdd:COG1574 10 LLLTNGRIYTMDPAQPVaeAVAVRDGRIVAVgsDAEVrALAGPATEVIDLGGKTVLPGFIDAHVHLLGGG 79
|
|
| PRK02382 |
PRK02382 |
dihydroorotase; Provisional |
4-93 |
3.21e-09 |
|
dihydroorotase; Provisional
Pssm-ID: 179417 [Multi-domain] Cd Length: 443 Bit Score: 58.12 E-value: 3.21e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507083921 4 LLTNARVFSPEDLGLCSLLIHADRIVAVEKDISLFDGvDEVIDCHGKWVIPGIIDQHVHLTGGGGE------AGfaSRTP 77
Cdd:PRK02382 5 LLKDGRVYYNNSLQPRDVRIDGGKITAVGKDLDGSSS-EEVIDARGMLLLPGGIDVHVHFREPGYThketwyTG--SRSA 81
|
90
....*....|....*.
gi 507083921 78 AVklrdliqAGITTVV 93
Cdd:PRK02382 82 AA-------GGVTTVV 90
|
|
| pyrC |
PRK09357 |
dihydroorotase; Validated |
1-69 |
3.55e-09 |
|
dihydroorotase; Validated
Pssm-ID: 236479 [Multi-domain] Cd Length: 423 Bit Score: 57.90 E-value: 3.55e-09
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507083921 1 MFTLLTNARVFSPEDLG-LCSLLIHADRIVAVEKDISLFDgvDEVIDCHGKWVIPGIIDQHVHLTGGGGE 69
Cdd:PRK09357 1 MMILIKNGRVIDPKGLDeVADVLIDDGKIAAIGENIEAEG--AEVIDATGLVVAPGLVDLHVHLREPGQE 68
|
|
| PRK08323 |
PRK08323 |
phenylhydantoinase; Validated |
1-63 |
8.55e-09 |
|
phenylhydantoinase; Validated
Pssm-ID: 236240 [Multi-domain] Cd Length: 459 Bit Score: 56.72 E-value: 8.55e-09
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 507083921 1 MFTLLTNARVFSPEDLGLCSLLIHADRIVAVEKDislfdGVDEVIDCHGKWVIPGIIDQHVHL 63
Cdd:PRK08323 1 MSTLIKNGTVVTADDTYKADVLIEDGKIAAIGAN-----LGDEVIDATGKYVMPGGIDPHTHM 58
|
|
| PRK09236 |
PRK09236 |
dihydroorotase; Reviewed |
3-62 |
1.48e-08 |
|
dihydroorotase; Reviewed
Pssm-ID: 181716 Cd Length: 444 Bit Score: 56.03 E-value: 1.48e-08
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 507083921 3 TLLTNARVFSPEDLGLCSLLIHADRIVAVEKDISLfDGVDEVIDCHGKWVIPGIIDQHVH 62
Cdd:PRK09236 4 ILIKNARIVNEGKIFEGDVLIENGRIAKIASSISA-KSADTVIDAAGRYLLPGMIDDQVH 62
|
|
| D-aminoacylase |
cd01297 |
D-aminoacylases (N-acyl-D-Amino acid amidohydrolases) catalyze the hydrolysis of ... |
3-349 |
1.60e-08 |
|
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: 55.77 E-value: 1.60e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507083921 3 TLLTNARVFSPE-------DLGlcsllIHADRIVAVeKDISLFDGvDEVIDCHGKWVIPGIIDQHVHltggggEAGFASR 75
Cdd:cd01297 2 LVIRNGTVVDGTgappftaDVG-----IRDGRIAAI-GPILSTSA-REVIDAAGLVVAPGFIDVHTH------YDGQVFW 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507083921 76 TPAvkLRDLIQAGITTVvgVLGTDAISRSPKDLYAKMQ-SLNLEGLRAFMHTGAYAVPSP-----TITRSIRD------- 142
Cdd:cd01297 69 DPD--LRPSSRQGVTTV--VLGNCGVSPAPANPDDLARlIMLMEGLVALGEGLPWGWATFaeyldALEARPPAvnvaalv 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507083921 143 ----------DMTFIPAI-------------------LGVKIALADHRGSYPSFQELLRIvsdirvASLLAGKKGLLHVH 193
Cdd:cd01297 145 ghaalrravmGLDAREATeeelakmrellrealeagaLGISTGLAYAPRLYAGTAELVAL------ARVAARYGGVYQTH 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507083921 194 LGNLP----EGMSQLIELCD-AGIPIH--HI------SPTHVARTAPLFEQAIAFAHRGGhIDVTSGGSRFMPQEQAILH 260
Cdd:cd01297 219 VRYEGdsilEALDELLRLGReTGRPVHisHLksagapNWGKIDRLLALIEAARAEGLQVT-ADVYPYGAGSEDDVRRIMA 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507083921 261 aleaqvpADRITISSDGngsvprfnaqgiveGLSAAPVAGNLNLLPRLI-----DVG-IPVPQAIAMLTANVARSLGISG 334
Cdd:cd01297 298 -------HPVVMGGSDG--------------GALGKPHPRSYGDFTRVLghyvrERKlLSLEEAVRKMTGLPARVFGLAD 356
|
410
....*....|....*.
gi 507083921 335 -GVLCAGERADICVLN 349
Cdd:cd01297 357 rGRIAPGYRADIVVFD 372
|
|
| D-HYD |
cd01314 |
D-hydantoinases (D-HYD) also called dihydropyrimidases (DHPase) and related proteins; DHPases ... |
3-63 |
1.62e-08 |
|
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: 56.07 E-value: 1.62e-08
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 507083921 3 TLLTNARVFSPEDLGLCSLLIHADRIVAVEKDISLFDGVdEVIDCHGKWVIPGIIDQHVHL 63
Cdd:cd01314 1 LIIKNGTIVTADGSFKADILIEDGKIVAIGPNLEAPGGV-EVIDATGKYVLPGGIDPHTHL 60
|
|
| YtcJ_like |
cd01300 |
YtcJ_like metal dependent amidohydrolases. YtcJ is a Bacillus subtilis ORF of unknown function. ... |
21-87 |
8.27e-08 |
|
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: 53.85 E-value: 8.27e-08
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507083921 21 LLIHADRIVAV--EKDISLFDGVD-EVIDCHGKWVIPGIIDQHVHLTGGGGEAGFASRTPAVKLRDLIQA 87
Cdd:cd01300 2 VAVRDGRIVAVgsDAEAKALKGPAtEVIDLKGKTVLPGFIDSHSHLLLGGLSLLWLDLSGVTSKEEALAR 71
|
|
| pyrC_multi |
TIGR00857 |
dihydroorotase, multifunctional complex type; In contrast to the homodimeric type of ... |
20-116 |
2.99e-07 |
|
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: 52.06 E-value: 2.99e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507083921 20 SLLIHADRIVAVEKdislFDGVD--EVIDCHGKWVIPGIIDQHVHLTGGGGE--AGFASRTPAVklrdlIQAGITTVVGV 95
Cdd:TIGR00857 7 DILVEGGRIKKIGK----LRIPPdaEVIDAKGLLVLPGFIDLHVHLRDPGEEykEDIESGSKAA-----AHGGFTTVADM 77
|
90 100
....*....|....*....|.
gi 507083921 96 LGTDAISRSPKDLYAKMQSLN 116
Cdd:TIGR00857 78 PNTKPPIDTPETLEWKLQRLK 98
|
|
| Met_dep_hydrolase_C |
cd01309 |
Metallo-dependent hydrolases, subgroup C is part of the superfamily of metallo-dependent ... |
27-351 |
1.16e-06 |
|
Metallo-dependent hydrolases, subgroup C is part of the superfamily of metallo-dependent hydrolases, a large group of proteins that show conservation in their 3-dimensional fold (TIM barrel) and in details of their active site. The vast majority of the members have a conserved metal binding site, involving four histidines and one aspartic acid residue. In the common reaction mechanism, the metal ion (or ions) deprotonate a water molecule for a nucleophilic attack on the substrate. The function of this subgroup is unknown.
Pssm-ID: 238634 [Multi-domain] Cd Length: 359 Bit Score: 50.00 E-value: 1.16e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507083921 27 RIVAVEKDISLFDGVdEVIDCHGKWVIPGIIDQHVHLTGGGGEAGFASR---------TPAVK-----------LRDLIQ 86
Cdd:cd01309 3 KIVAVGAEITTPADA-EVIDAKGKHVTPGLIDAHSHLGLDEEGGVRETSdaneetdpvTPHVRaidginpddeaFKRARA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507083921 87 AGITTVVGVLGtdaisrspkdlyakmqSLNLEGLRAFMHTgayavpsptiTRSIRDDMTFIPAILGVKIALA-------D 159
Cdd:cd01309 82 GGVTTVQVLPG----------------SANLIGGQGVVIK----------TDGGTIEDMFIKAPAGLKMALGenpkrvyG 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507083921 160 HRGSYPS--------FQELLrivsdIRVASLLAG-KKGLLHVHLGNLPE-GMSQLIELCDAGIPIHhispTHVARtAPLF 229
Cdd:cd01309 136 GKGKEPAtrmgvaalLRDAF-----IKAQEYGRKyDLGKNAKKDPPERDlKLEALLPVLKGEIPVR----IHAHR-ADDI 205
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507083921 230 EQAIAFAHRGGhIDVTsggsrfmpqeqaILHALEAQVPADRIT-----ISSDGNGSVPRF---------------NAQGI 289
Cdd:cd01309 206 LTAIRIAKEFG-IKIT------------IEHGAEGYKLADELAkhgipVIYGPTLTLPKKveevndaidtnayllKKGGV 272
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 507083921 290 VEGL-SAAPVAG--NLNLLPRL-IDVGIPVPQAIAMLTANVARSLGISG--GVLCAGERADICVLNDD 351
Cdd:cd01309 273 AFAIsSDHPVLNirNLNLEAAKaVKYGLSYEEALKAITINPAKILGIEDrvGSLEPGKDADLVVWNGD 340
|
|
| Cyclic_amidohydrolases |
cd01302 |
Cyclic amidohydrolases, including hydantoinase, dihydropyrimidinase, allantoinase, and ... |
50-353 |
1.20e-06 |
|
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: 49.70 E-value: 1.20e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507083921 50 KWVIPGIIDQHVHL---TGGGGEAGFASRTPAVKLrdliqAGITTVVGVLGTDAIsrsPKDLYAKMQSLNLEGLRAFMHT 126
Cdd:cd01302 1 LLVLPGFIDIHVHLrdpGGTTYKEDFESGSRAAAA-----GGVTTVIDMPNTGPP---PIDLPAIELKIKLAEESSYVDF 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507083921 127 GAYAVPSP-----TITRSIRDDMTFIPAILGVKIA---------LADHRGSYPSFQEllRIVSDIRVASLLAGKKGlLHV 192
Cdd:cd01302 73 SFHAGIGPgdvtdELKKLFDAGINSLKVFMNYYFGelfdvddgtLMRTFLEIASRGG--PVMVHAERAAQLAEEAG-ANV 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507083921 193 HLGNL--PEGMSQLIELCDAGIPIH-HISPTHVartapLFEQAIafAHRGGHIDVTSGGSRFMPQEQAILHALEAQVpad 269
Cdd:cd01302 150 HIAHVssGEALELIKFAKNKGVKVTcEVCPHHL-----FLDESM--LRLNGAWGKVNPPLRSKEDREALWEGVKNGK--- 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507083921 270 rI-TISSDGNGSvPRFNAQGIVEGLSAAPVAGNLNL-LPRLIDV----GIPVPQAIAMLTANVARSLGI-SGGVLCAGER 342
Cdd:cd01302 220 -IdTIASDHAPH-SKEEKESGKDIWKAPPGFPGLETrLPILLTEgvkrGLSLETLVEILSENPARIFGLyPKGTIAVGYD 297
|
330
....*....|.
gi 507083921 343 ADICVLNDDLS 353
Cdd:cd01302 298 ADLVIVDPKKE 308
|
|
| PRK08393 |
PRK08393 |
N-ethylammeline chlorohydrolase; Provisional |
1-364 |
1.61e-06 |
|
N-ethylammeline chlorohydrolase; Provisional
Pssm-ID: 181411 [Multi-domain] Cd Length: 424 Bit Score: 49.80 E-value: 1.61e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507083921 1 MFTLLTNARVFSPEDLGL--CSLLIHADRIVAVEKDISlfDGVDEVIDCHGKWVIPGIIDQHVHlTGGGGEAGFASRTPA 78
Cdd:PRK08393 1 MSILIKNGYVIYGENLKVirADVLIEGNKIVEVKRNIN--KPADTVIDASGSVVSPGFINAHTH-SPMVLLRGLADDVPL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507083921 79 V------------KLR-------------DLIQAGITTVVgvlgtdaisrspkDLYAKMQSL---NLE-GLRAFMHTGAY 129
Cdd:PRK08393 78 MewlqnyiwprerKLKrkdiywgaylgllEMIKSGTTTFV-------------DMYFHMEEVakaTLEvGLRGYLSYGMV 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507083921 130 AVPSPTITR-SIRDDMTFIPAILG-----VKIALADHrGSYPSFQELLRIVSDirvaslLAGKKG-LLHVHLGNLPEGMS 202
Cdd:PRK08393 145 DLGDEEKREkEIKETEKLMEFIEKlnsprVHFVFGPH-APYTCSLALLKWVRE------KAREWNkLITIHLSETMDEIK 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507083921 203 QLIELcdagipiHHISPTHVARTAPLFEQAIAFAH------RGGHIDVTSG-------------GSRFMPQEQailhALE 263
Cdd:PRK08393 218 QIREK-------YGKSPVVLLDEIGFLNEDVIAAHgvwlssRDIRILASAGvtvahnpasnmklGSGVMPLRK----LLN 286
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507083921 264 AQVpadRITISSDGNGSVprfNAQGIVEGLSAAPVAGNL-NLLPRLIDvgipVPQAIAMLTANVARSLGISGGVLCAGER 342
Cdd:PRK08393 287 AGV---NVALGTDGAASN---NNLDMLREMKLAALLHKVhNLDPTIAD----AETVFRMATQNGAKALGLKAGVIKEGYL 356
|
410 420
....*....|....*....|..
gi 507083921 343 ADICVLndDLSLAHLFAAGKPL 364
Cdd:PRK08393 357 ADIAVI--DFNRPHLRPINNPI 376
|
|
| AdeC |
COG1001 |
Adenine deaminase [Nucleotide transport and metabolism]; |
3-373 |
1.66e-06 |
|
Adenine deaminase [Nucleotide transport and metabolism];
Pssm-ID: 440625 [Multi-domain] Cd Length: 559 Bit Score: 49.71 E-value: 1.66e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507083921 3 TLLTNARVFS-------PEDLGlcsllIHADRIVAVEKDISlfDGVdEVIDCHGKWVIPGIIDQHVHLtggggE------ 69
Cdd:COG1001 7 LVIKNGRLVNvftgeilEGDIA-----IAGGRIAGVGDYIG--EAT-EVIDAAGRYLVPGFIDGHVHI-----Essmvtp 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507083921 70 AGFASrtpAVKLRdliqaGITTVV-------GVLGTDAISrspkdlYAKMQSLNLEgLRAFM-------------HTGAY 129
Cdd:COG1001 74 AEFAR---AVLPH-----GTTTVIadpheiaNVLGLEGVR------YMLEAAEGLP-LDIFVmlpscvpatpgleTAGAV 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507083921 130 aVPSPTITRSIRDDMtfipaILGvkiaLA---DHRGSYPSFQELLRIVsdirVASLLAGKkgllHVHlGNLPeGMSQLiE 206
Cdd:COG1001 139 -LGAEDLAELLDHPR-----VIG----LGevmNFPGVLNGDPRMLAKI----AAALAAGK----VID-GHAP-GLSGK-D 197
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507083921 207 LC---DAGipihhISPTHVARTAplfEQAIAFAHRGGHIdvtsggsrfMPQEQAILHALEAQVPA------DRITISSDG 277
Cdd:COG1001 198 LNayaAAG-----IRSDHECTTA---EEALEKLRRGMYV---------MIREGSAAKDLPALLPAvtelnsRRCALCTDD 260
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507083921 278 NgsvprfNAQGIVEglsaapvAGNLN-LLPRLIDVGIPVPQAIAMLTANVARSLGISG-GVLCAGERADICVLND--DLS 353
Cdd:COG1001 261 R------HPDDLLE-------EGHIDhVVRRAIELGLDPVTAIQMATLNAAEHFGLKDlGAIAPGRRADIVLLDDleDFK 327
|
410 420
....*....|....*....|
gi 507083921 354 LAHLFAAGKPLLRDGECLVT 373
Cdd:COG1001 328 VEKVYADGKLVAEDGKLLVD 347
|
|
| PRK15493 |
PRK15493 |
bifunctional S-methyl-5'-thioadenosine deaminase/S-adenosylhomocysteine deaminase; |
21-370 |
2.37e-06 |
|
bifunctional S-methyl-5'-thioadenosine deaminase/S-adenosylhomocysteine deaminase;
Pssm-ID: 185390 [Multi-domain] Cd Length: 435 Bit Score: 49.29 E-value: 2.37e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507083921 21 LLIHADRIVAVEK-DISLFDGVDEVIDCHGKWVIPGIIDQHVH-----LTGGGG---------------EAGF----ASR 75
Cdd:PRK15493 25 IIVENDQIIDVNSgEFASDFEVDEVIDMKGKWVLPGLVNTHTHvvmslLRGIGDdmllqpwletriwplESQFtpelAVA 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507083921 76 TPAVKLRDLIQAGITTVvgvlgTDAISRSPKDLYAKMQSLNLEGLRAFMHTGAYAVPSPTI-TRSIRDDMTFIPAIL--- 151
Cdd:PRK15493 105 STELGLLEMVKSGTTSF-----SDMFNPIGVDQDAIMETVSRSGMRAAVSRTLFSFGTKEDeKKAIEEAEKYVKRYYnes 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507083921 152 GVKIALADHRGSYPSFQELLRIVSDIRVASllagkKGLLHVHLGNlPEGMSQLIELCDAGIPIHHISpthvarTAPLFEQ 231
Cdd:PRK15493 180 GMLTTMVAPHSPYTCSTELLEECARIAVEN-----QTMVHIHLSE-TEREVRDIEAQYGKRPVEYAA------SCGLFKR 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507083921 232 AIAFAHrgghidvtsgGSRFMPQEQAILHALEAQV---PADRITISSdGNGSVPRFNAQGIVEGLSAAPVAGNLNL---- 304
Cdd:PRK15493 248 PTVIAH----------GVVLNDNERAFLAEHDVRVahnPNSNLKLGS-GIANVKAMLEAGIKVGIATDSVASNNNLdmfe 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507083921 305 ---LPRLIDVGI-------PVPQAIAMLTANVARSLGI-SGGVLCAGERADICVLND---------DLSLAHLFAA---- 360
Cdd:PRK15493 317 emrIATLLQKGIhqdatalPVETALTLATKGAAEVIGMkQTGSLEVGKCADFITIDPsnkphlqpaDEVLSHLVYAasgk 396
|
410
....*....|....*...
gi 507083921 361 --------GKPLLRDGEC 370
Cdd:PRK15493 397 disdviinGKRVVWNGEC 414
|
|
| PRK07228 |
PRK07228 |
5'-deoxyadenosine deaminase; |
21-64 |
1.14e-05 |
|
5'-deoxyadenosine deaminase;
Pssm-ID: 180895 [Multi-domain] Cd Length: 445 Bit Score: 46.92 E-value: 1.14e-05
10 20 30 40
....*....|....*....|....*....|....*....|....
gi 507083921 21 LLIHADRIVAVEKDISLfDGVDEVIDCHGKWVIPGIIDQHVHLT 64
Cdd:PRK07228 24 VLIEDDRIAAVGDRLDL-EDYDDHIDATGKVVIPGLIQGHIHLC 66
|
|
| PRK13404 |
PRK13404 |
dihydropyrimidinase; Provisional |
3-63 |
1.43e-05 |
|
dihydropyrimidinase; Provisional
Pssm-ID: 184033 [Multi-domain] Cd Length: 477 Bit Score: 47.00 E-value: 1.43e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 507083921 3 TLLTNARVFSPEDLGLCSLLIHADRIVAVEKDISlfdGVDEVIDCHGKWVIPGIIDQHVHL 63
Cdd:PRK13404 6 LVIRGGTVVTATDTFQADIGIRGGRIAALGEGLG---PGAREIDATGRLVLPGGVDSHCHI 63
|
|
| PRK12394 |
PRK12394 |
metallo-dependent hydrolase; |
4-347 |
1.76e-05 |
|
metallo-dependent hydrolase;
Pssm-ID: 183497 [Multi-domain] Cd Length: 379 Bit Score: 46.29 E-value: 1.76e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507083921 4 LLTNARVFSPE--DLGLCSLLIHADRIVAVEKDISLfdGVDEVIDCHGKWVIPGIIDQHVHLTGGGGEAGFasRTPAVKL 81
Cdd:PRK12394 6 LITNGHIIDPArnINEINNLRIINDIIVDADKYPVA--SETRIIHADGCIVTPGLIDYHAHVFYDGTEGGV--RPDMYMP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507083921 82 RDliqaGITTVV--GVLGTDAISRspkdLYAKMQSLNLEGLRAFMHT-----GAYAVPSPTITRSIRDDMT------FIP 148
Cdd:PRK12394 82 PN----GVTTVVdaGSAGTANFDA----FYRTVICASKVRIKAFLTVsppgqTWSGYQENYDPDNIDENKIhalfrqYRN 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507083921 149 AILGVKIALADHR-GSYPS--FQELLRIVSDIRVAsllagkkglLHVHLGNLPEGMSQLIELCDAGIPIHHIspTHVART 225
Cdd:PRK12394 154 VLQGLKLRVQTEDiAEYGLkpLTETLRIANDLRCP---------VAVHSTHPVLPMKELVSLLRRGDIIAHA--FHGKGS 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507083921 226 APLFEQAIAFA------HRGGHIDVTSGGSRFmpQEQAILHALEAQVPADriTISSDGNGSVPRfnaqgiveglsAAPVA 299
Cdd:PRK12394 223 TILTEEGAVLAevrqarERGVIFDAANGRSHF--DMNVARRAIANGFLPD--IISSDLSTITKL-----------AWPVY 287
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|
gi 507083921 300 GNLNLLPRLIDVGIPVPQAIAMLTANVARSLGISG--GVLCAGERADICV 347
Cdd:PRK12394 288 SLPWVLSKYLALGMALEDVINACTHTPAVLMGMAAeiGTLAPGAFADIAI 337
|
|
| PRK05985 |
PRK05985 |
cytosine deaminase; Provisional |
3-85 |
1.82e-05 |
|
cytosine deaminase; Provisional
Pssm-ID: 180337 [Multi-domain] Cd Length: 391 Bit Score: 46.46 E-value: 1.82e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507083921 3 TLLTNARvfsPEDLGLCSLLIHADRIVAVEKDISLFDGVdEVIDCHGKWVIPGIIDQHVHL-TGGGGEAgFASRTPAVKL 81
Cdd:PRK05985 4 LLFRNVR---PAGGAAVDILIRDGRIAAIGPALAAPPGA-EVEDGGGALALPGLVDGHIHLdKTFWGDP-WYPNEPGPSL 78
|
....
gi 507083921 82 RDLI 85
Cdd:PRK05985 79 RERI 82
|
|
| PRK07575 |
PRK07575 |
dihydroorotase; Provisional |
1-62 |
1.83e-05 |
|
dihydroorotase; Provisional
Pssm-ID: 236055 [Multi-domain] Cd Length: 438 Bit Score: 46.59 E-value: 1.83e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 507083921 1 MFTLLTNARVFSPE-DLGLCSLLIHADRIVAVEKDISLfDGVDEVIDCHGKWVIPGIIDQHVH 62
Cdd:PRK07575 3 MSLLIRNARILLPSgELLLGDVLVEDGKIVAIAPEISA-TAVDTVIDAEGLTLLPGVIDPQVH 64
|
|
| Bact_CD |
cd01293 |
Bacterial cytosine deaminase and related metal-dependent hydrolases. Cytosine deaminases (CDs) ... |
4-63 |
2.12e-05 |
|
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: 46.09 E-value: 2.12e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 507083921 4 LLTNARVFSpEDLGLCSLLIHADRIVAVEKDISLfDGVDEVIDCHGKWVIPGIIDQHVHL 63
Cdd:cd01293 1 LLRNARLAD-GGTALVDIAIEDGRIAAIGPALAV-PPDAEEVDAKGRLVLPAFVDPHIHL 58
|
|
| PRK09059 |
PRK09059 |
dihydroorotase; Validated |
3-101 |
2.83e-05 |
|
dihydroorotase; Validated
Pssm-ID: 181631 [Multi-domain] Cd Length: 429 Bit Score: 45.80 E-value: 2.83e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507083921 3 TLLTNARVFSPE-DL-GLCSLLIHADRIVAVEKDIsLFDGVDE---VIDCHGKWVIPGIIDQHVHLtgggGEAGFASR-T 76
Cdd:PRK09059 5 ILLANARIIDPSrGLdEIGTVLIEDGVIVAAGKGA-GNQGAPEgaeIVDCAGKAVAPGLVDARVFV----GEPGAEHReT 79
|
90 100
....*....|....*....|....*
gi 507083921 77 PAVKLRDLIQAGITTVVGVLGTDAI 101
Cdd:PRK09059 80 IASASRAAAAGGVTSIIMMPDTDPV 104
|
|
| AdeC |
cd01295 |
Adenine deaminase (AdeC) directly deaminates adenine to form hypoxanthine. This reaction is ... |
46-350 |
4.61e-05 |
|
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: 45.29 E-value: 4.61e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507083921 46 DCHGKWVIPGIIDQHVHLtggggeagFASR-TPAVKLRDLIQAGITTVV-------GVLGTDAIS-------RSPKDLY- 109
Cdd:cd01295 1 DAEGKYIVPGFIDAHLHI--------ESSMlTPSEFAKAVLPHGTTTVIadpheiaNVAGVDGIEfmledakKTPLDIFw 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507083921 110 ---AKMQSLNLEglrafmHTGAYavpsptITRSIRDDMTFIPAILGVKiALADHRGSYPSFQELLRIvsdirvasLLAGK 186
Cdd:cd01295 73 mlpSCVPATPFE------TSGAE------LTAEDIKELLEHPEVVGLG-EVMDFPGVIEGDDEMLAK--------IQAAK 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507083921 187 KGLLHVhLGNLPeGMSQLiELCD---AGIpihhiSPTHVARTAplfEQAIAFAHRGGHIdvtsggsrfMPQEQAILHALE 263
Cdd:cd01295 132 KAGKPV-DGHAP-GLSGE-ELNAymaAGI-----STDHEAMTG---EEALEKLRLGMYV---------MLREGSIAKNLE 191
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507083921 264 AQVPA------DRITISSDGngSVPRFnaqgIVEGlsaapvaGNLN-LLPRLIDVGIPVPQAIAMLTANVARSLGISG-G 335
Cdd:cd01295 192 ALLPAiteknfRRFMFCTDD--VHPDD----LLSE-------GHLDyIVRRAIEAGIPPEDAIQMATINPAECYGLHDlG 258
|
330
....*....|....*
gi 507083921 336 VLCAGERADICVLND 350
Cdd:cd01295 259 AIAPGRIADIVILDD 273
|
|
| Imidazolone-5PH |
cd01296 |
Imidazolonepropionase/imidazolone-5-propionate hydrolase (Imidazolone-5PH) catalyzes the third ... |
21-127 |
6.48e-05 |
|
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: 44.56 E-value: 6.48e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507083921 21 LLIHADRIVAV--EKDISLFDGV-DEVIDCHGKWVIPGIIDQHVHLT-GGGGEAGFASRTPAVKLRDLIQAGittvVGVL 96
Cdd:cd01296 1 IAIRDGRIAAVgpAASLPAPGPAaAEEIDAGGRAVTPGLVDCHTHLVfAGDRVDEFAARLAGASYEEILAAG----GGIL 76
|
90 100 110
....*....|....*....|....*....|...
gi 507083921 97 GTDAISR--SPKDLYAKMQSLnlegLRAFMHTG 127
Cdd:cd01296 77 STVRATRaaSEDELFASALRR----LARMLRHG 105
|
|
| DHOase_IIa |
cd01317 |
Dihydroorotase (DHOase), subgroup IIa; DHOases catalyze the reversible interconversion of ... |
42-351 |
1.90e-04 |
|
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: 42.99 E-value: 1.90e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507083921 42 DEVIDCHGKWVIPGIIDQHVHLtgggGEAGFASR-TPAVKLRDLIQAGITTVV------GVLGTDAISRSPKDLY----- 109
Cdd:cd01317 2 AEVIDAEGKILAPGLVDLHVHL----REPGFEYKeTLESGAKAAAAGGFTTVVcmpntnPVIDNPAVVELLKNRAkdvgi 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507083921 110 ------------------AKMQSLNLEGLRAFMHTGAYAVPSPTITRSIRDDMTFIPAILGV--KIALADH---RGSYPS 166
Cdd:cd01317 78 vrvlpigaltkglkgeelTEIGELLEAGAVGFSDDGKPIQDAELLRRALEYAAMLDLPIIVHpeDPSLAGGgvmNEGKVA 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507083921 167 FQELLRIVSDIRVASLLAGKKGLL-----HVHLGNLPEGMS-QLIELC-DAGIPIH-HISPTHVARTaplfEQAIAFahr 238
Cdd:cd01317 158 SRLGLPGIPPEAETIMVARDLELAeatgaRVHFQHLSTARSlELIRKAkAKGLPVTaEVTPHHLLLD----DEALES--- 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507083921 239 gghidvTSGGSRFMP----QE--QAILHALEAQVpadrIT-ISSDgngSVPRFNAQGIVEGLSAAPVAGNL-NLLP---- 306
Cdd:cd01317 231 ------YDTNAKVNPplrsEEdrEALIEALKDGT----IDaIASD---HAPHTDEEKDLPFAEAPPGIIGLeTALPllwt 297
|
330 340 350 360
....*....|....*....|....*....|....*....|....*.
gi 507083921 307 RLIDVG-IPVPQAIAMLTANVARSLGISGGVLCAGERADICVLNDD 351
Cdd:cd01317 298 LLVKGGlLTLPDLIRALSTNPAKILGLPPGRLEVGAPADLVLFDPD 343
|
|
| PhnM |
cd01306 |
PhnM is believed to be a subunit of the membrane associated C-P lyase complex. C-P lyase is ... |
310-357 |
1.98e-04 |
|
PhnM is believed to be a subunit of the membrane associated C-P lyase complex. C-P lyase is thought to catalyze the direct cleavage of inactivated C-P bonds to yield inorganic phosphate and the corresponding hydrocarbons. It is responsible for cleavage of alkylphosphonates, which are utilized as sole phosphorus sources by many bacteria.
Pssm-ID: 238631 Cd Length: 325 Bit Score: 43.04 E-value: 1.98e-04
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 507083921 310 DVGIPVPQAIAMLTANVARSLGISG-GVLCAGERADICVLNDDLSLAHL 357
Cdd:cd01306 270 LGGWSLPEAVALVSANPARAVGLTDrGSIAPGKRADLILVDDMDGVPVV 318
|
|
| PRK09060 |
PRK09060 |
dihydroorotase; Validated |
3-63 |
2.52e-04 |
|
dihydroorotase; Validated
Pssm-ID: 181632 [Multi-domain] Cd Length: 444 Bit Score: 42.98 E-value: 2.52e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 507083921 3 TLLTNARVFSPEDLGLCSLLIHADRIVAVEKDISlfDGVDEVIDCHGKWVIPGIIDQHVHL 63
Cdd:PRK09060 7 LILKGGTVVNPDGEGRADIGIRDGRIAAIGDLSG--ASAGEVIDCRGLHVLPGVIDSQVHF 65
|
|
| PLN02795 |
PLN02795 |
allantoinase |
3-94 |
3.02e-04 |
|
allantoinase
Pssm-ID: 178392 [Multi-domain] Cd Length: 505 Bit Score: 42.84 E-value: 3.02e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507083921 3 TLLTNARVFSPEDLGLCSLLIHADRIVAV--EKDISLFDGVDEVIDcHGKWVI-PGIIDQHVHLTGGGGE--AGFASRTP 77
Cdd:PLN02795 46 FVLYSKRVVTPAGVIPGAVEVEGGRIVSVtkEEEAPKSQKKPHVLD-YGNAVVmPGLIDVHVHLNEPGRTewEGFPTGTK 124
|
90
....*....|....*..
gi 507083921 78 AVKLrdliqAGITTVVG 94
Cdd:PLN02795 125 AAAA-----GGITTLVD 136
|
|
| PLN02942 |
PLN02942 |
dihydropyrimidinase |
18-63 |
4.47e-04 |
|
dihydropyrimidinase
Pssm-ID: 178530 Cd Length: 486 Bit Score: 42.14 E-value: 4.47e-04
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 507083921 18 LCSLLIHADRIVAVEKDISLFDGVdEVIDCHGKWVIPGIIDQHVHL 63
Cdd:PLN02942 22 LADVYVEDGIIVAVAPNLKVPDDV-RVIDATGKFVMPGGIDPHTHL 66
|
|
| PRK07627 |
PRK07627 |
dihydroorotase; Provisional |
295-351 |
5.06e-04 |
|
dihydroorotase; Provisional
Pssm-ID: 181059 [Multi-domain] Cd Length: 425 Bit Score: 41.97 E-value: 5.06e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 507083921 295 AAPVAGNLNLLPRLI-----DVGIPVPQAIAMLTANVARSLGISGGVLCAGERADICVLNDD 351
Cdd:PRK07627 322 ATPGATGLELLLPLTlkwadEAKVPLARALARITSAPARVLGLPAGRLAEGAPADLCVFDPD 383
|
|
| PRK06038 |
PRK06038 |
N-ethylammeline chlorohydrolase; Provisional |
4-357 |
6.46e-04 |
|
N-ethylammeline chlorohydrolase; Provisional
Pssm-ID: 180363 [Multi-domain] Cd Length: 430 Bit Score: 41.66 E-value: 6.46e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507083921 4 LLTNARVFSPE--DLGLCSLLIHADRIVAVEKDISlfDGVDEVIDCHGKWVIPGIIDQHVHLtGGGGEAGFASRTP-AVK 80
Cdd:PRK06038 5 IIKNAYVLTMDagDLKKGSVVIEDGTITEVSESTP--GDADTVIDAKGSVVMPGLVNTHTHA-AMTLFRGYADDLPlAEW 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507083921 81 LRDLI---QAGIT-------TVVGVL-----GTDAISrspkDLYAKM----QSLNLEGLRAFMHTGAYAVPSP-TITRSI 140
Cdd:PRK06038 82 LNDHIwpaEAKLTaedvyagSLLACLemiksGTTSFA----DMYFYMdevaKAVEESGLRAALSYGMIDLGDDeKGEAEL 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507083921 141 RDDMTFIPAILG-----VKIALADHrGSYPSFQELLRIVSDirvaslLAGKKGL-LHVHLGNLPEGMSQLIELcdagipi 214
Cdd:PRK06038 158 KEGKRFVKEWHGaadgrIKVMYGPH-APYTCSEEFLSKVKK------LANKDGVgIHIHVLETEAELNQMKEQ------- 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507083921 215 HHISPTHVARTAPLFEQAIAFAH----RGGHIDVTSGgsrfmpQEQAILHAleaqvPADRITISSdGNGSVPRFNAQGIV 290
Cdd:PRK06038 224 YGMCSVNYLDDIGFLGPDVLAAHcvwlSDGDIEILRE------RGVNVSHN-----PVSNMKLAS-GIAPVPKLLERGVN 291
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507083921 291 EGLSAAPVAGNLNL----------LPRLIDVG----IPVPQAIAMLTANVARSLGISGGVLCAGERADICVLndDLSLAH 356
Cdd:PRK06038 292 VSLGTDGCASNNNLdmfeemktaaLLHKVNTMdptaLPARQVLEMATVNGAKALGINTGMLKEGYLADIIIV--DMNKPH 369
|
.
gi 507083921 357 L 357
Cdd:PRK06038 370 L 370
|
|
| PRK09229 |
PRK09229 |
N-formimino-L-glutamate deiminase; Validated |
323-374 |
1.68e-03 |
|
N-formimino-L-glutamate deiminase; Validated
Pssm-ID: 236420 [Multi-domain] Cd Length: 456 Bit Score: 40.22 E-value: 1.68e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 507083921 323 TANVARSLGISGGVLCAGERADICVLN-DDLSLA----------HLFAAGKPLLRD----GECLVTG 374
Cdd:PRK09229 367 LAGGAQALGRAIGGLAVGARADLVVLDlDHPALAgregdalldrWVFAGGDAAVRDvwvaGRWVVRD 433
|
|
| Amidohydro_3 |
pfam07969 |
Amidohydrolase family; |
43-79 |
4.68e-03 |
|
Amidohydrolase family;
Pssm-ID: 400360 [Multi-domain] Cd Length: 464 Bit Score: 39.05 E-value: 4.68e-03
10 20 30
....*....|....*....|....*....|....*..
gi 507083921 43 EVIDCHGKWVIPGIIDQHVHLTGGGGEAGFASRTPAV 79
Cdd:pfam07969 1 EVIDAKGRLVLPGFVDPHTHLDGGGLNLRELRLPDVL 37
|
|
| PRK08203 |
PRK08203 |
hydroxydechloroatrazine ethylaminohydrolase; Reviewed |
21-63 |
4.69e-03 |
|
hydroxydechloroatrazine ethylaminohydrolase; Reviewed
Pssm-ID: 236184 [Multi-domain] Cd Length: 451 Bit Score: 38.68 E-value: 4.69e-03
10 20 30 40
....*....|....*....|....*....|....*....|...
gi 507083921 21 LLIHADRIVAVEKDISLFDGVDEVIDCHGKWVIPGIIDQHVHL 63
Cdd:PRK08203 26 LVVEGGRIVEVGPGGALPQPADEVFDARGHVVTPGLVNTHHHF 68
|
|
| PRK06189 |
PRK06189 |
allantoinase; Provisional |
4-91 |
5.23e-03 |
|
allantoinase; Provisional
Pssm-ID: 235732 [Multi-domain] Cd Length: 451 Bit Score: 38.53 E-value: 5.23e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507083921 4 LLTNARVFSPEDLGLCSLLIHADRIVAVEKDISlfDGVDEVIDCHGKWVIPGIIDQHVHLTGGGGE--AGFASRTPAvkl 81
Cdd:PRK06189 6 IIRGGKVVTPEGVYRADIGIKNGKIAEIAPEIS--SPAREIIDADGLYVFPGMIDVHVHFNEPGRThwEGFATGSAA--- 80
|
90
....*....|
gi 507083921 82 rdLIQAGITT 91
Cdd:PRK06189 81 --LAAGGCTT 88
|
|
| Amidohydro_3 |
pfam07969 |
Amidohydrolase family; |
309-352 |
7.45e-03 |
|
Amidohydrolase family;
Pssm-ID: 400360 [Multi-domain] Cd Length: 464 Bit Score: 38.28 E-value: 7.45e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 507083921 309 IDVGIPVPQAIAMLTANVARSLGISG--GVLCAGERADICVLNDDL 352
Cdd:pfam07969 395 PDEELSLEEALALYTSGPAKALGLEDrkGTLGVGKDADLVVLDDDP 440
|
|
| ureC |
PRK13308 |
urease subunit alpha; Reviewed |
4-94 |
9.13e-03 |
|
urease subunit alpha; Reviewed
Pssm-ID: 183965 [Multi-domain] Cd Length: 569 Bit Score: 38.15 E-value: 9.13e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507083921 4 LLTNARVFSPEdLGL--CSLLIHADRIVAVEK--DISLFDGVDE---------VIDCHGKWVIPGIIDQHVHL-TGGGGE 69
Cdd:PRK13308 71 VLCNVTVIDPV-LGIvkGDIGIRDGRIVGIGKagNPDIMDGVDPrlvvgpgtdVRPAEGLIATPGAIDVHVHFdSAQLVD 149
|
90 100
....*....|....*....|....*
gi 507083921 70 AGFASrtpavklrdliqaGITTVVG 94
Cdd:PRK13308 150 HALAS-------------GITTMLG 161
|
|
| |
