|
Name |
Accession |
Description |
Interval |
E-value |
| SsnA |
COG0402 |
Cytosine/adenosine deaminase or related metal-dependent hydrolase [Nucleotide transport and ... |
9-388 |
1.06e-62 |
|
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: 207.37 E-value: 1.06e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32445787 9 YRARWVMPIDGD--PIPNGMMIVQSGRIASISSFQDSKNEG---ELIDLGDVAILPGLVNTHTHLEFSDLpkpVGHT-GM 82
Cdd:COG0402 4 IRGAWVLTMDPAggVLEDGAVLVEDGRIAAVGPGAELPARYpaaEVIDAGGKLVLPGLVNTHTHLPQTLL---RGLAdDL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32445787 83 ELADWIREVI-TTRGMVDHQTRQQNVLKGHAEATASGTQLIADIETTPMESiAPNTIAFAEVLGL--------------- 146
Cdd:COG0402 81 PLLDWLEEYIwPLEARLDPEDVYAGALLALAEMLRSGTTTVADFYYVHPES-ADALAEAAAEAGIravlgrglmdrgfpd 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32445787 147 -SQERGDERMSQAERHLAN-NTSPDSRCDVAaISPHAPYSTPLPLIERCVQVAKQRKTTLAMHVAESPAERELLTNGSGp 224
Cdd:COG0402 160 gLREDADEGLADSERLIERwHGAADGRIRVA-LAPHAPYTVSPELLRAAAALARELGLPLHTHLAETRDEVEWVLELYG- 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32445787 225 faeslrtlglpieaffpwtkANPVSHLIQLLAKSPRALIVHGNDLSETEIEQVKSHpNCSIVYCPRTHHFFQHSNHPVAE 304
Cdd:COG0402 238 --------------------KRPVEYLDELGLLGPRTLLAHCVHLTDEEIALLAET-GASVAHCPTSNLKLGSGIAPVPR 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32445787 305 LLAAGINVAIGTDSRASNPDLDLWGEVQHLLK-------HRPDLNPTDVLRMATANGADALGRSATHGRLAAGMPANFIT 377
Cdd:COG0402 297 LLAAGVRVGLGTDGAASNNSLDMFEEMRLAALlqrlrggDPTALSAREALEMATLGGARALGLDDEIGSLEPGKRADLVV 376
|
410
....*....|....*...
gi 32445787 378 V-------ATSADRVDQL 388
Cdd:COG0402 377 LdldaphlAPLHDPLSAL 394
|
|
| Met_dep_hydrolase_D |
cd01312 |
Metallo-dependent hydrolases, subgroup D is part of the superfamily of metallo-dependent ... |
57-375 |
7.17e-49 |
|
Metallo-dependent hydrolases, subgroup D 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: 238637 [Multi-domain] Cd Length: 381 Bit Score: 170.32 E-value: 7.17e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32445787 57 ILPGLVNTHTHLEFSDLPKPvGHTGmELADWIREVITTRGMVDHQTRQQNVLKGHAEATASGTQLIADIET-----TPME 131
Cdd:cd01312 29 LLPGLINAHTHLEFSANVAQ-FTYG-RFRAWLLSVINSRDELLKQPWEEAIRQGIRQMLESGTTSIGAISSdgsllPALA 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32445787 132 SIAPNTIAFAEVLGLSQERGDERMSQAERHLANNTSPDSRCDVAAISPHAPYSTPLPLIERCVQVAKQRKTTLAMHVAES 211
Cdd:cd01312 107 SSGLRGVFFNEVIGSNPSAIDFKGETFLERFKRSKSFESQLFIPAISPHAPYSVHPELAQDLIDLAKKLNLPLSTHFLES 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32445787 212 PAERELLTNGSGPFAESLrtlglpiEAFFPWTK----ANPVSHLIQLLAKSPRALIVHGNDLSETEIEQVKSHpNCSIVY 287
Cdd:cd01312 187 KEEREWLEESKGWFKHFW-------ESFLKLPKpkklATAIDFLDMLGGLGTRVSFVHCVYANLEEAEILASR-GASIAL 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32445787 288 CPRTHHFFQHSNHPVAELLAAGINVAIGTDSRASNPDLDLWGEVQHLL-KHR-PDLN--PTDVLRMATANGADALGRSAt 363
Cdd:cd01312 259 CPRSNRLLNGGKLDVSELKKAGIPVSLGTDGLSSNISLSLLDELRALLdLHPeEDLLelASELLLMATLGGARALGLNN- 337
|
330
....*....|..
gi 32445787 364 hGRLAAGMPANF 375
Cdd:cd01312 338 -GEIEAGKRADF 348
|
|
| ATZ_TRZ_like |
cd01298 |
TRZ/ATZ family contains enzymes from the atrazine degradation pathway and related hydrolases. ... |
14-378 |
1.23e-43 |
|
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: 156.98 E-value: 1.23e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32445787 14 VMPIDGDPIPNGMMIVQSGRIASISS--FQDSKNEGELIDLGDVAILPGLVNTHTHLeFSDLPKPVGhTGMELADWIREV 91
Cdd:cd01298 9 VTTDPRRVLEDGDVLVEDGRIVAVGPalPLPAYPADEVIDAKGKVVMPGLVNTHTHL-AMTLLRGLA-DDLPLMEWLKDL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32445787 92 I------TTRGMVDHQTRQqnvlkGHAEATASGTQLIADiettpMESIAPNTIAFA-EVLGL-------SQERGDERMSQ 157
Cdd:cd01298 87 IwplerlLTEEDVYLGALL-----ALAEMIRSGTTTFAD-----MYFFYPDAVAEAaEELGIravlgrgIMDLGTEDVEE 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32445787 158 AERHLANNTS--------PDSRCDVAaISPHAPYSTPLPLIERCVQVAKQRKTTLAMHVAESPAERElltngsgpfaESL 229
Cdd:cd01298 157 TEEALAEAERlirewhgaADGRIRVA-LAPHAPYTCSDELLREVAELAREYGVPLHIHLAETEDEVE----------ESL 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32445787 230 RTLGLPieaffpwtkanPVSHLIQLLAKSPRALIVHGNDLSETEIEQVKSHpNCSIVYCPRthhffqhSNH-------PV 302
Cdd:cd01298 226 EKYGKR-----------PVEYLEELGLLGPDVVLAHCVWLTDEEIELLAET-GTGVAHNPA-------SNMklasgiaPV 286
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32445787 303 AELLAAGINVAIGTDSRASNPDLDLWGEV-QHLLKHRPD------LNPTDVLRMATANGADALGRSAThGRLAAGMPANF 375
Cdd:cd01298 287 PEMLEAGVNVGLGTDGAASNNNLDMFEEMrLAALLQKLAhgdptaLPAEEALEMATIGGAKALGLDEI-GSLEVGKKADL 365
|
...
gi 32445787 376 ITV 378
Cdd:cd01298 366 ILI 368
|
|
| PRK08418 |
PRK08418 |
metal-dependent hydrolase; |
34-378 |
4.10e-40 |
|
metal-dependent hydrolase;
Pssm-ID: 181419 [Multi-domain] Cd Length: 408 Bit Score: 147.42 E-value: 4.10e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32445787 34 IASISSFQDSKNEGELIDLGDVAILPGLVNTHTHLEFSdlpkpVGHTGMELAD---WIREVITTRGMVDHQTRQQNVLKG 110
Cdd:PRK08418 33 IGDYENLKKKYPNAKIQFFKNSVLLPAFINPHTHLEFS-----ANKTTLDYGDfipWLGSVINHREDLLEKCKGALIQQA 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32445787 111 HAEATASGTQLIADI-----ETTPMESIAPNTIAFAEVLGLSQERGDERMSQAERHLANNTSPDSRCDVAAISPHAPYST 185
Cdd:PRK08418 108 INEMLKSGVGTIGAIssfgiDLEICAKSPLRVVFFNEILGSNASAVDELYQDFLARFEESKKFKSKKFIPAIAIHSPYSV 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32445787 186 PLPLIERCVQVAKQRKTTLAMHVAESPAERELLTNGSGPFAESLrtlglpiEAFFPWTKA--NPVSHLIQLlaKSPRALI 263
Cdd:PRK08418 188 HPILAKKALQLAKKENLLVSTHFLESKAEREWLEESKGWFKKFF-------EKFLKEPKPlyTPKEFLELF--KGLRTLF 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32445787 264 VHGNDLSETEIEQVKShPNCSIVYCPRTHHFFQHSNHPVAELLAAGINVAIGTDSRASNPDLDLWGEVQ-HLLKHrPDLN 342
Cdd:PRK08418 259 THCVYASEEELEKIKS-KNASITHCPFSNRLLSNKALDLEKAKKAGINYSIATDGLSSNISLSLLDELRaALLTH-ANMP 336
|
330 340 350 360
....*....|....*....|....*....|....*....|
gi 32445787 343 P----TDVLRMATANGADALGRSAthGRLAAGMPANFITV 378
Cdd:PRK08418 337 LlelaKILLLSATRYGAKALGLNN--GEIKEGKDADLSVF 374
|
|
| PRK09045 |
PRK09045 |
TRZ/ATZ family hydrolase; |
11-382 |
9.91e-32 |
|
TRZ/ATZ family hydrolase;
Pssm-ID: 236366 [Multi-domain] Cd Length: 443 Bit Score: 125.02 E-value: 9.91e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32445787 11 ARWVMPID--GDPIPNGMMIVQSGRIASISSFQDSK---NEGELIDLGDVAILPGLVNTHTHLEFS-------DLPkpvg 78
Cdd:PRK09045 13 ARWIVPVEpaGVVLEDHAVAIRDGRIVAILPRAEARaryAAAETVELPDHVLIPGLINAHTHAAMSllrgladDLP---- 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32445787 79 htgmeLADWIREVI--TTRGMVDHQTRQQNVLKGHAEATASGTQLIADIETTP-----------ME-SIAPNTIAFAEVL 144
Cdd:PRK09045 89 -----LMTWLQDHIwpAEGAWVSEEFVRDGTLLAIAEMLRGGTTCFNDMYFFPeaaaeaahqagMRaQIGMPVLDFPTAW 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32445787 145 GLSQE----RGDERMSQAERHlanntspdSRCDVAaISPHAPYSTPLPLIERCVQVAKQRKTTLAMHVAESPAErelltn 220
Cdd:PRK09045 164 ASDADeylaKGLELHDQWRHH--------PLISTA-FAPHAPYTVSDENLERIRTLAEQLDLPIHIHLHETAQE------ 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32445787 221 gsgpFAESLRTLGLpieaffpwtkaNPVSHLIQLLAKSPRALIVHGNDLSETEIEQVKSHpNCSIVYCPRthhffqhSN- 299
Cdd:PRK09045 229 ----IADSLKQHGQ-----------RPLARLARLGLLGPRLIAVHMTQLTDAEIALLAET-GCSVVHCPE-------SNl 285
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32445787 300 ------HPVAELLAAGINVAIGTDSRASNPDLDLWGEVQH--LLKHRPDLNPTDV-----LRMATANGADALGRSATHGR 366
Cdd:PRK09045 286 klasgfCPVAKLLQAGVNVALGTDGAASNNDLDLFGEMRTaaLLAKAVAGDATALpahtaLRMATLNGARALGLDDEIGS 365
|
410
....*....|....*.
gi 32445787 367 LAAGMPANFITVATSA 382
Cdd:PRK09045 366 LEPGKQADLVAVDLSG 381
|
|
| Amidohydro_1 |
pfam01979 |
Amidohydrolase family; This family of enzymes are a a large metal dependent hydrolase ... |
57-380 |
9.67e-28 |
|
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: 112.21 E-value: 9.67e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32445787 57 ILPGLVNTHTHLEFSDLPKPVghtgmeladwirevittrgmVDHQTRQQNVLKGHAEATASGTQLIAD-IETTP------ 129
Cdd:pfam01979 2 VLPGLIDAHVHLEMGLLRGIP--------------------VPPEFAYEALRLGITTMLKSGTTTVLDmGATTStgieal 61
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32445787 130 ---MESIAPNTIAFAEVLGLSQER-GDERMSQAERHLAnntSPDSRCD------VAAISPHAPYSTPLPLIERCVQVAKQ 199
Cdd:pfam01979 62 leaAEELPLGLRFLGPGCSLDTDGeLEGRKALREKLKA---GAEFIKGmadgvvFVGLAPHGAPTFSDDELKAALEEAKK 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32445787 200 RKTTLAMHVAESPAERELLTNGSGPFAESlrtlGLPIEAffpwtkANPVSHLiqllaKSPRALIVHGNDLSETEIEQVKS 279
Cdd:pfam01979 139 YGLPVAIHALETKGEVEDAIAAFGGGIEH----GTHLEV------AESGGLL-----DIIKLILAHGVHLSPTEANLLAE 203
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32445787 280 H-PNCSIVYCPRTHHFFQHSNHPVAELLAAGINVAIGTDSRASNPDLDLWGEVQHLLKHRPD----LNPTDVLRMATANG 354
Cdd:pfam01979 204 HlKGAGVAHCPFSNSKLRSGRIALRKALEDGVKVGLGTDGAGSGNSLNMLEELRLALELQFDpeggLSPLEALRMATINP 283
|
330 340
....*....|....*....|....*.
gi 32445787 355 ADALGRSATHGRLAAGMPANFITVAT 380
Cdd:pfam01979 284 AKALGLDDKVGSIEVGKDADLVVVDL 309
|
|
| PRK06038 |
PRK06038 |
N-ethylammeline chlorohydrolase; Provisional |
13-378 |
4.03e-25 |
|
N-ethylammeline chlorohydrolase; Provisional
Pssm-ID: 180363 [Multi-domain] Cd Length: 430 Bit Score: 106.37 E-value: 4.03e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32445787 13 WVMPIDGDPIPNGMMIVQSGRIASISSfQDSKNEGELIDLGDVAILPGLVNTHTHLEFS-------DLPkpvghtgmeLA 85
Cdd:PRK06038 10 YVLTMDAGDLKKGSVVIEDGTITEVSE-STPGDADTVIDAKGSVVMPGLVNTHTHAAMTlfrgyadDLP---------LA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32445787 86 DWIREVITTrgmVDHQTRQQNVLKGH----AEATASGTQLIADIETTpMESIAPNTIAFAEVLGLS--------QERGDE 153
Cdd:PRK06038 80 EWLNDHIWP---AEAKLTAEDVYAGSllacLEMIKSGTTSFADMYFY-MDEVAKAVEESGLRAALSygmidlgdDEKGEA 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32445787 154 RMSQAERHLAN-NTSPDSRCDVAaISPHAPYSTPLPLIERCVQVAKQRKTTLAMHVAESPAERELLTNGSGpfaeslrtl 232
Cdd:PRK06038 156 ELKEGKRFVKEwHGAADGRIKVM-YGPHAPYTCSEEFLSKVKKLANKDGVGIHIHVLETEAELNQMKEQYG--------- 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32445787 233 glpieaffpwtkANPVSHLIQLLAKSPRALIVHGNDLSETEIEqVKSHPNCSIVYCPRTHHFFQHSNHPVAELLAAGINV 312
Cdd:PRK06038 226 ------------MCSVNYLDDIGFLGPDVLAAHCVWLSDGDIE-ILRERGVNVSHNPVSNMKLASGIAPVPKLLERGVNV 292
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 32445787 313 AIGTDSRASNPDLDLWGEVQ--HLLKHRPDLNPT-----DVLRMATANGADALGRSAthGRLAAGMPANFITV 378
Cdd:PRK06038 293 SLGTDGCASNNNLDMFEEMKtaALLHKVNTMDPTalparQVLEMATVNGAKALGINT--GMLKEGYLADIIIV 363
|
|
| PRK08393 |
PRK08393 |
N-ethylammeline chlorohydrolase; Provisional |
27-362 |
2.39e-23 |
|
N-ethylammeline chlorohydrolase; Provisional
Pssm-ID: 181411 [Multi-domain] Cd Length: 424 Bit Score: 101.03 E-value: 2.39e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32445787 27 MIVQSGRIASISSfQDSKNEGELIDLGDVAILPGLVNTHTHLEF-------SDLPkpvghtgmeLADWIREVITTRgmvD 99
Cdd:PRK08393 23 VLIEGNKIVEVKR-NINKPADTVIDASGSVVSPGFINAHTHSPMvllrglaDDVP---------LMEWLQNYIWPR---E 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32445787 100 HQTRQQNV----LKGHAEATASGTQLIADIETTpMESIAPNTIAFAEVLGLS--------QERGDERMSQAERHLANNTS 167
Cdd:PRK08393 90 RKLKRKDIywgaYLGLLEMIKSGTTTFVDMYFH-MEEVAKATLEVGLRGYLSygmvdlgdEEKREKEIKETEKLMEFIEK 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32445787 168 PDSRCDVAAISPHAPYSTPLPLIERCVQVAKQRKTTLAMHVAESPAERELLTNGSGpfaeslrtlglpieaffpwtkANP 247
Cdd:PRK08393 169 LNSPRVHFVFGPHAPYTCSLALLKWVREKAREWNKLITIHLSETMDEIKQIREKYG---------------------KSP 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32445787 248 VSHLIQLLAKSPRALIVHGNDLSETEIEQVKSHpNCSIVYCPRTHHFFQHSNHPVAELLAAGINVAIGTDSRASNPDLDL 327
Cdd:PRK08393 228 VVLLDEIGFLNEDVIAAHGVWLSSRDIRILASA-GVTVAHNPASNMKLGSGVMPLRKLLNAGVNVALGTDGAASNNNLDM 306
|
330 340 350 360
....*....|....*....|....*....|....*....|..
gi 32445787 328 WGEVQ--HLLKHRPDLNPT-----DVLRMATANGADALGRSA 362
Cdd:PRK08393 307 LREMKlaALLHKVHNLDPTiadaeTVFRMATQNGAKALGLKA 348
|
|
| PRK06687 |
PRK06687 |
TRZ/ATZ family protein; |
24-378 |
4.82e-23 |
|
TRZ/ATZ family protein;
Pssm-ID: 180657 [Multi-domain] Cd Length: 419 Bit Score: 100.08 E-value: 4.82e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32445787 24 NGMMIVQSGRIASISSFQDSKNE--GELIDLGDVAILPGLVNTHTHLEFSDLpkpvghTGME----LADWIREVI-TTRG 96
Cdd:PRK06687 21 DGILAVKDSQIVYVGQDKPAFLEqaEQIIDYQGAWIMPGLVNCHTHSAMTGL------RGIRddsnLHEWLNDYIwPAES 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32445787 97 MVDHQTRQQNVLKGHAEATASGTQLIAD---------------IETTPMESIAPNTIAFAEVlglsqERGDERMSQAERH 161
Cdd:PRK06687 95 EFTPDMTTNAVKEALTEMLQSGTTTFNDmynpngvdiqqiyqvVKTSKMRCYFSPTLFSSET-----ETTAETISRTRSI 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32445787 162 LANNTSPDSRCDVAAISPHAPYSTPLPLIERCVQVAKQRKTTLAMHVAESPAERELLTNGSGpfaeslrtlglpieaffp 241
Cdd:PRK06687 170 IDEILKYKNPNFKVMVAPHSPYSCSRDLLEASLEMAKELNIPLHVHVAETKEESGIILKRYG------------------ 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32445787 242 wtkANPVSHLIQLLAKSPRALIVHGNDLSETEIEQVKSHPnCSIVYCPRTHHFFQHSNHPVAELLAAGINVAIGTDSRAS 321
Cdd:PRK06687 232 ---KRPLAFLEELGYLDHPSVFAHGVELNEREIERLASSQ-VAIAHNPISNLKLASGIAPIIQLQKAGVAVGIATDSVAS 307
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 32445787 322 NPDLDLW--GEVQHLLKHRPDLNPTD-----VLRMATANGADALGRSATHGRLAAGMPANFITV 378
Cdd:PRK06687 308 NNNLDMFeeGRTAALLQKMKSGDASQfpietALKVLTIEGAKALGMENQIGSLEVGKQADFLVI 371
|
|
| HutI |
COG1228 |
Imidazolonepropionase or related amidohydrolase [Secondary metabolites biosynthesis, transport ... |
11-383 |
1.63e-21 |
|
Imidazolonepropionase or related amidohydrolase [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 440841 [Multi-domain] Cd Length: 386 Bit Score: 95.41 E-value: 1.63e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32445787 11 ARWVMPIDGDPIPNGMMIVQSGRIASISSFQDSK--NEGELIDLGDVAILPGLVNTHTHLEFSDLPKPVGHTGMELADWI 88
Cdd:COG1228 15 ATLVDGTGGGVIENGTVLVEDGKIAAVGPAADLAvpAGAEVIDATGKTVLPGLIDAHTHLGLGGGRAVEFEAGGGITPTV 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32445787 89 REVITTRGMVDhQTRQQNV---------LKGHAEATASGTQLIADietTPMesIAPNTIAFAEVLGLSQERGDERMSQAE 159
Cdd:COG1228 95 DLVNPADKRLR-RALAAGVttvrdlpggPLGLRDAIIAGESKLLP---GPR--VLAAGPALSLTGGAHARGPEEARAALR 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32445787 160 RHLANNTSpdsRCDVAAISPHAPYStpLPLIERCVQVAKQRKTTLAMHVAESPAERELLTNGsgpfAESLRTLGLPIEAf 239
Cdd:COG1228 169 ELLAEGAD---YIKVFAEGGAPDFS--LEELRAILEAAHALGLPVAAHAHQADDIRLAVEAG----VDSIEHGTYLDDE- 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32445787 240 fpwtkanpvshLIQLLAKSPRALIVHGNDLSETEIEQVKSHPNcsivycPRTHHFFQHSNHPVAELLAAGINVAIGTDS- 318
Cdd:COG1228 239 -----------VADLLAEAGTVVLVPTLSLFLALLEGAAAPVA------AKARKVREAALANARRLHDAGVPVALGTDAg 301
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 32445787 319 RASNPDLDLWGEVQHLLKHRpdLNPTDVLRMATANGADALGRSATHGRLAAGMPANFitVATSAD 383
Cdd:COG1228 302 VGVPPGRSLHRELALAVEAG--LTPEEALRAATINAAKALGLDDDVGSLEPGKLADL--VLLDGD 362
|
|
| PRK15493 |
PRK15493 |
bifunctional S-methyl-5'-thioadenosine deaminase/S-adenosylhomocysteine deaminase; |
22-378 |
2.95e-19 |
|
bifunctional S-methyl-5'-thioadenosine deaminase/S-adenosylhomocysteine deaminase;
Pssm-ID: 185390 [Multi-domain] Cd Length: 435 Bit Score: 89.35 E-value: 2.95e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32445787 22 IPNGMMIVQSGRIASISS--FQDSKNEGELIDLGDVAILPGLVNTHTHLEFSdLPKPVGHTgMELADWIREVI-TTRGMV 98
Cdd:PRK15493 20 IENGYIIVENDQIIDVNSgeFASDFEVDEVIDMKGKWVLPGLVNTHTHVVMS-LLRGIGDD-MLLQPWLETRIwPLESQF 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32445787 99 DHQTRQQNVLKGHAEATASGTQLIADI-------ETTPMESIAPNTIAFAEVLGL----SQERGDERMSQAERHLANNTS 167
Cdd:PRK15493 98 TPELAVASTELGLLEMVKSGTTSFSDMfnpigvdQDAIMETVSRSGMRAAVSRTLfsfgTKEDEKKAIEEAEKYVKRYYN 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32445787 168 pDSRCDVAAISPHAPYSTPLPLIERCVQVAKQRKTTLAMHVAESpaERELLTngsgpfaeslrtlglpIEAFFpwtKANP 247
Cdd:PRK15493 178 -ESGMLTTMVAPHSPYTCSTELLEECARIAVENQTMVHIHLSET--EREVRD----------------IEAQY---GKRP 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32445787 248 VSHLIQL-LAKSPrALIVHGNDLSETEIEQVKSHpNCSIVYCPRTHHFFQHSNHPVAELLAAGINVAIGTDSRASNPDLD 326
Cdd:PRK15493 236 VEYAASCgLFKRP-TVIAHGVVLNDNERAFLAEH-DVRVAHNPNSNLKLGSGIANVKAMLEAGIKVGIATDSVASNNNLD 313
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*....
gi 32445787 327 LWGE--VQHLLKHRPDLNPTDV-----LRMATANGADALGRSAThGRLAAGMPANFITV 378
Cdd:PRK15493 314 MFEEmrIATLLQKGIHQDATALpvetaLTLATKGAAEVIGMKQT-GSLEVGKCADFITI 371
|
|
| archeal_chlorohydrolases |
cd01305 |
Predicted chlorohydrolases. These metallo-dependent hydrolases from archea are part of the ... |
262-355 |
6.28e-19 |
|
Predicted chlorohydrolases. These metallo-dependent hydrolases from archea are 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. They 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. Some members of this subgroup are predicted to be chlorohyrolases.
Pssm-ID: 238630 [Multi-domain] Cd Length: 263 Bit Score: 85.92 E-value: 6.28e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32445787 262 LIVHGNDLSETEIEQVKSHpNCSIVYCPRTHHFFQHSNHPVAELLAAGINVAIGTDSRASNpDLDLWGEVQHLLKH---R 338
Cdd:cd01305 167 LLVHGTHLTDEDLELVREN-GVPVVLCPRSNLYFGVGIPPVAELLKLGIKVLLGTDNVMVN-EPDMWAEMEFLAKYsrlQ 244
|
90
....*....|....*..
gi 32445787 339 PDLNPTDVLRMATANGA 355
Cdd:cd01305 245 GYLSPLEILRMATVNAA 261
|
|
| metallo-dependent_hydrolases |
cd01292 |
Superfamily of metallo-dependent hydrolases (also called amidohydrolase superfamily) is a ... |
61-357 |
4.54e-17 |
|
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: 80.84 E-value: 4.54e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32445787 61 LVNTHTHLEFSDLPKPvghtgmeladWIREVITTRGMVDHQTRQQNVLKGHAEATASGTQLIADIETTPMESIAPNTIAF 140
Cdd:cd01292 1 FIDTHVHLDGSALRGT----------RLNLELKEAEELSPEDLYEDTLRALEALLAGGVTTVVDMGSTPPPTTTKAAIEA 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32445787 141 AEVLGLSQERGDERMSQAERHLANNTSPDSR------------CDVAAISPHAPYST---PLPLIERCVQVAKQRKTTLA 205
Cdd:cd01292 71 VAEAARASAGIRVVLGLGIPGVPAAVDEDAEalllellrrgleLGAVGLKLAGPYTAtglSDESLRRVLEEARKLGLPVV 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32445787 206 MHVAESPAERELLTNgsgpfaeslrtlglpieaffpwtkanpvshLIQLLAKSPRALIVHGNDLSETEIEQVKSHpNCSI 285
Cdd:cd01292 151 IHAGELPDPTRALED------------------------------LVALLRLGGRVVIGHVSHLDPELLELLKEA-GVSL 199
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 32445787 286 VYCPRTHHFFQHSN---HPVAELLAAGINVAIGTDSRASNPDLDLWGEVQHLLK-HRPDLNPTDVLRMATANGADA 357
Cdd:cd01292 200 EVCPLSNYLLGRDGegaEALRRLLELGIRVTLGTDGPPHPLGTDLLALLRLLLKvLRLGLSLEEALRLATINPARA 275
|
|
| PRK07213 |
PRK07213 |
chlorohydrolase; Provisional |
25-376 |
1.34e-15 |
|
chlorohydrolase; Provisional
Pssm-ID: 235969 [Multi-domain] Cd Length: 375 Bit Score: 77.77 E-value: 1.34e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32445787 25 GMMIVQSGRIASissFQDSKNEGELIDLGDVAIlPGLVNTHTH------------LEFSDLPKP---VGHTGM------E 83
Cdd:PRK07213 20 GNLVIEDGIIKG---FTNEVHEGNVIDAKGLVI-PPLINAHTHigdssikdigigKSLDELVKPpngLKHKFLnscsdkE 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32445787 84 LADWIREviTTRGMVDHQTR-----QQNVLKGhaeaTASGTQLIADIETTPMesiapntiafaeVLGLSQERGDERMSQA 158
Cdd:PRK07213 96 LVEGMKE--GLYDMYNNGIKafcdfREGGIKG----INLLKKASSDLPIKPI------------ILGRPTEADENELKKE 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32445787 159 ERHLANNtspdsrCDVAAISPHAPYSTP-LPLIercVQVAKQRKTTLAMHVAESPAERELltngsgpfaeSLRTLGLpie 237
Cdd:PRK07213 158 IREILKN------SDGIGLSGANEYSDEeLKFI---CKECKREKKIFSIHAAEHKGSVEY----------SLEKYGM--- 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32445787 238 affpwtkaNPVSHLIQLLAKSPraLIVHGNDLSETEIEQVKSHpNCSIVYCPRTHHFFQHSNHPVAELLAAGINVAIGTD 317
Cdd:PRK07213 216 --------TEIERLINLGFKPD--FIVHATHPSNDDLELLKEN-NIPVVVCPRANASFNVGLPPLNEMLEKGILLGIGTD 284
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 32445787 318 S-RASNPDLdlWGEVQHLLK--HrpdLNPTDVLRMATANGADALGRSAThGRLAAGMPANFI 376
Cdd:PRK07213 285 NfMANSPSI--FREMEFIYKlyH---IEPKEILKMATINGAKILGLINV-GLIEEGFKADFT 340
|
|
| PRK07228 |
PRK07228 |
5'-deoxyadenosine deaminase; |
22-385 |
2.35e-15 |
|
5'-deoxyadenosine deaminase;
Pssm-ID: 180895 [Multi-domain] Cd Length: 445 Bit Score: 77.35 E-value: 2.35e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32445787 22 IPNGMMIVQSGRIASISSFQDSKNEGELIDLGDVAILPGLVNTHTHLEFS-------DLpkpvghtgmELADWIRE-VIT 93
Cdd:PRK07228 19 IVDGDVLIEDDRIAAVGDRLDLEDYDDHIDATGKVVIPGLIQGHIHLCQTlfrgiadDL---------ELLDWLKDrIWP 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32445787 94 TRGMVDHQTRQQNVLKGHAEATASGTQLIADIET-----TPMESIAPNTI----------AFAEVLGLSQERGDERMSQA 158
Cdd:PRK07228 90 LEAAHDAESMYYSALLGIGELIESGTTTIVDMESvhhtdSAFEAAGESGIravlgkvmmdYGDDVPEGLQEDTEASLAES 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32445787 159 ER-----HLANNtspdSRCDVAaISPHAPYSTPLPLIERCVQVAKQRKTTLAMHVAESPAERELLTNGSGPF-AESLRTL 232
Cdd:PRK07228 170 VRllekwHGADN----GRIRYA-FTPRFAVSCTEELLRGVRDLADEYGVRIHTHASENRGEIETVEEETGMRnIHYLDEV 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32445787 233 GLpieaffpwtkANPvsHLIqlLAkspralivHGNDLSETE---IEQVKSHpncsIVYCPRTHHFFQHSNHPVAELLAAG 309
Cdd:PRK07228 245 GL----------TGE--DLI--LA--------HCVWLDEEEreiLAETGTH----VTHCPSSNLKLASGIAPVPDLLERG 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32445787 310 INVAIGTDSRASNPDLDLWGEV-QHLLKHRPD-LNPT-----DVLRMATANGADALGRSATHGRLAAGMPANFITVATSA 382
Cdd:PRK07228 299 INVALGADGAPCNNTLDPFTEMrQAALIQKVDrLGPTamparTVFEMATLGGAKAAGFEDEIGSLEEGKKADLAILDLDG 378
|
...
gi 32445787 383 DRV 385
Cdd:PRK07228 379 LHA 381
|
|
| PRK12393 |
PRK12393 |
amidohydrolase; Provisional |
29-376 |
1.79e-14 |
|
amidohydrolase; Provisional
Pssm-ID: 237088 [Multi-domain] Cd Length: 457 Bit Score: 74.72 E-value: 1.79e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32445787 29 VQSGRIASISSFQDSKNEgELIDLGDVAILPGLVNTHTHLeFSDLPKPVgHTGME--LADWIREV-ITTRGMVDHQTRQQ 105
Cdd:PRK12393 30 IRDGRIAAIGALTPLPGE-RVIDATDCVVYPGWVNTHHHL-FQSLLKGV-PAGINqsLTAWLAAVpYRFRARFDEDLFRL 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32445787 106 NVLKGHAEATASGTQLIADIETTPMESIAPNT--IAF--AEVLGL---------SQERGDER-MSQA------ERHLAN- 164
Cdd:PRK12393 107 AARIGLVELLRSGCTTVADHHYLYHPGMPFDTgdILFdeAEALGMrfvlcrggaTQTRGDHPgLPTAlrpetlDQMLADv 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32445787 165 --------NTSPDS--RCDVAAISPhaPYSTPLPLIERCVQVAKQRKTTLAMHVAEspaerellTNGSGPFAESLRTLgL 234
Cdd:PRK12393 187 erlvsryhDASPDSlrRVVVAPTTP--TFSLPPELLREVARAARGMGLRLHSHLSE--------TVDYVDFCREKYGM-T 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32445787 235 PIE--AFFPWTKANP-VSHLIQLLAKSPRALIVHGNdlseteieqvkshpncSIVYCPRTHHFFQHSNHPVAELLAAGIN 311
Cdd:PRK12393 256 PVQfvAEHDWLGPDVwFAHLVKLDAEEIALLAQTGT----------------GIAHCPQSNGRLGSGIAPALAMEAAGVP 319
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 32445787 312 VAIGTDSRASNPDLDLWGEVqHL--LKHRPD-----LNPTDVLRMATANGADALGRSAThGRLAAGMPANFI 376
Cdd:PRK12393 320 VSLGVDGAASNESADMLSEA-HAawLLHRAEggadaTTVEDVVHWGTAGGARVLGLDAI-GTLAVGQAADLA 389
|
|
| PRK08204 |
PRK08204 |
hypothetical protein; Provisional |
5-382 |
3.04e-12 |
|
hypothetical protein; Provisional
Pssm-ID: 181288 [Multi-domain] Cd Length: 449 Bit Score: 67.72 E-value: 3.04e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32445787 5 SKQTYRARWVMPIDGD--PIPNGMMIVQSGRIASISSFQDsKNEGELIDLGDVAILPGLVNTHTHLEFSDLpKPVGhTGM 82
Cdd:PRK08204 2 KRTLIRGGTVLTMDPAigDLPRGDILIEGDRIAAVAPSIE-APDAEVVDARGMIVMPGLVDTHRHTWQSVL-RGIG-ADW 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32445787 83 ELADWIREVitTRGMVDHQTRQQN---VLKGHAEATASGTQLIAD---IETTPMEsiapntiAFAEVLGLsQERGderMS 156
Cdd:PRK08204 79 TLQTYFREI--HGNLGPMFRPEDVyiaNLLGALEALDAGVTTLLDwshINNSPEH-------ADAAIRGL-AEAG---IR 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32445787 157 QAERHLANNTSPDSRCDvaaisphapySTPLPL--IERCVQVAKQRKT---TLAMHV----AESP--AERELltngsgpf 225
Cdd:PRK08204 146 AVFAHGSPGPSPYWPFD----------SVPHPRedIRRVKKRYFSSDDgllTLGLAIrgpeFSSWevARADF-------- 207
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32445787 226 aESLRTLGLPI---EAFFPWTK-ANPVSHLIQLLAKSPRALIVHGNDLSETEIEQVKSHpNCSIVYCPRTHHFFQHSNHP 301
Cdd:PRK08204 208 -RLARELGLPIsmhQGFGPWGAtPRGVEQLHDAGLLGPDLNLVHGNDLSDDELKLLADS-GGSFSVTPEIEMMMGHGYPV 285
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32445787 302 VAELLAAGINVAIGTDSRASNPDlDLWGEVQHLLKH------------------RPDLNPTDVLRMATANGADALGRSAT 363
Cdd:PRK08204 286 TGRLLAHGVRPSLGVDVVTSTGG-DMFTQMRFALQAerardnavhlreggmpppRLTLTARQVLEWATIEGARALGLEDR 364
|
410
....*....|....*....
gi 32445787 364 HGRLAAGMPANFITVATSA 382
Cdd:PRK08204 365 IGSLTPGKQADLVLIDATD 383
|
|
| PRK09228 |
PRK09228 |
guanine deaminase; Provisional |
4-389 |
6.82e-12 |
|
guanine deaminase; Provisional
Pssm-ID: 236419 [Multi-domain] Cd Length: 433 Bit Score: 66.75 E-value: 6.82e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32445787 4 SSKQTYRARwVMPIDGDP-----------IPNGMMIVQSGRIASISSFQDSK----NEGELIDLGDVAILPGLVNTHTHL 68
Cdd:PRK09228 1 MTTKAYRGR-LLHFTADPaevddedalryIEDGLLLVEDGRIVAAGPYAELRaqlpADAEVTDYRGKLILPGFIDTHIHY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32445787 69 EFSDLpkpVGHTGMELADWIREVI--TTRGMVDhqtrqqnvlKGHAEATASG--TQLIADIETTPMesiapntiAFAEVl 144
Cdd:PRK09228 80 PQTDM---IASYGEQLLDWLNTYTfpEERRFAD---------PAYAREVAEFflDELLRNGTTTAL--------VFGTV- 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32445787 145 glSQERGDERMSQAERH---------LANNTSPDSRCDVA----------------------AISPH-APYSTPLPLiER 192
Cdd:PRK09228 139 --HPQSVDALFEAAEARnmrmiagkvLMDRNAPDGLRDTAesgyddskalierwhgkgrllyAITPRfAPTSTPEQL-EA 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32445787 193 CVQVAKQRKTT-LAMHVAESPAE----RELltngsgpfaeslrtlglpieafFPWTKAN-PVSHLIQLLakSPRALIVHG 266
Cdd:PRK09228 216 AGALAREHPDVwIQTHLSENLDEiawvKEL----------------------FPEARDYlDVYERYGLL--GPRAVFAHC 271
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32445787 267 NDLSETEIeQVKSHPNCSIVYCPrTHHFFQHSN-HPVAELLAAGINVAIGTDSRASNP-----DLDLWGEVQHLLKHRpd 340
Cdd:PRK09228 272 IHLEDRER-RRLAETGAAIAFCP-TSNLFLGSGlFDLKRADAAGVRVGLGTDVGGGTSfsmlqTMNEAYKVQQLQGYR-- 347
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*..
gi 32445787 341 LNPTDVLRMATANGADALGRSATHGRLAAGMPANFITV---ATSA-----DRVDQLW 389
Cdd:PRK09228 348 LSPFQAFYLATLGGARALGLDDRIGNLAPGKEADFVVLdpaATPLlalrtARAESLE 404
|
|
| GDEase |
cd01303 |
Guanine deaminase (GDEase). Guanine deaminase is an aminohydrolase responsible for the ... |
24-389 |
9.93e-12 |
|
Guanine deaminase (GDEase). Guanine deaminase is an aminohydrolase responsible for the conversion of guanine to xanthine and ammonia, the first step to utilize guanine as a nitrogen source. This reaction also removes the guanine base from the pool and therefore can play a role in the regulation of cellular GTP and the guanylate nucleotide pool.
Pssm-ID: 238628 [Multi-domain] Cd Length: 429 Bit Score: 66.15 E-value: 9.93e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32445787 24 NGMMIVQSGRIASISS----FQDSKNEGELIDLGDVAILPGLVNTHTHleFSDLPKPVGHTGMELADWIrEVIT---TRG 96
Cdd:cd01303 26 DGLIVVVDGNIIAAGAaetlKRAAKPGARVIDSPNQFILPGFIDTHIH--APQYANIGSGLGEPLLDWL-ETYTfpeEAK 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32445787 97 MVDHQtrqqnvlkgHAEATASG--TQLIADIETTPM--ESIAP-NTIAFAEvlgLSQERGdermsqaERHLA-----NNT 166
Cdd:cd01303 103 FADPA---------YAREVYGRflDELLRNGTTTACyfATIHPeSTEALFE---EAAKRG-------QRAIAgkvcmDRN 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32445787 167 SPDSRCDVA-----------------------AISPH-APYSTPlPLIERCVQVAKQRKTTLAM-HVAESPAERElltng 221
Cdd:cd01303 164 APEYYRDTAessyrdtkrlierwhgksgrvkpAITPRfAPSCSE-ELLAALGKLAKEHPDLHIQtHISENLDEIA----- 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32445787 222 sgpFAESLrtlglpieafFPwtKANPVSHLIQ---LLakSPRALIVHGNDLSETEIEQVKSHpNCSIVYCPRTHHFFQHS 298
Cdd:cd01303 238 ---WVKEL----------FP--GARDYLDVYDkygLL--TEKTVLAHCVHLSEEEFNLLKER-GASVAHCPTSNLFLGSG 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32445787 299 NHPVAELLAAGINVAIGTDSRA-SNPD-LDLWGEV----QHL---LKHRPDLNPTDVLRMATANGADALGRSATHGRLAA 369
Cdd:cd01303 300 LFDVRKLLDAGIKVGLGTDVGGgTSFSmLDTLRQAykvsRLLgyeLGGHAKLSPAEAFYLATLGGAEALGLDDKIGNFEV 379
|
410 420
....*....|....*....|
gi 32445787 370 GMPANFITVATSADRVDQLW 389
Cdd:cd01303 380 GKEFDAVVIDPSATPLLADR 399
|
|
| PRK06380 |
PRK06380 |
metal-dependent hydrolase; Provisional |
48-368 |
2.52e-11 |
|
metal-dependent hydrolase; Provisional
Pssm-ID: 180548 [Multi-domain] Cd Length: 418 Bit Score: 64.90 E-value: 2.52e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32445787 48 ELIDLGDVAILPGLVNTHTHlefsdlpkpVGHTGME-LAD--WIREVITTRGMVDHQTRQQNVLK----GHAEATASGTQ 120
Cdd:PRK06380 43 YIIDATGKVVMPGLINTHAH---------VGMTASKgLFDdvDLEEFLMKTFKYDSKRTREGIYNsaklGMYEMINSGIT 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32445787 121 LIADIETTPmesiapNTIA-FAEVLG-------------LSQERGDErMSQAERHLANNTSPdsRCDVAAISPHAPYSTP 186
Cdd:PRK06380 114 AFVDLYYSE------DIIAkAAEELGiraflswavldeeITTQKGDP-LNNAENFIREHRNE--ELVTPSIGVQGIYVAN 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32445787 187 LPLIERCVQVAKQRKTTLAMHVAESPAErelltngsgpFAESLRTLGLpieaffpwtkaNPVSHLIQLLAKSPRALIVHG 266
Cdd:PRK06380 185 DETYLKAKEIAEKYDTIMHMHLSETRKE----------VYDHVKRTGE-----------RPVEHLEKIGFLNSKLIAAHC 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32445787 267 NDLSETEIeQVKSHPNCSIVYCPRTH-HFFQHSNHPVAELLAAGINVAIGTDSRASNPDLDLWGEVQ-HLLKH---RPD- 340
Cdd:PRK06380 244 VWATYHEI-KLLSKNGVKVSWNSVSNfKLGTGGSPPIPEMLDNGINVTIGTDSNGSNNSLDMFEAMKfSALSVkneRWDa 322
|
330 340 350
....*....|....*....|....*....|...
gi 32445787 341 --LNPTDVLRMATANGADAL---GRSATHGRLA 368
Cdd:PRK06380 323 siIKAQEILDFATINAAKALelnAGSIEVGKLA 355
|
|
| hutI |
TIGR01224 |
imidazolonepropionase; This enzyme catalyzes the third step in histidine degradation. [Energy ... |
22-376 |
3.60e-11 |
|
imidazolonepropionase; This enzyme catalyzes the third step in histidine degradation. [Energy metabolism, Amino acids and amines]
Pssm-ID: 273512 [Multi-domain] Cd Length: 377 Bit Score: 64.35 E-value: 3.60e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32445787 22 IPNGMMIVQSGRIASISSFQDSKNEG--ELIDLGDVAILPGLVNTHTHLEFSdlpkpvGHTGMELADWIR-----EVITT 94
Cdd:TIGR01224 1 IEDAVILIHGGKIVWIGQLAALPGEEatEIIDCGGGLVTPGLVDPHTHLVFA------GDRVNEFEMKLQgasylEILAQ 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32445787 95 RGMVDHQTRqqnvlkghAEATASGTQLIADIET--TPMESIAPNTIAFAEVLGLSQErGDERMSQAERHLANN--TSPDS 170
Cdd:TIGR01224 75 GGGILSTVR--------ATRAASEEELLKLALFrlKSMLRSGTTTAEVKSGYGLDLE-TELKMLRAAKALHEEqpVDVVT 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32445787 171 RCDVAAISPHAPYSTPLPLIER-CVQVAKQRKTtlamhvaESPAERELLTNGSGPF--AESLRTLGLPIEAFFPWT-KAN 246
Cdd:TIGR01224 146 TFLGAHAVPPEFQGRPDDYVDGiCEELIPQVAE-------EGLASFADVFCEAGVFsvEQSRRILQAAQEAGLPVKlHAE 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32445787 247 PVSHL--IQLLAKSPRALIVHGNDLSETEIEQVKSHpNCSIVYCPRTHHFFQHSNHPVAELLAAGINVAIGTD-SRASNP 323
Cdd:TIGR01224 219 ELSNLggAELAAKLGAVSADHLEHASDAGIKALAEA-GTVAVLLPGTTFYLRETYPPARQLIDYGVPVALATDlNPGSSP 297
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|...
gi 32445787 324 DLDLwGEVQHLLKHRPDLNPTDVLRMATANGADALGRSATHGRLAAGMPANFI 376
Cdd:TIGR01224 298 TLSM-QLIMSLACRLMKMTPEEALHAATVNAAYALGLGEERGTLEAGRDADLV 349
|
|
| PRK06151 |
PRK06151 |
N-ethylammeline chlorohydrolase; Provisional |
10-389 |
5.69e-11 |
|
N-ethylammeline chlorohydrolase; Provisional
Pssm-ID: 180428 [Multi-domain] Cd Length: 488 Bit Score: 63.91 E-value: 5.69e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32445787 10 RARWVMPIDGDP---IPNGMMIVQSGRIAsissFQDSKNEGEL---IDLGDVAILPGLVNT-------HTHLEFSDLPKp 76
Cdd:PRK06151 6 KARWVLGFDDGDhrlLRDGEVVFEGDRIL----FVGHRFDGEVdrvIDAGNALVGPGFIDLdalsdldTTILGLDNGPG- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32445787 77 VGHTGMELADWIRevittRGMVDHQTRQQNVLKghaeATASGTQLIADIETTPMEsIA--------------PNTIAFAE 142
Cdd:PRK06151 81 WAKGRVWSRDYVE-----AGRREMYTPEELAFQ----KRYAFAQLLRNGITTAMP-IAslfyrqwaetyaefAAAAEAAG 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32445787 143 VLGL-------------------------SQERGDERMSQAERHLANNTSPDSRCDVAAISPHAPYSTPLPLIERCVQVA 197
Cdd:PRK06151 151 RLGLrvylgpayrsggsvleadgslevvfDEARGLAGLEEAIAFIKRVDGAHNGLVRGMLAPDRIETCTVDLLRRTAAAA 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32445787 198 KQRKTTLAMHVAESPAERELLT--NGSGPfAESLRTLGLpieaffpwtkanpvshliqllaKSPRALIVHGNDLSETEIE 275
Cdd:PRK06151 231 RELGCPVRLHCAQGVLEVETVRrlHGTTP-LEWLADVGL----------------------LGPRLLIPHATYISGSPRL 287
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32445787 276 QVKSHPN--------CSIVYCPRThhFFQHSN--HPVAELLAAGINVAIGTDSraSNPD----LDLWGEVQHLLKHRPD- 340
Cdd:PRK06151 288 NYSGGDDlallaehgVSIVHCPLV--SARHGSalNSFDRYREAGINLALGTDT--FPPDmvmnMRVGLILGRVVEGDLDa 363
|
410 420 430 440
....*....|....*....|....*....|....*....|....*....
gi 32445787 341 LNPTDVLRMATANGADALGRSAThGRLAAGMPANFITVATSADRVDQLW 389
Cdd:PRK06151 364 ASAADLFDAATLGGARALGRDDL-GRLAPGAKADIVVFDLDGLHMGPVF 411
|
|
| Imidazolone-5PH |
cd01296 |
Imidazolonepropionase/imidazolone-5-propionate hydrolase (Imidazolone-5PH) catalyzes the third ... |
265-388 |
1.27e-10 |
|
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: 62.66 E-value: 1.27e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32445787 265 HGNDLSETEIEQVKShPNCSIVYCPRTHHFFQHSNHPVAELLAAGINVAIGTDSRASNPDLDLWGEVQHLLKHRPDLNPT 344
Cdd:cd01296 235 HLEHTSDEGIAALAE-AGTVAVLLPGTAFSLRETYPPARKLIDAGVPVALGTDFNPGSSPTSSMPLVMHLACRLMRMTPE 313
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 32445787 345 DVLRMATANGADALGRSATHGRLAAGMPANFITVatSADRVDQL 388
Cdd:cd01296 314 EALTAATINAAAALGLGETVGSLEVGKQADLVIL--DAPSYEHL 355
|
|
| PRK08203 |
PRK08203 |
hydroxydechloroatrazine ethylaminohydrolase; Reviewed |
22-375 |
3.41e-10 |
|
hydroxydechloroatrazine ethylaminohydrolase; Reviewed
Pssm-ID: 236184 [Multi-domain] Cd Length: 451 Bit Score: 61.41 E-value: 3.41e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32445787 22 IPNGMMIVQSGRIASI-SSFQDSKNEGELIDLGDVAILPGLVNTHTHLEFS---DLPKPVGHtgmELADWIREVITTRGM 97
Cdd:PRK08203 21 IADGGLVVEGGRIVEVgPGGALPQPADEVFDARGHVVTPGLVNTHHHFYQTltrALPAAQDA---ELFPWLTTLYPVWAR 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32445787 98 VDHQTRQQNVLKGHAEATASGTQLIAD---IETTPMESIAPNTIAFAEVLGL-------------SQ---------ERGD 152
Cdd:PRK08203 98 LTPEMVRVATQTALAELLLSGCTTSSDhhyLFPNGLRDALDDQIEAAREIGMrfhatrgsmslgeSDgglppdsvvEDED 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32445787 153 ERMSQAERHLA--NNTSPDSRCDVAaISPHAPYSTPLPLIERCVQVAKQRKTTLAMHVAESPAERELltngsgpfaeSLR 230
Cdd:PRK08203 178 AILADSQRLIDryHDPGPGAMLRIA-LAPCSPFSVSRELMRESAALARRLGVRLHTHLAETLDEEAF----------CLE 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32445787 231 TLGLpieaffpwtkaNPVSHLIQLLAKSPRALIVHGNDLSETEIEQVkSHPNCSIVYCPrthhffqHSNH-------PVA 303
Cdd:PRK08203 247 RFGM-----------RPVDYLEDLGWLGPDVWLAHCVHLDDAEIARL-ARTGTGVAHCP-------CSNMrlasgiaPVR 307
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 32445787 304 ELLAAGINVAIGTDSRASNPDLDLWGEVQHLL-----KHRPD-LNPTDVLRMATANGADALGRSAThGRLAAGMPANF 375
Cdd:PRK08203 308 ELRAAGVPVGLGVDGSASNDGSNLIGEARQALllqrlRYGPDaMTAREALEWATLGGARVLGRDDI-GSLAPGKLADL 384
|
|
| Met_dep_hydrolase_E |
cd01313 |
Metallo-dependent hydrolases, subgroup D is part of the superfamily of metallo-dependent ... |
206-379 |
5.87e-10 |
|
Metallo-dependent hydrolases, subgroup D 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: 238638 [Multi-domain] Cd Length: 418 Bit Score: 60.55 E-value: 5.87e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32445787 206 MHVAESPAErelltngsgpfaeslrtlglpIEAFFPWTKANPVSHLIQLLAKSPRALIVHGNDLSETEIEQV-KSHPNCS 284
Cdd:cd01313 224 IHLAEQPKE---------------------VDDCLAAHGRRPVELLLDHGHLDARWCLVHATHLTDNETLLLgRSGAVVG 282
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32445787 285 IvyCPRTHHFFQHSNHPVAELLAAGINVAIGTDSRASnpdLDL-----WGEVQHLLKHR--------PDLNPTDVLRMAT 351
Cdd:cd01313 283 L--CPTTEANLGDGIFPAAALLAAGGRIGIGSDSNAR---IDLleelrQLEYSQRLRDRarnvlataGGSSARALLDAAL 357
|
170 180
....*....|....*....|....*...
gi 32445787 352 ANGADALGRSAthGRLAAGMPANFITVA 379
Cdd:cd01313 358 AGGAQALGLAT--GALEAGARADLLSLD 383
|
|
| Met_dep_hydrolase_A |
cd01299 |
Metallo-dependent hydrolases, subgroup A is part of the superfamily of metallo-dependent ... |
302-379 |
6.58e-10 |
|
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: 60.00 E-value: 6.58e-10
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 32445787 302 VAELLAAGINVAIGTDSRASNPDLD-LWGEVQHLLKHrpDLNPTDVLRMATANGADALGRSATHGRLAAGMPANFITVA 379
Cdd:cd01299 256 LRRAHKAGVKIAFGTDAGFPVPPHGwNARELELLVKA--GGTPAEALRAATANAAELLGLSDELGVIEAGKLADLLVVD 332
|
|
| Bact_CD |
cd01293 |
Bacterial cytosine deaminase and related metal-dependent hydrolases. Cytosine deaminases (CDs) ... |
29-376 |
1.43e-09 |
|
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: 59.18 E-value: 1.43e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32445787 29 VQSGRIASISSFQDSKNEGELIDLGDVAILPGLVNTHTHLE---FSDLPKPV--GHTGMELADWIREVITTrgmvDHQTR 103
Cdd:cd01293 19 IEDGRIAAIGPALAVPPDAEEVDAKGRLVLPAFVDPHIHLDktfTGGRWPNNsgGTLLEAIIAWEERKLLL----TAEDV 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32445787 104 QQNVLKGHAEATASGTQLI---ADIeTTPMESIAPNTI----------------AFAEVLGLSQERGDERMSQAERHLAN 164
Cdd:cd01293 95 KERAERALELAIAHGTTAIrthVDV-DPAAGLKALEALlelreewadlidlqivAFPQHGLLSTPGGEELMREALKMGAD 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32445787 165 NtspdsrcdVAAIsPHAPY-STPLPLIERCVQVAKQRKTTLAMHVAES--PAERELLTngsgpFAESLRTLGlpieaffp 241
Cdd:cd01293 174 V--------VGGI-PPAEIdEDGEESLDTLFELAQEHGLDIDLHLDETddPGSRTLEE-----LAEEAERRG-------- 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32445787 242 WTKANPVSHLIQLLAKSPralivhgNDLSETeIEQVKSHpNCSIVYCPRTHHFFQHSNH---------PVAELLAAGINV 312
Cdd:cd01293 232 MQGRVTCSHATALGSLPE-------AEVSRL-ADLLAEA-GISVVSLPPINLYLQGREDttpkrrgvtPVKELRAAGVNV 302
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 32445787 313 AIGTDS------RASNPD-LDLWGEVQHLLKHRPDLNPTDVLRMATANGADALGrsATHGRLAAGMPANFI 376
Cdd:cd01293 303 ALGSDNvrdpwyPFGSGDmLEVANLAAHIAQLGTPEDLALALDLITGNAARALG--LEDYGIKVGCPADLV 371
|
|
| PRK09229 |
PRK09229 |
N-formimino-L-glutamate deiminase; Validated |
206-382 |
2.55e-07 |
|
N-formimino-L-glutamate deiminase; Validated
Pssm-ID: 236420 [Multi-domain] Cd Length: 456 Bit Score: 52.54 E-value: 2.55e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32445787 206 MHVAESPAErelltngsgpfaeslrtlglpIEAFFPWTKANPVSHLIQLLAKSPRALIVHGNDLSETEIEQV-KSHPNCS 284
Cdd:PRK09229 233 IHIAEQTKE---------------------VDDCLAWSGARPVEWLLDHAPVDARWCLVHATHLTDAETARLaRSGAVAG 291
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32445787 285 IvyCPRTHH-----FFqhsnhPVAELLAAGINVAIGTDSRASnpdLDLWGEVQHL-----LKHR---------PDLNPTD 345
Cdd:PRK09229 292 L--CPTTEAnlgdgIF-----PAVDYLAAGGRFGIGSDSHVS---IDLVEELRLLeygqrLRDRrrnvlaaaaQPSVGRR 361
|
170 180 190
....*....|....*....|....*....|....*..
gi 32445787 346 VLRMATANGADALGRSAthGRLAAGMPANFITVATSA 382
Cdd:PRK09229 362 LFDAALAGGAQALGRAI--GGLAVGARADLVVLDLDH 396
|
|
| Amidohydro_3 |
pfam07969 |
Amidohydrolase family; |
301-386 |
4.39e-07 |
|
Amidohydrolase family;
Pssm-ID: 400360 [Multi-domain] Cd Length: 464 Bit Score: 51.76 E-value: 4.39e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32445787 301 PVAELLAAGINVAIGTDSRASnpDLDLWGEVQHLLKHRP-----------DLNPTDVLRMATANGADALGRSATHGRLAA 369
Cdd:pfam07969 350 PVKELLNAGVKVALGSDAPVG--PFDPWPRIGAAVMRQTagggevlgpdeELSLEEALALYTSGPAKALGLEDRKGTLGV 427
|
90
....*....|....*..
gi 32445787 370 GMPANFITVATSADRVD 386
Cdd:pfam07969 428 GKDADLVVLDDDPLTVD 444
|
|
| YtcJ_like |
cd01300 |
YtcJ_like metal dependent amidohydrolases. YtcJ is a Bacillus subtilis ORF of unknown function. ... |
301-376 |
5.29e-05 |
|
YtcJ_like metal dependent amidohydrolases. YtcJ is a Bacillus subtilis ORF of unknown function. The Arabidopsis homolog LAF3 has been identified as a factor required for phytochrome A signalling.
Pssm-ID: 238625 [Multi-domain] Cd Length: 479 Bit Score: 45.38 E-value: 5.29e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32445787 301 PVAELLAAGINVAIGTDSRASnpDLDLWGEVQHLLKHRPD-----------LNPTDVLRMATANGADALGRSATHGRLAA 369
Cdd:cd01300 394 PFRSLLDAGVPVALGSDAPVA--PPDPLLGIWAAVTRKTPgggvlgnpeerLSLEEALRAYTIGAAYAIGEEDEKGSLEP 471
|
....*..
gi 32445787 370 GMPANFI 376
Cdd:cd01300 472 GKLADFV 478
|
|
| NagA |
COG1820 |
N-acetylglucosamine-6-phosphate deacetylase [Carbohydrate transport and metabolism]; |
324-376 |
6.08e-05 |
|
N-acetylglucosamine-6-phosphate deacetylase [Carbohydrate transport and metabolism];
Pssm-ID: 441425 [Multi-domain] Cd Length: 373 Bit Score: 44.70 E-value: 6.08e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 32445787 324 DLDLWGEVQHLLKHRpDLNPTDVLRMATANGADALGRSATHGRLAAGMPANFI 376
Cdd:COG1820 306 TLTMDDAVRNLVEWT-GLPLEEAVRMASLNPARALGLDDRKGSIAPGKDADLV 357
|
|
| PRK07203 |
PRK07203 |
putative aminohydrolase SsnA; |
22-378 |
2.50e-04 |
|
putative aminohydrolase SsnA;
Pssm-ID: 235963 [Multi-domain] Cd Length: 442 Bit Score: 43.00 E-value: 2.50e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32445787 22 IPNGMMIVQSGRIASISSFQDSKN---EGELIDLGDVAILPGLVNTHTHLeFSDLPKPVGHTG----------------- 81
Cdd:PRK07203 19 IEDGAIAIEGNVIVEIGTTDELKAkypDAEFIDAKGKLIMPGLINSHNHI-YSGLARGMMANIppppdfisilknlwwrl 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32445787 82 --------------MELADWIREVITTrgMVDHqtrqqnvlkgHAEATASGTQL--IADI------------ETTP---- 129
Cdd:PRK07203 98 draltledvyysalICSLEAIKNGVTT--VFDH----------HASPNYIGGSLftIADAakkvglramlcyETSDrdge 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32445787 130 ---MESIAPNtIAFAEvlgLSQERGDERMSqaerhlanntspdsrcdvAAISPHAPYSTPLPLIERCVQVAKQRKTTLAM 206
Cdd:PRK07203 166 kelQEGVEEN-IRFIK---HIDEAKDDMVE------------------AMFGLHASFTLSDATLEKCREAVKETGRGYHI 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32445787 207 HVAESPAERElltngsgpfaESLRTLGLPIeaffpwtkanpVSHLIQLLAKSPRALIVHGNDLSETEIEQVKsHPNCSIV 286
Cdd:PRK07203 224 HVAEGIYDVS----------DSHKKYGKDI-----------VERLADFGLLGEKTLAAHCIYLSDEEIDLLK-ETDTFVV 281
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32445787 287 YCPRthhffqhSN-------HPVAELLAAGINVAIGTDSRASnpdlDLWGEVQ-HLLKHRPDLNP-----TDVLRMATAN 353
Cdd:PRK07203 282 HNPE-------SNmgnavgyNPVLEMIKNGILLGLGTDGYTS----DMFESYKvANFKHKHAGGDpnvgwPESPAMLFEN 350
|
410 420
....*....|....*....|....*..
gi 32445787 354 GADALGR--SATHGRLAAGMPANFITV 378
Cdd:PRK07203 351 NNKIAERyfGAKFGILEEGAKADLIIV 377
|
|
| NagA |
cd00854 |
N-acetylglucosamine-6-phosphate deacetylase, NagA, catalyzes the hydrolysis of the N-acetyl ... |
17-67 |
2.81e-04 |
|
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: 42.57 E-value: 2.81e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 32445787 17 IDGDPIPNGMMIVQSGRIASISSFQDSKNEGELIDLGDVAILPGLVNTHTH 67
Cdd:cd00854 9 LTPGGLEDGAVLVEDGKIVAIGPEDELEEADEIIDLKGQYLVPGFIDIHIH 59
|
|
| PRK05985 |
PRK05985 |
cytosine deaminase; Provisional |
301-378 |
3.04e-04 |
|
cytosine deaminase; Provisional
Pssm-ID: 180337 [Multi-domain] Cd Length: 391 Bit Score: 42.61 E-value: 3.04e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32445787 301 PVAELLAAGINVAIGTDS-RAS-----NPDLdLwgEVQHLLKHRPDLNPTDVLR----MATANGADALGRsaTHGRLAAG 370
Cdd:PRK05985 280 PVAALRAAGVTVFGGNDGiRDTwwpygNGDM-L--ERAMLIGYRSGFRTDDELAaaldCVTHGGARALGL--EDYGLAVG 354
|
....*...
gi 32445787 371 MPANFITV 378
Cdd:PRK05985 355 ARADFVLV 362
|
|
| L-HYD_ALN |
cd01315 |
L-Hydantoinases (L-HYDs) and Allantoinase (ALN); L-Hydantoinases are a member of the ... |
28-68 |
9.71e-04 |
|
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: 41.12 E-value: 9.71e-04
10 20 30 40
....*....|....*....|....*....|....*....|.
gi 32445787 28 IVQSGRIASISSFQDSKNEGELIDLGDVAILPGLVNTHTHL 68
Cdd:cd01315 21 AVKGGKIAAIGPDIANTEAEEVIDAGGLVVMPGLIDTHVHI 61
|
|
| PRK05985 |
PRK05985 |
cytosine deaminase; Provisional |
14-68 |
1.49e-03 |
|
cytosine deaminase; Provisional
Pssm-ID: 180337 [Multi-domain] Cd Length: 391 Bit Score: 40.69 E-value: 1.49e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 32445787 14 VMPIDGDPIPngmMIVQSGRIASISSFQDSKNEGELIDLGDVAILPGLVNTHTHL 68
Cdd:PRK05985 9 VRPAGGAAVD---ILIRDGRIAAIGPALAAPPGAEVEDGGGALALPGLVDGHIHL 60
|
|
| NagA |
COG1820 |
N-acetylglucosamine-6-phosphate deacetylase [Carbohydrate transport and metabolism]; |
22-67 |
2.03e-03 |
|
N-acetylglucosamine-6-phosphate deacetylase [Carbohydrate transport and metabolism];
Pssm-ID: 441425 [Multi-domain] Cd Length: 373 Bit Score: 40.08 E-value: 2.03e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 32445787 22 IPNGMMIVQSGRIASISSfqDSKNEGELIDLGDVAILPGLVNTHTH 67
Cdd:COG1820 14 LEDGALLIEDGRIAAIGP--GAEPDAEVIDLGGGYLAPGFIDLHVH 57
|
|
| PRK06886 |
PRK06886 |
hypothetical protein; Validated |
295-359 |
5.25e-03 |
|
hypothetical protein; Validated
Pssm-ID: 180740 Cd Length: 329 Bit Score: 38.66 E-value: 5.25e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 32445787 295 FQHSNHPVAELLAAGINVAIGTDSRAS--NP--DLDLWGEVQHLLK--HRPDLNptDVLRMATANGADALG 359
Cdd:PRK06886 258 FHNALTPADEMIPEGITVALGTDNICDymVPlcEGDMWQELSLLAAgcRFYDLD--EMVNIASINGRKVLG 326
|
|
| PRK07583 |
PRK07583 |
cytosine deaminase; |
301-376 |
5.38e-03 |
|
cytosine deaminase;
Pssm-ID: 236062 Cd Length: 438 Bit Score: 38.81 E-value: 5.38e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32445787 301 PVAELLAAGINVAIGTDSrASNP-----DLDL---WGE---VQHLlkhrpDLNPTDVLRMATANGADALGRSAtHGRLAA 369
Cdd:PRK07583 315 LVHELKAAGIPVAVASDN-CRDPfyaygDHDMlevFREavrILHL-----DHPYDDWPAAVTTTPADIMGLPD-LGRIAV 387
|
....*..
gi 32445787 370 GMPANFI 376
Cdd:PRK07583 388 GAPADLV 394
|
|
| PLN02795 |
PLN02795 |
allantoinase |
29-68 |
7.01e-03 |
|
allantoinase
Pssm-ID: 178392 [Multi-domain] Cd Length: 505 Bit Score: 38.60 E-value: 7.01e-03
10 20 30 40
....*....|....*....|....*....|....*....|...
gi 32445787 29 VQSGRIASISSFQD---SKNEGELIDLGDVAILPGLVNTHTHL 68
Cdd:PLN02795 66 VEGGRIVSVTKEEEapkSQKKPHVLDYGNAVVMPGLIDVHVHL 108
|
|
| COG3964 |
COG3964 |
Predicted amidohydrolase [General function prediction only]; |
16-67 |
9.29e-03 |
|
Predicted amidohydrolase [General function prediction only];
Pssm-ID: 443164 [Multi-domain] Cd Length: 376 Bit Score: 37.84 E-value: 9.29e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 32445787 16 PIDGDPIPNGMM--IVQSGRIASISSFQDSKNEGELIDLGDVAILPGLVNTHTH 67
Cdd:COG3964 9 VIDPANGIDGVMdiAIKDGKIAAVAKDIDAAEAKKVIDASGLYVTPGLIDLHTH 62
|
|
| |
