|
Name |
Accession |
Description |
Interval |
E-value |
| Isoaspartyl-dipeptidase |
cd01308 |
Isoaspartyl dipeptidase hydrolyzes the beta-L-isoaspartyl linkages in dipeptides, as part of ... |
2-380 |
1.13e-148 |
|
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: 425.65 E-value: 1.13e-148
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2728837251 2 FKLIKNSILYAPESFGKKDILICGEKIALISDKIS-PNLPDVEIIDANGKTVTPGFIDQHVHITGAGGKHGFQSLTPEIA 80
Cdd:cd01308 1 FTLIKNAEVYAPEYLGKKDILIAGGKILAIEDQLNlPGYENVTVVDLHGKILVPGFIDQHVHIIGGGGEGGPSTRTPEVT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2728837251 81 LTEFITCGTTTVVGLLGTDGATKSLKALYAKTKALDNEGITAYMLTSYFGLPPITMMGSVLEDMLFIDKVLGCK-VAISD 159
Cdd:cd01308 81 LSDLTTAGVTTVVGCLGTDGISRSMEDLLAKARALEEEGITCFVYTGSYEVPTRTITGSIRKDLLLIDKVIGVGeIAISD 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2728837251 160 ERSSFPTAKELLSILKDVHVGGLTSGKKGIMHVHLGALKTNMQLLLDLVEQYDFPIRNISPTHVGRTAPLFEEAIRFAKL 239
Cdd:cd01308 161 HRSSQPTVEELARIAAEARVGGLLGGKAGIVHIHLGDGKRALSPIFELIEETEIPITQFLPTHINRTAPLFEQGVEFAKM 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2728837251 240 GGMIDITTGGTKFD------EPYKQVLYALDKGVPIENMTFSSDGNAGLGVNDKDGNLVGFKKAPIDLNYKQVQKLVKEA 313
Cdd:cd01308 241 GGTIDLTSSIDPQFrkegevRPSEALKRLLEQGVPLERITFSSDGNGSLPKFDENGNLVGLGVGSVDTLLREVREAVKCG 320
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2728837251 314 NMPIGQAIQLVTSGPARNLSLTQKGRVFAGGDADLCLFDSNFNLTDVIARGRVMMKEKEILVRGSFE 380
Cdd:cd01308 321 DIPLEVALRVITSNVARILKLRKKGEIQPGFDADLVILDKDLDINSVIAKGQIMVRNGKLLVKGTFE 387
|
|
| isoAsp_dipep |
TIGR01975 |
isoaspartyl dipeptidase IadA; The L-isoaspartyl derivative of Asp arises non-enzymatically ... |
2-380 |
3.75e-124 |
|
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: 363.34 E-value: 3.75e-124
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2728837251 2 FKLIKNSILYAPESFGKKDILICGEKIALISDKISP--NLPDVEII-DANGKTVTPGFIDQHVHITGAGGKHGFQSLTPE 78
Cdd:TIGR01975 1 FTLLKGAEVYAPEYIGKKDILIANDKIIAIADEIPStkDFVPNCVVvGLEGMIAVPGFIDQHVHIIGGGGEGGPTTRTPE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2728837251 79 IALTEFITCGTTTVVGLLGTDGATKSLKALYAKTKALDNEGITAYMLTSYFGLPPITMMGSVLEDMLFIDKVLGC-KVAI 157
Cdd:TIGR01975 81 LTLSDITKGGVTTVVGLLGTDGITRHMESLLAKARALEEEGISCYMLTGAYHVPSRTITGSVESDLLLIDKVIGVgEIAI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2728837251 158 SDERSSFPTAKELLSILKDVHVGGLTSGKKGIMHVHLGALKTNMQLLLDLVEQYDFPIRNISPTHVGRTAPLFEEAIRFA 237
Cdd:TIGR01975 161 SDHRSAQPTVEHLTNMAAEARVGGLLGGKPGIVNFHVGDSKRALQPIYELVENTDVPITQFLPTHINRNVPLFEAGLEFA 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2728837251 238 KLGGMIDITtggTKFDEPYKQ---------VLYALDKGVPIENMTFSSDGNAGLGVNDKDGNLVGFKKAPIDLNYKQVQK 308
Cdd:TIGR01975 241 KKGGTIDLT---SSIDPQFRKegevapaegIKKALEAGVPLEKVTFSSDGNGSQPFFDENGELTGLGVGSFETLFEEVRE 317
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2728837251 309 LVKEANMPIGQAIQLVTSGPARNLSLTQKGRVFAGGDADLCLFDSNFNLTDVIARGRVMMKEKEILVRGSFE 380
Cdd:TIGR01975 318 AVKDGDVPLEKALRVITSNVAGVLNLTGKGEISPGNDADLVVLDPDLRIHSVIARGKLMVKDGKACVKGTFE 389
|
|
| NagA |
cd00854 |
N-acetylglucosamine-6-phosphate deacetylase, NagA, catalyzes the hydrolysis of the N-acetyl ... |
3-364 |
1.64e-17 |
|
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: 83.01 E-value: 1.64e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2728837251 3 KLIKNSILYAPESFGKKDILICGEKIALISDKISPNlPDVEIIDANGKTVTPGFIDQHVHitGAGGkHGFQSLTPEIALT 82
Cdd:cd00854 1 LIIKNARILTPGGLEDGAVLVEDGKIVAIGPEDELE-EADEIIDLKGQYLVPGFIDIHIH--GGGG-ADFMDGTAEALKT 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2728837251 83 --EFI-TCGTTTVVGLLGTDGATKSLKALyAKTKALDNEGITAymltsyfglppitmmgsvledmlfidKVLGckvaisd 159
Cdd:cd00854 77 iaEALaKHGTTSFLPTTVTAPPEEIAKAL-AAIAEAIAEGQGA--------------------------EILG------- 122
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2728837251 160 erssfptakellsilkdVHVGG--LTSGKKGIMHVHLgALKTNMQLLLDLVEQYDFPIR--NISPTH------------- 222
Cdd:cd00854 123 -----------------IHLEGpfISPEKKGAHPPEY-LRAPDPEELKKWLEAAGGLIKlvTLAPELdgalelirylver 184
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2728837251 223 -----VGRTAPLFEEAIRFAKLG-------------------GMI-------DITTG----GTKFDEPYKQVLYALdkgV 267
Cdd:cd00854 185 giivsIGHSDATYEQAVAAFEAGathvthlfnamsplhhrepGVVgaalsddDVYAEliadGIHVHPAAVRLAYRA---K 261
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2728837251 268 PIENMTFSSDGNAGLGVND-------------------KDGNLVGfkkAPIDLNyKQVQKLVKEANMPIGQAIQLVTSGP 328
Cdd:cd00854 262 GADKIVLVTDAMAAAGLPDgeyelggqtvtvkdgvarlADGTLAG---STLTMD-QAVRNMVKWGGCPLEEAVRMASLNP 337
|
410 420 430
....*....|....*....|....*....|....*..
gi 2728837251 329 ARNLSLT-QKGRVFAGGDADLCLFDSNFNLTDVIARG 364
Cdd:cd00854 338 AKLLGLDdRKGSLKPGKDADLVVLDDDLNVKATWING 374
|
|
| HutI |
COG1228 |
Imidazolonepropionase or related amidohydrolase [Secondary metabolites biosynthesis, transport ... |
20-366 |
1.00e-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: 1.00e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2728837251 20 DILICGEKIALISDKISPNLP-DVEIIDANGKTVTPGFIDQHVHITGAGGKHGFQSLTPEIALT------------EFIT 86
Cdd:COG1228 30 TVLVEDGKIAAVGPAADLAVPaGAEVIDATGKTVLPGLIDAHTHLGLGGGRAVEFEAGGGITPTvdlvnpadkrlrRALA 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2728837251 87 CGTTTVVGLLGTDGAtkslkalyakTKALDNEGITAYMLTS--YFGLPPITMMGSV-------LEDML---FIDKVLGCK 154
Cdd:COG1228 110 AGVTTVRDLPGGPLG----------LRDAIIAGESKLLPGPrvLAAGPALSLTGGAhargpeeARAALrelLAEGADYIK 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2728837251 155 VAISDERSSFP---------TAKELLSILKdVHVGGLTS-------GKKGIMHVHLGALKTnmqllLDLVEQYDfpirni 218
Cdd:COG1228 180 VFAEGGAPDFSleelraileAAHALGLPVA-AHAHQADDirlaveaGVDSIEHGTYLDDEV-----ADLLAEAG------ 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2728837251 219 sPTHVGRTAPLFEEAIRFAKLGGMIDITTGgtkFDEPYKQVLYALDKGVPIenmTFSSDGNAGlgvndkdgnlvgfkKAP 298
Cdd:COG1228 248 -TVVLVPTLSLFLALLEGAAAPVAAKARKV---REAALANARRLHDAGVPV---ALGTDAGVG--------------VPP 306
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2728837251 299 IDLNYKQVQKLVKeANMPIGQAIQLVTSGPARNLSLTQK-GRVFAGGDADLCLFDSNfNLTD---------VIARGRV 366
Cdd:COG1228 307 GRSLHRELALAVE-AGLTPEEALRAATINAAKALGLDDDvGSLEPGKLADLVLLDGD-PLEDiayledvraVMKDGRV 382
|
|
| AllB |
COG0044 |
Dihydroorotase or related cyclic amidohydrolase [Nucleotide transport and metabolism]; ... |
4-379 |
2.32e-15 |
|
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: 77.05 E-value: 2.32e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2728837251 4 LIKNSILYAPESFGKKDILICGEKIALISDKISPnLPDVEIIDANGKTVTPGFIDQHVHITGAGGKH--GFQSLTpeial 81
Cdd:COG0044 1 LIKNGRVVDPGGLERADVLIEDGRIAAIGPDLAA-PEAAEVIDATGLLVLPGLIDLHVHLREPGLEHkeDIETGT----- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2728837251 82 tefITC---GTTTVVGLLGTDGATKSLKALYAKTKALDNEGITAYMLtsYFGlppITM-MGSVLEDMLFIDKvLGCkVAI 157
Cdd:COG0044 75 ---RAAaagGVTTVVDMPNTNPVTDTPEALEFKLARAEEKALVDVGP--HGA---LTKgLGENLAELGALAE-AGA-VAF 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2728837251 158 -----SDERSSFPTAKELLSILKDVH-VGGLTS--------GKKGIMHVHLGALKTNM------------QLLLDLVEQY 211
Cdd:COG0044 145 kvfmgSDDGNPVLDDGLLRRALEYAAeFGALVAvhaedpdlIRGGVMNEGKTSPRLGLkgrpaeaeeeavARDIALAEET 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2728837251 212 DFPIrnisptHVGR--TAplfE--EAIRFAKLGGmIDIT----------------TGGTKF-------DEPYKQVLY-AL 263
Cdd:COG0044 225 GARL------HIVHvsTA---EavELIREAKARG-LPVTaevcphhltltdedleRYGTNFkvnpplrTEEDREALWeGL 294
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2728837251 264 DKGVpIEnmTFSSDgNAGLGVNDKDGNlvgFKKAP---------IDLNYkqvQKLVKEANMPIGQAIQLVTSGPARNLSL 334
Cdd:COG0044 295 ADGT-ID--VIATD-HAPHTLEEKELP---FAEAPngipgletaLPLLL---TELVHKGRLSLERLVELLSTNPARIFGL 364
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2728837251 335 TQKGRVFAGGDADLCLFD-------SNFNL------------------TDVIARGRVMMKEKEIL--VRGSF 379
Cdd:COG0044 365 PRKGRIAVGADADLVLFDpdaewtvTAEDLhskskntpfegreltgrvVATIVRGRVVYEDGEVVgePRGRF 436
|
|
| PRK09237 |
PRK09237 |
amidohydrolase/deacetylase family metallohydrolase; |
4-360 |
3.61e-14 |
|
amidohydrolase/deacetylase family metallohydrolase;
Pssm-ID: 236423 [Multi-domain] Cd Length: 380 Bit Score: 72.96 E-value: 3.61e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2728837251 4 LIKNSILYAPESF--GKKDILICGEKIALISDKISPNlPDVEIIDANGKTVTPGFIDQHVHItgaggkhgFQSLTP---- 77
Cdd:PRK09237 2 LLRGGRVIDPANGidGVIDIAIEDGKIAAVAGDIDGS-QAKKVIDLSGLYVSPGWIDLHVHV--------YPGSTPygde 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2728837251 78 --EIAltefITCGTTTVVGlLGTDGAtKSLKALYAKTKALDNEGITAYMLTSYFGLppitMMGSVLEDMLFIDKVLGCKV 155
Cdd:PRK09237 73 pdEVG----VRSGVTTVVD-AGSAGA-DNFDDFRKLTIEASKTRVLAFLNISRIGL----LAQDELADLEDIDADAVAEA 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2728837251 156 AISDerssfptaKELLSILKdVHVGGLTSGKKGI----------------MHVHLGALKTNMQLLLDLVEQYD------- 212
Cdd:PRK09237 143 VKRN--------PDFIVGIK-ARMSSSVVGDNGIeplelakaiaaeanlpLMVHIGNPPPSLEEILELLRPGDilthcfn 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2728837251 213 -FPIRNISPThvGRTAPLFEEAIrfaKLGGMIDITTGGTKFDepYKQVLYALDKGVPIEnmTFSSDGNAGlgvNDKDGnl 291
Cdd:PRK09237 214 gKPNRILDED--GELRPSVLEAL---ERGVRLDVGHGTASFS--FKVAEAAIAAGILPD--TISTDIYCR---NRING-- 279
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2728837251 292 vgfkkaPIdlnYKQVQKLVK--EANMPIGQAIQLVTSGPARNLSLTQKGRVFAGGDADLCLFD---SNFNLTDV 360
Cdd:PRK09237 280 ------PV---YSLATVMSKflALGMPLEEVIAAVTKNAADALRLPELGRLQVGSDADLTLFTlkdGPFTLTDS 344
|
|
| Met_dep_hydrolase_C |
cd01309 |
Metallo-dependent hydrolases, subgroup C is part of the superfamily of metallo-dependent ... |
27-367 |
1.15e-12 |
|
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: 68.49 E-value: 1.15e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2728837251 27 KIALISDKISPnLPDVEIIDANGKTVTPGFIDQHVHITGAGGKHGFQ---------SLTPEI-----------ALTEFIT 86
Cdd:cd01309 3 KIVAVGAEITT-PADAEVIDAKGKHVTPGLIDAHSHLGLDEEGGVREtsdaneetdPVTPHVraidginpddeAFKRARA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2728837251 87 CGTTTVVGLLGTD---GATKSLKALYAKT---KALDNE-------GITAYMLTSYFGLPPITMMGSVLEdmlfidkvlgc 153
Cdd:cd01309 82 GGVTTVQVLPGSAnliGGQGVVIKTDGGTiedMFIKAPaglkmalGENPKRVYGGKGKEPATRMGVAAL----------- 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2728837251 154 kvaisdERSSFPTAKELLSILKDVHVGGLTSGKKGI-MHVHLGALKTNMQL------------LLDLVEQYDFPIRnisP 220
Cdd:cd01309 151 ------LRDAFIKAQEYGRKYDLGKNAKKDPPERDLkLEALLPVLKGEIPVrihahraddiltAIRIAKEFGIKIT---I 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2728837251 221 THVGRTAPLFEEaIRFAKLGGMIDITTGGTKFDEP----YKQVLYALDKGVPieNMTFSSDGNAGLGVNdkdgnlvgfkk 296
Cdd:cd01309 222 EHGAEGYKLADE-LAKHGIPVIYGPTLTLPKKVEEvndaIDTNAYLLKKGGV--AFAISSDHPVLNIRN----------- 287
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2728837251 297 apidLNYkQVQKLVKEAnMPIGQAIQLVTSGPARNLSLTQK-GRVFAGGDADLCLFDSN-FNLT----DVIARGRVM 367
Cdd:cd01309 288 ----LNL-EAAKAVKYG-LSYEEALKAITINPAKILGIEDRvGSLEPGKDADLVVWNGDpLEPTskpeQVYIDGRLV 358
|
|
| NagA |
COG1820 |
N-acetylglucosamine-6-phosphate deacetylase [Carbohydrate transport and metabolism]; |
4-365 |
1.24e-12 |
|
N-acetylglucosamine-6-phosphate deacetylase [Carbohydrate transport and metabolism];
Pssm-ID: 441425 [Multi-domain] Cd Length: 373 Bit Score: 68.59 E-value: 1.24e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2728837251 4 LIKNSILYAPESF-GKKDILICGEKIALISDKISPnlpDVEIIDANGKTVTPGFIDQHVHitGAGGkHGFQSLTPE--IA 80
Cdd:COG1820 1 AITNARIFTGDGVlEDGALLIEDGRIAAIGPGAEP---DAEVIDLGGGYLAPGFIDLHVH--GGGG-VDFMDGTPEalRT 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2728837251 81 LTEFI-TCGTTTVVGLLGTDGATKSLKALyAKTKALDNEGITAYML------------------TSYFGLPPITMMGSVL 141
Cdd:COG1820 75 IARAHaRHGTTSFLPTTITAPPEDLLRAL-AAIAEAIEQGGGAGILgihlegpflspekkgahpPEYIRPPDPEELDRLL 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2728837251 142 EdmLFIDKVLgcKVAISDERssfPTAKELLSILKD--VHV-GGLTSG---------KKGIMHV-HL-------------- 194
Cdd:COG1820 154 E--AAGGLIK--LVTLAPEL---PGALEFIRYLVEagVVVsLGHTDAtyeqaraafEAGATHVtHLfnamsplhhrepgv 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2728837251 195 -GALKTNMQLLL----DLVeqydfpirnisptHVgrtAPlfeEAIRFAK----LGGMIDIT----TGGTKFDEpykqvlY 261
Cdd:COG1820 227 vGAALDDDDVYAeliaDGI-------------HV---HP---AAVRLALrakgPDRLILVTdamaAAGLPDGE------Y 281
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2728837251 262 ALDkGVPIEnmtfSSDGNAGLgvndKDGNLVGfkkAPIDLNyKQVQKLVKEANMPIGQAIQLVTSGPARNLSLT-QKGRV 340
Cdd:COG1820 282 ELG-GLEVT----VKDGVARL----ADGTLAG---STLTMD-DAVRNLVEWTGLPLEEAVRMASLNPARALGLDdRKGSI 348
|
410 420
....*....|....*....|....*
gi 2728837251 341 FAGGDADLCLFDSNFNLTDVIARGR 365
Cdd:COG1820 349 APGKDADLVVLDDDLNVRATWVGGE 373
|
|
| AdeC |
COG1001 |
Adenine deaminase [Nucleotide transport and metabolism]; |
20-375 |
8.89e-12 |
|
Adenine deaminase [Nucleotide transport and metabolism];
Pssm-ID: 440625 [Multi-domain] Cd Length: 559 Bit Score: 66.28 E-value: 8.89e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2728837251 20 DILICGEKIALISDKISPNLpdvEIIDANGKTVTPGFIDQHVHItgaggkhgfQS--LTPEialtEF----ITCGTTTVV 93
Cdd:COG1001 26 DIAIAGGRIAGVGDYIGEAT---EVIDAAGRYLVPGFIDGHVHI---------ESsmVTPA----EFaravLPHGTTTVI 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2728837251 94 -------GLLGTDGatksLKALYAKTKALDnegitaymLTSYFGLP---PIT----MMGSVL--EDML-FID--KVLGck 154
Cdd:COG1001 90 adpheiaNVLGLEG----VRYMLEAAEGLP--------LDIFVMLPscvPATpgleTAGAVLgaEDLAeLLDhpRVIG-- 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2728837251 155 VAisdERSSFP----TAKELLSILKDvhvgGLTSGKkgimHV--HlGALKTNMQLlldlveqydfpirN------ISPTH 222
Cdd:COG1001 156 LG---EVMNFPgvlnGDPRMLAKIAA----ALAAGK----VIdgH-APGLSGKDL-------------NayaaagIRSDH 210
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2728837251 223 VGRTAplfEEAIrfAKLG-GM-IDITTGGTKFDepykqvLYALDKGVPIEN---MTFSSDgnaglgvnDKDgnlvgfkka 297
Cdd:COG1001 211 ECTTA---EEAL--EKLRrGMyVMIREGSAAKD------LPALLPAVTELNsrrCALCTD--------DRH--------- 262
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2728837251 298 PIDL------NYkQVQKLVkEANMPIGQAIQLVTSGPARNLSLTQKGRVFAGGDADLCLFDS--NFNLTDVIARGRVMMK 369
Cdd:COG1001 263 PDDLleeghiDH-VVRRAI-ELGLDPVTAIQMATLNAAEHFGLKDLGAIAPGRRADIVLLDDleDFKVEKVYADGKLVAE 340
|
....*.
gi 2728837251 370 EKEILV 375
Cdd:COG1001 341 DGKLLV 346
|
|
| COG3964 |
COG3964 |
Predicted amidohydrolase [General function prediction only]; |
4-360 |
1.17e-11 |
|
Predicted amidohydrolase [General function prediction only];
Pssm-ID: 443164 [Multi-domain] Cd Length: 376 Bit Score: 65.57 E-value: 1.17e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2728837251 4 LIKNSILYAPES--FGKKDILICGEKIALISDKISPNlPDVEIIDANGKTVTPGFIDQHVHItgaggkhgFQSLTP---- 77
Cdd:COG3964 3 LIKGGRVIDPANgiDGVMDIAIKDGKIAAVAKDIDAA-EAKKVIDASGLYVTPGLIDLHTHV--------FPGGTDygvd 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2728837251 78 --EIAltefITCGTTTVVGlLGTDGAtKSLKALY------AKTKaldnegITAYMLTSYFGLppitMMGSVLEDMLFIDK 149
Cdd:COG3964 74 pdGVG----VRSGVTTVVD-AGSAGA-ANFDGFRkyvidpSKTR------VLAFLNISGIGL----VGGNELQDLDDIDP 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2728837251 150 -------------VLGCKVAISderSSFPTAKELLSILKDVHVGGLTsgKKGIMhVHLGALKTNMQLLLDLVEQYD---- 212
Cdd:COG3964 138 dataaaaeanpdfIVGIKVRAS---KGVVGDNGIEPLKRAKEAAKEA--GLPLM-VHIGNPPPPLDEVLDLLRPGDilth 211
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2728837251 213 ----FPIRNISPThvGRTAPLFEEA----IRFaklggmiDITTGGTKFDepYKQVLYALDKG-VPienMTFSSDGNAglg 283
Cdd:COG3964 212 cfngKPNGILDED--GKVRPSVREArkrgVLF-------DVGHGGASFS--FKVAEPAIAQGfLP---DTISTDLHT--- 274
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2728837251 284 vndkdGNLvgfkKAPIdlnYKQVQKLVK--EANMPIGQAIQLVTSGPARNLSLTQKGRVFAGGDADLCLF---DSNFNLT 358
Cdd:COG3964 275 -----RNM----NGPV---FDLATVMSKflALGMPLEEVIAAVTWNPARAIGLPELGTLSVGADADITIFdlrEGPFGFT 342
|
..
gi 2728837251 359 DV 360
Cdd:COG3964 343 DS 344
|
|
| COG3653 |
COG3653 |
N-acyl-D-aspartate/D-glutamate deacylase [Secondary metabolites biosynthesis, transport and ... |
20-100 |
7.49e-11 |
|
N-acyl-D-aspartate/D-glutamate deacylase [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 442870 [Multi-domain] Cd Length: 528 Bit Score: 63.65 E-value: 7.49e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2728837251 20 DILICGEKIALISDKisPNLPDVEIIDANGKTVTPGFIDQHVHITGAggkhgfqsLTPEIALTEFITCGTTTVVglLGTD 99
Cdd:COG3653 23 DVAIKGGRIVAVGDL--AAAEAARVIDATGLVVAPGFIDIHTHYDLQ--------LLWDPRLEPSLRQGVTTVV--MGNC 90
|
.
gi 2728837251 100 G 100
Cdd:COG3653 91 G 91
|
|
| pyrC |
PRK09357 |
dihydroorotase; Validated |
1-62 |
1.34e-10 |
|
dihydroorotase; Validated
Pssm-ID: 236479 [Multi-domain] Cd Length: 423 Bit Score: 62.52 E-value: 1.34e-10
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2728837251 1 MFKLIKNSILYAPESFG-KKDILICGEKIALISDKISPnlPDVEIIDANGKTVTPGFIDQHVH 62
Cdd:PRK09357 1 MMILIKNGRVIDPKGLDeVADVLIDDGKIAAIGENIEA--EGAEVIDATGLVVAPGLVDLHVH 61
|
|
| D-HYD |
cd01314 |
D-hydantoinases (D-HYD) also called dihydropyrimidases (DHPase) and related proteins; DHPases ... |
3-93 |
2.35e-10 |
|
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: 61.85 E-value: 2.35e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2728837251 3 KLIKNSILYAPESFGKKDILICGEKIALISDKISPnLPDVEIIDANGKTVTPGFIDQHVHI----TGAGGKHGFQSLTpE 78
Cdd:cd01314 1 LIIKNGTIVTADGSFKADILIEDGKIVAIGPNLEA-PGGVEVIDATGKYVLPGGIDPHTHLelpfMGTVTADDFESGT-R 78
|
90
....*....|....*
gi 2728837251 79 IALTEfitcGTTTVV 93
Cdd:cd01314 79 AAAAG----GTTTII 89
|
|
| metallo-dependent_hydrolases |
cd01292 |
Superfamily of metallo-dependent hydrolases (also called amidohydrolase superfamily) is a ... |
56-330 |
4.12e-10 |
|
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: 60.04 E-value: 4.12e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2728837251 56 FIDQHVHI--TGAGGKHGFQSL-------------TPEIALTEFITCGTTTVVGLLGTDGATKSLKALYAK-TKALDNEG 119
Cdd:cd01292 1 FIDTHVHLdgSALRGTRLNLELkeaeelspedlyeDTLRALEALLAGGVTTVVDMGSTPPPTTTKAAIEAVaEAARASAG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2728837251 120 ITAYMLTSYFGLPPITMMGSVLEDMLFIDKV-------LGCKVAISDERSSFPTAKELLSILKDVHVggltsgkkgIMHV 192
Cdd:cd01292 81 IRVVLGLGIPGVPAAVDEDAEALLLELLRRGlelgavgLKLAGPYTATGLSDESLRRVLEEARKLGL---------PVVI 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2728837251 193 HLGALKTNMQLLLDLVeQYDFPIRNISPTHVGRTAPlfEEAIRFAKLGGMIDITTGGTKFDEPYKQVLY----ALDKGVP 268
Cdd:cd01292 152 HAGELPDPTRALEDLV-ALLRLGGRVVIGHVSHLDP--ELLELLKEAGVSLEVCPLSNYLLGRDGEGAEalrrLLELGIR 228
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2728837251 269 IenmTFSSDGNAGLGvndkDGNLvgfkkapidLNYKQVQKLVKEANMPIGQAIQLVTSGPAR 330
Cdd:cd01292 229 V---TLGTDGPPHPL----GTDL---------LALLRLLLKVLRLGLSLEEALRLATINPAR 274
|
|
| pyrC_multi |
TIGR00857 |
dihydroorotase, multifunctional complex type; In contrast to the homodimeric type of ... |
20-371 |
4.74e-09 |
|
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: 57.45 E-value: 4.74e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2728837251 20 DILICGEKIALISDKISPnlPDVEIIDANGKTVTPGFIDQHVHITGAGG--KHGFQSLTPEIALTefitcGTTTVVGLLG 97
Cdd:TIGR00857 7 DILVEGGRIKKIGKLRIP--PDAEVIDAKGLLVLPGFIDLHVHLRDPGEeyKEDIESGSKAAAHG-----GFTTVADMPN 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2728837251 98 TD----------------------------GATKSLKA-LYAKTKALDNEGITAYMLTSYFG-LPPITMMGSVLEDMLFI 147
Cdd:TIGR00857 80 TKppidtpetlewklqrlkkvslvdvhlygGVTQGNQGkELTEAYELKEAGAVGRMFTDDGSeVQDILSMRRALEYAAIA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2728837251 148 DK--VLGC--------------KVAISDERSSFPTAKELLSILKDVHVGGLTSGKKGIMHVhlgALKTNMQLLLDLVEQY 211
Cdd:TIGR00857 160 GVpiALHAedpdliyggvmhegPSAAQLGLPARPPEAEEVAVARLLELAKHAGCPVHICHI---STKESLELIVKAKSQG 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2728837251 212 DFPIRNISPTHVgrtapLFEEAiRFAKLGGMIdittggtKFDEPYKQV-----LYA--LDKGVPIenmtFSSDgNAGLGV 284
Cdd:TIGR00857 237 IKITAEVTPHHL-----LLSEE-DVARLDGNG-------KVNPPLREKedrlaLIEglKDGIIDI----IATD-HAPHTL 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2728837251 285 NDKdgnLVGFKKAP-----IDLNYKQVQKLVKEANMPIGQAIQLVTSGPARNLSLTQKGRVFAGGDADLCLFDsnFNLTD 359
Cdd:TIGR00857 299 EEK---TKEFAAAPpgipgLETALPLLLQLLVKGLISLKDLIRMLSINPARIFGLPDKGTLEEGNPADITVFD--LKKEW 373
|
410
....*....|..
gi 2728837251 360 VIARGRVMMKEK 371
Cdd:TIGR00857 374 TINAETFYSKAK 385
|
|
| PRK06189 |
PRK06189 |
allantoinase; Provisional |
4-74 |
5.48e-09 |
|
allantoinase; Provisional
Pssm-ID: 235732 [Multi-domain] Cd Length: 451 Bit Score: 57.40 E-value: 5.48e-09
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2728837251 4 LIKNSILYAPESFGKKDILICGEKIALISDKISPnlPDVEIIDANGKTVTPGFIDQHVHITGAGGKH--GFQS 74
Cdd:PRK06189 6 IIRGGKVVTPEGVYRADIGIKNGKIAEIAPEISS--PAREIIDADGLYVFPGMIDVHVHFNEPGRTHweGFAT 76
|
|
| L-HYD_ALN |
cd01315 |
L-Hydantoinases (L-HYDs) and Allantoinase (ALN); L-Hydantoinases are a member of the ... |
4-76 |
8.35e-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: 56.91 E-value: 8.35e-09
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2728837251 4 LIKNSILYAPESFGKKDILICGEKIALISDKIsPNLPDVEIIDANGKTVTPGFIDQHVHITGAGGKH--GFQSLT 76
Cdd:cd01315 3 VIKNGRVVTPDGVREADIAVKGGKIAAIGPDI-ANTEAEEVIDAGGLVVMPGLIDTHVHINEPGRTEweGFETGT 76
|
|
| PRK08323 |
PRK08323 |
phenylhydantoinase; Validated |
1-63 |
2.21e-08 |
|
phenylhydantoinase; Validated
Pssm-ID: 236240 [Multi-domain] Cd Length: 459 Bit Score: 55.56 E-value: 2.21e-08
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2728837251 1 MFKLIKNSILYAPESFGKKDILICGEKIAlisdKISPNLPDvEIIDANGKTVTPGFIDQHVHI 63
Cdd:PRK08323 1 MSTLIKNGTVVTADDTYKADVLIEDGKIA----AIGANLGD-EVIDATGKYVMPGGIDPHTHM 58
|
|
| YtcJ |
COG1574 |
Predicted amidohydrolase YtcJ [General function prediction only]; |
40-67 |
3.98e-08 |
|
Predicted amidohydrolase YtcJ [General function prediction only];
Pssm-ID: 441182 [Multi-domain] Cd Length: 535 Bit Score: 54.80 E-value: 3.98e-08
10 20
....*....|....*....|....*...
gi 2728837251 40 PDVEIIDANGKTVTPGFIDQHVHITGAG 67
Cdd:COG1574 52 PATEVIDLGGKTVLPGFIDAHVHLLGGG 79
|
|
| PRK02382 |
PRK02382 |
dihydroorotase; Provisional |
4-120 |
4.02e-08 |
|
dihydroorotase; Provisional
Pssm-ID: 179417 [Multi-domain] Cd Length: 443 Bit Score: 54.66 E-value: 4.02e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2728837251 4 LIKNSILYAPESFGKKDILICGEKIALISDKISPNLPDvEIIDANGKTVTPGFIDQHVHITGAGGKHGFQSLTPEIALte 83
Cdd:PRK02382 5 LLKDGRVYYNNSLQPRDVRIDGGKITAVGKDLDGSSSE-EVIDARGMLLLPGGIDVHVHFREPGYTHKETWYTGSRSA-- 81
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 2728837251 84 fITCGTTTVVGLLGT-----DGATKSLKALYAKTKALDNEGI 120
Cdd:PRK02382 82 -AAGGVTTVVDQPNTdpptvDGESFDEKAELAARKSIVDFGI 122
|
|
| PRK08204 |
PRK08204 |
hypothetical protein; Provisional |
18-93 |
4.51e-08 |
|
hypothetical protein; Provisional
Pssm-ID: 181288 [Multi-domain] Cd Length: 449 Bit Score: 54.62 E-value: 4.51e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2728837251 18 KKDILICGEKIALISDKISPnlPDVEIIDANGKTVTPGFIDQHVHI---------TGAGGKHGFQSL--------TPE-- 78
Cdd:PRK08204 23 RGDILIEGDRIAAVAPSIEA--PDAEVVDARGMIVMPGLVDTHRHTwqsvlrgigADWTLQTYFREIhgnlgpmfRPEdv 100
|
90 100
....*....|....*....|
gi 2728837251 79 -IA----LTEFITCGTTTVV 93
Cdd:PRK08204 101 yIAnllgALEALDAGVTTLL 120
|
|
| AdeC |
cd01295 |
Adenine deaminase (AdeC) directly deaminates adenine to form hypoxanthine. This reaction is ... |
46-368 |
1.04e-07 |
|
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: 53.38 E-value: 1.04e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2728837251 46 DANGKTVTPGFIDQHVHItgaggkhgFQSLTPEialTEFITC----GTTTVV-------GLLGTDGATKSLKAlyAKTKA 114
Cdd:cd01295 1 DAEGKYIVPGFIDAHLHI--------ESSMLTP---SEFAKAvlphGTTTVIadpheiaNVAGVDGIEFMLED--AKKTP 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2728837251 115 LDnegitaymltSYFGLP---PITMM---GSVL-----EDMLFIDKVLGckVAisdERSSFPtakellsilkdvhvgGLT 183
Cdd:cd01295 68 LD----------IFWMLPscvPATPFetsGAELtaediKELLEHPEVVG--LG---EVMDFP---------------GVI 117
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2728837251 184 SGKKGIMHVHLGALKTNMQL-----LLDLVEQYDFPIRNISPTHVGRTAplfEEAIRFAKLGGMIDITTGGTKFDEPykq 258
Cdd:cd01295 118 EGDDEMLAKIQAAKKAGKPVdghapGLSGEELNAYMAAGISTDHEAMTG---EEALEKLRLGMYVMLREGSIAKNLE--- 191
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2728837251 259 VLYALDKGVPIENMTFSSDgnaGLGVNDKDGNlvgfkkapIDLNYkQVQKLVkEANMPIGQAIQLVTSGPARNLSLTQKG 338
Cdd:cd01295 192 ALLPAITEKNFRRFMFCTD---DVHPDDLLSE--------GHLDY-IVRRAI-EAGIPPEDAIQMATINPAECYGLHDLG 258
|
330 340 350
....*....|....*....|....*....|..
gi 2728837251 339 RVFAGGDADLCLFDS--NFNLTDVIARGRVMM 368
Cdd:cd01295 259 AIAPGRIADIVILDDleNFNITTVLAKGIAVV 290
|
|
| DHOase_IIa |
cd01317 |
Dihydroorotase (DHOase), subgroup IIa; DHOases catalyze the reversible interconversion of ... |
41-352 |
1.08e-07 |
|
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: 53.39 E-value: 1.08e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2728837251 41 DVEIIDANGKTVTPGFIDQHVHIT--GAGGKHGFQSLTPEIALTefitcGTTTVVgllgtdgatkslkaLYAKTK-ALDN 117
Cdd:cd01317 1 DAEVIDAEGKILAPGLVDLHVHLRepGFEYKETLESGAKAAAAG-----GFTTVV--------------CMPNTNpVIDN 61
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2728837251 118 EGITAYMLTSYF--GLPPITMMGSV--------LEDMLFIDKVlGCkVAISDERSSFPTAKELLSIL-----KD----VH 178
Cdd:cd01317 62 PAVVELLKNRAKdvGIVRVLPIGALtkglkgeeLTEIGELLEA-GA-VGFSDDGKPIQDAELLRRALeyaamLDlpiiVH 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2728837251 179 VGGLTSGKKGIMHVhlGALKTNMQL--------------LLDLVEQYDFPIR--NISpthvgrTAPLFeEAIRFAKLGGm 242
Cdd:cd01317 140 PEDPSLAGGGVMNE--GKVASRLGLpgippeaetimvarDLELAEATGARVHfqHLS------TARSL-ELIRKAKAKG- 209
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2728837251 243 IDITTGGTkfdePYKQVLyaldkgvpIENMTFSSDGNAGL-----GVND--------KDGNLVGF-----------KKAP 298
Cdd:cd01317 210 LPVTAEVT----PHHLLL--------DDEALESYDTNAKVnpplrSEEDrealiealKDGTIDAIasdhaphtdeeKDLP 277
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2728837251 299 IDL------NYKQV-----QKLVKEANMPIGQAIQLVTSGPARNLSLTQkGRVFAGGDADLCLFD 352
Cdd:cd01317 278 FAEappgiiGLETAlpllwTLLVKGGLLTLPDLIRALSTNPAKILGLPP-GRLEVGAPADLVLFD 341
|
|
| D-aminoacylase |
cd01297 |
D-aminoacylases (N-acyl-D-Amino acid amidohydrolases) catalyze the hydrolysis of ... |
20-352 |
1.39e-07 |
|
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: 53.07 E-value: 1.39e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2728837251 20 DILICGEKIALISDKISPNLPDVeiIDANGKTVTPGFIDQHVHITGAggkhgfqsLTPEIALTEFITCGTTTVVglLGTD 99
Cdd:cd01297 21 DVGIRDGRIAAIGPILSTSAREV--IDAAGLVVAPGFIDVHTHYDGQ--------VFWDPDLRPSSRQGVTTVV--LGNC 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2728837251 100 GATKSLKALYAKTKALDN-EGITAYMLT---------SYFGLppITMMGSVLEDMLFI------DKVLGckvaisdERSS 163
Cdd:cd01297 89 GVSPAPANPDDLARLIMLmEGLVALGEGlpwgwatfaEYLDA--LEARPPAVNVAALVghaalrRAVMG-------LDAR 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2728837251 164 FPTAKELLSILKDVHvGGLTSGKKGI---MHVH--LGALKTNMQLLLDLVEQYDFPIRNISPTHVGRTAPLFEEAIRFAK 238
Cdd:cd01297 160 EATEEELAKMRELLR-EALEAGALGIstgLAYAprLYAGTAELVALARVAARYGGVYQTHVRYEGDSILEALDELLRLGR 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2728837251 239 LGG----MIDITTGGTKFDEPYKQVLYALDK----GVPI---------------------ENMTFSSDGnaGLGVNDKDG 289
Cdd:cd01297 239 ETGrpvhISHLKSAGAPNWGKIDRLLALIEAaraeGLQVtadvypygagseddvrrimahPVVMGGSDG--GALGKPHPR 316
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2728837251 290 NLVGFKKApidlnykqVQKLVKEAN-MPIGQAIQLVTSGPARNLSLTQKGRVFAGGDADLCLFD 352
Cdd:cd01297 317 SYGDFTRV--------LGHYVRERKlLSLEEAVRKMTGLPARVFGLADRGRIAPGYRADIVVFD 372
|
|
| Met_dep_hydrolase_B |
cd01307 |
Metallo-dependent hydrolases, subgroup B is part of the superfamily of metallo-dependent ... |
20-352 |
1.47e-07 |
|
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: 52.72 E-value: 1.47e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2728837251 20 DILICGEKIALISDKISPNLPDvEIIDANGKTVTPGFIDQHVHItgaggkhgFQSLTP------EIAltefITCGTTTVV 93
Cdd:cd01307 1 DVAIENGKIAAVGAALAAPAAT-QIVDAGGCYVSPGWIDLHVHV--------YQGGTRygdrpdMIG----VKSGVTTVV 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2728837251 94 GlLGTDGATKSLKALYAKTKAlDNEGITAYMLTSYFGLppitMMGSVLEDMLFIDKvlgckvaiSDERSSFPTAKELLSI 173
Cdd:cd01307 68 D-AGSAGADNIDGFRYTVIER-SATRVYAFLNISRVGL----VAQDELPDPDNIDE--------DAVVAAAREYPDVIVG 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2728837251 174 LKdVHVGGLTSGKKGIMHVHLGAlktNMQLLLDLveqydfPIRnispTHVGRTAPLFEEAIRFAKLGgmiDITT------ 247
Cdd:cd01307 134 LK-ARASKSVVGEWGIKPLELAK---KIAKEADL------PLM----VHIGSPPPILDEVVPLLRRG---DVLThcfngk 196
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2728837251 248 GGTKFDE---PYKQVLYALDKGVPIE----NMTFSSDG-----NAGL----------GVNDKDGNLvgFKKAPIdlnykq 305
Cdd:cd01307 197 PNGIVDEegeVLPLVRRARERGVIFDvghgTASFSFRVaraaiAAGLlpdtissdihGRNRTNGPV--YALATT------ 268
|
330 340 350 360
....*....|....*....|....*....|....*....|....*..
gi 2728837251 306 VQKLVKeANMPIGQAIQLVTSGPARNLSLTQKGRVFAGGDADLCLFD 352
Cdd:cd01307 269 LSKLLA-LGMPLEEVIEAVTANPARMLGLAEIGTLAVGYDADLTVFD 314
|
|
| SsnA |
COG0402 |
Cytosine/adenosine deaminase or related metal-dependent hydrolase [Nucleotide transport and ... |
20-93 |
1.90e-07 |
|
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: 52.52 E-value: 1.90e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2728837251 20 DILICGEKIALI--SDKISPNLPDVEIIDANGKTVTPGFIDQHVH-----ITGAGGKHGFQS------------LTPE-- 78
Cdd:COG0402 23 AVLVEDGRIAAVgpGAELPARYPAAEVIDAGGKLVLPGLVNTHTHlpqtlLRGLADDLPLLDwleeyiwplearLDPEdv 102
|
90 100
....*....|....*....|
gi 2728837251 79 -----IALTEFITCGTTTVV 93
Cdd:COG0402 103 yagalLALAEMLRSGTTTVA 122
|
|
| PRK12394 |
PRK12394 |
metallo-dependent hydrolase; |
4-133 |
2.09e-07 |
|
metallo-dependent hydrolase;
Pssm-ID: 183497 [Multi-domain] Cd Length: 379 Bit Score: 52.46 E-value: 2.09e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2728837251 4 LIKNSILYAPES--FGKKDILICGEKIALISDkiSPNLPDVEIIDANGKTVTPGFIDQHVHITGAGGKHGfqsLTPEIAL 81
Cdd:PRK12394 6 LITNGHIIDPARniNEINNLRIINDIIVDADK--YPVASETRIIHADGCIVTPGLIDYHAHVFYDGTEGG---VRPDMYM 80
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 2728837251 82 tefITCGTTTVVGlLGTDGaTKSLKALYAKTKALDNEGITAYMLTSYFGLPP 133
Cdd:PRK12394 81 ---PPNGVTTVVD-AGSAG-TANFDAFYRTVICASKVRIKAFLTVSPPGQTW 127
|
|
| Amidohydro_1 |
pfam01979 |
Amidohydrolase family; This family of enzymes are a a large metal dependent hydrolase ... |
51-367 |
2.63e-07 |
|
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: 51.73 E-value: 2.63e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2728837251 51 TVTPGFIDQHVHI-----TGAGGKHGFQSLTPEIALTEFITCGTTTVVGLlGTDGATKSLKALYAKTKALDNEGITAyml 125
Cdd:pfam01979 1 IVLPGLIDAHVHLemgllRGIPVPPEFAYEALRLGITTMLKSGTTTVLDM-GATTSTGIEALLEAAEELPLGLRFLG--- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2728837251 126 tsyfGLPPITMMGSVLEDMLFIDKVL-----------GCKVAISDERSSFPTAKELLS-ILKDVHVGGLtsgkkgIMHVH 193
Cdd:pfam01979 77 ----PGCSLDTDGELEGRKALREKLKagaefikgmadGVVFVGLAPHGAPTFSDDELKaALEEAKKYGL------PVAIH 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2728837251 194 LG---ALKTNMQLLLDLVEQYDFPIRNISPTHVGRTA---------PLFEEAIRFAKLGGMIDITTGgtKFDEPYKQ--- 258
Cdd:pfam01979 147 ALetkGEVEDAIAAFGGGIEHGTHLEVAESGGLLDIIklilahgvhLSPTEANLLAEHLKGAGVAHC--PFSNSKLRsgr 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2728837251 259 --VLYALDKGVpieNMTFSSDGnAGLGVNdkdGNLVgfkkapIDLNYKQVQKLVKEANMPIGQAIQLVTSGPARNLSLT- 335
Cdd:pfam01979 225 iaLRKALEDGV---KVGLGTDG-AGSGNS---LNML------EELRLALELQFDPEGGLSPLEALRMATINPAKALGLDd 291
|
330 340 350 360
....*....|....*....|....*....|....*....|...
gi 2728837251 336 QKGRVFAGGDADLCLFD-----------SNFNLTDVIARGRVM 367
Cdd:pfam01979 292 KVGSIEVGKDADLVVVDldplaaffglkPDGNVKKVIVKGKIV 334
|
|
| PRK07228 |
PRK07228 |
5'-deoxyadenosine deaminase; |
20-109 |
4.00e-07 |
|
5'-deoxyadenosine deaminase;
Pssm-ID: 180895 [Multi-domain] Cd Length: 445 Bit Score: 51.54 E-value: 4.00e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2728837251 20 DILICGEKIALISDKISPNLPDvEIIDANGKTVTPGFIDQHVHIT---GAG-------------------GKHGFQSL-- 75
Cdd:PRK07228 23 DVLIEDDRIAAVGDRLDLEDYD-DHIDATGKVVIPGLIQGHIHLCqtlFRGiaddlelldwlkdriwpleAAHDAESMyy 101
|
90 100 110
....*....|....*....|....*....|....
gi 2728837251 76 TPEIALTEFITCGTTTVVGLLGTDGATKSLKALY 109
Cdd:PRK07228 102 SALLGIGELIESGTTTIVDMESVHHTDSAFEAAG 135
|
|
| YtcJ_like |
cd01300 |
YtcJ_like metal dependent amidohydrolases. YtcJ is a Bacillus subtilis ORF of unknown function. ... |
40-67 |
5.77e-07 |
|
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: 51.16 E-value: 5.77e-07
10 20
....*....|....*....|....*...
gi 2728837251 40 PDVEIIDANGKTVTPGFIDQHVHITGAG 67
Cdd:cd01300 24 PATEVIDLKGKTVLPGFIDSHSHLLLGG 51
|
|
| PRK09236 |
PRK09236 |
dihydroorotase; Reviewed |
20-62 |
1.03e-06 |
|
dihydroorotase; Reviewed
Pssm-ID: 181716 Cd Length: 444 Bit Score: 50.25 E-value: 1.03e-06
10 20 30 40
....*....|....*....|....*....|....*....|...
gi 2728837251 20 DILICGEKIALISDKISPnLPDVEIIDANGKTVTPGFIDQHVH 62
Cdd:PRK09236 21 DVLIENGRIAKIASSISA-KSADTVIDAAGRYLLPGMIDDQVH 62
|
|
| ureC |
PRK13206 |
urease subunit alpha; Reviewed |
31-107 |
2.70e-06 |
|
urease subunit alpha; Reviewed
Pssm-ID: 237304 [Multi-domain] Cd Length: 573 Bit Score: 49.32 E-value: 2.70e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2728837251 31 ISDKISPNL---PDVEIIDANGKTVTPGFIDQHVHItgaggkhgfqsLTPEIaLTEFITCGTTTVVGllGTDGATKSLKA 107
Cdd:PRK13206 109 IMDGVHPDLvigPSTEIIAGNGRILTAGAIDCHVHF-----------ICPQI-VDEALAAGITTLIG--GGTGPAEGSKA 174
|
|
| Amidohydro_3 |
pfam07969 |
Amidohydrolase family; |
43-67 |
4.40e-06 |
|
Amidohydrolase family;
Pssm-ID: 400360 [Multi-domain] Cd Length: 464 Bit Score: 48.30 E-value: 4.40e-06
|
| Bact_CD |
cd01293 |
Bacterial cytosine deaminase and related metal-dependent hydrolases. Cytosine deaminases (CDs) ... |
20-63 |
4.47e-06 |
|
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: 48.40 E-value: 4.47e-06
10 20 30 40
....*....|....*....|....*....|....*....|....
gi 2728837251 20 DILICGEKIALIsDKISPNLPDVEIIDANGKTVTPGFIDQHVHI 63
Cdd:cd01293 16 DIAIEDGRIAAI-GPALAVPPDAEEVDAKGRLVLPAFVDPHIHL 58
|
|
| Imidazolone-5PH |
cd01296 |
Imidazolonepropionase/imidazolone-5-propionate hydrolase (Imidazolone-5PH) catalyzes the third ... |
21-67 |
6.88e-06 |
|
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: 47.64 E-value: 6.88e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 2728837251 21 ILICGEKIALI---SDKISPNLPDVEIIDANGKTVTPGFIDQHVHITGAG 67
Cdd:cd01296 1 IAIRDGRIAAVgpaASLPAPGPAAAEEIDAGGRAVTPGLVDCHTHLVFAG 50
|
|
| ade |
TIGR01178 |
adenine deaminase; The family described by this model includes an experimentally characterized ... |
18-365 |
8.98e-06 |
|
adenine deaminase; The family described by this model includes an experimentally characterized adenine deaminase of Bacillus subtilis. It also include a member from Methanobacterium thermoautotrophicum, in which adenine deaminase activity has been detected. [Purines, pyrimidines, nucleosides, and nucleotides, Salvage of nucleosides and nucleotides]
Pssm-ID: 130246 [Multi-domain] Cd Length: 552 Bit Score: 47.46 E-value: 8.98e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2728837251 18 KKDILICGEKIALIsDKISpnlpDVEIIDANGKTVTPGFIDQHVHITGAggkhgfqSLTPEIALTEFITCGTTTVV---- 93
Cdd:TIGR01178 19 PGDIAIANGHIAGV-GKYN----GVKVIDALGEYAVPGFIDAHIHIESS-------MLTPSEFAKLVLPHGVTTVVsdph 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2728837251 94 ---GLLGTDGATKSLKAlyAKTKALDnegitaymltSYFGLP------PITMMGSVL--EDM---LFIDKVLGCKvaisd 159
Cdd:TIGR01178 87 eiaNVNGEDGINFMLNN--AKKTPLN----------FYFMLPscvpalQFETSGAVLtaEDIdelMELDEVLGLA----- 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2728837251 160 ERSSFPTA----KELLSILKDVHVGGLtsgkkgIMHVHLGALKTNmqllldlvEQYDFPIRNISPTHVGRTaplFEEAIR 235
Cdd:TIGR01178 150 EVMDYPGVinadIEMLNKINSARKRNK------VIDGHCPGLSGK--------LLNKYISAGISNDHESTS---IEEARE 212
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2728837251 236 FAKLGGMIDITTGGTKFDepykqvLYALDKGVPIEN----MTFSSDGNaglgVNDKDgnlvgfKKAPIDLnykQVQKLVK 311
Cdd:TIGR01178 213 KLRLGMKLMIREGSAAKN------LEALHPLINEKNcrslMLCTDDRH----VNDIL------NEGHINH---IVRRAIE 273
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*.
gi 2728837251 312 EANMPIgQAIQLVTSGPARNLSLTQKGRVFAGGDADLCLFDS--NFNLTDVIARGR 365
Cdd:TIGR01178 274 HGVDPF-DALQMASINPAEHFGIDVGGLIAPGDPADFVILKDlrNFKVNKTYVKGK 328
|
|
| PRK07627 |
PRK07627 |
dihydroorotase; Provisional |
308-352 |
1.08e-05 |
|
dihydroorotase; Provisional
Pssm-ID: 181059 [Multi-domain] Cd Length: 425 Bit Score: 46.98 E-value: 1.08e-05
10 20 30 40
....*....|....*....|....*....|....*....|....*
gi 2728837251 308 KLVKEANMPIGQAIQLVTSGPARNLSLtQKGRVFAGGDADLCLFD 352
Cdd:PRK07627 338 KWADEAKVPLARALARITSAPARVLGL-PAGRLAEGAPADLCVFD 381
|
|
| PRK13404 |
PRK13404 |
dihydropyrimidinase; Provisional |
9-93 |
1.20e-05 |
|
dihydropyrimidinase; Provisional
Pssm-ID: 184033 [Multi-domain] Cd Length: 477 Bit Score: 47.00 E-value: 1.20e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2728837251 9 ILYAPESFgKKDILICGEKIALISDKISPNlpdVEIIDANGKTVTPGFIDQHVHI---TGAGGKHG--FQSLTPEIALTe 83
Cdd:PRK13404 13 VVTATDTF-QADIGIRGGRIAALGEGLGPG---AREIDATGRLVLPGGVDSHCHIdqpSGDGIMMAddFYTGTVSAAFG- 87
|
90
....*....|
gi 2728837251 84 fitcGTTTVV 93
Cdd:PRK13404 88 ----GTTTVI 93
|
|
| PRK09060 |
PRK09060 |
dihydroorotase; Validated |
4-62 |
1.25e-05 |
|
dihydroorotase; Validated
Pssm-ID: 181632 [Multi-domain] Cd Length: 444 Bit Score: 46.84 E-value: 1.25e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 2728837251 4 LIKNSILYAPESFGKKDILICGEKIALISDkISPNLPDvEIIDANGKTVTPGFIDQHVH 62
Cdd:PRK09060 8 ILKGGTVVNPDGEGRADIGIRDGRIAAIGD-LSGASAG-EVIDCRGLHVLPGVIDSQVH 64
|
|
| Met_dep_hydrolase_A |
cd01299 |
Metallo-dependent hydrolases, subgroup A is part of the superfamily of metallo-dependent ... |
42-354 |
1.37e-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: 46.52 E-value: 1.37e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2728837251 42 VEIIDANGKTVTPGFIDQHVHITGAGGKHGFQSLTPEI--------ALTEFITCGTTTVVGLLGTDgatkslkaLYAKTK 113
Cdd:cd01299 1 AQVIDLGGKTLMPGLIDAHTHLGSDPGDLPLDLALPVEyrtiratrQARAALRAGFTTVRDAGGAD--------YGLLRD 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2728837251 114 ALDnEGITA--------YMLTSYFGLPPIT---MMGSVLEDMLFIDKVLGC---------------KVAISDERSS--FP 165
Cdd:cd01299 73 AID-AGLIPgprvfasgRALSQTGGHGDPRglsGLFPAGGLAAVVDGVEEVraavreqlrrgadqiKIMATGGVLSpgDP 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2728837251 166 TAKELLS--ILKDV-------------HVGG-------LTSGKKGIMHvhlGALKTNMQLLLdLVEQYDFpirnISPTHV 223
Cdd:cd01299 152 PPDTQFSeeELRAIvdeahkaglyvaaHAYGaeairraIRAGVDTIEH---GFLIDDETIEL-MKEKGIF----LVPTLA 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2728837251 224 grtapLFEEAIRFAKLGGMIDITTggTKFDEPYKQVLYAL----DKGVPIenmTFSSDgnaglgvndkdgnlVGFKKAPI 299
Cdd:cd01299 224 -----TYEALAAEGAAPGLPADSA--EKVALVLEAGRDALrrahKAGVKI---AFGTD--------------AGFPVPPH 279
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*.
gi 2728837251 300 DLNYKQVQKLVKeANMPIGQAIQLVTSGPARNLSLTQK-GRVFAGGDADLCLFDSN 354
Cdd:cd01299 280 GWNARELELLVK-AGGTPAEALRAATANAAELLGLSDElGVIEAGKLADLLVVDGD 334
|
|
| PRK08044 |
PRK08044 |
allantoinase AllB; |
4-70 |
1.92e-05 |
|
allantoinase AllB;
Pssm-ID: 169193 [Multi-domain] Cd Length: 449 Bit Score: 46.39 E-value: 1.92e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2728837251 4 LIKNSILYAPESFGKKDILICGEKIALISDKISPNlpdVEIIDANGKTVTPGFIDQHVHITGAGGKH 70
Cdd:PRK08044 6 IIKNGTVILENEARVVDIAVKGGKIAAIGQDLGDA---KEVMDASGLVVSPGMVDAHTHISEPGRSH 69
|
|
| Amidohydro_3 |
pfam07969 |
Amidohydrolase family; |
219-355 |
1.96e-05 |
|
Amidohydrolase family;
Pssm-ID: 400360 [Multi-domain] Cd Length: 464 Bit Score: 46.37 E-value: 1.96e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2728837251 219 SPTHVGRTAPLFEEAI-RFAKLGGMIDITTGGTKFDEPYKQVLY-------------ALDKGVPienMTFSSDGNAGlgv 284
Cdd:pfam07969 297 RIEHAQGVVPYTYSQIeRVAALGGAAGVQPVFDPLWGDWLQDRLgaerargltpvkeLLNAGVK---VALGSDAPVG--- 370
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2728837251 285 ndkdgnlvGFKKAP--IDLNYKQVQKLVKEANM----PIGQAIQLVTSGPARNLSLTQ-KGRVFAGGDADLCLFDSNF 355
Cdd:pfam07969 371 --------PFDPWPriGAAVMRQTAGGGEVLGPdeelSLEEALALYTSGPAKALGLEDrKGTLGVGKDADLVVLDDDP 440
|
|
| PRK07575 |
PRK07575 |
dihydroorotase; Provisional |
4-70 |
2.06e-05 |
|
dihydroorotase; Provisional
Pssm-ID: 236055 [Multi-domain] Cd Length: 438 Bit Score: 46.21 E-value: 2.06e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2728837251 4 LIKNSILYAPE-SFGKKDILICGEKIALISDKISPNLPDvEIIDANGKTVTPGFIDQHVHITGAGGKH 70
Cdd:PRK07575 6 LIRNARILLPSgELLLGDVLVEDGKIVAIAPEISATAVD-TVIDAEGLTLLPGVIDPQVHFREPGLEH 72
|
|
| PRK05985 |
PRK05985 |
cytosine deaminase; Provisional |
4-62 |
3.55e-05 |
|
cytosine deaminase; Provisional
Pssm-ID: 180337 [Multi-domain] Cd Length: 391 Bit Score: 45.31 E-value: 3.55e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 2728837251 4 LIKNSILYAPESfgkKDILICGEKIALISDKISPNlPDVEIIDANGKTVTPGFIDQHVH 62
Cdd:PRK05985 5 LFRNVRPAGGAA---VDILIRDGRIAAIGPALAAP-PGAEVEDGGGALALPGLVDGHIH 59
|
|
| PRK07572 |
PRK07572 |
cytosine deaminase; Validated |
1-63 |
4.36e-05 |
|
cytosine deaminase; Validated
Pssm-ID: 181039 Cd Length: 426 Bit Score: 45.40 E-value: 4.36e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2728837251 1 MFKLI-KNSILyaPESFGKKDILICGEKIAlisdKISPNL--PDVEIIDANGKTVTPGFIDQHVHI 63
Cdd:PRK07572 1 MFDLIvRNANL--PDGRTGIDIGIAGGRIA----AVEPGLqaEAAEEIDAAGRLVSPPFVDPHFHM 60
|
|
| PRK10027 |
PRK10027 |
cryptic adenine deaminase; Provisional |
1-93 |
5.71e-05 |
|
cryptic adenine deaminase; Provisional
Pssm-ID: 182201 [Multi-domain] Cd Length: 588 Bit Score: 45.21 E-value: 5.71e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2728837251 1 MFKLIKNSILYAPesfgkkdILICGEKIALISDKISpNLPDVEIIDANGKTVTPGFIDQHVHITGAggkhgfqSLTPEIA 80
Cdd:PRK10027 39 ILDLINGGEISGP-------IVIKGRYIAGVGAEYA-DAPALQRIDARGATAVPGFIDAHLHIESS-------MMTPVTF 103
|
90
....*....|...
gi 2728837251 81 LTEFITCGTTTVV 93
Cdd:PRK10027 104 ETATLPRGLTTVI 116
|
|
| ATZ_TRZ_like |
cd01298 |
TRZ/ATZ family contains enzymes from the atrazine degradation pathway and related hydrolases. ... |
20-63 |
6.11e-05 |
|
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: 44.89 E-value: 6.11e-05
10 20 30 40
....*....|....*....|....*....|....*....|....*
gi 2728837251 20 DILICGEKIALISDKIS-PNLPDVEIIDANGKTVTPGFIDQHVHI 63
Cdd:cd01298 21 DVLVEDGRIVAVGPALPlPAYPADEVIDAKGKVVMPGLVNTHTHL 65
|
|
| PRK15446 |
PRK15446 |
phosphonate metabolism protein PhnM; Provisional |
308-366 |
7.80e-05 |
|
phosphonate metabolism protein PhnM; Provisional
Pssm-ID: 237967 [Multi-domain] Cd Length: 383 Bit Score: 44.40 E-value: 7.80e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2728837251 308 KLVKEANMPIGQAIQLVTSGPARNLSLTQKGRVFAGGDADLCLFDSNFNL---TDVIARGRV 366
Cdd:PRK15446 317 RLADDGGLDLPQAVALVTANPARAAGLDDRGEIAPGKRADLVRVRRAGGLpvvRAVWRGGRR 378
|
|
| nagA |
TIGR00221 |
N-acetylglucosamine-6-phosphate deacetylase; [Central intermediary metabolism, Amino sugars] |
1-365 |
1.10e-04 |
|
N-acetylglucosamine-6-phosphate deacetylase; [Central intermediary metabolism, Amino sugars]
Pssm-ID: 272968 Cd Length: 380 Bit Score: 44.05 E-value: 1.10e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2728837251 1 MFKLIKN-SILYAPESFGKKDILICGEKIALISDKiSPNLPDVEIIDANGKTVTPGFIDQHVHitGAGGkHGF------- 72
Cdd:TIGR00221 3 ESYLLKDiAIVTGNEVIDNGAVGINDGKISTVSTE-AELEPEIKEIDLPGNVLTPGFIDIHIH--GCGG-VDTndasfet 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2728837251 73 ----QSLTPEIALTEFITCGTTTVVGLLGTdgATKSLKALYAKTKALDNEGItaYMLTSYFGL------PPITMMGSVLE 142
Cdd:TIGR00221 79 leimSERLPKSGCTSFLPTLITQPDENIKQ--AVKNMREYLAKEKNAQALGL--HLEGPFLSPekkgahPPEYIREPDVE 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2728837251 143 DML-FIDKVLG--CKVAISDERSsfPTAkELLSILKD----VHVG--------GLTSGKKGIMHV-HL-GALKT----NM 201
Cdd:TIGR00221 155 LFKkFLCEAGGviTKVTLAPEED--QHF-ELIRHLKDagiiVSAGhtnatyelAKAAFKAGATHAtHLyNAMSPihhrEP 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2728837251 202 QLLLDLVEQYDFPIRNISPTHvgRTAPLFEEAIRFAKLGGMIDITTGGTKfdepykqvlyalDKGVPIENMTFSSDG--N 279
Cdd:TIGR00221 232 GVIGAVLDHDDVYTEIIADGI--HIHPLNIRLAKKLKGDSKLCLVTDSMA------------AAGAKDGVFIFGGKTvyI 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2728837251 280 AGLGVNDKDGNLVGfkkAPIDLNyKQVQKLVKEANMPIGQAIQLVTSGPARNLSL-TQKGRVFAGGDADLCLFDSNFNLT 358
Cdd:TIGR00221 298 REGTCLDSNGTLAG---SSLTMI-EGARNLVEFTNISLTDAARMSSLNPARALGIdDRLGSVTVGKDANLVVFTPDFEVI 373
|
....*..
gi 2728837251 359 DVIARGR 365
Cdd:TIGR00221 374 LTIVNGN 380
|
|
| PhnM |
cd01306 |
PhnM is believed to be a subunit of the membrane associated C-P lyase complex. C-P lyase is ... |
308-352 |
1.22e-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: 43.42 E-value: 1.22e-04
10 20 30 40
....*....|....*....|....*....|....*....|....*
gi 2728837251 308 KLVKEANMPIGQAIQLVTSGPARNLSLTQKGRVFAGGDADLCLFD 352
Cdd:cd01306 266 RLADLGGWSLPEAVALVSANPARAVGLTDRGSIAPGKRADLILVD 310
|
|
| PRK06846 |
PRK06846 |
putative deaminase; Validated |
20-77 |
1.30e-04 |
|
putative deaminase; Validated
Pssm-ID: 235873 [Multi-domain] Cd Length: 410 Bit Score: 43.85 E-value: 1.30e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2728837251 20 DILICGEKIALISDKISPNLPDVEIIDANGKTVTPGFIDQHVHI--TGAGGkhGFQSLTP 77
Cdd:PRK06846 33 TLEIQDGKIVAIRPNKQVPDATLPTYDANGLLMLPAFREMHIHLdkTYYGG--PWKACRP 90
|
|
| PRK08393 |
PRK08393 |
N-ethylammeline chlorohydrolase; Provisional |
1-62 |
1.36e-04 |
|
N-ethylammeline chlorohydrolase; Provisional
Pssm-ID: 181411 [Multi-domain] Cd Length: 424 Bit Score: 43.64 E-value: 1.36e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2728837251 1 MFKLIKNSILYAPESFG--KKDILICGEKIALISDKIspNLPDVEIIDANGKTVTPGFIDQHVH 62
Cdd:PRK08393 1 MSILIKNGYVIYGENLKviRADVLIEGNKIVEVKRNI--NKPADTVIDASGSVVSPGFINAHTH 62
|
|
| FMDH_A |
cd01304 |
Formylmethanofuran dehydrogenase (FMDH) subunit A; Methanogenic bacteria and archea derive ... |
5-69 |
1.44e-04 |
|
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: 43.94 E-value: 1.44e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2728837251 5 IKNSILYAPESfG----KKDILICGEKIAlisdKISPNLPDVEIIDANGKTVTPGFIDQHVHItgAGGK 69
Cdd:cd01304 1 IKNGTVYDPLN-GingeKMDIFIRDGKIV----ESSSGAKPAKVIDASGKVVMAGGVDMHSHI--AGGK 62
|
|
| PRK06380 |
PRK06380 |
metal-dependent hydrolase; Provisional |
1-85 |
2.72e-04 |
|
metal-dependent hydrolase; Provisional
Pssm-ID: 180548 [Multi-domain] Cd Length: 418 Bit Score: 42.56 E-value: 2.72e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2728837251 1 MFKLIKNSILYAPES---FGKKDILICGEKIALISDKispNLPDVEIIDANGKTVTPGFIDQHVHItgagGKHGFQSLTP 77
Cdd:PRK06380 1 MSILIKNAWIVTQNEkreILQGNVYIEGNKIVYVGDV---NEEADYIIDATGKVVMPGLINTHAHV----GMTASKGLFD 73
|
....*...
gi 2728837251 78 EIALTEFI 85
Cdd:PRK06380 74 DVDLEEFL 81
|
|
| PRK09230 |
PRK09230 |
cytosine deaminase; Provisional |
3-63 |
4.97e-04 |
|
cytosine deaminase; Provisional
Pssm-ID: 181713 Cd Length: 426 Bit Score: 42.00 E-value: 4.97e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2728837251 3 KLIKNSILYAPEsfGKKDILICGEKIALISDKISPNLPDVEIIDANGKTVTPGFIDQHVHI 63
Cdd:PRK09230 6 MTIKNARLPGKE--GLWQITIEDGKISAIEPQSEASLEAGEVLDAEGGLAIPPFIEPHIHL 64
|
|
| PLN02795 |
PLN02795 |
allantoinase |
25-175 |
5.43e-04 |
|
allantoinase
Pssm-ID: 178392 [Multi-domain] Cd Length: 505 Bit Score: 42.07 E-value: 5.43e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2728837251 25 GEKIALISDK--ISPNLPDVEIIDANGKTVTPGFIDQHVHITGAGGK--HGFQSLTPEIAltefiTCGTTTVVGL-LGTD 99
Cdd:PLN02795 68 GGRIVSVTKEeeAPKSQKKPHVLDYGNAVVMPGLIDVHVHLNEPGRTewEGFPTGTKAAA-----AGGITTLVDMpLNSF 142
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2728837251 100 GATKSLKALYAKTKALDNegiTAYMLTSYFG--LPPITMMGSVLEDMLfiDK-VLG-----CKVAISDERSSFPT-AKEL 170
Cdd:PLN02795 143 PSTTSVETLELKIEAAKG---KLYVDVGFWGglVPENAHNASVLEELL--DAgALGlksfmCPSGINDFPMTTAThIKAA 217
|
....*
gi 2728837251 171 LSILK 175
Cdd:PLN02795 218 LPVLA 222
|
|
| PRK07203 |
PRK07203 |
putative aminohydrolase SsnA; |
20-92 |
7.32e-04 |
|
putative aminohydrolase SsnA;
Pssm-ID: 235963 [Multi-domain] Cd Length: 442 Bit Score: 41.46 E-value: 7.32e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2728837251 20 DILICGEKIALI--SDKISPNLPDVEIIDANGKTVTPGFIDQHVHI-------TGAGGK--HGFQS------------LT 76
Cdd:PRK07203 23 AIAIEGNVIVEIgtTDELKAKYPDAEFIDAKGKLIMPGLINSHNHIysglargMMANIPppPDFISilknlwwrldraLT 102
|
90 100
....*....|....*....|...
gi 2728837251 77 PE-------IALTEFITCGTTTV 92
Cdd:PRK07203 103 LEdvyysalICSLEAIKNGVTTV 125
|
|
| PRK09061 |
PRK09061 |
D-glutamate deacylase; Validated |
20-75 |
7.36e-04 |
|
D-glutamate deacylase; Validated
Pssm-ID: 236369 [Multi-domain] Cd Length: 509 Bit Score: 41.60 E-value: 7.36e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 2728837251 20 DILICGEKIALISDkiSPNLPDvEIIDANGKTVTPGFIDQHVHITGAGGkHGFQSL 75
Cdd:PRK09061 40 DVGIKGGKIAAVGT--AAIEGD-RTIDATGLVVAPGFIDLHAHGQSVAA-YRMQAF 91
|
|
| Urease_alpha |
cd00375 |
Urease alpha-subunit; Urease is a nickel-dependent metalloenzyme that catalyzes the hydrolysis ... |
18-94 |
1.52e-03 |
|
Urease alpha-subunit; Urease is a nickel-dependent metalloenzyme that catalyzes the hydrolysis of urea to form ammonia and carbon dioxide. Nickel-dependent ureases are found in bacteria, fungi and plants. Their primary role is to allow the use of external and internally generated urea as a nitrogen source. The enzyme consists of 3 subunits, alpha, beta and gamma, which can be fused and present on a single protein chain and which in turn forms multimers, mainly trimers. The large alpha subunit is the catalytic domain containing an active site with a bi-nickel center complexed by a carbamylated lysine. The beta and gamma subunits play a role in subunit association to form the higher order trimers.
Pssm-ID: 238221 [Multi-domain] Cd Length: 567 Bit Score: 40.39 E-value: 1.52e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2728837251 18 KKDILICGEKIALIS--------DKISPNL---PDVEIIDANGKTVTPGFIDQHVHItgaggkhgfqsLTPEIAlTEFIT 86
Cdd:cd00375 82 KADIGIKDGRIVAIGkagnpdimDGVTPNMivgPSTEVIAGEGKIVTAGGIDTHVHF-----------ICPQQI-EEALA 149
|
....*...
gi 2728837251 87 CGTTTVVG 94
Cdd:cd00375 150 SGITTMIG 157
|
|
| PRK09228 |
PRK09228 |
guanine deaminase; Provisional |
33-93 |
1.66e-03 |
|
guanine deaminase; Provisional
Pssm-ID: 236419 [Multi-domain] Cd Length: 433 Bit Score: 40.17 E-value: 1.66e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2728837251 33 DKISPNLP-DVEIIDANGKTVTPGFIDQHVHI--TGAGGKHGFQSLT-------PE------------IA---LTEFITC 87
Cdd:PRK09228 48 AELRAQLPaDAEVTDYRGKLILPGFIDTHIHYpqTDMIASYGEQLLDwlntytfPEerrfadpayareVAeffLDELLRN 127
|
....*.
gi 2728837251 88 GTTTVV 93
Cdd:PRK09228 128 GTTTAL 133
|
|
| guan_deamin |
TIGR02967 |
guanine deaminase; This model describes guanine deaminase, which hydrolyzes guanine to ... |
40-92 |
2.54e-03 |
|
guanine deaminase; This model describes guanine deaminase, which hydrolyzes guanine to xanthine and ammonia. Xanthine can then be converted to urate by xanthine dehydrogenase, and urate subsequently degraded. In some bacteria, the guanine deaminase gene is found near the xdhABC genes for xanthine dehydrogenase. Non-homologous forms of guanine deaminase also exist, as well as distantly related forms outside the scope of this model. [Purines, pyrimidines, nucleosides, and nucleotides, Other]
Pssm-ID: 132012 [Multi-domain] Cd Length: 401 Bit Score: 39.55 E-value: 2.54e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2728837251 40 PDVEIIDANGKTVTPGFIDQHVH-----ITGAGGK--------------HGFQSL-----TPEIALTEFITCGTTTV 92
Cdd:TIGR02967 31 AGVEIDDYRGHLIMPGFIDTHIHypqteMIASYGEqllewlekytfpteARFADPdhaeeVAEFFLDELLRNGTTTA 107
|
|
| PRK07583 |
PRK07583 |
cytosine deaminase; |
315-363 |
3.64e-03 |
|
cytosine deaminase;
Pssm-ID: 236062 Cd Length: 438 Bit Score: 39.20 E-value: 3.64e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 2728837251 315 MPIGQAIQLVTSGPARNLSLTQKGRVFAGGDADLCLFdSNFNLTDVIAR 363
Cdd:PRK07583 360 HPYDDWPAAVTTTPADIMGLPDLGRIAVGAPADLVLF-KARSFSELLSR 407
|
|
| PLN02942 |
PLN02942 |
dihydropyrimidinase |
35-63 |
4.35e-03 |
|
dihydropyrimidinase
Pssm-ID: 178530 Cd Length: 486 Bit Score: 39.06 E-value: 4.35e-03
10 20 30
....*....|....*....|....*....|..
gi 2728837251 35 ISPNLP---DVEIIDANGKTVTPGFIDQHVHI 63
Cdd:PLN02942 35 VAPNLKvpdDVRVIDATGKFVMPGGIDPHTHL 66
|
|
| PRK07369 |
PRK07369 |
dihydroorotase; Provisional |
20-74 |
4.46e-03 |
|
dihydroorotase; Provisional
Pssm-ID: 236002 [Multi-domain] Cd Length: 418 Bit Score: 38.81 E-value: 4.46e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 2728837251 20 DILICGEKIALISDKISPNLPDVEIIDANGKTVTPGFIDQHVHitgaGGKHGFQS 74
Cdd:PRK07369 23 DVLIEDGKIQAIEPHIDPIPPDTQIIDASGLILGPGLVDLYSH----SGEPGFEE 73
|
|
| PRK09059 |
PRK09059 |
dihydroorotase; Validated |
20-70 |
8.35e-03 |
|
dihydroorotase; Validated
Pssm-ID: 181631 [Multi-domain] Cd Length: 429 Bit Score: 38.09 E-value: 8.35e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 2728837251 20 DILICGEKI-ALISDKISPNLPD-VEIIDANGKTVTPGFIDQHVHITGAGGKH 70
Cdd:PRK09059 24 TVLIEDGVIvAAGKGAGNQGAPEgAEIVDCAGKAVAPGLVDARVFVGEPGAEH 76
|
|
| |
